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***  MEMBRANE PROTEIN 10-FEB-15 4Y3U  ***

elNémo ID: 22012420165326416

Job options:

ID        	=	 22012420165326416
JOBID     	=	 MEMBRANE PROTEIN 10-FEB-15 4Y3U
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    MEMBRANE PROTEIN                        10-FEB-15   4Y3U              
TITLE     THE STRUCTURE OF PHOSPHOLAMBAN BOUND TO THE CALCIUM PUMP SERCA1A      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1;       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: SR CA(2+)-ATPASE 1,CALCIUM PUMP 1,CALCIUM-TRANSPORTING      
COMPND   5 ATPASE SARCOPLASMIC RETICULUM TYPE,FAST TWITCH SKELETAL MUSCLE       
COMPND   6 ISOFORM,ENDOPLASMIC RETICULUM CLASS 1/2 CA(2+) ATPASE;               
COMPND   7 EC: 3.6.3.8;                                                         
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CARDIAC PHOSPHOLAMBAN;                                     
COMPND  10 CHAIN: B;                                                            
COMPND  11 SYNONYM: PLB;                                                        
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: CARDIAC PHOSPHOLAMBAN;                                     
COMPND  15 CHAIN: C;                                                            
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 OTHER_DETAILS: THIS IS A SECOND COPY OF PHOSPHOLAMBAN BOUND IN THIS  
COMPND  18 STRUCTURE, BUT THE SIDE CHAIN ELECTRON DENSITY IS INSUFFICIENT TO    
COMPND  19 ASSIGN THE CORRECT SEQUENCE REGISTER                                 
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;                          
SOURCE   3 ORGANISM_COMMON: RABBIT;                                             
SOURCE   4 ORGANISM_TAXID: 9986;                                                
SOURCE   5 ORGAN: MUSCLE;                                                       
SOURCE   6 TISSUE: SKELETAL MUSCLE;                                             
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: CANIS FAMILIARIS;                               
SOURCE   9 ORGANISM_COMMON: DOG;                                                
SOURCE  10 ORGANISM_TAXID: 9615;                                                
SOURCE  11 GENE: PLN;                                                           
SOURCE  12 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  14 EXPRESSION_SYSTEM_CELL_LINE: SF21;                                   
SOURCE  15 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PVL1393;                                  
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: CANIS FAMILIARIS;                               
SOURCE  19 ORGANISM_COMMON: DOG;                                                
SOURCE  20 ORGANISM_TAXID: 9615;                                                
SOURCE  21 GENE: PLN;                                                           
SOURCE  22 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  23 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    CA-ATPASE, SERCA1A, MEMBRANE PROTEIN                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.D.HURLEY                                                            
REVDAT   3   04-DEC-19 4Y3U    1       REMARK                                   
REVDAT   2   20-SEP-17 4Y3U    1       SOURCE REMARK                            
REVDAT   1   25-FEB-15 4Y3U    0                                                
JRNL        AUTH   B.L.AKIN,T.D.HURLEY,Z.CHEN,L.R.JONES                         
JRNL        TITL   THE STRUCTURAL BASIS FOR PHOSPHOLAMBAN INHIBITION OF THE     
JRNL        TITL 2 CALCIUM PUMP IN SARCOPLASMIC RETICULUM.                      
JRNL        REF    J. BIOL. CHEM.                V. 288 30181 2013              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   23996003                                                     
JRNL        DOI    10.1074/JBC.M113.501585                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.51 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.51                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.79                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 22031                          
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) : 0.237                           
REMARK   3   R VALUE            (WORKING SET) : 0.235                           
REMARK   3   FREE R VALUE                     : 0.277                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1195                            
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) : 3.51                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.60                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1581                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.65                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2850                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 100                          
REMARK   3   BIN FREE R VALUE                    : 0.3600                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7811                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 135.9                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.54000                                              
REMARK   3    B22 (A**2) : 1.61000                                              
REMARK   3    B33 (A**2) : -3.15000                                             
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.592         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.404         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 56.647        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.894                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.852                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7955 ; 0.005 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10783 ; 1.021 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1009 ; 5.277 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   321 ;36.734 ;24.393       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1399 ;18.114 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    48 ;13.558 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1272 ; 0.068 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5847 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4060 ; 2.509 ; 7.422       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5061 ; 4.291 ;11.115       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3895 ; 2.643 ; 7.769       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 12083 ; 8.479 ;63.032       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
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     1        A   330                          
REMARK   3    ORIGIN FOR THE GROUP (A): -44.5734 -31.6363-123.6795              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7714 T22:   0.7984                                     
REMARK   3      T33:   0.4719 T12:   0.0323                                     
REMARK   3      T13:  -0.0047 T23:   0.0602                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3569 L22:   0.7871                                     
REMARK   3      L33:   0.9847 L12:  -0.3844                                     
REMARK   3      L13:   0.5631 L23:  -0.5620                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2042 S12:   0.0289 S13:  -0.1562                       
REMARK   3      S21:  -0.4126 S22:   0.0299 S23:  -0.1972                       
REMARK   3      S31:   0.0789 S32:   0.1027 S33:  -0.2342                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   331        A   803                          
REMARK   3    ORIGIN FOR THE GROUP (A): -55.5198 -18.3549 -89.6622              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5685 T22:   0.6105                                     
REMARK   3      T33:   0.6781 T12:  -0.0466                                     
REMARK   3      T13:  -0.0912 T23:   0.0384                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3729 L22:   0.2968                                     
REMARK   3      L33:   1.3842 L12:   0.0468                                     
REMARK   3      L13:   0.5882 L23:   0.4096                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0430 S12:  -0.0054 S13:   0.1140                       
REMARK   3      S21:  -0.0003 S22:  -0.0226 S23:   0.0105                       
REMARK   3      S31:   0.0342 S32:   0.0030 S33:  -0.0204                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   804        A   992                          
REMARK   3    ORIGIN FOR THE GROUP (A): -59.1910   1.3371-144.6857              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5085 T22:   0.5257                                     
REMARK   3      T33:   0.2740 T12:   0.0642                                     
REMARK   3      T13:  -0.1837 T23:   0.3112                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8074 L22:   0.0500                                     
REMARK   3      L33:   5.1200 L12:  -0.0938                                     
REMARK   3      L13:   0.1236 L23:  -0.2315                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3260 S12:   0.1156 S13:   0.1132                       
REMARK   3      S21:  -0.0121 S22:  -0.1124 S23:  -0.0968                       
REMARK   3      S31:  -1.1613 S32:  -0.3378 S33:   0.4384                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    21        B    41                          
REMARK   3    ORIGIN FOR THE GROUP (A): -38.9497  -7.0594-132.6139              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8026 T22:   1.0367                                     
REMARK   3      T33:   1.2021 T12:  -0.4155                                     
REMARK   3      T13:   0.0478 T23:   0.2385                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5598 L22:   3.8830                                     
REMARK   3      L33:   0.2687 L12:  -1.4611                                     
REMARK   3      L13:   0.3807 L23:  -0.9991                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0446 S12:   0.2436 S13:   0.8126                       
REMARK   3      S21:   0.2597 S22:  -0.5230 S23:  -2.1149                       
REMARK   3      S31:   0.0270 S32:   0.0737 S33:   0.5676                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    42        B    50                          
REMARK   3    ORIGIN FOR THE GROUP (A): -35.0001  -8.5086-155.2720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6911 T22:   0.6525                                     
REMARK   3      T33:   0.4725 T12:  -0.2095                                     
REMARK   3      T13:   0.2080 T23:   0.0611                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3105 L22:   3.5953                                     
REMARK   3      L33:  49.1656 L12:  -3.9340                                     
REMARK   3      L13:  -3.2679 L23:   3.2694                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3476 S12:  -0.1747 S13:  -0.7322                       
REMARK   3      S21:  -0.2870 S22:   0.1758 S23:   0.6899                       
REMARK   3      S31:  -0.6692 S32:   0.4392 S33:  -0.5234                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   101        C   116                          
REMARK   3    ORIGIN FOR THE GROUP (A): -27.5760  -7.1484-147.5218              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8312 T22:   1.7272                                     
REMARK   3      T33:   0.8536 T12:  -0.1606                                     
REMARK   3      T13:   0.3309 T23:  -0.3646                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0775 L22:   0.1948                                     
REMARK   3      L33:   0.0505 L12:  -0.0919                                     
REMARK   3      L13:  -0.0355 L23:   0.0963                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1311 S12:   0.2261 S13:  -0.1106                       
REMARK   3      S21:   0.0516 S22:  -0.3353 S23:   0.3714                       
REMARK   3      S31:   0.0721 S32:  -0.1538 S33:   0.2042                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
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: NULL                                      
REMARK   4                                                                      
REMARK   4 4Y3U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-FEB-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000206820.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-AUG-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.987                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23282                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.200                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : 0.08700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 16.4600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.56                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.470                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4KYT                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.73                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 UL OF SERCA1A AT 15 MG/ML IN 2% N-     
REMARK 280  NONYL-BETA-D-MALTOPYRANOSIDE (NONYL MALTOSIDE) (ANATRACE), 20%      
REMARK 280  GLYCEROL, 100 MM MOPS (PH 7.0), 0.12 M SUCROSE, 80 MM KCL, 3 MM     
REMARK 280  MGCL2, AND 2.8 MM EGTA WAS MIXED WITH 1 UL OF PHOSPHOLAMBAN AT      
REMARK 280  2.1 MG/ML IN 20 MM MOPS (PH 7.2), 20% GLYCEROL, AND 0.1 %           
REMARK 280  DECYLMALTOSIDE OR 0.01% DODECYL MALTOSIDE. THIS PROTEIN MIXTURE     
REMARK 280  WAS THEN ADDED TO AN EQUAL VOLUME OF CRYSTALLIZATION LIQUOR; 15 %   
REMARK 280  GLYCEROL, 17% (W/V) PEG-2000, 200MM NAOAC, AND 5 MM BETA-           
REMARK 280  MERCOPTOETHANOL), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K   
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       30.87250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      158.12800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.91250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      158.12800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.87250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.91250            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 46570 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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     GLY A    46                                                      
REMARK 465     LYS A    47                                                      
REMARK 465     GLU A    79                                                      
REMARK 465     GLU A    80                                                      
REMARK 465     GLY A    81                                                      
REMARK 465     GLU A    82                                                      
REMARK 465     GLU A    83                                                      
REMARK 465     THR A    84                                                      
REMARK 465     ILE A    85                                                      
REMARK 465     ALA A   241                                                      
REMARK 465     THR A   242                                                      
REMARK 465     GLU A   243                                                      
REMARK 465     VAL A   283                                                      
REMARK 465     HIS A   284                                                      
REMARK 465     GLY A   285                                                      
REMARK 465     GLY A   286                                                      
REMARK 465     SER A   287                                                      
REMARK 465     TRP A   288                                                      
REMARK 465     ILE A   289                                                      
REMARK 465     SER A   504                                                      
REMARK 465     ARG A   505                                                      
REMARK 465     ALA A   506                                                      
REMARK 465     GLU A   993                                                      
REMARK 465     GLY A   994                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     LYS B     3                                                      
REMARK 465     VAL B     4                                                      
REMARK 465     GLN B     5                                                      
REMARK 465     TYR B     6                                                      
REMARK 465     LEU B     7                                                      
REMARK 465     THR B     8                                                      
REMARK 465     ARG B     9                                                      
REMARK 465     SER B    10                                                      
REMARK 465     ALA B    11                                                      
REMARK 465     ILE B    12                                                      
REMARK 465     ARG B    13                                                      
REMARK 465     ARG B    14                                                      
REMARK 465     ALA B    15                                                      
REMARK 465     SER B    16                                                      
REMARK 465     THR B    17                                                      
REMARK 465     ILE B    18                                                      
REMARK 465     GLU B    19                                                      
REMARK 465     MET B    20                                                      
REMARK 465     UNK C   117                                                      
REMARK 465     UNK C   118                                                      
REMARK 465     UNK C   119                                                      
REMARK 465     UNK C   120                                                      
REMARK 465     UNK C   121                                                      
REMARK 465     UNK C   122                                                      
REMARK 465     UNK C   123                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 246    CG   CD   CE   NZ                                   
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    LEU A  49     -100.65     59.49                                   
REMARK 500    SER A 178      -46.65    -28.55                                   
REMARK 500    GLU A 183      102.30    -57.76                                   
REMARK 500    ALA A 199      129.89    -37.03                                   
REMARK 500    ASP A 245      132.43    178.43                                   
REMARK 500    ILE A 276      -84.22    -67.75                                   
REMARK 500    ASP A 281      -64.82    -29.17                                   
REMARK 500    ASN A 330       17.03     89.71                                   
REMARK 500    ASP A 370      -61.09   -102.16                                   
REMARK 500    THR A 388     -157.05    -90.45                                   
REMARK 500    ASP A 399       -0.91     56.47                                   
REMARK 500    CYS A 420       46.80    -67.61                                   
REMARK 500    ALA A 468      -37.09    -37.79                                   
REMARK 500    LYS A 502     -102.75     43.04                                   
REMARK 500    THR A 558       62.32     39.40                                   
REMARK 500    GLU A 646      135.87    -39.39                                   
REMARK 500    ALA A 649      -39.24    -38.29                                   
REMARK 500    ASP A 703      -19.16   -154.57                                   
REMARK 500    ASP A 738       16.13     49.41                                   
REMARK 500    PHE A 856      -83.08    -77.49                                   
REMARK 500    GLU A 860       60.81   -103.43                                   
REMARK 500    ASP A 861       48.32   -149.50                                   
REMARK 500    TYR A 867      -80.53    -66.73                                   
REMARK 500    HIS A 868       84.23    170.84                                   
REMARK 500    HIS A 872       46.92    -96.31                                   
REMARK 500    CYS A 876      -51.35   -146.48                                   
REMARK 500    ASP A 879       41.75   -100.94                                   
REMARK 500    GLU A 884      -90.09   -132.75                                   
REMARK 500    GLU A 889      -12.65   -149.61                                   
REMARK 500    PHE A 891      -40.96   -132.59                                   
REMARK 500    PRO A 894       30.71    -86.52                                   
REMARK 500    PHE A 957     -110.03    -99.39                                   
REMARK 500    LEU A 964      -32.37   -131.24                                   
REMARK 500    ASN A 990       39.66    -95.56                                   
REMARK 500    TYR A 991      -37.68   -135.59                                   
REMARK 500    GLN B  22      -72.32   -119.57                                   
REMARK 500    LEU B  43       26.77    -76.48                                   
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                               K A1001   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU A 711   O                                                      
REMARK 620 2 LYS A 712   O    67.2                                              
REMARK 620 3 ALA A 714   O    76.8  72.3                                        
REMARK 620 4 GLU A 732   OE1  86.6 152.8 110.0                                  
REMARK 620 5 GLU A 732   OE2 115.8 145.2 142.2  41.5                            
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 K A 1001                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4KYT   RELATED DB: PDB                                   
REMARK 900 4KYT CONTAINED A HIGH-AFFINITY MUTANT OF PHOSPHOLAMBAN. THIS ENTRY   
REMARK 900 CONTAINS THE WILD-TYPE SEQUENCE FOR PHOSPHOLAMBAN                    
DBREF  4Y3U A    1   994  UNP    P04191   AT2A1_RABIT      1    994             
DBREF  4Y3U B    1    50  UNP    P61012   PPLA_CANFA       1     50             
DBREF  4Y3U C  101   123  PDB    4Y3U     4Y3U           101    123             
SEQRES   1 A  994  MET GLU ALA ALA HIS SER LYS SER THR GLU GLU CYS LEU          
SEQRES   2 A  994  ALA TYR PHE GLY VAL SER GLU THR THR GLY LEU THR PRO          
SEQRES   3 A  994  ASP GLN VAL LYS ARG HIS LEU GLU LYS TYR GLY HIS ASN          
SEQRES   4 A  994  GLU LEU PRO ALA GLU GLU GLY LYS SER LEU TRP GLU LEU          
SEQRES   5 A  994  VAL ILE GLU GLN PHE GLU ASP LEU LEU VAL ARG ILE LEU          
SEQRES   6 A  994  LEU LEU ALA ALA CYS ILE SER PHE VAL LEU ALA TRP PHE          
SEQRES   7 A  994  GLU GLU GLY GLU GLU THR ILE THR ALA PHE VAL GLU PRO          
SEQRES   8 A  994  PHE VAL ILE LEU LEU ILE LEU ILE ALA ASN ALA ILE VAL          
SEQRES   9 A  994  GLY VAL TRP GLN GLU ARG ASN ALA GLU ASN ALA ILE GLU          
SEQRES  10 A  994  ALA LEU LYS GLU TYR GLU PRO GLU MET GLY LYS VAL TYR          
SEQRES  11 A  994  ARG ALA ASP ARG LYS SER VAL GLN ARG ILE LYS ALA ARG          
SEQRES  12 A  994  ASP ILE VAL PRO GLY ASP ILE VAL GLU VAL ALA VAL GLY          
SEQRES  13 A  994  ASP LYS VAL PRO ALA ASP ILE ARG ILE LEU SER ILE LYS          
SEQRES  14 A  994  SER THR THR LEU ARG VAL ASP GLN SER ILE LEU THR GLY          
SEQRES  15 A  994  GLU SER VAL SER VAL ILE LYS HIS THR GLU PRO VAL PRO          
SEQRES  16 A  994  ASP PRO ARG ALA VAL ASN GLN ASP LYS LYS ASN MET LEU          
SEQRES  17 A  994  PHE SER GLY THR ASN ILE ALA ALA GLY LYS ALA LEU GLY          
SEQRES  18 A  994  ILE VAL ALA THR THR GLY VAL SER THR GLU ILE GLY LYS          
SEQRES  19 A  994  ILE ARG ASP GLN MET ALA ALA THR GLU GLN ASP LYS THR          
SEQRES  20 A  994  PRO LEU GLN GLN LYS LEU ASP GLU PHE GLY GLU GLN LEU          
SEQRES  21 A  994  SER LYS VAL ILE SER LEU ILE CYS VAL ALA VAL TRP LEU          
SEQRES  22 A  994  ILE ASN ILE GLY HIS PHE ASN ASP PRO VAL HIS GLY GLY          
SEQRES  23 A  994  SER TRP ILE ARG GLY ALA ILE TYR TYR PHE LYS ILE ALA          
SEQRES  24 A  994  VAL ALA LEU ALA VAL ALA ALA ILE PRO GLU GLY LEU PRO          
SEQRES  25 A  994  ALA VAL ILE THR THR CYS LEU ALA LEU GLY THR ARG ARG          
SEQRES  26 A  994  MET ALA LYS LYS ASN ALA ILE VAL ARG SER LEU PRO SER          
SEQRES  27 A  994  VAL GLU THR LEU GLY CYS THR SER VAL ILE CYS SER ASP          
SEQRES  28 A  994  LYS THR GLY THR LEU THR THR ASN GLN MET SER VAL CYS          
SEQRES  29 A  994  LYS MET PHE ILE ILE ASP LYS VAL ASP GLY ASP PHE CYS          
SEQRES  30 A  994  SER LEU ASN GLU PHE SER ILE THR GLY SER THR TYR ALA          
SEQRES  31 A  994  PRO GLU GLY GLU VAL LEU LYS ASN ASP LYS PRO ILE ARG          
SEQRES  32 A  994  SER GLY GLN PHE ASP GLY LEU VAL GLU LEU ALA THR ILE          
SEQRES  33 A  994  CYS ALA LEU CYS ASN ASP SER SER LEU ASP PHE ASN GLU          
SEQRES  34 A  994  THR LYS GLY VAL TYR GLU LYS VAL GLY GLU ALA THR GLU          
SEQRES  35 A  994  THR ALA LEU THR THR LEU VAL GLU LYS MET ASN VAL PHE          
SEQRES  36 A  994  ASN THR GLU VAL ARG ASN LEU SER LYS VAL GLU ARG ALA          
SEQRES  37 A  994  ASN ALA CYS ASN SER VAL ILE ARG GLN LEU MET LYS LYS          
SEQRES  38 A  994  GLU PHE THR LEU GLU PHE SER ARG ASP ARG LYS SER MET          
SEQRES  39 A  994  SER VAL TYR CYS SER PRO ALA LYS SER SER ARG ALA ALA          
SEQRES  40 A  994  VAL GLY ASN LYS MET PHE VAL LYS GLY ALA PRO GLU GLY          
SEQRES  41 A  994  VAL ILE ASP ARG CYS ASN TYR VAL ARG VAL GLY THR THR          
SEQRES  42 A  994  ARG VAL PRO MET THR GLY PRO VAL LYS GLU LYS ILE LEU          
SEQRES  43 A  994  SER VAL ILE LYS GLU TRP GLY THR GLY ARG ASP THR LEU          
SEQRES  44 A  994  ARG CYS LEU ALA LEU ALA THR ARG ASP THR PRO PRO LYS          
SEQRES  45 A  994  ARG GLU GLU MET VAL LEU ASP ASP SER SER ARG PHE MET          
SEQRES  46 A  994  GLU TYR GLU THR ASP LEU THR PHE VAL GLY VAL VAL GLY          
SEQRES  47 A  994  MET LEU ASP PRO PRO ARG LYS GLU VAL MET GLY SER ILE          
SEQRES  48 A  994  GLN LEU CYS ARG ASP ALA GLY ILE ARG VAL ILE MET ILE          
SEQRES  49 A  994  THR GLY ASP ASN LYS GLY THR ALA ILE ALA ILE CYS ARG          
SEQRES  50 A  994  ARG ILE GLY ILE PHE GLY GLU ASN GLU GLU VAL ALA ASP          
SEQRES  51 A  994  ARG ALA TYR THR GLY ARG GLU PHE ASP ASP LEU PRO LEU          
SEQRES  52 A  994  ALA GLU GLN ARG GLU ALA CYS ARG ARG ALA CYS CYS PHE          
SEQRES  53 A  994  ALA ARG VAL GLU PRO SER HIS LYS SER LYS ILE VAL GLU          
SEQRES  54 A  994  TYR LEU GLN SER TYR ASP GLU ILE THR ALA MET THR GLY          
SEQRES  55 A  994  ASP GLY VAL ASN ASP ALA PRO ALA LEU LYS LYS ALA GLU          
SEQRES  56 A  994  ILE GLY ILE ALA MET GLY SER GLY THR ALA VAL ALA LYS          
SEQRES  57 A  994  THR ALA SER GLU MET VAL LEU ALA ASP ASP ASN PHE SER          
SEQRES  58 A  994  THR ILE VAL ALA ALA VAL GLU GLU GLY ARG ALA ILE TYR          
SEQRES  59 A  994  ASN ASN MET LYS GLN PHE ILE ARG TYR LEU ILE SER SER          
SEQRES  60 A  994  ASN VAL GLY GLU VAL VAL CYS ILE PHE LEU THR ALA ALA          
SEQRES  61 A  994  LEU GLY LEU PRO GLU ALA LEU ILE PRO VAL GLN LEU LEU          
SEQRES  62 A  994  TRP VAL ASN LEU VAL THR ASP GLY LEU PRO ALA THR ALA          
SEQRES  63 A  994  LEU GLY PHE ASN PRO PRO ASP LEU ASP ILE MET ASP ARG          
SEQRES  64 A  994  PRO PRO ARG SER PRO LYS GLU PRO LEU ILE SER GLY TRP          
SEQRES  65 A  994  LEU PHE PHE ARG TYR MET ALA ILE GLY GLY TYR VAL GLY          
SEQRES  66 A  994  ALA ALA THR VAL GLY ALA ALA ALA TRP TRP PHE MET TYR          
SEQRES  67 A  994  ALA GLU ASP GLY PRO GLY VAL THR TYR HIS GLN LEU THR          
SEQRES  68 A  994  HIS PHE MET GLN CYS THR GLU ASP HIS PRO HIS PHE GLU          
SEQRES  69 A  994  GLY LEU ASP CYS GLU ILE PHE GLU ALA PRO GLU PRO MET          
SEQRES  70 A  994  THR MET ALA LEU SER VAL LEU VAL THR ILE GLU MET CYS          
SEQRES  71 A  994  ASN ALA LEU ASN SER LEU SER GLU ASN GLN SER LEU MET          
SEQRES  72 A  994  ARG MET PRO PRO TRP VAL ASN ILE TRP LEU LEU GLY SER          
SEQRES  73 A  994  ILE CYS LEU SER MET SER LEU HIS PHE LEU ILE LEU TYR          
SEQRES  74 A  994  VAL ASP PRO LEU PRO MET ILE PHE LYS LEU LYS ALA LEU          
SEQRES  75 A  994  ASP LEU THR GLN TRP LEU MET VAL LEU LYS ILE SER LEU          
SEQRES  76 A  994  PRO VAL ILE GLY LEU ASP GLU ILE LEU LYS PHE ILE ALA          
SEQRES  77 A  994  ARG ASN TYR LEU GLU GLY                                      
SEQRES   1 B   50  MET ASP LYS VAL GLN TYR LEU THR ARG SER ALA ILE ARG          
SEQRES   2 B   50  ARG ALA SER THR ILE GLU MET PRO GLN GLN ALA ARG GLN          
SEQRES   3 B   50  ASN LEU GLN ASN LEU PHE ILE ASN PHE CYS LEU ILE LEU          
SEQRES   4 B   50  ILE CYS LEU LEU LEU ILE CYS ILE ILE VAL MET                  
SEQRES   1 C   23  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   2 C   23  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK                      
HET      K  A1001       1                                                       
HETNAM       K POTASSIUM ION                                                    
FORMUL   4    K    K 1+                                                         
HELIX    1 AA1 ALA A    3  LYS A    7  5                                   5    
HELIX    2 AA2 SER A    8  GLY A   17  1                                  10    
HELIX    3 AA3 THR A   25  GLY A   37  1                                  13    
HELIX    4 AA4 LEU A   49  ILE A   54  1                                   6    
HELIX    5 AA5 GLU A   55  GLU A   58  5                                   4    
HELIX    6 AA6 ASP A   59  ALA A   69  1                                  11    
HELIX    7 AA7 SER A   72  PHE A   78  1                                   7    
HELIX    8 AA8 VAL A   89  ALA A  118  1                                  30    
HELIX    9 AA9 LEU A  119  GLU A  123  5                                   5    
HELIX   10 AB1 ARG A  143  ILE A  145  5                                   3    
HELIX   11 AB2 THR A  226  SER A  229  5                                   4    
HELIX   12 AB3 THR A  230  MET A  239  1                                  10    
HELIX   13 AB4 THR A  247  ASN A  275  1                                  29    
HELIX   14 AB5 GLY A  291  ALA A  306  1                                  16    
HELIX   15 AB6 PRO A  312  LYS A  328  1                                  17    
HELIX   16 AB7 PRO A  337  CYS A  344  1                                   8    
HELIX   17 AB8 ARG A  403  GLN A  406  5                                   4    
HELIX   18 AB9 PHE A  407  CYS A  420  1                                  14    
HELIX   19 AC1 GLU A  439  ASN A  453  1                                  15    
HELIX   20 AC2 SER A  463  ALA A  468  1                                   6    
HELIX   21 AC3 ASN A  469  GLN A  477  1                                   9    
HELIX   22 AC4 ALA A  517  ARG A  524  1                                   8    
HELIX   23 AC5 THR A  538  GLY A  555  1                                  18    
HELIX   24 AC6 ASP A  580  THR A  589  5                                  10    
HELIX   25 AC7 GLU A  606  GLY A  618  1                                  13    
HELIX   26 AC8 ASN A  628  ILE A  639  1                                  12    
HELIX   27 AC9 GLY A  655  ASP A  660  1                                   6    
HELIX   28 AD1 PRO A  662  ALA A  673  1                                  12    
HELIX   29 AD2 SER A  682  TYR A  694  1                                  13    
HELIX   30 AD3 GLY A  704  ASN A  706  5                                   3    
HELIX   31 AD4 ASP A  707  ALA A  714  1                                   8    
HELIX   32 AD5 THR A  724  ALA A  730  1                                   7    
HELIX   33 AD6 ASN A  739  GLY A  782  1                                  44    
HELIX   34 AD7 ILE A  788  THR A  799  1                                  12    
HELIX   35 AD8 LEU A  802  LEU A  807  1                                   6    
HELIX   36 AD9 GLY A  808  ASN A  810  5                                   3    
HELIX   37 AE1 ASP A  815  ARG A  819  5                                   5    
HELIX   38 AE2 SER A  830  TYR A  858  1                                  29    
HELIX   39 AE3 GLN A  869  PHE A  873  5                                   5    
HELIX   40 AE4 PRO A  896  ASN A  914  1                                  19    
HELIX   41 AE5 PRO A  926  VAL A  929  5                                   4    
HELIX   42 AE6 ASN A  930  VAL A  950  1                                  21    
HELIX   43 AE7 LEU A  964  LEU A  975  1                                  12    
HELIX   44 AE8 LEU A  975  ASN A  990  1                                  16    
HELIX   45 AE9 ALA B   24  CYS B   46  1                                  23    
HELIX   46 AF1 UNK C  102  UNK C  106  1                                   5    
HELIX   47 AF2 UNK C  106  UNK C  114  1                                   9    
SHEET    1 AA1 6 GLN A 138  LYS A 141  0                                        
SHEET    2 AA1 6 MET A 126  TYR A 130 -1  N  VAL A 129   O  GLN A 138           
SHEET    3 AA1 6 ILE A 150  ALA A 154 -1  O  GLU A 152   N  LYS A 128           
SHEET    4 AA1 6 LYS A 218  THR A 225 -1  O  GLY A 221   N  VAL A 151           
SHEET    5 AA1 6 ASP A 162  ILE A 168 -1  N  SER A 167   O  LEU A 220           
SHEET    6 AA1 6 MET A 207  LEU A 208 -1  O  LEU A 208   N  ILE A 163           
SHEET    1 AA2 3 VAL A 187  ILE A 188  0                                        
SHEET    2 AA2 3 ARG A 174  ASP A 176 -1  N  VAL A 175   O  VAL A 187           
SHEET    3 AA2 3 ASN A 213  ALA A 216 -1  O  ALA A 216   N  ARG A 174           
SHEET    1 AA3 8 ALA A 331  VAL A 333  0                                        
SHEET    2 AA3 8 MET A 733  LEU A 735 -1  O  VAL A 734   N  ILE A 332           
SHEET    3 AA3 8 ILE A 716  MET A 720  1  N  ALA A 719   O  MET A 733           
SHEET    4 AA3 8 THR A 698  GLY A 702  1  N  MET A 700   O  ILE A 718           
SHEET    5 AA3 8 VAL A 347  ASP A 351  1  N  CYS A 349   O  ALA A 699           
SHEET    6 AA3 8 ARG A 620  THR A 625  1  O  ILE A 622   N  ILE A 348           
SHEET    7 AA3 8 CYS A 675  ALA A 677  1  O  PHE A 676   N  MET A 623           
SHEET    8 AA3 8 ALA A 652  THR A 654  1  N  TYR A 653   O  CYS A 675           
SHEET    1 AA4 9 LYS A 400  PRO A 401  0                                        
SHEET    2 AA4 9 VAL A 395  LYS A 397 -1  N  LYS A 397   O  LYS A 400           
SHEET    3 AA4 9 PHE A 376  ILE A 384 -1  N  SER A 383   O  LEU A 396           
SHEET    4 AA4 9 SER A 362  ASP A 373 -1  N  ILE A 368   O  ASN A 380           
SHEET    5 AA4 9 LEU A 591  LEU A 600 -1  O  GLY A 598   N  LYS A 365           
SHEET    6 AA4 9 ARG A 560  ARG A 567 -1  N  THR A 566   O  THR A 592           
SHEET    7 AA4 9 LYS A 511  GLY A 516 -1  N  VAL A 514   O  ALA A 565           
SHEET    8 AA4 9 SER A 493  PRO A 500 -1  N  CYS A 498   O  LYS A 511           
SHEET    9 AA4 9 MET A 479  LEU A 485 -1  N  LEU A 485   O  SER A 495           
SHEET    1 AA5 7 LYS A 400  PRO A 401  0                                        
SHEET    2 AA5 7 VAL A 395  LYS A 397 -1  N  LYS A 397   O  LYS A 400           
SHEET    3 AA5 7 PHE A 376  ILE A 384 -1  N  SER A 383   O  LEU A 396           
SHEET    4 AA5 7 SER A 362  ASP A 373 -1  N  ILE A 368   O  ASN A 380           
SHEET    5 AA5 7 LEU A 591  LEU A 600 -1  O  GLY A 598   N  LYS A 365           
SHEET    6 AA5 7 CYS A 525  VAL A 530  1  N  ARG A 529   O  PHE A 593           
SHEET    7 AA5 7 THR A 533  PRO A 536 -1  O  THR A 533   N  VAL A 530           
SHEET    1 AA6 2 LEU A 425  PHE A 427  0                                        
SHEET    2 AA6 2 TYR A 434  LYS A 436 -1  O  GLU A 435   N  ASP A 426           
SSBOND   1 CYS A  876    CYS A  888                          1555   1555  2.03  
LINK         O   LEU A 711                 K     K A1001     1555   1555  3.20  
LINK         O   LYS A 712                 K     K A1001     1555   1555  3.03  
LINK         O   ALA A 714                 K     K A1001     1555   1555  2.86  
LINK         OE1 GLU A 732                 K     K A1001     1555   1555  2.79  
LINK         OE2 GLU A 732                 K     K A1001     1555   1555  3.27  
LINK         C   UNK C 101                 N   UNK C 102     1555   1555  1.33  
LINK         C   UNK C 102                 N   UNK C 103     1555   1555  1.33  
LINK         C   UNK C 103                 N   UNK C 104     1555   1555  1.33  
LINK         C   UNK C 104                 N   UNK C 105     1555   1555  1.33  
LINK         C   UNK C 105                 N   UNK C 106     1555   1555  1.33  
LINK         C   UNK C 106                 N   UNK C 107     1555   1555  1.33  
LINK         C   UNK C 107                 N   UNK C 108     1555   1555  1.33  
LINK         C   UNK C 108                 N   UNK C 109     1555   1555  1.33  
LINK         C   UNK C 109                 N   UNK C 110     1555   1555  1.33  
LINK         C   UNK C 110                 N   UNK C 111     1555   1555  1.33  
LINK         C   UNK C 111                 N   UNK C 112     1555   1555  1.33  
LINK         C   UNK C 112                 N   UNK C 113     1555   1555  1.33  
LINK         C   UNK C 113                 N   UNK C 114     1555   1555  1.33  
LINK         C   UNK C 114                 N   UNK C 115     1555   1555  1.33  
LINK         C   UNK C 115                 N   UNK C 116     1555   1555  1.33  
SITE     1 AC1  4 LEU A 711  LYS A 712  ALA A 714  GLU A 732                    
CRYST1   61.745   91.825  316.256  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      0.016196  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010890  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003162        0.00000                         
ATOM      1  N   MET A   1     -30.556 -50.203-109.658  1.00108.59           N  
ANISOU    1  N   MET A   1    13164  14818  13277    650  -1253    187       N  
ATOM      2  CA  MET A   1     -30.948 -51.460-108.942  1.00115.60           C  
ANISOU    2  CA  MET A   1    14063  15654  14204    637  -1440    212       C  
ATOM      3  C   MET A   1     -32.384 -51.857-109.265  1.00118.89           C  
ANISOU    3  C   MET A   1    14596  16019  14559    596  -1572    273       C  
ATOM      4  O   MET A   1     -33.317 -51.089-109.033  1.00120.08           O  
ANISOU    4  O   MET A   1    14735  16208  14678    518  -1564    342       O  
ATOM      5  CB  MET A   1     -30.764 -51.313-107.426  1.00114.37           C  
ANISOU    5  CB  MET A   1    13765  15554  14135    563  -1480    254       C  
ATOM      6  CG  MET A   1     -30.859 -52.625-106.657  1.00112.26           C  
ANISOU    6  CG  MET A   1    13491  15240  13921    560  -1655    271       C  
ATOM      7  SD  MET A   1     -30.258 -52.510-104.964  1.00107.47           S  
ANISOU    7  SD  MET A   1    12715  14697  13420    502  -1678    296       S  
ATOM      8  CE  MET A   1     -30.399 -54.214-104.446  1.00105.71           C  
ANISOU    8  CE  MET A   1    12524  14397  13241    519  -1887    307       C  
ATOM      9  N   GLU A   2     -32.557 -53.075-109.771  1.00126.06           N  
ANISOU    9  N   GLU A   2    15613  16835  15448    651  -1699    253       N  
ATOM     10  CA  GLU A   2     -33.813 -53.467-110.412  1.00131.49           C  
ANISOU   10  CA  GLU A   2    16435  17456  16067    628  -1817    300       C  
ATOM     11  C   GLU A   2     -34.748 -54.315-109.549  1.00129.40           C  
ANISOU   11  C   GLU A   2    16165  17161  15838    550  -2019    388       C  
ATOM     12  O   GLU A   2     -35.960 -54.326-109.779  1.00132.32           O  
ANISOU   12  O   GLU A   2    16600  17510  16165    492  -2107    464       O  
ATOM     13  CB  GLU A   2     -33.530 -54.175-111.747  1.00137.13           C  
ANISOU   13  CB  GLU A   2    17308  18076  16718    742  -1833    224       C  
ATOM     14  CG  GLU A   2     -34.586 -53.940-112.823  1.00140.96           C  
ANISOU   14  CG  GLU A   2    17936  18514  17107    735  -1856    250       C  
ATOM     15  CD  GLU A   2     -34.638 -52.496-113.312  1.00141.75           C  
ANISOU   15  CD  GLU A   2    18011  18689  17158    718  -1669    249       C  
ATOM     16  OE1 GLU A   2     -33.572 -51.932-113.648  1.00143.19           O  
ANISOU   16  OE1 GLU A   2    18151  18914  17341    782  -1503    182       O  
ATOM     17  OE2 GLU A   2     -35.751 -51.926-113.371  1.00139.64           O  
ANISOU   17  OE2 GLU A   2    17766  18438  16852    641  -1691    321       O  
ATOM     18  N   ALA A   3     -34.196 -55.022-108.567  1.00123.92           N  
ANISOU   18  N   ALA A   3    15391  16468  15225    546  -2094    386       N  
ATOM     19  CA  ALA A   3     -34.998 -55.947-107.773  1.00121.61           C  
ANISOU   19  CA  ALA A   3    15095  16141  14968    477  -2292    471       C  
ATOM     20  C   ALA A   3     -35.063 -55.548-106.307  1.00119.40           C  
ANISOU   20  C   ALA A   3    14657  15953  14754    394  -2290    539       C  
ATOM     21  O   ALA A   3     -35.326 -56.384-105.439  1.00120.61           O  
ANISOU   21  O   ALA A   3    14777  16090  14959    352  -2437    595       O  
ATOM     22  CB  ALA A   3     -34.454 -57.358-107.918  1.00126.26           C  
ANISOU   22  CB  ALA A   3    15756  16629  15585    547  -2425    418       C  
ATOM     23  N   ALA A   4     -34.857 -54.260-106.048  1.00115.78           N  
ANISOU   23  N   ALA A   4    14112  15587  14289    372  -2130    538       N  
ATOM     24  CA  ALA A   4     -34.647 -53.745-104.694  1.00111.74           C  
ANISOU   24  CA  ALA A   4    13456  15163  13835    316  -2100    578       C  
ATOM     25  C   ALA A   4     -35.646 -54.226-103.644  1.00108.65           C  
ANISOU   25  C   ALA A   4    13023  14792  13467    233  -2251    696       C  
ATOM     26  O   ALA A   4     -35.259 -54.493-102.510  1.00108.27           O  
ANISOU   26  O   ALA A   4    12878  14774  13483    212  -2291    713       O  
ATOM     27  CB  ALA A   4     -34.581 -52.225-104.712  1.00110.87           C  
ANISOU   27  CB  ALA A   4    13293  15137  13694    296  -1927    575       C  
ATOM     28  N   HIS A   5     -36.914 -54.355-104.024  1.00108.40           N  
ANISOU   28  N   HIS A   5    13058  14743  13383    188  -2335    781       N  
ATOM     29  CA  HIS A   5     -37.962 -54.774-103.088  1.00108.84           C  
ANISOU   29  CA  HIS A   5    13068  14829  13455    107  -2475    913       C  
ATOM     30  C   HIS A   5     -37.694 -56.152-102.486  1.00109.31           C  
ANISOU   30  C   HIS A   5    13119  14828  13583    103  -2640    925       C  
ATOM     31  O   HIS A   5     -37.905 -56.364-101.292  1.00108.46           O  
ANISOU   31  O   HIS A   5    12919  14771  13519     53  -2705   1000       O  
ATOM     32  CB  HIS A   5     -39.348 -54.732-103.752  1.00109.68           C  
ANISOU   32  CB  HIS A   5    13253  14923  13497     62  -2542   1006       C  
ATOM     33  CG  HIS A   5     -39.576 -55.817-104.760  1.00110.89           C  
ANISOU   33  CG  HIS A   5    13542  14953  13636     84  -2675    987       C  
ATOM     34  ND1 HIS A   5     -39.153 -55.719-106.068  1.00111.48           N  
ANISOU   34  ND1 HIS A   5    13734  14960  13662    157  -2609    886       N  
ATOM     35  CD2 HIS A   5     -40.184 -57.023-104.650  1.00110.91           C  
ANISOU   35  CD2 HIS A   5    13591  14885  13662     46  -2877   1059       C  
ATOM     36  CE1 HIS A   5     -39.489 -56.818-106.720  1.00112.36           C  
ANISOU   36  CE1 HIS A   5    13966  14961  13765    169  -2766    891       C  
ATOM     37  NE2 HIS A   5     -40.115 -57.626-105.882  1.00111.93           N  
ANISOU   37  NE2 HIS A   5    13871  14899  13757     98  -2935    995       N  
ATOM     38  N   SER A   6     -37.212 -57.070-103.322  1.00112.55           N  
ANISOU   38  N   SER A   6    13634  15132  13998    163  -2705    848       N  
ATOM     39  CA  SER A   6     -37.001 -58.464-102.939  1.00113.03           C  
ANISOU   39  CA  SER A   6    13718  15114  14114    167  -2880    853       C  
ATOM     40  C   SER A   6     -35.792 -58.630-102.043  1.00112.89           C  
ANISOU   40  C   SER A   6    13601  15120  14169    201  -2840    788       C  
ATOM     41  O   SER A   6     -35.698 -59.608-101.307  1.00115.72           O  
ANISOU   41  O   SER A   6    13938  15446  14584    183  -2978    818       O  
ATOM     42  CB  SER A   6     -36.840 -59.343-104.182  1.00114.93           C  
ANISOU   42  CB  SER A   6    14118  15225  14323    236  -2960    783       C  
ATOM     43  OG  SER A   6     -35.658 -59.014-104.891  1.00115.69           O  
ANISOU   43  OG  SER A   6    14241  15307  14405    341  -2813    645       O  
ATOM     44  N   LYS A   7     -34.876 -57.668-102.115  1.00111.77           N  
ANISOU   44  N   LYS A   7    13403  15036  14029    248  -2657    705       N  
ATOM     45  CA  LYS A   7     -33.622 -57.707-101.370  1.00109.62           C  
ANISOU   45  CA  LYS A   7    13034  14789  13827    285  -2603    635       C  
ATOM     46  C   LYS A   7     -33.697 -56.839-100.114  1.00107.19           C  
ANISOU   46  C   LYS A   7    12590  14588  13547    222  -2542    694       C  
ATOM     47  O   LYS A   7     -34.553 -55.962-100.017  1.00109.06           O  
ANISOU   47  O   LYS A   7    12811  14889  13736    170  -2493    764       O  
ATOM     48  CB  LYS A   7     -32.481 -57.280-102.286  1.00111.31           C  
ANISOU   48  CB  LYS A   7    13271  14991  14030    380  -2449    510       C  
ATOM     49  CG  LYS A   7     -32.269 -58.245-103.445  1.00116.62           C  
ANISOU   49  CG  LYS A   7    14083  15555  14672    465  -2513    443       C  
ATOM     50  CD  LYS A   7     -31.655 -57.563-104.656  1.00121.47           C  
ANISOU   50  CD  LYS A   7    14747  16170  15233    548  -2346    354       C  
ATOM     51  CE  LYS A   7     -31.069 -58.572-105.634  1.00124.93           C  
ANISOU   51  CE  LYS A   7    15307  16509  15649    664  -2393    267       C  
ATOM     52  NZ  LYS A   7     -29.811 -59.189-105.123  1.00126.88           N  
ANISOU   52  NZ  LYS A   7    15488  16750  15969    733  -2394    199       N  
ATOM     53  N   SER A   8     -32.811 -57.093 -99.154  1.00105.26           N  
ANISOU   53  N   SER A   8    12256  14362  13376    233  -2551    664       N  
ATOM     54  CA  SER A   8     -32.845 -56.418 -97.848  1.00104.03           C  
ANISOU   54  CA  SER A   8    11981  14296  13249    179  -2520    718       C  
ATOM     55  C   SER A   8     -32.371 -54.962 -97.900  1.00104.65           C  
ANISOU   55  C   SER A   8    12006  14447  13308    187  -2336    676       C  
ATOM     56  O   SER A   8     -31.680 -54.565 -98.840  1.00107.84           O  
ANISOU   56  O   SER A   8    12440  14832  13700    240  -2224    591       O  
ATOM     57  CB  SER A   8     -31.986 -57.186 -96.847  1.00101.65           C  
ANISOU   57  CB  SER A   8    11608  13981  13033    191  -2595    694       C  
ATOM     58  OG  SER A   8     -30.618 -56.876 -97.015  1.00100.13           O  
ANISOU   58  OG  SER A   8    11373  13788  12883    254  -2484    583       O  
ATOM     59  N   THR A   9     -32.727 -54.174 -96.884  1.00101.89           N  
ANISOU   59  N   THR A   9    11580  14178  12954    137  -2308    740       N  
ATOM     60  CA  THR A   9     -32.226 -52.803 -96.779  1.00 99.61           C  
ANISOU   60  CA  THR A   9    11242  13949  12654    140  -2154    702       C  
ATOM     61  C   THR A   9     -30.710 -52.819 -96.832  1.00101.81           C  
ANISOU   61  C   THR A   9    11472  14208  13004    189  -2087    596       C  
ATOM     62  O   THR A   9     -30.104 -52.022 -97.543  1.00104.91           O  
ANISOU   62  O   THR A   9    11866  14607  13385    216  -1955    533       O  
ATOM     63  CB  THR A   9     -32.655 -52.096 -95.478  1.00 97.58           C  
ANISOU   63  CB  THR A   9    10912  13773  12389     93  -2155    777       C  
ATOM     64  OG1 THR A   9     -32.085 -52.760 -94.344  1.00 95.52           O  
ANISOU   64  OG1 THR A   9    10580  13511  12201     90  -2240    779       O  
ATOM     65  CG2 THR A   9     -34.163 -52.052 -95.351  1.00 98.40           C  
ANISOU   65  CG2 THR A   9    11049  13915  12422     50  -2215    896       C  
ATOM     66  N   GLU A  10     -30.113 -53.741 -96.081  1.00103.21           N  
ANISOU   66  N   GLU A  10    11601  14360  13254    199  -2180    582       N  
ATOM     67  CA  GLU A  10     -28.667 -53.932 -96.053  1.00104.83           C  
ANISOU   67  CA  GLU A  10    11749  14544  13534    250  -2136    489       C  
ATOM     68  C   GLU A  10     -28.093 -54.242 -97.430  1.00106.08           C  
ANISOU   68  C   GLU A  10    11971  14651  13682    322  -2074    408       C  
ATOM     69  O   GLU A  10     -27.043 -53.717 -97.789  1.00108.03           O  
ANISOU   69  O   GLU A  10    12174  14912  13958    361  -1957    340       O  
ATOM     70  CB  GLU A  10     -28.296 -55.040 -95.069  1.00107.14           C  
ANISOU   70  CB  GLU A  10    11996  14811  13899    251  -2270    496       C  
ATOM     71  CG  GLU A  10     -27.639 -54.573 -93.778  1.00110.99           C  
ANISOU   71  CG  GLU A  10    12376  15347  14448    226  -2260    498       C  
ATOM     72  CD  GLU A  10     -28.489 -53.614 -92.958  1.00113.21           C  
ANISOU   72  CD  GLU A  10    12634  15697  14681    165  -2245    579       C  
ATOM     73  OE1 GLU A  10     -27.977 -52.522 -92.622  1.00114.48           O  
ANISOU   73  OE1 GLU A  10    12744  15900  14851    155  -2150    557       O  
ATOM     74  OE2 GLU A  10     -29.656 -53.948 -92.640  1.00113.61           O  
ANISOU   74  OE2 GLU A  10    12719  15760  14686    130  -2331    669       O  
ATOM     75  N   GLU A  11     -28.786 -55.084 -98.196  1.00106.81           N  
ANISOU   75  N   GLU A  11    12167  14683  13730    342  -2155    421       N  
ATOM     76  CA  GLU A  11     -28.340 -55.460 -99.540  1.00107.15           C  
ANISOU   76  CA  GLU A  11    12293  14671  13748    424  -2109    345       C  
ATOM     77  C   GLU A  11     -28.354 -54.264-100.485  1.00103.99           C  
ANISOU   77  C   GLU A  11    11916  14305  13288    433  -1946    323       C  
ATOM     78  O   GLU A  11     -27.426 -54.089-101.272  1.00105.18           O  
ANISOU   78  O   GLU A  11    12067  14450  13443    502  -1839    249       O  
ATOM     79  CB  GLU A  11     -29.196 -56.597-100.110  1.00112.80           C  
ANISOU   79  CB  GLU A  11    13131  15305  14422    437  -2252    371       C  
ATOM     80  CG  GLU A  11     -28.917 -57.970 -99.507  1.00119.20           C  
ANISOU   80  CG  GLU A  11    13941  16055  15291    456  -2412    368       C  
ATOM     81  CD  GLU A  11     -29.889 -59.041 -99.984  1.00123.05           C  
ANISOU   81  CD  GLU A  11    14555  16458  15739    450  -2575    410       C  
ATOM     82  OE1 GLU A  11     -30.562 -59.668 -99.135  1.00123.21           O  
ANISOU   82  OE1 GLU A  11    14562  16468  15782    386  -2722    491       O  
ATOM     83  OE2 GLU A  11     -29.983 -59.259-101.211  1.00125.86           O  
ANISOU   83  OE2 GLU A  11    15025  16755  16038    509  -2561    366       O  
ATOM     84  N   CYS A  12     -29.407 -53.449-100.388  1.00100.66           N  
ANISOU   84  N   CYS A  12    11512  13924  12810    365  -1927    393       N  
ATOM     85  CA  CYS A  12     -29.568 -52.239-101.202  1.00 97.79           C  
ANISOU   85  CA  CYS A  12    11175  13595  12385    362  -1781    383       C  
ATOM     86  C   CYS A  12     -28.510 -51.200-100.874  1.00 96.25           C  
ANISOU   86  C   CYS A  12    10879  13456  12234    360  -1646    343       C  
ATOM     87  O   CYS A  12     -27.853 -50.675-101.769  1.00 97.39           O  
ANISOU   87  O   CYS A  12    11031  13604  12365    402  -1520    289       O  
ATOM     88  CB  CYS A  12     -30.954 -51.626-101.001  1.00 97.06           C  
ANISOU   88  CB  CYS A  12    11115  13536  12225    291  -1805    473       C  
ATOM     89  SG  CYS A  12     -32.322 -52.662-101.562  1.00 99.84           S  
ANISOU   89  SG  CYS A  12    11588  13826  12520    279  -1957    537       S  
ATOM     90  N   LEU A  13     -28.350 -50.907 -99.585  1.00 94.24           N  
ANISOU   90  N   LEU A  13    10532  13243  12031    310  -1678    375       N  
ATOM     91  CA  LEU A  13     -27.328 -49.973 -99.126  1.00 91.72           C  
ANISOU   91  CA  LEU A  13    10115  12969  11763    299  -1576    344       C  
ATOM     92  C   LEU A  13     -25.962 -50.407 -99.635  1.00 93.65           C  
ANISOU   92  C   LEU A  13    10318  13193  12071    368  -1521    265       C  
ATOM     93  O   LEU A  13     -25.231 -49.601-100.208  1.00 95.99           O  
ANISOU   93  O   LEU A  13    10583  13513  12373    384  -1390    231       O  
ATOM     94  CB  LEU A  13     -27.339 -49.846 -97.597  1.00 87.87           C  
ANISOU   94  CB  LEU A  13     9547  12515  11324    247  -1650    387       C  
ATOM     95  CG  LEU A  13     -28.514 -49.062 -97.001  1.00 85.92           C  
ANISOU   95  CG  LEU A  13     9321  12311  11011    186  -1666    466       C  
ATOM     96  CD1 LEU A  13     -28.735 -49.431 -95.547  1.00 85.59           C  
ANISOU   96  CD1 LEU A  13     9225  12291  11004    154  -1779    517       C  
ATOM     97  CD2 LEU A  13     -28.335 -47.557 -97.149  1.00 85.20           C  
ANISOU   97  CD2 LEU A  13     9217  12260  10891    162  -1539    459       C  
ATOM     98  N   ALA A  14     -25.652 -51.691 -99.458  1.00 94.77           N  
ANISOU   98  N   ALA A  14    10461  13291  12255    413  -1623    242       N  
ATOM     99  CA  ALA A  14     -24.378 -52.273 -99.876  1.00 96.29           C  
ANISOU   99  CA  ALA A  14    10614  13464  12506    495  -1585    170       C  
ATOM    100  C   ALA A  14     -24.141 -52.147-101.374  1.00 97.55           C  
ANISOU  100  C   ALA A  14    10844  13610  12610    568  -1474    124       C  
ATOM    101  O   ALA A  14     -23.031 -51.848-101.809  1.00100.49           O  
ANISOU  101  O   ALA A  14    11156  14007  13018    618  -1362     80       O  
ATOM    102  CB  ALA A  14     -24.306 -53.731 -99.461  1.00 96.81           C  
ANISOU  102  CB  ALA A  14    10697  13476  12610    533  -1732    158       C  
ATOM    103  N   TYR A  15     -25.191 -52.380-102.153  1.00 97.19           N  
ANISOU  103  N   TYR A  15    10924  13527  12477    575  -1506    141       N  
ATOM    104  CA  TYR A  15     -25.121 -52.324-103.609  1.00 98.13           C  
ANISOU  104  CA  TYR A  15    11132  13624  12528    649  -1415    100       C  
ATOM    105  C   TYR A  15     -24.636 -50.962-104.105  1.00 97.87           C  
ANISOU  105  C   TYR A  15    11050  13651  12482    635  -1237     93       C  
ATOM    106  O   TYR A  15     -23.815 -50.886-105.016  1.00 99.43           O  
ANISOU  106  O   TYR A  15    11248  13857  12673    713  -1127     46       O  
ATOM    107  CB  TYR A  15     -26.494 -52.666-104.193  1.00 98.84           C  
ANISOU  107  CB  TYR A  15    11363  13662  12527    635  -1497    134       C  
ATOM    108  CG  TYR A  15     -26.614 -52.564-105.694  1.00 99.62           C  
ANISOU  108  CG  TYR A  15    11576  13733  12542    705  -1415     97       C  
ATOM    109  CD1 TYR A  15     -26.955 -51.364-106.296  1.00 99.97           C  
ANISOU  109  CD1 TYR A  15    11638  13816  12528    674  -1291    113       C  
ATOM    110  CD2 TYR A  15     -26.423 -53.677-106.506  1.00101.85           C  
ANISOU  110  CD2 TYR A  15    11959  13944  12795    808  -1470     46       C  
ATOM    111  CE1 TYR A  15     -27.078 -51.263-107.665  1.00103.01           C  
ANISOU  111  CE1 TYR A  15    12132  14175  12832    740  -1216     81       C  
ATOM    112  CE2 TYR A  15     -26.550 -53.588-107.881  1.00103.30           C  
ANISOU  112  CE2 TYR A  15    12258  14098  12891    880  -1398     12       C  
ATOM    113  CZ  TYR A  15     -26.877 -52.374-108.453  1.00103.99           C  
ANISOU  113  CZ  TYR A  15    12355  14230  12925    844  -1269     31       C  
ATOM    114  OH  TYR A  15     -27.012 -52.250-109.816  1.00107.71           O  
ANISOU  114  OH  TYR A  15    12943  14674  13307    916  -1195      0       O  
ATOM    115  N   PHE A  16     -25.143 -49.893-103.499  1.00 97.07           N  
ANISOU  115  N   PHE A  16    10912  13593  12375    541  -1212    143       N  
ATOM    116  CA  PHE A  16     -24.770 -48.538-103.892  1.00 97.08           C  
ANISOU  116  CA  PHE A  16    10874  13645  12364    514  -1060    145       C  
ATOM    117  C   PHE A  16     -23.581 -48.012-103.095  1.00 99.31           C  
ANISOU  117  C   PHE A  16    11012  13974  12745    488  -1009    138       C  
ATOM    118  O   PHE A  16     -23.085 -46.915-103.367  1.00102.24           O  
ANISOU  118  O   PHE A  16    11337  14386  13124    463   -889    142       O  
ATOM    119  CB  PHE A  16     -25.962 -47.586-103.751  1.00 94.14           C  
ANISOU  119  CB  PHE A  16    10552  13290  11924    434  -1058    202       C  
ATOM    120  CG  PHE A  16     -27.041 -47.805-104.776  1.00 92.83           C  
ANISOU  120  CG  PHE A  16    10524  13088  11657    456  -1072    212       C  
ATOM    121  CD1 PHE A  16     -26.796 -47.578-106.125  1.00 92.70           C  
ANISOU  121  CD1 PHE A  16    10572  13061  11587    516   -962    174       C  
ATOM    122  CD2 PHE A  16     -28.310 -48.223-104.391  1.00 91.61           C  
ANISOU  122  CD2 PHE A  16    10432  12912  11462    416  -1196    265       C  
ATOM    123  CE1 PHE A  16     -27.791 -47.776-107.066  1.00 92.15           C  
ANISOU  123  CE1 PHE A  16    10636  12951  11423    536   -982    182       C  
ATOM    124  CE2 PHE A  16     -29.308 -48.423-105.326  1.00 90.19           C  
ANISOU  124  CE2 PHE A  16    10376  12695  11195    430  -1219    280       C  
ATOM    125  CZ  PHE A  16     -29.048 -48.198-106.665  1.00 91.25           C  
ANISOU  125  CZ  PHE A  16    10582  12811  11275    490  -1115    235       C  
ATOM    126  N   GLY A  17     -23.128 -48.799-102.119  1.00 99.40           N  
ANISOU  126  N   GLY A  17    10955  13976  12834    492  -1108    131       N  
ATOM    127  CA  GLY A  17     -22.049 -48.404-101.217  1.00 97.51           C  
ANISOU  127  CA  GLY A  17    10578  13773  12695    461  -1089    129       C  
ATOM    128  C   GLY A  17     -22.327 -47.061-100.576  1.00 96.82           C  
ANISOU  128  C   GLY A  17    10458  13723  12606    366  -1056    173       C  
ATOM    129  O   GLY A  17     -21.485 -46.162-100.607  1.00 99.02           O  
ANISOU  129  O   GLY A  17    10659  14035  12928    341   -962    171       O  
ATOM    130  N   VAL A  18     -23.522 -46.920-100.012  1.00 95.17           N  
ANISOU  130  N   VAL A  18    10310  13507  12343    314  -1136    216       N  
ATOM    131  CA  VAL A  18     -23.952 -45.661 -99.411  1.00 94.00           C  
ANISOU  131  CA  VAL A  18    10154  13389  12172    236  -1114    258       C  
ATOM    132  C   VAL A  18     -24.223 -45.842 -97.921  1.00 93.03           C  
ANISOU  132  C   VAL A  18     9991  13271  12082    193  -1234    291       C  
ATOM    133  O   VAL A  18     -24.758 -46.866 -97.496  1.00 93.43           O  
ANISOU  133  O   VAL A  18    10066  13302  12130    208  -1345    306       O  
ATOM    134  CB  VAL A  18     -25.180 -45.066-100.146  1.00 93.89           C  
ANISOU  134  CB  VAL A  18    10252  13377  12045    221  -1075    288       C  
ATOM    135  CG1 VAL A  18     -26.351 -46.041-100.151  1.00 94.35           C  
ANISOU  135  CG1 VAL A  18    10393  13408  12047    236  -1184    315       C  
ATOM    136  CG2 VAL A  18     -25.582 -43.724 -99.550  1.00 93.03           C  
ANISOU  136  CG2 VAL A  18    10142  13298  11906    152  -1049    327       C  
ATOM    137  N   SER A  19     -23.824 -44.851 -97.133  1.00 93.03           N  
ANISOU  137  N   SER A  19     9935  13295  12115    141  -1217    306       N  
ATOM    138  CA  SER A  19     -24.011 -44.894 -95.693  1.00 93.60           C  
ANISOU  138  CA  SER A  19     9974  13374  12214    105  -1324    336       C  
ATOM    139  C   SER A  19     -25.367 -44.329 -95.375  1.00 92.75           C  
ANISOU  139  C   SER A  19     9946  13284  12007     76  -1351    392       C  
ATOM    140  O   SER A  19     -25.659 -43.196 -95.739  1.00 96.71           O  
ANISOU  140  O   SER A  19    10488  13802  12455     51  -1275    403       O  
ATOM    141  CB  SER A  19     -22.935 -44.072 -94.995  1.00 95.78           C  
ANISOU  141  CB  SER A  19    10161  13660  12568     67  -1302    325       C  
ATOM    142  OG  SER A  19     -23.267 -43.879 -93.635  1.00 98.21           O  
ANISOU  142  OG  SER A  19    10462  13975  12877     34  -1398    357       O  
ATOM    143  N   GLU A  20     -26.200 -45.108 -94.698  1.00 92.25           N  
ANISOU  143  N   GLU A  20     9907  13223  11919     80  -1459    431       N  
ATOM    144  CA  GLU A  20     -27.581 -44.691 -94.449  1.00 93.45           C  
ANISOU  144  CA  GLU A  20    10130  13402  11972     62  -1485    497       C  
ATOM    145  C   GLU A  20     -27.641 -43.421 -93.603  1.00 93.34           C  
ANISOU  145  C   GLU A  20    10113  13418  11932     30  -1467    519       C  
ATOM    146  O   GLU A  20     -28.530 -42.578 -93.764  1.00 92.21           O  
ANISOU  146  O   GLU A  20    10036  13300  11700     21  -1431    556       O  
ATOM    147  CB  GLU A  20     -28.356 -45.816 -93.774  1.00 93.31           C  
ANISOU  147  CB  GLU A  20    10120  13387  11946     70  -1611    547       C  
ATOM    148  CG  GLU A  20     -29.720 -45.403 -93.262  1.00 93.58           C  
ANISOU  148  CG  GLU A  20    10203  13465  11886     54  -1645    630       C  
ATOM    149  CD  GLU A  20     -30.453 -46.546 -92.612  1.00 96.14           C  
ANISOU  149  CD  GLU A  20    10523  13796  12208     55  -1770    693       C  
ATOM    150  OE1 GLU A  20     -29.781 -47.472 -92.105  1.00 97.24           O  
ANISOU  150  OE1 GLU A  20    10610  13910  12426     62  -1843    670       O  
ATOM    151  OE2 GLU A  20     -31.702 -46.515 -92.612  1.00 99.24           O  
ANISOU  151  OE2 GLU A  20    10961  14222  12521     49  -1797    770       O  
ATOM    152  N   THR A  21     -26.664 -43.300 -92.714  1.00 94.32           N  
ANISOU  152  N   THR A  21    10166  13535  12135     17  -1498    496       N  
ATOM    153  CA  THR A  21     -26.585 -42.211 -91.756  1.00 93.39           C  
ANISOU  153  CA  THR A  21    10048  13432  12003     -9  -1507    512       C  
ATOM    154  C   THR A  21     -25.947 -40.965 -92.382  1.00 90.96           C  
ANISOU  154  C   THR A  21     9745  13113  11701    -35  -1404    480       C  
ATOM    155  O   THR A  21     -25.944 -39.892 -91.790  1.00 91.30           O  
ANISOU  155  O   THR A  21     9810  13159  11718    -59  -1404    492       O  
ATOM    156  CB  THR A  21     -25.830 -42.681 -90.482  1.00 95.08           C  
ANISOU  156  CB  THR A  21    10189  13637  12300    -13  -1602    504       C  
ATOM    157  OG1 THR A  21     -25.718 -41.605 -89.549  1.00 99.24           O  
ANISOU  157  OG1 THR A  21    10727  14168  12808    -34  -1620    515       O  
ATOM    158  CG2 THR A  21     -24.434 -43.214 -90.811  1.00 95.51           C  
ANISOU  158  CG2 THR A  21    10154  13660  12474    -13  -1586    444       C  
ATOM    159  N   THR A  22     -25.454 -41.111 -93.606  1.00 89.93           N  
ANISOU  159  N   THR A  22     9602  12969  11598    -29  -1319    444       N  
ATOM    160  CA  THR A  22     -24.631 -40.093 -94.246  1.00 88.66           C  
ANISOU  160  CA  THR A  22     9423  12798  11464    -57  -1221    417       C  
ATOM    161  C   THR A  22     -25.153 -39.672 -95.616  1.00 88.33           C  
ANISOU  161  C   THR A  22     9450  12761  11349    -48  -1115    416       C  
ATOM    162  O   THR A  22     -25.275 -38.483 -95.902  1.00 87.94           O  
ANISOU  162  O   THR A  22     9443  12714  11257    -77  -1054    425       O  
ATOM    163  CB  THR A  22     -23.181 -40.592 -94.337  1.00 87.81           C  
ANISOU  163  CB  THR A  22     9206  12676  11481    -57  -1208    376       C  
ATOM    164  OG1 THR A  22     -22.590 -40.484 -93.042  1.00 89.58           O  
ANISOU  164  OG1 THR A  22     9371  12891  11772    -83  -1294    379       O  
ATOM    165  CG2 THR A  22     -22.363 -39.794 -95.315  1.00 87.71           C  
ANISOU  165  CG2 THR A  22     9165  12661  11498    -77  -1091    358       C  
ATOM    166  N   GLY A  23     -25.472 -40.656 -96.446  1.00 88.74           N  
ANISOU  166  N   GLY A  23     9521  12810  11385     -7  -1103    405       N  
ATOM    167  CA  GLY A  23     -25.893 -40.404 -97.808  1.00 89.53           C  
ANISOU  167  CA  GLY A  23     9689  12909  11420      8  -1007    399       C  
ATOM    168  C   GLY A  23     -24.677 -40.404 -98.694  1.00 90.52           C  
ANISOU  168  C   GLY A  23     9755  13026  11611     21   -913    356       C  
ATOM    169  O   GLY A  23     -23.574 -40.686 -98.232  1.00 90.47           O  
ANISOU  169  O   GLY A  23     9653  13018  11704     18   -930    336       O  
ATOM    170  N   LEU A  24     -24.881 -40.088 -99.968  1.00 93.22           N  
ANISOU  170  N   LEU A  24    10152  13367  11897     38   -814    347       N  
ATOM    171  CA  LEU A  24     -23.801 -40.117-100.948  1.00 95.85           C  
ANISOU  171  CA  LEU A  24    10436  13703  12279     64   -710    314       C  
ATOM    172  C   LEU A  24     -22.824 -38.956-100.789  1.00 98.97           C  
ANISOU  172  C   LEU A  24    10760  14111  12733      8   -645    322       C  
ATOM    173  O   LEU A  24     -23.205 -37.848-100.396  1.00 98.17           O  
ANISOU  173  O   LEU A  24    10694  14009  12596    -46   -647    349       O  
ATOM    174  CB  LEU A  24     -24.357 -40.120-102.372  1.00 94.69           C  
ANISOU  174  CB  LEU A  24    10380  13551  12045    103   -624    306       C  
ATOM    175  CG  LEU A  24     -25.282 -41.234-102.854  1.00 93.46           C  
ANISOU  175  CG  LEU A  24    10309  13373  11827    159   -679    298       C  
ATOM    176  CD1 LEU A  24     -25.799 -40.847-104.226  1.00 94.41           C  
ANISOU  176  CD1 LEU A  24    10525  13487  11857    184   -584    294       C  
ATOM    177  CD2 LEU A  24     -24.589 -42.584-102.917  1.00 94.31           C  
ANISOU  177  CD2 LEU A  24    10370  13464  11997    223   -720    261       C  
ATOM    178  N   THR A  25     -21.560 -39.232-101.095  1.00103.75           N  
ANISOU  178  N   THR A  25    11266  14728  13427     26   -593    303       N  
ATOM    179  CA  THR A  25     -20.525 -38.207-101.144  1.00107.55           C  
ANISOU  179  CA  THR A  25    11667  15223  13973    -26   -523    320       C  
ATOM    180  C   THR A  25     -20.716 -37.392-102.418  1.00111.13           C  
ANISOU  180  C   THR A  25    12179  15687  14358    -29   -396    331       C  
ATOM    181  O   THR A  25     -21.202 -37.929-103.416  1.00112.75           O  
ANISOU  181  O   THR A  25    12451  15892  14494     33   -345    312       O  
ATOM    182  CB  THR A  25     -19.114 -38.827-101.135  1.00107.18           C  
ANISOU  182  CB  THR A  25    11483  15196  14044      0   -501    306       C  
ATOM    183  OG1 THR A  25     -19.019 -39.819-102.164  1.00108.05           O  
ANISOU  183  OG1 THR A  25    11606  15316  14131     93   -442    276       O  
ATOM    184  CG2 THR A  25     -18.814 -39.463 -99.784  1.00106.00           C  
ANISOU  184  CG2 THR A  25    11269  15034  13973    -10   -630    299       C  
ATOM    185  N   PRO A  26     -20.333 -36.098-102.398  1.00113.62           N  
ANISOU  185  N   PRO A  26    12475  16005  14690   -101   -350    362       N  
ATOM    186  CA  PRO A  26     -20.494 -35.242-103.578  1.00114.85           C  
ANISOU  186  CA  PRO A  26    12685  16169  14781   -111   -230    377       C  
ATOM    187  C   PRO A  26     -19.863 -35.872-104.817  1.00116.49           C  
ANISOU  187  C   PRO A  26    12855  16406  14997    -38   -116    363       C  
ATOM    188  O   PRO A  26     -20.237 -35.548-105.949  1.00114.62           O  
ANISOU  188  O   PRO A  26    12691  16176  14682    -15    -20    364       O  
ATOM    189  CB  PRO A  26     -19.731 -33.975-103.195  1.00115.69           C  
ANISOU  189  CB  PRO A  26    12732  16274  14951   -203   -216    416       C  
ATOM    190  CG  PRO A  26     -19.742 -33.963-101.708  1.00115.80           C  
ANISOU  190  CG  PRO A  26    12721  16264  15013   -244   -351    418       C  
ATOM    191  CD  PRO A  26     -19.625 -35.398-101.311  1.00114.90           C  
ANISOU  191  CD  PRO A  26    12559  16158  14938   -178   -411    385       C  
ATOM    192  N   ASP A  27     -18.912 -36.772-104.578  1.00119.10           N  
ANISOU  192  N   ASP A  27    13077  16756  15419      2   -129    348       N  
ATOM    193  CA  ASP A  27     -18.243 -37.516-105.628  1.00120.46           C  
ANISOU  193  CA  ASP A  27    13209  16960  15600     92    -31    331       C  
ATOM    194  C   ASP A  27     -19.142 -38.627-106.161  1.00117.10           C  
ANISOU  194  C   ASP A  27    12894  16511  15086    185    -58    286       C  
ATOM    195  O   ASP A  27     -19.321 -38.756-107.372  1.00118.22           O  
ANISOU  195  O   ASP A  27    13100  16661  15155    248     34    274       O  
ATOM    196  CB  ASP A  27     -16.931 -38.097-105.103  1.00123.72           C  
ANISOU  196  CB  ASP A  27    13465  17400  16140    109    -46    332       C  
ATOM    197  CG  ASP A  27     -16.021 -38.552-106.214  1.00128.40           C  
ANISOU  197  CG  ASP A  27    13994  18041  16749    197     80    331       C  
ATOM    198  OD1 ASP A  27     -15.356 -37.687-106.820  1.00131.04           O  
ANISOU  198  OD1 ASP A  27    14268  18414  17106    165    191    376       O  
ATOM    199  OD2 ASP A  27     -15.974 -39.772-106.483  1.00131.19           O  
ANISOU  199  OD2 ASP A  27    14361  18394  17090    301     67    289       O  
ATOM    200  N   GLN A  28     -19.698 -39.428-105.253  1.00113.58           N  
ANISOU  200  N   GLN A  28    12472  16035  14645    192   -189    264       N  
ATOM    201  CA  GLN A  28     -20.643 -40.474-105.622  1.00111.04           C  
ANISOU  201  CA  GLN A  28    12260  15683  14245    264   -242    232       C  
ATOM    202  C   GLN A  28     -21.782 -39.886-106.433  1.00111.77           C  
ANISOU  202  C   GLN A  28    12488  15760  14217    255   -201    241       C  
ATOM    203  O   GLN A  28     -22.062 -40.354-107.533  1.00113.05           O  
ANISOU  203  O   GLN A  28    12728  15913  14310    328   -149    219       O  
ATOM    204  CB  GLN A  28     -21.190 -41.174-104.384  1.00108.45           C  
ANISOU  204  CB  GLN A  28    11937  15329  13940    245   -397    227       C  
ATOM    205  CG  GLN A  28     -20.344 -42.343-103.930  1.00108.99           C  
ANISOU  205  CG  GLN A  28    11919  15396  14095    300   -453    199       C  
ATOM    206  CD  GLN A  28     -20.828 -42.939-102.629  1.00107.80           C  
ANISOU  206  CD  GLN A  28    11765  15221  13973    272   -606    202       C  
ATOM    207  OE1 GLN A  28     -21.063 -42.226-101.657  1.00108.29           O  
ANISOU  207  OE1 GLN A  28    11807  15286  14051    194   -656    232       O  
ATOM    208  NE2 GLN A  28     -20.968 -44.258-102.600  1.00108.21           N  
ANISOU  208  NE2 GLN A  28    11840  15247  14026    338   -683    174       N  
ATOM    209  N   VAL A  29     -22.414 -38.845-105.889  1.00112.66           N  
ANISOU  209  N   VAL A  29    12632  15869  14303    171   -226    273       N  
ATOM    210  CA  VAL A  29     -23.472 -38.100-106.577  1.00111.22           C  
ANISOU  210  CA  VAL A  29    12570  15676  14010    153   -184    289       C  
ATOM    211  C   VAL A  29     -23.064 -37.795-108.021  1.00114.05           C  
ANISOU  211  C   VAL A  29    12954  16050  14330    195    -41    281       C  
ATOM    212  O   VAL A  29     -23.827 -38.058-108.947  1.00114.19           O  
ANISOU  212  O   VAL A  29    13081  16050  14254    243    -16    268       O  
ATOM    213  CB  VAL A  29     -23.835 -36.797-105.818  1.00108.21           C  
ANISOU  213  CB  VAL A  29    12196  15296  13620     60   -206    326       C  
ATOM    214  CG1 VAL A  29     -24.669 -35.864-106.681  1.00109.22           C  
ANISOU  214  CG1 VAL A  29    12434  15419  13643     44   -136    342       C  
ATOM    215  CG2 VAL A  29     -24.585 -37.114-104.536  1.00105.30           C  
ANISOU  215  CG2 VAL A  29    11841  14915  13251     36   -344    337       C  
ATOM    216  N   LYS A  30     -21.850 -37.273-108.197  1.00117.84           N  
ANISOU  216  N   LYS A  30    13329  16563  14881    178     48    295       N  
ATOM    217  CA  LYS A  30     -21.309 -36.949-109.517  1.00119.87           C  
ANISOU  217  CA  LYS A  30    13588  16846  15109    220    195    299       C  
ATOM    218  C   LYS A  30     -21.218 -38.177-110.423  1.00118.78           C  
ANISOU  218  C   LYS A  30    13491  16706  14933    343    225    257       C  
ATOM    219  O   LYS A  30     -21.741 -38.164-111.536  1.00119.12           O  
ANISOU  219  O   LYS A  30    13640  16738  14879    394    289    246       O  
ATOM    220  CB  LYS A  30     -19.937 -36.276-109.382  1.00124.37           C  
ANISOU  220  CB  LYS A  30    14013  17460  15782    176    271    335       C  
ATOM    221  CG  LYS A  30     -19.378 -35.706-110.676  1.00128.23           C  
ANISOU  221  CG  LYS A  30    14493  17986  16241    201    431    359       C  
ATOM    222  CD  LYS A  30     -17.915 -35.330-110.517  1.00131.94           C  
ANISOU  222  CD  LYS A  30    14795  18508  16828    170    497    403       C  
ATOM    223  CE  LYS A  30     -17.295 -34.952-111.852  1.00135.80           C  
ANISOU  223  CE  LYS A  30    15263  19047  17288    213    664    434       C  
ATOM    224  NZ  LYS A  30     -15.812 -34.830-111.763  1.00138.36           N  
ANISOU  224  NZ  LYS A  30    15405  19434  17731    203    731    483       N  
ATOM    225  N   ARG A  31     -20.563 -39.232-109.938  1.00119.19           N  
ANISOU  225  N   ARG A  31    13465  16762  15057    396    172    233       N  
ATOM    226  CA  ARG A  31     -20.371 -40.457-110.719  1.00120.35           C  
ANISOU  226  CA  ARG A  31    13653  16902  15173    524    188    189       C  
ATOM    227  C   ARG A  31     -21.684 -41.180-110.990  1.00115.97           C  
ANISOU  227  C   ARG A  31    13255  16288  14520    562     97    158       C  
ATOM    228  O   ARG A  31     -21.884 -41.721-112.073  1.00116.95           O  
ANISOU  228  O   ARG A  31    13474  16394  14567    655    138    129       O  
ATOM    229  CB  ARG A  31     -19.392 -41.406-110.027  1.00126.55           C  
ANISOU  229  CB  ARG A  31    14320  17701  16060    568    138    170       C  
ATOM    230  CG  ARG A  31     -17.940 -40.955-110.056  1.00134.85           C  
ANISOU  230  CG  ARG A  31    15211  18818  17206    565    243    200       C  
ATOM    231  CD  ARG A  31     -17.007 -42.015-109.482  1.00143.29           C  
ANISOU  231  CD  ARG A  31    16173  19901  18368    628    194    178       C  
ATOM    232  NE  ARG A  31     -17.196 -42.224-108.044  1.00147.51           N  
ANISOU  232  NE  ARG A  31    16664  20408  18976    553     47    177       N  
ATOM    233  CZ  ARG A  31     -17.856 -43.249-107.506  1.00148.54           C  
ANISOU  233  CZ  ARG A  31    16860  20489  19090    582    -84    141       C  
ATOM    234  NH1 ARG A  31     -18.402 -44.183-108.278  1.00150.83           N  
ANISOU  234  NH1 ARG A  31    17267  20743  19296    681   -100     99       N  
ATOM    235  NH2 ARG A  31     -17.969 -43.340-106.189  1.00147.22           N  
ANISOU  235  NH2 ARG A  31    16644  20304  18989    511   -206    149       N  
ATOM    236  N   HIS A  32     -22.565 -41.188-109.995  1.00112.16           N  
ANISOU  236  N   HIS A  32    12799  15776  14041    491    -29    170       N  
ATOM    237  CA  HIS A  32     -23.887 -41.791-110.114  1.00109.83           C  
ANISOU  237  CA  HIS A  32    12638  15429  13662    506   -130    160       C  
ATOM    238  C   HIS A  32     -24.751 -41.036-111.119  1.00111.04           C  
ANISOU  238  C   HIS A  32    12911  15572  13706    497    -62    173       C  
ATOM    239  O   HIS A  32     -25.576 -41.632-111.816  1.00111.35           O  
ANISOU  239  O   HIS A  32    13074  15570  13663    548   -100    156       O  
ATOM    240  CB  HIS A  32     -24.589 -41.772-108.762  1.00106.85           C  
ANISOU  240  CB  HIS A  32    12242  15040  13315    424   -264    188       C  
ATOM    241  CG  HIS A  32     -24.208 -42.896-107.855  1.00104.81           C  
ANISOU  241  CG  HIS A  32    11919  14768  13133    447   -375    171       C  
ATOM    242  ND1 HIS A  32     -25.084 -43.903-107.520  1.00103.94           N  
ANISOU  242  ND1 HIS A  32    11878  14617  12998    463   -510    169       N  
ATOM    243  CD2 HIS A  32     -23.058 -43.162-107.194  1.00107.02           C  
ANISOU  243  CD2 HIS A  32    12072  15072  13518    453   -378    160       C  
ATOM    244  CE1 HIS A  32     -24.487 -44.748-106.699  1.00106.21           C  
ANISOU  244  CE1 HIS A  32    12087  14899  13367    479   -589    154       C  
ATOM    245  NE2 HIS A  32     -23.256 -44.322-106.484  1.00106.98           N  
ANISOU  245  NE2 HIS A  32    12066  15036  13544    476   -511    146       N  
ATOM    246  N   LEU A  33     -24.565 -39.718-111.169  1.00111.85           N  
ANISOU  246  N   LEU A  33    12980  15707  13809    429     27    205       N  
ATOM    247  CA  LEU A  33     -25.305 -38.848-112.075  1.00112.09           C  
ANISOU  247  CA  LEU A  33    13115  15732  13742    412     99    220       C  
ATOM    248  C   LEU A  33     -24.861 -39.100-113.502  1.00114.45           C  
ANISOU  248  C   LEU A  33    13464  16033  13986    507    215    193       C  
ATOM    249  O   LEU A  33     -25.684 -39.154-114.412  1.00114.48           O  
ANISOU  249  O   LEU A  33    13600  16007  13890    543    226    184       O  
ATOM    250  CB  LEU A  33     -25.083 -37.381-111.695  1.00112.11           C  
ANISOU  250  CB  LEU A  33    13062  15764  13767    315    159    261       C  
ATOM    251  CG  LEU A  33     -26.047 -36.289-112.158  1.00111.35           C  
ANISOU  251  CG  LEU A  33    13068  15659  13578    267    195    286       C  
ATOM    252  CD1 LEU A  33     -27.485 -36.786-112.236  1.00111.66           C  
ANISOU  252  CD1 LEU A  33    13232  15661  13532    284    100    284       C  
ATOM    253  CD2 LEU A  33     -25.935 -35.089-111.226  1.00109.73           C  
ANISOU  253  CD2 LEU A  33    12805  15470  13415    166    185    324       C  
ATOM    254  N   GLU A  34     -23.550 -39.256-113.675  1.00118.22           N  
ANISOU  254  N   GLU A  34    13837  16551  14530    551    299    185       N  
ATOM    255  CA  GLU A  34     -22.951 -39.660-114.940  1.00121.06           C  
ANISOU  255  CA  GLU A  34    14227  16923  14844    664    410    161       C  
ATOM    256  C   GLU A  34     -23.542 -41.000-115.381  1.00117.52           C  
ANISOU  256  C   GLU A  34    13900  16418  14333    767    324    111       C  
ATOM    257  O   GLU A  34     -24.087 -41.116-116.475  1.00118.78           O  
ANISOU  257  O   GLU A  34    14192  16549  14389    829    359     93       O  
ATOM    258  CB  GLU A  34     -21.427 -39.765-114.780  1.00127.31           C  
ANISOU  258  CB  GLU A  34    14861  17775  15735    697    490    168       C  
ATOM    259  CG  GLU A  34     -20.648 -40.006-116.066  1.00136.56           C  
ANISOU  259  CG  GLU A  34    16041  18982  16864    818    633    157       C  
ATOM    260  CD  GLU A  34     -20.631 -38.798-116.989  1.00143.19           C  
ANISOU  260  CD  GLU A  34    16904  19853  17646    788    776    196       C  
ATOM    261  OE1 GLU A  34     -20.426 -37.666-116.496  1.00146.94           O  
ANISOU  261  OE1 GLU A  34    17298  20355  18175    671    804    247       O  
ATOM    262  OE2 GLU A  34     -20.814 -38.982-118.213  1.00146.43           O  
ANISOU  262  OE2 GLU A  34    17421  20257  17955    882    855    177       O  
ATOM    263  N   LYS A  35     -23.455 -41.986-114.495  1.00115.22           N  
ANISOU  263  N   LYS A  35    13567  16105  14103    779    202     91       N  
ATOM    264  CA  LYS A  35     -23.867 -43.363-114.756  1.00113.03           C  
ANISOU  264  CA  LYS A  35    13390  15768  13786    872     98     46       C  
ATOM    265  C   LYS A  35     -25.355 -43.513-115.065  1.00109.86           C  
ANISOU  265  C   LYS A  35    13147  15302  13290    851      3     49       C  
ATOM    266  O   LYS A  35     -25.728 -44.215-116.004  1.00109.56           O  
ANISOU  266  O   LYS A  35    13241  15216  13171    941    -16     16       O  
ATOM    267  CB  LYS A  35     -23.501 -44.227-113.544  1.00114.13           C  
ANISOU  267  CB  LYS A  35    13439  15901  14025    862    -22     37       C  
ATOM    268  CG  LYS A  35     -23.609 -45.731-113.727  1.00115.12           C  
ANISOU  268  CG  LYS A  35    13643  15966  14129    966   -129    -10       C  
ATOM    269  CD  LYS A  35     -23.344 -46.426-112.399  1.00116.40           C  
ANISOU  269  CD  LYS A  35    13709  16122  14392    932   -254     -9       C  
ATOM    270  CE  LYS A  35     -22.915 -47.871-112.577  1.00119.15           C  
ANISOU  270  CE  LYS A  35    14095  16429  14747   1052   -327    -61       C  
ATOM    271  NZ  LYS A  35     -23.965 -48.677-113.256  1.00121.04           N  
ANISOU  271  NZ  LYS A  35    14515  16583  14889   1103   -429    -83       N  
ATOM    272  N   TYR A  36     -26.196 -42.849-114.276  1.00108.28           N  
ANISOU  272  N   TYR A  36    12936  15104  13099    736    -59     91       N  
ATOM    273  CA  TYR A  36     -27.638 -43.088-114.310  1.00106.69           C  
ANISOU  273  CA  TYR A  36    12859  14850  12827    705   -174    108       C  
ATOM    274  C   TYR A  36     -28.477 -41.960-114.909  1.00107.32           C  
ANISOU  274  C   TYR A  36    13015  14935  12824    654   -110    138       C  
ATOM    275  O   TYR A  36     -29.665 -42.151-115.172  1.00105.90           O  
ANISOU  275  O   TYR A  36    12948  14713  12575    642   -191    154       O  
ATOM    276  CB  TYR A  36     -28.151 -43.394-112.904  1.00104.38           C  
ANISOU  276  CB  TYR A  36    12507  14553  12597    627   -317    140       C  
ATOM    277  CG  TYR A  36     -27.654 -44.691-112.308  1.00103.57           C  
ANISOU  277  CG  TYR A  36    12361  14427  12562    674   -420    113       C  
ATOM    278  CD1 TYR A  36     -27.921 -45.915-112.922  1.00104.29           C  
ANISOU  278  CD1 TYR A  36    12559  14453  12611    759   -503     79       C  
ATOM    279  CD2 TYR A  36     -26.945 -44.698-111.113  1.00102.36           C  
ANISOU  279  CD2 TYR A  36    12069  14310  12513    632   -447    122       C  
ATOM    280  CE1 TYR A  36     -27.476 -47.105-112.371  1.00104.22           C  
ANISOU  280  CE1 TYR A  36    12518  14416  12662    803   -605     54       C  
ATOM    281  CE2 TYR A  36     -26.501 -45.883-110.552  1.00102.93           C  
ANISOU  281  CE2 TYR A  36    12103  14359  12647    675   -544     98       C  
ATOM    282  CZ  TYR A  36     -26.768 -47.081-111.184  1.00103.92           C  
ANISOU  282  CZ  TYR A  36    12335  14419  12728    760   -622     64       C  
ATOM    283  OH  TYR A  36     -26.328 -48.258-110.628  1.00105.95           O  
ANISOU  283  OH  TYR A  36    12562  14649  13045    804   -725     39       O  
ATOM    284  N   GLY A  37     -27.869 -40.792-115.104  1.00110.32           N  
ANISOU  284  N   GLY A  37    13335  15367  13215    621     26    152       N  
ATOM    285  CA  GLY A  37     -28.571 -39.631-115.655  1.00111.84           C  
ANISOU  285  CA  GLY A  37    13596  15566  13332    571     93    181       C  
ATOM    286  C   GLY A  37     -29.458 -38.923-114.644  1.00112.55           C  
ANISOU  286  C   GLY A  37    13668  15665  13429    466     19    228       C  
ATOM    287  O   GLY A  37     -29.650 -39.407-113.524  1.00115.15           O  
ANISOU  287  O   GLY A  37    13941  15994  13815    432    -92    242       O  
ATOM    288  N   HIS A  38     -29.997 -37.773-115.045  1.00111.91           N  
ANISOU  288  N   HIS A  38    13639  15595  13287    420     84    255       N  
ATOM    289  CA  HIS A  38     -30.916 -37.004-114.208  1.00109.37           C  
ANISOU  289  CA  HIS A  38    13319  15285  12952    335     25    301       C  
ATOM    290  C   HIS A  38     -32.226 -37.749-114.010  1.00109.47           C  
ANISOU  290  C   HIS A  38    13410  15265  12918    338   -110    321       C  
ATOM    291  O   HIS A  38     -32.682 -38.464-114.899  1.00109.77           O  
ANISOU  291  O   HIS A  38    13547  15261  12899    394   -136    304       O  
ATOM    292  CB  HIS A  38     -31.201 -35.639-114.828  1.00109.91           C  
ANISOU  292  CB  HIS A  38    13440  15366  12955    298    126    321       C  
ATOM    293  CG  HIS A  38     -29.997 -34.758-114.934  1.00112.25           C  
ANISOU  293  CG  HIS A  38    13653  15695  13299    274    250    319       C  
ATOM    294  ND1 HIS A  38     -29.344 -34.254-113.830  1.00113.01           N  
ANISOU  294  ND1 HIS A  38    13634  15819  13482    212    237    336       N  
ATOM    295  CD2 HIS A  38     -29.335 -34.280-116.014  1.00113.62           C  
ANISOU  295  CD2 HIS A  38    13842  15879  13449    302    384    309       C  
ATOM    296  CE1 HIS A  38     -28.327 -33.509-114.224  1.00114.16           C  
ANISOU  296  CE1 HIS A  38    13724  15989  13660    195    352    340       C  
ATOM    297  NE2 HIS A  38     -28.300 -33.508-115.545  1.00115.35           N  
ANISOU  297  NE2 HIS A  38    13948  16134  13745    249    448    327       N  
ATOM    298  N   ASN A  39     -32.821 -37.578-112.833  1.00111.61           N  
ANISOU  298  N   ASN A  39    13638  15556  13213    279   -199    363       N  
ATOM    299  CA  ASN A  39     -34.101 -38.189-112.509  1.00110.95           C  
ANISOU  299  CA  ASN A  39    13609  15456  13092    271   -329    403       C  
ATOM    300  C   ASN A  39     -35.200 -37.456-113.255  1.00112.62           C  
ANISOU  300  C   ASN A  39    13927  15660  13200    258   -304    433       C  
ATOM    301  O   ASN A  39     -35.801 -36.519-112.722  1.00113.01           O  
ANISOU  301  O   ASN A  39    13970  15743  13223    210   -301    475       O  
ATOM    302  CB  ASN A  39     -34.343 -38.146-110.997  1.00109.20           C  
ANISOU  302  CB  ASN A  39    13299  15269  12921    219   -418    446       C  
ATOM    303  CG  ASN A  39     -35.716 -38.665-110.598  1.00109.42           C  
ANISOU  303  CG  ASN A  39    13368  15294  12909    204   -545    506       C  
ATOM    304  OD1 ASN A  39     -36.260 -39.585-111.212  1.00110.05           O  
ANISOU  304  OD1 ASN A  39    13517  15334  12961    233   -613    510       O  
ATOM    305  ND2 ASN A  39     -36.281 -38.072-109.555  1.00109.12           N  
ANISOU  305  ND2 ASN A  39    13290  15302  12868    160   -582    560       N  
ATOM    306  N   GLU A  40     -35.430 -37.881-114.499  1.00115.30           N  
ANISOU  306  N   GLU A  40    14370  15957  13481    309   -285    408       N  
ATOM    307  CA  GLU A  40     -36.418 -37.263-115.391  1.00118.90           C  
ANISOU  307  CA  GLU A  40    14939  16398  13837    306   -258    430       C  
ATOM    308  C   GLU A  40     -36.592 -38.058-116.672  1.00123.71           C  
ANISOU  308  C   GLU A  40    15664  16947  14391    373   -269    397       C  
ATOM    309  O   GLU A  40     -35.743 -38.877-117.025  1.00126.03           O  
ANISOU  309  O   GLU A  40    15954  17214  14716    432   -259    347       O  
ATOM    310  CB  GLU A  40     -36.021 -35.823-115.750  1.00115.96           C  
ANISOU  310  CB  GLU A  40    14566  16055  13436    282   -117    423       C  
ATOM    311  CG  GLU A  40     -34.805 -35.697-116.655  1.00114.73           C  
ANISOU  311  CG  GLU A  40    14408  15892  13291    327     12    368       C  
ATOM    312  CD  GLU A  40     -34.229 -34.295-116.665  1.00115.64           C  
ANISOU  312  CD  GLU A  40    14485  16042  13408    283    135    374       C  
ATOM    313  OE1 GLU A  40     -34.895 -33.374-116.149  1.00115.45           O  
ANISOU  313  OE1 GLU A  40    14468  16038  13358    228    121    412       O  
ATOM    314  OE2 GLU A  40     -33.110 -34.111-117.187  1.00116.38           O  
ANISOU  314  OE2 GLU A  40    14543  16145  13530    307    244    344       O  
ATOM    315  N   LEU A  41     -37.702 -37.808-117.360  1.00130.35           N  
ANISOU  315  N   LEU A  41    16614  17766  15147    368   -293    426       N  
ATOM    316  CA  LEU A  41     -37.887 -38.281-118.723  1.00136.23           C  
ANISOU  316  CA  LEU A  41    17490  18449  15821    432   -285    392       C  
ATOM    317  C   LEU A  41     -37.086 -37.355-119.640  1.00141.03           C  
ANISOU  317  C   LEU A  41    18123  19069  16391    462   -112    350       C  
ATOM    318  O   LEU A  41     -36.949 -36.166-119.338  1.00145.01           O  
ANISOU  318  O   LEU A  41    18578  19620  16897    412    -26    369       O  
ATOM    319  CB  LEU A  41     -39.371 -38.266-119.102  1.00135.71           C  
ANISOU  319  CB  LEU A  41    17525  18356  15680    409   -375    445       C  
ATOM    320  CG  LEU A  41     -40.291 -39.301-118.446  1.00136.89           C  
ANISOU  320  CG  LEU A  41    17670  18486  15856    383   -556    501       C  
ATOM    321  CD1 LEU A  41     -41.738 -38.837-118.511  1.00137.94           C  
ANISOU  321  CD1 LEU A  41    17853  18629  15927    337   -617    578       C  
ATOM    322  CD2 LEU A  41     -40.137 -40.677-119.082  1.00137.47           C  
ANISOU  322  CD2 LEU A  41    17824  18478  15929    445   -649    463       C  
ATOM    323  N   PRO A  42     -36.534 -37.896-120.746  1.00142.64           N  
ANISOU  323  N   PRO A  42    18406  19231  16560    546    -64    296       N  
ATOM    324  CA  PRO A  42     -35.755 -37.065-121.670  1.00144.20           C  
ANISOU  324  CA  PRO A  42    18625  19447  16718    580    105    265       C  
ATOM    325  C   PRO A  42     -36.614 -36.033-122.402  1.00150.08           C  
ANISOU  325  C   PRO A  42    19466  20186  17370    552    154    290       C  
ATOM    326  O   PRO A  42     -37.799 -36.274-122.648  1.00150.48           O  
ANISOU  326  O   PRO A  42    19611  20198  17365    543     56    316       O  
ATOM    327  CB  PRO A  42     -35.188 -38.082-122.664  1.00142.92           C  
ANISOU  327  CB  PRO A  42    18542  19235  16523    692    117    207       C  
ATOM    328  CG  PRO A  42     -36.113 -39.248-122.592  1.00141.54           C  
ANISOU  328  CG  PRO A  42    18449  18994  16334    707    -59    213       C  
ATOM    329  CD  PRO A  42     -36.553 -39.311-121.162  1.00140.53           C  
ANISOU  329  CD  PRO A  42    18210  18898  16285    618   -164    264       C  
ATOM    330  N   ALA A  43     -36.018 -34.890-122.731  1.00158.91           N  
ANISOU  330  N   ALA A  43    20559  21342  18476    535    301    288       N  
ATOM    331  CA  ALA A  43     -36.699 -33.857-123.509  1.00166.93           C  
ANISOU  331  CA  ALA A  43    21671  22352  19402    515    362    307       C  
ATOM    332  C   ALA A  43     -36.611 -34.184-125.001  1.00175.56           C  
ANISOU  332  C   ALA A  43    22898  23399  20406    605    421    268       C  
ATOM    333  O   ALA A  43     -35.521 -34.168-125.585  1.00179.71           O  
ANISOU  333  O   ALA A  43    23406  23940  20934    662    540    236       O  
ATOM    334  CB  ALA A  43     -36.109 -32.484-123.214  1.00162.95           C  
ANISOU  334  CB  ALA A  43    21089  21902  18921    455    483    326       C  
ATOM    335  N   GLU A  44     -37.760 -34.495-125.601  1.00180.19           N  
ANISOU  335  N   GLU A  44    23617  23932  20914    621    335    276       N  
ATOM    336  CA  GLU A  44     -37.840 -34.869-127.021  1.00182.84           C  
ANISOU  336  CA  GLU A  44    24106  24211  21154    710    366    239       C  
ATOM    337  C   GLU A  44     -37.564 -33.692-127.962  1.00183.25           C  
ANISOU  337  C   GLU A  44    24207  24282  21135    718    526    236       C  
ATOM    338  O   GLU A  44     -38.420 -32.830-128.184  1.00182.30           O  
ANISOU  338  O   GLU A  44    24144  24158  20960    668    530    268       O  
ATOM    339  CB  GLU A  44     -39.178 -35.558-127.351  1.00183.83           C  
ANISOU  339  CB  GLU A  44    24360  24265  21222    717    208    254       C  
ATOM    340  CG  GLU A  44     -40.342 -35.259-126.410  1.00184.97           C  
ANISOU  340  CG  GLU A  44    24461  24427  21392    620     94    321       C  
ATOM    341  CD  GLU A  44     -40.833 -33.824-126.490  1.00186.40           C  
ANISOU  341  CD  GLU A  44    24647  24647  21529    561    175    357       C  
ATOM    342  OE1 GLU A  44     -41.822 -33.573-127.212  1.00187.67           O  
ANISOU  342  OE1 GLU A  44    24924  24772  21608    562    142    376       O  
ATOM    343  OE2 GLU A  44     -40.230 -32.946-125.836  1.00185.14           O  
ANISOU  343  OE2 GLU A  44    24379  24547  21415    515    265    366       O  
ATOM    344  N   GLU A  45     -36.352 -33.679-128.511  1.00182.91           N  
ANISOU  344  N   GLU A  45    24139  24262  21094    782    660    203       N  
ATOM    345  CA  GLU A  45     -35.844 -32.551-129.282  1.00180.59           C  
ANISOU  345  CA  GLU A  45    23860  24003  20753    783    827    210       C  
ATOM    346  C   GLU A  45     -36.440 -32.504-130.682  1.00175.13           C  
ANISOU  346  C   GLU A  45    23350  23257  19932    850    853    193       C  
ATOM    347  O   GLU A  45     -36.783 -31.433-131.178  1.00170.28           O  
ANISOU  347  O   GLU A  45    22786  22650  19261    813    926    216       O  
ATOM    348  CB  GLU A  45     -34.318 -32.623-129.359  1.00186.97           C  
ANISOU  348  CB  GLU A  45    24563  24864  21613    832    960    194       C  
ATOM    349  CG  GLU A  45     -33.629 -31.275-129.505  1.00192.86           C  
ANISOU  349  CG  GLU A  45    25237  25670  22369    778   1117    229       C  
ATOM    350  CD  GLU A  45     -32.116 -31.369-129.388  1.00196.04           C  
ANISOU  350  CD  GLU A  45    25504  26135  22844    810   1233    229       C  
ATOM    351  OE1 GLU A  45     -31.519 -32.302-129.969  1.00198.68           O  
ANISOU  351  OE1 GLU A  45    25863  26466  23157    926   1264    193       O  
ATOM    352  OE2 GLU A  45     -31.519 -30.500-128.719  1.00196.07           O  
ANISOU  352  OE2 GLU A  45    25379  26192  22925    723   1290    269       O  
ATOM    353  N   SER A  48     -38.991 -28.293-135.742  1.00160.39           N  
ANISOU  353  N   SER A  48    22103  21288  17551    867   1183    240       N  
ATOM    354  CA  SER A  48     -38.964 -26.865-135.427  1.00163.55           C  
ANISOU  354  CA  SER A  48    22440  21732  17966    770   1264    285       C  
ATOM    355  C   SER A  48     -38.056 -26.057-136.372  1.00166.21           C  
ANISOU  355  C   SER A  48    22795  22102  18254    798   1451    292       C  
ATOM    356  O   SER A  48     -37.347 -26.633-137.204  1.00164.91           O  
ANISOU  356  O   SER A  48    22673  21937  18047    901   1530    264       O  
ATOM    357  CB  SER A  48     -38.591 -26.643-133.953  1.00160.29           C  
ANISOU  357  CB  SER A  48    21847  21374  17680    679   1232    311       C  
ATOM    358  OG  SER A  48     -37.402 -27.328-133.604  1.00159.70           O  
ANISOU  358  OG  SER A  48    21659  21335  17682    717   1276    293       O  
ATOM    359  N   LEU A  49     -38.102 -24.728-136.234  1.00168.42           N  
ANISOU  359  N   LEU A  49    23046  22409  18535    711   1517    334       N  
ATOM    360  CA  LEU A  49     -37.364 -23.774-137.087  1.00169.40           C  
ANISOU  360  CA  LEU A  49    23186  22563  18613    714   1687    357       C  
ATOM    361  C   LEU A  49     -37.730 -23.882-138.574  1.00166.65           C  
ANISOU  361  C   LEU A  49    23021  22170  18128    808   1737    335       C  
ATOM    362  O   LEU A  49     -38.762 -23.367-139.006  1.00161.63           O  
ANISOU  362  O   LEU A  49    22507  21488  17415    787   1694    340       O  
ATOM    363  CB  LEU A  49     -35.836 -23.871-136.878  1.00171.47           C  
ANISOU  363  CB  LEU A  49    23300  22895  18955    727   1807    372       C  
ATOM    364  CG  LEU A  49     -35.170 -23.260-135.634  1.00169.55           C  
ANISOU  364  CG  LEU A  49    22874  22706  18840    617   1814    411       C  
ATOM    365  CD1 LEU A  49     -33.779 -23.843-135.435  1.00167.92           C  
ANISOU  365  CD1 LEU A  49    22527  22560  18714    659   1894    415       C  
ATOM    366  CD2 LEU A  49     -35.102 -21.739-135.703  1.00166.77           C  
ANISOU  366  CD2 LEU A  49    22513  22369  18480    520   1889    464       C  
ATOM    367  N   TRP A  50     -36.872 -24.557-139.336  1.00168.12           N  
ANISOU  367  N   TRP A  50    23226  22369  18281    918   1827    312       N  
ATOM    368  CA  TRP A  50     -37.055 -24.784-140.768  1.00169.58           C  
ANISOU  368  CA  TRP A  50    23587  22514  18331   1030   1883    286       C  
ATOM    369  C   TRP A  50     -38.260 -25.695-141.021  1.00166.02           C  
ANISOU  369  C   TRP A  50    23288  21973  17817   1081   1717    240       C  
ATOM    370  O   TRP A  50     -39.042 -25.455-141.942  1.00163.89           O  
ANISOU  370  O   TRP A  50    23182  21648  17438   1111   1703    232       O  
ATOM    371  CB  TRP A  50     -35.765 -25.390-141.345  1.00176.15           C  
ANISOU  371  CB  TRP A  50    24383  23393  19151   1147   2014    275       C  
ATOM    372  CG  TRP A  50     -35.751 -25.693-142.827  1.00180.09           C  
ANISOU  372  CG  TRP A  50    25059  23861  19506   1286   2089    247       C  
ATOM    373  CD1 TRP A  50     -36.215 -26.825-143.436  1.00180.70           C  
ANISOU  373  CD1 TRP A  50    25289  23865  19501   1409   2001    187       C  
ATOM    374  CD2 TRP A  50     -35.200 -24.876-143.872  1.00183.70           C  
ANISOU  374  CD2 TRP A  50    25560  24357  19881   1322   2266    282       C  
ATOM    375  NE1 TRP A  50     -36.010 -26.755-144.792  1.00184.53           N  
ANISOU  375  NE1 TRP A  50    25919  24340  19853   1525   2111    177       N  
ATOM    376  CE2 TRP A  50     -35.389 -25.570-145.089  1.00186.60           C  
ANISOU  376  CE2 TRP A  50    26114  24674  20112   1475   2280    236       C  
ATOM    377  CE3 TRP A  50     -34.576 -23.620-143.900  1.00184.34           C  
ANISOU  377  CE3 TRP A  50    25545  24506  19989   1238   2409    351       C  
ATOM    378  CZ2 TRP A  50     -34.977 -25.050-146.323  1.00188.37           C  
ANISOU  378  CZ2 TRP A  50    26428  24921  20222   1553   2440    258       C  
ATOM    379  CZ3 TRP A  50     -34.166 -23.103-145.129  1.00186.47           C  
ANISOU  379  CZ3 TRP A  50    25898  24800  20152   1306   2566    378       C  
ATOM    380  CH2 TRP A  50     -34.369 -23.820-146.322  1.00187.02           C  
ANISOU  380  CH2 TRP A  50    26150  24825  20082   1465   2584    331       C  
ATOM    381  N   GLU A  51     -38.405 -26.723-140.185  1.00164.21           N  
ANISOU  381  N   GLU A  51    23001  21728  17661   1085   1586    216       N  
ATOM    382  CA  GLU A  51     -39.502 -27.689-140.294  1.00161.80           C  
ANISOU  382  CA  GLU A  51    22820  21338  17317   1122   1409    183       C  
ATOM    383  C   GLU A  51     -40.857 -27.047-140.052  1.00156.82           C  
ANISOU  383  C   GLU A  51    22242  20672  16668   1028   1303    213       C  
ATOM    384  O   GLU A  51     -41.858 -27.471-140.626  1.00153.07           O  
ANISOU  384  O   GLU A  51    21916  20122  16119   1061   1194    198       O  
ATOM    385  CB  GLU A  51     -39.308 -28.849-139.311  1.00165.29           C  
ANISOU  385  CB  GLU A  51    23166  21780  17857   1129   1293    163       C  
ATOM    386  CG  GLU A  51     -38.534 -30.036-139.868  1.00170.61           C  
ANISOU  386  CG  GLU A  51    23889  22434  18501   1270   1311    112       C  
ATOM    387  CD  GLU A  51     -38.568 -31.247-138.950  1.00171.07           C  
ANISOU  387  CD  GLU A  51    23883  22471  18644   1276   1163     90       C  
ATOM    388  OE1 GLU A  51     -38.104 -31.139-137.794  1.00171.03           O  
ANISOU  388  OE1 GLU A  51    23700  22526  18758   1200   1163    113       O  
ATOM    389  OE2 GLU A  51     -39.051 -32.313-139.389  1.00172.46           O  
ANISOU  389  OE2 GLU A  51    24191  22565  18768   1356   1040     51       O  
ATOM    390  N   LEU A  52     -40.876 -26.029-139.197  1.00157.14           N  
ANISOU  390  N   LEU A  52    22161  20766  16776    914   1332    257       N  
ATOM    391  CA  LEU A  52     -42.107 -25.331-138.845  1.00161.29           C  
ANISOU  391  CA  LEU A  52    22719  21273  17290    828   1241    291       C  
ATOM    392  C   LEU A  52     -42.571 -24.348-139.920  1.00165.26           C  
ANISOU  392  C   LEU A  52    23359  21750  17681    831   1314    302       C  
ATOM    393  O   LEU A  52     -43.738 -23.947-139.933  1.00167.34           O  
ANISOU  393  O   LEU A  52    23693  21981  17905    790   1227    323       O  
ATOM    394  CB  LEU A  52     -41.958 -24.618-137.496  1.00162.59           C  
ANISOU  394  CB  LEU A  52    22716  21501  17561    717   1238    331       C  
ATOM    395  CG  LEU A  52     -42.331 -25.381-136.219  1.00162.54           C  
ANISOU  395  CG  LEU A  52    22604  21504  17650    679   1092    339       C  
ATOM    396  CD1 LEU A  52     -41.877 -24.612-134.986  1.00161.25           C  
ANISOU  396  CD1 LEU A  52    22277  21406  17583    587   1122    371       C  
ATOM    397  CD2 LEU A  52     -43.826 -25.664-136.149  1.00162.59           C  
ANISOU  397  CD2 LEU A  52    22694  21463  17619    662    933    358       C  
ATOM    398  N   VAL A  53     -41.659 -23.964-140.813  1.00166.12           N  
ANISOU  398  N   VAL A  53    23501  21878  17739    883   1473    293       N  
ATOM    399  CA  VAL A  53     -41.986 -23.061-141.921  1.00159.20           C  
ANISOU  399  CA  VAL A  53    22761  20977  16750    895   1555    303       C  
ATOM    400  C   VAL A  53     -42.702 -23.819-143.041  1.00157.21           C  
ANISOU  400  C   VAL A  53    22705  20642  16384    995   1486    265       C  
ATOM    401  O   VAL A  53     -43.732 -23.367-143.543  1.00154.21           O  
ANISOU  401  O   VAL A  53    22447  20214  15929    978   1433    274       O  
ATOM    402  CB  VAL A  53     -40.736 -22.334-142.461  1.00157.50           C  
ANISOU  402  CB  VAL A  53    22502  20818  16521    910   1755    320       C  
ATOM    403  CG1 VAL A  53     -41.100 -21.425-143.624  1.00157.85           C  
ANISOU  403  CG1 VAL A  53    22693  20835  16445    923   1835    333       C  
ATOM    404  CG2 VAL A  53     -40.077 -21.522-141.357  1.00154.60           C  
ANISOU  404  CG2 VAL A  53    21951  20522  16268    800   1805    363       C  
ATOM    405  N   ILE A  54     -42.160 -24.980-143.407  1.00158.88           N  
ANISOU  405  N   ILE A  54    22949  20835  16583   1101   1479    222       N  
ATOM    406  CA  ILE A  54     -42.761 -25.849-144.423  1.00163.01           C  
ANISOU  406  CA  ILE A  54    23667  21269  17001   1206   1395    180       C  
ATOM    407  C   ILE A  54     -44.087 -26.448-143.929  1.00164.54           C  
ANISOU  407  C   ILE A  54    23902  21397  17216   1162   1178    184       C  
ATOM    408  O   ILE A  54     -44.874 -26.974-144.719  1.00166.13           O  
ANISOU  408  O   ILE A  54    24275  21514  17333   1219   1076    162       O  
ATOM    409  CB  ILE A  54     -41.789 -26.971-144.867  1.00164.47           C  
ANISOU  409  CB  ILE A  54    23877  21448  17166   1340   1437    131       C  
ATOM    410  CG1 ILE A  54     -40.351 -26.443-144.946  1.00165.80           C  
ANISOU  410  CG1 ILE A  54    23928  21710  17356   1363   1647    147       C  
ATOM    411  CG2 ILE A  54     -42.216 -27.559-146.209  1.00164.72           C  
ANISOU  411  CG2 ILE A  54    24141  21388  17055   1466   1399     87       C  
ATOM    412  CD1 ILE A  54     -39.294 -27.525-144.976  1.00167.63           C  
ANISOU  412  CD1 ILE A  54    24119  21963  17607   1478   1686    110       C  
ATOM    413  N   GLU A  55     -44.326 -26.355-142.622  1.00169.47           N  
ANISOU  413  N   GLU A  55    24371  22063  17954   1060   1105    217       N  
ATOM    414  CA  GLU A  55     -45.600 -26.753-142.018  1.00176.73           C  
ANISOU  414  CA  GLU A  55    25299  22943  18906   1002    911    242       C  
ATOM    415  C   GLU A  55     -46.783 -26.007-142.640  1.00179.83           C  
ANISOU  415  C   GLU A  55    25818  23295  19214    972    868    269       C  
ATOM    416  O   GLU A  55     -47.849 -26.590-142.851  1.00181.78           O  
ANISOU  416  O   GLU A  55    26160  23474  19431    977    710    277       O  
ATOM    417  CB  GLU A  55     -45.573 -26.496-140.506  1.00178.20           C  
ANISOU  417  CB  GLU A  55    25287  23200  19218    898    877    282       C  
ATOM    418  CG  GLU A  55     -44.914 -27.586-139.672  1.00179.32           C  
ANISOU  418  CG  GLU A  55    25314  23360  19457    915    825    264       C  
ATOM    419  CD  GLU A  55     -45.887 -28.308-138.756  1.00179.17           C  
ANISOU  419  CD  GLU A  55    25249  23322  19502    863    631    295       C  
ATOM    420  OE1 GLU A  55     -45.644 -28.321-137.531  1.00176.85           O  
ANISOU  420  OE1 GLU A  55    24795  23088  19312    801    611    318       O  
ATOM    421  OE2 GLU A  55     -46.895 -28.856-139.251  1.00180.52           O  
ANISOU  421  OE2 GLU A  55    25544  23421  19621    882    496    301       O  
ATOM    422  N   GLN A  56     -46.579 -24.724-142.937  1.00180.02           N  
ANISOU  422  N   GLN A  56    25841  23356  19200    938   1005    286       N  
ATOM    423  CA  GLN A  56     -47.647 -23.846-143.422  1.00176.46           C  
ANISOU  423  CA  GLN A  56    25493  22877  18676    902    978    315       C  
ATOM    424  C   GLN A  56     -48.025 -24.104-144.878  1.00175.45           C  
ANISOU  424  C   GLN A  56    25579  22666  18418    990    969    284       C  
ATOM    425  O   GLN A  56     -49.149 -23.810-145.290  1.00174.93           O  
ANISOU  425  O   GLN A  56    25619  22553  18294    972    883    305       O  
ATOM    426  CB  GLN A  56     -47.274 -22.370-143.222  1.00175.60           C  
ANISOU  426  CB  GLN A  56    25317  22831  18571    835   1121    345       C  
ATOM    427  CG  GLN A  56     -47.005 -21.972-141.774  1.00175.20           C  
ANISOU  427  CG  GLN A  56    25073  22855  18638    745   1119    377       C  
ATOM    428  CD  GLN A  56     -48.158 -22.295-140.838  1.00174.05           C  
ANISOU  428  CD  GLN A  56    24878  22708  18542    693    947    413       C  
ATOM    429  OE1 GLN A  56     -49.307 -21.934-141.096  1.00171.91           O  
ANISOU  429  OE1 GLN A  56    24690  22408  18217    675    871    441       O  
ATOM    430  NE2 GLN A  56     -47.852 -22.975-139.737  1.00173.80           N  
ANISOU  430  NE2 GLN A  56    24708  22713  18614    669    888    418       N  
ATOM    431  N   PHE A  57     -47.089 -24.655-145.647  1.00176.92           N  
ANISOU  431  N   PHE A  57    25828  22834  18556   1091   1055    236       N  
ATOM    432  CA  PHE A  57     -47.326 -24.956-147.060  1.00180.91           C  
ANISOU  432  CA  PHE A  57    26548  23258  18930   1193   1054    201       C  
ATOM    433  C   PHE A  57     -47.996 -26.313-147.276  1.00181.82           C  
ANISOU  433  C   PHE A  57    26774  23281  19028   1251    861    174       C  
ATOM    434  O   PHE A  57     -48.290 -26.691-148.413  1.00186.42           O  
ANISOU  434  O   PHE A  57    27551  23781  19499   1340    827    141       O  
ATOM    435  CB  PHE A  57     -46.027 -24.850-147.872  1.00182.06           C  
ANISOU  435  CB  PHE A  57    26725  23432  19015   1290   1245    167       C  
ATOM    436  CG  PHE A  57     -45.454 -23.461-147.921  1.00180.38           C  
ANISOU  436  CG  PHE A  57    26440  23294  18799   1235   1427    202       C  
ATOM    437  CD1 PHE A  57     -46.086 -22.458-148.647  1.00180.47           C  
ANISOU  437  CD1 PHE A  57    26564  23281  18723   1211   1462    222       C  
ATOM    438  CD2 PHE A  57     -44.278 -23.156-147.245  1.00180.15           C  
ANISOU  438  CD2 PHE A  57    26233  23356  18857   1203   1557    218       C  
ATOM    439  CE1 PHE A  57     -45.563 -21.175-148.692  1.00180.80           C  
ANISOU  439  CE1 PHE A  57    26546  23385  18763   1155   1620    257       C  
ATOM    440  CE2 PHE A  57     -43.748 -21.874-147.287  1.00179.17           C  
ANISOU  440  CE2 PHE A  57    26046  23294  18735   1144   1711    257       C  
ATOM    441  CZ  PHE A  57     -44.392 -20.883-148.011  1.00179.01           C  
ANISOU  441  CZ  PHE A  57    26143  23245  18626   1119   1741    277       C  
ATOM    442  N   GLU A  58     -48.240 -27.037-146.185  1.00177.60           N  
ANISOU  442  N   GLU A  58    26121  22756  18600   1199    731    190       N  
ATOM    443  CA  GLU A  58     -48.973 -28.301-146.238  1.00178.68           C  
ANISOU  443  CA  GLU A  58    26346  22804  18738   1230    523    180       C  
ATOM    444  C   GLU A  58     -50.462 -28.050-146.499  1.00177.78           C  
ANISOU  444  C   GLU A  58    26328  22632  18585   1174    376    224       C  
ATOM    445  O   GLU A  58     -51.182 -28.953-146.932  1.00178.84           O  
ANISOU  445  O   GLU A  58    26592  22672  18687   1207    205    218       O  
ATOM    446  CB  GLU A  58     -48.772 -29.096-144.943  1.00183.31           C  
ANISOU  446  CB  GLU A  58    26765  23426  19456   1182    433    194       C  
ATOM    447  CG  GLU A  58     -49.106 -30.581-145.047  1.00188.59           C  
ANISOU  447  CG  GLU A  58    27523  24003  20128   1236    243    171       C  
ATOM    448  CD  GLU A  58     -49.078 -31.297-143.704  1.00190.35           C  
ANISOU  448  CD  GLU A  58    27577  24262  20486   1172    137    199       C  
ATOM    449  OE1 GLU A  58     -49.595 -30.744-142.708  1.00191.50           O  
ANISOU  449  OE1 GLU A  58    27577  24472  20710   1061    111    261       O  
ATOM    450  OE2 GLU A  58     -48.547 -32.426-143.644  1.00190.00           O  
ANISOU  450  OE2 GLU A  58    27549  24178  20461   1238     78    159       O  
ATOM    451  N   ASP A  59     -50.906 -26.819-146.231  1.00175.49           N  
ANISOU  451  N   ASP A  59    25977  22398  18301   1091    438    270       N  
ATOM    452  CA  ASP A  59     -52.274 -26.378-146.515  1.00175.51           C  
ANISOU  452  CA  ASP A  59    26062  22361  18261   1042    327    317       C  
ATOM    453  C   ASP A  59     -52.528 -26.418-148.019  1.00176.56           C  
ANISOU  453  C   ASP A  59    26429  22400  18257   1129    326    279       C  
ATOM    454  O   ASP A  59     -51.719 -25.916-148.804  1.00180.72           O  
ANISOU  454  O   ASP A  59    27023  22934  18706   1194    492    238       O  
ATOM    455  CB  ASP A  59     -52.502 -24.960-145.966  1.00176.19           C  
ANISOU  455  CB  ASP A  59    26040  22532  18370    954    424    365       C  
ATOM    456  CG  ASP A  59     -53.967 -24.513-146.035  1.00177.79           C  
ANISOU  456  CG  ASP A  59    26294  22711  18545    899    301    424       C  
ATOM    457  OD1 ASP A  59     -54.860 -25.346-146.310  1.00178.55           O  
ANISOU  457  OD1 ASP A  59    26475  22735  18629    908    123    443       O  
ATOM    458  OD2 ASP A  59     -54.226 -23.312-145.802  1.00176.66           O  
ANISOU  458  OD2 ASP A  59    26104  22623  18394    846    378    457       O  
ATOM    459  N   LEU A  60     -53.650 -27.019-148.408  1.00176.17           N  
ANISOU  459  N   LEU A  60    26498  22261  18176   1129    134    299       N  
ATOM    460  CA  LEU A  60     -53.960 -27.255-149.821  1.00175.96           C  
ANISOU  460  CA  LEU A  60    26712  22126  18019   1217     95    261       C  
ATOM    461  C   LEU A  60     -54.333 -25.980-150.582  1.00174.34           C  
ANISOU  461  C   LEU A  60    26593  21927  17722   1208    197    273       C  
ATOM    462  O   LEU A  60     -54.066 -25.876-151.779  1.00174.06           O  
ANISOU  462  O   LEU A  60    26733  21833  17568   1298    263    226       O  
ATOM    463  CB  LEU A  60     -55.065 -28.308-149.969  1.00174.66           C  
ANISOU  463  CB  LEU A  60    26647  21856  17857   1210   -161    286       C  
ATOM    464  CG  LEU A  60     -54.974 -29.222-151.195  1.00176.96           C  
ANISOU  464  CG  LEU A  60    27178  22017  18041   1331   -239    222       C  
ATOM    465  CD1 LEU A  60     -54.064 -30.415-150.924  1.00176.05           C  
ANISOU  465  CD1 LEU A  60    27047  21881  17962   1403   -263    170       C  
ATOM    466  CD2 LEU A  60     -56.357 -29.696-151.612  1.00177.28           C  
ANISOU  466  CD2 LEU A  60    27351  21950  18056   1301   -478    265       C  
ATOM    467  N   LEU A  61     -54.942 -25.021-149.885  1.00171.75           N  
ANISOU  467  N   LEU A  61    26145  21668  17444   1106    208    335       N  
ATOM    468  CA  LEU A  61     -55.318 -23.736-150.481  1.00170.54           C  
ANISOU  468  CA  LEU A  61    26058  21525  17211   1088    301    351       C  
ATOM    469  C   LEU A  61     -54.111 -22.856-150.788  1.00170.96           C  
ANISOU  469  C   LEU A  61    26092  21638  17227   1119    540    314       C  
ATOM    470  O   LEU A  61     -54.148 -22.056-151.722  1.00176.19           O  
ANISOU  470  O   LEU A  61    26876  22278  17788   1148    632    304       O  
ATOM    471  CB  LEU A  61     -56.303 -22.982-149.585  1.00170.63           C  
ANISOU  471  CB  LEU A  61    25946  21598  17287    980    241    429       C  
ATOM    472  CG  LEU A  61     -57.768 -23.430-149.629  1.00174.59           C  
ANISOU  472  CG  LEU A  61    26503  22042  17790    945     22    487       C  
ATOM    473  CD1 LEU A  61     -58.510 -22.963-148.383  1.00177.04           C  
ANISOU  473  CD1 LEU A  61    26630  22440  18193    847    -33    569       C  
ATOM    474  CD2 LEU A  61     -58.468 -22.944-150.893  1.00172.82           C  
ANISOU  474  CD2 LEU A  61    26479  21740  17444    980      1    482       C  
ATOM    475  N   VAL A  62     -53.051 -23.002-149.998  1.00168.31           N  
ANISOU  475  N   VAL A  62    25600  21376  16973   1111    637    302       N  
ATOM    476  CA  VAL A  62     -51.794 -22.296-150.245  1.00167.13           C  
ANISOU  476  CA  VAL A  62    25414  21286  16802   1139    858    276       C  
ATOM    477  C   VAL A  62     -51.036 -22.949-151.402  1.00168.36           C  
ANISOU  477  C   VAL A  62    25721  21387  16860   1270    925    215       C  
ATOM    478  O   VAL A  62     -50.375 -22.264-152.186  1.00169.45           O  
ANISOU  478  O   VAL A  62    25920  21542  16919   1315   1092    200       O  
ATOM    479  CB  VAL A  62     -50.916 -22.242-148.975  1.00167.84           C  
ANISOU  479  CB  VAL A  62    25279  21473  17018   1082    929    289       C  
ATOM    480  CG1 VAL A  62     -49.530 -21.692-149.284  1.00166.00           C  
ANISOU  480  CG1 VAL A  62    25006  21297  16768   1117   1146    268       C  
ATOM    481  CG2 VAL A  62     -51.592 -21.399-147.902  1.00170.15           C  
ANISOU  481  CG2 VAL A  62    25437  21824  17386    966    890    348       C  
ATOM    482  N   ARG A  63     -51.147 -24.271-151.506  1.00169.06           N  
ANISOU  482  N   ARG A  63    25873  21410  16951   1334    792    183       N  
ATOM    483  CA  ARG A  63     -50.521 -25.016-152.597  1.00172.44           C  
ANISOU  483  CA  ARG A  63    26465  21775  17277   1476    830    120       C  
ATOM    484  C   ARG A  63     -51.262 -24.869-153.930  1.00172.68           C  
ANISOU  484  C   ARG A  63    26738  21707  17163   1539    783    104       C  
ATOM    485  O   ARG A  63     -50.635 -24.895-154.992  1.00175.24           O  
ANISOU  485  O   ARG A  63    27202  22007  17375   1655    893     61       O  
ATOM    486  CB  ARG A  63     -50.342 -26.488-152.224  1.00176.26           C  
ANISOU  486  CB  ARG A  63    26943  22216  17810   1529    696     88       C  
ATOM    487  CG  ARG A  63     -48.963 -26.803-151.668  1.00179.25           C  
ANISOU  487  CG  ARG A  63    27176  22676  18254   1566    829     65       C  
ATOM    488  CD  ARG A  63     -48.602 -28.263-151.886  1.00184.42           C  
ANISOU  488  CD  ARG A  63    27914  23262  18892   1679    734     10       C  
ATOM    489  NE  ARG A  63     -48.696 -29.055-150.663  1.00182.88           N  
ANISOU  489  NE  ARG A  63    27571  23084  18832   1615    603     25       N  
ATOM    490  CZ  ARG A  63     -47.647 -29.509-149.982  1.00184.40           C  
ANISOU  490  CZ  ARG A  63    27622  23340  19101   1638    674      8       C  
ATOM    491  NH1 ARG A  63     -46.412 -29.256-150.401  1.00185.68           N  
ANISOU  491  NH1 ARG A  63    27765  23562  19223   1724    876    -19       N  
ATOM    492  NH2 ARG A  63     -47.832 -30.222-148.880  1.00184.92           N  
ANISOU  492  NH2 ARG A  63    27562  23413  19286   1575    543     25       N  
ATOM    493  N   ILE A  64     -52.586 -24.724-153.869  1.00169.22           N  
ANISOU  493  N   ILE A  64    26349  21218  16730   1468    621    141       N  
ATOM    494  CA  ILE A  64     -53.403 -24.437-155.054  1.00167.00           C  
ANISOU  494  CA  ILE A  64    26284  20845  16321   1508    568    135       C  
ATOM    495  C   ILE A  64     -52.990 -23.104-155.684  1.00166.93           C  
ANISOU  495  C   ILE A  64    26306  20886  16234   1513    773    139       C  
ATOM    496  O   ILE A  64     -52.904 -22.995-156.907  1.00169.02           O  
ANISOU  496  O   ILE A  64    26761  21091  16365   1606    825    106       O  
ATOM    497  CB  ILE A  64     -54.919 -24.462-154.729  1.00164.79           C  
ANISOU  497  CB  ILE A  64    26015  20518  16079   1416    354    190       C  
ATOM    498  CG1 ILE A  64     -55.475 -25.882-154.886  1.00165.09           C  
ANISOU  498  CG1 ILE A  64    26160  20447  16120   1457    127    175       C  
ATOM    499  CG2 ILE A  64     -55.699 -23.499-155.614  1.00163.62           C  
ANISOU  499  CG2 ILE A  64    26006  20331  15829   1407    367    208       C  
ATOM    500  CD1 ILE A  64     -56.911 -26.051-154.425  1.00162.61           C  
ANISOU  500  CD1 ILE A  64    25822  20096  15864   1358    -93    245       C  
ATOM    501  N   LEU A  65     -52.721 -22.107-154.840  1.00165.24           N  
ANISOU  501  N   LEU A  65    25908  20775  16100   1413    883    182       N  
ATOM    502  CA  LEU A  65     -52.289 -20.782-155.288  1.00164.46           C  
ANISOU  502  CA  LEU A  65    25815  20728  15944   1398   1073    196       C  
ATOM    503  C   LEU A  65     -50.926 -20.809-155.977  1.00167.66           C  
ANISOU  503  C   LEU A  65    26253  21164  16285   1500   1269    159       C  
ATOM    504  O   LEU A  65     -50.729 -20.137-156.990  1.00170.13           O  
ANISOU  504  O   LEU A  65    26690  21465  16487   1549   1387    155       O  
ATOM    505  CB  LEU A  65     -52.250 -19.798-154.116  1.00159.11           C  
ANISOU  505  CB  LEU A  65    24929  20148  15375   1270   1130    248       C  
ATOM    506  CG  LEU A  65     -51.970 -18.338-154.475  1.00157.61           C  
ANISOU  506  CG  LEU A  65    24744  20002  15136   1232   1296    273       C  
ATOM    507  CD1 LEU A  65     -53.263 -17.619-154.813  1.00155.80           C  
ANISOU  507  CD1 LEU A  65    24617  19725  14852   1187   1205    302       C  
ATOM    508  CD2 LEU A  65     -51.249 -17.629-153.343  1.00158.34           C  
ANISOU  508  CD2 LEU A  65    24620  20199  15341   1141   1400    307       C  
ATOM    509  N   LEU A  66     -49.994 -21.579-155.418  1.00168.80           N  
ANISOU  509  N   LEU A  66    26282  21352  16499   1534   1305    139       N  
ATOM    510  CA  LEU A  66     -48.636 -21.683-155.958  1.00172.71           C  
ANISOU  510  CA  LEU A  66    26780  21893  16946   1636   1494    114       C  
ATOM    511  C   LEU A  66     -48.572 -22.413-157.307  1.00181.78           C  
ANISOU  511  C   LEU A  66    28167  22955  17945   1798   1486     59       C  
ATOM    512  O   LEU A  66     -47.753 -22.067-158.162  1.00188.38           O  
ANISOU  512  O   LEU A  66    29068  23821  18687   1886   1661     52       O  
ATOM    513  CB  LEU A  66     -47.690 -22.330-154.938  1.00166.74           C  
ANISOU  513  CB  LEU A  66    25831  21209  16311   1629   1524    109       C  
ATOM    514  CG  LEU A  66     -47.270 -21.488-153.727  1.00161.78           C  
ANISOU  514  CG  LEU A  66    24964  20688  15817   1495   1602    160       C  
ATOM    515  CD1 LEU A  66     -46.742 -22.384-152.621  1.00161.04           C  
ANISOU  515  CD1 LEU A  66    24703  20635  15850   1482   1551    150       C  
ATOM    516  CD2 LEU A  66     -46.235 -20.435-154.094  1.00161.05           C  
ANISOU  516  CD2 LEU A  66    24817  20676  15697   1492   1831    189       C  
ATOM    517  N   LEU A  67     -49.437 -23.410-157.494  1.00184.14           N  
ANISOU  517  N   LEU A  67    28596  23147  18219   1837   1279     27       N  
ATOM    518  CA  LEU A  67     -49.537 -24.131-158.770  1.00186.18           C  
ANISOU  518  CA  LEU A  67    29107  23302  18328   1991   1235    -27       C  
ATOM    519  C   LEU A  67     -50.463 -23.426-159.770  1.00188.88           C  
ANISOU  519  C   LEU A  67    29640  23572  18553   1990   1203    -19       C  
ATOM    520  O   LEU A  67     -50.541 -23.818-160.936  1.00190.51           O  
ANISOU  520  O   LEU A  67    30072  23693  18618   2119   1186    -62       O  
ATOM    521  CB  LEU A  67     -49.958 -25.588-158.541  1.00183.64           C  
ANISOU  521  CB  LEU A  67    28852  22889  18034   2038   1017    -66       C  
ATOM    522  CG  LEU A  67     -48.826 -26.509-158.070  1.00183.94           C  
ANISOU  522  CG  LEU A  67    28792  22973  18123   2116   1070    -99       C  
ATOM    523  CD1 LEU A  67     -49.313 -27.544-157.065  1.00180.37           C  
ANISOU  523  CD1 LEU A  67    28259  22482  17791   2058    858   -100       C  
ATOM    524  CD2 LEU A  67     -48.130 -27.173-159.251  1.00186.55           C  
ANISOU  524  CD2 LEU A  67    29322  23252  18303   2316   1138   -162       C  
ATOM    525  N   ALA A  68     -51.160 -22.391-159.298  1.00188.88           N  
ANISOU  525  N   ALA A  68    29553  23605  18609   1852   1192     34       N  
ATOM    526  CA  ALA A  68     -51.927 -21.491-160.161  1.00189.83           C  
ANISOU  526  CA  ALA A  68    29822  23678  18627   1837   1196     50       C  
ATOM    527  C   ALA A  68     -51.076 -20.285-160.557  1.00192.12           C  
ANISOU  527  C   ALA A  68    30074  24053  18868   1837   1442     73       C  
ATOM    528  O   ALA A  68     -51.402 -19.574-161.508  1.00197.49           O  
ANISOU  528  O   ALA A  68    30902  24697  19435   1861   1492     78       O  
ATOM    529  CB  ALA A  68     -53.205 -21.037-159.470  1.00184.57           C  
ANISOU  529  CB  ALA A  68    29091  22996  18038   1697   1041     98       C  
ATOM    530  N   ALA A  69     -49.995 -20.060-159.811  1.00190.28           N  
ANISOU  530  N   ALA A  69    29640  23930  18725   1804   1589     93       N  
ATOM    531  CA  ALA A  69     -49.009 -19.030-160.135  1.00188.95           C  
ANISOU  531  CA  ALA A  69    29416  23851  18524   1803   1826    124       C  
ATOM    532  C   ALA A  69     -47.838 -19.624-160.920  1.00191.40           C  
ANISOU  532  C   ALA A  69    29791  24184  18748   1961   1970     92       C  
ATOM    533  O   ALA A  69     -46.952 -18.895-161.373  1.00193.43           O  
ANISOU  533  O   ALA A  69    30021  24513  18959   1986   2174    122       O  
ATOM    534  CB  ALA A  69     -48.515 -18.344-158.871  1.00185.84           C  
ANISOU  534  CB  ALA A  69    28764  23565  18279   1668   1899    174       C  
ATOM    535  N   CYS A  70     -47.841 -20.948-161.068  1.00190.84           N  
ANISOU  535  N   CYS A  70    29805  24051  18654   2070   1861     36       N  
ATOM    536  CA  CYS A  70     -46.861 -21.647-161.897  1.00192.61           C  
ANISOU  536  CA  CYS A  70    30126  24280  18773   2249   1973     -1       C  
ATOM    537  C   CYS A  70     -47.415 -21.945-163.286  1.00193.55           C  
ANISOU  537  C   CYS A  70    30541  24286  18713   2383   1918    -45       C  
ATOM    538  O   CYS A  70     -46.726 -21.744-164.286  1.00195.64           O  
ANISOU  538  O   CYS A  70    30912  24573  18849   2507   2081    -50       O  
ATOM    539  CB  CYS A  70     -46.381 -22.930-161.219  1.00192.78           C  
ANISOU  539  CB  CYS A  70    30068  24307  18873   2304   1897    -39       C  
ATOM    540  SG  CYS A  70     -45.076 -22.649-160.004  1.00192.85           S  
ANISOU  540  SG  CYS A  70    29756  24475  19042   2227   2062      6       S  
ATOM    541  N   ILE A  71     -48.660 -22.416-163.342  1.00192.01           N  
ANISOU  541  N   ILE A  71    30475  23970  18508   2358   1687    -72       N  
ATOM    542  CA  ILE A  71     -49.363 -22.607-164.613  1.00194.69           C  
ANISOU  542  CA  ILE A  71    31102  24188  18684   2462   1604   -110       C  
ATOM    543  C   ILE A  71     -49.674 -21.249-165.263  1.00195.69           C  
ANISOU  543  C   ILE A  71    31287  24330  18736   2411   1714    -69       C  
ATOM    544  O   ILE A  71     -50.054 -21.179-166.429  1.00198.76           O  
ANISOU  544  O   ILE A  71    31907  24637  18973   2504   1701    -93       O  
ATOM    545  CB  ILE A  71     -50.627 -23.492-164.444  1.00193.72           C  
ANISOU  545  CB  ILE A  71    31089  23930  18584   2435   1310   -139       C  
ATOM    546  CG1 ILE A  71     -50.217 -24.940-164.140  1.00195.05           C  
ANISOU  546  CG1 ILE A  71    31268  24061  18781   2530   1208   -190       C  
ATOM    547  CG2 ILE A  71     -51.509 -23.458-165.687  1.00194.04           C  
ANISOU  547  CG2 ILE A  71    31413  23841  18470   2507   1211   -165       C  
ATOM    548  CD1 ILE A  71     -51.367 -25.881-163.837  1.00194.10           C  
ANISOU  548  CD1 ILE A  71    31227  23814  18706   2490    912   -207       C  
ATOM    549  N   SER A  72     -49.490 -20.171-164.506  1.00193.63           N  
ANISOU  549  N   SER A  72    30820  24170  18578   2266   1819     -8       N  
ATOM    550  CA  SER A  72     -49.589 -18.822-165.054  1.00192.45           C  
ANISOU  550  CA  SER A  72    30705  24049  18366   2215   1947     35       C  
ATOM    551  C   SER A  72     -48.237 -18.358-165.602  1.00194.77           C  
ANISOU  551  C   SER A  72    30965  24441  18594   2296   2212     59       C  
ATOM    552  O   SER A  72     -48.184 -17.634-166.597  1.00197.93           O  
ANISOU  552  O   SER A  72    31495  24836  18871   2340   2323     76       O  
ATOM    553  CB  SER A  72     -50.104 -17.845-163.995  1.00188.28           C  
ANISOU  553  CB  SER A  72    29991  23573  17974   2022   1918     92       C  
ATOM    554  OG  SER A  72     -50.571 -16.648-164.590  1.00187.54           O  
ANISOU  554  OG  SER A  72    29981  23468  17809   1974   1974    125       O  
ATOM    555  N   PHE A  73     -47.153 -18.781-164.951  1.00193.82           N  
ANISOU  555  N   PHE A  73    30667  24415  18559   2314   2310     67       N  
ATOM    556  CA  PHE A  73     -45.793 -18.440-165.377  1.00194.34           C  
ANISOU  556  CA  PHE A  73    30672  24590  18579   2391   2561    101       C  
ATOM    557  C   PHE A  73     -45.361 -19.242-166.602  1.00198.53           C  
ANISOU  557  C   PHE A  73    31414  25080  18937   2612   2616     53       C  
ATOM    558  O   PHE A  73     -44.853 -18.674-167.571  1.00201.16           O  
ANISOU  558  O   PHE A  73    31833  25449  19147   2691   2789     81       O  
ATOM    559  CB  PHE A  73     -44.792 -18.644-164.229  1.00191.54           C  
ANISOU  559  CB  PHE A  73    30047  24348  18378   2335   2637    129       C  
ATOM    560  CG  PHE A  73     -43.347 -18.619-164.662  1.00193.03           C  
ANISOU  560  CG  PHE A  73    30170  24648  18523   2443   2875    162       C  
ATOM    561  CD1 PHE A  73     -42.655 -17.416-164.758  1.00192.75           C  
ANISOU  561  CD1 PHE A  73    30022  24714  18499   2371   3072    245       C  
ATOM    562  CD2 PHE A  73     -42.673 -19.801-164.965  1.00194.36           C  
ANISOU  562  CD2 PHE A  73    30388  24822  18638   2617   2897    116       C  
ATOM    563  CE1 PHE A  73     -41.326 -17.391-165.154  1.00195.03           C  
ANISOU  563  CE1 PHE A  73    30237  25114  18751   2466   3291    290       C  
ATOM    564  CE2 PHE A  73     -41.345 -19.782-165.363  1.00195.79           C  
ANISOU  564  CE2 PHE A  73    30500  25115  18775   2725   3121    154       C  
ATOM    565  CZ  PHE A  73     -40.670 -18.575-165.456  1.00196.37           C  
ANISOU  565  CZ  PHE A  73    30448  25297  18866   2647   3321    246       C  
ATOM    566  N   VAL A  74     -45.556 -20.560-166.545  1.00198.07           N  
ANISOU  566  N   VAL A  74    31440  24947  18868   2712   2468    -15       N  
ATOM    567  CA  VAL A  74     -45.125 -21.469-167.613  1.00200.24           C  
ANISOU  567  CA  VAL A  74    31924  25178  18980   2939   2500    -71       C  
ATOM    568  C   VAL A  74     -45.908 -21.238-168.912  1.00202.18           C  
ANISOU  568  C   VAL A  74    32458  25312  19046   3021   2453    -97       C  
ATOM    569  O   VAL A  74     -45.351 -21.377-170.003  1.00208.02           O  
ANISOU  569  O   VAL A  74    33357  26055  19624   3197   2579   -111       O  
ATOM    570  CB  VAL A  74     -45.157 -22.950-167.157  1.00198.10           C  
ANISOU  570  CB  VAL A  74    31675  24844  18749   3019   2332   -140       C  
ATOM    571  CG1 VAL A  74     -44.817 -23.896-168.301  1.00199.89           C  
ANISOU  571  CG1 VAL A  74    32150  25005  18793   3264   2342   -204       C  
ATOM    572  CG2 VAL A  74     -44.180 -23.164-166.011  1.00196.46           C  
ANISOU  572  CG2 VAL A  74    31188  24758  18697   2966   2417   -112       C  
ATOM    573  N   LEU A  75     -47.184 -20.869-168.795  1.00197.15           N  
ANISOU  573  N   LEU A  75    31888  24583  18437   2899   2277    -99       N  
ATOM    574  CA  LEU A  75     -47.972 -20.476-169.966  1.00197.23           C  
ANISOU  574  CA  LEU A  75    32155  24493  18291   2951   2234   -115       C  
ATOM    575  C   LEU A  75     -47.473 -19.165-170.576  1.00201.82           C  
ANISOU  575  C   LEU A  75    32719  25160  18801   2933   2466    -51       C  
ATOM    576  O   LEU A  75     -47.528 -18.982-171.794  1.00206.80           O  
ANISOU  576  O   LEU A  75    33568  25746  19260   3054   2525    -63       O  
ATOM    577  CB  LEU A  75     -49.465 -20.371-169.636  1.00189.65           C  
ANISOU  577  CB  LEU A  75    31248  23422  17388   2817   1988   -122       C  
ATOM    578  CG  LEU A  75     -50.302 -21.641-169.434  1.00186.42           C  
ANISOU  578  CG  LEU A  75    30949  22883  17000   2846   1713   -182       C  
ATOM    579  CD1 LEU A  75     -51.778 -21.276-169.398  1.00183.16           C  
ANISOU  579  CD1 LEU A  75    30610  22371  16610   2724   1508   -170       C  
ATOM    580  CD2 LEU A  75     -50.049 -22.699-170.496  1.00188.67           C  
ANISOU  580  CD2 LEU A  75    31492  23073  17119   3068   1675   -254       C  
ATOM    581  N   ALA A  76     -46.987 -18.262-169.725  1.00200.83           N  
ANISOU  581  N   ALA A  76    32340  25155  18808   2783   2590     19       N  
ATOM    582  CA  ALA A  76     -46.458 -16.974-170.174  1.00202.46           C  
ANISOU  582  CA  ALA A  76    32504  25449  18971   2743   2806     92       C  
ATOM    583  C   ALA A  76     -45.073 -17.100-170.812  1.00208.29           C  
ANISOU  583  C   ALA A  76    33229  26290  19618   2897   3047    118       C  
ATOM    584  O   ALA A  76     -44.807 -16.477-171.842  1.00214.33           O  
ANISOU  584  O   ALA A  76    34114  27075  20247   2968   3193    150       O  
ATOM    585  CB  ALA A  76     -46.432 -15.975-169.027  1.00196.97           C  
ANISOU  585  CB  ALA A  76    31553  24836  18448   2529   2836    159       C  
ATOM    586  N   TRP A  77     -44.204 -17.907-170.204  1.00209.25           N  
ANISOU  586  N   TRP A  77    33206  26481  19815   2950   3088    109       N  
ATOM    587  CA  TRP A  77     -42.829 -18.092-170.687  1.00212.55           C  
ANISOU  587  CA  TRP A  77    33581  27015  20164   3099   3319    142       C  
ATOM    588  C   TRP A  77     -42.784 -18.777-172.055  1.00215.88           C  
ANISOU  588  C   TRP A  77    34288  27371  20366   3341   3343     87       C  
ATOM    589  O   TRP A  77     -41.967 -18.419-172.905  1.00217.49           O  
ANISOU  589  O   TRP A  77    34531  27655  20450   3457   3556    134       O  
ATOM    590  CB  TRP A  77     -41.992 -18.863-169.658  1.00210.98           C  
ANISOU  590  CB  TRP A  77    33162  26897  20102   3100   3334    139       C  
ATOM    591  CG  TRP A  77     -40.501 -18.613-169.737  1.00211.46           C  
ANISOU  591  CG  TRP A  77    33057  27122  20165   3163   3598    215       C  
ATOM    592  CD1 TRP A  77     -39.876 -17.491-170.208  1.00211.65           C  
ANISOU  592  CD1 TRP A  77    33017  27246  20151   3130   3812    311       C  
ATOM    593  CD2 TRP A  77     -39.457 -19.492-169.292  1.00211.63           C  
ANISOU  593  CD2 TRP A  77    32942  27228  20237   3262   3669    210       C  
ATOM    594  NE1 TRP A  77     -38.513 -17.626-170.103  1.00213.19           N  
ANISOU  594  NE1 TRP A  77    33042  27587  20372   3202   4013    372       N  
ATOM    595  CE2 TRP A  77     -38.227 -18.843-169.543  1.00213.26           C  
ANISOU  595  CE2 TRP A  77    33003  27591  20433   3287   3932    310       C  
ATOM    596  CE3 TRP A  77     -39.441 -20.770-168.713  1.00209.14           C  
ANISOU  596  CE3 TRP A  77    32615  26872  19975   3332   3533    135       C  
ATOM    597  CZ2 TRP A  77     -36.994 -19.426-169.235  1.00213.44           C  
ANISOU  597  CZ2 TRP A  77    32864  27735  20498   3384   4065    338       C  
ATOM    598  CZ3 TRP A  77     -38.213 -21.350-168.409  1.00208.76           C  
ANISOU  598  CZ3 TRP A  77    32415  26939  19964   3431   3664    155       C  
ATOM    599  CH2 TRP A  77     -37.007 -20.676-168.670  1.00210.96           C  
ANISOU  599  CH2 TRP A  77    32544  27377  20232   3457   3930    256       C  
ATOM    600  N   PHE A  78     -43.665 -19.756-172.257  1.00216.92           N  
ANISOU  600  N   PHE A  78    34618  27355  20444   3416   3120     -5       N  
ATOM    601  CA  PHE A  78     -43.844 -20.388-173.561  1.00223.05           C  
ANISOU  601  CA  PHE A  78    35705  28038  21006   3637   3096    -67       C  
ATOM    602  C   PHE A  78     -44.968 -19.693-174.332  1.00226.97           C  
ANISOU  602  C   PHE A  78    36408  28422  21405   3591   3005    -74       C  
ATOM    603  O   PHE A  78     -46.117 -20.145-174.310  1.00228.68           O  
ANISOU  603  O   PHE A  78    36769  28495  21624   3559   2761   -134       O  
ATOM    604  CB  PHE A  78     -44.159 -21.885-173.417  1.00220.27           C  
ANISOU  604  CB  PHE A  78    35477  27574  20641   3755   2888   -165       C  
ATOM    605  CG  PHE A  78     -43.041 -22.703-172.825  1.00218.64           C  
ANISOU  605  CG  PHE A  78    35110  27463  20499   3842   2972   -170       C  
ATOM    606  CD1 PHE A  78     -41.785 -22.740-173.422  1.00221.94           C  
ANISOU  606  CD1 PHE A  78    35512  27999  20813   4016   3219   -138       C  
ATOM    607  CD2 PHE A  78     -43.258 -23.469-171.686  1.00214.70           C  
ANISOU  607  CD2 PHE A  78    34480  26936  20159   3757   2802   -204       C  
ATOM    608  CE1 PHE A  78     -40.762 -23.503-172.879  1.00221.57           C  
ANISOU  608  CE1 PHE A  78    35315  28043  20825   4102   3294   -141       C  
ATOM    609  CE2 PHE A  78     -42.241 -24.236-171.139  1.00215.12           C  
ANISOU  609  CE2 PHE A  78    34390  27074  20272   3839   2873   -211       C  
ATOM    610  CZ  PHE A  78     -40.991 -24.253-171.737  1.00218.39           C  
ANISOU  610  CZ  PHE A  78    34787  27606  20583   4013   3119   -181       C  
ATOM    611  N   THR A  86     -43.594  -8.229-164.623  1.00202.02           N  
ANISOU  611  N   THR A  86    30965  26013  19779   1481   3462    688       N  
ATOM    612  CA  THR A  86     -44.448  -8.318-163.441  1.00199.02           C  
ANISOU  612  CA  THR A  86    30509  25589  19518   1377   3274    648       C  
ATOM    613  C   THR A  86     -45.000  -9.734-163.253  1.00199.73           C  
ANISOU  613  C   THR A  86    30650  25627  19609   1474   3127    559       C  
ATOM    614  O   THR A  86     -44.836 -10.327-162.186  1.00203.59           O  
ANISOU  614  O   THR A  86    30985  26145  20224   1437   3057    542       O  
ATOM    615  CB  THR A  86     -45.604  -7.289-163.473  1.00195.59           C  
ANISOU  615  CB  THR A  86    30179  25079  19055   1280   3173    651       C  
ATOM    616  OG1 THR A  86     -46.564  -7.658-164.469  1.00196.60           O  
ANISOU  616  OG1 THR A  86    30540  25113  19044   1381   3094    595       O  
ATOM    617  CG2 THR A  86     -45.079  -5.892-163.774  1.00196.71           C  
ANISOU  617  CG2 THR A  86    30298  25259  19181   1190   3311    738       C  
ATOM    618  N   ALA A  87     -45.644 -10.270-164.291  1.00199.04           N  
ANISOU  618  N   ALA A  87    30783  25459  19381   1597   3076    506       N  
ATOM    619  CA  ALA A  87     -46.129 -11.653-164.285  1.00195.03           C  
ANISOU  619  CA  ALA A  87    30353  24890  18858   1702   2934    426       C  
ATOM    620  C   ALA A  87     -44.980 -12.634-164.523  1.00198.67           C  
ANISOU  620  C   ALA A  87    30770  25411  19302   1836   3046    414       C  
ATOM    621  O   ALA A  87     -45.173 -13.853-164.506  1.00196.76           O  
ANISOU  621  O   ALA A  87    30584  25124  19048   1934   2942    349       O  
ATOM    622  CB  ALA A  87     -47.224 -11.842-165.323  1.00190.88           C  
ANISOU  622  CB  ALA A  87    30088  24247  18187   1783   2828    377       C  
ATOM    623  N   PHE A  88     -43.788 -12.081-164.742  1.00204.90           N  
ANISOU  623  N   PHE A  88    31459  26302  20090   1838   3254    482       N  
ATOM    624  CA  PHE A  88     -42.562 -12.853-164.913  1.00211.87           C  
ANISOU  624  CA  PHE A  88    32267  27267  20964   1959   3389    490       C  
ATOM    625  C   PHE A  88     -42.097 -13.399-163.566  1.00210.65           C  
ANISOU  625  C   PHE A  88    31885  27169  20984   1892   3340    486       C  
ATOM    626  O   PHE A  88     -41.691 -14.558-163.467  1.00211.53           O  
ANISOU  626  O   PHE A  88    31980  27290  21101   2003   3322    442       O  
ATOM    627  CB  PHE A  88     -41.467 -11.972-165.521  1.00217.08           C  
ANISOU  627  CB  PHE A  88    32872  28029  21580   1964   3628    585       C  
ATOM    628  CG  PHE A  88     -40.509 -12.712-166.413  1.00225.87           C  
ANISOU  628  CG  PHE A  88    34037  29198  22582   2157   3781    587       C  
ATOM    629  CD1 PHE A  88     -39.609 -13.636-165.888  1.00228.09           C  
ANISOU  629  CD1 PHE A  88    34174  29552  22935   2226   3823    579       C  
ATOM    630  CD2 PHE A  88     -40.494 -12.471-167.784  1.00231.48           C  
ANISOU  630  CD2 PHE A  88    34945  29893  23112   2278   3888    600       C  
ATOM    631  CE1 PHE A  88     -38.724 -14.313-166.714  1.00235.13           C  
ANISOU  631  CE1 PHE A  88    35118  30502  23717   2419   3969    583       C  
ATOM    632  CE2 PHE A  88     -39.610 -13.143-168.615  1.00237.29           C  
ANISOU  632  CE2 PHE A  88    35736  30688  23736   2472   4036    605       C  
ATOM    633  CZ  PHE A  88     -38.723 -14.065-168.079  1.00238.78           C  
ANISOU  633  CZ  PHE A  88    35779  30952  23995   2545   4077    597       C  
ATOM    634  N   VAL A  89     -42.159 -12.553-162.538  1.00209.05           N  
ANISOU  634  N   VAL A  89    31513  26998  20916   1715   3314    532       N  
ATOM    635  CA  VAL A  89     -41.774 -12.935-161.175  1.00206.65           C  
ANISOU  635  CA  VAL A  89    30988  26745  20784   1633   3259    533       C  
ATOM    636  C   VAL A  89     -42.957 -12.904-160.196  1.00202.46           C  
ANISOU  636  C   VAL A  89    30438  26144  20341   1518   3048    495       C  
ATOM    637  O   VAL A  89     -42.807 -12.509-159.039  1.00202.00           O  
ANISOU  637  O   VAL A  89    30199  26127  20422   1389   3017    524       O  
ATOM    638  CB  VAL A  89     -40.599 -12.078-160.630  1.00206.47           C  
ANISOU  638  CB  VAL A  89    30747  26838  20865   1528   3416    627       C  
ATOM    639  CG1 VAL A  89     -39.273 -12.540-161.217  1.00209.42           C  
ANISOU  639  CG1 VAL A  89    31066  27305  21197   1653   3605    664       C  
ATOM    640  CG2 VAL A  89     -40.827 -10.592-160.886  1.00206.55           C  
ANISOU  640  CG2 VAL A  89    30783  26843  20852   1409   3469    694       C  
ATOM    641  N   GLU A  90     -44.131 -13.323-160.664  1.00199.30           N  
ANISOU  641  N   GLU A  90    30226  25640  19858   1569   2902    435       N  
ATOM    642  CA  GLU A  90     -45.310 -13.407-159.802  1.00192.71           C  
ANISOU  642  CA  GLU A  90    29377  24743  19098   1478   2698    405       C  
ATOM    643  C   GLU A  90     -45.246 -14.608-158.847  1.00191.32           C  
ANISOU  643  C   GLU A  90    29089  24574  19028   1493   2584    364       C  
ATOM    644  O   GLU A  90     -45.588 -14.466-157.673  1.00188.96           O  
ANISOU  644  O   GLU A  90    28652  24291  18854   1380   2488    374       O  
ATOM    645  CB  GLU A  90     -46.606 -13.425-160.616  1.00191.21           C  
ANISOU  645  CB  GLU A  90    29416  24443  18791   1518   2573    367       C  
ATOM    646  CG  GLU A  90     -47.832 -13.013-159.815  1.00188.44           C  
ANISOU  646  CG  GLU A  90    29041  24048  18508   1398   2401    368       C  
ATOM    647  CD  GLU A  90     -49.108 -13.671-160.304  1.00189.61           C  
ANISOU  647  CD  GLU A  90    29371  24087  18583   1454   2219    319       C  
ATOM    648  OE1 GLU A  90     -49.115 -14.909-160.485  1.00191.40           O  
ANISOU  648  OE1 GLU A  90    29655  24275  18792   1552   2142    270       O  
ATOM    649  OE2 GLU A  90     -50.111 -12.952-160.493  1.00188.55           O  
ANISOU  649  OE2 GLU A  90    29324  23904  18411   1400   2145    331       O  
ATOM    650  N   PRO A  91     -44.816 -15.792-159.341  1.00193.44           N  
ANISOU  650  N   PRO A  91    29423  24830  19244   1637   2591    318       N  
ATOM    651  CA  PRO A  91     -44.608 -16.904-158.406  1.00192.40           C  
ANISOU  651  CA  PRO A  91    29172  24712  19219   1649   2497    284       C  
ATOM    652  C   PRO A  91     -43.402 -16.696-157.487  1.00191.66           C  
ANISOU  652  C   PRO A  91    28834  24732  19254   1587   2617    329       C  
ATOM    653  O   PRO A  91     -43.330 -17.312-156.424  1.00190.14           O  
ANISOU  653  O   PRO A  91    28505  24558  19181   1546   2529    314       O  
ATOM    654  CB  PRO A  91     -44.373 -18.107-159.328  1.00194.77           C  
ANISOU  654  CB  PRO A  91    29629  24966  19409   1832   2492    226       C  
ATOM    655  CG  PRO A  91     -43.903 -17.520-160.612  1.00198.24           C  
ANISOU  655  CG  PRO A  91    30197  25420  19705   1919   2664    248       C  
ATOM    656  CD  PRO A  91     -44.647 -16.226-160.742  1.00197.14           C  
ANISOU  656  CD  PRO A  91    30096  25258  19548   1800   2659    288       C  
ATOM    657  N   PHE A  92     -42.472 -15.836-157.901  1.00193.45           N  
ANISOU  657  N   PHE A  92    29009  25034  19458   1577   2811    388       N  
ATOM    658  CA  PHE A  92     -41.303 -15.492-157.090  1.00193.18           C  
ANISOU  658  CA  PHE A  92    28742  25109  19546   1505   2929    444       C  
ATOM    659  C   PHE A  92     -41.659 -14.628-155.883  1.00190.41           C  
ANISOU  659  C   PHE A  92    28247  24773  19327   1324   2857    480       C  
ATOM    660  O   PHE A  92     -41.098 -14.812-154.806  1.00193.05           O  
ANISOU  660  O   PHE A  92    28392  25163  19794   1262   2848    494       O  
ATOM    661  CB  PHE A  92     -40.233 -14.793-157.934  1.00196.58           C  
ANISOU  661  CB  PHE A  92    29161  25616  19913   1542   3153    511       C  
ATOM    662  CG  PHE A  92     -39.186 -15.720-158.482  1.00199.12           C  
ANISOU  662  CG  PHE A  92    29474  25994  20186   1702   3273    503       C  
ATOM    663  CD1 PHE A  92     -38.033 -15.990-157.755  1.00198.79           C  
ANISOU  663  CD1 PHE A  92    29218  26053  20259   1689   3357    539       C  
ATOM    664  CD2 PHE A  92     -39.347 -16.317-159.728  1.00200.63           C  
ANISOU  664  CD2 PHE A  92    29876  26139  20215   1873   3300    460       C  
ATOM    665  CE1 PHE A  92     -37.061 -16.842-158.257  1.00201.74           C  
ANISOU  665  CE1 PHE A  92    29581  26485  20586   1847   3472    535       C  
ATOM    666  CE2 PHE A  92     -38.380 -17.171-160.235  1.00202.91           C  
ANISOU  666  CE2 PHE A  92    30164  26482  20448   2037   3413    452       C  
ATOM    667  CZ  PHE A  92     -37.235 -17.433-159.498  1.00204.04           C  
ANISOU  667  CZ  PHE A  92    30086  26732  20707   2026   3502    490       C  
ATOM    668  N   VAL A  93     -42.586 -13.689-156.066  1.00186.81           N  
ANISOU  668  N   VAL A  93    27884  24264  18829   1248   2805    493       N  
ATOM    669  CA  VAL A  93     -43.004 -12.802-154.979  1.00182.34           C  
ANISOU  669  CA  VAL A  93    27206  23706  18369   1090   2733    524       C  
ATOM    670  C   VAL A  93     -43.946 -13.519-154.011  1.00179.55           C  
ANISOU  670  C   VAL A  93    26823  23309  18089   1062   2534    477       C  
ATOM    671  O   VAL A  93     -43.737 -13.478-152.797  1.00180.64           O  
ANISOU  671  O   VAL A  93    26792  23488  18355    977   2490    491       O  
ATOM    672  CB  VAL A  93     -43.649 -11.496-155.498  1.00181.83           C  
ANISOU  672  CB  VAL A  93    27252  23602  18231   1023   2748    557       C  
ATOM    673  CG1 VAL A  93     -44.047 -10.596-154.338  1.00178.84           C  
ANISOU  673  CG1 VAL A  93    26763  23230  17955    874   2671    587       C  
ATOM    674  CG2 VAL A  93     -42.692 -10.751-156.414  1.00185.17           C  
ANISOU  674  CG2 VAL A  93    27694  24073  18588   1040   2945    616       C  
ATOM    675  N   ILE A  94     -44.970 -14.181-154.552  1.00177.86           N  
ANISOU  675  N   ILE A  94    26771  23013  17792   1135   2413    426       N  
ATOM    676  CA  ILE A  94     -45.927 -14.942-153.740  1.00176.00           C  
ANISOU  676  CA  ILE A  94    26516  22736  17618   1115   2218    391       C  
ATOM    677  C   ILE A  94     -45.224 -15.922-152.792  1.00174.38           C  
ANISOU  677  C   ILE A  94    26148  22579  17530   1124   2194    375       C  
ATOM    678  O   ILE A  94     -45.535 -15.957-151.599  1.00173.99           O  
ANISOU  678  O   ILE A  94    25969  22548  17590   1039   2096    384       O  
ATOM    679  CB  ILE A  94     -46.999 -15.643-154.612  1.00177.38           C  
ANISOU  679  CB  ILE A  94    26898  22812  17683   1203   2093    344       C  
ATOM    680  CG1 ILE A  94     -48.095 -14.641-154.997  1.00176.74           C  
ANISOU  680  CG1 ILE A  94    26934  22681  17536   1148   2043    364       C  
ATOM    681  CG2 ILE A  94     -47.611 -16.842-153.892  1.00175.38           C  
ANISOU  681  CG2 ILE A  94    26613  22525  17498   1215   1910    310       C  
ATOM    682  CD1 ILE A  94     -49.102 -15.158-156.003  1.00178.34           C  
ANISOU  682  CD1 ILE A  94    27353  22785  17620   1231   1934    327       C  
ATOM    683  N   LEU A  95     -44.267 -16.688-153.316  1.00172.46           N  
ANISOU  683  N   LEU A  95    25909  22360  17258   1231   2288    355       N  
ATOM    684  CA  LEU A  95     -43.489 -17.614-152.494  1.00169.96           C  
ANISOU  684  CA  LEU A  95    25439  22091  17045   1250   2280    341       C  
ATOM    685  C   LEU A  95     -42.675 -16.884-151.429  1.00170.72           C  
ANISOU  685  C   LEU A  95    25317  22276  17271   1134   2357    393       C  
ATOM    686  O   LEU A  95     -42.605 -17.337-150.289  1.00175.43           O  
ANISOU  686  O   LEU A  95    25774  22897  17985   1085   2276    387       O  
ATOM    687  CB  LEU A  95     -42.570 -18.491-153.349  1.00170.72           C  
ANISOU  687  CB  LEU A  95    25592  22201  17072   1402   2381    312       C  
ATOM    688  CG  LEU A  95     -41.866 -19.653-152.633  1.00169.81           C  
ANISOU  688  CG  LEU A  95    25351  22120  17046   1449   2353    285       C  
ATOM    689  CD1 LEU A  95     -42.838 -20.789-152.344  1.00168.98           C  
ANISOU  689  CD1 LEU A  95    25324  21931  16949   1482   2143    228       C  
ATOM    690  CD2 LEU A  95     -40.681 -20.165-153.438  1.00171.02           C  
ANISOU  690  CD2 LEU A  95    25524  22320  17136   1592   2510    278       C  
ATOM    691  N   LEU A  96     -42.071 -15.757-151.802  1.00170.43           N  
ANISOU  691  N   LEU A  96    25257  22284  17214   1089   2507    446       N  
ATOM    692  CA  LEU A  96     -41.262 -14.969-150.868  1.00169.75           C  
ANISOU  692  CA  LEU A  96    24976  22274  17247    973   2577    503       C  
ATOM    693  C   LEU A  96     -42.076 -14.310-149.753  1.00165.34           C  
ANISOU  693  C   LEU A  96    24355  21697  16768    843   2452    515       C  
ATOM    694  O   LEU A  96     -41.589 -14.159-148.631  1.00161.46           O  
ANISOU  694  O   LEU A  96    23694  21254  16399    762   2439    538       O  
ATOM    695  CB  LEU A  96     -40.433 -13.918-151.609  1.00171.88           C  
ANISOU  695  CB  LEU A  96    25245  22590  17471    954   2760    567       C  
ATOM    696  CG  LEU A  96     -39.156 -14.397-152.301  1.00176.21           C  
ANISOU  696  CG  LEU A  96    25755  23205  17991   1057   2927    587       C  
ATOM    697  CD1 LEU A  96     -38.581 -13.274-153.149  1.00183.35           C  
ANISOU  697  CD1 LEU A  96    26686  24146  18833   1034   3093    660       C  
ATOM    698  CD2 LEU A  96     -38.121 -14.906-151.308  1.00175.17           C  
ANISOU  698  CD2 LEU A  96    25409  23150  17997   1034   2952    603       C  
ATOM    699  N   ILE A  97     -43.307 -13.916-150.069  1.00163.52           N  
ANISOU  699  N   ILE A  97    24264  21399  16465    829   2358    502       N  
ATOM    700  CA  ILE A  97     -44.208 -13.356-149.068  1.00163.27           C  
ANISOU  700  CA  ILE A  97    24190  21351  16491    727   2232    512       C  
ATOM    701  C   ILE A  97     -44.700 -14.442-148.117  1.00162.66           C  
ANISOU  701  C   ILE A  97    24042  21267  16491    736   2081    477       C  
ATOM    702  O   ILE A  97     -44.710 -14.245-146.904  1.00166.13           O  
ANISOU  702  O   ILE A  97    24347  21739  17034    656   2023    494       O  
ATOM    703  CB  ILE A  97     -45.389 -12.590-149.711  1.00164.43           C  
ANISOU  703  CB  ILE A  97    24505  21434  16535    715   2181    514       C  
ATOM    704  CG1 ILE A  97     -44.953 -11.167-150.076  1.00166.90           C  
ANISOU  704  CG1 ILE A  97    24832  21763  16817    649   2303    565       C  
ATOM    705  CG2 ILE A  97     -46.595 -12.546-148.778  1.00163.08           C  
ANISOU  705  CG2 ILE A  97    24317  21239  16406    661   2012    509       C  
ATOM    706  CD1 ILE A  97     -45.982 -10.364-150.849  1.00167.51           C  
ANISOU  706  CD1 ILE A  97    25084  21779  16783    646   2274    568       C  
ATOM    707  N   LEU A  98     -45.079 -15.593-148.664  1.00162.35           N  
ANISOU  707  N   LEU A  98    24098  21185  16402    834   2015    432       N  
ATOM    708  CA  LEU A  98     -45.665 -16.661-147.855  1.00160.89           C  
ANISOU  708  CA  LEU A  98    23864  20983  16282    842   1856    405       C  
ATOM    709  C   LEU A  98     -44.665 -17.417-146.975  1.00161.89           C  
ANISOU  709  C   LEU A  98    23819  21167  16523    843   1874    398       C  
ATOM    710  O   LEU A  98     -45.052 -17.953-145.936  1.00159.22           O  
ANISOU  710  O   LEU A  98    23390  20835  16269    807   1752    394       O  
ATOM    711  CB  LEU A  98     -46.489 -17.623-148.716  1.00161.10           C  
ANISOU  711  CB  LEU A  98    24060  20931  16218    937   1753    363       C  
ATOM    712  CG  LEU A  98     -47.786 -17.068-149.318  1.00160.18           C  
ANISOU  712  CG  LEU A  98    24100  20751  16010    926   1674    371       C  
ATOM    713  CD1 LEU A  98     -48.475 -18.129-150.160  1.00162.58           C  
ANISOU  713  CD1 LEU A  98    24568  20973  16233   1021   1565    331       C  
ATOM    714  CD2 LEU A  98     -48.734 -16.539-148.251  1.00157.13           C  
ANISOU  714  CD2 LEU A  98    23635  20377  15688    826   1560    405       C  
ATOM    715  N   ILE A  99     -43.393 -17.459-147.381  1.00165.79           N  
ANISOU  715  N   ILE A  99    24266  21706  17018    885   2025    402       N  
ATOM    716  CA  ILE A  99     -42.342 -17.985-146.499  1.00167.76           C  
ANISOU  716  CA  ILE A  99    24335  22020  17384    874   2058    404       C  
ATOM    717  C   ILE A  99     -42.067 -16.996-145.368  1.00168.08           C  
ANISOU  717  C   ILE A  99    24220  22111  17529    744   2071    451       C  
ATOM    718  O   ILE A  99     -41.691 -17.394-144.270  1.00172.91           O  
ANISOU  718  O   ILE A  99    24683  22760  18252    705   2026    452       O  
ATOM    719  CB  ILE A  99     -41.013 -18.361-147.219  1.00170.22           C  
ANISOU  719  CB  ILE A  99    24625  22376  17672    964   2218    403       C  
ATOM    720  CG1 ILE A  99     -40.291 -17.125-147.773  1.00172.03           C  
ANISOU  720  CG1 ILE A  99    24840  22651  17871    925   2390    459       C  
ATOM    721  CG2 ILE A  99     -41.238 -19.421-148.292  1.00171.43           C  
ANISOU  721  CG2 ILE A  99    24943  22475  17716   1110   2198    350       C  
ATOM    722  CD1 ILE A  99     -38.784 -17.273-147.834  1.00173.89           C  
ANISOU  722  CD1 ILE A  99    24946  22969  18153    958   2545    489       C  
ATOM    723  N   ALA A 100     -42.263 -15.709-145.645  1.00167.77           N  
ANISOU  723  N   ALA A 100    24225  22069  17450    679   2127    488       N  
ATOM    724  CA  ALA A 100     -42.142 -14.678-144.623  1.00167.20           C  
ANISOU  724  CA  ALA A 100    24038  22029  17462    557   2120    531       C  
ATOM    725  C   ALA A 100     -43.391 -14.648-143.749  1.00167.33           C  
ANISOU  725  C   ALA A 100    24062  22014  17500    512   1955    521       C  
ATOM    726  O   ALA A 100     -43.300 -14.444-142.539  1.00169.49           O  
ANISOU  726  O   ALA A 100    24209  22317  17869    441   1902    536       O  
ATOM    727  CB  ALA A 100     -41.894 -13.319-145.259  1.00168.96           C  
ANISOU  727  CB  ALA A 100    24315  22252  17629    507   2232    576       C  
ATOM    728  N   ASN A 101     -44.550 -14.862-144.369  1.00169.09           N  
ANISOU  728  N   ASN A 101    24433  22180  17632    557   1874    499       N  
ATOM    729  CA  ASN A 101     -45.827 -14.910-143.656  1.00170.64           C  
ANISOU  729  CA  ASN A 101    24643  22354  17840    527   1717    500       C  
ATOM    730  C   ASN A 101     -45.878 -16.104-142.710  1.00171.32           C  
ANISOU  730  C   ASN A 101    24621  22457  18015    541   1609    482       C  
ATOM    731  O   ASN A 101     -46.479 -16.027-141.634  1.00170.46           O  
ANISOU  731  O   ASN A 101    24437  22364  17964    490   1507    498       O  
ATOM    732  CB  ASN A 101     -47.000 -14.959-144.642  1.00172.14           C  
ANISOU  732  CB  ASN A 101    25013  22478  17912    577   1655    487       C  
ATOM    733  CG  ASN A 101     -48.299 -14.441-144.042  1.00169.31           C  
ANISOU  733  CG  ASN A 101    24674  22107  17548    530   1531    511       C  
ATOM    734  OD1 ASN A 101     -49.293 -15.164-143.972  1.00168.82           O  
ANISOU  734  OD1 ASN A 101    24651  22017  17474    558   1401    505       O  
ATOM    735  ND2 ASN A 101     -48.298 -13.183-143.612  1.00165.48           N  
ANISOU  735  ND2 ASN A 101    24162  21642  17070    460   1568    542       N  
ATOM    736  N   ALA A 102     -45.240 -17.200-143.120  1.00170.29           N  
ANISOU  736  N   ALA A 102    24487  22324  17891    614   1635    449       N  
ATOM    737  CA  ALA A 102     -45.082 -18.374-142.268  1.00166.67           C  
ANISOU  737  CA  ALA A 102    23923  21882  17522    629   1546    431       C  
ATOM    738  C   ALA A 102     -44.233 -18.037-141.044  1.00164.46           C  
ANISOU  738  C   ALA A 102    23457  21667  17360    556   1581    453       C  
ATOM    739  O   ALA A 102     -44.694 -18.200-139.915  1.00165.93           O  
ANISOU  739  O   ALA A 102    23555  21870  17617    510   1474    464       O  
ATOM    740  CB  ALA A 102     -44.472 -19.531-143.046  1.00165.23           C  
ANISOU  740  CB  ALA A 102    23788  21680  17310    733   1578    389       C  
ATOM    741  N   ILE A 103     -43.016 -17.541-141.273  1.00160.79           N  
ANISOU  741  N   ILE A 103    22934  21240  16916    545   1726    465       N  
ATOM    742  CA  ILE A 103     -42.078 -17.230-140.185  1.00159.35           C  
ANISOU  742  CA  ILE A 103    22577  21118  16851    475   1762    488       C  
ATOM    743  C   ILE A 103     -42.647 -16.211-139.191  1.00160.59           C  
ANISOU  743  C   ILE A 103    22691  21281  17044    378   1698    520       C  
ATOM    744  O   ILE A 103     -42.439 -16.339-137.984  1.00163.28           O  
ANISOU  744  O   ILE A 103    22904  21653  17481    332   1641    528       O  
ATOM    745  CB  ILE A 103     -40.692 -16.779-140.708  1.00158.72           C  
ANISOU  745  CB  ILE A 103    22444  21078  16783    474   1932    510       C  
ATOM    746  CG1 ILE A 103     -40.083 -17.847-141.621  1.00163.00           C  
ANISOU  746  CG1 ILE A 103    23023  21622  17286    588   1999    479       C  
ATOM    747  CG2 ILE A 103     -39.737 -16.503-139.551  1.00156.59           C  
ANISOU  747  CG2 ILE A 103    21991  20864  16642    396   1952    539       C  
ATOM    748  CD1 ILE A 103     -38.872 -17.387-142.409  1.00167.41           C  
ANISOU  748  CD1 ILE A 103    23557  22224  17825    608   2179    510       C  
ATOM    749  N   VAL A 104     -43.375 -15.217-139.695  1.00162.98           N  
ANISOU  749  N   VAL A 104    23107  21553  17264    355   1704    537       N  
ATOM    750  CA  VAL A 104     -44.027 -14.225-138.834  1.00163.69           C  
ANISOU  750  CA  VAL A 104    23181  21643  17367    281   1638    564       C  
ATOM    751  C   VAL A 104     -44.998 -14.872-137.839  1.00162.54           C  
ANISOU  751  C   VAL A 104    22996  21503  17258    286   1486    559       C  
ATOM    752  O   VAL A 104     -45.005 -14.513-136.663  1.00167.33           O  
ANISOU  752  O   VAL A 104    23508  22138  17931    233   1435    577       O  
ATOM    753  CB  VAL A 104     -44.743 -13.122-139.654  1.00164.39           C  
ANISOU  753  CB  VAL A 104    23418  21693  17349    271   1664    580       C  
ATOM    754  CG1 VAL A 104     -45.775 -12.384-138.810  1.00162.13           C  
ANISOU  754  CG1 VAL A 104    23144  21402  17056    228   1561    600       C  
ATOM    755  CG2 VAL A 104     -43.732 -12.136-140.216  1.00165.10           C  
ANISOU  755  CG2 VAL A 104    23512  21790  17429    229   1805    606       C  
ATOM    756  N   GLY A 105     -45.791 -15.834-138.311  1.00160.04           N  
ANISOU  756  N   GLY A 105    22750  21158  16897    349   1410    538       N  
ATOM    757  CA  GLY A 105     -46.818 -16.480-137.485  1.00156.43           C  
ANISOU  757  CA  GLY A 105    22262  20706  16467    353   1261    547       C  
ATOM    758  C   GLY A 105     -46.462 -17.845-136.914  1.00152.03           C  
ANISOU  758  C   GLY A 105    21606  20165  15991    379   1199    528       C  
ATOM    759  O   GLY A 105     -47.297 -18.496-136.279  1.00147.29           O  
ANISOU  759  O   GLY A 105    20978  19570  15416    383   1072    541       O  
ATOM    760  N   VAL A 106     -45.229 -18.283-137.151  1.00151.28           N  
ANISOU  760  N   VAL A 106    21459  20083  15938    399   1289    503       N  
ATOM    761  CA  VAL A 106     -44.724 -19.538-136.599  1.00150.73           C  
ANISOU  761  CA  VAL A 106    21291  20029  15949    426   1242    482       C  
ATOM    762  C   VAL A 106     -43.754 -19.256-135.457  1.00154.40           C  
ANISOU  762  C   VAL A 106    21592  20548  16522    369   1278    494       C  
ATOM    763  O   VAL A 106     -43.821 -19.895-134.404  1.00157.10           O  
ANISOU  763  O   VAL A 106    21834  20914  16943    355   1189    496       O  
ATOM    764  CB  VAL A 106     -44.095 -20.432-137.695  1.00146.86           C  
ANISOU  764  CB  VAL A 106    20866  19511  15422    511   1302    442       C  
ATOM    765  CG1 VAL A 106     -42.821 -21.115-137.220  1.00143.76           C  
ANISOU  765  CG1 VAL A 106    20342  19157  15120    526   1352    424       C  
ATOM    766  CG2 VAL A 106     -45.114 -21.447-138.191  1.00146.12           C  
ANISOU  766  CG2 VAL A 106    20881  19361  15274    570   1178    425       C  
ATOM    767  N   TRP A 107     -42.870 -18.284-135.669  1.00158.21           N  
ANISOU  767  N   TRP A 107    22052  21049  17010    332   1401    505       N  
ATOM    768  CA  TRP A 107     -41.940 -17.837-134.640  1.00163.24           C  
ANISOU  768  CA  TRP A 107    22545  21730  17747    267   1433    523       C  
ATOM    769  C   TRP A 107     -42.681 -17.187-133.462  1.00160.19           C  
ANISOU  769  C   TRP A 107    22123  21355  17387    207   1336    549       C  
ATOM    770  O   TRP A 107     -42.245 -17.294-132.313  1.00162.77           O  
ANISOU  770  O   TRP A 107    22326  21713  17804    169   1298    556       O  
ATOM    771  CB  TRP A 107     -40.902 -16.886-135.241  1.00171.71           C  
ANISOU  771  CB  TRP A 107    23613  22814  18813    235   1579    543       C  
ATOM    772  CG  TRP A 107     -40.179 -16.083-134.225  1.00184.79           C  
ANISOU  772  CG  TRP A 107    25151  24502  20559    148   1593    573       C  
ATOM    773  CD1 TRP A 107     -39.102 -16.474-133.487  1.00188.08           C  
ANISOU  773  CD1 TRP A 107    25419  24957  21084    125   1611    577       C  
ATOM    774  CD2 TRP A 107     -40.489 -14.748-133.812  1.00193.31           C  
ANISOU  774  CD2 TRP A 107    26257  25569  21623     75   1580    604       C  
ATOM    775  NE1 TRP A 107     -38.716 -15.463-132.640  1.00195.43           N  
ANISOU  775  NE1 TRP A 107    26283  25898  22071     37   1605    609       N  
ATOM    776  CE2 TRP A 107     -39.551 -14.392-132.819  1.00196.84           C  
ANISOU  776  CE2 TRP A 107    26571  26043  22174      7   1584    625       C  
ATOM    777  CE3 TRP A 107     -41.469 -13.818-134.185  1.00196.30           C  
ANISOU  777  CE3 TRP A 107    26763  25913  21909     64   1559    615       C  
ATOM    778  CZ2 TRP A 107     -39.561 -13.142-132.193  1.00198.39           C  
ANISOU  778  CZ2 TRP A 107    26769  26228  22382    -70   1563    655       C  
ATOM    779  CZ3 TRP A 107     -41.478 -12.576-133.563  1.00198.71           C  
ANISOU  779  CZ3 TRP A 107    27067  26210  22224     -8   1544    644       C  
ATOM    780  CH2 TRP A 107     -40.528 -12.250-132.579  1.00197.66           C  
ANISOU  780  CH2 TRP A 107    26810  26099  22193    -74   1543    663       C  
ATOM    781  N   GLN A 108     -43.795 -16.519-133.760  1.00154.15           N  
ANISOU  781  N   GLN A 108    21468  20564  16536    205   1297    563       N  
ATOM    782  CA  GLN A 108     -44.694 -15.979-132.740  1.00147.60           C  
ANISOU  782  CA  GLN A 108    20624  19746  15709    173   1200    589       C  
ATOM    783  C   GLN A 108     -45.306 -17.106-131.916  1.00144.05           C  
ANISOU  783  C   GLN A 108    20109  19318  15305    198   1077    590       C  
ATOM    784  O   GLN A 108     -45.438 -16.991-130.697  1.00141.10           O  
ANISOU  784  O   GLN A 108    19649  18976  14984    171   1012    608       O  
ATOM    785  CB  GLN A 108     -45.809 -15.168-133.397  1.00149.35           C  
ANISOU  785  CB  GLN A 108    20986  19938  15821    183   1186    604       C  
ATOM    786  CG  GLN A 108     -45.507 -13.689-133.581  1.00151.23           C  
ANISOU  786  CG  GLN A 108    21273  20162  16023    134   1261    620       C  
ATOM    787  CD  GLN A 108     -46.325 -12.795-132.666  1.00153.69           C  
ANISOU  787  CD  GLN A 108    21595  20482  16314    110   1185    647       C  
ATOM    788  OE1 GLN A 108     -45.850 -11.749-132.226  1.00158.93           O  
ANISOU  788  OE1 GLN A 108    22249  21143  16993     60   1214    659       O  
ATOM    789  NE2 GLN A 108     -47.564 -13.195-132.385  1.00152.98           N  
ANISOU  789  NE2 GLN A 108    21532  20404  16189    150   1084    660       N  
ATOM    790  N   GLU A 109     -45.671 -18.191-132.596  1.00142.66           N  
ANISOU  790  N   GLU A 109    19979  19120  15104    253   1041    573       N  
ATOM    791  CA  GLU A 109     -46.252 -19.365-131.953  1.00142.47           C  
ANISOU  791  CA  GLU A 109    19901  19107  15121    275    918    579       C  
ATOM    792  C   GLU A 109     -45.243 -20.100-131.066  1.00145.05           C  
ANISOU  792  C   GLU A 109    20086  19465  15559    264    914    564       C  
ATOM    793  O   GLU A 109     -45.554 -20.430-129.920  1.00148.43           O  
ANISOU  793  O   GLU A 109    20425  19926  16044    246    825    585       O  
ATOM    794  CB  GLU A 109     -46.848 -20.315-133.000  1.00141.35           C  
ANISOU  794  CB  GLU A 109    19862  18920  14922    334    873    564       C  
ATOM    795  CG  GLU A 109     -47.504 -21.570-132.433  1.00140.57           C  
ANISOU  795  CG  GLU A 109    19719  18824  14865    351    731    579       C  
ATOM    796  CD  GLU A 109     -48.763 -21.281-131.632  1.00140.14           C  
ANISOU  796  CD  GLU A 109    19644  18800  14802    327    624    636       C  
ATOM    797  OE1 GLU A 109     -49.779 -20.875-132.236  1.00139.76           O  
ANISOU  797  OE1 GLU A 109    19697  18731  14672    338    594    661       O  
ATOM    798  OE2 GLU A 109     -48.739 -21.473-130.397  1.00139.03           O  
ANISOU  798  OE2 GLU A 109    19385  18707  14732    302    569    660       O  
ATOM    799  N   ARG A 110     -44.042 -20.349-131.588  1.00145.53           N  
ANISOU  799  N   ARG A 110    20124  19521  15648    278   1012    531       N  
ATOM    800  CA  ARG A 110     -43.024 -21.078-130.831  1.00145.71           C  
ANISOU  800  CA  ARG A 110    20012  19573  15775    273   1014    516       C  
ATOM    801  C   ARG A 110     -42.542 -20.292-129.618  1.00144.29           C  
ANISOU  801  C   ARG A 110    19721  19433  15668    205   1019    537       C  
ATOM    802  O   ARG A 110     -42.220 -20.883-128.591  1.00150.22           O  
ANISOU  802  O   ARG A 110    20360  20211  16503    193    962    537       O  
ATOM    803  CB  ARG A 110     -41.842 -21.495-131.712  1.00151.84           C  
ANISOU  803  CB  ARG A 110    20788  20343  16561    313   1126    482       C  
ATOM    804  CG  ARG A 110     -41.041 -22.656-131.133  1.00157.93           C  
ANISOU  804  CG  ARG A 110    21447  21134  17425    337   1099    460       C  
ATOM    805  CD  ARG A 110     -39.947 -23.157-132.067  1.00164.53           C  
ANISOU  805  CD  ARG A 110    22289  21968  18256    399   1209    429       C  
ATOM    806  NE  ARG A 110     -38.810 -22.238-132.147  1.00168.26           N  
ANISOU  806  NE  ARG A 110    22694  22475  18760    360   1344    446       N  
ATOM    807  CZ  ARG A 110     -37.565 -22.594-132.460  1.00170.12           C  
ANISOU  807  CZ  ARG A 110    22860  22739  19036    394   1443    436       C  
ATOM    808  NH1 ARG A 110     -37.265 -23.862-132.715  1.00169.24           N  
ANISOU  808  NH1 ARG A 110    22747  22622  18934    477   1424    400       N  
ATOM    809  NH2 ARG A 110     -36.608 -21.676-132.506  1.00170.78           N  
ANISOU  809  NH2 ARG A 110    22877  22857  19152    345   1557    467       N  
ATOM    810  N   ASN A 111     -42.502 -18.967-129.737  1.00141.90           N  
ANISOU  810  N   ASN A 111    19457  19128  15329    162   1079    555       N  
ATOM    811  CA  ASN A 111     -42.163 -18.098-128.609  1.00141.88           C  
ANISOU  811  CA  ASN A 111    19375  19149  15381    100   1068    577       C  
ATOM    812  C   ASN A 111     -43.188 -18.143-127.480  1.00137.35           C  
ANISOU  812  C   ASN A 111    18779  18596  14809     97    944    599       C  
ATOM    813  O   ASN A 111     -42.824 -18.230-126.304  1.00133.13           O  
ANISOU  813  O   ASN A 111    18142  18090  14350     71    898    606       O  
ATOM    814  CB  ASN A 111     -41.965 -16.656-129.072  1.00147.91           C  
ANISOU  814  CB  ASN A 111    20207  19895  16096     56   1149    593       C  
ATOM    815  CG  ASN A 111     -40.506 -16.256-129.114  1.00153.17           C  
ANISOU  815  CG  ASN A 111    20795  20569  16831     10   1247    596       C  
ATOM    816  OD1 ASN A 111     -39.938 -16.045-130.186  1.00154.89           O  
ANISOU  816  OD1 ASN A 111    21053  20777  17020     15   1353    596       O  
ATOM    817  ND2 ASN A 111     -39.887 -16.156-127.940  1.00155.10           N  
ANISOU  817  ND2 ASN A 111    20926  20837  17168    -35   1211    605       N  
ATOM    818  N   ALA A 112     -44.465 -18.084-127.853  1.00135.33           N  
ANISOU  818  N   ALA A 112    18620  18329  14469    128    891    616       N  
ATOM    819  CA  ALA A 112     -45.569 -18.152-126.901  1.00131.25           C  
ANISOU  819  CA  ALA A 112    18086  17841  13941    138    778    650       C  
ATOM    820  C   ALA A 112     -45.551 -19.472-126.139  1.00129.88           C  
ANISOU  820  C   ALA A 112    17808  17694  13843    153    693    652       C  
ATOM    821  O   ALA A 112     -45.688 -19.491-124.916  1.00130.46           O  
ANISOU  821  O   ALA A 112    17801  17806  13961    141    628    674       O  
ATOM    822  CB  ALA A 112     -46.899 -17.966-127.616  1.00128.84           C  
ANISOU  822  CB  ALA A 112    17896  17520  13533    171    741    673       C  
ATOM    823  N   GLU A 113     -45.362 -20.568-126.871  1.00129.41           N  
ANISOU  823  N   GLU A 113    17760  17612  13795    184    693    628       N  
ATOM    824  CA  GLU A 113     -45.333 -21.903-126.284  1.00128.56           C  
ANISOU  824  CA  GLU A 113    17569  17519  13757    200    607    628       C  
ATOM    825  C   GLU A 113     -44.147 -22.084-125.339  1.00128.44           C  
ANISOU  825  C   GLU A 113    17424  17530  13844    173    628    610       C  
ATOM    826  O   GLU A 113     -44.277 -22.725-124.296  1.00127.22           O  
ANISOU  826  O   GLU A 113    17181  17405  13749    169    543    627       O  
ATOM    827  CB  GLU A 113     -45.332 -22.972-127.378  1.00131.07           C  
ANISOU  827  CB  GLU A 113    17950  17795  14055    245    601    601       C  
ATOM    828  CG  GLU A 113     -46.626 -23.024-128.183  1.00137.24           C  
ANISOU  828  CG  GLU A 113    18852  18547  14746    271    545    625       C  
ATOM    829  CD  GLU A 113     -46.671 -24.172-129.179  1.00143.50           C  
ANISOU  829  CD  GLU A 113    19716  19287  15518    320    514    598       C  
ATOM    830  OE1 GLU A 113     -46.050 -25.225-128.916  1.00150.04           O  
ANISOU  830  OE1 GLU A 113    20484  20112  16413    336    483    574       O  
ATOM    831  OE2 GLU A 113     -47.339 -24.028-130.227  1.00142.00           O  
ANISOU  831  OE2 GLU A 113    19652  19057  15244    344    512    599       O  
ATOM    832  N   ASN A 114     -43.005 -21.505-125.704  1.00130.69           N  
ANISOU  832  N   ASN A 114    17697  17806  14152    152    739    583       N  
ATOM    833  CA  ASN A 114     -41.814 -21.523-124.855  1.00132.13           C  
ANISOU  833  CA  ASN A 114    17757  18013  14435    118    764    571       C  
ATOM    834  C   ASN A 114     -42.039 -20.783-123.551  1.00131.95           C  
ANISOU  834  C   ASN A 114    17681  18018  14435     78    709    599       C  
ATOM    835  O   ASN A 114     -41.666 -21.270-122.486  1.00134.68           O  
ANISOU  835  O   ASN A 114    17923  18389  14859     67    655    601       O  
ATOM    836  CB  ASN A 114     -40.607 -20.922-125.580  1.00134.89           C  
ANISOU  836  CB  ASN A 114    18103  18349  14797     98    896    552       C  
ATOM    837  CG  ASN A 114     -39.898 -21.923-126.475  1.00138.83           C  
ANISOU  837  CG  ASN A 114    18598  18838  15312    147    952    519       C  
ATOM    838  OD1 ASN A 114     -40.420 -22.999-126.773  1.00140.27           O  
ANISOU  838  OD1 ASN A 114    18813  19006  15476    199    892    505       O  
ATOM    839  ND2 ASN A 114     -38.697 -21.567-126.913  1.00142.95           N  
ANISOU  839  ND2 ASN A 114    19080  19367  15866    133   1066    512       N  
ATOM    840  N   ALA A 115     -42.658 -19.608-123.646  1.00131.31           N  
ANISOU  840  N   ALA A 115    17680  17930  14282     64    721    620       N  
ATOM    841  CA  ALA A 115     -42.950 -18.778-122.478  1.00130.85           C  
ANISOU  841  CA  ALA A 115    17599  17893  14224     40    670    646       C  
ATOM    842  C   ALA A 115     -43.954 -19.443-121.534  1.00127.33           C  
ANISOU  842  C   ALA A 115    17115  17485  13776     73    554    677       C  
ATOM    843  O   ALA A 115     -43.914 -19.231-120.316  1.00126.91           O  
ANISOU  843  O   ALA A 115    17001  17461  13756     64    501    692       O  
ATOM    844  CB  ALA A 115     -43.454 -17.411-122.916  1.00133.25           C  
ANISOU  844  CB  ALA A 115    18015  18175  14437     30    706    659       C  
ATOM    845  N   ILE A 116     -44.850 -20.242-122.106  1.00121.96           N  
ANISOU  845  N   ILE A 116    16475  16807  13057    111    513    690       N  
ATOM    846  CA  ILE A 116     -45.816 -20.998-121.327  1.00117.35           C  
ANISOU  846  CA  ILE A 116    15847  16263  12476    137    402    733       C  
ATOM    847  C   ILE A 116     -45.151 -22.224-120.714  1.00120.07           C  
ANISOU  847  C   ILE A 116    16080  16620  12920    133    358    719       C  
ATOM    848  O   ILE A 116     -45.419 -22.566-119.563  1.00123.04           O  
ANISOU  848  O   ILE A 116    16380  17037  13332    136    281    750       O  
ATOM    849  CB  ILE A 116     -47.038 -21.387-122.174  1.00114.30           C  
ANISOU  849  CB  ILE A 116    15543  15869  12015    170    361    763       C  
ATOM    850  CG1 ILE A 116     -47.957 -20.174-122.336  1.00113.43           C  
ANISOU  850  CG1 ILE A 116    15523  15768  11807    182    374    794       C  
ATOM    851  CG2 ILE A 116     -47.796 -22.536-121.527  1.00114.69           C  
ANISOU  851  CG2 ILE A 116    15528  15954  12095    189    244    809       C  
ATOM    852  CD1 ILE A 116     -48.849 -20.213-123.558  1.00112.19           C  
ANISOU  852  CD1 ILE A 116    15475  15583  11570    205    374    806       C  
ATOM    853  N   GLU A 117     -44.274 -22.870-121.480  1.00122.23           N  
ANISOU  853  N   GLU A 117    16348  16859  13235    132    409    675       N  
ATOM    854  CA  GLU A 117     -43.490 -24.004-120.981  1.00125.56           C  
ANISOU  854  CA  GLU A 117    16667  17286  13752    133    376    654       C  
ATOM    855  C   GLU A 117     -42.581 -23.594-119.812  1.00123.87           C  
ANISOU  855  C   GLU A 117    16352  17098  13615     98    385    647       C  
ATOM    856  O   GLU A 117     -42.422 -24.343-118.844  1.00121.96           O  
ANISOU  856  O   GLU A 117    16018  16881  13440     97    315    655       O  
ATOM    857  CB  GLU A 117     -42.670 -24.631-122.121  1.00130.43           C  
ANISOU  857  CB  GLU A 117    17309  17862  14383    152    445    605       C  
ATOM    858  CG  GLU A 117     -41.995 -25.961-121.792  1.00134.91           C  
ANISOU  858  CG  GLU A 117    17793  18430  15037    169    403    582       C  
ATOM    859  CD  GLU A 117     -42.967 -27.037-121.328  1.00137.69           C  
ANISOU  859  CD  GLU A 117    18132  18788  15395    187    268    616       C  
ATOM    860  OE1 GLU A 117     -44.033 -27.211-121.959  1.00140.83           O  
ANISOU  860  OE1 GLU A 117    18618  19168  15724    206    222    641       O  
ATOM    861  OE2 GLU A 117     -42.657 -27.720-120.328  1.00137.65           O  
ANISOU  861  OE2 GLU A 117    18027  18806  15466    179    205    622       O  
ATOM    862  N   ALA A 118     -42.014 -22.392-119.905  1.00122.61           N  
ANISOU  862  N   ALA A 118    16214  16928  13443     66    463    636       N  
ATOM    863  CA  ALA A 118     -41.078 -21.882-118.904  1.00122.26           C  
ANISOU  863  CA  ALA A 118    16087  16895  13470     26    470    629       C  
ATOM    864  C   ALA A 118     -41.741 -21.501-117.580  1.00121.06           C  
ANISOU  864  C   ALA A 118    15913  16776  13307     28    383    664       C  
ATOM    865  O   ALA A 118     -41.045 -21.229-116.597  1.00122.43           O  
ANISOU  865  O   ALA A 118    16018  16958  13541      1    364    660       O  
ATOM    866  CB  ALA A 118     -40.291 -20.706-119.465  1.00125.01           C  
ANISOU  866  CB  ALA A 118    16473  17215  13809    -13    570    615       C  
ATOM    867  N   LEU A 119     -43.075 -21.484-117.553  1.00118.45           N  
ANISOU  867  N   LEU A 119    15639  16467  12896     64    329    702       N  
ATOM    868  CA  LEU A 119     -43.816 -21.250-116.313  1.00116.99           C  
ANISOU  868  CA  LEU A 119    15431  16327  12690     84    247    745       C  
ATOM    869  C   LEU A 119     -43.493 -22.325-115.295  1.00118.10           C  
ANISOU  869  C   LEU A 119    15457  16498  12917     86    175    751       C  
ATOM    870  O   LEU A 119     -43.567 -22.081-114.092  1.00121.14           O  
ANISOU  870  O   LEU A 119    15800  16915  13313     93    123    772       O  
ATOM    871  CB  LEU A 119     -45.327 -21.237-116.550  1.00114.93           C  
ANISOU  871  CB  LEU A 119    15236  16095  12335    128    203    796       C  
ATOM    872  CG  LEU A 119     -45.987 -20.059-117.264  1.00115.19           C  
ANISOU  872  CG  LEU A 119    15388  16112  12264    141    249    805       C  
ATOM    873  CD1 LEU A 119     -47.495 -20.238-117.224  1.00113.02           C  
ANISOU  873  CD1 LEU A 119    15145  15882  11913    189    185    869       C  
ATOM    874  CD2 LEU A 119     -45.595 -18.729-116.639  1.00117.94           C  
ANISOU  874  CD2 LEU A 119    15768  16451  12591    129    272    795       C  
ATOM    875  N   LYS A 120     -43.128 -23.507-115.791  1.00116.87           N  
ANISOU  875  N   LYS A 120    15258  16328  12816     85    171    732       N  
ATOM    876  CA  LYS A 120     -42.812 -24.660-114.947  1.00116.97           C  
ANISOU  876  CA  LYS A 120    15166  16363  12913     87    100    736       C  
ATOM    877  C   LYS A 120     -41.618 -24.427-114.026  1.00118.10           C  
ANISOU  877  C   LYS A 120    15226  16505  13139     56    109    707       C  
ATOM    878  O   LYS A 120     -41.505 -25.063-112.979  1.00117.43           O  
ANISOU  878  O   LYS A 120    15059  16448  13110     60     38    721       O  
ATOM    879  CB  LYS A 120     -42.599 -25.911-115.802  1.00116.18           C  
ANISOU  879  CB  LYS A 120    15058  16235  12848     97     96    713       C  
ATOM    880  CG  LYS A 120     -43.868 -26.364-116.502  1.00118.83           C  
ANISOU  880  CG  LYS A 120    15465  16570  13113    125     49    752       C  
ATOM    881  CD  LYS A 120     -43.714 -27.709-117.183  1.00120.67           C  
ANISOU  881  CD  LYS A 120    15697  16770  13382    140     16    732       C  
ATOM    882  CE  LYS A 120     -45.010 -28.095-117.879  1.00121.44           C  
ANISOU  882  CE  LYS A 120    15873  16859  13410    160    -44    776       C  
ATOM    883  NZ  LYS A 120     -44.891 -29.377-118.625  1.00125.87           N  
ANISOU  883  NZ  LYS A 120    16457  17373  13995    178    -88    754       N  
ATOM    884  N   GLU A 121     -40.748 -23.496-114.412  1.00121.78           N  
ANISOU  884  N   GLU A 121    15715  16940  13615     23    191    674       N  
ATOM    885  CA  GLU A 121     -39.580 -23.139-113.610  1.00124.89           C  
ANISOU  885  CA  GLU A 121    16035  17326  14089    -14    198    652       C  
ATOM    886  C   GLU A 121     -39.947 -22.496-112.272  1.00122.19           C  
ANISOU  886  C   GLU A 121    15688  17008  13729    -10    128    680       C  
ATOM    887  O   GLU A 121     -39.161 -22.539-111.324  1.00124.90           O  
ANISOU  887  O   GLU A 121    15957  17351  14145    -31     95    669       O  
ATOM    888  CB  GLU A 121     -38.641 -22.227-114.401  1.00131.74           C  
ANISOU  888  CB  GLU A 121    16932  18155  14968    -57    299    625       C  
ATOM    889  CG  GLU A 121     -37.792 -22.966-115.424  1.00141.55           C  
ANISOU  889  CG  GLU A 121    18138  19381  16260    -59    372    594       C  
ATOM    890  CD  GLU A 121     -36.563 -22.186-115.857  1.00151.31           C  
ANISOU  890  CD  GLU A 121    19354  20595  17542   -109    464    579       C  
ATOM    891  OE1 GLU A 121     -36.097 -21.304-115.098  1.00154.72           O  
ANISOU  891  OE1 GLU A 121    19765  21018  18003   -155    447    589       O  
ATOM    892  OE2 GLU A 121     -36.052 -22.467-116.962  1.00157.80           O  
ANISOU  892  OE2 GLU A 121    20180  21406  18368   -102    549    563       O  
ATOM    893  N   TYR A 122     -41.139 -21.908-112.201  1.00118.02           N  
ANISOU  893  N   TYR A 122    15241  16500  13100     24    104    715       N  
ATOM    894  CA  TYR A 122     -41.634 -21.296-110.969  1.00115.13           C  
ANISOU  894  CA  TYR A 122    14885  16162  12694     51     39    745       C  
ATOM    895  C   TYR A 122     -41.944 -22.338-109.907  1.00114.01           C  
ANISOU  895  C   TYR A 122    14656  16070  12589     80    -47    775       C  
ATOM    896  O   TYR A 122     -41.770 -22.085-108.710  1.00112.12           O  
ANISOU  896  O   TYR A 122    14388  15849  12364     90    -99    784       O  
ATOM    897  CB  TYR A 122     -42.886 -20.467-111.244  1.00113.65           C  
ANISOU  897  CB  TYR A 122    14805  15992  12381     94     41    781       C  
ATOM    898  CG  TYR A 122     -42.605 -19.074-111.736  1.00113.06           C  
ANISOU  898  CG  TYR A 122    14828  15871  12259     71     99    758       C  
ATOM    899  CD1 TYR A 122     -42.370 -18.825-113.087  1.00115.33           C  
ANISOU  899  CD1 TYR A 122    15167  16117  12533     41    182    735       C  
ATOM    900  CD2 TYR A 122     -42.581 -18.001-110.853  1.00112.21           C  
ANISOU  900  CD2 TYR A 122    14767  15754  12113     83     66    762       C  
ATOM    901  CE1 TYR A 122     -42.111 -17.543-113.543  1.00116.76           C  
ANISOU  901  CE1 TYR A 122    15437  16253  12671     14    232    721       C  
ATOM    902  CE2 TYR A 122     -42.325 -16.715-111.297  1.00114.49           C  
ANISOU  902  CE2 TYR A 122    15153  15990  12357     58    107    744       C  
ATOM    903  CZ  TYR A 122     -42.090 -16.491-112.640  1.00116.05           C  
ANISOU  903  CZ  TYR A 122    15392  16151  12548     19    191    726       C  
ATOM    904  OH  TYR A 122     -41.839 -15.213-113.079  1.00115.82           O  
ANISOU  904  OH  TYR A 122    15459  16069  12477    -10    228    714       O  
ATOM    905  N   GLU A 123     -42.406 -23.505-110.352  1.00113.01           N  
ANISOU  905  N   GLU A 123    14495  15964  12478     93    -67    793       N  
ATOM    906  CA  GLU A 123     -42.770 -24.584-109.444  1.00113.53           C  
ANISOU  906  CA  GLU A 123    14479  16077  12580    115   -153    830       C  
ATOM    907  C   GLU A 123     -42.001 -25.868-109.771  1.00112.93           C  
ANISOU  907  C   GLU A 123    14326  15979  12604     90   -161    799       C  
ATOM    908  O   GLU A 123     -42.601 -26.853-110.210  1.00114.31           O  
ANISOU  908  O   GLU A 123    14493  16162  12776    103   -197    824       O  
ATOM    909  CB  GLU A 123     -44.286 -24.820-109.483  1.00113.34           C  
ANISOU  909  CB  GLU A 123    14485  16105  12471    162   -199    903       C  
ATOM    910  CG  GLU A 123     -44.879 -25.294-108.162  1.00115.87           C  
ANISOU  910  CG  GLU A 123    14740  16494  12791    197   -287    966       C  
ATOM    911  CD  GLU A 123     -44.749 -24.264-107.045  1.00116.70           C  
ANISOU  911  CD  GLU A 123    14861  16620  12860    225   -295    968       C  
ATOM    912  OE1 GLU A 123     -44.834 -23.053-107.332  1.00117.65           O  
ANISOU  912  OE1 GLU A 123    15070  16719  12912    235   -248    951       O  
ATOM    913  OE2 GLU A 123     -44.566 -24.662-105.873  1.00116.70           O  
ANISOU  913  OE2 GLU A 123    14792  16652  12895    240   -354    987       O  
ATOM    914  N   PRO A 124     -40.667 -25.866-109.552  1.00111.50           N  
ANISOU  914  N   PRO A 124    14089  15766  12510     55   -133    747       N  
ATOM    915  CA  PRO A 124     -39.870 -27.034-109.916  1.00109.82           C  
ANISOU  915  CA  PRO A 124    13807  15531  12386     41   -132    714       C  
ATOM    916  C   PRO A 124     -40.161 -28.213-109.004  1.00110.10           C  
ANISOU  916  C   PRO A 124    13765  15600  12466     58   -232    744       C  
ATOM    917  O   PRO A 124     -40.494 -28.024-107.833  1.00111.74           O  
ANISOU  917  O   PRO A 124    13944  15845  12665     69   -291    780       O  
ATOM    918  CB  PRO A 124     -38.422 -26.565-109.705  1.00109.68           C  
ANISOU  918  CB  PRO A 124    13740  15484  12447      1    -83    665       C  
ATOM    919  CG  PRO A 124     -38.489 -25.099-109.437  1.00110.73           C  
ANISOU  919  CG  PRO A 124    13934  15610  12527    -14    -57    671       C  
ATOM    920  CD  PRO A 124     -39.847 -24.850-108.870  1.00111.35           C  
ANISOU  920  CD  PRO A 124    14063  15729  12513     29   -116    724       C  
ATOM    921  N   GLU A 125     -40.046 -29.417-109.553  1.00110.78           N  
ANISOU  921  N   GLU A 125    13826  15670  12595     63   -253    733       N  
ATOM    922  CA  GLU A 125     -40.187 -30.642-108.778  1.00110.40           C  
ANISOU  922  CA  GLU A 125    13703  15642  12600     72   -351    759       C  
ATOM    923  C   GLU A 125     -39.002 -30.783-107.812  1.00107.52           C  
ANISOU  923  C   GLU A 125    13246  15275  12331     54   -363    725       C  
ATOM    924  O   GLU A 125     -37.840 -30.793-108.234  1.00108.01           O  
ANISOU  924  O   GLU A 125    13281  15304  12455     37   -304    668       O  
ATOM    925  CB  GLU A 125     -40.272 -31.844-109.723  1.00113.14           C  
ANISOU  925  CB  GLU A 125    14064  15956  12966     84   -372    746       C  
ATOM    926  CG  GLU A 125     -41.112 -32.999-109.203  1.00118.05           C  
ANISOU  926  CG  GLU A 125    14654  16601  13598     94   -492    805       C  
ATOM    927  CD  GLU A 125     -42.595 -32.832-109.490  1.00120.55           C  
ANISOU  927  CD  GLU A 125    15031  16945  13825    105   -530    879       C  
ATOM    928  OE1 GLU A 125     -43.211 -31.892-108.943  1.00125.66           O  
ANISOU  928  OE1 GLU A 125    15690  17639  14413    112   -518    923       O  
ATOM    929  OE2 GLU A 125     -43.152 -33.654-110.252  1.00119.78           O  
ANISOU  929  OE2 GLU A 125    14973  16821  13714    111   -577    898       O  
ATOM    930  N   MET A 126     -39.303 -30.879-106.518  1.00101.71           N  
ANISOU  930  N   MET A 126    12461  14580  11604     60   -440    765       N  
ATOM    931  CA  MET A 126     -38.270 -30.935-105.478  1.00 98.78           C  
ANISOU  931  CA  MET A 126    12007  14206  11315     43   -464    738       C  
ATOM    932  C   MET A 126     -38.124 -32.316-104.814  1.00 95.01           C  
ANISOU  932  C   MET A 126    11448  13740  10911     49   -553    750       C  
ATOM    933  O   MET A 126     -38.893 -33.239-105.096  1.00 95.13           O  
ANISOU  933  O   MET A 126    11470  13764  10910     64   -607    787       O  
ATOM    934  CB  MET A 126     -38.529 -29.856-104.417  1.00 99.27           C  
ANISOU  934  CB  MET A 126    12086  14298  11333     50   -481    765       C  
ATOM    935  CG  MET A 126     -38.442 -28.431-104.940  1.00101.15           C  
ANISOU  935  CG  MET A 126    12404  14514  11512     38   -402    744       C  
ATOM    936  SD  MET A 126     -36.771 -27.927-105.390  1.00105.28           S  
ANISOU  936  SD  MET A 126    12897  14979  12125    -15   -325    672       S  
ATOM    937  CE  MET A 126     -37.039 -26.208-105.837  1.00104.37           C  
ANISOU  937  CE  MET A 126    12892  14843  11919    -27   -259    673       C  
ATOM    938  N   GLY A 127     -37.124 -32.443-103.943  1.00 89.99           N  
ANISOU  938  N   GLY A 127    10737  13099  10357     34   -576    722       N  
ATOM    939  CA  GLY A 127     -36.883 -33.663-103.174  1.00 87.03           C  
ANISOU  939  CA  GLY A 127    10281  12732  10054     39   -663    731       C  
ATOM    940  C   GLY A 127     -36.031 -33.384-101.949  1.00 85.35           C  
ANISOU  940  C   GLY A 127    10001  12524   9903     25   -693    715       C  
ATOM    941  O   GLY A 127     -35.401 -32.340-101.860  1.00 86.57           O  
ANISOU  941  O   GLY A 127    10168  12662  10062      6   -643    686       O  
ATOM    942  N   LYS A 128     -36.007 -34.311-100.997  1.00 83.35           N  
ANISOU  942  N   LYS A 128     9682  12288   9698     33   -783    737       N  
ATOM    943  CA  LYS A 128     -35.232 -34.119 -99.772  1.00 81.71           C  
ANISOU  943  CA  LYS A 128     9414  12084   9548     23   -824    723       C  
ATOM    944  C   LYS A 128     -34.214 -35.239 -99.543  1.00 82.54           C  
ANISOU  944  C   LYS A 128     9430  12164   9767     12   -863    686       C  
ATOM    945  O   LYS A 128     -34.574 -36.354 -99.153  1.00 83.24           O  
ANISOU  945  O   LYS A 128     9484  12266   9877     26   -942    715       O  
ATOM    946  CB  LYS A 128     -36.155 -34.008 -98.559  1.00 80.50           C  
ANISOU  946  CB  LYS A 128     9266  11983   9335     51   -899    791       C  
ATOM    947  CG  LYS A 128     -37.005 -32.756 -98.504  1.00 79.03           C  
ANISOU  947  CG  LYS A 128     9163  11825   9037     74   -865    825       C  
ATOM    948  CD  LYS A 128     -37.924 -32.789 -97.293  1.00 78.07           C  
ANISOU  948  CD  LYS A 128     9039  11768   8853    118   -938    899       C  
ATOM    949  CE  LYS A 128     -39.189 -33.579 -97.574  1.00 77.70           C  
ANISOU  949  CE  LYS A 128     8992  11771   8757    139   -972    978       C  
ATOM    950  NZ  LYS A 128     -40.074 -33.644 -96.380  1.00 78.60           N  
ANISOU  950  NZ  LYS A 128     9091  11961   8812    186  -1038   1063       N  
ATOM    951  N   VAL A 129     -32.941 -34.938 -99.771  1.00 81.48           N  
ANISOU  951  N   VAL A 129     9256  11994   9707    -11   -812    627       N  
ATOM    952  CA  VAL A 129     -31.894 -35.937 -99.620  1.00 80.28           C  
ANISOU  952  CA  VAL A 129     9017  11821   9664    -15   -839    589       C  
ATOM    953  C   VAL A 129     -30.991 -35.646 -98.435  1.00 81.92           C  
ANISOU  953  C   VAL A 129     9157  12024   9943    -37   -882    575       C  
ATOM    954  O   VAL A 129     -30.813 -34.489 -98.062  1.00 84.77           O  
ANISOU  954  O   VAL A 129     9542  12382  10284    -58   -862    575       O  
ATOM    955  CB  VAL A 129     -31.025 -36.053-100.888  1.00 79.30           C  
ANISOU  955  CB  VAL A 129     8882  11665   9583    -18   -747    536       C  
ATOM    956  CG1 VAL A 129     -31.796 -36.744-101.999  1.00 79.26           C  
ANISOU  956  CG1 VAL A 129     8938  11653   9523     13   -731    542       C  
ATOM    957  CG2 VAL A 129     -30.516 -34.691-101.333  1.00 78.44           C  
ANISOU  957  CG2 VAL A 129     8796  11545   9461    -49   -653    519       C  
ATOM    958  N   TYR A 130     -30.443 -36.707 -97.841  1.00 82.12           N  
ANISOU  958  N   TYR A 130     9105  12045  10050    -30   -950    563       N  
ATOM    959  CA  TYR A 130     -29.310 -36.603 -96.928  1.00 81.87           C  
ANISOU  959  CA  TYR A 130     8996  12000  10111    -53   -984    538       C  
ATOM    960  C   TYR A 130     -28.050 -36.934 -97.686  1.00 84.91           C  
ANISOU  960  C   TYR A 130     9314  12358  10590    -62   -924    486       C  
ATOM    961  O   TYR A 130     -27.949 -38.018 -98.271  1.00 86.83           O  
ANISOU  961  O   TYR A 130     9536  12595  10860    -33   -923    469       O  
ATOM    962  CB  TYR A 130     -29.467 -37.557 -95.760  1.00 80.25           C  
ANISOU  962  CB  TYR A 130     8744  11808   9937    -36  -1098    560       C  
ATOM    963  CG  TYR A 130     -30.490 -37.069 -94.796  1.00 81.62           C  
ANISOU  963  CG  TYR A 130     8968  12016  10025    -23  -1154    615       C  
ATOM    964  CD1 TYR A 130     -30.177 -36.096 -93.855  1.00 82.80           C  
ANISOU  964  CD1 TYR A 130     9127  12163  10170    -35  -1176    615       C  
ATOM    965  CD2 TYR A 130     -31.786 -37.547 -94.843  1.00 82.95           C  
ANISOU  965  CD2 TYR A 130     9180  12221  10115      4  -1186    672       C  
ATOM    966  CE1 TYR A 130     -31.127 -35.633 -92.970  1.00 84.36           C  
ANISOU  966  CE1 TYR A 130     9379  12396  10276     -6  -1223    666       C  
ATOM    967  CE2 TYR A 130     -32.747 -37.087 -93.970  1.00 84.09           C  
ANISOU  967  CE2 TYR A 130     9364  12409  10174     27  -1228    733       C  
ATOM    968  CZ  TYR A 130     -32.414 -36.132 -93.037  1.00 85.15           C  
ANISOU  968  CZ  TYR A 130     9512  12543  10296     28  -1243    727       C  
ATOM    969  OH  TYR A 130     -33.385 -35.680 -92.175  1.00 88.55           O  
ANISOU  969  OH  TYR A 130     9991  13022  10631     67  -1281    787       O  
ATOM    970  N   ARG A 131     -27.098 -36.000 -97.695  1.00 87.14           N  
ANISOU  970  N   ARG A 131     9564  12624  10918   -101   -875    466       N  
ATOM    971  CA  ARG A 131     -25.821 -36.211 -98.394  1.00 88.39           C  
ANISOU  971  CA  ARG A 131     9643  12769  11169   -110   -807    429       C  
ATOM    972  C   ARG A 131     -24.582 -36.003 -97.511  1.00 89.40           C  
ANISOU  972  C   ARG A 131     9674  12885  11408   -147   -846    418       C  
ATOM    973  O   ARG A 131     -24.651 -35.338 -96.476  1.00 89.95           O  
ANISOU  973  O   ARG A 131     9756  12946  11473   -176   -910    434       O  
ATOM    974  CB  ARG A 131     -25.770 -35.394 -99.691  1.00 87.38           C  
ANISOU  974  CB  ARG A 131     9561  12639  11000   -121   -685    424       C  
ATOM    975  CG  ARG A 131     -26.580 -36.045-100.804  1.00 86.88           C  
ANISOU  975  CG  ARG A 131     9564  12581  10865    -72   -642    420       C  
ATOM    976  CD  ARG A 131     -26.762 -35.156-102.019  1.00 86.34           C  
ANISOU  976  CD  ARG A 131     9561  12511  10733    -81   -529    420       C  
ATOM    977  NE  ARG A 131     -27.543 -35.844-103.043  1.00 85.80           N  
ANISOU  977  NE  ARG A 131     9563  12442  10596    -31   -501    415       N  
ATOM    978  CZ  ARG A 131     -27.780 -35.366-104.258  1.00 85.55           C  
ANISOU  978  CZ  ARG A 131     9597  12406  10502    -22   -405    411       C  
ATOM    979  NH1 ARG A 131     -27.294 -34.189-104.614  1.00 86.30           N  
ANISOU  979  NH1 ARG A 131     9692  12500  10596    -62   -322    415       N  
ATOM    980  NH2 ARG A 131     -28.503 -36.067-105.121  1.00 85.63           N  
ANISOU  980  NH2 ARG A 131     9676  12409  10450     24   -398    405       N  
ATOM    981  N   ALA A 132     -23.461 -36.596 -97.917  1.00 89.91           N  
ANISOU  981  N   ALA A 132     9644  12949  11569   -140   -810    391       N  
ATOM    982  CA  ALA A 132     -22.242 -36.603 -97.105  1.00 90.50           C  
ANISOU  982  CA  ALA A 132     9610  13015  11760   -171   -854    384       C  
ATOM    983  C   ALA A 132     -21.722 -35.220 -96.753  1.00 92.36           C  
ANISOU  983  C   ALA A 132     9839  13232  12019   -241   -846    402       C  
ATOM    984  O   ALA A 132     -21.076 -35.047 -95.723  1.00 94.53           O  
ANISOU  984  O   ALA A 132    10058  13491  12365   -275   -924    406       O  
ATOM    985  CB  ALA A 132     -21.154 -37.400 -97.794  1.00 90.52           C  
ANISOU  985  CB  ALA A 132     9512  13028  11852   -142   -797    359       C  
ATOM    986  N   ASP A 133     -22.012 -34.243 -97.604  1.00 94.47           N  
ANISOU  986  N   ASP A 133    10169  13498  12225   -263   -761    415       N  
ATOM    987  CA  ASP A 133     -21.465 -32.896 -97.460  1.00 96.21           C  
ANISOU  987  CA  ASP A 133    10389  13695  12468   -335   -748    436       C  
ATOM    988  C   ASP A 133     -22.164 -32.028 -96.412  1.00 93.08           C  
ANISOU  988  C   ASP A 133    10086  13272  12008   -358   -839    451       C  
ATOM    989  O   ASP A 133     -21.630 -31.005 -95.998  1.00 93.78           O  
ANISOU  989  O   ASP A 133    10175  13327  12127   -417   -868    466       O  
ATOM    990  CB  ASP A 133     -21.452 -32.183 -98.816  1.00101.40           C  
ANISOU  990  CB  ASP A 133    11079  14359  13087   -350   -621    446       C  
ATOM    991  CG  ASP A 133     -22.830 -32.094 -99.445  1.00104.22           C  
ANISOU  991  CG  ASP A 133    11565  14725  13309   -310   -584    445       C  
ATOM    992  OD1 ASP A 133     -23.817 -32.478 -98.782  1.00106.02           O  
ANISOU  992  OD1 ASP A 133    11854  14955  13472   -275   -659    445       O  
ATOM    993  OD2 ASP A 133     -22.927 -31.639-100.605  1.00107.18           O  
ANISOU  993  OD2 ASP A 133    11975  15106  13640   -312   -480    450       O  
ATOM    994  N   ARG A 134     -23.359 -32.425 -95.995  1.00 90.87           N  
ANISOU  994  N   ARG A 134     9886  13005  11635   -308   -887    453       N  
ATOM    995  CA  ARG A 134     -24.108 -31.654 -95.002  1.00 91.49           C  
ANISOU  995  CA  ARG A 134    10057  13068  11635   -308   -967    470       C  
ATOM    996  C   ARG A 134     -24.810 -32.559 -93.990  1.00 91.38           C  
ANISOU  996  C   ARG A 134    10052  13075  11590   -256  -1061    476       C  
ATOM    997  O   ARG A 134     -25.332 -33.615 -94.351  1.00 91.78           O  
ANISOU  997  O   ARG A 134    10090  13157  11623   -213  -1049    475       O  
ATOM    998  CB  ARG A 134     -25.129 -30.738 -95.689  1.00 90.67           C  
ANISOU  998  CB  ARG A 134    10075  12967  11406   -300   -907    486       C  
ATOM    999  CG  ARG A 134     -24.528 -29.723 -96.649  1.00 87.88           C  
ANISOU  999  CG  ARG A 134     9728  12590  11071   -355   -819    487       C  
ATOM   1000  CD  ARG A 134     -25.597 -28.832 -97.244  1.00 84.89           C  
ANISOU 1000  CD  ARG A 134     9477  12211  10563   -343   -770    502       C  
ATOM   1001  NE  ARG A 134     -25.055 -27.639 -97.889  1.00 83.73           N  
ANISOU 1001  NE  ARG A 134     9354  12031  10427   -404   -712    510       N  
ATOM   1002  CZ  ARG A 134     -24.562 -26.587 -97.236  1.00 84.18           C  
ANISOU 1002  CZ  ARG A 134     9437  12041  10506   -457   -771    520       C  
ATOM   1003  NH1 ARG A 134     -24.505 -26.574 -95.906  1.00 83.78           N  
ANISOU 1003  NH1 ARG A 134     9394  11969  10467   -450   -889    518       N  
ATOM   1004  NH2 ARG A 134     -24.109 -25.546 -97.916  1.00 84.66           N  
ANISOU 1004  NH2 ARG A 134     9519  12070  10575   -518   -719    534       N  
ATOM   1005  N   LYS A 135     -24.828 -32.145 -92.726  1.00 91.63           N  
ANISOU 1005  N   LYS A 135    10111  13090  11614   -258  -1159    485       N  
ATOM   1006  CA  LYS A 135     -25.463 -32.954 -91.689  1.00 95.11           C  
ANISOU 1006  CA  LYS A 135    10556  13555  12023   -208  -1249    498       C  
ATOM   1007  C   LYS A 135     -26.984 -32.902 -91.814  1.00 93.71           C  
ANISOU 1007  C   LYS A 135    10478  13419  11707   -154  -1235    532       C  
ATOM   1008  O   LYS A 135     -27.672 -33.912 -91.633  1.00 91.42           O  
ANISOU 1008  O   LYS A 135    10175  13167  11392   -112  -1263    553       O  
ATOM   1009  CB  LYS A 135     -25.002 -32.522 -90.289  1.00100.09           C  
ANISOU 1009  CB  LYS A 135    11191  14155  12680   -219  -1358    499       C  
ATOM   1010  CG  LYS A 135     -25.399 -33.483 -89.170  1.00104.61           C  
ANISOU 1010  CG  LYS A 135    11746  14754  13245   -171  -1452    513       C  
ATOM   1011  CD  LYS A 135     -24.687 -33.149 -87.866  1.00110.75           C  
ANISOU 1011  CD  LYS A 135    12515  15492  14070   -185  -1560    504       C  
ATOM   1012  CE  LYS A 135     -25.112 -34.077 -86.733  1.00113.76           C  
ANISOU 1012  CE  LYS A 135    12883  15903  14436   -134  -1651    523       C  
ATOM   1013  NZ  LYS A 135     -24.223 -33.958 -85.538  1.00114.14           N  
ANISOU 1013  NZ  LYS A 135    12905  15908  14553   -151  -1757    507       N  
ATOM   1014  N   SER A 136     -27.489 -31.718 -92.145  1.00 94.97           N  
ANISOU 1014  N   SER A 136    10734  13570  11779   -157  -1194    543       N  
ATOM   1015  CA  SER A 136     -28.921 -31.463 -92.253  1.00 95.04           C  
ANISOU 1015  CA  SER A 136    10840  13619  11651   -105  -1178    580       C  
ATOM   1016  C   SER A 136     -29.505 -32.041 -93.538  1.00 95.37           C  
ANISOU 1016  C   SER A 136    10880  13689  11667    -95  -1095    587       C  
ATOM   1017  O   SER A 136     -28.767 -32.392 -94.470  1.00 96.81           O  
ANISOU 1017  O   SER A 136    11004  13853  11924   -127  -1033    556       O  
ATOM   1018  CB  SER A 136     -29.171 -29.960 -92.223  1.00 94.84           C  
ANISOU 1018  CB  SER A 136    10922  13567  11543   -109  -1164    584       C  
ATOM   1019  OG  SER A 136     -28.617 -29.356 -93.378  1.00 96.47           O  
ANISOU 1019  OG  SER A 136    11129  13741  11782   -163  -1078    561       O  
ATOM   1020  N   VAL A 137     -30.834 -32.133 -93.584  1.00 93.78           N  
ANISOU 1020  N   VAL A 137    10742  13532  11355    -46  -1094    630       N  
ATOM   1021  CA  VAL A 137     -31.518 -32.568 -94.796  1.00 92.00           C  
ANISOU 1021  CA  VAL A 137    10533  13328  11092    -37  -1025    641       C  
ATOM   1022  C   VAL A 137     -31.394 -31.477 -95.849  1.00 90.67           C  
ANISOU 1022  C   VAL A 137    10427  13133  10891    -64   -932    620       C  
ATOM   1023  O   VAL A 137     -31.434 -30.288 -95.521  1.00 90.29           O  
ANISOU 1023  O   VAL A 137    10444  13067  10793    -69   -931    622       O  
ATOM   1024  CB  VAL A 137     -32.994 -32.962 -94.543  1.00 91.53           C  
ANISOU 1024  CB  VAL A 137    10518  13327  10930     16  -1058    706       C  
ATOM   1025  CG1 VAL A 137     -33.848 -31.750 -94.192  1.00 92.17           C  
ANISOU 1025  CG1 VAL A 137    10698  13430  10891     50  -1050    739       C  
ATOM   1026  CG2 VAL A 137     -33.560 -33.704 -95.746  1.00 90.82           C  
ANISOU 1026  CG2 VAL A 137    10430  13249  10828     18  -1012    716       C  
ATOM   1027  N   GLN A 138     -31.201 -31.902 -97.097  1.00 89.32           N  
ANISOU 1027  N   GLN A 138    10236  12953  10747    -79   -857    600       N  
ATOM   1028  CA  GLN A 138     -31.049 -31.009 -98.236  1.00 88.75           C  
ANISOU 1028  CA  GLN A 138    10214  12857  10648   -105   -759    583       C  
ATOM   1029  C   GLN A 138     -32.248 -31.110 -99.146  1.00 89.02           C  
ANISOU 1029  C   GLN A 138    10321  12917  10585    -73   -715    608       C  
ATOM   1030  O   GLN A 138     -32.649 -32.209 -99.531  1.00 89.59           O  
ANISOU 1030  O   GLN A 138    10370  13006  10662    -50   -726    617       O  
ATOM   1031  CB  GLN A 138     -29.818 -31.381 -99.041  1.00 88.50           C  
ANISOU 1031  CB  GLN A 138    10105  12799  10721   -139   -698    541       C  
ATOM   1032  CG  GLN A 138     -28.575 -30.614 -98.669  1.00 90.04           C  
ANISOU 1032  CG  GLN A 138    10253  12959  10996   -193   -696    521       C  
ATOM   1033  CD  GLN A 138     -27.331 -31.407 -98.978  1.00 91.93           C  
ANISOU 1033  CD  GLN A 138    10378  13191  11360   -211   -672    492       C  
ATOM   1034  OE1 GLN A 138     -27.075 -32.445 -98.352  1.00 92.77           O  
ANISOU 1034  OE1 GLN A 138    10415  13308  11526   -192   -736    485       O  
ATOM   1035  NE2 GLN A 138     -26.548 -30.933 -99.949  1.00 90.82           N  
ANISOU 1035  NE2 GLN A 138    10213  13037  11258   -245   -579    480       N  
ATOM   1036  N   ARG A 139     -32.804 -29.956 -99.499  1.00 89.17           N  
ANISOU 1036  N   ARG A 139    10431  12933  10515    -72   -671    621       N  
ATOM   1037  CA  ARG A 139     -33.947 -29.898-100.389  1.00 88.52           C  
ANISOU 1037  CA  ARG A 139    10424  12872  10336    -44   -628    647       C  
ATOM   1038  C   ARG A 139     -33.524 -29.474-101.804  1.00 87.48           C  
ANISOU 1038  C   ARG A 139    10320  12709  10208    -72   -522    615       C  
ATOM   1039  O   ARG A 139     -33.529 -28.294-102.145  1.00 88.16           O  
ANISOU 1039  O   ARG A 139    10472  12776  10247    -91   -474    612       O  
ATOM   1040  CB  ARG A 139     -35.030 -28.989 -99.806  1.00 89.87           C  
ANISOU 1040  CB  ARG A 139    10682  13072  10392     -9   -654    690       C  
ATOM   1041  CG  ARG A 139     -36.371 -29.120-100.495  1.00 94.22           C  
ANISOU 1041  CG  ARG A 139    11295  13660  10845     27   -632    733       C  
ATOM   1042  CD  ARG A 139     -37.426 -28.268 -99.814  1.00 99.03           C  
ANISOU 1042  CD  ARG A 139    11980  14307  11339     75   -659    782       C  
ATOM   1043  NE  ARG A 139     -38.421 -27.798-100.780  1.00102.71           N  
ANISOU 1043  NE  ARG A 139    12527  14787  11709     95   -604    807       N  
ATOM   1044  CZ  ARG A 139     -38.309 -26.674-101.486  1.00104.53           C  
ANISOU 1044  CZ  ARG A 139    12836  14983  11896     79   -537    781       C  
ATOM   1045  NH1 ARG A 139     -37.242 -25.887-101.339  1.00106.38           N  
ANISOU 1045  NH1 ARG A 139    13076  15165  12176     39   -520    735       N  
ATOM   1046  NH2 ARG A 139     -39.268 -26.333-102.338  1.00104.96           N  
ANISOU 1046  NH2 ARG A 139    12962  15053  11862    101   -494    807       N  
ATOM   1047  N   ILE A 140     -33.153 -30.461-102.612  1.00 86.10           N  
ANISOU 1047  N   ILE A 140    10100  12528  10086    -71   -491    593       N  
ATOM   1048  CA  ILE A 140     -32.744 -30.246-103.996  1.00 86.26           C  
ANISOU 1048  CA  ILE A 140    10143  12525  10107    -85   -388    565       C  
ATOM   1049  C   ILE A 140     -33.864 -30.565-104.988  1.00 86.94           C  
ANISOU 1049  C   ILE A 140    10307  12621  10105    -50   -362    583       C  
ATOM   1050  O   ILE A 140     -34.871 -31.165-104.618  1.00 86.01           O  
ANISOU 1050  O   ILE A 140    10206  12529   9945    -21   -430    619       O  
ATOM   1051  CB  ILE A 140     -31.525 -31.113-104.329  1.00 86.60           C  
ANISOU 1051  CB  ILE A 140    10091  12553  10258    -92   -362    527       C  
ATOM   1052  CG1 ILE A 140     -31.860 -32.596-104.152  1.00 86.47           C  
ANISOU 1052  CG1 ILE A 140    10040  12549  10265    -52   -431    529       C  
ATOM   1053  CG2 ILE A 140     -30.358 -30.722-103.442  1.00 88.54           C  
ANISOU 1053  CG2 ILE A 140    10256  12787  10597   -133   -385    514       C  
ATOM   1054  CD1 ILE A 140     -30.929 -33.531-104.889  1.00 88.09           C  
ANISOU 1054  CD1 ILE A 140    10187  12738  10543    -35   -391    488       C  
ATOM   1055  N   LYS A 141     -33.683 -30.170-106.248  1.00 90.06           N  
ANISOU 1055  N   LYS A 141    10747  12995  10474    -56   -266    563       N  
ATOM   1056  CA  LYS A 141     -34.665 -30.469-107.296  1.00 92.95           C  
ANISOU 1056  CA  LYS A 141    11194  13361  10759    -25   -241    575       C  
ATOM   1057  C   LYS A 141     -34.642 -31.957-107.607  1.00 94.65           C  
ANISOU 1057  C   LYS A 141    11375  13571  11014      6   -281    563       C  
ATOM   1058  O   LYS A 141     -33.566 -32.528-107.800  1.00 97.06           O  
ANISOU 1058  O   LYS A 141    11615  13861  11399      8   -256    524       O  
ATOM   1059  CB  LYS A 141     -34.390 -29.676-108.579  1.00 94.47           C  
ANISOU 1059  CB  LYS A 141    11448  13531  10916    -36   -127    553       C  
ATOM   1060  CG  LYS A 141     -33.919 -28.243-108.371  1.00 97.45           C  
ANISOU 1060  CG  LYS A 141    11841  13898  11287    -80    -80    554       C  
ATOM   1061  CD  LYS A 141     -34.628 -27.256-109.292  1.00100.13           C  
ANISOU 1061  CD  LYS A 141    12291  14226  11525    -81    -15    566       C  
ATOM   1062  CE  LYS A 141     -34.508 -27.611-110.772  1.00104.75           C  
ANISOU 1062  CE  LYS A 141    12913  14797  12090    -62     71    544       C  
ATOM   1063  NZ  LYS A 141     -33.130 -27.439-111.314  1.00109.25           N  
ANISOU 1063  NZ  LYS A 141    13424  15352  12732    -88    159    517       N  
ATOM   1064  N   ALA A 142     -35.823 -32.580-107.651  1.00 95.08           N  
ANISOU 1064  N   ALA A 142    11473  13638  11012     32   -346    600       N  
ATOM   1065  CA  ALA A 142     -35.952 -34.024-107.909  1.00 95.38           C  
ANISOU 1065  CA  ALA A 142    11495  13662  11081     60   -408    596       C  
ATOM   1066  C   ALA A 142     -35.146 -34.423-109.137  1.00 97.24           C  
ANISOU 1066  C   ALA A 142    11747  13860  11339     82   -331    540       C  
ATOM   1067  O   ALA A 142     -34.572 -35.513-109.206  1.00 95.91           O  
ANISOU 1067  O   ALA A 142    11537  13673  11230    107   -362    512       O  
ATOM   1068  CB  ALA A 142     -37.413 -34.405-108.088  1.00 94.34           C  
ANISOU 1068  CB  ALA A 142    11428  13543  10873     76   -476    653       C  
ATOM   1069  N   ARG A 143     -35.113 -33.497-110.090  1.00 99.67           N  
ANISOU 1069  N   ARG A 143    12118  14157  11592     78   -230    527       N  
ATOM   1070  CA  ARG A 143     -34.324 -33.583-111.305  1.00101.39           C  
ANISOU 1070  CA  ARG A 143    12358  14349  11816    103   -132    480       C  
ATOM   1071  C   ARG A 143     -32.898 -34.099-111.088  1.00101.55           C  
ANISOU 1071  C   ARG A 143    12276  14368  11939    112   -105    440       C  
ATOM   1072  O   ARG A 143     -32.349 -34.790-111.946  1.00102.24           O  
ANISOU 1072  O   ARG A 143    12371  14436  12038    158    -63    404       O  
ATOM   1073  CB  ARG A 143     -34.269 -32.194-111.935  1.00103.11           C  
ANISOU 1073  CB  ARG A 143    12627  14568  11980     78    -25    481       C  
ATOM   1074  CG  ARG A 143     -34.127 -32.231-113.436  1.00106.02           C  
ANISOU 1074  CG  ARG A 143    13069  14911  12300    113     67    454       C  
ATOM   1075  CD  ARG A 143     -33.642 -30.908-113.983  1.00107.04           C  
ANISOU 1075  CD  ARG A 143    13218  15044  12406     82    185    452       C  
ATOM   1076  NE  ARG A 143     -32.580 -31.150-114.949  1.00107.55           N  
ANISOU 1076  NE  ARG A 143    13263  15102  12498    113    286    418       N  
ATOM   1077  CZ  ARG A 143     -31.297 -30.910-114.714  1.00109.10           C  
ANISOU 1077  CZ  ARG A 143    13358  15316  12777     92    345    410       C  
ATOM   1078  NH1 ARG A 143     -30.917 -30.394-113.548  1.00109.84           N  
ANISOU 1078  NH1 ARG A 143    13372  15425  12937     34    304    427       N  
ATOM   1079  NH2 ARG A 143     -30.396 -31.170-115.650  1.00110.58           N  
ANISOU 1079  NH2 ARG A 143    13527  15508  12981    132    444    387       N  
ATOM   1080  N   ASP A 144     -32.316 -33.760-109.940  1.00100.95           N  
ANISOU 1080  N   ASP A 144    12110  14312  11932     72   -132    448       N  
ATOM   1081  CA  ASP A 144     -30.917 -34.055-109.640  1.00100.06           C  
ANISOU 1081  CA  ASP A 144    11889  14204  11924     70   -105    418       C  
ATOM   1082  C   ASP A 144     -30.737 -35.244-108.708  1.00 97.87           C  
ANISOU 1082  C   ASP A 144    11540  13928  11716     87   -212    412       C  
ATOM   1083  O   ASP A 144     -29.608 -35.583-108.343  1.00 98.94           O  
ANISOU 1083  O   ASP A 144    11580  14068  11942     89   -204    389       O  
ATOM   1084  CB  ASP A 144     -30.243 -32.819-109.044  1.00103.14           C  
ANISOU 1084  CB  ASP A 144    12227  14609  12353      9    -65    430       C  
ATOM   1085  CG  ASP A 144     -30.201 -31.655-110.016  1.00107.85           C  
ANISOU 1085  CG  ASP A 144    12883  15200  12893    -11     46    435       C  
ATOM   1086  OD1 ASP A 144     -29.750 -31.858-111.166  1.00110.92           O  
ANISOU 1086  OD1 ASP A 144    13286  15584  13273     21    136    415       O  
ATOM   1087  OD2 ASP A 144     -30.619 -30.539-109.632  1.00108.66           O  
ANISOU 1087  OD2 ASP A 144    13024  15302  12957    -55     41    460       O  
ATOM   1088  N   ILE A 145     -31.846 -35.875-108.327  1.00 94.87           N  
ANISOU 1088  N   ILE A 145    11205  13546  11296     99   -314    439       N  
ATOM   1089  CA  ILE A 145     -31.796 -37.041-107.447  1.00 91.90           C  
ANISOU 1089  CA  ILE A 145    10769  13168  10980    112   -425    442       C  
ATOM   1090  C   ILE A 145     -31.272 -38.268-108.190  1.00 93.54           C  
ANISOU 1090  C   ILE A 145    10978  13345  11218    170   -427    399       C  
ATOM   1091  O   ILE A 145     -31.603 -38.511-109.354  1.00 93.80           O  
ANISOU 1091  O   ILE A 145    11094  13352  11190    209   -390    384       O  
ATOM   1092  CB  ILE A 145     -33.139 -37.279-106.723  1.00 88.92           C  
ANISOU 1092  CB  ILE A 145    10427  12804  10552    100   -536    499       C  
ATOM   1093  CG1 ILE A 145     -33.239 -36.325-105.531  1.00 87.29           C  
ANISOU 1093  CG1 ILE A 145    10182  12633  10350     58   -554    531       C  
ATOM   1094  CG2 ILE A 145     -33.273 -38.717-106.242  1.00 87.77           C  
ANISOU 1094  CG2 ILE A 145    10249  12645  10451    122   -652    505       C  
ATOM   1095  CD1 ILE A 145     -34.633 -36.150-104.976  1.00 87.21           C  
ANISOU 1095  CD1 ILE A 145    10218  12652  10265     53   -625    597       C  
ATOM   1096  N   VAL A 146     -30.433 -39.023-107.493  1.00 94.76           N  
ANISOU 1096  N   VAL A 146    11042  13500  11462    181   -474    379       N  
ATOM   1097  CA  VAL A 146     -29.652 -40.097-108.081  1.00 95.20           C  
ANISOU 1097  CA  VAL A 146    11082  13530  11559    244   -467    332       C  
ATOM   1098  C   VAL A 146     -30.013 -41.447-107.456  1.00 94.63           C  
ANISOU 1098  C   VAL A 146    11004  13435  11516    265   -608    338       C  
ATOM   1099  O   VAL A 146     -30.399 -41.494-106.287  1.00 96.50           O  
ANISOU 1099  O   VAL A 146    11197  13689  11779    223   -697    375       O  
ATOM   1100  CB  VAL A 146     -28.159 -39.773-107.896  1.00 95.74           C  
ANISOU 1100  CB  VAL A 146    11039  13622  11716    243   -386    303       C  
ATOM   1101  CG1 VAL A 146     -27.349 -41.004-107.537  1.00 96.59           C  
ANISOU 1101  CG1 VAL A 146    11077  13718  11904    290   -443    271       C  
ATOM   1102  CG2 VAL A 146     -27.621 -39.086-109.138  1.00 98.45           C  
ANISOU 1102  CG2 VAL A 146    11408  13971  12026    266   -240    284       C  
ATOM   1103  N   PRO A 147     -29.918 -42.547-108.232  1.00 93.95           N  
ANISOU 1103  N   PRO A 147    10969  13308  11420    332   -634    304       N  
ATOM   1104  CA  PRO A 147     -30.090 -43.862-107.615  1.00 94.72           C  
ANISOU 1104  CA  PRO A 147    11055  13376  11557    351   -773    307       C  
ATOM   1105  C   PRO A 147     -28.973 -44.134-106.611  1.00 96.67           C  
ANISOU 1105  C   PRO A 147    11175  13643  11909    346   -790    287       C  
ATOM   1106  O   PRO A 147     -27.798 -44.194-106.980  1.00 99.09           O  
ANISOU 1106  O   PRO A 147    11430  13954  12263    390   -710    241       O  
ATOM   1107  CB  PRO A 147     -30.004 -44.828-108.798  1.00 93.41           C  
ANISOU 1107  CB  PRO A 147    10980  13155  11354    435   -778    263       C  
ATOM   1108  CG  PRO A 147     -30.381 -44.006-109.975  1.00 94.91           C  
ANISOU 1108  CG  PRO A 147    11258  13344  11457    446   -673    259       C  
ATOM   1109  CD  PRO A 147     -29.814 -42.645-109.695  1.00 95.19           C  
ANISOU 1109  CD  PRO A 147    11214  13436  11515    397   -552    267       C  
ATOM   1110  N   GLY A 148     -29.340 -44.263-105.342  1.00 95.42           N  
ANISOU 1110  N   GLY A 148    10965  13501  11788    296   -890    328       N  
ATOM   1111  CA  GLY A 148     -28.358 -44.502-104.309  1.00 93.53           C  
ANISOU 1111  CA  GLY A 148    10610  13277  11647    287   -918    313       C  
ATOM   1112  C   GLY A 148     -28.503 -43.626-103.088  1.00 92.60           C  
ANISOU 1112  C   GLY A 148    10430  13201  11552    217   -937    354       C  
ATOM   1113  O   GLY A 148     -28.189 -44.065-101.981  1.00 93.83           O  
ANISOU 1113  O   GLY A 148    10514  13364  11773    202  -1018    363       O  
ATOM   1114  N   ASP A 149     -28.973 -42.393-103.261  1.00 90.74           N  
ANISOU 1114  N   ASP A 149    10227  12991  11259    179   -867    380       N  
ATOM   1115  CA  ASP A 149     -29.012 -41.487-102.109  1.00 90.81           C  
ANISOU 1115  CA  ASP A 149    10186  13033  11282    123   -882    412       C  
ATOM   1116  C   ASP A 149     -30.272 -41.594-101.256  1.00 87.49           C  
ANISOU 1116  C   ASP A 149     9798  12631  10812    100   -984    477       C  
ATOM   1117  O   ASP A 149     -31.344 -41.986-101.726  1.00 83.39           O  
ANISOU 1117  O   ASP A 149     9352  12105  10225    111  -1021    510       O  
ATOM   1118  CB  ASP A 149     -28.671 -40.018-102.460  1.00 91.28           C  
ANISOU 1118  CB  ASP A 149    10250  13110  11320     91   -766    407       C  
ATOM   1119  CG  ASP A 149     -29.521 -39.468-103.578  1.00 91.07           C  
ANISOU 1119  CG  ASP A 149    10327  13080  11194     97   -698    419       C  
ATOM   1120  OD1 ASP A 149     -30.582 -40.065-103.853  1.00 91.42           O  
ANISOU 1120  OD1 ASP A 149    10441  13115  11179    116   -756    445       O  
ATOM   1121  OD2 ASP A 149     -29.128 -38.442-104.178  1.00 89.82           O  
ANISOU 1121  OD2 ASP A 149    10180  12927  11020     81   -593    407       O  
ATOM   1122  N   ILE A 150     -30.078 -41.255 -99.985  1.00 86.56           N  
ANISOU 1122  N   ILE A 150     9620  12537  10729     71  -1031    497       N  
ATOM   1123  CA  ILE A 150     -31.082 -41.326 -98.941  1.00 84.54           C  
ANISOU 1123  CA  ILE A 150     9374  12311  10435     56  -1125    563       C  
ATOM   1124  C   ILE A 150     -32.101 -40.189 -99.093  1.00 84.14           C  
ANISOU 1124  C   ILE A 150     9394  12292  10283     42  -1081    607       C  
ATOM   1125  O   ILE A 150     -31.734 -39.020 -99.179  1.00 84.23           O  
ANISOU 1125  O   ILE A 150     9415  12307  10280     25  -1004    589       O  
ATOM   1126  CB  ILE A 150     -30.398 -41.237 -97.552  1.00 83.67           C  
ANISOU 1126  CB  ILE A 150     9182  12215  10393     38  -1179    562       C  
ATOM   1127  CG1 ILE A 150     -29.177 -42.179 -97.443  1.00 82.54           C  
ANISOU 1127  CG1 ILE A 150     8960  12041  10359     52  -1205    509       C  
ATOM   1128  CG2 ILE A 150     -31.411 -41.396 -96.426  1.00 82.88           C  
ANISOU 1128  CG2 ILE A 150     9088  12152  10250     34  -1276    634       C  
ATOM   1129  CD1 ILE A 150     -29.459 -43.655 -97.632  1.00 82.81           C  
ANISOU 1129  CD1 ILE A 150     8999  12052  10411     82  -1289    513       C  
ATOM   1130  N   VAL A 151     -33.382 -40.537 -99.135  1.00 84.37           N  
ANISOU 1130  N   VAL A 151     9473  12340  10242     49  -1135    670       N  
ATOM   1131  CA  VAL A 151     -34.438 -39.533 -99.261  1.00 83.56           C  
ANISOU 1131  CA  VAL A 151     9436  12273  10039     45  -1099    719       C  
ATOM   1132  C   VAL A 151     -35.301 -39.515 -97.997  1.00 83.62           C  
ANISOU 1132  C   VAL A 151     9426  12334  10009     47  -1181    798       C  
ATOM   1133  O   VAL A 151     -35.390 -40.516 -97.269  1.00 83.47           O  
ANISOU 1133  O   VAL A 151     9359  12323  10030     49  -1276    829       O  
ATOM   1134  CB  VAL A 151     -35.295 -39.723-100.549  1.00 82.80           C  
ANISOU 1134  CB  VAL A 151     9420  12163   9877     55  -1073    735       C  
ATOM   1135  CG1 VAL A 151     -36.396 -38.676-100.642  1.00 82.30           C  
ANISOU 1135  CG1 VAL A 151     9419  12139   9708     54  -1038    789       C  
ATOM   1136  CG2 VAL A 151     -34.431 -39.612-101.792  1.00 82.92           C  
ANISOU 1136  CG2 VAL A 151     9460  12131   9915     64   -978    658       C  
ATOM   1137  N   GLU A 152     -35.895 -38.350 -97.736  1.00 82.93           N  
ANISOU 1137  N   GLU A 152     9381  12284   9842     52  -1142    830       N  
ATOM   1138  CA  GLU A 152     -36.853 -38.151 -96.660  1.00 81.52           C  
ANISOU 1138  CA  GLU A 152     9202  12169   9601     70  -1200    913       C  
ATOM   1139  C   GLU A 152     -38.205 -37.744 -97.250  1.00 81.86           C  
ANISOU 1139  C   GLU A 152     9311  12250   9538     85  -1177    979       C  
ATOM   1140  O   GLU A 152     -38.292 -36.836 -98.089  1.00 82.09           O  
ANISOU 1140  O   GLU A 152     9404  12266   9518     85  -1093    952       O  
ATOM   1141  CB  GLU A 152     -36.336 -37.079 -95.711  1.00 80.66           C  
ANISOU 1141  CB  GLU A 152     9091  12072   9484     78  -1181    892       C  
ATOM   1142  CG  GLU A 152     -37.189 -36.837 -94.485  1.00 81.82           C  
ANISOU 1142  CG  GLU A 152     9239  12286   9563    113  -1237    971       C  
ATOM   1143  CD  GLU A 152     -36.349 -36.373 -93.314  1.00 84.86           C  
ANISOU 1143  CD  GLU A 152     9598  12662   9980    119  -1264    940       C  
ATOM   1144  OE1 GLU A 152     -36.346 -35.156 -93.016  1.00 85.56           O  
ANISOU 1144  OE1 GLU A 152     9742  12754  10010    137  -1229    929       O  
ATOM   1145  OE2 GLU A 152     -35.667 -37.231 -92.704  1.00 85.89           O  
ANISOU 1145  OE2 GLU A 152     9660  12777  10196    107  -1326    923       O  
ATOM   1146  N   VAL A 153     -39.255 -38.439 -96.824  1.00 81.46           N  
ANISOU 1146  N   VAL A 153     9244  12250   9457     96  -1254   1072       N  
ATOM   1147  CA  VAL A 153     -40.621 -38.111 -97.219  1.00 80.30           C  
ANISOU 1147  CA  VAL A 153     9144  12153   9212    112  -1246   1155       C  
ATOM   1148  C   VAL A 153     -41.518 -38.020 -95.986  1.00 82.01           C  
ANISOU 1148  C   VAL A 153     9330  12458   9371    145  -1301   1259       C  
ATOM   1149  O   VAL A 153     -41.407 -38.830 -95.057  1.00 81.60           O  
ANISOU 1149  O   VAL A 153     9212  12426   9364    144  -1380   1296       O  
ATOM   1150  CB  VAL A 153     -41.192 -39.137 -98.214  1.00 79.69           C  
ANISOU 1150  CB  VAL A 153     9080  12049   9147     89  -1289   1185       C  
ATOM   1151  CG1 VAL A 153     -40.489 -39.022 -99.555  1.00 80.50           C  
ANISOU 1151  CG1 VAL A 153     9235  12074   9274     75  -1217   1089       C  
ATOM   1152  CG2 VAL A 153     -41.066 -40.555 -97.676  1.00 79.97           C  
ANISOU 1152  CG2 VAL A 153     9050  12075   9258     71  -1401   1217       C  
ATOM   1153  N   ALA A 154     -42.398 -37.025 -95.971  1.00 83.92           N  
ANISOU 1153  N   ALA A 154     9620  12755   9509    181  -1255   1309       N  
ATOM   1154  CA  ALA A 154     -43.326 -36.846 -94.853  1.00 87.13           C  
ANISOU 1154  CA  ALA A 154    10003  13259   9844    230  -1293   1417       C  
ATOM   1155  C   ALA A 154     -44.705 -36.392 -95.322  1.00 88.06           C  
ANISOU 1155  C   ALA A 154    10157  13442   9857    258  -1269   1509       C  
ATOM   1156  O   ALA A 154     -44.900 -36.094 -96.502  1.00 87.77           O  
ANISOU 1156  O   ALA A 154    10176  13368   9802    239  -1220   1480       O  
ATOM   1157  CB  ALA A 154     -42.758 -35.873 -93.833  1.00 89.47           C  
ANISOU 1157  CB  ALA A 154    10315  13566  10110    272  -1267   1377       C  
ATOM   1158  N   VAL A 155     -45.653 -36.353 -94.385  1.00 88.65           N  
ANISOU 1158  N   VAL A 155    10200  13618   9864    308  -1303   1624       N  
ATOM   1159  CA  VAL A 155     -47.047 -35.996 -94.671  1.00 89.19           C  
ANISOU 1159  CA  VAL A 155    10285  13769   9834    343  -1288   1735       C  
ATOM   1160  C   VAL A 155     -47.173 -34.786 -95.614  1.00 88.41           C  
ANISOU 1160  C   VAL A 155    10282  13641   9665    361  -1193   1678       C  
ATOM   1161  O   VAL A 155     -46.701 -33.677 -95.312  1.00 86.74           O  
ANISOU 1161  O   VAL A 155    10129  13417   9409    400  -1134   1612       O  
ATOM   1162  CB  VAL A 155     -47.874 -35.822 -93.367  1.00 91.01           C  
ANISOU 1162  CB  VAL A 155    10473  14122   9985    418  -1313   1857       C  
ATOM   1163  CG1 VAL A 155     -47.318 -34.706 -92.483  1.00 91.26           C  
ANISOU 1163  CG1 VAL A 155    10554  14159   9959    487  -1266   1795       C  
ATOM   1164  CG2 VAL A 155     -49.345 -35.592 -93.682  1.00 92.80           C  
ANISOU 1164  CG2 VAL A 155    10697  14443  10117    454  -1302   1988       C  
ATOM   1165  N   GLY A 156     -47.787 -35.035 -96.769  1.00 86.80           N  
ANISOU 1165  N   GLY A 156    10100  13422   9456    327  -1188   1704       N  
ATOM   1166  CA  GLY A 156     -47.938 -34.024 -97.810  1.00 86.60           C  
ANISOU 1166  CA  GLY A 156    10166  13364   9371    335  -1104   1652       C  
ATOM   1167  C   GLY A 156     -46.901 -34.059 -98.924  1.00 86.62           C  
ANISOU 1167  C   GLY A 156    10217  13250   9443    277  -1063   1523       C  
ATOM   1168  O   GLY A 156     -46.959 -33.247 -99.852  1.00 85.86           O  
ANISOU 1168  O   GLY A 156    10199  13122   9302    279   -991   1478       O  
ATOM   1169  N   ASP A 157     -45.961 -34.998 -98.842  1.00 88.23           N  
ANISOU 1169  N   ASP A 157    10375  13396   9753    232  -1106   1468       N  
ATOM   1170  CA  ASP A 157     -44.884 -35.108 -99.828  1.00 90.59           C  
ANISOU 1170  CA  ASP A 157    10707  13592  10119    189  -1063   1349       C  
ATOM   1171  C   ASP A 157     -45.281 -35.885-101.068  1.00 90.00           C  
ANISOU 1171  C   ASP A 157    10658  13475  10062    153  -1086   1359       C  
ATOM   1172  O   ASP A 157     -46.092 -36.803-101.001  1.00 92.05           O  
ANISOU 1172  O   ASP A 157    10881  13764  10328    141  -1171   1449       O  
ATOM   1173  CB  ASP A 157     -43.650 -35.765 -99.205  1.00 94.53           C  
ANISOU 1173  CB  ASP A 157    11146  14048  10721    166  -1097   1284       C  
ATOM   1174  CG  ASP A 157     -42.799 -34.785 -98.414  1.00 98.95           C  
ANISOU 1174  CG  ASP A 157    11711  14603  11279    186  -1051   1223       C  
ATOM   1175  OD1 ASP A 157     -42.633 -33.632 -98.877  1.00103.07           O  
ANISOU 1175  OD1 ASP A 157    12302  15106  11753    195   -971   1176       O  
ATOM   1176  OD2 ASP A 157     -42.283 -35.168 -97.340  1.00 97.37           O  
ANISOU 1176  OD2 ASP A 157    11452  14415  11128    190  -1102   1222       O  
ATOM   1177  N   LYS A 158     -44.698 -35.513-102.199  1.00 89.53           N  
ANISOU 1177  N   LYS A 158    10664  13343  10009    138  -1014   1268       N  
ATOM   1178  CA  LYS A 158     -44.806 -36.306-103.415  1.00 88.77           C  
ANISOU 1178  CA  LYS A 158    10604  13187   9937    110  -1035   1252       C  
ATOM   1179  C   LYS A 158     -43.480 -37.038-103.619  1.00 88.42           C  
ANISOU 1179  C   LYS A 158    10536  13067   9991     90  -1037   1155       C  
ATOM   1180  O   LYS A 158     -42.456 -36.418-103.911  1.00 90.23           O  
ANISOU 1180  O   LYS A 158    10784  13258  10241     90   -952   1063       O  
ATOM   1181  CB  LYS A 158     -45.136 -35.420-104.617  1.00 88.37           C  
ANISOU 1181  CB  LYS A 158    10648  13112   9816    117   -951   1223       C  
ATOM   1182  CG  LYS A 158     -45.286 -36.171-105.927  1.00 89.54           C  
ANISOU 1182  CG  LYS A 158    10851  13194   9975     97   -972   1204       C  
ATOM   1183  CD  LYS A 158     -44.519 -35.485-107.052  1.00 92.80           C  
ANISOU 1183  CD  LYS A 158    11341  13543  10375    100   -862   1101       C  
ATOM   1184  CE  LYS A 158     -45.225 -34.241-107.581  1.00 94.37           C  
ANISOU 1184  CE  LYS A 158    11614  13765  10477    115   -787   1119       C  
ATOM   1185  NZ  LYS A 158     -46.255 -34.564-108.606  1.00 95.32           N  
ANISOU 1185  NZ  LYS A 158    11800  13870  10547    112   -821   1166       N  
ATOM   1186  N   VAL A 159     -43.512 -38.356-103.436  1.00 86.55           N  
ANISOU 1186  N   VAL A 159    10256  12813   9814     73  -1138   1183       N  
ATOM   1187  CA  VAL A 159     -42.353 -39.233-103.602  1.00 85.05           C  
ANISOU 1187  CA  VAL A 159    10043  12555   9715     63  -1157   1102       C  
ATOM   1188  C   VAL A 159     -41.568 -38.941-104.895  1.00 86.38           C  
ANISOU 1188  C   VAL A 159    10281  12653   9887     71  -1064    999       C  
ATOM   1189  O   VAL A 159     -42.079 -39.140-106.000  1.00 86.95           O  
ANISOU 1189  O   VAL A 159    10427  12690   9920     73  -1065   1002       O  
ATOM   1190  CB  VAL A 159     -42.802 -40.703-103.557  1.00 84.07           C  
ANISOU 1190  CB  VAL A 159     9897  12410   9633     46  -1291   1157       C  
ATOM   1191  CG1 VAL A 159     -41.627 -41.636-103.784  1.00 85.95           C  
ANISOU 1191  CG1 VAL A 159    10123  12575   9959     48  -1313   1070       C  
ATOM   1192  CG2 VAL A 159     -43.476 -40.999-102.227  1.00 83.02           C  
ANISOU 1192  CG2 VAL A 159     9685  12354   9503     38  -1376   1264       C  
ATOM   1193  N   PRO A 160     -40.312 -38.478-104.755  1.00 86.85           N  
ANISOU 1193  N   PRO A 160    10313  12693   9992     75   -987    914       N  
ATOM   1194  CA  PRO A 160     -39.561 -37.915-105.881  1.00 87.48           C  
ANISOU 1194  CA  PRO A 160    10448  12726  10064     84   -875    830       C  
ATOM   1195  C   PRO A 160     -38.970 -38.926-106.862  1.00 89.72           C  
ANISOU 1195  C   PRO A 160    10759  12942  10388    101   -883    772       C  
ATOM   1196  O   PRO A 160     -38.660 -38.551-107.991  1.00 93.33           O  
ANISOU 1196  O   PRO A 160    11279  13364  10815    117   -797    721       O  
ATOM   1197  CB  PRO A 160     -38.436 -37.141-105.196  1.00 87.10           C  
ANISOU 1197  CB  PRO A 160    10342  12689  10062     76   -809    779       C  
ATOM   1198  CG  PRO A 160     -38.214 -37.858-103.910  1.00 87.22           C  
ANISOU 1198  CG  PRO A 160    10270  12726  10142     70   -901    804       C  
ATOM   1199  CD  PRO A 160     -39.526 -38.478-103.507  1.00 86.74           C  
ANISOU 1199  CD  PRO A 160    10212  12702  10042     70  -1005    900       C  
ATOM   1200  N   ALA A 161     -38.794 -40.176-106.433  1.00 89.96           N  
ANISOU 1200  N   ALA A 161    10747  12953  10480    104   -985    778       N  
ATOM   1201  CA  ALA A 161     -38.229 -41.236-107.279  1.00 90.20           C  
ANISOU 1201  CA  ALA A 161    10811  12915  10546    133  -1008    722       C  
ATOM   1202  C   ALA A 161     -38.656 -42.599-106.748  1.00 91.62           C  
ANISOU 1202  C   ALA A 161    10968  13077  10765    126  -1160    768       C  
ATOM   1203  O   ALA A 161     -39.433 -42.669-105.795  1.00 91.85           O  
ANISOU 1203  O   ALA A 161    10953  13153  10791     96  -1237    851       O  
ATOM   1204  CB  ALA A 161     -36.710 -41.133-107.336  1.00 89.56           C  
ANISOU 1204  CB  ALA A 161    10682  12816  10530    155   -923    633       C  
ATOM   1205  N   ASP A 162     -38.167 -43.677-107.364  1.00 93.89           N  
ANISOU 1205  N   ASP A 162    11291  13297  11086    158  -1205    720       N  
ATOM   1206  CA  ASP A 162     -38.432 -45.028-106.860  1.00 96.20           C  
ANISOU 1206  CA  ASP A 162    11565  13560  11425    150  -1359    757       C  
ATOM   1207  C   ASP A 162     -37.544 -45.368-105.664  1.00 95.87           C  
ANISOU 1207  C   ASP A 162    11414  13540  11469    146  -1383    739       C  
ATOM   1208  O   ASP A 162     -36.324 -45.487-105.789  1.00 97.12           O  
ANISOU 1208  O   ASP A 162    11545  13676  11678    180  -1325    656       O  
ATOM   1209  CB  ASP A 162     -38.292 -46.074-107.961  1.00 99.31           C  
ANISOU 1209  CB  ASP A 162    12054  13864  11813    193  -1413    711       C  
ATOM   1210  CG  ASP A 162     -39.628 -46.493-108.545  1.00103.89           C  
ANISOU 1210  CG  ASP A 162    12724  14413  12335    171  -1517    784       C  
ATOM   1211  OD1 ASP A 162     -40.682 -45.967-108.112  1.00103.56           O  
ANISOU 1211  OD1 ASP A 162    12660  14428  12258    124  -1540    876       O  
ATOM   1212  OD2 ASP A 162     -39.620 -47.362-109.444  1.00109.52           O  
ANISOU 1212  OD2 ASP A 162    13532  15044  13037    206  -1581    751       O  
ATOM   1213  N   ILE A 163     -38.177 -45.524-104.505  1.00 93.44           N  
ANISOU 1213  N   ILE A 163    11043  13281  11176    107  -1470    823       N  
ATOM   1214  CA  ILE A 163     -37.467 -45.576-103.235  1.00 90.38           C  
ANISOU 1214  CA  ILE A 163    10551  12928  10857     97  -1483    817       C  
ATOM   1215  C   ILE A 163     -37.761 -46.861-102.475  1.00 90.22           C  
ANISOU 1215  C   ILE A 163    10496  12895  10887     81  -1639    872       C  
ATOM   1216  O   ILE A 163     -38.917 -47.263-102.334  1.00 90.52           O  
ANISOU 1216  O   ILE A 163    10551  12947  10894     51  -1736    969       O  
ATOM   1217  CB  ILE A 163     -37.824 -44.345-102.371  1.00 88.88           C  
ANISOU 1217  CB  ILE A 163    10314  12821  10633     73  -1424    864       C  
ATOM   1218  CG1 ILE A 163     -37.127 -43.099-102.921  1.00 88.72           C  
ANISOU 1218  CG1 ILE A 163    10312  12805  10591     87  -1273    793       C  
ATOM   1219  CG2 ILE A 163     -37.439 -44.557-100.914  1.00 89.20           C  
ANISOU 1219  CG2 ILE A 163    10259  12900  10733     61  -1479    887       C  
ATOM   1220  CD1 ILE A 163     -37.831 -41.799-102.600  1.00 88.17           C  
ANISOU 1220  CD1 ILE A 163    10252  12797  10451     71  -1214    841       C  
ATOM   1221  N   ARG A 164     -36.697 -47.510-102.011  1.00 89.45           N  
ANISOU 1221  N   ARG A 164    10346  12771  10869     99  -1664    815       N  
ATOM   1222  CA  ARG A 164     -36.810 -48.612-101.065  1.00 88.07           C  
ANISOU 1222  CA  ARG A 164    10122  12590  10750     81  -1805    864       C  
ATOM   1223  C   ARG A 164     -36.821 -48.014 -99.666  1.00 87.03           C  
ANISOU 1223  C   ARG A 164     9896  12537  10633     55  -1797    911       C  
ATOM   1224  O   ARG A 164     -35.887 -47.305 -99.285  1.00 87.53           O  
ANISOU 1224  O   ARG A 164     9911  12620  10725     68  -1708    850       O  
ATOM   1225  CB  ARG A 164     -35.633 -49.580-101.231  1.00 87.66           C  
ANISOU 1225  CB  ARG A 164    10063  12470  10771    121  -1836    776       C  
ATOM   1226  CG  ARG A 164     -35.473 -50.612-100.122  1.00 86.32           C  
ANISOU 1226  CG  ARG A 164     9830  12294  10671    106  -1967    809       C  
ATOM   1227  CD  ARG A 164     -36.562 -51.666-100.162  1.00 85.48           C  
ANISOU 1227  CD  ARG A 164     9769  12155  10551     75  -2125    899       C  
ATOM   1228  NE  ARG A 164     -36.094 -52.945 -99.636  1.00 86.02           N  
ANISOU 1228  NE  ARG A 164     9817  12175  10692     81  -2252    890       N  
ATOM   1229  CZ  ARG A 164     -36.423 -53.438 -98.448  1.00 85.78           C  
ANISOU 1229  CZ  ARG A 164     9718  12176  10698     41  -2356    970       C  
ATOM   1230  NH1 ARG A 164     -37.232 -52.762 -97.647  1.00 86.06           N  
ANISOU 1230  NH1 ARG A 164     9699  12299  10700      0  -2345   1067       N  
ATOM   1231  NH2 ARG A 164     -35.947 -54.612 -98.061  1.00 86.24           N  
ANISOU 1231  NH2 ARG A 164     9765  12179  10820     49  -2472    955       N  
ATOM   1232  N   ILE A 165     -37.876 -48.294 -98.905  1.00 85.38           N  
ANISOU 1232  N   ILE A 165     9663  12373  10403     21  -1891   1024       N  
ATOM   1233  CA  ILE A 165     -37.995 -47.759 -97.547  1.00 84.43           C  
ANISOU 1233  CA  ILE A 165     9463  12333  10283      8  -1889   1078       C  
ATOM   1234  C   ILE A 165     -36.956 -48.396 -96.623  1.00 85.26           C  
ANISOU 1234  C   ILE A 165     9498  12420  10476     14  -1938   1036       C  
ATOM   1235  O   ILE A 165     -36.851 -49.617 -96.531  1.00 86.18           O  
ANISOU 1235  O   ILE A 165     9609  12491  10644      9  -2049   1044       O  
ATOM   1236  CB  ILE A 165     -39.421 -47.933 -96.981  1.00 82.67           C  
ANISOU 1236  CB  ILE A 165     9226  12174  10010    -21  -1974   1223       C  
ATOM   1237  CG1 ILE A 165     -40.440 -47.331 -97.948  1.00 81.15           C  
ANISOU 1237  CG1 ILE A 165     9102  11996   9734    -26  -1929   1266       C  
ATOM   1238  CG2 ILE A 165     -39.534 -47.289 -95.605  1.00 81.58           C  
ANISOU 1238  CG2 ILE A 165     9016  12123   9856    -17  -1958   1276       C  
ATOM   1239  CD1 ILE A 165     -41.873 -47.736 -97.695  1.00 80.90           C  
ANISOU 1239  CD1 ILE A 165     9061  12015   9662    -58  -2027   1415       C  
ATOM   1240  N   LEU A 166     -36.171 -47.556 -95.962  1.00 86.25           N  
ANISOU 1240  N   LEU A 166     9574  12575  10619     26  -1861    988       N  
ATOM   1241  CA  LEU A 166     -35.163 -48.034 -95.025  1.00 88.15           C  
ANISOU 1241  CA  LEU A 166     9744  12804  10943     31  -1903    948       C  
ATOM   1242  C   LEU A 166     -35.692 -48.027 -93.596  1.00 88.51           C  
ANISOU 1242  C   LEU A 166     9734  12916  10978     17  -1972   1038       C  
ATOM   1243  O   LEU A 166     -35.470 -48.975 -92.843  1.00 90.38           O  
ANISOU 1243  O   LEU A 166     9926  13142  11271     10  -2072   1059       O  
ATOM   1244  CB  LEU A 166     -33.893 -47.190 -95.118  1.00 88.52           C  
ANISOU 1244  CB  LEU A 166     9767  12838  11027     49  -1792    846       C  
ATOM   1245  CG  LEU A 166     -33.074 -47.304 -96.399  1.00 89.23           C  
ANISOU 1245  CG  LEU A 166     9891  12867  11144     74  -1721    751       C  
ATOM   1246  CD1 LEU A 166     -32.097 -46.146 -96.465  1.00 90.73           C  
ANISOU 1246  CD1 LEU A 166    10054  13068  11351     78  -1598    683       C  
ATOM   1247  CD2 LEU A 166     -32.340 -48.633 -96.464  1.00 89.92           C  
ANISOU 1247  CD2 LEU A 166     9958  12897  11311     95  -1799    707       C  
ATOM   1248  N   SER A 167     -36.374 -46.950 -93.221  1.00 87.54           N  
ANISOU 1248  N   SER A 167     9618  12862  10778     19  -1916   1091       N  
ATOM   1249  CA  SER A 167     -37.029 -46.881 -91.925  1.00 87.67           C  
ANISOU 1249  CA  SER A 167     9593  12953  10764     19  -1972   1189       C  
ATOM   1250  C   SER A 167     -38.196 -45.904 -91.951  1.00 87.98           C  
ANISOU 1250  C   SER A 167     9665  13068  10695     30  -1920   1270       C  
ATOM   1251  O   SER A 167     -38.133 -44.848 -92.592  1.00 86.18           O  
ANISOU 1251  O   SER A 167     9483  12837  10421     42  -1817   1223       O  
ATOM   1252  CB  SER A 167     -36.039 -46.522 -90.810  1.00 88.07           C  
ANISOU 1252  CB  SER A 167     9592  13011  10858     34  -1965   1140       C  
ATOM   1253  OG  SER A 167     -36.023 -45.130 -90.552  1.00 88.50           O  
ANISOU 1253  OG  SER A 167     9669  13103  10853     54  -1874   1124       O  
ATOM   1254  N   ILE A 168     -39.263 -46.289 -91.258  1.00 89.02           N  
ANISOU 1254  N   ILE A 168     9769  13266  10785     27  -1993   1397       N  
ATOM   1255  CA  ILE A 168     -40.420 -45.438 -91.060  1.00 89.59           C  
ANISOU 1255  CA  ILE A 168     9859  13428  10753     49  -1953   1492       C  
ATOM   1256  C   ILE A 168     -40.243 -44.772 -89.703  1.00 94.03           C  
ANISOU 1256  C   ILE A 168    10390  14052  11282     89  -1938   1510       C  
ATOM   1257  O   ILE A 168     -40.248 -45.444 -88.669  1.00 95.91           O  
ANISOU 1257  O   ILE A 168    10573  14320  11547     91  -2018   1565       O  
ATOM   1258  CB  ILE A 168     -41.730 -46.246 -91.151  1.00 87.59           C  
ANISOU 1258  CB  ILE A 168     9588  13220  10471     24  -2040   1635       C  
ATOM   1259  CG1 ILE A 168     -41.976 -46.649 -92.609  1.00 86.98           C  
ANISOU 1259  CG1 ILE A 168     9566  13076  10406     -8  -2045   1611       C  
ATOM   1260  CG2 ILE A 168     -42.909 -45.433 -90.629  1.00 87.89           C  
ANISOU 1260  CG2 ILE A 168     9619  13373  10402     59  -2005   1753       C  
ATOM   1261  CD1 ILE A 168     -42.696 -47.962 -92.796  1.00 86.91           C  
ANISOU 1261  CD1 ILE A 168     9540  13052  10429    -53  -2177   1708       C  
ATOM   1262  N   LYS A 169     -40.047 -43.453 -89.723  1.00 98.34           N  
ANISOU 1262  N   LYS A 169    10980  14612  11772    123  -1840   1459       N  
ATOM   1263  CA  LYS A 169     -39.809 -42.665 -88.508  1.00 99.82           C  
ANISOU 1263  CA  LYS A 169    11162  14844  11919    170  -1824   1460       C  
ATOM   1264  C   LYS A 169     -41.113 -42.393 -87.765  1.00101.86           C  
ANISOU 1264  C   LYS A 169    11415  15217  12071    217  -1837   1598       C  
ATOM   1265  O   LYS A 169     -41.109 -42.026 -86.593  1.00100.62           O  
ANISOU 1265  O   LYS A 169    11248  15111  11872    266  -1849   1628       O  
ATOM   1266  CB  LYS A 169     -39.102 -41.346 -88.848  1.00 99.17           C  
ANISOU 1266  CB  LYS A 169    11139  14723  11815    186  -1726   1355       C  
ATOM   1267  CG  LYS A 169     -37.821 -41.495 -89.658  1.00 98.91           C  
ANISOU 1267  CG  LYS A 169    11106  14591  11882    144  -1697   1228       C  
ATOM   1268  CD  LYS A 169     -36.748 -42.259 -88.899  1.00100.71           C  
ANISOU 1268  CD  LYS A 169    11272  14779  12212    129  -1764   1181       C  
ATOM   1269  CE  LYS A 169     -35.405 -42.147 -89.605  1.00104.58           C  
ANISOU 1269  CE  LYS A 169    11758  15184  12792    100  -1718   1057       C  
ATOM   1270  NZ  LYS A 169     -34.294 -42.772 -88.830  1.00107.47           N  
ANISOU 1270  NZ  LYS A 169    12061  15513  13257     90  -1779   1009       N  
ATOM   1271  N   SER A 170     -42.224 -42.588 -88.468  1.00107.65           N  
ANISOU 1271  N   SER A 170    12153  15989  12757    206  -1836   1686       N  
ATOM   1272  CA  SER A 170     -43.555 -42.414 -87.918  1.00114.77           C  
ANISOU 1272  CA  SER A 170    13037  17009  13561    249  -1845   1835       C  
ATOM   1273  C   SER A 170     -44.043 -43.694 -87.227  1.00119.72           C  
ANISOU 1273  C   SER A 170    13581  17681  14224    225  -1956   1955       C  
ATOM   1274  O   SER A 170     -43.361 -44.724 -87.249  1.00119.70           O  
ANISOU 1274  O   SER A 170    13547  17610  14324    174  -2029   1915       O  
ATOM   1275  CB  SER A 170     -44.504 -42.033 -89.050  1.00115.66           C  
ANISOU 1275  CB  SER A 170    13188  17140  13615    241  -1797   1878       C  
ATOM   1276  OG  SER A 170     -45.707 -41.487 -88.548  1.00124.71           O  
ANISOU 1276  OG  SER A 170    14327  18406  14648    301  -1776   2006       O  
ATOM   1277  N   THR A 171     -45.218 -43.616 -86.602  1.00127.12           N  
ANISOU 1277  N   THR A 171    14484  18738  15077    266  -1968   2107       N  
ATOM   1278  CA  THR A 171     -45.886 -44.796 -86.039  1.00132.23           C  
ANISOU 1278  CA  THR A 171    15047  19442  15750    237  -2072   2251       C  
ATOM   1279  C   THR A 171     -46.579 -45.572 -87.165  1.00131.90           C  
ANISOU 1279  C   THR A 171    14995  19375  15745    164  -2124   2313       C  
ATOM   1280  O   THR A 171     -46.728 -46.792 -87.097  1.00136.19           O  
ANISOU 1280  O   THR A 171    15486  19900  16358    105  -2232   2381       O  
ATOM   1281  CB  THR A 171     -46.908 -44.428 -84.936  1.00132.88           C  
ANISOU 1281  CB  THR A 171    15088  19675  15725    314  -2062   2406       C  
ATOM   1282  OG1 THR A 171     -46.448 -43.286 -84.200  1.00133.78           O  
ANISOU 1282  OG1 THR A 171    15253  19811  15766    402  -1986   2336       O  
ATOM   1283  CG2 THR A 171     -47.111 -45.600 -83.968  1.00131.28           C  
ANISOU 1283  CG2 THR A 171    14796  19520  15565    292  -2169   2524       C  
ATOM   1284  N   THR A 172     -46.993 -44.850 -88.201  1.00128.49           N  
ANISOU 1284  N   THR A 172    14620  18934  15266    168  -2052   2289       N  
ATOM   1285  CA  THR A 172     -47.564 -45.453 -89.399  1.00128.82           C  
ANISOU 1285  CA  THR A 172    14673  18933  15339    101  -2097   2326       C  
ATOM   1286  C   THR A 172     -47.212 -44.609 -90.618  1.00124.69           C  
ANISOU 1286  C   THR A 172    14241  18338  14798    104  -2003   2198       C  
ATOM   1287  O   THR A 172     -47.104 -43.384 -90.523  1.00125.64           O  
ANISOU 1287  O   THR A 172    14405  18487  14846    163  -1899   2147       O  
ATOM   1288  CB  THR A 172     -49.100 -45.613 -89.291  1.00135.98           C  
ANISOU 1288  CB  THR A 172    15525  19958  16182    102  -2133   2526       C  
ATOM   1289  OG1 THR A 172     -49.644 -45.973 -90.571  1.00138.80           O  
ANISOU 1289  OG1 THR A 172    15913  20265  16559     41  -2167   2547       O  
ATOM   1290  CG2 THR A 172     -49.766 -44.315 -88.799  1.00140.46           C  
ANISOU 1290  CG2 THR A 172    16100  20645  16621    196  -2027   2580       C  
ATOM   1291  N   LEU A 173     -47.024 -45.266 -91.758  1.00118.10           N  
ANISOU 1291  N   LEU A 173    13440  17405  14025     43  -2043   2148       N  
ATOM   1292  CA  LEU A 173     -46.803 -44.557 -93.011  1.00112.05           C  
ANISOU 1292  CA  LEU A 173    12760  16574  13238     43  -1959   2044       C  
ATOM   1293  C   LEU A 173     -47.905 -44.906 -94.008  1.00110.19           C  
ANISOU 1293  C   LEU A 173    12544  16341  12981      4  -2003   2136       C  
ATOM   1294  O   LEU A 173     -48.004 -46.049 -94.459  1.00110.63           O  
ANISOU 1294  O   LEU A 173    12594  16336  13101    -53  -2110   2164       O  
ATOM   1295  CB  LEU A 173     -45.412 -44.868 -93.582  1.00107.91           C  
ANISOU 1295  CB  LEU A 173    12277  15923  12800     20  -1948   1877       C  
ATOM   1296  CG  LEU A 173     -44.990 -44.120 -94.855  1.00104.77           C  
ANISOU 1296  CG  LEU A 173    11967  15455  12385     24  -1850   1758       C  
ATOM   1297  CD1 LEU A 173     -44.490 -42.716 -94.548  1.00103.05           C  
ANISOU 1297  CD1 LEU A 173    11776  15261  12115     75  -1728   1683       C  
ATOM   1298  CD2 LEU A 173     -43.934 -44.907 -95.614  1.00103.06           C  
ANISOU 1298  CD2 LEU A 173    11778  15119  12258     -5  -1876   1641       C  
ATOM   1299  N   ARG A 174     -48.733 -43.917 -94.334  1.00108.41           N  
ANISOU 1299  N   ARG A 174    12345  16181  12663     39  -1927   2184       N  
ATOM   1300  CA  ARG A 174     -49.833 -44.107 -95.274  1.00111.57           C  
ANISOU 1300  CA  ARG A 174    12764  16590  13035      6  -1963   2276       C  
ATOM   1301  C   ARG A 174     -49.519 -43.439 -96.608  1.00109.66           C  
ANISOU 1301  C   ARG A 174    12625  16267  12773      7  -1881   2154       C  
ATOM   1302  O   ARG A 174     -49.267 -42.235 -96.660  1.00110.20           O  
ANISOU 1302  O   ARG A 174    12737  16353  12780     58  -1764   2084       O  
ATOM   1303  CB  ARG A 174     -51.145 -43.551 -94.708  1.00118.01           C  
ANISOU 1303  CB  ARG A 174    13527  17552  13759     46  -1945   2441       C  
ATOM   1304  CG  ARG A 174     -51.583 -44.106 -93.355  1.00128.33           C  
ANISOU 1304  CG  ARG A 174    14727  18963  15068     57  -2013   2583       C  
ATOM   1305  CD  ARG A 174     -51.882 -45.598 -93.397  1.00136.23           C  
ANISOU 1305  CD  ARG A 174    15673  19932  16156    -27  -2167   2679       C  
ATOM   1306  NE  ARG A 174     -53.179 -45.912 -92.799  1.00143.98           N  
ANISOU 1306  NE  ARG A 174    16558  21044  17101    -31  -2228   2896       N  
ATOM   1307  CZ  ARG A 174     -54.297 -46.114 -93.496  1.00147.08           C  
ANISOU 1307  CZ  ARG A 174    16938  21466  17478    -71  -2278   3022       C  
ATOM   1308  NH1 ARG A 174     -54.281 -46.046 -94.821  1.00146.76           N  
ANISOU 1308  NH1 ARG A 174    16984  21327  17450   -108  -2278   2945       N  
ATOM   1309  NH2 ARG A 174     -55.435 -46.390 -92.871  1.00150.65           N  
ANISOU 1309  NH2 ARG A 174    17288  22049  17903    -75  -2331   3231       N  
ATOM   1310  N   VAL A 175     -49.545 -44.226 -97.682  1.00106.35           N  
ANISOU 1310  N   VAL A 175    12251  15755  12400    -46  -1948   2133       N  
ATOM   1311  CA  VAL A 175     -49.161 -43.748 -99.010  1.00104.37           C  
ANISOU 1311  CA  VAL A 175    12104  15416  12136    -46  -1878   2013       C  
ATOM   1312  C   VAL A 175     -50.355 -43.788 -99.952  1.00105.46           C  
ANISOU 1312  C   VAL A 175    12278  15561  12230    -71  -1916   2106       C  
ATOM   1313  O   VAL A 175     -51.074 -44.781 -99.999  1.00109.62           O  
ANISOU 1313  O   VAL A 175    12773  16087  12788   -121  -2045   2218       O  
ATOM   1314  CB  VAL A 175     -48.007 -44.597 -99.596  1.00104.34           C  
ANISOU 1314  CB  VAL A 175    12143  15281  12218    -72  -1915   1884       C  
ATOM   1315  CG1 VAL A 175     -47.565 -44.084-100.966  1.00101.51           C  
ANISOU 1315  CG1 VAL A 175    11890  14838  11839    -62  -1832   1762       C  
ATOM   1316  CG2 VAL A 175     -46.828 -44.618 -98.634  1.00105.75           C  
ANISOU 1316  CG2 VAL A 175    12275  15455  12450    -51  -1887   1801       C  
ATOM   1317  N   ASP A 176     -50.552 -42.702-100.697  1.00105.42           N  
ANISOU 1317  N   ASP A 176    12341  15560  12154    -40  -1811   2060       N  
ATOM   1318  CA  ASP A 176     -51.611 -42.604-101.700  1.00105.26           C  
ANISOU 1318  CA  ASP A 176    12368  15538  12087    -60  -1834   2130       C  
ATOM   1319  C   ASP A 176     -51.087 -43.024-103.078  1.00104.62           C  
ANISOU 1319  C   ASP A 176    12393  15321  12037    -87  -1849   2018       C  
ATOM   1320  O   ASP A 176     -50.595 -42.196-103.847  1.00101.52           O  
ANISOU 1320  O   ASP A 176    12080  14885  11608    -58  -1739   1905       O  
ATOM   1321  CB  ASP A 176     -52.167 -41.174-101.734  1.00107.28           C  
ANISOU 1321  CB  ASP A 176    12644  15875  12240     -5  -1714   2148       C  
ATOM   1322  CG  ASP A 176     -53.385 -41.037-102.627  1.00110.14           C  
ANISOU 1322  CG  ASP A 176    13041  16256  12551    -21  -1742   2242       C  
ATOM   1323  OD1 ASP A 176     -54.338 -41.831-102.465  1.00114.74           O  
ANISOU 1323  OD1 ASP A 176    13564  16880  13152    -61  -1859   2390       O  
ATOM   1324  OD2 ASP A 176     -53.395 -40.131-103.490  1.00108.68           O  
ANISOU 1324  OD2 ASP A 176    12940  16044  12309      3  -1651   2173       O  
ATOM   1325  N   GLN A 177     -51.201 -44.316-103.380  1.00108.10           N  
ANISOU 1325  N   GLN A 177    12839  15693  12541   -139  -1988   2053       N  
ATOM   1326  CA  GLN A 177     -50.616 -44.896-104.599  1.00111.68           C  
ANISOU 1326  CA  GLN A 177    13398  16008  13025   -153  -2019   1944       C  
ATOM   1327  C   GLN A 177     -51.513 -44.749-105.826  1.00114.00           C  
ANISOU 1327  C   GLN A 177    13778  16267  13268   -169  -2044   1980       C  
ATOM   1328  O   GLN A 177     -51.090 -45.020-106.955  1.00114.71           O  
ANISOU 1328  O   GLN A 177    13976  16247  13361   -166  -2049   1884       O  
ATOM   1329  CB  GLN A 177     -50.264 -46.369-104.381  1.00112.80           C  
ANISOU 1329  CB  GLN A 177    13525  16078  13254   -193  -2167   1953       C  
ATOM   1330  CG  GLN A 177     -49.264 -46.600-103.260  1.00119.52           C  
ANISOU 1330  CG  GLN A 177    14300  16947  14162   -176  -2149   1901       C  
ATOM   1331  CD  GLN A 177     -48.481 -47.887-103.417  1.00123.81           C  
ANISOU 1331  CD  GLN A 177    14871  17381  14787   -194  -2255   1838       C  
ATOM   1332  OE1 GLN A 177     -49.011 -48.899-103.880  1.00127.45           O  
ANISOU 1332  OE1 GLN A 177    15370  17780  15274   -237  -2400   1898       O  
ATOM   1333  NE2 GLN A 177     -47.207 -47.853-103.031  1.00122.38           N  
ANISOU 1333  NE2 GLN A 177    14674  17175  14647   -160  -2189   1717       N  
ATOM   1334  N   SER A 178     -52.748 -44.318-105.584  1.00113.04           N  
ANISOU 1334  N   SER A 178    13609  16242  13096   -180  -2058   2123       N  
ATOM   1335  CA  SER A 178     -53.780 -44.143-106.608  1.00110.26           C  
ANISOU 1335  CA  SER A 178    13322  15877  12695   -199  -2093   2187       C  
ATOM   1336  C   SER A 178     -53.285 -43.818-108.021  1.00108.16           C  
ANISOU 1336  C   SER A 178    13197  15498  12398   -179  -2031   2048       C  
ATOM   1337  O   SER A 178     -53.733 -44.426-108.985  1.00109.03           O  
ANISOU 1337  O   SER A 178    13387  15527  12511   -211  -2129   2066       O  
ATOM   1338  CB  SER A 178     -54.785 -43.095-106.138  1.00111.19           C  
ANISOU 1338  CB  SER A 178    13377  16132  12737   -174  -2023   2300       C  
ATOM   1339  OG  SER A 178     -54.133 -42.083-105.390  1.00110.44           O  
ANISOU 1339  OG  SER A 178    13250  16101  12609   -113  -1879   2228       O  
ATOM   1340  N   ILE A 179     -52.357 -42.871-108.134  1.00108.96           N  
ANISOU 1340  N   ILE A 179    13333  15595  12471   -127  -1873   1913       N  
ATOM   1341  CA  ILE A 179     -51.842 -42.413-109.433  1.00110.40           C  
ANISOU 1341  CA  ILE A 179    13642  15688  12617   -100  -1790   1784       C  
ATOM   1342  C   ILE A 179     -51.185 -43.530-110.258  1.00110.05           C  
ANISOU 1342  C   ILE A 179    13684  15508  12620   -109  -1872   1699       C  
ATOM   1343  O   ILE A 179     -51.068 -43.420-111.481  1.00105.93           O  
ANISOU 1343  O   ILE A 179    13280  14905  12063    -92  -1847   1627       O  
ATOM   1344  CB  ILE A 179     -50.863 -41.217-109.257  1.00112.39           C  
ANISOU 1344  CB  ILE A 179    13897  15964  12839    -49  -1610   1664       C  
ATOM   1345  CG1 ILE A 179     -50.723 -40.409-110.558  1.00113.05           C  
ANISOU 1345  CG1 ILE A 179    14100  15993  12859    -22  -1508   1576       C  
ATOM   1346  CG2 ILE A 179     -49.511 -41.682-108.720  1.00112.16           C  
ANISOU 1346  CG2 ILE A 179    13834  15898  12884    -37  -1591   1563       C  
ATOM   1347  CD1 ILE A 179     -50.053 -39.056-110.388  1.00111.78           C  
ANISOU 1347  CD1 ILE A 179    13941  15871  12659     16  -1340   1493       C  
ATOM   1348  N   LEU A 180     -50.776 -44.603-109.582  1.00113.77           N  
ANISOU 1348  N   LEU A 180    14101  15956  13168   -131  -1973   1711       N  
ATOM   1349  CA  LEU A 180     -50.014 -45.678-110.213  1.00117.04           C  
ANISOU 1349  CA  LEU A 180    14595  16245  13629   -125  -2048   1622       C  
ATOM   1350  C   LEU A 180     -50.734 -47.023-110.222  1.00122.13           C  
ANISOU 1350  C   LEU A 180    15248  16835  14317   -180  -2258   1725       C  
ATOM   1351  O   LEU A 180     -50.633 -47.767-111.196  1.00129.79           O  
ANISOU 1351  O   LEU A 180    16335  17689  15291   -177  -2343   1678       O  
ATOM   1352  CB  LEU A 180     -48.643 -45.831-109.546  1.00112.86           C  
ANISOU 1352  CB  LEU A 180    14015  15709  13156    -93  -1984   1516       C  
ATOM   1353  CG  LEU A 180     -47.636 -46.733-110.263  1.00111.57           C  
ANISOU 1353  CG  LEU A 180    13939  15423  13030    -61  -2018   1396       C  
ATOM   1354  CD1 LEU A 180     -46.969 -46.003-111.418  1.00110.75           C  
ANISOU 1354  CD1 LEU A 180    13936  15271  12872     -4  -1877   1269       C  
ATOM   1355  CD2 LEU A 180     -46.597 -47.252-109.288  1.00111.38           C  
ANISOU 1355  CD2 LEU A 180    13831  15405  13082    -50  -2022   1348       C  
ATOM   1356  N   THR A 181     -51.454 -47.338-109.151  1.00123.87           N  
ANISOU 1356  N   THR A 181    15354  17140  14571   -229  -2344   1867       N  
ATOM   1357  CA  THR A 181     -52.087 -48.653-109.034  1.00129.56           C  
ANISOU 1357  CA  THR A 181    16069  17812  15345   -292  -2554   1977       C  
ATOM   1358  C   THR A 181     -53.605 -48.628-109.196  1.00131.59           C  
ANISOU 1358  C   THR A 181    16305  18117  15575   -350  -2652   2151       C  
ATOM   1359  O   THR A 181     -54.194 -49.577-109.717  1.00135.86           O  
ANISOU 1359  O   THR A 181    16901  18577  16140   -401  -2825   2219       O  
ATOM   1360  CB  THR A 181     -51.744 -49.330-107.697  1.00131.05           C  
ANISOU 1360  CB  THR A 181    16139  18046  15607   -314  -2615   2026       C  
ATOM   1361  OG1 THR A 181     -52.098 -48.453-106.624  1.00131.89           O  
ANISOU 1361  OG1 THR A 181    16118  18302  15691   -308  -2520   2105       O  
ATOM   1362  CG2 THR A 181     -50.253 -49.659-107.620  1.00131.69           C  
ANISOU 1362  CG2 THR A 181    16248  18057  15729   -265  -2562   1863       C  
ATOM   1363  N   GLY A 182     -54.229 -47.545-108.748  1.00132.11           N  
ANISOU 1363  N   GLY A 182    16291  18313  15589   -339  -2546   2224       N  
ATOM   1364  CA  GLY A 182     -55.682 -47.429-108.766  1.00131.86           C  
ANISOU 1364  CA  GLY A 182    16215  18354  15532   -386  -2623   2403       C  
ATOM   1365  C   GLY A 182     -56.258 -47.497-107.366  1.00132.31           C  
ANISOU 1365  C   GLY A 182    16106  18551  15613   -411  -2652   2561       C  
ATOM   1366  O   GLY A 182     -57.313 -46.917-107.098  1.00130.98           O  
ANISOU 1366  O   GLY A 182    15867  18498  15402   -417  -2634   2698       O  
ATOM   1367  N   GLU A 183     -55.561 -48.203-106.474  1.00134.52           N  
ANISOU 1367  N   GLU A 183    16326  18826  15957   -419  -2693   2544       N  
ATOM   1368  CA  GLU A 183     -55.991 -48.340-105.081  1.00137.89           C  
ANISOU 1368  CA  GLU A 183    16600  19384  16408   -436  -2719   2687       C  
ATOM   1369  C   GLU A 183     -56.130 -46.969-104.426  1.00138.75           C  
ANISOU 1369  C   GLU A 183    16639  19634  16443   -369  -2542   2696       C  
ATOM   1370  O   GLU A 183     -55.139 -46.324-104.063  1.00138.03           O  
ANISOU 1370  O   GLU A 183    16556  19550  16337   -310  -2408   2563       O  
ATOM   1371  CB  GLU A 183     -55.062 -49.276-104.289  1.00138.84           C  
ANISOU 1371  CB  GLU A 183    16684  19461  16607   -448  -2781   2640       C  
ATOM   1372  CG  GLU A 183     -53.579 -48.929-104.345  1.00140.10           C  
ANISOU 1372  CG  GLU A 183    16900  19558  16772   -383  -2654   2430       C  
ATOM   1373  CD  GLU A 183     -52.665 -50.096-103.992  1.00142.80           C  
ANISOU 1373  CD  GLU A 183    17247  19812  17199   -401  -2752   2368       C  
ATOM   1374  OE1 GLU A 183     -53.008 -50.893-103.089  1.00147.68           O  
ANISOU 1374  OE1 GLU A 183    17775  20468  17867   -447  -2869   2489       O  
ATOM   1375  OE2 GLU A 183     -51.585 -50.209-104.612  1.00136.84           O  
ANISOU 1375  OE2 GLU A 183    16583  18951  16457   -363  -2708   2200       O  
ATOM   1376  N   SER A 184     -57.378 -46.525-104.307  1.00139.84           N  
ANISOU 1376  N   SER A 184    16715  19884  16534   -377  -2549   2857       N  
ATOM   1377  CA  SER A 184     -57.676 -45.161-103.891  1.00139.87           C  
ANISOU 1377  CA  SER A 184    16678  20014  16450   -304  -2388   2869       C  
ATOM   1378  C   SER A 184     -57.649 -44.991-102.371  1.00137.00           C  
ANISOU 1378  C   SER A 184    16185  19785  16082   -268  -2347   2946       C  
ATOM   1379  O   SER A 184     -57.596 -43.868-101.867  1.00137.49           O  
ANISOU 1379  O   SER A 184    16227  19938  16073   -192  -2207   2921       O  
ATOM   1380  CB  SER A 184     -59.013 -44.707-104.476  1.00146.11           C  
ANISOU 1380  CB  SER A 184    17463  20867  17182   -315  -2405   3003       C  
ATOM   1381  OG  SER A 184     -58.907 -43.395-105.005  1.00149.23           O  
ANISOU 1381  OG  SER A 184    17929  21277  17493   -247  -2248   2905       O  
ATOM   1382  N   VAL A 185     -57.687 -46.108-101.650  1.00133.37           N  
ANISOU 1382  N   VAL A 185    15646  19331  15695   -321  -2475   3039       N  
ATOM   1383  CA  VAL A 185     -57.397 -46.114-100.215  1.00129.55           C  
ANISOU 1383  CA  VAL A 185    15055  18947  15218   -287  -2443   3081       C  
ATOM   1384  C   VAL A 185     -55.876 -46.172-100.009  1.00128.19           C  
ANISOU 1384  C   VAL A 185    14937  18682  15087   -260  -2387   2882       C  
ATOM   1385  O   VAL A 185     -55.166 -46.903-100.711  1.00127.30           O  
ANISOU 1385  O   VAL A 185    14902  18429  15036   -299  -2451   2775       O  
ATOM   1386  CB  VAL A 185     -58.078 -47.297 -99.495  1.00127.49           C  
ANISOU 1386  CB  VAL A 185    14682  18737  15021   -357  -2606   3274       C  
ATOM   1387  CG1 VAL A 185     -57.889 -47.195 -97.987  1.00125.37           C  
ANISOU 1387  CG1 VAL A 185    14302  18589  14743   -311  -2562   3331       C  
ATOM   1388  CG2 VAL A 185     -59.559 -47.347 -99.837  1.00128.19           C  
ANISOU 1388  CG2 VAL A 185    14716  18905  15084   -398  -2679   3477       C  
ATOM   1389  N   SER A 186     -55.380 -45.393 -99.053  1.00123.56           N  
ANISOU 1389  N   SER A 186    14310  18173  14461   -189  -2269   2837       N  
ATOM   1390  CA  SER A 186     -53.949 -45.325 -98.791  1.00119.28           C  
ANISOU 1390  CA  SER A 186    13809  17555  13956   -162  -2208   2658       C  
ATOM   1391  C   SER A 186     -53.416 -46.635 -98.214  1.00119.36           C  
ANISOU 1391  C   SER A 186    13774  17514  14063   -212  -2333   2668       C  
ATOM   1392  O   SER A 186     -54.014 -47.219 -97.310  1.00121.44           O  
ANISOU 1392  O   SER A 186    13937  17859  14343   -235  -2417   2820       O  
ATOM   1393  CB  SER A 186     -53.617 -44.149 -97.870  1.00117.52           C  
ANISOU 1393  CB  SER A 186    13559  17425  13666    -75  -2068   2618       C  
ATOM   1394  OG  SER A 186     -54.262 -44.277 -96.617  1.00116.63           O  
ANISOU 1394  OG  SER A 186    13334  17446  13532    -54  -2097   2772       O  
ATOM   1395  N   VAL A 187     -52.287 -47.082 -98.757  1.00117.01           N  
ANISOU 1395  N   VAL A 187    13550  17082  13824   -225  -2343   2509       N  
ATOM   1396  CA  VAL A 187     -51.644 -48.333 -98.363  1.00113.75           C  
ANISOU 1396  CA  VAL A 187    13115  16597  13504   -267  -2461   2491       C  
ATOM   1397  C   VAL A 187     -50.768 -48.122 -97.128  1.00109.55           C  
ANISOU 1397  C   VAL A 187    12522  16110  12989   -224  -2402   2437       C  
ATOM   1398  O   VAL A 187     -50.158 -47.064 -96.977  1.00109.54           O  
ANISOU 1398  O   VAL A 187    12542  16130  12947   -164  -2264   2333       O  
ATOM   1399  CB  VAL A 187     -50.770 -48.883 -99.516  1.00115.04           C  
ANISOU 1399  CB  VAL A 187    13392  16599  13717   -283  -2490   2337       C  
ATOM   1400  CG1 VAL A 187     -50.504 -50.373 -99.340  1.00120.34           C  
ANISOU 1400  CG1 VAL A 187    14056  17189  14478   -337  -2657   2360       C  
ATOM   1401  CG2 VAL A 187     -51.436 -48.640-100.861  1.00113.34           C  
ANISOU 1401  CG2 VAL A 187    13268  16336  13459   -298  -2493   2340       C  
ATOM   1402  N   ILE A 188     -50.718 -49.123 -96.248  1.00107.44           N  
ANISOU 1402  N   ILE A 188    12183  15855  12783   -257  -2514   2512       N  
ATOM   1403  CA  ILE A 188     -49.751 -49.148 -95.139  1.00107.77           C  
ANISOU 1403  CA  ILE A 188    12177  15912  12857   -224  -2483   2448       C  
ATOM   1404  C   ILE A 188     -48.415 -49.659 -95.685  1.00104.75           C  
ANISOU 1404  C   ILE A 188    11864  15388  12547   -229  -2493   2270       C  
ATOM   1405  O   ILE A 188     -48.393 -50.371 -96.691  1.00103.69           O  
ANISOU 1405  O   ILE A 188    11797  15150  12448   -267  -2569   2237       O  
ATOM   1406  CB  ILE A 188     -50.215 -50.051 -93.967  1.00111.58           C  
ANISOU 1406  CB  ILE A 188    12555  16464  13375   -257  -2601   2603       C  
ATOM   1407  CG1 ILE A 188     -51.748 -50.066 -93.844  1.00118.81           C  
ANISOU 1407  CG1 ILE A 188    13406  17492  14243   -283  -2652   2816       C  
ATOM   1408  CG2 ILE A 188     -49.579 -49.602 -92.658  1.00108.60           C  
ANISOU 1408  CG2 ILE A 188    12120  16156  12987   -200  -2532   2572       C  
ATOM   1409  CD1 ILE A 188     -52.318 -51.330 -93.219  1.00122.97           C  
ANISOU 1409  CD1 ILE A 188    13850  18043  14829   -353  -2818   2983       C  
ATOM   1410  N   LYS A 189     -47.307 -49.297 -95.039  1.00102.88           N  
ANISOU 1410  N   LYS A 189    11613  15146  12330   -187  -2418   2157       N  
ATOM   1411  CA  LYS A 189     -45.979 -49.676 -95.545  1.00103.68           C  
ANISOU 1411  CA  LYS A 189    11769  15126  12498   -180  -2409   1987       C  
ATOM   1412  C   LYS A 189     -45.055 -50.306 -94.499  1.00105.18           C  
ANISOU 1412  C   LYS A 189    11902  15301  12758   -176  -2456   1950       C  
ATOM   1413  O   LYS A 189     -45.283 -50.156 -93.298  1.00107.60           O  
ANISOU 1413  O   LYS A 189    12131  15698  13052   -165  -2461   2030       O  
ATOM   1414  CB  LYS A 189     -45.292 -48.467 -96.183  1.00102.15           C  
ANISOU 1414  CB  LYS A 189    11635  14912  12265   -132  -2250   1847       C  
ATOM   1415  CG  LYS A 189     -45.913 -47.997 -97.487  1.00 99.10           C  
ANISOU 1415  CG  LYS A 189    11329  14499  11822   -136  -2207   1843       C  
ATOM   1416  CD  LYS A 189     -45.529 -48.889 -98.651  1.00 98.34           C  
ANISOU 1416  CD  LYS A 189    11315  14276  11772   -157  -2273   1768       C  
ATOM   1417  CE  LYS A 189     -46.353 -48.526 -99.868  1.00100.60           C  
ANISOU 1417  CE  LYS A 189    11681  14544  11998   -166  -2255   1792       C  
ATOM   1418  NZ  LYS A 189     -45.936 -49.299-101.065  1.00103.92           N  
ANISOU 1418  NZ  LYS A 189    12199  14835  12449   -172  -2309   1707       N  
ATOM   1419  N   HIS A 190     -44.017 -51.006 -94.963  1.00106.10           N  
ANISOU 1419  N   HIS A 190    12060  15306  12947   -179  -2489   1829       N  
ATOM   1420  CA  HIS A 190     -43.034 -51.619 -94.061  1.00111.42           C  
ANISOU 1420  CA  HIS A 190    12684  15955  13693   -172  -2533   1779       C  
ATOM   1421  C   HIS A 190     -41.606 -51.706 -94.639  1.00111.35           C  
ANISOU 1421  C   HIS A 190    12721  15846  13739   -140  -2481   1601       C  
ATOM   1422  O   HIS A 190     -41.377 -51.354 -95.793  1.00111.36           O  
ANISOU 1422  O   HIS A 190    12796  15794  13721   -123  -2414   1518       O  
ATOM   1423  CB  HIS A 190     -43.524 -52.992 -93.590  1.00117.25           C  
ANISOU 1423  CB  HIS A 190    13389  16678  14483   -223  -2708   1891       C  
ATOM   1424  CG  HIS A 190     -43.507 -54.038 -94.658  1.00123.18           C  
ANISOU 1424  CG  HIS A 190    14218  17310  15274   -253  -2816   1862       C  
ATOM   1425  ND1 HIS A 190     -42.499 -54.971 -94.771  1.00124.98           N  
ANISOU 1425  ND1 HIS A 190    14474  17435  15576   -245  -2883   1764       N  
ATOM   1426  CD2 HIS A 190     -44.375 -54.299 -95.663  1.00128.18           C  
ANISOU 1426  CD2 HIS A 190    14915  17906  15880   -286  -2874   1918       C  
ATOM   1427  CE1 HIS A 190     -42.747 -55.762 -95.798  1.00128.93           C  
ANISOU 1427  CE1 HIS A 190    15059  17838  16088   -265  -2978   1758       C  
ATOM   1428  NE2 HIS A 190     -43.879 -55.376 -96.357  1.00131.61           N  
ANISOU 1428  NE2 HIS A 190    15424  18213  16368   -294  -2978   1850       N  
ATOM   1429  N   THR A 191     -40.663 -52.178 -93.818  1.00110.15           N  
ANISOU 1429  N   THR A 191    12520  15675  13653   -130  -2513   1550       N  
ATOM   1430  CA  THR A 191     -39.229 -52.220 -94.149  1.00107.89           C  
ANISOU 1430  CA  THR A 191    12252  15314  13425    -94  -2458   1393       C  
ATOM   1431  C   THR A 191     -38.730 -53.585 -94.648  1.00109.26           C  
ANISOU 1431  C   THR A 191    12465  15380  13667    -97  -2572   1346       C  
ATOM   1432  O   THR A 191     -37.748 -53.653 -95.391  1.00107.35           O  
ANISOU 1432  O   THR A 191    12264  15068  13454    -59  -2521   1220       O  
ATOM   1433  CB  THR A 191     -38.389 -51.766 -92.932  1.00108.22           C  
ANISOU 1433  CB  THR A 191    12218  15400  13498    -72  -2413   1355       C  
ATOM   1434  OG1 THR A 191     -38.347 -50.336 -92.896  1.00109.24           O  
ANISOU 1434  OG1 THR A 191    12348  15588  13570    -49  -2275   1328       O  
ATOM   1435  CG2 THR A 191     -36.961 -52.299 -92.989  1.00107.26           C  
ANISOU 1435  CG2 THR A 191    12089  15201  13463    -48  -2416   1229       C  
ATOM   1436  N   GLU A 192     -39.406 -54.658 -94.234  1.00111.31           N  
ANISOU 1436  N   GLU A 192    12712  15630  13949   -139  -2726   1451       N  
ATOM   1437  CA  GLU A 192     -39.027 -56.040 -94.577  1.00110.27           C  
ANISOU 1437  CA  GLU A 192    12624  15392  13880   -145  -2861   1420       C  
ATOM   1438  C   GLU A 192     -38.989 -56.307 -96.087  1.00108.08           C  
ANISOU 1438  C   GLU A 192    12461  15019  13583   -123  -2862   1349       C  
ATOM   1439  O   GLU A 192     -39.767 -55.717 -96.837  1.00108.30           O  
ANISOU 1439  O   GLU A 192    12535  15065  13548   -134  -2816   1383       O  
ATOM   1440  CB  GLU A 192     -39.972 -57.031 -93.890  1.00113.11           C  
ANISOU 1440  CB  GLU A 192    12953  15764  14257   -207  -3033   1571       C  
ATOM   1441  CG  GLU A 192     -39.867 -57.042 -92.374  1.00117.56           C  
ANISOU 1441  CG  GLU A 192    13412  16407  14847   -219  -3054   1635       C  
ATOM   1442  CD  GLU A 192     -38.554 -57.625 -91.888  1.00123.79           C  
ANISOU 1442  CD  GLU A 192    14180  17138  15714   -187  -3078   1528       C  
ATOM   1443  OE1 GLU A 192     -38.367 -58.854 -92.001  1.00128.48           O  
ANISOU 1443  OE1 GLU A 192    14806  17647  16361   -200  -3216   1525       O  
ATOM   1444  OE2 GLU A 192     -37.707 -56.854 -91.390  1.00128.46           O  
ANISOU 1444  OE2 GLU A 192    14727  17767  16315   -148  -2965   1448       O  
ATOM   1445  N   PRO A 193     -38.070 -57.187 -96.538  1.00106.87           N  
ANISOU 1445  N   PRO A 193    12359  14765  13482    -85  -2914   1248       N  
ATOM   1446  CA  PRO A 193     -37.987 -57.507 -97.969  1.00107.08           C  
ANISOU 1446  CA  PRO A 193    12506  14696  13483    -50  -2920   1175       C  
ATOM   1447  C   PRO A 193     -39.181 -58.313 -98.480  1.00108.00           C  
ANISOU 1447  C   PRO A 193    12699  14759  13576   -101  -3080   1280       C  
ATOM   1448  O   PRO A 193     -39.665 -59.208 -97.789  1.00106.40           O  
ANISOU 1448  O   PRO A 193    12470  14546  13410   -153  -3235   1379       O  
ATOM   1449  CB  PRO A 193     -36.688 -58.317 -98.085  1.00106.66           C  
ANISOU 1449  CB  PRO A 193    12474  14559  13491     12  -2946   1053       C  
ATOM   1450  CG  PRO A 193     -36.402 -58.811 -96.712  1.00106.07           C  
ANISOU 1450  CG  PRO A 193    12304  14516  13482    -14  -3022   1095       C  
ATOM   1451  CD  PRO A 193     -36.969 -57.795 -95.768  1.00106.04           C  
ANISOU 1451  CD  PRO A 193    12202  14634  13453    -59  -2948   1183       C  
ATOM   1452  N   VAL A 194     -39.650 -57.971 -99.680  1.00112.29           N  
ANISOU 1452  N   VAL A 194    13336  15268  14059    -90  -3044   1264       N  
ATOM   1453  CA  VAL A 194     -40.761 -58.667-100.340  1.00115.75           C  
ANISOU 1453  CA  VAL A 194    13862  15643  14471   -137  -3195   1356       C  
ATOM   1454  C   VAL A 194     -40.173 -59.710-101.300  1.00121.28           C  
ANISOU 1454  C   VAL A 194    14696  16199  15185    -82  -3289   1256       C  
ATOM   1455  O   VAL A 194     -39.939 -59.411-102.475  1.00122.46           O  
ANISOU 1455  O   VAL A 194    14945  16296  15286    -26  -3217   1167       O  
ATOM   1456  CB  VAL A 194     -41.693 -57.675-101.082  1.00111.67           C  
ANISOU 1456  CB  VAL A 194    13378  15174  13876   -155  -3111   1403       C  
ATOM   1457  CG1 VAL A 194     -42.865 -58.401-101.724  1.00112.66           C  
ANISOU 1457  CG1 VAL A 194    13588  15234  13981   -211  -3279   1508       C  
ATOM   1458  CG2 VAL A 194     -42.211 -56.611-100.127  1.00108.83           C  
ANISOU 1458  CG2 VAL A 194    12895  14958  13495   -190  -3012   1492       C  
ATOM   1459  N   PRO A 195     -39.953 -60.947-100.801  1.00125.09           N  
ANISOU 1459  N   PRO A 195    15186  16613  15728    -95  -3454   1274       N  
ATOM   1460  CA  PRO A 195     -39.050 -61.940-101.401  1.00127.48           C  
ANISOU 1460  CA  PRO A 195    15595  16788  16053    -20  -3527   1157       C  
ATOM   1461  C   PRO A 195     -39.325 -62.306-102.858  1.00129.93           C  
ANISOU 1461  C   PRO A 195    16077  16983  16307     19  -3584   1110       C  
ATOM   1462  O   PRO A 195     -38.385 -62.633-103.582  1.00132.05           O  
ANISOU 1462  O   PRO A 195    16433  17173  16565    119  -3553    976       O  
ATOM   1463  CB  PRO A 195     -39.222 -63.167-100.494  1.00127.04           C  
ANISOU 1463  CB  PRO A 195    15514  16689  16064    -74  -3730   1237       C  
ATOM   1464  CG  PRO A 195     -39.736 -62.619 -99.207  1.00125.93           C  
ANISOU 1464  CG  PRO A 195    15218  16682  15946   -151  -3697   1358       C  
ATOM   1465  CD  PRO A 195     -40.658 -61.517 -99.640  1.00126.28           C  
ANISOU 1465  CD  PRO A 195    15250  16804  15923   -184  -3594   1422       C  
ATOM   1466  N   ASP A 196     -40.586 -62.255-103.278  1.00131.15           N  
ANISOU 1466  N   ASP A 196    16278  17130  16423    -50  -3667   1221       N  
ATOM   1467  CA  ASP A 196     -40.955 -62.566-104.660  1.00135.91           C  
ANISOU 1467  CA  ASP A 196    17052  17621  16967    -18  -3733   1187       C  
ATOM   1468  C   ASP A 196     -40.405 -61.510-105.638  1.00137.25           C  
ANISOU 1468  C   ASP A 196    17265  17814  17070     68  -3520   1065       C  
ATOM   1469  O   ASP A 196     -40.753 -60.330-105.527  1.00137.93           O  
ANISOU 1469  O   ASP A 196    17272  18008  17126     40  -3373   1098       O  
ATOM   1470  CB  ASP A 196     -42.482 -62.691-104.778  1.00137.08           C  
ANISOU 1470  CB  ASP A 196    17219  17766  17096   -127  -3873   1352       C  
ATOM   1471  CG  ASP A 196     -42.946 -63.098-106.173  1.00140.23           C  
ANISOU 1471  CG  ASP A 196    17805  18037  17437   -103  -3973   1327       C  
ATOM   1472  OD1 ASP A 196     -42.164 -63.710-106.936  1.00140.18           O  
ANISOU 1472  OD1 ASP A 196    17933  17913  17413     -8  -4004   1199       O  
ATOM   1473  OD2 ASP A 196     -44.116 -62.808-106.502  1.00142.62           O  
ANISOU 1473  OD2 ASP A 196    18122  18356  17708   -177  -4024   1440       O  
ATOM   1474  N   PRO A 197     -39.532 -61.928-106.586  1.00137.51           N  
ANISOU 1474  N   PRO A 197    17424  17748  17076    180  -3502    926       N  
ATOM   1475  CA  PRO A 197     -39.008 -60.998-107.594  1.00138.10           C  
ANISOU 1475  CA  PRO A 197    17546  17839  17083    266  -3307    817       C  
ATOM   1476  C   PRO A 197     -40.062 -60.574-108.615  1.00140.99           C  
ANISOU 1476  C   PRO A 197    18017  18180  17373    239  -3320    864       C  
ATOM   1477  O   PRO A 197     -39.909 -59.534-109.258  1.00140.04           O  
ANISOU 1477  O   PRO A 197    17902  18108  17196    277  -3144    812       O  
ATOM   1478  CB  PRO A 197     -37.901 -61.806-108.288  1.00136.18           C  
ANISOU 1478  CB  PRO A 197    17419  17489  16831    396  -3323    677       C  
ATOM   1479  CG  PRO A 197     -37.592 -62.933-107.365  1.00136.39           C  
ANISOU 1479  CG  PRO A 197    17413  17473  16935    380  -3481    697       C  
ATOM   1480  CD  PRO A 197     -38.899 -63.252-106.703  1.00137.80           C  
ANISOU 1480  CD  PRO A 197    17555  17659  17141    241  -3651    861       C  
ATOM   1481  N   ARG A 198     -41.119 -61.376-108.751  1.00145.29           N  
ANISOU 1481  N   ARG A 198    18638  18646  17916    169  -3532    966       N  
ATOM   1482  CA  ARG A 198     -42.207 -61.113-109.700  1.00146.10           C  
ANISOU 1482  CA  ARG A 198    18845  18712  17953    133  -3580   1024       C  
ATOM   1483  C   ARG A 198     -43.274 -60.152-109.165  1.00141.72           C  
ANISOU 1483  C   ARG A 198    18167  18284  17396     26  -3526   1161       C  
ATOM   1484  O   ARG A 198     -43.839 -59.367-109.930  1.00138.98           O  
ANISOU 1484  O   ARG A 198    17865  17957  16984     23  -3451   1171       O  
ATOM   1485  CB  ARG A 198     -42.876 -62.426-110.118  1.00151.27           C  
ANISOU 1485  CB  ARG A 198    19644  19218  18611    102  -3850   1080       C  
ATOM   1486  CG  ARG A 198     -42.102 -63.238-111.141  1.00157.31           C  
ANISOU 1486  CG  ARG A 198    20600  19834  19335    228  -3908    941       C  
ATOM   1487  CD  ARG A 198     -42.731 -64.611-111.325  1.00163.26           C  
ANISOU 1487  CD  ARG A 198    21488  20436  20105    187  -4201   1005       C  
ATOM   1488  NE  ARG A 198     -42.162 -65.333-112.462  1.00169.18           N  
ANISOU 1488  NE  ARG A 198    22454  21033  20795    315  -4268    876       N  
ATOM   1489  CZ  ARG A 198     -41.060 -66.081-112.416  1.00171.26           C  
ANISOU 1489  CZ  ARG A 198    22769  21230  21069    424  -4285    762       C  
ATOM   1490  NH1 ARG A 198     -40.380 -66.218-111.283  1.00170.75           N  
ANISOU 1490  NH1 ARG A 198    22555  21237  21082    414  -4243    758       N  
ATOM   1491  NH2 ARG A 198     -40.633 -66.694-113.512  1.00173.73           N  
ANISOU 1491  NH2 ARG A 198    23290  21405  21312    552  -4345    651       N  
ATOM   1492  N   ALA A 199     -43.534 -60.228-107.857  1.00137.78           N  
ANISOU 1492  N   ALA A 199    17516  17870  16961    -53  -3565   1264       N  
ATOM   1493  CA  ALA A 199     -44.650 -59.537-107.194  1.00131.74           C  
ANISOU 1493  CA  ALA A 199    16631  17226  16198   -154  -3552   1419       C  
ATOM   1494  C   ALA A 199     -44.958 -58.146-107.738  1.00129.88           C  
ANISOU 1494  C   ALA A 199    16383  17072  15891   -139  -3365   1405       C  
ATOM   1495  O   ALA A 199     -44.063 -57.311-107.878  1.00127.88           O  
ANISOU 1495  O   ALA A 199    16108  16863  15617    -68  -3171   1289       O  
ATOM   1496  CB  ALA A 199     -44.418 -59.479-105.692  1.00129.86           C  
ANISOU 1496  CB  ALA A 199    16221  17095  16025   -194  -3527   1478       C  
ATOM   1497  N   VAL A 200     -46.237 -57.919-108.039  1.00130.14           N  
ANISOU 1497  N   VAL A 200    16430  17124  15892   -209  -3432   1529       N  
ATOM   1498  CA  VAL A 200     -46.722 -56.651-108.604  1.00127.45           C  
ANISOU 1498  CA  VAL A 200    16090  16855  15480   -203  -3280   1534       C  
ATOM   1499  C   VAL A 200     -46.662 -55.508-107.589  1.00123.32           C  
ANISOU 1499  C   VAL A 200    15404  16491  14959   -214  -3110   1566       C  
ATOM   1500  O   VAL A 200     -46.566 -55.745-106.383  1.00124.17           O  
ANISOU 1500  O   VAL A 200    15392  16665  15122   -248  -3138   1626       O  
ATOM   1501  CB  VAL A 200     -48.158 -56.774-109.182  1.00127.53           C  
ANISOU 1501  CB  VAL A 200    16156  16841  15458   -276  -3414   1669       C  
ATOM   1502  CG1 VAL A 200     -48.162 -57.615-110.450  1.00127.62           C  
ANISOU 1502  CG1 VAL A 200    16362  16684  15442   -245  -3549   1608       C  
ATOM   1503  CG2 VAL A 200     -49.126 -57.341-108.150  1.00127.08           C  
ANISOU 1503  CG2 VAL A 200    15987  16839  15458   -383  -3572   1858       C  
ATOM   1504  N   ASN A 201     -46.733 -54.278-108.090  1.00117.33           N  
ANISOU 1504  N   ASN A 201    14652  15791  14136   -184  -2940   1527       N  
ATOM   1505  CA  ASN A 201     -46.549 -53.076-107.278  1.00115.96           C  
ANISOU 1505  CA  ASN A 201    14353  15753  13951   -178  -2765   1531       C  
ATOM   1506  C   ASN A 201     -47.306 -53.025-105.948  1.00116.95           C  
ANISOU 1506  C   ASN A 201    14334  15994  14106   -245  -2815   1685       C  
ATOM   1507  O   ASN A 201     -46.759 -52.562-104.937  1.00115.23           O  
ANISOU 1507  O   ASN A 201    14010  15859  13910   -230  -2722   1669       O  
ATOM   1508  CB  ASN A 201     -46.870 -51.835-108.106  1.00116.91           C  
ANISOU 1508  CB  ASN A 201    14519  15910  13991   -153  -2619   1503       C  
ATOM   1509  CG  ASN A 201     -45.889 -51.621-109.240  1.00119.42           C  
ANISOU 1509  CG  ASN A 201    14951  16145  14275    -73  -2514   1339       C  
ATOM   1510  OD1 ASN A 201     -44.761 -52.121-109.211  1.00117.95           O  
ANISOU 1510  OD1 ASN A 201    14779  15907  14127    -22  -2498   1233       O  
ATOM   1511  ND2 ASN A 201     -46.313 -50.867-110.249  1.00123.24           N  
ANISOU 1511  ND2 ASN A 201    15516  16621  14685    -56  -2439   1322       N  
ATOM   1512  N   GLN A 202     -48.552 -53.500-105.955  1.00116.77           N  
ANISOU 1512  N   GLN A 202    14307  15976  14082   -315  -2962   1838       N  
ATOM   1513  CA  GLN A 202     -49.405 -53.495-104.762  1.00115.49           C  
ANISOU 1513  CA  GLN A 202    14006  15932  13940   -377  -3015   2008       C  
ATOM   1514  C   GLN A 202     -48.822 -54.366-103.661  1.00115.15           C  
ANISOU 1514  C   GLN A 202    13887  15888  13974   -392  -3095   2019       C  
ATOM   1515  O   GLN A 202     -48.933 -54.039-102.478  1.00114.24           O  
ANISOU 1515  O   GLN A 202    13645  15887  13871   -403  -3055   2092       O  
ATOM   1516  CB  GLN A 202     -50.824 -53.962-105.095  1.00115.81           C  
ANISOU 1516  CB  GLN A 202    14060  15968  13973   -454  -3174   2177       C  
ATOM   1517  CG  GLN A 202     -51.610 -53.011-105.982  1.00117.79           C  
ANISOU 1517  CG  GLN A 202    14358  16247  14146   -448  -3097   2200       C  
ATOM   1518  CD  GLN A 202     -51.368 -53.234-107.464  1.00120.60           C  
ANISOU 1518  CD  GLN A 202    14886  16461  14473   -420  -3124   2088       C  
ATOM   1519  OE1 GLN A 202     -50.236 -53.451-107.902  1.00120.63           O  
ANISOU 1519  OE1 GLN A 202    14971  16377  14485   -360  -3077   1928       O  
ATOM   1520  NE2 GLN A 202     -52.439 -53.174-108.248  1.00124.60           N  
ANISOU 1520  NE2 GLN A 202    15450  16948  14943   -460  -3197   2176       N  
ATOM   1521  N   ASP A 203     -48.200 -55.471-104.067  1.00116.52           N  
ANISOU 1521  N   ASP A 203    14145  15931  14194   -384  -3211   1946       N  
ATOM   1522  CA  ASP A 203     -47.554 -56.398-103.141  1.00118.94           C  
ANISOU 1522  CA  ASP A 203    14398  16216  14575   -393  -3299   1941       C  
ATOM   1523  C   ASP A 203     -46.223 -55.847-102.622  1.00118.34           C  
ANISOU 1523  C   ASP A 203    14275  16173  14514   -321  -3136   1798       C  
ATOM   1524  O   ASP A 203     -45.743 -56.270-101.565  1.00121.45           O  
ANISOU 1524  O   ASP A 203    14586  16595  14964   -327  -3167   1808       O  
ATOM   1525  CB  ASP A 203     -47.340 -57.767-103.803  1.00122.63           C  
ANISOU 1525  CB  ASP A 203    14987  16524  15082   -402  -3484   1905       C  
ATOM   1526  CG  ASP A 203     -48.646 -58.443-104.208  1.00124.14           C  
ANISOU 1526  CG  ASP A 203    15221  16671  15273   -487  -3679   2061       C  
ATOM   1527  OD1 ASP A 203     -49.642 -58.336-103.460  1.00124.81           O  
ANISOU 1527  OD1 ASP A 203    15194  16858  15366   -560  -3727   2235       O  
ATOM   1528  OD2 ASP A 203     -48.670 -59.095-105.274  1.00124.81           O  
ANISOU 1528  OD2 ASP A 203    15453  16619  15348   -479  -3789   2013       O  
ATOM   1529  N   LYS A 204     -45.637 -54.907-103.368  1.00114.03           N  
ANISOU 1529  N   LYS A 204    13781  15623  13921   -257  -2969   1671       N  
ATOM   1530  CA  LYS A 204     -44.376 -54.261-102.990  1.00108.02           C  
ANISOU 1530  CA  LYS A 204    12976  14894  13172   -193  -2808   1539       C  
ATOM   1531  C   LYS A 204     -44.591 -53.274-101.845  1.00105.54           C  
ANISOU 1531  C   LYS A 204    12534  14721  12846   -205  -2705   1603       C  
ATOM   1532  O   LYS A 204     -44.523 -52.061-102.039  1.00105.62           O  
ANISOU 1532  O   LYS A 204    12536  14788  12803   -176  -2549   1564       O  
ATOM   1533  CB  LYS A 204     -43.752 -53.548-104.193  1.00104.79           C  
ANISOU 1533  CB  LYS A 204    12662  14439  12714   -126  -2666   1400       C  
ATOM   1534  CG  LYS A 204     -43.210 -54.471-105.268  1.00103.36           C  
ANISOU 1534  CG  LYS A 204    12613  14119  12540    -82  -2738   1303       C  
ATOM   1535  CD  LYS A 204     -42.636 -53.661-106.413  1.00104.07           C  
ANISOU 1535  CD  LYS A 204    12785  14183  12573    -13  -2580   1179       C  
ATOM   1536  CE  LYS A 204     -42.386 -54.528-107.633  1.00107.09           C  
ANISOU 1536  CE  LYS A 204    13321  14430  12938     37  -2660   1103       C  
ATOM   1537  NZ  LYS A 204     -42.127 -53.709-108.850  1.00108.68           N  
ANISOU 1537  NZ  LYS A 204    13613  14613  13067     97  -2517   1013       N  
ATOM   1538  N   LYS A 205     -44.834 -53.807-100.651  1.00103.80           N  
ANISOU 1538  N   LYS A 205    12218  14551  12670   -245  -2795   1702       N  
ATOM   1539  CA  LYS A 205     -45.236 -52.999 -99.503  1.00105.45           C  
ANISOU 1539  CA  LYS A 205    12311  14896  12857   -254  -2725   1789       C  
ATOM   1540  C   LYS A 205     -44.058 -52.364 -98.761  1.00106.04           C  
ANISOU 1540  C   LYS A 205    12330  15008  12952   -205  -2598   1681       C  
ATOM   1541  O   LYS A 205     -44.227 -51.785 -97.681  1.00107.98           O  
ANISOU 1541  O   LYS A 205    12487  15355  13184   -203  -2551   1740       O  
ATOM   1542  CB  LYS A 205     -46.103 -53.830 -98.552  1.00109.29           C  
ANISOU 1542  CB  LYS A 205    12719  15431  13375   -317  -2878   1959       C  
ATOM   1543  CG  LYS A 205     -47.505 -54.084 -99.079  1.00116.33           C  
ANISOU 1543  CG  LYS A 205    13632  16332  14234   -375  -2979   2107       C  
ATOM   1544  CD  LYS A 205     -48.268 -55.102 -98.244  1.00121.33           C  
ANISOU 1544  CD  LYS A 205    14190  16995  14912   -446  -3152   2278       C  
ATOM   1545  CE  LYS A 205     -49.637 -55.376 -98.858  1.00122.40           C  
ANISOU 1545  CE  LYS A 205    14347  17133  15024   -510  -3263   2430       C  
ATOM   1546  NZ  LYS A 205     -50.354 -56.494 -98.185  1.00123.80           N  
ANISOU 1546  NZ  LYS A 205    14459  17322  15255   -590  -3453   2603       N  
ATOM   1547  N   ASN A 206     -42.869 -52.474 -99.344  1.00104.71           N  
ANISOU 1547  N   ASN A 206    12215  14756  12814   -160  -2545   1528       N  
ATOM   1548  CA  ASN A 206     -41.673 -51.853 -98.782  1.00101.88           C  
ANISOU 1548  CA  ASN A 206    11807  14421  12482   -117  -2426   1421       C  
ATOM   1549  C   ASN A 206     -41.117 -50.791 -99.722  1.00101.17           C  
ANISOU 1549  C   ASN A 206    11772  14317  12349    -72  -2265   1308       C  
ATOM   1550  O   ASN A 206     -40.000 -50.294 -99.534  1.00101.77           O  
ANISOU 1550  O   ASN A 206    11822  14394  12452    -37  -2164   1205       O  
ATOM   1551  CB  ASN A 206     -40.612 -52.911 -98.443  1.00100.51           C  
ANISOU 1551  CB  ASN A 206    11620  14176  12392   -102  -2501   1349       C  
ATOM   1552  CG  ASN A 206     -40.101 -53.657 -99.666  1.00101.08           C  
ANISOU 1552  CG  ASN A 206    11797  14128  12480    -71  -2537   1254       C  
ATOM   1553  OD1 ASN A 206     -40.401 -53.304-100.812  1.00100.41           O  
ANISOU 1553  OD1 ASN A 206    11797  14010  12342    -56  -2490   1225       O  
ATOM   1554  ND2 ASN A 206     -39.314 -54.700 -99.423  1.00100.71           N  
ANISOU 1554  ND2 ASN A 206    11749  14014  12501    -54  -2623   1202       N  
ATOM   1555  N   MET A 207     -41.923 -50.442-100.722  1.00 99.04           N  
ANISOU 1555  N   MET A 207    11577  14037  12016    -79  -2246   1335       N  
ATOM   1556  CA  MET A 207     -41.493 -49.569-101.806  1.00 97.92           C  
ANISOU 1556  CA  MET A 207    11505  13869  11830    -40  -2109   1235       C  
ATOM   1557  C   MET A 207     -42.282 -48.260-101.874  1.00 97.39           C  
ANISOU 1557  C   MET A 207    11436  13884  11684    -46  -2008   1286       C  
ATOM   1558  O   MET A 207     -43.483 -48.233-101.595  1.00100.42           O  
ANISOU 1558  O   MET A 207    11801  14321  12029    -80  -2068   1411       O  
ATOM   1559  CB  MET A 207     -41.631 -50.313-103.129  1.00 97.39           C  
ANISOU 1559  CB  MET A 207    11552  13699  11750    -29  -2171   1199       C  
ATOM   1560  CG  MET A 207     -40.464 -50.107-104.067  1.00 96.54           C  
ANISOU 1560  CG  MET A 207    11507  13529  11646     32  -2063   1052       C  
ATOM   1561  SD  MET A 207     -39.008 -50.965-103.457  1.00 93.55           S  
ANISOU 1561  SD  MET A 207    11074  13108  11361     69  -2090    961       S  
ATOM   1562  CE  MET A 207     -37.756 -50.184-104.465  1.00 94.76           C  
ANISOU 1562  CE  MET A 207    11265  13237  11500    141  -1907    814       C  
ATOM   1563  N   LEU A 208     -41.599 -47.177-102.241  1.00 94.16           N  
ANISOU 1563  N   LEU A 208    11043  13484  11249    -13  -1857   1194       N  
ATOM   1564  CA  LEU A 208     -42.253 -45.897-102.501  1.00 91.83           C  
ANISOU 1564  CA  LEU A 208    10768  13248  10873    -11  -1756   1223       C  
ATOM   1565  C   LEU A 208     -42.087 -45.560-103.971  1.00 93.80           C  
ANISOU 1565  C   LEU A 208    11121  13436  11083     11  -1681   1146       C  
ATOM   1566  O   LEU A 208     -40.965 -45.549-104.489  1.00 92.44           O  
ANISOU 1566  O   LEU A 208    10972  13211  10939     43  -1611   1034       O  
ATOM   1567  CB  LEU A 208     -41.665 -44.779-101.640  1.00 88.39           C  
ANISOU 1567  CB  LEU A 208    10271  12877  10433      5  -1647   1191       C  
ATOM   1568  CG  LEU A 208     -41.875 -44.768-100.128  1.00 86.08           C  
ANISOU 1568  CG  LEU A 208     9886  12664  10157     -4  -1693   1267       C  
ATOM   1569  CD1 LEU A 208     -40.910 -43.777 -99.504  1.00 86.11           C  
ANISOU 1569  CD1 LEU A 208     9855  12692  10171     18  -1589   1193       C  
ATOM   1570  CD2 LEU A 208     -43.300 -44.429 -99.740  1.00 85.17           C  
ANISOU 1570  CD2 LEU A 208     9757  12633   9970    -15  -1725   1403       C  
ATOM   1571  N   PHE A 209     -43.207 -45.281-104.636  1.00 96.77           N  
ANISOU 1571  N   PHE A 209    11555  13821  11390     -2  -1693   1212       N  
ATOM   1572  CA  PHE A 209     -43.214 -45.106-106.086  1.00 98.74           C  
ANISOU 1572  CA  PHE A 209    11916  14004  11595     18  -1645   1152       C  
ATOM   1573  C   PHE A 209     -43.188 -43.657-106.528  1.00 97.90           C  
ANISOU 1573  C   PHE A 209    11839  13935  11423     36  -1492   1116       C  
ATOM   1574  O   PHE A 209     -43.932 -42.823-106.006  1.00 95.76           O  
ANISOU 1574  O   PHE A 209    11536  13742  11105     23  -1463   1188       O  
ATOM   1575  CB  PHE A 209     -44.394 -45.846-106.712  1.00100.49           C  
ANISOU 1575  CB  PHE A 209    12201  14190  11789     -9  -1772   1239       C  
ATOM   1576  CG  PHE A 209     -44.315 -47.333-106.547  1.00102.73           C  
ANISOU 1576  CG  PHE A 209    12486  14409  12136    -26  -1930   1258       C  
ATOM   1577  CD1 PHE A 209     -43.354 -48.071-107.232  1.00103.38           C  
ANISOU 1577  CD1 PHE A 209    12634  14394  12252     13  -1943   1149       C  
ATOM   1578  CD2 PHE A 209     -45.184 -47.994-105.691  1.00104.90           C  
ANISOU 1578  CD2 PHE A 209    12697  14723  12436    -76  -2066   1388       C  
ATOM   1579  CE1 PHE A 209     -43.264 -49.443-107.071  1.00105.23           C  
ANISOU 1579  CE1 PHE A 209    12879  14560  12541      3  -2096   1163       C  
ATOM   1580  CE2 PHE A 209     -45.104 -49.369-105.527  1.00107.90           C  
ANISOU 1580  CE2 PHE A 209    13083  15037  12877    -96  -2222   1409       C  
ATOM   1581  CZ  PHE A 209     -44.143 -50.094-106.219  1.00108.37           C  
ANISOU 1581  CZ  PHE A 209    13217  14990  12968    -56  -2240   1293       C  
ATOM   1582  N   SER A 210     -42.321 -43.376-107.499  1.00 99.02           N  
ANISOU 1582  N   SER A 210    12042  14021  11559     70  -1396   1007       N  
ATOM   1583  CA  SER A 210     -42.151 -42.027-108.023  1.00100.29           C  
ANISOU 1583  CA  SER A 210    12237  14204  11662     85  -1249    964       C  
ATOM   1584  C   SER A 210     -43.462 -41.526-108.599  1.00 97.85           C  
ANISOU 1584  C   SER A 210    11993  13915  11269     71  -1257   1037       C  
ATOM   1585  O   SER A 210     -44.091 -42.213-109.404  1.00 96.68           O  
ANISOU 1585  O   SER A 210    11916  13716  11099     68  -1335   1063       O  
ATOM   1586  CB  SER A 210     -41.070 -41.994-109.099  1.00103.56           C  
ANISOU 1586  CB  SER A 210    12711  14552  12083    124  -1156    849       C  
ATOM   1587  OG  SER A 210     -40.766 -40.658-109.465  1.00106.91           O  
ANISOU 1587  OG  SER A 210    13153  15002  12464    131  -1012    810       O  
ATOM   1588  N   GLY A 211     -43.864 -40.335-108.166  1.00 94.66           N  
ANISOU 1588  N   GLY A 211    11566  13582  10815     66  -1183   1072       N  
ATOM   1589  CA  GLY A 211     -45.141 -39.760-108.551  1.00 92.68           C  
ANISOU 1589  CA  GLY A 211    11362  13367  10483     58  -1186   1151       C  
ATOM   1590  C   GLY A 211     -46.260 -39.920-107.532  1.00 91.65           C  
ANISOU 1590  C   GLY A 211    11162  13318  10341     37  -1277   1284       C  
ATOM   1591  O   GLY A 211     -47.309 -39.294-107.678  1.00 94.61           O  
ANISOU 1591  O   GLY A 211    11558  13742  10646     37  -1268   1359       O  
ATOM   1592  N   THR A 212     -46.055 -40.741-106.502  1.00 89.12           N  
ANISOU 1592  N   THR A 212    10756  13017  10085     23  -1362   1319       N  
ATOM   1593  CA  THR A 212     -47.099 -40.965-105.486  1.00 90.40           C  
ANISOU 1593  CA  THR A 212    10843  13265  10238      6  -1449   1457       C  
ATOM   1594  C   THR A 212     -46.985 -40.029-104.262  1.00 88.25           C  
ANISOU 1594  C   THR A 212    10501  13085   9944     31  -1383   1477       C  
ATOM   1595  O   THR A 212     -45.967 -39.366-104.079  1.00 88.22           O  
ANISOU 1595  O   THR A 212    10500  13067   9953     50  -1291   1380       O  
ATOM   1596  CB  THR A 212     -47.196 -42.457-105.060  1.00 94.11           C  
ANISOU 1596  CB  THR A 212    11265  13709  10781    -26  -1601   1512       C  
ATOM   1597  OG1 THR A 212     -46.053 -42.839-104.283  1.00 96.83           O  
ANISOU 1597  OG1 THR A 212    11553  14039  11198    -19  -1598   1444       O  
ATOM   1598  CG2 THR A 212     -47.292 -43.368-106.280  1.00 95.28           C  
ANISOU 1598  CG2 THR A 212    11501  13754  10943    -43  -1677   1487       C  
ATOM   1599  N   ASN A 213     -48.034 -39.971-103.440  1.00 87.41           N  
ANISOU 1599  N   ASN A 213    10337  13072   9802     32  -1433   1606       N  
ATOM   1600  CA  ASN A 213     -48.086 -39.064-102.283  1.00 87.72           C  
ANISOU 1600  CA  ASN A 213    10324  13203   9801     70  -1377   1636       C  
ATOM   1601  C   ASN A 213     -47.944 -39.743-100.938  1.00 88.29           C  
ANISOU 1601  C   ASN A 213    10299  13323   9922     68  -1452   1693       C  
ATOM   1602  O   ASN A 213     -48.203 -40.935-100.805  1.00 93.73           O  
ANISOU 1602  O   ASN A 213    10946  14001  10666     32  -1565   1755       O  
ATOM   1603  CB  ASN A 213     -49.396 -38.288-102.262  1.00 89.93           C  
ANISOU 1603  CB  ASN A 213    10613  13573   9984     97  -1356   1745       C  
ATOM   1604  CG  ASN A 213     -49.573 -37.412-103.483  1.00 95.63           C  
ANISOU 1604  CG  ASN A 213    11433  14255  10643    107  -1272   1691       C  
ATOM   1605  OD1 ASN A 213     -48.703 -37.343-104.365  1.00 96.99           O  
ANISOU 1605  OD1 ASN A 213    11670  14337  10843     94  -1221   1573       O  
ATOM   1606  ND2 ASN A 213     -50.712 -36.733-103.548  1.00 99.93           N  
ANISOU 1606  ND2 ASN A 213    11990  14875  11103    133  -1253   1782       N  
ATOM   1607  N   ILE A 214     -47.546 -38.969 -99.936  1.00 85.14           N  
ANISOU 1607  N   ILE A 214     9871  12976   9502    108  -1395   1673       N  
ATOM   1608  CA  ILE A 214     -47.497 -39.454 -98.566  1.00 82.59           C  
ANISOU 1608  CA  ILE A 214     9459  12712   9208    117  -1458   1735       C  
ATOM   1609  C   ILE A 214     -48.723 -38.886 -97.851  1.00 84.85           C  
ANISOU 1609  C   ILE A 214     9714  13123   9402    163  -1454   1871       C  
ATOM   1610  O   ILE A 214     -48.770 -37.689 -97.537  1.00 86.42           O  
ANISOU 1610  O   ILE A 214     9945  13364   9524    219  -1370   1852       O  
ATOM   1611  CB  ILE A 214     -46.184 -39.035 -97.852  1.00 79.33           C  
ANISOU 1611  CB  ILE A 214     9037  12270   8834    136  -1408   1624       C  
ATOM   1612  CG1 ILE A 214     -44.943 -39.479 -98.655  1.00 76.94           C  
ANISOU 1612  CG1 ILE A 214     8762  11853   8617    101  -1393   1491       C  
ATOM   1613  CG2 ILE A 214     -46.168 -39.503 -96.393  1.00 78.08           C  
ANISOU 1613  CG2 ILE A 214     8794  12174   8697    152  -1474   1690       C  
ATOM   1614  CD1 ILE A 214     -44.797 -40.969 -98.891  1.00 75.52           C  
ANISOU 1614  CD1 ILE A 214     8551  11621   8520     59  -1499   1502       C  
ATOM   1615  N   ALA A 215     -49.715 -39.745 -97.615  1.00 84.65           N  
ANISOU 1615  N   ALA A 215     9627  13155   9380    142  -1550   2012       N  
ATOM   1616  CA  ALA A 215     -50.967 -39.329 -96.978  1.00 85.03           C  
ANISOU 1616  CA  ALA A 215     9631  13335   9342    188  -1550   2163       C  
ATOM   1617  C   ALA A 215     -50.840 -39.057 -95.472  1.00 85.91           C  
ANISOU 1617  C   ALA A 215     9682  13533   9425    247  -1542   2204       C  
ATOM   1618  O   ALA A 215     -51.588 -38.245 -94.924  1.00 87.53           O  
ANISOU 1618  O   ALA A 215     9881  13843   9533    318  -1495   2282       O  
ATOM   1619  CB  ALA A 215     -52.066 -40.335 -97.257  1.00 86.17           C  
ANISOU 1619  CB  ALA A 215     9720  13513   9505    138  -1659   2313       C  
ATOM   1620  N   ALA A 216     -49.910 -39.743 -94.809  1.00 86.19           N  
ANISOU 1620  N   ALA A 216     9680  13527   9540    225  -1588   2152       N  
ATOM   1621  CA  ALA A 216     -49.537 -39.428 -93.422  1.00 88.24           C  
ANISOU 1621  CA  ALA A 216     9902  13846   9778    282  -1576   2157       C  
ATOM   1622  C   ALA A 216     -48.278 -40.183 -93.002  1.00 90.19           C  
ANISOU 1622  C   ALA A 216    10124  14011  10131    243  -1623   2062       C  
ATOM   1623  O   ALA A 216     -47.973 -41.248 -93.557  1.00 90.95           O  
ANISOU 1623  O   ALA A 216    10205  14034  10317    175  -1693   2042       O  
ATOM   1624  CB  ALA A 216     -50.681 -39.717 -92.459  1.00 88.41           C  
ANISOU 1624  CB  ALA A 216     9840  14006   9746    321  -1623   2340       C  
ATOM   1625  N   GLY A 217     -47.555 -39.620 -92.030  1.00 90.52           N  
ANISOU 1625  N   GLY A 217    10170  14063  10161    292  -1589   2003       N  
ATOM   1626  CA  GLY A 217     -46.317 -40.218 -91.513  1.00 89.95           C  
ANISOU 1626  CA  GLY A 217    10071  13919  10185    263  -1630   1912       C  
ATOM   1627  C   GLY A 217     -45.023 -39.695 -92.125  1.00 89.82           C  
ANISOU 1627  C   GLY A 217    10116  13793  10219    244  -1567   1742       C  
ATOM   1628  O   GLY A 217     -45.018 -38.688 -92.842  1.00 90.03           O  
ANISOU 1628  O   GLY A 217    10213  13799  10195    259  -1483   1686       O  
ATOM   1629  N   LYS A 218     -43.922 -40.390 -91.844  1.00 89.30           N  
ANISOU 1629  N   LYS A 218    10016  13658  10252    210  -1610   1665       N  
ATOM   1630  CA  LYS A 218     -42.590 -39.981 -92.312  1.00 88.64           C  
ANISOU 1630  CA  LYS A 218     9970  13478  10228    192  -1556   1513       C  
ATOM   1631  C   LYS A 218     -41.637 -41.182 -92.481  1.00 88.62           C  
ANISOU 1631  C   LYS A 218     9924  13397  10349    141  -1619   1452       C  
ATOM   1632  O   LYS A 218     -41.462 -41.992 -91.561  1.00 88.58           O  
ANISOU 1632  O   LYS A 218     9858  13407  10390    137  -1699   1488       O  
ATOM   1633  CB  LYS A 218     -41.992 -38.944 -91.351  1.00 86.82           C  
ANISOU 1633  CB  LYS A 218     9759  13262   9967    238  -1515   1465       C  
ATOM   1634  CG  LYS A 218     -40.632 -38.399 -91.740  1.00 85.05           C  
ANISOU 1634  CG  LYS A 218     9563  12946   9803    215  -1461   1325       C  
ATOM   1635  CD  LYS A 218     -39.941 -37.813 -90.523  1.00 85.07           C  
ANISOU 1635  CD  LYS A 218     9563  12953   9805    247  -1472   1291       C  
ATOM   1636  CE  LYS A 218     -38.999 -36.689 -90.920  1.00 86.27           C  
ANISOU 1636  CE  LYS A 218     9771  13039   9967    238  -1399   1183       C  
ATOM   1637  NZ  LYS A 218     -38.528 -35.903 -89.744  1.00 87.46           N  
ANISOU 1637  NZ  LYS A 218     9942  13194  10093    276  -1415   1162       N  
ATOM   1638  N   ALA A 219     -41.022 -41.286 -93.656  1.00 86.30           N  
ANISOU 1638  N   ALA A 219     9666  13022  10102    110  -1580   1361       N  
ATOM   1639  CA  ALA A 219     -40.116 -42.392 -93.935  1.00 85.12           C  
ANISOU 1639  CA  ALA A 219     9485  12796  10059     76  -1632   1297       C  
ATOM   1640  C   ALA A 219     -38.757 -41.935 -94.438  1.00 85.73           C  
ANISOU 1640  C   ALA A 219     9579  12800  10193     71  -1557   1162       C  
ATOM   1641  O   ALA A 219     -38.624 -40.876 -95.060  1.00 85.53           O  
ANISOU 1641  O   ALA A 219     9606  12765  10126     78  -1461   1116       O  
ATOM   1642  CB  ALA A 219     -40.742 -43.337 -94.939  1.00 85.68           C  
ANISOU 1642  CB  ALA A 219     9577  12835  10140     47  -1683   1334       C  
ATOM   1643  N   LEU A 220     -37.751 -42.756 -94.162  1.00 85.70           N  
ANISOU 1643  N   LEU A 220     9527  12748  10285     58  -1603   1106       N  
ATOM   1644  CA  LEU A 220     -36.426 -42.572 -94.725  1.00 85.36           C  
ANISOU 1644  CA  LEU A 220     9484  12638  10310     52  -1541    989       C  
ATOM   1645  C   LEU A 220     -36.088 -43.779 -95.594  1.00 85.15           C  
ANISOU 1645  C   LEU A 220     9458  12549  10345     42  -1580    953       C  
ATOM   1646  O   LEU A 220     -36.318 -44.916 -95.184  1.00 87.31           O  
ANISOU 1646  O   LEU A 220     9700  12817  10654     35  -1685    996       O  
ATOM   1647  CB  LEU A 220     -35.405 -42.436 -93.610  1.00 86.22           C  
ANISOU 1647  CB  LEU A 220     9533  12745  10482     54  -1559    949       C  
ATOM   1648  CG  LEU A 220     -34.092 -41.824 -94.076  1.00 88.19           C  
ANISOU 1648  CG  LEU A 220     9776  12944  10787     47  -1476    844       C  
ATOM   1649  CD1 LEU A 220     -34.236 -40.304 -94.125  1.00 87.02           C  
ANISOU 1649  CD1 LEU A 220     9677  12816  10569     50  -1391    837       C  
ATOM   1650  CD2 LEU A 220     -32.940 -42.275 -93.178  1.00 88.32           C  
ANISOU 1650  CD2 LEU A 220     9717  12937  10901     42  -1526    800       C  
ATOM   1651  N   GLY A 221     -35.551 -43.538 -96.787  1.00 82.56           N  
ANISOU 1651  N   GLY A 221     9171  12173  10025     47  -1499    878       N  
ATOM   1652  CA  GLY A 221     -35.285 -44.628 -97.716  1.00 81.38           C  
ANISOU 1652  CA  GLY A 221     9043  11961   9917     53  -1532    841       C  
ATOM   1653  C   GLY A 221     -34.162 -44.367 -98.695  1.00 82.21           C  
ANISOU 1653  C   GLY A 221     9161  12017  10056     72  -1433    738       C  
ATOM   1654  O   GLY A 221     -33.618 -43.270 -98.747  1.00 83.16           O  
ANISOU 1654  O   GLY A 221     9274  12150  10170     69  -1335    700       O  
ATOM   1655  N   ILE A 222     -33.821 -45.392 -99.472  1.00 82.71           N  
ANISOU 1655  N   ILE A 222     9247  12024  10154     94  -1464    698       N  
ATOM   1656  CA  ILE A 222     -32.786 -45.310-100.507  1.00 82.90           C  
ANISOU 1656  CA  ILE A 222     9287  12006  10205    126  -1370    607       C  
ATOM   1657  C   ILE A 222     -33.412 -45.377-101.919  1.00 84.70           C  
ANISOU 1657  C   ILE A 222     9618  12201  10363    146  -1337    602       C  
ATOM   1658  O   ILE A 222     -34.286 -46.219-102.179  1.00 85.63           O  
ANISOU 1658  O   ILE A 222     9788  12293  10452    146  -1433    646       O  
ATOM   1659  CB  ILE A 222     -31.721 -46.420-100.300  1.00 82.21           C  
ANISOU 1659  CB  ILE A 222     9147  11878  10209    156  -1422    553       C  
ATOM   1660  CG1 ILE A 222     -30.638 -46.357-101.380  1.00 82.64           C  
ANISOU 1660  CG1 ILE A 222     9212  11901  10287    203  -1318    467       C  
ATOM   1661  CG2 ILE A 222     -32.368 -47.802-100.224  1.00 81.32           C  
ANISOU 1661  CG2 ILE A 222     9067  11729  10101    162  -1565    591       C  
ATOM   1662  CD1 ILE A 222     -29.520 -47.353-101.191  1.00 83.45           C  
ANISOU 1662  CD1 ILE A 222     9259  11972  10477    244  -1356    412       C  
ATOM   1663  N   VAL A 223     -32.980 -44.485-102.818  1.00 84.40           N  
ANISOU 1663  N   VAL A 223     9610  12161  10296    161  -1207    554       N  
ATOM   1664  CA  VAL A 223     -33.490 -44.465-104.198  1.00 82.90           C  
ANISOU 1664  CA  VAL A 223     9523  11938  10035    185  -1165    543       C  
ATOM   1665  C   VAL A 223     -32.961 -45.654-104.985  1.00 82.99           C  
ANISOU 1665  C   VAL A 223     9572  11886  10073    241  -1198    488       C  
ATOM   1666  O   VAL A 223     -31.748 -45.847-105.107  1.00 81.66           O  
ANISOU 1666  O   VAL A 223     9358  11706   9962    279  -1146    422       O  
ATOM   1667  CB  VAL A 223     -33.166 -43.154-104.950  1.00 83.14           C  
ANISOU 1667  CB  VAL A 223     9578  11986  10024    185  -1013    510       C  
ATOM   1668  CG1 VAL A 223     -33.515 -43.277-106.424  1.00 82.92           C  
ANISOU 1668  CG1 VAL A 223     9658  11918   9930    222   -969    487       C  
ATOM   1669  CG2 VAL A 223     -33.943 -41.994-104.359  1.00 83.74           C  
ANISOU 1669  CG2 VAL A 223     9652  12114  10049    139   -992    568       C  
ATOM   1670  N   ALA A 224     -33.897 -46.439-105.511  1.00 84.38           N  
ANISOU 1670  N   ALA A 224     9834  12020  10204    250  -1291    520       N  
ATOM   1671  CA  ALA A 224     -33.591 -47.646-106.268  1.00 85.67           C  
ANISOU 1671  CA  ALA A 224    10062  12111  10377    308  -1351    473       C  
ATOM   1672  C   ALA A 224     -33.500 -47.393-107.775  1.00 86.69           C  
ANISOU 1672  C   ALA A 224    10294  12203  10440    362  -1258    422       C  
ATOM   1673  O   ALA A 224     -32.565 -47.856-108.423  1.00 89.52           O  
ANISOU 1673  O   ALA A 224    10672  12526  10814    433  -1215    350       O  
ATOM   1674  CB  ALA A 224     -34.604 -48.736-105.956  1.00 84.10           C  
ANISOU 1674  CB  ALA A 224     9904  11875  10174    284  -1526    539       C  
ATOM   1675  N   THR A 225     -34.462 -46.660-108.329  1.00 87.43           N  
ANISOU 1675  N   THR A 225    10456  12308  10455    335  -1226    462       N  
ATOM   1676  CA  THR A 225     -34.466 -46.341-109.758  1.00 89.60           C  
ANISOU 1676  CA  THR A 225    10836  12550  10658    383  -1137    419       C  
ATOM   1677  C   THR A 225     -34.976 -44.930-110.032  1.00 90.98           C  
ANISOU 1677  C   THR A 225    11023  12773  10772    343  -1029    447       C  
ATOM   1678  O   THR A 225     -35.968 -44.507-109.439  1.00 92.18           O  
ANISOU 1678  O   THR A 225    11162  12960  10901    284  -1076    521       O  
ATOM   1679  CB  THR A 225     -35.310 -47.347-110.566  1.00 89.87           C  
ANISOU 1679  CB  THR A 225    10999  12505  10640    410  -1257    432       C  
ATOM   1680  OG1 THR A 225     -36.426 -47.789-109.786  1.00 88.81           O  
ANISOU 1680  OG1 THR A 225    10853  12375  10513    344  -1405    523       O  
ATOM   1681  CG2 THR A 225     -34.479 -48.551-110.944  1.00 92.35           C  
ANISOU 1681  CG2 THR A 225    11349  12752  10985    490  -1307    363       C  
ATOM   1682  N   THR A 226     -34.291 -44.206-110.917  1.00 91.98           N  
ANISOU 1682  N   THR A 226    11173  12904  10871    380   -884    392       N  
ATOM   1683  CA  THR A 226     -34.746 -42.879-111.353  1.00 93.47           C  
ANISOU 1683  CA  THR A 226    11393  13127  10994    349   -779    413       C  
ATOM   1684  C   THR A 226     -34.969 -42.829-112.860  1.00 97.88           C  
ANISOU 1684  C   THR A 226    12079  13640  11470    400   -722    381       C  
ATOM   1685  O   THR A 226     -34.570 -43.745-113.580  1.00103.60           O  
ANISOU 1685  O   THR A 226    12864  14310  12189    470   -744    333       O  
ATOM   1686  CB  THR A 226     -33.773 -41.743-110.952  1.00 92.39           C  
ANISOU 1686  CB  THR A 226    11161  13044  10896    327   -648    391       C  
ATOM   1687  OG1 THR A 226     -32.530 -41.868-111.656  1.00 92.28           O  
ANISOU 1687  OG1 THR A 226    11133  13019  10908    386   -548    324       O  
ATOM   1688  CG2 THR A 226     -33.517 -41.748-109.467  1.00 93.34           C  
ANISOU 1688  CG2 THR A 226    11165  13205  11094    280   -706    418       C  
ATOM   1689  N   GLY A 227     -35.605 -41.757-113.329  1.00 99.50           N  
ANISOU 1689  N   GLY A 227    12333  13865  11605    372   -652    407       N  
ATOM   1690  CA  GLY A 227     -35.781 -41.517-114.762  1.00102.45           C  
ANISOU 1690  CA  GLY A 227    12827  14202  11895    418   -580    377       C  
ATOM   1691  C   GLY A 227     -36.858 -42.372-115.403  1.00104.41           C  
ANISOU 1691  C   GLY A 227    13199  14387  12085    437   -702    399       C  
ATOM   1692  O   GLY A 227     -37.992 -42.411-114.941  1.00105.99           O  
ANISOU 1692  O   GLY A 227    13407  14593  12269    383   -803    470       O  
ATOM   1693  N   VAL A 228     -36.504 -43.060-116.479  1.00106.50           N  
ANISOU 1693  N   VAL A 228    13561  14588  12315    516   -696    343       N  
ATOM   1694  CA  VAL A 228     -37.473 -43.874-117.196  1.00107.65           C  
ANISOU 1694  CA  VAL A 228    13842  14659  12402    538   -820    359       C  
ATOM   1695  C   VAL A 228     -37.525 -45.278-116.599  1.00108.66           C  
ANISOU 1695  C   VAL A 228    13960  14739  12586    545   -988    368       C  
ATOM   1696  O   VAL A 228     -38.364 -46.096-116.977  1.00110.05           O  
ANISOU 1696  O   VAL A 228    14236  14846  12730    548  -1128    394       O  
ATOM   1697  CB  VAL A 228     -37.156 -43.940-118.702  1.00110.34           C  
ANISOU 1697  CB  VAL A 228    14318  14943  12662    628   -745    294       C  
ATOM   1698  CG1 VAL A 228     -38.428 -44.222-119.487  1.00112.47           C  
ANISOU 1698  CG1 VAL A 228    14734  15147  12851    623   -851    328       C  
ATOM   1699  CG2 VAL A 228     -36.518 -42.638-119.180  1.00110.02           C  
ANISOU 1699  CG2 VAL A 228    14250  14958  12592    637   -548    268       C  
ATOM   1700  N   SER A 229     -36.628 -45.541-115.652  1.00110.21           N  
ANISOU 1700  N   SER A 229    14034  14970  12868    543   -979    349       N  
ATOM   1701  CA  SER A 229     -36.533 -46.845-114.996  1.00111.25           C  
ANISOU 1701  CA  SER A 229    14145  15062  13063    551  -1130    354       C  
ATOM   1702  C   SER A 229     -37.558 -47.000-113.879  1.00110.38           C  
ANISOU 1702  C   SER A 229    13974  14978  12987    456  -1263    451       C  
ATOM   1703  O   SER A 229     -37.821 -48.117-113.429  1.00109.20           O  
ANISOU 1703  O   SER A 229    13829  14785  12876    448  -1418    476       O  
ATOM   1704  CB  SER A 229     -35.124 -47.068-114.442  1.00112.59           C  
ANISOU 1704  CB  SER A 229    14207  15259  13310    592  -1066    296       C  
ATOM   1705  OG  SER A 229     -34.139 -46.879-115.443  1.00115.10           O  
ANISOU 1705  OG  SER A 229    14566  15569  13598    683   -930    218       O  
ATOM   1706  N   THR A 230     -38.122 -45.878-113.431  1.00111.06           N  
ANISOU 1706  N   THR A 230    14003  15136  13057    390  -1203    507       N  
ATOM   1707  CA  THR A 230     -39.160 -45.887-112.401  1.00112.23           C  
ANISOU 1707  CA  THR A 230    14092  15326  13225    310  -1310    609       C  
ATOM   1708  C   THR A 230     -40.484 -46.406-112.950  1.00114.06           C  
ANISOU 1708  C   THR A 230    14424  15508  13403    286  -1442    677       C  
ATOM   1709  O   THR A 230     -40.713 -46.375-114.158  1.00116.25           O  
ANISOU 1709  O   THR A 230    14823  15730  13613    324  -1423    646       O  
ATOM   1710  CB  THR A 230     -39.370 -44.500-111.751  1.00111.45           C  
ANISOU 1710  CB  THR A 230    13910  15320  13114    260  -1205    648       C  
ATOM   1711  OG1 THR A 230     -40.509 -44.552-110.884  1.00114.93           O  
ANISOU 1711  OG1 THR A 230    14309  15804  13555    198  -1310    755       O  
ATOM   1712  CG2 THR A 230     -39.615 -43.429-112.791  1.00110.39           C  
ANISOU 1712  CG2 THR A 230    13854  15190  12898    273  -1084    629       C  
ATOM   1713  N   GLU A 231     -41.344 -46.877-112.051  1.00115.83           N  
ANISOU 1713  N   GLU A 231    14596  15755  13658    224  -1577    775       N  
ATOM   1714  CA  GLU A 231     -42.642 -47.444-112.416  1.00120.93           C  
ANISOU 1714  CA  GLU A 231    15318  16360  14269    188  -1725    862       C  
ATOM   1715  C   GLU A 231     -43.545 -46.514-113.241  1.00123.87           C  
ANISOU 1715  C   GLU A 231    15760  16747  14555    175  -1668    896       C  
ATOM   1716  O   GLU A 231     -44.110 -46.930-114.260  1.00123.99           O  
ANISOU 1716  O   GLU A 231    15899  16687  14522    187  -1738    900       O  
ATOM   1717  CB  GLU A 231     -43.371 -47.940-111.168  1.00120.96           C  
ANISOU 1717  CB  GLU A 231    15222  16411  14324    117  -1858    978       C  
ATOM   1718  CG  GLU A 231     -42.924 -49.321-110.719  1.00123.98           C  
ANISOU 1718  CG  GLU A 231    15594  16733  14778    123  -1996    968       C  
ATOM   1719  CD  GLU A 231     -43.171 -50.384-111.773  1.00126.52           C  
ANISOU 1719  CD  GLU A 231    16060  16931  15078    149  -2126    948       C  
ATOM   1720  OE1 GLU A 231     -44.345 -50.617-112.130  1.00126.47           O  
ANISOU 1720  OE1 GLU A 231    16112  16900  15040    103  -2240   1038       O  
ATOM   1721  OE2 GLU A 231     -42.186 -50.987-112.246  1.00131.08           O  
ANISOU 1721  OE2 GLU A 231    16697  17437  15669    220  -2118    845       O  
ATOM   1722  N   ILE A 232     -43.674 -45.263-112.803  1.00123.28           N  
ANISOU 1722  N   ILE A 232    15616  16764  14459    153  -1546    918       N  
ATOM   1723  CA  ILE A 232     -44.457 -44.276-113.540  1.00119.97           C  
ANISOU 1723  CA  ILE A 232    15260  16365  13958    145  -1479    944       C  
ATOM   1724  C   ILE A 232     -43.699 -43.767-114.771  1.00124.70           C  
ANISOU 1724  C   ILE A 232    15956  16916  14507    207  -1345    834       C  
ATOM   1725  O   ILE A 232     -44.300 -43.211-115.687  1.00132.11           O  
ANISOU 1725  O   ILE A 232    16984  17839  15371    213  -1309    841       O  
ATOM   1726  CB  ILE A 232     -44.911 -43.108-112.636  1.00116.30           C  
ANISOU 1726  CB  ILE A 232    14698  16011  13479    108  -1404   1009       C  
ATOM   1727  CG1 ILE A 232     -46.232 -42.522-113.150  1.00115.63           C  
ANISOU 1727  CG1 ILE A 232    14667  15948  13317     84  -1419   1091       C  
ATOM   1728  CG2 ILE A 232     -43.818 -42.054-112.513  1.00115.22           C  
ANISOU 1728  CG2 ILE A 232    14522  15910  13343    136  -1230    923       C  
ATOM   1729  CD1 ILE A 232     -47.142 -41.967-112.071  1.00114.57           C  
ANISOU 1729  CD1 ILE A 232    14435  15919  13175     43  -1438   1206       C  
ATOM   1730  N   GLY A 233     -42.382 -43.960-114.789  1.00126.23           N  
ANISOU 1730  N   GLY A 233    16129  17092  14741    256  -1270    739       N  
ATOM   1731  CA  GLY A 233     -41.567 -43.598-115.949  1.00128.88           C  
ANISOU 1731  CA  GLY A 233    16547  17387  15033    323  -1143    641       C  
ATOM   1732  C   GLY A 233     -41.759 -44.580-117.088  1.00129.89           C  
ANISOU 1732  C   GLY A 233    16821  17411  15119    375  -1231    608       C  
ATOM   1733  O   GLY A 233     -41.649 -44.215-118.262  1.00128.15           O  
ANISOU 1733  O   GLY A 233    16708  17153  14828    424  -1152    558       O  
ATOM   1734  N   LYS A 234     -42.038 -45.832-116.726  1.00132.25           N  
ANISOU 1734  N   LYS A 234    17128  17658  15460    366  -1400    639       N  
ATOM   1735  CA  LYS A 234     -42.349 -46.882-117.688  1.00136.42           C  
ANISOU 1735  CA  LYS A 234    17805  18075  15952    409  -1525    619       C  
ATOM   1736  C   LYS A 234     -43.725 -46.638-118.309  1.00138.17           C  
ANISOU 1736  C   LYS A 234    18117  18273  16107    366  -1599    695       C  
ATOM   1737  O   LYS A 234     -43.898 -46.775-119.523  1.00142.13           O  
ANISOU 1737  O   LYS A 234    18766  18697  16537    415  -1608    656       O  
ATOM   1738  CB  LYS A 234     -42.289 -48.265-117.028  1.00137.47           C  
ANISOU 1738  CB  LYS A 234    17918  18157  16154    400  -1700    640       C  
ATOM   1739  CG  LYS A 234     -40.893 -48.722-116.621  1.00136.47           C  
ANISOU 1739  CG  LYS A 234    17732  18032  16088    461  -1646    554       C  
ATOM   1740  CD  LYS A 234     -40.799 -50.241-116.623  1.00138.45           C  
ANISOU 1740  CD  LYS A 234    18048  18184  16369    492  -1825    542       C  
ATOM   1741  CE  LYS A 234     -39.440 -50.738-116.156  1.00138.84           C  
ANISOU 1741  CE  LYS A 234    18032  18238  16482    555  -1780    462       C  
ATOM   1742  NZ  LYS A 234     -39.354 -50.824-114.671  1.00138.37           N  
ANISOU 1742  NZ  LYS A 234    17810  18247  16514    483  -1819    518       N  
ATOM   1743  N   ILE A 235     -44.691 -46.268-117.467  1.00136.07           N  
ANISOU 1743  N   ILE A 235    17761  18076  15860    280  -1650    805       N  
ATOM   1744  CA  ILE A 235     -46.033 -45.890-117.915  1.00132.70           C  
ANISOU 1744  CA  ILE A 235    17391  17652  15377    233  -1708    893       C  
ATOM   1745  C   ILE A 235     -45.969 -44.742-118.918  1.00134.89           C  
ANISOU 1745  C   ILE A 235    17743  17937  15570    270  -1551    840       C  
ATOM   1746  O   ILE A 235     -46.577 -44.817-119.983  1.00143.43           O  
ANISOU 1746  O   ILE A 235    18957  18952  16585    285  -1595    842       O  
ATOM   1747  CB  ILE A 235     -46.960 -45.539-116.718  1.00128.90           C  
ANISOU 1747  CB  ILE A 235    16775  17270  14930    147  -1757   1023       C  
ATOM   1748  CG1 ILE A 235     -47.649 -46.806-116.191  1.00126.56           C  
ANISOU 1748  CG1 ILE A 235    16460  16937  14688     95  -1973   1118       C  
ATOM   1749  CG2 ILE A 235     -47.994 -44.480-117.094  1.00125.89           C  
ANISOU 1749  CG2 ILE A 235    16414  16939  14479    118  -1707   1088       C  
ATOM   1750  CD1 ILE A 235     -48.295 -46.661-114.827  1.00121.64           C  
ANISOU 1750  CD1 ILE A 235    15683  16422  14112     24  -2017   1242       C  
ATOM   1751  N   ARG A 236     -45.203 -43.705-118.593  1.00137.31           N  
ANISOU 1751  N   ARG A 236    17972  18320  15880    283  -1374    793       N  
ATOM   1752  CA  ARG A 236     -45.179 -42.483-119.395  1.00143.56           C  
ANISOU 1752  CA  ARG A 236    18817  19132  16596    305  -1220    757       C  
ATOM   1753  C   ARG A 236     -44.436 -42.614-120.722  1.00146.65           C  
ANISOU 1753  C   ARG A 236    19341  19446  16933    390  -1145    653       C  
ATOM   1754  O   ARG A 236     -44.283 -41.629-121.445  1.00148.68           O  
ANISOU 1754  O   ARG A 236    19645  19717  17128    413  -1009    617       O  
ATOM   1755  CB  ARG A 236     -44.635 -41.309-118.582  1.00148.16           C  
ANISOU 1755  CB  ARG A 236    19276  19815  17201    285  -1070    750       C  
ATOM   1756  CG  ARG A 236     -45.535 -40.903-117.429  1.00152.06           C  
ANISOU 1756  CG  ARG A 236    19664  20394  17717    215  -1120    856       C  
ATOM   1757  CD  ARG A 236     -45.204 -39.509-116.928  1.00156.72           C  
ANISOU 1757  CD  ARG A 236    20182  21069  18295    204   -969    847       C  
ATOM   1758  NE  ARG A 236     -45.570 -39.329-115.524  1.00159.27           N  
ANISOU 1758  NE  ARG A 236    20379  21474  18660    160  -1009    924       N  
ATOM   1759  CZ  ARG A 236     -46.810 -39.154-115.071  1.00162.68           C  
ANISOU 1759  CZ  ARG A 236    20785  21957  19066    123  -1083   1032       C  
ATOM   1760  NH1 ARG A 236     -47.851 -39.140-115.902  1.00162.92           N  
ANISOU 1760  NH1 ARG A 236    20903  21962  19036    116  -1134   1081       N  
ATOM   1761  NH2 ARG A 236     -47.010 -38.998-113.771  1.00162.97           N  
ANISOU 1761  NH2 ARG A 236    20709  22074  19138     97  -1107   1095       N  
ATOM   1762  N   ASP A 237     -43.978 -43.823-121.037  1.00152.52           N  
ANISOU 1762  N   ASP A 237    20146  20107  17695    441  -1236    606       N  
ATOM   1763  CA  ASP A 237     -43.447 -44.124-122.367  1.00162.03           C  
ANISOU 1763  CA  ASP A 237    21502  21229  18834    536  -1194    517       C  
ATOM   1764  C   ASP A 237     -44.504 -44.810-123.236  1.00169.84           C  
ANISOU 1764  C   ASP A 237    22649  22117  19763    539  -1354    549       C  
ATOM   1765  O   ASP A 237     -44.572 -44.573-124.446  1.00170.04           O  
ANISOU 1765  O   ASP A 237    22814  22088  19702    596  -1309    505       O  
ATOM   1766  CB  ASP A 237     -42.166 -44.960-122.278  1.00159.39           C  
ANISOU 1766  CB  ASP A 237    21152  20864  18543    613  -1177    433       C  
ATOM   1767  CG  ASP A 237     -40.921 -44.107-122.047  1.00156.38           C  
ANISOU 1767  CG  ASP A 237    20667  20562  18186    642   -973    375       C  
ATOM   1768  OD1 ASP A 237     -41.011 -43.070-121.353  1.00154.08           O  
ANISOU 1768  OD1 ASP A 237    20263  20359  17920    575   -888    414       O  
ATOM   1769  OD2 ASP A 237     -39.845 -44.477-122.561  1.00153.19           O  
ANISOU 1769  OD2 ASP A 237    20295  20132  17775    734   -902    293       O  
ATOM   1770  N   GLN A 238     -45.327 -45.646-122.602  1.00178.05           N  
ANISOU 1770  N   GLN A 238    23666  23133  20852    476  -1545    632       N  
ATOM   1771  CA  GLN A 238     -46.454 -46.316-123.261  1.00180.92           C  
ANISOU 1771  CA  GLN A 238    24161  23403  21175    455  -1727    687       C  
ATOM   1772  C   GLN A 238     -47.661 -45.384-123.371  1.00180.09           C  
ANISOU 1772  C   GLN A 238    24047  23349  21030    384  -1721    778       C  
ATOM   1773  O   GLN A 238     -48.573 -45.629-124.161  1.00182.48           O  
ANISOU 1773  O   GLN A 238    24472  23579  21281    374  -1833    816       O  
ATOM   1774  CB  GLN A 238     -46.853 -47.595-122.508  1.00182.09           C  
ANISOU 1774  CB  GLN A 238    24279  23507  21397    407  -1943    753       C  
ATOM   1775  CG  GLN A 238     -45.692 -48.451-122.012  1.00187.43           C  
ANISOU 1775  CG  GLN A 238    24918  24162  22135    460  -1951    681       C  
ATOM   1776  CD  GLN A 238     -44.698 -48.817-123.103  1.00191.18           C  
ANISOU 1776  CD  GLN A 238    25534  24552  22551    589  -1888    551       C  
ATOM   1777  OE1 GLN A 238     -43.535 -48.411-123.058  1.00190.85           O  
ANISOU 1777  OE1 GLN A 238    25438  24558  22515    653  -1719    469       O  
ATOM   1778  NE2 GLN A 238     -45.154 -49.581-124.092  1.00193.53           N  
ANISOU 1778  NE2 GLN A 238    26016  24724  22790    630  -2027    537       N  
ATOM   1779  N   MET A 239     -47.655 -44.324-122.563  1.00180.59           N  
ANISOU 1779  N   MET A 239    23967  23531  21115    340  -1596    813       N  
ATOM   1780  CA  MET A 239     -48.688 -43.292-122.589  1.00184.58           C  
ANISOU 1780  CA  MET A 239    24451  24099  21578    285  -1562    892       C  
ATOM   1781  C   MET A 239     -48.603 -42.479-123.882  1.00190.65           C  
ANISOU 1781  C   MET A 239    25351  24836  22251    339  -1440    827       C  
ATOM   1782  O   MET A 239     -47.533 -41.976-124.240  1.00192.11           O  
ANISOU 1782  O   MET A 239    25547  25030  22414    400  -1278    730       O  
ATOM   1783  CB  MET A 239     -48.552 -42.378-121.361  1.00182.26           C  
ANISOU 1783  CB  MET A 239    23984  23937  21328    241  -1455    932       C  
ATOM   1784  CG  MET A 239     -49.464 -41.155-121.353  1.00185.28           C  
ANISOU 1784  CG  MET A 239    24342  24394  21659    203  -1389   1001       C  
ATOM   1785  SD  MET A 239     -49.096 -40.004-120.010  1.00189.97           S  
ANISOU 1785  SD  MET A 239    24764  25128  22288    177  -1248   1021       S  
ATOM   1786  CE  MET A 239     -49.971 -38.533-120.557  1.00183.41           C  
ANISOU 1786  CE  MET A 239    23977  24345  21363    169  -1150   1058       C  
ATOM   1787  N   ALA A 240     -49.736 -42.369-124.577  1.00194.07           N  
ANISOU 1787  N   ALA A 240    25879  25232  22627    315  -1523    886       N  
ATOM   1788  CA  ALA A 240     -49.830 -41.592-125.813  1.00197.38           C  
ANISOU 1788  CA  ALA A 240    26428  25618  22948    359  -1425    836       C  
ATOM   1789  C   ALA A 240     -50.672 -40.333-125.620  1.00201.96           C  
ANISOU 1789  C   ALA A 240    26953  26286  23495    308  -1353    908       C  
ATOM   1790  O   ALA A 240     -51.719 -40.365-124.971  1.00203.96           O  
ANISOU 1790  O   ALA A 240    27133  26586  23776    239  -1457   1023       O  
ATOM   1791  CB  ALA A 240     -50.397 -42.446-126.937  1.00194.86           C  
ANISOU 1791  CB  ALA A 240    26290  25169  22576    387  -1576    832       C  
ATOM   1792  N   GLN A 244     -56.102 -34.441-123.594  1.00196.33           N  
ANISOU 1792  N   GLN A 244    25915  26085  22594    116  -1160   1406       N  
ATOM   1793  CA  GLN A 244     -57.157 -34.534-124.597  1.00192.12           C  
ANISOU 1793  CA  GLN A 244    25486  25502  22009    106  -1250   1459       C  
ATOM   1794  C   GLN A 244     -58.479 -33.957-124.070  1.00187.61           C  
ANISOU 1794  C   GLN A 244    24835  25032  21414     80  -1291   1599       C  
ATOM   1795  O   GLN A 244     -59.280 -34.673-123.457  1.00190.45           O  
ANISOU 1795  O   GLN A 244    25107  25431  21822     38  -1429   1722       O  
ATOM   1796  CB  GLN A 244     -57.330 -35.992-125.052  1.00199.13           C  
ANISOU 1796  CB  GLN A 244    26432  26289  22938     83  -1428   1477       C  
ATOM   1797  CG  GLN A 244     -58.251 -36.184-126.254  1.00204.92           C  
ANISOU 1797  CG  GLN A 244    27302  26941  23616     75  -1531   1512       C  
ATOM   1798  CD  GLN A 244     -58.458 -37.646-126.626  1.00207.61           C  
ANISOU 1798  CD  GLN A 244    27706  27175  24000     49  -1728   1537       C  
ATOM   1799  OE1 GLN A 244     -57.749 -38.533-126.146  1.00212.73           O  
ANISOU 1799  OE1 GLN A 244    28319  27796  24713     48  -1773   1503       O  
ATOM   1800  NE2 GLN A 244     -59.431 -37.901-127.494  1.00206.41           N  
ANISOU 1800  NE2 GLN A 244    27654  26957  23812     28  -1855   1596       N  
ATOM   1801  N   ASP A 245     -58.682 -32.657-124.302  1.00173.81           N  
ANISOU 1801  N   ASP A 245    23115  23329  19593    109  -1167   1584       N  
ATOM   1802  CA  ASP A 245     -59.937 -31.968-123.971  1.00163.44           C  
ANISOU 1802  CA  ASP A 245    21748  22110  18239    103  -1188   1708       C  
ATOM   1803  C   ASP A 245     -59.872 -30.481-124.311  1.00153.58           C  
ANISOU 1803  C   ASP A 245    20556  20891  16904    146  -1032   1655       C  
ATOM   1804  O   ASP A 245     -58.904 -29.800-123.961  1.00150.11           O  
ANISOU 1804  O   ASP A 245    20106  20468  16460    172   -898   1566       O  
ATOM   1805  CB  ASP A 245     -60.302 -32.142-122.491  1.00168.61           C  
ANISOU 1805  CB  ASP A 245    22230  22886  18947     88  -1227   1816       C  
ATOM   1806  CG  ASP A 245     -61.794 -32.353-122.276  1.00173.10           C  
ANISOU 1806  CG  ASP A 245    22733  23525  19511     61  -1353   1988       C  
ATOM   1807  OD1 ASP A 245     -62.583 -32.177-123.233  1.00170.13           O  
ANISOU 1807  OD1 ASP A 245    22443  23112  19087     55  -1398   2023       O  
ATOM   1808  OD2 ASP A 245     -62.177 -32.705-121.140  1.00179.26           O  
ANISOU 1808  OD2 ASP A 245    23372  24401  20338     45  -1407   2095       O  
ATOM   1809  N   LYS A 246     -60.914 -29.990-124.985  1.00144.55           N  
ANISOU 1809  N   LYS A 246    19473  19752  15696    150  -1059   1716       N  
ATOM   1810  CA  LYS A 246     -60.989 -28.593-125.421  1.00133.15           C  
ANISOU 1810  CA  LYS A 246    18099  18328  14164    190   -928   1674       C  
ATOM   1811  C   LYS A 246     -61.792 -27.735-124.448  1.00126.86           C  
ANISOU 1811  C   LYS A 246    17200  17664  13337    213   -901   1774       C  
ATOM   1812  O   LYS A 246     -62.950 -28.031-124.150  1.00122.22           O  
ANISOU 1812  O   LYS A 246    16544  17140  12753    201  -1005   1910       O  
ATOM   1813  CB  LYS A 246     -61.564 -28.495-126.830  1.00126.97           C  
ANISOU 1813  CB  LYS A 246    17462  17461  13317    191   -964   1666       C  
ATOM   1814  N   THR A 247     -61.147 -26.680-123.953  1.00124.24           N  
ANISOU 1814  N   THR A 247    16859  17373  12973    250   -762   1709       N  
ATOM   1815  CA  THR A 247     -61.771 -25.695-123.065  1.00119.82           C  
ANISOU 1815  CA  THR A 247    16228  16932  12366    292   -716   1781       C  
ATOM   1816  C   THR A 247     -62.947 -24.995-123.769  1.00119.28           C  
ANISOU 1816  C   THR A 247    16224  16883  12213    316   -728   1847       C  
ATOM   1817  O   THR A 247     -62.843 -24.679-124.953  1.00120.15           O  
ANISOU 1817  O   THR A 247    16466  16907  12279    313   -697   1780       O  
ATOM   1818  CB  THR A 247     -60.729 -24.680-122.505  1.00115.79           C  
ANISOU 1818  CB  THR A 247    15722  16435  11835    325   -573   1681       C  
ATOM   1819  OG1 THR A 247     -61.364 -23.437-122.191  1.00113.58           O  
ANISOU 1819  OG1 THR A 247    15452  16230  11472    378   -513   1720       O  
ATOM   1820  CG2 THR A 247     -59.613 -24.413-123.498  1.00114.17           C  
ANISOU 1820  CG2 THR A 247    15638  16118  11622    313   -482   1539       C  
ATOM   1821  N   PRO A 248     -64.073 -24.779-123.044  1.00117.20           N  
ANISOU 1821  N   PRO A 248    15865  16736  11927    342   -775   1984       N  
ATOM   1822  CA  PRO A 248     -65.313 -24.195-123.560  1.00116.45           C  
ANISOU 1822  CA  PRO A 248    15804  16680  11758    369   -801   2072       C  
ATOM   1823  C   PRO A 248     -65.104 -23.100-124.599  1.00120.53           C  
ANISOU 1823  C   PRO A 248    16476  17128  12190    396   -701   1973       C  
ATOM   1824  O   PRO A 248     -65.840 -23.046-125.590  1.00123.99           O  
ANISOU 1824  O   PRO A 248    16993  17528  12589    389   -747   2004       O  
ATOM   1825  CB  PRO A 248     -65.949 -23.583-122.314  1.00113.95           C  
ANISOU 1825  CB  PRO A 248    15370  16514  11409    430   -776   2174       C  
ATOM   1826  CG  PRO A 248     -65.461 -24.414-121.186  1.00115.62           C  
ANISOU 1826  CG  PRO A 248    15455  16770  11703    410   -811   2198       C  
ATOM   1827  CD  PRO A 248     -64.217 -25.142-121.622  1.00118.46           C  
ANISOU 1827  CD  PRO A 248    15868  17007  12132    353   -808   2071       C  
ATOM   1828  N   LEU A 249     -64.111 -22.241-124.369  1.00119.40           N  
ANISOU 1828  N   LEU A 249    16377  16968  12021    423   -573   1861       N  
ATOM   1829  CA  LEU A 249     -63.834 -21.119-125.257  1.00116.69           C  
ANISOU 1829  CA  LEU A 249    16175  16563  11598    447   -471   1770       C  
ATOM   1830  C   LEU A 249     -63.215 -21.562-126.579  1.00115.19           C  
ANISOU 1830  C   LEU A 249    16108  16240  11419    404   -466   1674       C  
ATOM   1831  O   LEU A 249     -63.505 -20.981-127.625  1.00114.61           O  
ANISOU 1831  O   LEU A 249    16155  16112  11277    414   -438   1646       O  
ATOM   1832  CB  LEU A 249     -62.931 -20.099-124.569  1.00116.34           C  
ANISOU 1832  CB  LEU A 249    16137  16537  11530    481   -348   1687       C  
ATOM   1833  CG  LEU A 249     -63.347 -18.645-124.788  1.00117.11           C  
ANISOU 1833  CG  LEU A 249    16321  16654  11521    538   -271   1679       C  
ATOM   1834  CD1 LEU A 249     -64.421 -18.255-123.777  1.00116.24           C  
ANISOU 1834  CD1 LEU A 249    16120  16676  11368    604   -304   1799       C  
ATOM   1835  CD2 LEU A 249     -62.141 -17.718-124.709  1.00115.36           C  
ANISOU 1835  CD2 LEU A 249    16166  16382  11281    542   -151   1557       C  
ATOM   1836  N   GLN A 250     -62.363 -22.585-126.524  1.00114.13           N  
ANISOU 1836  N   GLN A 250    15945  16052  11365    364   -493   1624       N  
ATOM   1837  CA  GLN A 250     -61.775 -23.170-127.729  1.00115.63           C  
ANISOU 1837  CA  GLN A 250    16247  16121  11566    335   -498   1539       C  
ATOM   1838  C   GLN A 250     -62.843 -23.769-128.631  1.00116.39           C  
ANISOU 1838  C   GLN A 250    16402  16177  11644    319   -621   1610       C  
ATOM   1839  O   GLN A 250     -62.797 -23.594-129.846  1.00117.53           O  
ANISOU 1839  O   GLN A 250    16684  16232  11737    322   -603   1554       O  
ATOM   1840  CB  GLN A 250     -60.728 -24.229-127.376  1.00116.95           C  
ANISOU 1840  CB  GLN A 250    16361  16249  11823    306   -516   1484       C  
ATOM   1841  CG  GLN A 250     -59.361 -23.654-127.047  1.00117.70           C  
ANISOU 1841  CG  GLN A 250    16454  16334  11932    314   -380   1375       C  
ATOM   1842  CD  GLN A 250     -58.289 -24.717-126.893  1.00117.07           C  
ANISOU 1842  CD  GLN A 250    16336  16207  11936    291   -393   1313       C  
ATOM   1843  OE1 GLN A 250     -58.446 -25.677-126.135  1.00114.11           O  
ANISOU 1843  OE1 GLN A 250    15861  15864  11632    271   -489   1368       O  
ATOM   1844  NE2 GLN A 250     -57.181 -24.541-127.608  1.00117.83           N  
ANISOU 1844  NE2 GLN A 250    16512  16230  12026    295   -296   1202       N  
ATOM   1845  N   GLN A 251     -63.802 -24.469-128.028  1.00118.47           N  
ANISOU 1845  N   GLN A 251    16559  16505  11948    301   -749   1738       N  
ATOM   1846  CA  GLN A 251     -64.912 -25.069-128.763  1.00121.81           C  
ANISOU 1846  CA  GLN A 251    17019  16897  12364    276   -888   1828       C  
ATOM   1847  C   GLN A 251     -65.789 -24.009-129.429  1.00121.85           C  
ANISOU 1847  C   GLN A 251    17104  16917  12275    309   -857   1859       C  
ATOM   1848  O   GLN A 251     -66.341 -24.243-130.502  1.00121.85           O  
ANISOU 1848  O   GLN A 251    17205  16844  12245    294   -929   1872       O  
ATOM   1849  CB  GLN A 251     -65.765 -25.937-127.838  1.00127.25           C  
ANISOU 1849  CB  GLN A 251    17556  17672  13121    246  -1026   1978       C  
ATOM   1850  CG  GLN A 251     -65.121 -27.248-127.414  1.00133.90           C  
ANISOU 1850  CG  GLN A 251    18338  18475  14059    202  -1105   1965       C  
ATOM   1851  CD  GLN A 251     -65.977 -28.035-126.429  1.00141.97           C  
ANISOU 1851  CD  GLN A 251    19201  19592  15148    169  -1237   2125       C  
ATOM   1852  OE1 GLN A 251     -65.455 -28.743-125.563  1.00143.96           O  
ANISOU 1852  OE1 GLN A 251    19357  19867  15473    149  -1263   2130       O  
ATOM   1853  NE2 GLN A 251     -67.298 -27.916-126.555  1.00143.19           N  
ANISOU 1853  NE2 GLN A 251    19322  19804  15279    164  -1322   2264       N  
ATOM   1854  N   LYS A 252     -65.911 -22.850-128.788  1.00121.62           N  
ANISOU 1854  N   LYS A 252    17036  16978  12195    356   -755   1869       N  
ATOM   1855  CA  LYS A 252     -66.709 -21.747-129.326  1.00123.02           C  
ANISOU 1855  CA  LYS A 252    17287  17176  12278    397   -717   1896       C  
ATOM   1856  C   LYS A 252     -65.940 -20.916-130.361  1.00123.21           C  
ANISOU 1856  C   LYS A 252    17475  17101  12235    412   -598   1758       C  
ATOM   1857  O   LYS A 252     -66.541 -20.167-131.137  1.00123.74           O  
ANISOU 1857  O   LYS A 252    17640  17150  12224    435   -581   1764       O  
ATOM   1858  CB  LYS A 252     -67.241 -20.859-128.196  1.00123.23           C  
ANISOU 1858  CB  LYS A 252    17210  17340  12269    453   -668   1971       C  
ATOM   1859  CG  LYS A 252     -68.237 -21.555-127.279  1.00123.38           C  
ANISOU 1859  CG  LYS A 252    17067  17474  12335    448   -783   2134       C  
ATOM   1860  CD  LYS A 252     -69.071 -20.552-126.497  1.00123.59           C  
ANISOU 1860  CD  LYS A 252    17026  17637  12296    524   -740   2225       C  
ATOM   1861  CE  LYS A 252     -70.029 -21.246-125.543  1.00122.27           C  
ANISOU 1861  CE  LYS A 252    16684  17596  12174    526   -844   2398       C  
ATOM   1862  NZ  LYS A 252     -69.321 -21.763-124.342  1.00120.59           N  
ANISOU 1862  NZ  LYS A 252    16356  17432  12027    519   -831   2391       N  
ATOM   1863  N   LEU A 253     -64.614 -21.057-130.360  1.00121.73           N  
ANISOU 1863  N   LEU A 253    17315  16856  12080    398   -517   1641       N  
ATOM   1864  CA  LEU A 253     -63.750 -20.411-131.348  1.00117.46           C  
ANISOU 1864  CA  LEU A 253    16920  16222  11487    406   -404   1515       C  
ATOM   1865  C   LEU A 253     -63.589 -21.287-132.588  1.00119.98           C  
ANISOU 1865  C   LEU A 253    17351  16425  11811    381   -462   1471       C  
ATOM   1866  O   LEU A 253     -63.659 -20.790-133.708  1.00121.48           O  
ANISOU 1866  O   LEU A 253    17680  16545  11929    395   -425   1425       O  
ATOM   1867  CB  LEU A 253     -62.379 -20.090-130.742  1.00111.83           C  
ANISOU 1867  CB  LEU A 253    16173  15510  10807    405   -285   1420       C  
ATOM   1868  CG  LEU A 253     -61.371 -19.307-131.591  1.00107.72           C  
ANISOU 1868  CG  LEU A 253    15778  14912  10239    411   -151   1301       C  
ATOM   1869  CD1 LEU A 253     -61.624 -17.807-131.518  1.00104.77           C  
ANISOU 1869  CD1 LEU A 253    15451  14571   9783    443    -64   1298       C  
ATOM   1870  CD2 LEU A 253     -59.948 -19.628-131.165  1.00104.04           C  
ANISOU 1870  CD2 LEU A 253    15263  14426   9840    392    -79   1218       C  
ATOM   1871  N   ASP A 254     -63.371 -22.585-132.380  1.00123.98           N  
ANISOU 1871  N   ASP A 254    17803  16906  12397    350   -557   1484       N  
ATOM   1872  CA  ASP A 254     -63.255 -23.546-133.479  1.00127.87           C  
ANISOU 1872  CA  ASP A 254    18406  17284  12894    335   -635   1446       C  
ATOM   1873  C   ASP A 254     -64.567 -23.667-134.246  1.00131.61           C  
ANISOU 1873  C   ASP A 254    18948  17731  13324    328   -757   1531       C  
ATOM   1874  O   ASP A 254     -64.566 -23.795-135.473  1.00132.54           O  
ANISOU 1874  O   ASP A 254    19218  17747  13393    336   -774   1481       O  
ATOM   1875  CB  ASP A 254     -62.816 -24.918-132.961  1.00128.77           C  
ANISOU 1875  CB  ASP A 254    18441  17381  13103    305   -727   1452       C  
ATOM   1876  CG  ASP A 254     -61.419 -24.903-132.362  1.00133.47           C  
ANISOU 1876  CG  ASP A 254    18982  17986  13743    312   -611   1359       C  
ATOM   1877  OD1 ASP A 254     -60.849 -23.806-132.174  1.00138.92           O  
ANISOU 1877  OD1 ASP A 254    19675  18708  14399    333   -468   1305       O  
ATOM   1878  OD2 ASP A 254     -60.890 -25.996-132.070  1.00135.63           O  
ANISOU 1878  OD2 ASP A 254    19212  18231  14088    295   -671   1342       O  
ATOM   1879  N   GLU A 255     -65.679 -23.625-133.512  1.00135.32           N  
ANISOU 1879  N   GLU A 255    19305  18297  13812    318   -841   1662       N  
ATOM   1880  CA  GLU A 255     -67.019 -23.633-134.095  1.00141.11           C  
ANISOU 1880  CA  GLU A 255    20076  19027  14510    310   -957   1764       C  
ATOM   1881  C   GLU A 255     -67.213 -22.400-134.975  1.00139.28           C  
ANISOU 1881  C   GLU A 255    19976  18770  14174    349   -861   1717       C  
ATOM   1882  O   GLU A 255     -67.668 -22.510-136.113  1.00142.28           O  
ANISOU 1882  O   GLU A 255    20486  19065  14508    346   -921   1712       O  
ATOM   1883  CB  GLU A 255     -68.076 -23.673-132.988  1.00149.77           C  
ANISOU 1883  CB  GLU A 255    21002  20258  15644    301  -1035   1920       C  
ATOM   1884  CG  GLU A 255     -69.453 -24.155-133.425  1.00159.50           C  
ANISOU 1884  CG  GLU A 255    22230  21491  16880    272  -1204   2056       C  
ATOM   1885  CD  GLU A 255     -70.410 -24.362-132.258  1.00166.20           C  
ANISOU 1885  CD  GLU A 255    22887  22483  17778    261  -1283   2224       C  
ATOM   1886  OE1 GLU A 255     -69.954 -24.429-131.090  1.00162.17           O  
ANISOU 1886  OE1 GLU A 255    22248  22056  17313    269  -1232   2233       O  
ATOM   1887  OE2 GLU A 255     -71.630 -24.468-132.514  1.00172.10           O  
ANISOU 1887  OE2 GLU A 255    23610  23260  18519    246  -1397   2354       O  
ATOM   1888  N   PHE A 256     -66.850 -21.235-134.440  1.00135.75           N  
ANISOU 1888  N   PHE A 256    19500  18390  13687    385   -717   1681       N  
ATOM   1889  CA  PHE A 256     -66.847 -19.984-135.196  1.00131.93           C  
ANISOU 1889  CA  PHE A 256    19142  17878  13104    422   -609   1623       C  
ATOM   1890  C   PHE A 256     -65.776 -20.022-136.290  1.00130.99           C  
ANISOU 1890  C   PHE A 256    19177  17637  12956    422   -530   1487       C  
ATOM   1891  O   PHE A 256     -65.898 -19.344-137.311  1.00127.76           O  
ANISOU 1891  O   PHE A 256    18907  17169  12465    442   -484   1446       O  
ATOM   1892  CB  PHE A 256     -66.614 -18.798-134.253  1.00130.20           C  
ANISOU 1892  CB  PHE A 256    18856  17755  12859    459   -486   1615       C  
ATOM   1893  CG  PHE A 256     -66.754 -17.454-134.912  1.00130.00           C  
ANISOU 1893  CG  PHE A 256    18951  17710  12730    496   -389   1574       C  
ATOM   1894  CD1 PHE A 256     -67.988 -16.816-134.962  1.00129.75           C  
ANISOU 1894  CD1 PHE A 256    18922  17735  12639    529   -431   1664       C  
ATOM   1895  CD2 PHE A 256     -65.648 -16.817-135.474  1.00129.87           C  
ANISOU 1895  CD2 PHE A 256    19043  17622  12677    500   -258   1450       C  
ATOM   1896  CE1 PHE A 256     -68.118 -15.574-135.568  1.00130.22           C  
ANISOU 1896  CE1 PHE A 256    19100  17773  12603    565   -346   1624       C  
ATOM   1897  CE2 PHE A 256     -65.772 -15.577-136.083  1.00128.33           C  
ANISOU 1897  CE2 PHE A 256    18963  17407  12389    530   -174   1416       C  
ATOM   1898  CZ  PHE A 256     -67.009 -14.954-136.130  1.00128.76           C  
ANISOU 1898  CZ  PHE A 256    19028  17510  12382    563   -220   1499       C  
ATOM   1899  N   GLY A 257     -64.733 -20.820-136.059  1.00131.54           N  
ANISOU 1899  N   GLY A 257    19216  17673  13089    404   -513   1423       N  
ATOM   1900  CA  GLY A 257     -63.661 -21.032-137.027  1.00132.61           C  
ANISOU 1900  CA  GLY A 257    19479  17701  13203    413   -442   1303       C  
ATOM   1901  C   GLY A 257     -64.184 -21.589-138.334  1.00137.06           C  
ANISOU 1901  C   GLY A 257    20192  18160  13722    416   -538   1301       C  
ATOM   1902  O   GLY A 257     -63.829 -21.099-139.402  1.00139.29           O  
ANISOU 1902  O   GLY A 257    20623  18371  13930    443   -461   1226       O  
ATOM   1903  N   GLU A 258     -65.036 -22.610-138.247  1.00140.13           N  
ANISOU 1903  N   GLU A 258    20545  18540  14157    389   -712   1387       N  
ATOM   1904  CA  GLU A 258     -65.712 -23.156-139.423  1.00140.44           C  
ANISOU 1904  CA  GLU A 258    20725  18477  14156    388   -836   1402       C  
ATOM   1905  C   GLU A 258     -66.735 -22.169-139.968  1.00139.69           C  
ANISOU 1905  C   GLU A 258    20697  18397  13981    401   -837   1453       C  
ATOM   1906  O   GLU A 258     -66.722 -21.856-141.156  1.00142.84           O  
ANISOU 1906  O   GLU A 258    21262  18709  14301    426   -813   1396       O  
ATOM   1907  CB  GLU A 258     -66.380 -24.498-139.107  1.00143.05           C  
ANISOU 1907  CB  GLU A 258    20991  18794  14565    345  -1038   1495       C  
ATOM   1908  CG  GLU A 258     -65.413 -25.662-138.938  1.00149.34           C  
ANISOU 1908  CG  GLU A 258    21779  19534  15426    338  -1069   1433       C  
ATOM   1909  CD  GLU A 258     -64.790 -26.132-140.245  1.00154.58           C  
ANISOU 1909  CD  GLU A 258    22640  20056  16034    375  -1069   1325       C  
ATOM   1910  OE1 GLU A 258     -64.426 -25.285-141.094  1.00154.92           O  
ANISOU 1910  OE1 GLU A 258    22806  20063  15989    417   -944   1248       O  
ATOM   1911  OE2 GLU A 258     -64.649 -27.362-140.418  1.00157.06           O  
ANISOU 1911  OE2 GLU A 258    22990  20295  16390    366  -1195   1319       O  
ATOM   1912  N   GLN A 259     -67.608 -21.681-139.087  1.00138.87           N  
ANISOU 1912  N   GLN A 259    20461  18407  13895    391   -862   1560       N  
ATOM   1913  CA  GLN A 259     -68.621 -20.673-139.420  1.00140.12           C  
ANISOU 1913  CA  GLN A 259    20658  18601  13981    411   -858   1618       C  
ATOM   1914  C   GLN A 259     -68.089 -19.579-140.353  1.00137.78           C  
ANISOU 1914  C   GLN A 259    20518  18245  13583    450   -712   1512       C  
ATOM   1915  O   GLN A 259     -68.702 -19.277-141.376  1.00135.67           O  
ANISOU 1915  O   GLN A 259    20382  17918  13247    462   -748   1517       O  
ATOM   1916  CB  GLN A 259     -69.155 -20.027-138.137  1.00143.84           C  
ANISOU 1916  CB  GLN A 259    20959  19221  14472    420   -829   1710       C  
ATOM   1917  CG  GLN A 259     -69.988 -20.937-137.247  1.00144.47           C  
ANISOU 1917  CG  GLN A 259    20875  19378  14636    386   -979   1851       C  
ATOM   1918  CD  GLN A 259     -71.477 -20.699-137.391  1.00147.33           C  
ANISOU 1918  CD  GLN A 259    21210  19794  14973    387  -1085   1989       C  
ATOM   1919  OE1 GLN A 259     -72.019 -20.713-138.499  1.00150.21           O  
ANISOU 1919  OE1 GLN A 259    21702  20076  15292    382  -1154   1993       O  
ATOM   1920  NE2 GLN A 259     -72.151 -20.482-136.264  1.00145.78           N  
ANISOU 1920  NE2 GLN A 259    20845  19738  14804    399  -1100   2107       N  
ATOM   1921  N   LEU A 260     -66.948 -18.998-139.983  1.00136.64           N  
ANISOU 1921  N   LEU A 260    20359  18120  13436    465   -553   1421       N  
ATOM   1922  CA  LEU A 260     -66.296 -17.941-140.752  1.00132.89           C  
ANISOU 1922  CA  LEU A 260    20017  17597  12875    495   -403   1324       C  
ATOM   1923  C   LEU A 260     -65.632 -18.503-142.002  1.00134.84           C  
ANISOU 1923  C   LEU A 260    20423  17719  13090    504   -393   1234       C  
ATOM   1924  O   LEU A 260     -65.720 -17.910-143.074  1.00137.18           O  
ANISOU 1924  O   LEU A 260    20872  17951  13299    528   -349   1194       O  
ATOM   1925  CB  LEU A 260     -65.245 -17.240-139.888  1.00130.01           C  
ANISOU 1925  CB  LEU A 260    19572  17292  12532    499   -252   1268       C  
ATOM   1926  CG  LEU A 260     -64.485 -16.049-140.471  1.00128.45           C  
ANISOU 1926  CG  LEU A 260    19485  17061  12259    520    -90   1180       C  
ATOM   1927  CD1 LEU A 260     -65.166 -14.744-140.089  1.00125.63           C  
ANISOU 1927  CD1 LEU A 260    19118  16770  11846    540    -52   1224       C  
ATOM   1928  CD2 LEU A 260     -63.041 -16.058-139.991  1.00128.17           C  
ANISOU 1928  CD2 LEU A 260    19396  17031  12272    508     28   1101       C  
ATOM   1929  N   SER A 261     -64.968 -19.647-141.848  1.00138.50           N  
ANISOU 1929  N   SER A 261    20854  18148  13619    492   -434   1202       N  
ATOM   1930  CA  SER A 261     -64.223 -20.290-142.932  1.00139.88           C  
ANISOU 1930  CA  SER A 261    21174  18210  13764    515   -421   1113       C  
ATOM   1931  C   SER A 261     -65.118 -20.745-144.082  1.00141.74           C  
ANISOU 1931  C   SER A 261    21560  18349  13943    525   -556   1137       C  
ATOM   1932  O   SER A 261     -64.724 -20.671-145.248  1.00144.81           O  
ANISOU 1932  O   SER A 261    22118  18646  14255    563   -509   1062       O  
ATOM   1933  CB  SER A 261     -63.432 -21.485-142.394  1.00137.98           C  
ANISOU 1933  CB  SER A 261    20855  17960  13611    505   -456   1086       C  
ATOM   1934  OG  SER A 261     -62.652 -22.086-143.408  1.00138.16           O  
ANISOU 1934  OG  SER A 261    21018  17879  13596    543   -434    996       O  
ATOM   1935  N   LYS A 262     -66.316 -21.214-143.749  1.00142.42           N  
ANISOU 1935  N   LYS A 262    21586  18459  14068    492   -724   1246       N  
ATOM   1936  CA  LYS A 262     -67.218 -21.775-144.750  1.00144.87           C  
ANISOU 1936  CA  LYS A 262    22028  18675  14341    491   -883   1283       C  
ATOM   1937  C   LYS A 262     -68.089 -20.716-145.426  1.00144.75           C  
ANISOU 1937  C   LYS A 262    22103  18658  14238    506   -869   1313       C  
ATOM   1938  O   LYS A 262     -68.626 -20.949-146.509  1.00149.24           O  
ANISOU 1938  O   LYS A 262    22824  19130  14750    517   -962   1314       O  
ATOM   1939  CB  LYS A 262     -68.053 -22.926-144.166  1.00145.65           C  
ANISOU 1939  CB  LYS A 262    22024  18785  14530    442  -1090   1393       C  
ATOM   1940  CG  LYS A 262     -67.234 -24.128-143.685  1.00148.98           C  
ANISOU 1940  CG  LYS A 262    22391  19182  15032    430  -1132   1358       C  
ATOM   1941  CD  LYS A 262     -66.115 -24.514-144.654  1.00151.60           C  
ANISOU 1941  CD  LYS A 262    22889  19398  15311    482  -1064   1223       C  
ATOM   1942  CE  LYS A 262     -65.423 -25.814-144.266  1.00148.80           C  
ANISOU 1942  CE  LYS A 262    22497  19008  15033    477  -1133   1194       C  
ATOM   1943  NZ  LYS A 262     -64.343 -26.187-145.224  1.00144.51           N  
ANISOU 1943  NZ  LYS A 262    22118  18359  14429    544  -1062   1066       N  
ATOM   1944  N   VAL A 263     -68.213 -19.552-144.793  1.00141.06           N  
ANISOU 1944  N   VAL A 263    21549  18292  13756    510   -757   1336       N  
ATOM   1945  CA  VAL A 263     -68.860 -18.411-145.431  1.00139.16           C  
ANISOU 1945  CA  VAL A 263    21402  18049  13423    532   -715   1348       C  
ATOM   1946  C   VAL A 263     -67.914 -17.817-146.474  1.00142.49           C  
ANISOU 1946  C   VAL A 263    21995  18389  13756    572   -568   1225       C  
ATOM   1947  O   VAL A 263     -68.320 -17.590-147.614  1.00149.95           O  
ANISOU 1947  O   VAL A 263    23103  19253  14618    594   -595   1208       O  
ATOM   1948  CB  VAL A 263     -69.345 -17.355-144.405  1.00137.02           C  
ANISOU 1948  CB  VAL A 263    20992  17910  13158    533   -653   1415       C  
ATOM   1949  CG1 VAL A 263     -69.500 -15.979-145.040  1.00134.02           C  
ANISOU 1949  CG1 VAL A 263    20725  17521  12674    568   -546   1382       C  
ATOM   1950  CG2 VAL A 263     -70.662 -17.795-143.779  1.00135.30           C  
ANISOU 1950  CG2 VAL A 263    20649  17764  12993    508   -816   1560       C  
ATOM   1951  N   ILE A 264     -66.653 -17.602-146.094  1.00144.06           N  
ANISOU 1951  N   ILE A 264    22154  18609  13971    580   -417   1145       N  
ATOM   1952  CA  ILE A 264     -65.653 -17.015-147.002  1.00146.60           C  
ANISOU 1952  CA  ILE A 264    22616  18869  14215    615   -262   1038       C  
ATOM   1953  C   ILE A 264     -65.341 -17.928-148.195  1.00150.37           C  
ANISOU 1953  C   ILE A 264    23258  19224  14650    646   -312    979       C  
ATOM   1954  O   ILE A 264     -65.131 -17.443-149.309  1.00154.53           O  
ANISOU 1954  O   ILE A 264    23950  19682  15081    683   -242    924       O  
ATOM   1955  CB  ILE A 264     -64.353 -16.594-146.269  1.00143.49           C  
ANISOU 1955  CB  ILE A 264    22126  18532  13858    610    -95    979       C  
ATOM   1956  CG1 ILE A 264     -64.658 -15.550-145.187  1.00141.67           C  
ANISOU 1956  CG1 ILE A 264    21768  18410  13650    590    -43   1029       C  
ATOM   1957  CG2 ILE A 264     -63.337 -16.017-147.248  1.00142.12           C  
ANISOU 1957  CG2 ILE A 264    22091  18301  13608    642     62    885       C  
ATOM   1958  CD1 ILE A 264     -63.527 -15.310-144.208  1.00137.57           C  
ANISOU 1958  CD1 ILE A 264    21125  17954  13192    574     75    991       C  
ATOM   1959  N   SER A 265     -65.333 -19.240-147.963  1.00151.48           N  
ANISOU 1959  N   SER A 265    23361  19336  14859    636   -436    992       N  
ATOM   1960  CA  SER A 265     -65.112 -20.211-149.039  1.00152.08           C  
ANISOU 1960  CA  SER A 265    23600  19288  14893    675   -510    939       C  
ATOM   1961  C   SER A 265     -66.253 -20.231-150.070  1.00152.83           C  
ANISOU 1961  C   SER A 265    23852  19298  14915    684   -646    977       C  
ATOM   1962  O   SER A 265     -66.012 -20.505-151.248  1.00153.13           O  
ANISOU 1962  O   SER A 265    24079  19229  14872    734   -652    913       O  
ATOM   1963  CB  SER A 265     -64.848 -21.612-148.477  1.00152.24           C  
ANISOU 1963  CB  SER A 265    23544  19294  15006    661   -625    947       C  
ATOM   1964  OG  SER A 265     -65.974 -22.117-147.783  1.00153.10           O  
ANISOU 1964  OG  SER A 265    23544  19437  15188    605   -804   1059       O  
ATOM   1965  N   LEU A 266     -67.480 -19.942-149.630  1.00153.03           N  
ANISOU 1965  N   LEU A 266    23800  19376  14969    641   -754   1082       N  
ATOM   1966  CA  LEU A 266     -68.626 -19.807-150.543  1.00153.84           C  
ANISOU 1966  CA  LEU A 266    24034  19410  15006    644   -879   1129       C  
ATOM   1967  C   LEU A 266     -68.536 -18.546-151.400  1.00154.05           C  
ANISOU 1967  C   LEU A 266    24194  19418  14919    682   -741   1078       C  
ATOM   1968  O   LEU A 266     -68.778 -18.593-152.606  1.00155.23           O  
ANISOU 1968  O   LEU A 266    24535  19463  14982    716   -784   1046       O  
ATOM   1969  CB  LEU A 266     -69.964 -19.826-149.792  1.00152.55           C  
ANISOU 1969  CB  LEU A 266    23732  19322  14907    589  -1027   1268       C  
ATOM   1970  CG  LEU A 266     -70.682 -21.154-149.515  1.00155.14           C  
ANISOU 1970  CG  LEU A 266    24005  19621  15319    544  -1256   1356       C  
ATOM   1971  CD1 LEU A 266     -72.042 -20.889-148.883  1.00153.90           C  
ANISOU 1971  CD1 LEU A 266    23712  19554  15207    498  -1370   1504       C  
ATOM   1972  CD2 LEU A 266     -70.848 -22.003-150.768  1.00156.30           C  
ANISOU 1972  CD2 LEU A 266    24361  19609  15415    565  -1396   1321       C  
ATOM   1973  N   ILE A 267     -68.190 -17.426-150.769  1.00153.01           N  
ANISOU 1973  N   ILE A 267    23967  19383  14786    677   -583   1072       N  
ATOM   1974  CA  ILE A 267     -68.011 -16.157-151.473  1.00155.59           C  
ANISOU 1974  CA  ILE A 267    24409  19697  15010    708   -441   1025       C  
ATOM   1975  C   ILE A 267     -66.800 -16.212-152.422  1.00160.63           C  
ANISOU 1975  C   ILE A 267    25196  20256  15579    756   -311    912       C  
ATOM   1976  O   ILE A 267     -66.810 -15.570-153.474  1.00166.77           O  
ANISOU 1976  O   ILE A 267    26137  20973  16252    791   -252    874       O  
ATOM   1977  CB  ILE A 267     -67.949 -14.954-150.490  1.00153.22           C  
ANISOU 1977  CB  ILE A 267    23971  19515  14728    689   -319   1051       C  
ATOM   1978  CG1 ILE A 267     -69.345 -14.675-149.906  1.00148.77           C  
ANISOU 1978  CG1 ILE A 267    23314  19021  14190    666   -441   1167       C  
ATOM   1979  CG2 ILE A 267     -67.402 -13.703-151.171  1.00156.31           C  
ANISOU 1979  CG2 ILE A 267    24480  19886  15022    716   -150    986       C  
ATOM   1980  CD1 ILE A 267     -69.461 -13.414-149.071  1.00140.95           C  
ANISOU 1980  CD1 ILE A 267    22224  18136  13194    665   -337   1194       C  
ATOM   1981  N   CYS A 268     -65.782 -16.994-152.060  1.00163.83           N  
ANISOU 1981  N   CYS A 268    25544  20664  16040    763   -269    864       N  
ATOM   1982  CA  CYS A 268     -64.591 -17.184-152.905  1.00165.84           C  
ANISOU 1982  CA  CYS A 268    25923  20855  16233    819   -147    764       C  
ATOM   1983  C   CYS A 268     -64.902 -17.836-154.255  1.00163.54           C  
ANISOU 1983  C   CYS A 268    25851  20432  15853    874   -245    732       C  
ATOM   1984  O   CYS A 268     -64.368 -17.422-155.285  1.00160.55           O  
ANISOU 1984  O   CYS A 268    25628  19999  15373    929   -135    668       O  
ATOM   1985  CB  CYS A 268     -63.514 -17.991-152.171  1.00168.91           C  
ANISOU 1985  CB  CYS A 268    26193  21278  16707    819   -101    728       C  
ATOM   1986  SG  CYS A 268     -62.358 -17.004-151.191  1.00170.85           S  
ANISOU 1986  SG  CYS A 268    26274  21639  17001    791    115    705       S  
ATOM   1987  N   VAL A 269     -65.758 -18.856-154.237  1.00164.43           N  
ANISOU 1987  N   VAL A 269    25976  20494  16004    859   -454    780       N  
ATOM   1988  CA  VAL A 269     -66.192 -19.538-155.458  1.00167.08           C  
ANISOU 1988  CA  VAL A 269    26525  20696  16262    906   -584    758       C  
ATOM   1989  C   VAL A 269     -67.245 -18.707-156.201  1.00172.01           C  
ANISOU 1989  C   VAL A 269    27263  21285  16805    902   -631    796       C  
ATOM   1990  O   VAL A 269     -67.324 -18.754-157.431  1.00178.32           O  
ANISOU 1990  O   VAL A 269    28274  21979  17499    958   -652    752       O  
ATOM   1991  CB  VAL A 269     -66.689 -20.976-155.164  1.00164.99           C  
ANISOU 1991  CB  VAL A 269    26237  20379  16073    885   -808    799       C  
ATOM   1992  CG1 VAL A 269     -67.481 -21.554-156.330  1.00163.83           C  
ANISOU 1992  CG1 VAL A 269    26304  20091  15852    916   -988    802       C  
ATOM   1993  CG2 VAL A 269     -65.509 -21.879-154.833  1.00163.79           C  
ANISOU 1993  CG2 VAL A 269    26045  20221  15963    918   -757    733       C  
ATOM   1994  N   ALA A 270     -68.033 -17.936-155.451  1.00172.59           N  
ANISOU 1994  N   ALA A 270    27201  21450  16923    844   -643    877       N  
ATOM   1995  CA  ALA A 270     -69.024 -17.022-156.033  1.00168.99           C  
ANISOU 1995  CA  ALA A 270    26831  20980  16397    840   -673    919       C  
ATOM   1996  C   ALA A 270     -68.377 -15.873-156.815  1.00166.05           C  
ANISOU 1996  C   ALA A 270    26584  20594  15913    885   -478    846       C  
ATOM   1997  O   ALA A 270     -68.996 -15.312-157.718  1.00165.29           O  
ANISOU 1997  O   ALA A 270    26634  20441  15727    905   -502    850       O  
ATOM   1998  CB  ALA A 270     -69.951 -16.479-154.954  1.00168.01           C  
ANISOU 1998  CB  ALA A 270    26519  20969  16346    780   -721   1024       C  
ATOM   1999  N   VAL A 271     -67.140 -15.530-156.458  1.00164.01           N  
ANISOU 1999  N   VAL A 271    26263  20388  15664    897   -289    785       N  
ATOM   2000  CA  VAL A 271     -66.350 -14.526-157.179  1.00164.60           C  
ANISOU 2000  CA  VAL A 271    26445  20453  15641    935    -95    720       C  
ATOM   2001  C   VAL A 271     -65.889 -15.078-158.537  1.00169.14           C  
ANISOU 2001  C   VAL A 271    27241  20909  16113   1012    -87    647       C  
ATOM   2002  O   VAL A 271     -65.813 -14.344-159.527  1.00173.06           O  
ANISOU 2002  O   VAL A 271    27894  21361  16499   1050     -3    615       O  
ATOM   2003  CB  VAL A 271     -65.159 -14.025-156.316  1.00161.31           C  
ANISOU 2003  CB  VAL A 271    25879  20133  15279    915     92    691       C  
ATOM   2004  CG1 VAL A 271     -64.058 -13.399-157.162  1.00160.70           C  
ANISOU 2004  CG1 VAL A 271    25917  20031  15111    960    286    619       C  
ATOM   2005  CG2 VAL A 271     -65.644 -13.031-155.269  1.00158.91           C  
ANISOU 2005  CG2 VAL A 271    25420  19930  15027    857    116    753       C  
ATOM   2006  N   TRP A 272     -65.610 -16.378-158.573  1.00170.28           N  
ANISOU 2006  N   TRP A 272    27402  21003  16290   1040   -179    623       N  
ATOM   2007  CA  TRP A 272     -65.192 -17.075-159.790  1.00172.54           C  
ANISOU 2007  CA  TRP A 272    27903  21175  16480   1127   -194    553       C  
ATOM   2008  C   TRP A 272     -66.341 -17.253-160.789  1.00174.27           C  
ANISOU 2008  C   TRP A 272    28313  21281  16620   1147   -367    574       C  
ATOM   2009  O   TRP A 272     -66.117 -17.240-162.001  1.00175.06           O  
ANISOU 2009  O   TRP A 272    28626  21290  16599   1224   -335    518       O  
ATOM   2010  CB  TRP A 272     -64.613 -18.439-159.413  1.00171.83           C  
ANISOU 2010  CB  TRP A 272    27768  21064  16455   1151   -261    526       C  
ATOM   2011  CG  TRP A 272     -63.800 -19.110-160.474  1.00172.90           C  
ANISOU 2011  CG  TRP A 272    28094  21107  16493   1259   -220    440       C  
ATOM   2012  CD1 TRP A 272     -62.585 -18.714-160.947  1.00173.63           C  
ANISOU 2012  CD1 TRP A 272    28234  21221  16515   1326     -6    375       C  
ATOM   2013  CD2 TRP A 272     -64.124 -20.323-161.164  1.00174.82           C  
ANISOU 2013  CD2 TRP A 272    28504  21223  16696   1318   -400    416       C  
ATOM   2014  NE1 TRP A 272     -62.136 -19.594-161.901  1.00176.01           N  
ANISOU 2014  NE1 TRP A 272    28722  21424  16729   1434    -32    309       N  
ATOM   2015  CE2 TRP A 272     -63.061 -20.593-162.054  1.00177.16           C  
ANISOU 2015  CE2 TRP A 272    28952  21471  16888   1433   -277    328       C  
ATOM   2016  CE3 TRP A 272     -65.213 -21.204-161.123  1.00174.25           C  
ANISOU 2016  CE3 TRP A 272    28470  21072  16665   1285   -660    464       C  
ATOM   2017  CZ2 TRP A 272     -63.053 -21.709-162.899  1.00179.39           C  
ANISOU 2017  CZ2 TRP A 272    29436  21623  17098   1526   -405    279       C  
ATOM   2018  CZ3 TRP A 272     -65.205 -22.315-161.964  1.00177.09           C  
ANISOU 2018  CZ3 TRP A 272    29029  21296  16960   1365   -797    418       C  
ATOM   2019  CH2 TRP A 272     -64.130 -22.556-162.840  1.00178.93           C  
ANISOU 2019  CH2 TRP A 272    29424  21478  17082   1489   -670    321       C  
ATOM   2020  N   LEU A 273     -67.562 -17.415-160.272  1.00173.37           N  
ANISOU 2020  N   LEU A 273    28120  21176  16574   1080   -549    660       N  
ATOM   2021  CA  LEU A 273     -68.754 -17.642-161.101  1.00172.40           C  
ANISOU 2021  CA  LEU A 273    28155  20951  16398   1085   -742    697       C  
ATOM   2022  C   LEU A 273     -69.449 -16.357-161.558  1.00173.42           C  
ANISOU 2022  C   LEU A 273    28342  21093  16456   1073   -696    726       C  
ATOM   2023  O   LEU A 273     -70.099 -16.346-162.604  1.00174.39           O  
ANISOU 2023  O   LEU A 273    28655  21114  16490   1104   -793    724       O  
ATOM   2024  CB  LEU A 273     -69.767 -18.548-160.387  1.00168.80           C  
ANISOU 2024  CB  LEU A 273    27586  20494  16054   1017   -980    789       C  
ATOM   2025  CG  LEU A 273     -69.419 -20.005-160.057  1.00168.17           C  
ANISOU 2025  CG  LEU A 273    27482  20369  16044   1022  -1103    776       C  
ATOM   2026  CD1 LEU A 273     -70.636 -20.696-159.461  1.00166.75           C  
ANISOU 2026  CD1 LEU A 273    27202  20188  15967    943  -1349    890       C  
ATOM   2027  CD2 LEU A 273     -68.917 -20.774-161.271  1.00168.79           C  
ANISOU 2027  CD2 LEU A 273    27811  20303  16019   1117  -1140    687       C  
ATOM   2028  N   ILE A 274     -69.328 -15.290-160.767  1.00173.50           N  
ANISOU 2028  N   ILE A 274    28196  21222  16503   1030   -559    753       N  
ATOM   2029  CA  ILE A 274     -69.833 -13.968-161.159  1.00175.98           C  
ANISOU 2029  CA  ILE A 274    28566  21553  16744   1025   -490    771       C  
ATOM   2030  C   ILE A 274     -69.110 -13.492-162.424  1.00180.39           C  
ANISOU 2030  C   ILE A 274    29339  22036  17164   1098   -350    686       C  
ATOM   2031  O   ILE A 274     -69.728 -12.907-163.316  1.00182.50           O  
ANISOU 2031  O   ILE A 274    29759  22243  17337   1119   -377    690       O  
ATOM   2032  CB  ILE A 274     -69.731 -12.935-160.002  1.00173.46           C  
ANISOU 2032  CB  ILE A 274    28044  21373  16490    972   -367    810       C  
ATOM   2033  CG1 ILE A 274     -70.914 -13.078-159.025  1.00171.70           C  
ANISOU 2033  CG1 ILE A 274    27653  21219  16365    913   -525    918       C  
ATOM   2034  CG2 ILE A 274     -69.635 -11.508-160.527  1.00173.00           C  
ANISOU 2034  CG2 ILE A 274    28072  21323  16335    987   -220    789       C  
ATOM   2035  CD1 ILE A 274     -72.255 -12.571-159.528  1.00169.36           C  
ANISOU 2035  CD1 ILE A 274    27433  20894  16020    907   -646    984       C  
ATOM   2036  N   ASN A 275     -67.807 -13.761-162.499  1.00184.47           N  
ANISOU 2036  N   ASN A 275    29862  22559  17668   1139   -203    614       N  
ATOM   2037  CA  ASN A 275     -67.043 -13.560-163.728  1.00189.07           C  
ANISOU 2037  CA  ASN A 275    30648  23071  18118   1222    -78    538       C  
ATOM   2038  C   ASN A 275     -67.318 -14.687-164.727  1.00196.80           C  
ANISOU 2038  C   ASN A 275    31829  23914  19030   1292   -231    504       C  
ATOM   2039  O   ASN A 275     -66.508 -15.601-164.896  1.00196.07           O  
ANISOU 2039  O   ASN A 275    31777  23789  18931   1350   -213    450       O  
ATOM   2040  CB  ASN A 275     -65.548 -13.437-163.421  1.00184.01           C  
ANISOU 2040  CB  ASN A 275    29926  22496  17490   1243    136    485       C  
ATOM   2041  CG  ASN A 275     -65.187 -12.087-162.837  1.00179.37           C  
ANISOU 2041  CG  ASN A 275    29216  22011  16923   1189    307    506       C  
ATOM   2042  OD1 ASN A 275     -64.910 -11.138-163.567  1.00176.14           O  
ANISOU 2042  OD1 ASN A 275    28915  21590  16419   1211    435    487       O  
ATOM   2043  ND2 ASN A 275     -65.184 -11.996-161.515  1.00178.13           N  
ANISOU 2043  ND2 ASN A 275    28838  21952  16890   1118    305    547       N  
ATOM   2044  N   ILE A 276     -68.479 -14.603-165.378  1.00205.28           N  
ANISOU 2044  N   ILE A 276    33035  24909  20054   1289   -389    537       N  
ATOM   2045  CA  ILE A 276     -68.966 -15.639-166.300  1.00210.98           C  
ANISOU 2045  CA  ILE A 276    33956  25489  20715   1345   -577    518       C  
ATOM   2046  C   ILE A 276     -68.135 -15.761-167.581  1.00212.98           C  
ANISOU 2046  C   ILE A 276    34449  25653  20820   1462   -474    426       C  
ATOM   2047  O   ILE A 276     -67.232 -16.597-167.660  1.00212.65           O  
ANISOU 2047  O   ILE A 276    34437  25591  20770   1525   -433    369       O  
ATOM   2048  CB  ILE A 276     -70.477 -15.474-166.637  1.00213.34           C  
ANISOU 2048  CB  ILE A 276    34325  25728  21005   1304   -783    588       C  
ATOM   2049  CG1 ILE A 276     -70.875 -13.989-166.735  1.00208.83           C  
ANISOU 2049  CG1 ILE A 276    33740  25215  20390   1275   -673    617       C  
ATOM   2050  CG2 ILE A 276     -71.330 -16.204-165.608  1.00213.45           C  
ANISOU 2050  CG2 ILE A 276    34160  25776  21163   1220   -983    677       C  
ATOM   2051  CD1 ILE A 276     -72.193 -13.730-167.440  1.00202.16           C  
ANISOU 2051  CD1 ILE A 276    33025  24291  19493   1265   -843    666       C  
ATOM   2052  N   GLY A 277     -68.440 -14.920-168.569  1.00215.39           N  
ANISOU 2052  N   GLY A 277    34923  25909  21004   1495   -428    414       N  
ATOM   2053  CA  GLY A 277     -67.766 -14.947-169.865  1.00218.65           C  
ANISOU 2053  CA  GLY A 277    35578  26237  21260   1612   -331    336       C  
ATOM   2054  C   GLY A 277     -66.631 -13.949-169.984  1.00216.55           C  
ANISOU 2054  C   GLY A 277    35281  26057  20939   1638    -47    303       C  
ATOM   2055  O   GLY A 277     -66.197 -13.619-171.092  1.00222.07           O  
ANISOU 2055  O   GLY A 277    36172  26704  21497   1725     58    257       O  
ATOM   2056  N   HIS A 278     -66.148 -13.469-168.840  1.00207.14           N  
ANISOU 2056  N   HIS A 278    33847  24995  19859   1562     73    332       N  
ATOM   2057  CA  HIS A 278     -65.000 -12.571-168.796  1.00202.60           C  
ANISOU 2057  CA  HIS A 278    33211  24509  19256   1570    334    311       C  
ATOM   2058  C   HIS A 278     -63.687 -13.336-168.970  1.00203.82           C  
ANISOU 2058  C   HIS A 278    33379  24673  19388   1656    454    253       C  
ATOM   2059  O   HIS A 278     -62.607 -12.739-168.947  1.00201.88           O  
ANISOU 2059  O   HIS A 278    33076  24504  19125   1669    673    240       O  
ATOM   2060  CB  HIS A 278     -64.986 -11.789-167.482  1.00199.53           C  
ANISOU 2060  CB  HIS A 278    32567  24249  18996   1458    401    365       C  
ATOM   2061  CG  HIS A 278     -65.934 -10.630-167.451  1.00196.51           C  
ANISOU 2061  CG  HIS A 278    32183  23878  18601   1395    374    415       C  
ATOM   2062  ND1 HIS A 278     -65.506  -9.322-167.366  1.00195.68           N  
ANISOU 2062  ND1 HIS A 278    32036  23840  18473   1361    550    426       N  
ATOM   2063  CD2 HIS A 278     -67.287 -10.581-167.485  1.00194.03           C  
ANISOU 2063  CD2 HIS A 278    31905  23521  18296   1361    188    461       C  
ATOM   2064  CE1 HIS A 278     -66.553  -8.518-167.348  1.00192.86           C  
ANISOU 2064  CE1 HIS A 278    31696  23477  18106   1316    475    470       C  
ATOM   2065  NE2 HIS A 278     -67.646  -9.256-167.421  1.00192.83           N  
ANISOU 2065  NE2 HIS A 278    31733  23411  18120   1317    260    493       N  
ATOM   2066  N   PHE A 279     -63.792 -14.654-169.152  1.00206.13           N  
ANISOU 2066  N   PHE A 279    33750  24887  19680   1716    306    222       N  
ATOM   2067  CA  PHE A 279     -62.631 -15.523-169.367  1.00209.19           C  
ANISOU 2067  CA  PHE A 279    34171  25272  20038   1817    394    163       C  
ATOM   2068  C   PHE A 279     -62.017 -15.346-170.761  1.00210.61           C  
ANISOU 2068  C   PHE A 279    34587  25394  20038   1949    523    110       C  
ATOM   2069  O   PHE A 279     -61.011 -15.982-171.089  1.00210.97           O  
ANISOU 2069  O   PHE A 279    34682  25441  20033   2054    619     61       O  
ATOM   2070  CB  PHE A 279     -63.004 -17.003-169.158  1.00211.72           C  
ANISOU 2070  CB  PHE A 279    34522  25512  20407   1844    174    146       C  
ATOM   2071  CG  PHE A 279     -63.548 -17.329-167.785  1.00211.36           C  
ANISOU 2071  CG  PHE A 279    34244  25527  20537   1724     45    203       C  
ATOM   2072  CD1 PHE A 279     -63.131 -16.630-166.653  1.00208.50           C  
ANISOU 2072  CD1 PHE A 279    33630  25302  20286   1632    177    240       C  
ATOM   2073  CD2 PHE A 279     -64.457 -18.370-167.623  1.00210.21           C  
ANISOU 2073  CD2 PHE A 279    34132  25295  20442   1704   -214    222       C  
ATOM   2074  CE1 PHE A 279     -63.627 -16.947-165.397  1.00203.04           C  
ANISOU 2074  CE1 PHE A 279    32730  24666  19746   1531     61    293       C  
ATOM   2075  CE2 PHE A 279     -64.956 -18.692-166.370  1.00205.73           C  
ANISOU 2075  CE2 PHE A 279    33347  24787  20032   1596   -330    283       C  
ATOM   2076  CZ  PHE A 279     -64.539 -17.981-165.256  1.00203.51           C  
ANISOU 2076  CZ  PHE A 279    32820  24649  19854   1515   -187    317       C  
ATOM   2077  N   ASN A 280     -62.620 -14.473-171.568  1.00210.31           N  
ANISOU 2077  N   ASN A 280    34692  25312  19903   1948    530    122       N  
ATOM   2078  CA  ASN A 280     -62.254 -14.321-172.976  1.00208.80           C  
ANISOU 2078  CA  ASN A 280    34753  25050  19529   2076    620     77       C  
ATOM   2079  C   ASN A 280     -61.360 -13.127-173.313  1.00205.36           C  
ANISOU 2079  C   ASN A 280    34295  24702  19029   2084    890     88       C  
ATOM   2080  O   ASN A 280     -60.462 -13.253-174.147  1.00208.70           O  
ANISOU 2080  O   ASN A 280    34842  25121  19333   2204   1036     51       O  
ATOM   2081  CB  ASN A 280     -63.513 -14.293-173.850  1.00212.22           C  
ANISOU 2081  CB  ASN A 280    35407  25350  19874   2090    429     78       C  
ATOM   2082  CG  ASN A 280     -64.258 -15.617-173.850  1.00215.47           C  
ANISOU 2082  CG  ASN A 280    35905  25649  20314   2114    160     62       C  
ATOM   2083  OD1 ASN A 280     -64.569 -16.173-172.794  1.00214.39           O  
ANISOU 2083  OD1 ASN A 280    35591  25544  20322   2032     40     92       O  
ATOM   2084  ND2 ASN A 280     -64.558 -16.124-175.041  1.00218.67           N  
ANISOU 2084  ND2 ASN A 280    36589  25917  20577   2227     58     17       N  
ATOM   2085  N   ASP A 281     -61.607 -11.986-172.665  1.00197.92           N  
ANISOU 2085  N   ASP A 281    33198  23839  18161   1960    953    142       N  
ATOM   2086  CA  ASP A 281     -60.951 -10.703-172.996  1.00196.51           C  
ANISOU 2086  CA  ASP A 281    33009  23730  17925   1945   1180    165       C  
ATOM   2087  C   ASP A 281     -59.529 -10.771-173.596  1.00202.31           C  
ANISOU 2087  C   ASP A 281    33784  24512  18572   2050   1407    141       C  
ATOM   2088  O   ASP A 281     -59.339 -10.362-174.743  1.00204.29           O  
ANISOU 2088  O   ASP A 281    34223  24723  18672   2133   1500    130       O  
ATOM   2089  CB  ASP A 281     -60.983  -9.733-171.807  1.00189.90           C  
ANISOU 2089  CB  ASP A 281    31928  23001  17223   1798   1236    222       C  
ATOM   2090  CG  ASP A 281     -60.140  -8.491-172.048  1.00187.35           C  
ANISOU 2090  CG  ASP A 281    31576  22751  16855   1776   1471    249       C  
ATOM   2091  OD1 ASP A 281     -60.600  -7.598-172.785  1.00190.03           O  
ANISOU 2091  OD1 ASP A 281    32051  23051  17101   1772   1491    263       O  
ATOM   2092  OD2 ASP A 281     -59.015  -8.412-171.512  1.00182.25           O  
ANISOU 2092  OD2 ASP A 281    30773  22202  16269   1759   1629    261       O  
ATOM   2093  N   PRO A 282     -58.529 -11.264-172.829  1.00203.48           N  
ANISOU 2093  N   PRO A 282    33752  24749  18812   2050   1501    139       N  
ATOM   2094  CA  PRO A 282     -57.180 -11.269-173.380  1.00205.66           C  
ANISOU 2094  CA  PRO A 282    34049  25083  19008   2149   1725    129       C  
ATOM   2095  C   PRO A 282     -56.794 -12.623-173.978  1.00207.46           C  
ANISOU 2095  C   PRO A 282    34418  25251  19156   2310   1682     66       C  
ATOM   2096  O   PRO A 282     -57.435 -13.090-174.919  1.00206.63           O  
ANISOU 2096  O   PRO A 282    34552  25026  18930   2403   1560     26       O  
ATOM   2097  CB  PRO A 282     -56.317 -10.971-172.153  1.00202.18           C  
ANISOU 2097  CB  PRO A 282    33321  24777  18720   2052   1847    168       C  
ATOM   2098  CG  PRO A 282     -57.112 -11.481-170.986  1.00200.33           C  
ANISOU 2098  CG  PRO A 282    32944  24534  18636   1955   1650    169       C  
ATOM   2099  CD  PRO A 282     -58.523 -11.760-171.441  1.00200.98           C  
ANISOU 2099  CD  PRO A 282    33198  24492  18670   1961   1424    152       C  
ATOM   2100  N   ARG A 290     -59.194 -21.633-169.749  1.00195.08           N  
ANISOU 2100  N   ARG A 290    32627  23305  18189   2324    254   -102       N  
ATOM   2101  CA  ARG A 290     -57.955 -21.084-170.287  1.00199.19           C  
ANISOU 2101  CA  ARG A 290    33165  23905  18613   2423    531   -130       C  
ATOM   2102  C   ARG A 290     -57.674 -19.691-169.732  1.00194.06           C  
ANISOU 2102  C   ARG A 290    32310  23393  18029   2305    729    -72       C  
ATOM   2103  O   ARG A 290     -56.588 -19.431-169.214  1.00190.70           O  
ANISOU 2103  O   ARG A 290    31714  23086  17654   2301    923    -64       O  
ATOM   2104  CB  ARG A 290     -58.003 -21.043-171.819  1.00209.69           C  
ANISOU 2104  CB  ARG A 290    34802  25130  19738   2571    551   -176       C  
ATOM   2105  CG  ARG A 290     -58.072 -22.406-172.498  1.00219.13           C  
ANISOU 2105  CG  ARG A 290    36234  26185  20840   2720    381   -243       C  
ATOM   2106  CD  ARG A 290     -56.756 -23.166-172.402  1.00225.11           C  
ANISOU 2106  CD  ARG A 290    36958  26995  21577   2850    514   -291       C  
ATOM   2107  NE  ARG A 290     -56.814 -24.456-173.089  1.00229.85           N  
ANISOU 2107  NE  ARG A 290    37805  27451  22074   3007    348   -361       N  
ATOM   2108  CZ  ARG A 290     -55.867 -25.389-173.033  1.00232.04           C  
ANISOU 2108  CZ  ARG A 290    38096  27740  22328   3137    394   -411       C  
ATOM   2109  NH1 ARG A 290     -54.766 -25.194-172.317  1.00231.86           N  
ANISOU 2109  NH1 ARG A 290    37842  27868  22383   3127    605   -396       N  
ATOM   2110  NH2 ARG A 290     -56.022 -26.526-173.696  1.00236.03           N  
ANISOU 2110  NH2 ARG A 290    38850  28099  22730   3281    222   -476       N  
ATOM   2111  N   GLY A 291     -58.657 -18.801-169.852  1.00192.09           N  
ANISOU 2111  N   GLY A 291    32083  23123  17777   2212    671    -30       N  
ATOM   2112  CA  GLY A 291     -58.552 -17.445-169.322  1.00191.09           C  
ANISOU 2112  CA  GLY A 291    31783  23111  17711   2095    825     24       C  
ATOM   2113  C   GLY A 291     -59.157 -17.322-167.936  1.00190.48           C  
ANISOU 2113  C   GLY A 291    31468  23094  17812   1940    721     78       C  
ATOM   2114  O   GLY A 291     -59.115 -16.254-167.323  1.00188.11           O  
ANISOU 2114  O   GLY A 291    31010  22887  17575   1838    826    124       O  
ATOM   2115  N   ALA A 292     -59.716 -18.427-167.446  1.00193.18           N  
ANISOU 2115  N   ALA A 292    31790  23379  18228   1925    510     75       N  
ATOM   2116  CA  ALA A 292     -60.323 -18.489-166.117  1.00191.30           C  
ANISOU 2116  CA  ALA A 292    31331  23198  18157   1790    394    130       C  
ATOM   2117  C   ALA A 292     -59.286 -18.523-164.995  1.00191.09           C  
ANISOU 2117  C   ALA A 292    31059  23295  18248   1749    531    136       C  
ATOM   2118  O   ALA A 292     -59.597 -18.188-163.851  1.00188.44           O  
ANISOU 2118  O   ALA A 292    30518  23038  18043   1633    503    187       O  
ATOM   2119  CB  ALA A 292     -61.251 -19.692-166.020  1.00190.30           C  
ANISOU 2119  CB  ALA A 292    31269  22966  18067   1787    118    134       C  
ATOM   2120  N   ILE A 293     -58.059 -18.918-165.335  1.00195.25           N  
ANISOU 2120  N   ILE A 293    31613  23844  18726   1852    678     87       N  
ATOM   2121  CA  ILE A 293     -56.965 -19.080-164.369  1.00196.69           C  
ANISOU 2121  CA  ILE A 293    31579  24138  19014   1831    806     88       C  
ATOM   2122  C   ILE A 293     -56.601 -17.779-163.643  1.00198.28           C  
ANISOU 2122  C   ILE A 293    31585  24465  19288   1722    974    137       C  
ATOM   2123  O   ILE A 293     -56.081 -17.816-162.526  1.00201.53           O  
ANISOU 2123  O   ILE A 293    31780  24966  19825   1656   1020    157       O  
ATOM   2124  CB  ILE A 293     -55.718 -19.727-165.026  1.00199.22           C  
ANISOU 2124  CB  ILE A 293    31985  24458  19250   1980    940     29       C  
ATOM   2125  CG1 ILE A 293     -56.074 -21.112-165.581  1.00201.90           C  
ANISOU 2125  CG1 ILE A 293    32513  24669  19530   2088    750    -23       C  
ATOM   2126  CG2 ILE A 293     -54.564 -19.847-164.035  1.00195.94           C  
ANISOU 2126  CG2 ILE A 293    31337  24163  18946   1955   1078     35       C  
ATOM   2127  CD1 ILE A 293     -55.121 -21.629-166.638  1.00207.93           C  
ANISOU 2127  CD1 ILE A 293    33453  25400  20151   2269    863    -86       C  
ATOM   2128  N   TYR A 294     -56.884 -16.637-164.268  1.00200.16           N  
ANISOU 2128  N   TYR A 294    31904  24701  19447   1702   1056    157       N  
ATOM   2129  CA  TYR A 294     -56.694 -15.342-163.610  1.00200.02           C  
ANISOU 2129  CA  TYR A 294    31724  24782  19491   1593   1185    207       C  
ATOM   2130  C   TYR A 294     -57.732 -15.111-162.507  1.00198.33           C  
ANISOU 2130  C   TYR A 294    31368  24590  19396   1469   1036    256       C  
ATOM   2131  O   TYR A 294     -57.376 -14.754-161.381  1.00195.39           O  
ANISOU 2131  O   TYR A 294    30787  24311  19138   1385   1089    285       O  
ATOM   2132  CB  TYR A 294     -56.709 -14.185-164.620  1.00200.38           C  
ANISOU 2132  CB  TYR A 294    31907  24813  19412   1610   1308    216       C  
ATOM   2133  CG  TYR A 294     -56.792 -12.813-163.973  1.00199.05           C  
ANISOU 2133  CG  TYR A 294    31603  24723  19302   1490   1393    270       C  
ATOM   2134  CD1 TYR A 294     -55.683 -12.250-163.336  1.00199.02           C  
ANISOU 2134  CD1 TYR A 294    31426  24823  19366   1443   1569    292       C  
ATOM   2135  CD2 TYR A 294     -57.981 -12.083-163.990  1.00196.43           C  
ANISOU 2135  CD2 TYR A 294    31319  24356  18957   1426   1290    301       C  
ATOM   2136  CE1 TYR A 294     -55.757 -11.000-162.738  1.00197.09           C  
ANISOU 2136  CE1 TYR A 294    31072  24638  19172   1335   1631    339       C  
ATOM   2137  CE2 TYR A 294     -58.065 -10.833-163.395  1.00194.67           C  
ANISOU 2137  CE2 TYR A 294    30986  24197  18779   1326   1360    346       C  
ATOM   2138  CZ  TYR A 294     -56.952 -10.297-162.772  1.00196.00           C  
ANISOU 2138  CZ  TYR A 294    30996  24461  19013   1281   1527    363       C  
ATOM   2139  OH  TYR A 294     -57.031  -9.056-162.181  1.00195.19           O  
ANISOU 2139  OH  TYR A 294    30799  24412  18953   1185   1583    407       O  
ATOM   2140  N   TYR A 295     -59.007 -15.323-162.839  1.00200.25           N  
ANISOU 2140  N   TYR A 295    31727  24749  19608   1461    848    267       N  
ATOM   2141  CA  TYR A 295     -60.118 -15.119-161.899  1.00199.67           C  
ANISOU 2141  CA  TYR A 295    31533  24697  19633   1356    699    323       C  
ATOM   2142  C   TYR A 295     -60.189 -16.209-160.827  1.00196.47           C  
ANISOU 2142  C   TYR A 295    30974  24315  19357   1323    571    334       C  
ATOM   2143  O   TYR A 295     -61.032 -16.159-159.926  1.00193.55           O  
ANISOU 2143  O   TYR A 295    30480  23978  19080   1240    451    388       O  
ATOM   2144  CB  TYR A 295     -61.454 -15.023-162.647  1.00205.12           C  
ANISOU 2144  CB  TYR A 295    32392  25292  20249   1360    537    341       C  
ATOM   2145  CG  TYR A 295     -61.482 -13.968-163.730  1.00207.03           C  
ANISOU 2145  CG  TYR A 295    32797  25503  20359   1393    646    331       C  
ATOM   2146  CD1 TYR A 295     -61.816 -12.646-163.438  1.00204.78           C  
ANISOU 2146  CD1 TYR A 295    32451  25273  20082   1319    715    374       C  
ATOM   2147  CD2 TYR A 295     -61.172 -14.293-165.047  1.00211.82           C  
ANISOU 2147  CD2 TYR A 295    33628  26023  20829   1503    679    280       C  
ATOM   2148  CE1 TYR A 295     -61.840 -11.679-164.430  1.00208.14           C  
ANISOU 2148  CE1 TYR A 295    33029  25666  20387   1345    811    367       C  
ATOM   2149  CE2 TYR A 295     -61.193 -13.335-166.046  1.00216.86           C  
ANISOU 2149  CE2 TYR A 295    34418  26633  21344   1533    780    274       C  
ATOM   2150  CZ  TYR A 295     -61.527 -12.030-165.735  1.00215.13           C  
ANISOU 2150  CZ  TYR A 295    34130  26468  21140   1450    845    319       C  
ATOM   2151  OH  TYR A 295     -61.545 -11.083-166.735  1.00217.97           O  
ANISOU 2151  OH  TYR A 295    34644  26796  21376   1478    941    315       O  
ATOM   2152  N   PHE A 296     -59.297 -17.190-160.942  1.00193.07           N  
ANISOU 2152  N   PHE A 296    30556  23871  18928   1396    601    286       N  
ATOM   2153  CA  PHE A 296     -59.173 -18.271-159.976  1.00185.55           C  
ANISOU 2153  CA  PHE A 296    29466  22939  18092   1375    498    289       C  
ATOM   2154  C   PHE A 296     -58.100 -17.937-158.946  1.00184.65           C  
ANISOU 2154  C   PHE A 296    29134  22947  18077   1330    658    295       C  
ATOM   2155  O   PHE A 296     -58.351 -18.010-157.742  1.00187.90           O  
ANISOU 2155  O   PHE A 296    29360  23421  18611   1247    596    335       O  
ATOM   2156  CB  PHE A 296     -58.854 -19.582-160.698  1.00183.28           C  
ANISOU 2156  CB  PHE A 296    29332  22558  17747   1487    421    231       C  
ATOM   2157  CG  PHE A 296     -58.612 -20.746-159.782  1.00177.99           C  
ANISOU 2157  CG  PHE A 296    28536  21902  17190   1475    321    228       C  
ATOM   2158  CD1 PHE A 296     -59.666 -21.345-159.101  1.00175.23           C  
ANISOU 2158  CD1 PHE A 296    28122  21526  16929   1402    101    277       C  
ATOM   2159  CD2 PHE A 296     -57.329 -21.259-159.618  1.00176.63           C  
ANISOU 2159  CD2 PHE A 296    28308  21770  17033   1539    444    182       C  
ATOM   2160  CE1 PHE A 296     -59.444 -22.425-158.263  1.00173.61           C  
ANISOU 2160  CE1 PHE A 296    27804  21331  16827   1389      6    278       C  
ATOM   2161  CE2 PHE A 296     -57.100 -22.340-158.785  1.00174.90           C  
ANISOU 2161  CE2 PHE A 296    27979  21559  16916   1531    349    177       C  
ATOM   2162  CZ  PHE A 296     -58.160 -22.924-158.107  1.00174.16           C  
ANISOU 2162  CZ  PHE A 296    27827  21434  16909   1454    128    224       C  
ATOM   2163  N   LYS A 297     -56.913 -17.559-159.423  1.00183.31           N  
ANISOU 2163  N   LYS A 297    28986  22812  17852   1387    860    260       N  
ATOM   2164  CA  LYS A 297     -55.803 -17.184-158.543  1.00181.29           C  
ANISOU 2164  CA  LYS A 297    28529  22666  17684   1345   1020    268       C  
ATOM   2165  C   LYS A 297     -56.051 -15.860-157.803  1.00177.77           C  
ANISOU 2165  C   LYS A 297    27952  22297  17294   1233   1082    321       C  
ATOM   2166  O   LYS A 297     -55.372 -15.556-156.822  1.00175.63           O  
ANISOU 2166  O   LYS A 297    27496  22115  17120   1174   1166    339       O  
ATOM   2167  CB  LYS A 297     -54.473 -17.153-159.310  1.00182.65           C  
ANISOU 2167  CB  LYS A 297    28758  22858  17781   1438   1218    229       C  
ATOM   2168  CG  LYS A 297     -54.335 -16.017-160.310  1.00186.33           C  
ANISOU 2168  CG  LYS A 297    29346  23319  18129   1458   1361    236       C  
ATOM   2169  CD  LYS A 297     -52.959 -16.012-160.951  1.00190.49           C  
ANISOU 2169  CD  LYS A 297    29897  23885  18593   1547   1565    213       C  
ATOM   2170  CE  LYS A 297     -52.832 -14.878-161.953  1.00193.56           C  
ANISOU 2170  CE  LYS A 297    30406  24270  18864   1562   1706    230       C  
ATOM   2171  NZ  LYS A 297     -51.516 -14.891-162.646  1.00196.47           N  
ANISOU 2171  NZ  LYS A 297    30800  24683  19164   1657   1908    219       N  
ATOM   2172  N   ILE A 298     -57.021 -15.083-158.279  1.00176.84           N  
ANISOU 2172  N   ILE A 298    27937  22141  17111   1207   1034    346       N  
ATOM   2173  CA  ILE A 298     -57.433 -13.851-157.605  1.00173.43           C  
ANISOU 2173  CA  ILE A 298    27404  21768  16720   1111   1064    395       C  
ATOM   2174  C   ILE A 298     -58.566 -14.142-156.615  1.00166.68           C  
ANISOU 2174  C   ILE A 298    26447  20925  15956   1045    881    439       C  
ATOM   2175  O   ILE A 298     -58.934 -13.292-155.802  1.00163.17           O  
ANISOU 2175  O   ILE A 298    25891  20541  15563    971    885    482       O  
ATOM   2176  CB  ILE A 298     -57.828 -12.746-158.623  1.00176.91           C  
ANISOU 2176  CB  ILE A 298    28006  22169  17041   1120   1125    402       C  
ATOM   2177  CG1 ILE A 298     -57.621 -11.349-158.024  1.00176.02           C  
ANISOU 2177  CG1 ILE A 298    27789  22129  16961   1037   1236    439       C  
ATOM   2178  CG2 ILE A 298     -59.256 -12.934-159.126  1.00178.08           C  
ANISOU 2178  CG2 ILE A 298    28289  22236  17136   1130    945    416       C  
ATOM   2179  CD1 ILE A 298     -57.526 -10.241-159.052  1.00177.01           C  
ANISOU 2179  CD1 ILE A 298    28058  22226  16969   1051   1351    440       C  
ATOM   2180  N   ALA A 299     -59.108 -15.355-156.697  1.00163.95           N  
ANISOU 2180  N   ALA A 299    26143  20522  15625   1078    717    432       N  
ATOM   2181  CA  ALA A 299     -60.164 -15.807-155.797  1.00161.40           C  
ANISOU 2181  CA  ALA A 299    25719  20213  15391   1020    534    484       C  
ATOM   2182  C   ALA A 299     -59.626 -16.792-154.761  1.00158.03           C  
ANISOU 2182  C   ALA A 299    25128  19832  15082   1004    497    481       C  
ATOM   2183  O   ALA A 299     -60.268 -17.038-153.739  1.00159.58           O  
ANISOU 2183  O   ALA A 299    25188  20071  15372    944    383    532       O  
ATOM   2184  CB  ALA A 299     -61.305 -16.429-156.586  1.00163.70           C  
ANISOU 2184  CB  ALA A 299    26170  20404  15624   1051    348    494       C  
ATOM   2185  N   VAL A 300     -58.450 -17.351-155.038  1.00154.59           N  
ANISOU 2185  N   VAL A 300    24707  19390  14638   1062    596    425       N  
ATOM   2186  CA  VAL A 300     -57.760 -18.244-154.105  1.00150.46           C  
ANISOU 2186  CA  VAL A 300    24032  18912  14221   1054    585    415       C  
ATOM   2187  C   VAL A 300     -56.813 -17.445-153.201  1.00149.99           C  
ANISOU 2187  C   VAL A 300    23794  18960  14234   1002    749    423       C  
ATOM   2188  O   VAL A 300     -56.548 -17.841-152.064  1.00151.37           O  
ANISOU 2188  O   VAL A 300    23798  19195  14520    959    723    439       O  
ATOM   2189  CB  VAL A 300     -57.049 -19.403-154.852  1.00148.77           C  
ANISOU 2189  CB  VAL A 300    23930  18631  13962   1156    582    352       C  
ATOM   2190  CG1 VAL A 300     -55.948 -20.038-154.016  1.00145.69           C  
ANISOU 2190  CG1 VAL A 300    23384  18303  13667   1160    645    331       C  
ATOM   2191  CG2 VAL A 300     -58.065 -20.458-155.261  1.00148.31           C  
ANISOU 2191  CG2 VAL A 300    23996  18471  13884   1183    359    357       C  
ATOM   2192  N   ALA A 301     -56.331 -16.308-153.699  1.00149.97           N  
ANISOU 2192  N   ALA A 301    23835  18978  14168   1001    910    417       N  
ATOM   2193  CA  ALA A 301     -55.516 -15.392-152.898  1.00146.97           C  
ANISOU 2193  CA  ALA A 301    23301  18690  13850    941   1054    433       C  
ATOM   2194  C   ALA A 301     -56.339 -14.737-151.795  1.00145.67           C  
ANISOU 2194  C   ALA A 301    23015  18577  13756    854    980    488       C  
ATOM   2195  O   ALA A 301     -55.793 -14.338-150.767  1.00150.33           O  
ANISOU 2195  O   ALA A 301    23445  19241  14429    799   1039    504       O  
ATOM   2196  CB  ALA A 301     -54.870 -14.336-153.776  1.00148.87           C  
ANISOU 2196  CB  ALA A 301    23631  18930  14001    958   1229    422       C  
ATOM   2197  N   LEU A 302     -57.647 -14.622-152.021  1.00143.23           N  
ANISOU 2197  N   LEU A 302    22783  18229  13408    846    849    519       N  
ATOM   2198  CA  LEU A 302     -58.585 -14.181-150.989  1.00139.68           C  
ANISOU 2198  CA  LEU A 302    22222  17830  13018    782    756    578       C  
ATOM   2199  C   LEU A 302     -58.800 -15.292-149.956  1.00141.30           C  
ANISOU 2199  C   LEU A 302    22287  18066  13332    762    629    600       C  
ATOM   2200  O   LEU A 302     -58.928 -15.025-148.759  1.00140.04           O  
ANISOU 2200  O   LEU A 302    21971  17982  13254    711    612    638       O  
ATOM   2201  CB  LEU A 302     -59.920 -13.759-151.610  1.00132.58           C  
ANISOU 2201  CB  LEU A 302    21448  16884  12042    787    655    611       C  
ATOM   2202  CG  LEU A 302     -61.056 -13.375-150.656  1.00128.16           C  
ANISOU 2202  CG  LEU A 302    20787  16378  11530    738    545    682       C  
ATOM   2203  CD1 LEU A 302     -60.755 -12.078-149.917  1.00124.88           C  
ANISOU 2203  CD1 LEU A 302    20284  16035  11130    696    655    697       C  
ATOM   2204  CD2 LEU A 302     -62.374 -13.284-151.406  1.00127.03           C  
ANISOU 2204  CD2 LEU A 302    20773  16179  11314    754    423    716       C  
ATOM   2205  N   ALA A 303     -58.830 -16.535-150.431  1.00143.07           N  
ANISOU 2205  N   ALA A 303    22575  18229  13553    807    538    577       N  
ATOM   2206  CA  ALA A 303     -58.965 -17.701-149.563  1.00141.79           C  
ANISOU 2206  CA  ALA A 303    22297  18086  13491    792    413    596       C  
ATOM   2207  C   ALA A 303     -57.748 -17.889-148.655  1.00139.60           C  
ANISOU 2207  C   ALA A 303    21862  17877  13303    776    514    572       C  
ATOM   2208  O   ALA A 303     -57.831 -18.564-147.631  1.00141.66           O  
ANISOU 2208  O   ALA A 303    21985  18177  13660    745    431    598       O  
ATOM   2209  CB  ALA A 303     -59.213 -18.953-150.392  1.00144.41           C  
ANISOU 2209  CB  ALA A 303    22760  18320  13788    848    289    571       C  
ATOM   2210  N   VAL A 304     -56.623 -17.290-149.036  1.00136.92           N  
ANISOU 2210  N   VAL A 304    21541  17551  12931    795    691    528       N  
ATOM   2211  CA  VAL A 304     -55.409 -17.334-148.229  1.00136.76           C  
ANISOU 2211  CA  VAL A 304    21371  17597  12993    777    799    509       C  
ATOM   2212  C   VAL A 304     -55.342 -16.129-147.291  1.00138.06           C  
ANISOU 2212  C   VAL A 304    21413  17839  13202    705    869    545       C  
ATOM   2213  O   VAL A 304     -54.837 -16.228-146.171  1.00140.71           O  
ANISOU 2213  O   VAL A 304    21589  18239  13635    666    882    555       O  
ATOM   2214  CB  VAL A 304     -54.149 -17.423-149.119  1.00138.53           C  
ANISOU 2214  CB  VAL A 304    21666  17800  13166    839    952    452       C  
ATOM   2215  CG1 VAL A 304     -52.877 -17.167-148.324  1.00137.51           C  
ANISOU 2215  CG1 VAL A 304    21377  17749  13119    808   1083    445       C  
ATOM   2216  CG2 VAL A 304     -54.078 -18.787-149.785  1.00142.18           C  
ANISOU 2216  CG2 VAL A 304    22227  18193  13600    920    873    412       C  
ATOM   2217  N   ALA A 305     -55.878 -15.002-147.747  1.00140.04           N  
ANISOU 2217  N   ALA A 305    21748  18079  13379    691    903    563       N  
ATOM   2218  CA  ALA A 305     -55.785 -13.746-147.006  1.00141.85           C  
ANISOU 2218  CA  ALA A 305    21896  18368  13631    632    973    591       C  
ATOM   2219  C   ALA A 305     -56.887 -13.539-145.968  1.00140.32           C  
ANISOU 2219  C   ALA A 305    21615  18218  13479    595    852    647       C  
ATOM   2220  O   ALA A 305     -56.664 -12.877-144.954  1.00139.29           O  
ANISOU 2220  O   ALA A 305    21372  18149  13402    552    885    667       O  
ATOM   2221  CB  ALA A 305     -55.744 -12.570-147.970  1.00145.12           C  
ANISOU 2221  CB  ALA A 305    22444  18751  13943    637   1076    584       C  
ATOM   2222  N   ALA A 306     -58.067 -14.101-146.222  1.00142.24           N  
ANISOU 2222  N   ALA A 306    21913  18431  13699    614    710    677       N  
ATOM   2223  CA  ALA A 306     -59.237 -13.864-145.370  1.00145.36           C  
ANISOU 2223  CA  ALA A 306    22234  18873  14120    589    596    744       C  
ATOM   2224  C   ALA A 306     -59.588 -15.031-144.447  1.00147.31           C  
ANISOU 2224  C   ALA A 306    22352  19155  14461    578    467    779       C  
ATOM   2225  O   ALA A 306     -60.327 -14.856-143.475  1.00148.11           O  
ANISOU 2225  O   ALA A 306    22351  19321  14603    555    394    840       O  
ATOM   2226  CB  ALA A 306     -60.442 -13.476-146.216  1.00144.28           C  
ANISOU 2226  CB  ALA A 306    22234  18692  13893    609    524    773       C  
ATOM   2227  N   ILE A 307     -59.065 -16.214-144.753  1.00148.63           N  
ANISOU 2227  N   ILE A 307    22530  19282  14659    598    437    745       N  
ATOM   2228  CA  ILE A 307     -59.326 -17.398-143.942  1.00151.11           C  
ANISOU 2228  CA  ILE A 307    22731  19620  15064    585    310    777       C  
ATOM   2229  C   ILE A 307     -58.115 -17.729-143.068  1.00153.74           C  
ANISOU 2229  C   ILE A 307    22929  20000  15485    570    386    744       C  
ATOM   2230  O   ILE A 307     -57.005 -17.900-143.585  1.00152.17           O  
ANISOU 2230  O   ILE A 307    22768  19771  15276    594    489    680       O  
ATOM   2231  CB  ILE A 307     -59.747 -18.609-144.807  1.00153.70           C  
ANISOU 2231  CB  ILE A 307    23167  19862  15370    618    185    770       C  
ATOM   2232  CG1 ILE A 307     -61.148 -18.378-145.384  1.00156.95           C  
ANISOU 2232  CG1 ILE A 307    23674  20239  15718    618     70    826       C  
ATOM   2233  CG2 ILE A 307     -59.718 -19.901-143.996  1.00153.70           C  
ANISOU 2233  CG2 ILE A 307    23052  19876  15469    603     68    792       C  
ATOM   2234  CD1 ILE A 307     -61.478 -19.217-146.603  1.00161.53           C  
ANISOU 2234  CD1 ILE A 307    24423  20710  16241    658    -26    803       C  
ATOM   2235  N   PRO A 308     -58.327 -17.801-141.736  1.00155.18           N  
ANISOU 2235  N   PRO A 308    22950  20259  15750    533    337    791       N  
ATOM   2236  CA  PRO A 308     -57.274 -18.161-140.798  1.00152.63           C  
ANISOU 2236  CA  PRO A 308    22490  19983  15518    516    388    767       C  
ATOM   2237  C   PRO A 308     -57.246 -19.665-140.530  1.00154.91           C  
ANISOU 2237  C   PRO A 308    22728  20254  15876    522    274    771       C  
ATOM   2238  O   PRO A 308     -58.130 -20.190-139.852  1.00151.49           O  
ANISOU 2238  O   PRO A 308    22221  19851  15488    502    141    836       O  
ATOM   2239  CB  PRO A 308     -57.660 -17.389-139.528  1.00148.83           C  
ANISOU 2239  CB  PRO A 308    21882  19590  15076    480    384    821       C  
ATOM   2240  CG  PRO A 308     -59.100 -16.993-139.699  1.00147.86           C  
ANISOU 2240  CG  PRO A 308    21809  19474  14897    485    291    887       C  
ATOM   2241  CD  PRO A 308     -59.582 -17.483-141.031  1.00151.34           C  
ANISOU 2241  CD  PRO A 308    22402  19827  15271    513    235    875       C  
ATOM   2242  N   GLU A 309     -56.245 -20.347-141.083  1.00163.47           N  
ANISOU 2242  N   GLU A 309    23854  21291  16965    554    325    705       N  
ATOM   2243  CA  GLU A 309     -56.049 -21.776-140.841  1.00168.37           C  
ANISOU 2243  CA  GLU A 309    24435  21887  17650    567    224    697       C  
ATOM   2244  C   GLU A 309     -55.053 -21.986-139.708  1.00165.19           C  
ANISOU 2244  C   GLU A 309    23869  21549  17345    544    280    682       C  
ATOM   2245  O   GLU A 309     -53.911 -21.527-139.779  1.00164.52           O  
ANISOU 2245  O   GLU A 309    23765  21479  17264    553    424    632       O  
ATOM   2246  CB  GLU A 309     -55.591 -22.499-142.114  1.00176.57           C  
ANISOU 2246  CB  GLU A 309    25626  22832  18628    631    232    633       C  
ATOM   2247  CG  GLU A 309     -56.725 -22.984-143.013  1.00183.80           C  
ANISOU 2247  CG  GLU A 309    26687  23666  19479    652     89    657       C  
ATOM   2248  CD  GLU A 309     -57.327 -24.311-142.564  1.00186.67           C  
ANISOU 2248  CD  GLU A 309    27012  24004  19909    638   -102    698       C  
ATOM   2249  OE1 GLU A 309     -57.860 -24.391-141.435  1.00186.55           O  
ANISOU 2249  OE1 GLU A 309    26851  24057  19971    583   -178    767       O  
ATOM   2250  OE2 GLU A 309     -57.279 -25.279-143.353  1.00188.56           O  
ANISOU 2250  OE2 GLU A 309    27372  24153  20118    685   -182    664       O  
ATOM   2251  N   GLY A 310     -55.500 -22.676-138.662  1.00163.99           N  
ANISOU 2251  N   GLY A 310    23596  21436  17274    513    161    733       N  
ATOM   2252  CA  GLY A 310     -54.729 -22.808-137.429  1.00162.86           C  
ANISOU 2252  CA  GLY A 310    23289  21361  17227    486    197    731       C  
ATOM   2253  C   GLY A 310     -54.942 -21.590-136.548  1.00160.93           C  
ANISOU 2253  C   GLY A 310    22958  21197  16991    447    254    769       C  
ATOM   2254  O   GLY A 310     -55.095 -20.474-137.054  1.00163.77           O  
ANISOU 2254  O   GLY A 310    23392  21553  17280    449    334    764       O  
ATOM   2255  N   LEU A 311     -54.958 -21.805-135.233  1.00156.46           N  
ANISOU 2255  N   LEU A 311    22242  20699  16506    417    209    807       N  
ATOM   2256  CA  LEU A 311     -55.173 -20.730-134.260  1.00148.17           C  
ANISOU 2256  CA  LEU A 311    21108  19725  15463    391    248    845       C  
ATOM   2257  C   LEU A 311     -54.215 -19.556-134.465  1.00146.07           C  
ANISOU 2257  C   LEU A 311    20869  19460  15169    386    406    792       C  
ATOM   2258  O   LEU A 311     -52.995 -19.751-134.481  1.00144.89           O  
ANISOU 2258  O   LEU A 311    20688  19301  15062    383    488    738       O  
ATOM   2259  CB  LEU A 311     -55.018 -21.253-132.832  1.00144.10           C  
ANISOU 2259  CB  LEU A 311    20430  19277  15044    368    193    878       C  
ATOM   2260  CG  LEU A 311     -54.981 -20.161-131.762  1.00140.90           C  
ANISOU 2260  CG  LEU A 311    19943  18946  14647    351    245    902       C  
ATOM   2261  CD1 LEU A 311     -56.338 -20.025-131.095  1.00142.25           C  
ANISOU 2261  CD1 LEU A 311    20070  19179  14800    355    143    994       C  
ATOM   2262  CD2 LEU A 311     -53.895 -20.444-130.740  1.00140.47           C  
ANISOU 2262  CD2 LEU A 311    19762  18925  14682    332    279    874       C  
ATOM   2263  N   PRO A 312     -54.766 -18.333-134.611  1.00143.87           N  
ANISOU 2263  N   PRO A 312    20648  19194  14822    383    444    813       N  
ATOM   2264  CA  PRO A 312     -53.960 -17.119-134.760  1.00143.69           C  
ANISOU 2264  CA  PRO A 312    20654  19168  14771    369    579    776       C  
ATOM   2265  C   PRO A 312     -52.855 -17.020-133.703  1.00144.63           C  
ANISOU 2265  C   PRO A 312    20646  19329  14975    339    633    756       C  
ATOM   2266  O   PRO A 312     -53.089 -17.311-132.525  1.00146.27           O  
ANISOU 2266  O   PRO A 312    20742  19591  15242    329    564    790       O  
ATOM   2267  CB  PRO A 312     -54.986 -16.002-134.583  1.00140.10           C  
ANISOU 2267  CB  PRO A 312    20242  18740  14248    371    561    822       C  
ATOM   2268  CG  PRO A 312     -56.258 -16.595-135.080  1.00139.42           C  
ANISOU 2268  CG  PRO A 312    20211  18640  14122    396    449    868       C  
ATOM   2269  CD  PRO A 312     -56.212 -18.043-134.682  1.00140.75           C  
ANISOU 2269  CD  PRO A 312    20295  18814  14370    394    355    880       C  
ATOM   2270  N   ALA A 313     -51.663 -16.620-134.140  1.00144.53           N  
ANISOU 2270  N   ALA A 313    20650  19293  14970    325    753    706       N  
ATOM   2271  CA  ALA A 313     -50.469 -16.618-133.294  1.00143.63           C  
ANISOU 2271  CA  ALA A 313    20418  19209  14945    294    806    685       C  
ATOM   2272  C   ALA A 313     -50.529 -15.621-132.138  1.00143.35           C  
ANISOU 2272  C   ALA A 313    20319  19218  14927    262    801    712       C  
ATOM   2273  O   ALA A 313     -49.954 -15.865-131.079  1.00145.68           O  
ANISOU 2273  O   ALA A 313    20498  19550  15304    241    786    712       O  
ATOM   2274  CB  ALA A 313     -49.228 -16.379-134.137  1.00145.43           C  
ANISOU 2274  CB  ALA A 313    20680  19405  15171    287    937    640       C  
ATOM   2275  N   VAL A 314     -51.228 -14.507-132.348  1.00142.53           N  
ANISOU 2275  N   VAL A 314    20302  19109  14744    264    810    733       N  
ATOM   2276  CA  VAL A 314     -51.342 -13.446-131.338  1.00140.29           C  
ANISOU 2276  CA  VAL A 314    19988  18857  14458    247    803    755       C  
ATOM   2277  C   VAL A 314     -52.243 -13.858-130.161  1.00140.27           C  
ANISOU 2277  C   VAL A 314    19903  18916  14477    271    691    802       C  
ATOM   2278  O   VAL A 314     -52.102 -13.328-129.052  1.00142.89           O  
ANISOU 2278  O   VAL A 314    20174  19283  14832    264    675    815       O  
ATOM   2279  CB  VAL A 314     -51.800 -12.107-131.969  1.00137.97           C  
ANISOU 2279  CB  VAL A 314    19823  18533  14064    249    845    760       C  
ATOM   2280  CG1 VAL A 314     -51.839 -10.985-130.939  1.00137.15           C  
ANISOU 2280  CG1 VAL A 314    19705  18453  13953    238    834    777       C  
ATOM   2281  CG2 VAL A 314     -50.883 -11.720-133.121  1.00137.96           C  
ANISOU 2281  CG2 VAL A 314    19897  18477  14043    223    959    723       C  
ATOM   2282  N   ILE A 315     -53.148 -14.810-130.397  1.00136.27           N  
ANISOU 2282  N   ILE A 315    19393  18421  13962    300    609    832       N  
ATOM   2283  CA  ILE A 315     -53.972 -15.375-129.322  1.00133.28           C  
ANISOU 2283  CA  ILE A 315    18920  18107  13612    321    502    890       C  
ATOM   2284  C   ILE A 315     -53.092 -16.023-128.246  1.00135.83           C  
ANISOU 2284  C   ILE A 315    19108  18461  14038    299    491    877       C  
ATOM   2285  O   ILE A 315     -53.180 -15.663-127.067  1.00134.60           O  
ANISOU 2285  O   ILE A 315    18883  18357  13902    304    463    902       O  
ATOM   2286  CB  ILE A 315     -55.048 -16.355-129.857  1.00129.13           C  
ANISOU 2286  CB  ILE A 315    18413  17581  13068    345    409    933       C  
ATOM   2287  CG1 ILE A 315     -56.222 -15.563-130.444  1.00128.06           C  
ANISOU 2287  CG1 ILE A 315    18381  17444  12831    374    392    972       C  
ATOM   2288  CG2 ILE A 315     -55.548 -17.286-128.755  1.00125.58           C  
ANISOU 2288  CG2 ILE A 315    17837  17196  12681    351    303    992       C  
ATOM   2289  CD1 ILE A 315     -57.189 -16.386-131.270  1.00129.38           C  
ANISOU 2289  CD1 ILE A 315    18596  17589  12972    389    309   1009       C  
ATOM   2290  N   THR A 316     -52.229 -16.951-128.656  1.00137.35           N  
ANISOU 2290  N   THR A 316    19271  18621  14292    281    513    835       N  
ATOM   2291  CA  THR A 316     -51.322 -17.608-127.713  1.00136.44           C  
ANISOU 2291  CA  THR A 316    19032  18531  14278    260    504    819       C  
ATOM   2292  C   THR A 316     -50.234 -16.674-127.194  1.00135.95           C  
ANISOU 2292  C   THR A 316    18940  18468  14245    228    586    786       C  
ATOM   2293  O   THR A 316     -49.701 -16.897-126.110  1.00139.66           O  
ANISOU 2293  O   THR A 316    19304  18970  14787    213    563    786       O  
ATOM   2294  CB  THR A 316     -50.694 -18.904-128.277  1.00134.81           C  
ANISOU 2294  CB  THR A 316    18802  18290  14127    260    501    784       C  
ATOM   2295  OG1 THR A 316     -50.700 -18.866-129.709  1.00136.25           O  
ANISOU 2295  OG1 THR A 316    19106  18413  14247    275    552    755       O  
ATOM   2296  CG2 THR A 316     -51.482 -20.121-127.809  1.00135.00           C  
ANISOU 2296  CG2 THR A 316    18767  18341  14187    275    374    829       C  
ATOM   2297  N   THR A 317     -49.921 -15.626-127.957  1.00135.17           N  
ANISOU 2297  N   THR A 317    18935  18330  14092    214    672    762       N  
ATOM   2298  CA  THR A 317     -48.938 -14.628-127.528  1.00138.24           C  
ANISOU 2298  CA  THR A 317    19308  18711  14506    174    739    740       C  
ATOM   2299  C   THR A 317     -49.455 -13.817-126.338  1.00138.52           C  
ANISOU 2299  C   THR A 317    19325  18782  14521    183    685    772       C  
ATOM   2300  O   THR A 317     -48.700 -13.539-125.407  1.00140.48           O  
ANISOU 2300  O   THR A 317    19505  19041  14828    156    685    763       O  
ATOM   2301  CB  THR A 317     -48.508 -13.683-128.674  1.00140.94           C  
ANISOU 2301  CB  THR A 317    19759  19000  14792    152    841    717       C  
ATOM   2302  OG1 THR A 317     -48.094 -14.456-129.806  1.00144.53           O  
ANISOU 2302  OG1 THR A 317    20239  19425  15250    160    893    690       O  
ATOM   2303  CG2 THR A 317     -47.345 -12.784-128.242  1.00139.53           C  
ANISOU 2303  CG2 THR A 317    19548  18808  14657     97    903    702       C  
ATOM   2304  N   CYS A 318     -50.737 -13.456-126.356  1.00136.99           N  
ANISOU 2304  N   CYS A 318    19195  18609  14246    226    634    811       N  
ATOM   2305  CA  CYS A 318     -51.305 -12.679-125.247  1.00136.60           C  
ANISOU 2305  CA  CYS A 318    19139  18600  14161    254    584    843       C  
ATOM   2306  C   CYS A 318     -51.717 -13.513-124.021  1.00131.16           C  
ANISOU 2306  C   CYS A 318    18333  17980  13519    283    496    882       C  
ATOM   2307  O   CYS A 318     -51.859 -12.971-122.921  1.00127.65           O  
ANISOU 2307  O   CYS A 318    17863  17571  13064    307    462    901       O  
ATOM   2308  CB  CYS A 318     -52.423 -11.729-125.719  1.00137.83           C  
ANISOU 2308  CB  CYS A 318    19415  18753  14201    296    578    871       C  
ATOM   2309  SG  CYS A 318     -53.995 -12.476-126.206  1.00138.09           S  
ANISOU 2309  SG  CYS A 318    19463  18826  14177    351    506    931       S  
ATOM   2310  N   LEU A 319     -51.889 -14.824-124.217  1.00125.73           N  
ANISOU 2310  N   LEU A 319    17581  17309  12881    284    457    895       N  
ATOM   2311  CA  LEU A 319     -52.081 -15.768-123.107  1.00121.45           C  
ANISOU 2311  CA  LEU A 319    16916  16827  12401    298    378    931       C  
ATOM   2312  C   LEU A 319     -50.763 -16.042-122.379  1.00121.11           C  
ANISOU 2312  C   LEU A 319    16784  16777  12456    258    399    888       C  
ATOM   2313  O   LEU A 319     -50.714 -16.035-121.144  1.00122.04           O  
ANISOU 2313  O   LEU A 319    16827  16938  12603    271    354    908       O  
ATOM   2314  CB  LEU A 319     -52.678 -17.096-123.586  1.00116.26           C  
ANISOU 2314  CB  LEU A 319    16227  16180  11767    305    318    961       C  
ATOM   2315  CG  LEU A 319     -52.802 -18.163-122.484  1.00110.97           C  
ANISOU 2315  CG  LEU A 319    15426  15567  11170    310    233   1001       C  
ATOM   2316  CD1 LEU A 319     -54.196 -18.170-121.883  1.00109.80           C  
ANISOU 2316  CD1 LEU A 319    15252  15494  10971    358    152   1092       C  
ATOM   2317  CD2 LEU A 319     -52.444 -19.546-122.993  1.00109.41           C  
ANISOU 2317  CD2 LEU A 319    15190  15339  11042    286    203    984       C  
ATOM   2318  N   ALA A 320     -49.711 -16.308-123.153  1.00117.89           N  
ANISOU 2318  N   ALA A 320    16381  16314  12095    216    466    835       N  
ATOM   2319  CA  ALA A 320     -48.371 -16.495-122.612  1.00116.26           C  
ANISOU 2319  CA  ALA A 320    16091  16097  11983    175    497    795       C  
ATOM   2320  C   ALA A 320     -47.944 -15.273-121.810  1.00118.64           C  
ANISOU 2320  C   ALA A 320    16404  16397  12277    159    512    789       C  
ATOM   2321  O   ALA A 320     -47.411 -15.406-120.705  1.00120.42           O  
ANISOU 2321  O   ALA A 320    16544  16644  12565    148    478    788       O  
ATOM   2322  CB  ALA A 320     -47.378 -16.765-123.729  1.00115.64           C  
ANISOU 2322  CB  ALA A 320    16033  15967  11937    143    583    747       C  
ATOM   2323  N   LEU A 321     -48.199 -14.088-122.368  1.00119.15           N  
ANISOU 2323  N   LEU A 321    16580  16430  12261    159    554    787       N  
ATOM   2324  CA  LEU A 321     -47.859 -12.827-121.714  1.00120.48           C  
ANISOU 2324  CA  LEU A 321    16785  16580  12408    145    559    781       C  
ATOM   2325  C   LEU A 321     -48.691 -12.581-120.463  1.00119.53           C  
ANISOU 2325  C   LEU A 321    16652  16513  12250    202    475    819       C  
ATOM   2326  O   LEU A 321     -48.195 -12.028-119.481  1.00120.73           O  
ANISOU 2326  O   LEU A 321    16786  16662  12423    194    450    811       O  
ATOM   2327  CB  LEU A 321     -47.990 -11.652-122.687  1.00123.15           C  
ANISOU 2327  CB  LEU A 321    17258  16868  12665    133    618    772       C  
ATOM   2328  CG  LEU A 321     -46.825 -11.448-123.666  1.00126.24           C  
ANISOU 2328  CG  LEU A 321    17664  17203  13096     66    713    738       C  
ATOM   2329  CD1 LEU A 321     -47.227 -10.535-124.819  1.00126.67           C  
ANISOU 2329  CD1 LEU A 321    17855  17214  13057     66    768    738       C  
ATOM   2330  CD2 LEU A 321     -45.572 -10.929-122.965  1.00125.79           C  
ANISOU 2330  CD2 LEU A 321    17554  17122  13116      5    725    723       C  
ATOM   2331  N   GLY A 322     -49.949 -13.006-120.500  1.00118.15           N  
ANISOU 2331  N   GLY A 322    16484  16388  12018    261    429    863       N  
ATOM   2332  CA  GLY A 322     -50.829 -12.900-119.341  1.00118.47           C  
ANISOU 2332  CA  GLY A 322    16499  16496  12017    328    355    912       C  
ATOM   2333  C   GLY A 322     -50.386 -13.735-118.155  1.00115.98           C  
ANISOU 2333  C   GLY A 322    16056  16222  11786    326    303    920       C  
ATOM   2334  O   GLY A 322     -50.259 -13.227-117.040  1.00115.20           O  
ANISOU 2334  O   GLY A 322    15947  16143  11680    352    268    925       O  
ATOM   2335  N   THR A 323     -50.148 -15.018-118.403  1.00113.47           N  
ANISOU 2335  N   THR A 323    15652  15915  11547    299    294    920       N  
ATOM   2336  CA  THR A 323     -49.719 -15.947-117.364  1.00113.44           C  
ANISOU 2336  CA  THR A 323    15523  15947  11628    293    243    927       C  
ATOM   2337  C   THR A 323     -48.339 -15.591-116.811  1.00117.20           C  
ANISOU 2337  C   THR A 323    15968  16384  12179    244    267    875       C  
ATOM   2338  O   THR A 323     -48.063 -15.802-115.621  1.00116.37           O  
ANISOU 2338  O   THR A 323    15790  16309  12115    254    218    882       O  
ATOM   2339  CB  THR A 323     -49.686 -17.387-117.888  1.00111.46           C  
ANISOU 2339  CB  THR A 323    15202  15701  11445    271    226    932       C  
ATOM   2340  OG1 THR A 323     -48.915 -17.430-119.095  1.00111.04           O  
ANISOU 2340  OG1 THR A 323    15192  15580  11416    224    300    877       O  
ATOM   2341  CG2 THR A 323     -51.097 -17.892-118.157  1.00110.18           C  
ANISOU 2341  CG2 THR A 323    15048  15587  11226    315    171   1001       C  
ATOM   2342  N   ARG A 324     -47.479 -15.060-117.681  1.00120.90           N  
ANISOU 2342  N   ARG A 324    16486  16785  12663    190    342    827       N  
ATOM   2343  CA  ARG A 324     -46.162 -14.568-117.276  1.00124.66           C  
ANISOU 2343  CA  ARG A 324    16938  17219  13208    134    367    786       C  
ATOM   2344  C   ARG A 324     -46.290 -13.408-116.280  1.00118.50           C  
ANISOU 2344  C   ARG A 324    16212  16435  12377    158    325    794       C  
ATOM   2345  O   ARG A 324     -45.599 -13.387-115.264  1.00116.16           O  
ANISOU 2345  O   ARG A 324    15859  16137  12139    143    287    783       O  
ATOM   2346  CB  ARG A 324     -45.323 -14.181-118.506  1.00133.44           C  
ANISOU 2346  CB  ARG A 324    18095  18268  14336     74    459    750       C  
ATOM   2347  CG  ARG A 324     -43.935 -13.605-118.223  1.00145.40           C  
ANISOU 2347  CG  ARG A 324    19581  19739  15926      5    489    721       C  
ATOM   2348  CD  ARG A 324     -43.039 -14.534-117.411  1.00155.00           C  
ANISOU 2348  CD  ARG A 324    20660  20974  17258    -18    461    709       C  
ATOM   2349  NE  ARG A 324     -42.819 -15.830-118.056  1.00164.34           N  
ANISOU 2349  NE  ARG A 324    21772  22173  18495    -17    491    698       N  
ATOM   2350  CZ  ARG A 324     -41.969 -16.758-117.619  1.00169.50           C  
ANISOU 2350  CZ  ARG A 324    22309  22839  19251    -37    480    683       C  
ATOM   2351  NH1 ARG A 324     -41.234 -16.550-116.531  1.00167.76           N  
ANISOU 2351  NH1 ARG A 324    22024  22619  19098    -65    441    679       N  
ATOM   2352  NH2 ARG A 324     -41.847 -17.903-118.278  1.00170.95           N  
ANISOU 2352  NH2 ARG A 324    22449  23032  19469    -25    504    672       N  
ATOM   2353  N   ARG A 325     -47.189 -12.465-116.568  1.00112.82           N  
ANISOU 2353  N   ARG A 325    15606  15711  11546    202    327    812       N  
ATOM   2354  CA  ARG A 325     -47.503 -11.376-115.642  1.00110.57           C  
ANISOU 2354  CA  ARG A 325    15394  15426  11192    248    278    821       C  
ATOM   2355  C   ARG A 325     -48.026 -11.907-114.305  1.00108.84           C  
ANISOU 2355  C   ARG A 325    15104  15280  10969    316    201    856       C  
ATOM   2356  O   ARG A 325     -47.677 -11.390-113.243  1.00108.09           O  
ANISOU 2356  O   ARG A 325    15018  15176  10873    333    154    848       O  
ATOM   2357  CB  ARG A 325     -48.542 -10.430-116.248  1.00111.82           C  
ANISOU 2357  CB  ARG A 325    15684  15578  11222    300    292    840       C  
ATOM   2358  CG  ARG A 325     -48.056  -9.611-117.428  1.00112.98           C  
ANISOU 2358  CG  ARG A 325    15926  15648  11353    239    362    809       C  
ATOM   2359  CD  ARG A 325     -48.951  -8.405-117.664  1.00116.00           C  
ANISOU 2359  CD  ARG A 325    16452  16014  11605    295    356    822       C  
ATOM   2360  NE  ARG A 325     -50.310  -8.755-118.084  1.00117.23           N  
ANISOU 2360  NE  ARG A 325    16627  16230  11682    368    351    864       N  
ATOM   2361  CZ  ARG A 325     -50.732  -8.785-119.348  1.00120.36           C  
ANISOU 2361  CZ  ARG A 325    17076  16610  12043    356    402    866       C  
ATOM   2362  NH1 ARG A 325     -49.904  -8.496-120.345  1.00123.00           N  
ANISOU 2362  NH1 ARG A 325    17451  16874  12408    279    469    829       N  
ATOM   2363  NH2 ARG A 325     -51.990  -9.106-119.621  1.00119.29           N  
ANISOU 2363  NH2 ARG A 325    16952  16531  11839    422    383    911       N  
ATOM   2364  N   MET A 326     -48.867 -12.937-114.377  1.00107.52           N  
ANISOU 2364  N   MET A 326    14871  15182  10800    354    184    899       N  
ATOM   2365  CA  MET A 326     -49.467 -13.557-113.198  1.00105.39           C  
ANISOU 2365  CA  MET A 326    14523  14993  10525    419    115    948       C  
ATOM   2366  C   MET A 326     -48.414 -14.160-112.281  1.00103.60           C  
ANISOU 2366  C   MET A 326    14196  14761  10406    380     84    922       C  
ATOM   2367  O   MET A 326     -48.449 -13.967-111.064  1.00101.78           O  
ANISOU 2367  O   MET A 326    13949  14561  10161    427     29    937       O  
ATOM   2368  CB  MET A 326     -50.453 -14.650-113.608  1.00106.30           C  
ANISOU 2368  CB  MET A 326    14577  15175  10637    444    100   1004       C  
ATOM   2369  CG  MET A 326     -51.665 -14.164-114.378  1.00106.10           C  
ANISOU 2369  CG  MET A 326    14637  15171  10504    493    115   1044       C  
ATOM   2370  SD  MET A 326     -53.005 -15.355-114.242  1.00106.73           S  
ANISOU 2370  SD  MET A 326    14626  15354  10573    543     58   1142       S  
ATOM   2371  CE  MET A 326     -53.887 -15.021-115.760  1.00110.60           C  
ANISOU 2371  CE  MET A 326    15214  15821  10987    545     95   1157       C  
ATOM   2372  N   ALA A 327     -47.485 -14.901-112.872  1.00103.36           N  
ANISOU 2372  N   ALA A 327    14099  14693  10479    301    118    886       N  
ATOM   2373  CA  ALA A 327     -46.392 -15.486-112.114  1.00104.82           C  
ANISOU 2373  CA  ALA A 327    14184  14867  10773    257     94    859       C  
ATOM   2374  C   ALA A 327     -45.549 -14.389-111.458  1.00104.71           C  
ANISOU 2374  C   ALA A 327    14219  14799  10765    236     82    824       C  
ATOM   2375  O   ALA A 327     -45.168 -14.508-110.294  1.00103.06           O  
ANISOU 2375  O   ALA A 327    13962  14603  10593    247     24    824       O  
ATOM   2376  CB  ALA A 327     -45.548 -16.377-113.008  1.00105.19           C  
ANISOU 2376  CB  ALA A 327    14165  14882  10919    186    143    826       C  
ATOM   2377  N   LYS A 328     -45.296 -13.311-112.199  1.00107.47           N  
ANISOU 2377  N   LYS A 328    14670  15086  11075    204    128    800       N  
ATOM   2378  CA  LYS A 328     -44.559 -12.159-111.675  1.00109.91           C  
ANISOU 2378  CA  LYS A 328    15045  15331  11383    177    105    773       C  
ATOM   2379  C   LYS A 328     -45.418 -11.344-110.714  1.00107.40           C  
ANISOU 2379  C   LYS A 328    14818  15036  10954    271     39    795       C  
ATOM   2380  O   LYS A 328     -44.991 -10.297-110.237  1.00110.71           O  
ANISOU 2380  O   LYS A 328    15319  15397  11348    265      4    775       O  
ATOM   2381  CB  LYS A 328     -44.042 -11.256-112.805  1.00115.77           C  
ANISOU 2381  CB  LYS A 328    15871  15999  12118    110    171    748       C  
ATOM   2382  CG  LYS A 328     -43.268 -11.962-113.915  1.00125.50           C  
ANISOU 2382  CG  LYS A 328    17031  17214  13438     33    252    730       C  
ATOM   2383  CD  LYS A 328     -41.766 -12.038-113.667  1.00131.61           C  
ANISOU 2383  CD  LYS A 328    17723  17946  14335    -53    259    706       C  
ATOM   2384  CE  LYS A 328     -41.048 -12.616-114.884  1.00134.14           C  
ANISOU 2384  CE  LYS A 328    17987  18256  14724   -113    353    693       C  
ATOM   2385  NZ  LYS A 328     -39.601 -12.881-114.640  1.00134.80           N  
ANISOU 2385  NZ  LYS A 328    17964  18316  14935   -189    365    679       N  
ATOM   2386  N   LYS A 329     -46.634 -11.816-110.452  1.00103.01           N  
ANISOU 2386  N   LYS A 329    14248  14562  10327    360     20    841       N  
ATOM   2387  CA  LYS A 329     -47.480 -11.245-109.411  1.00100.14           C  
ANISOU 2387  CA  LYS A 329    13947  14242   9858    469    -40    873       C  
ATOM   2388  C   LYS A 329     -47.681 -12.262-108.295  1.00 99.33           C  
ANISOU 2388  C   LYS A 329    13731  14219   9790    515    -93    907       C  
ATOM   2389  O   LYS A 329     -48.374 -11.988-107.309  1.00 98.84           O  
ANISOU 2389  O   LYS A 329    13698  14211   9646    616   -142    942       O  
ATOM   2390  CB  LYS A 329     -48.834 -10.824-109.974  1.00101.22           C  
ANISOU 2390  CB  LYS A 329    14166  14424   9869    549    -18    914       C  
ATOM   2391  CG  LYS A 329     -48.881  -9.428-110.565  1.00102.90           C  
ANISOU 2391  CG  LYS A 329    14533  14564   9998    551      2    887       C  
ATOM   2392  CD  LYS A 329     -50.254  -8.813-110.323  1.00105.42           C  
ANISOU 2392  CD  LYS A 329    14942  14942  10169    679    -15    933       C  
ATOM   2393  CE  LYS A 329     -50.619  -7.776-111.374  1.00107.49           C  
ANISOU 2393  CE  LYS A 329    15340  15151  10349    678     24    919       C  
ATOM   2394  NZ  LYS A 329     -50.931  -8.404-112.689  1.00105.35           N  
ANISOU 2394  NZ  LYS A 329    15029  14892  10107    626     90    932       N  
ATOM   2395  N   ASN A 330     -47.069 -13.434-108.467  1.00 99.11           N  
ANISOU 2395  N   ASN A 330    13577  14199   9881    446    -81    899       N  
ATOM   2396  CA  ASN A 330     -47.124 -14.537-107.494  1.00100.11           C  
ANISOU 2396  CA  ASN A 330    13583  14393  10060    472   -131    931       C  
ATOM   2397  C   ASN A 330     -48.279 -15.517-107.686  1.00 99.95           C  
ANISOU 2397  C   ASN A 330    13496  14466  10014    518   -134   1000       C  
ATOM   2398  O   ASN A 330     -48.607 -16.282-106.776  1.00103.33           O  
ANISOU 2398  O   ASN A 330    13840  14964  10456    560   -183   1045       O  
ATOM   2399  CB  ASN A 330     -47.093 -14.019-106.049  1.00 98.18           C  
ANISOU 2399  CB  ASN A 330    13368  14163   9772    542   -200    937       C  
ATOM   2400  CG  ASN A 330     -45.737 -13.485-105.661  1.00 98.13           C  
ANISOU 2400  CG  ASN A 330    13382  14065   9837    473   -223    873       C  
ATOM   2401  OD1 ASN A 330     -44.713 -13.931-106.183  1.00 97.85           O  
ANISOU 2401  OD1 ASN A 330    13280  13981   9916    372   -194    836       O  
ATOM   2402  ND2 ASN A 330     -45.718 -12.528-104.743  1.00 98.64           N  
ANISOU 2402  ND2 ASN A 330    13541  14106   9833    531   -279    864       N  
ATOM   2403  N   ALA A 331     -48.887 -15.496-108.865  1.00 99.38           N  
ANISOU 2403  N   ALA A 331    12008  12986  12764   -597   -798    789       N  
ATOM   2404  CA  ALA A 331     -49.959 -16.419-109.174  1.00 96.97           C  
ANISOU 2404  CA  ALA A 331    11730  12636  12478   -513   -826    781       C  
ATOM   2405  C   ALA A 331     -49.468 -17.402-110.219  1.00 98.22           C  
ANISOU 2405  C   ALA A 331    11853  12894  12571   -469   -823    764       C  
ATOM   2406  O   ALA A 331     -49.586 -17.159-111.425  1.00102.20           O  
ANISOU 2406  O   ALA A 331    12373  13419  13039   -487   -818    798       O  
ATOM   2407  CB  ALA A 331     -51.178 -15.663-109.668  1.00 97.79           C  
ANISOU 2407  CB  ALA A 331    11902  12636  12614   -523   -845    827       C  
ATOM   2408  N   ILE A 332     -48.898 -18.508-109.751  1.00 96.25           N  
ANISOU 2408  N   ILE A 332    11560  12706  12304   -410   -830    707       N  
ATOM   2409  CA  ILE A 332     -48.366 -19.539-110.642  1.00 95.43           C  
ANISOU 2409  CA  ILE A 332    11420  12702  12134   -352   -836    677       C  
ATOM   2410  C   ILE A 332     -49.492 -20.413-111.206  1.00 95.15           C  
ANISOU 2410  C   ILE A 332    11432  12609  12111   -278   -873    681       C  
ATOM   2411  O   ILE A 332     -50.107 -21.201-110.484  1.00 96.76           O  
ANISOU 2411  O   ILE A 332    11661  12752  12349   -225   -904    656       O  
ATOM   2412  CB  ILE A 332     -47.280 -20.368-109.930  1.00 94.21           C  
ANISOU 2412  CB  ILE A 332    11208  12636  11951   -307   -841    608       C  
ATOM   2413  CG1 ILE A 332     -46.132 -19.439-109.546  1.00 95.65           C  
ANISOU 2413  CG1 ILE A 332    11335  12892  12113   -389   -802    605       C  
ATOM   2414  CG2 ILE A 332     -46.786 -21.510-110.811  1.00 93.21           C  
ANISOU 2414  CG2 ILE A 332    11050  12609  11756   -228   -860    565       C  
ATOM   2415  CD1 ILE A 332     -45.259 -19.951-108.422  1.00100.26           C  
ANISOU 2415  CD1 ILE A 332    11873  13525  12695   -356   -809    541       C  
ATOM   2416  N   VAL A 333     -49.769 -20.250-112.496  1.00 93.87           N  
ANISOU 2416  N   VAL A 333    11284  12465  11917   -283   -869    714       N  
ATOM   2417  CA  VAL A 333     -50.824 -21.012-113.154  1.00 94.26           C  
ANISOU 2417  CA  VAL A 333    11376  12464  11973   -219   -903    719       C  
ATOM   2418  C   VAL A 333     -50.323 -22.427-113.425  1.00 94.20           C  
ANISOU 2418  C   VAL A 333    11344  12531  11917   -132   -930    664       C  
ATOM   2419  O   VAL A 333     -49.371 -22.614-114.179  1.00 96.92           O  
ANISOU 2419  O   VAL A 333    11641  12990  12194   -122   -917    644       O  
ATOM   2420  CB  VAL A 333     -51.276 -20.342-114.475  1.00 95.25           C  
ANISOU 2420  CB  VAL A 333    11530  12582  12077   -250   -894    773       C  
ATOM   2421  CG1 VAL A 333     -52.438 -21.105-115.098  1.00 94.34           C  
ANISOU 2421  CG1 VAL A 333    11459  12411  11975   -183   -931    776       C  
ATOM   2422  CG2 VAL A 333     -51.657 -18.883-114.248  1.00 94.13           C  
ANISOU 2422  CG2 VAL A 333    11423  12365  11974   -333   -877    825       C  
ATOM   2423  N   ARG A 334     -50.947 -23.416-112.792  1.00 93.75           N  
ANISOU 2423  N   ARG A 334    11320  12412  11889    -72   -972    635       N  
ATOM   2424  CA  ARG A 334     -50.582 -24.817-113.016  1.00 95.18           C  
ANISOU 2424  CA  ARG A 334    11498  12641  12024     17  -1014    581       C  
ATOM   2425  C   ARG A 334     -51.352 -25.389-114.204  1.00 96.53           C  
ANISOU 2425  C   ARG A 334    11704  12796  12176     62  -1042    596       C  
ATOM   2426  O   ARG A 334     -50.758 -25.939-115.136  1.00 98.16           O  
ANISOU 2426  O   ARG A 334    11886  13089  12318    112  -1052    570       O  
ATOM   2427  CB  ARG A 334     -50.803 -25.667-111.756  1.00 93.84           C  
ANISOU 2427  CB  ARG A 334    11359  12410  11884     54  -1054    544       C  
ATOM   2428  CG  ARG A 334     -49.767 -25.440-110.666  1.00 95.00           C  
ANISOU 2428  CG  ARG A 334    11466  12599  12031     37  -1038    510       C  
ATOM   2429  CD  ARG A 334     -49.984 -26.348-109.467  1.00 95.15           C  
ANISOU 2429  CD  ARG A 334    11526  12554  12070     75  -1084    475       C  
ATOM   2430  NE  ARG A 334     -49.357 -27.665-109.615  1.00 97.75           N  
ANISOU 2430  NE  ARG A 334    11866  12931  12342    168  -1140    413       N  
ATOM   2431  CZ  ARG A 334     -49.983 -28.764-110.038  1.00 98.06           C  
ANISOU 2431  CZ  ARG A 334    11965  12927  12364    228  -1197    403       C  
ATOM   2432  NH1 ARG A 334     -51.265 -28.717-110.373  1.00101.19           N  
ANISOU 2432  NH1 ARG A 334    12409  13242  12797    201  -1201    450       N  
ATOM   2433  NH2 ARG A 334     -49.334 -29.918-110.131  1.00 96.42           N  
ANISOU 2433  NH2 ARG A 334    11774  12759  12101    319  -1257    342       N  
ATOM   2434  N   SER A 335     -52.675 -25.252-114.160  1.00 96.66           N  
ANISOU 2434  N   SER A 335    11773  12708  12245     48  -1055    632       N  
ATOM   2435  CA  SER A 335     -53.547 -25.681-115.247  1.00 95.68           C  
ANISOU 2435  CA  SER A 335    11685  12558  12110     83  -1081    650       C  
ATOM   2436  C   SER A 335     -53.876 -24.479-116.109  1.00 94.12           C  
ANISOU 2436  C   SER A 335    11486  12356  11918     28  -1045    705       C  
ATOM   2437  O   SER A 335     -54.401 -23.482-115.610  1.00 93.48           O  
ANISOU 2437  O   SER A 335    11419  12212  11887    -29  -1025    738       O  
ATOM   2438  CB  SER A 335     -54.832 -26.294-114.687  1.00 96.38           C  
ANISOU 2438  CB  SER A 335    11830  12543  12247     97  -1121    651       C  
ATOM   2439  OG  SER A 335     -55.947 -26.008-115.514  1.00 96.18           O  
ANISOU 2439  OG  SER A 335    11833  12471  12240     90  -1126    688       O  
ATOM   2440  N   LEU A 336     -53.571 -24.570-117.400  1.00 91.75           N  
ANISOU 2440  N   LEU A 336    11176  12122  11562     49  -1042    713       N  
ATOM   2441  CA  LEU A 336     -53.813 -23.448-118.299  1.00 89.63           C  
ANISOU 2441  CA  LEU A 336    10916  11850  11286     -5  -1012    767       C  
ATOM   2442  C   LEU A 336     -55.292 -23.069-118.431  1.00 87.18           C  
ANISOU 2442  C   LEU A 336    10662  11428  11032    -11  -1032    804       C  
ATOM   2443  O   LEU A 336     -55.623 -21.887-118.294  1.00 85.61           O  
ANISOU 2443  O   LEU A 336    10481  11180  10864    -70  -1013    843       O  
ATOM   2444  CB  LEU A 336     -53.170 -23.666-119.671  1.00 90.78           C  
ANISOU 2444  CB  LEU A 336    11038  12099  11352     16  -1005    767       C  
ATOM   2445  CG  LEU A 336     -51.676 -23.356-119.801  1.00 92.30           C  
ANISOU 2445  CG  LEU A 336    11164  12426  11480    -18   -964    749       C  
ATOM   2446  CD1 LEU A 336     -51.256 -23.540-121.250  1.00 93.72           C  
ANISOU 2446  CD1 LEU A 336    11323  12707  11578      0   -957    752       C  
ATOM   2447  CD2 LEU A 336     -51.321 -21.955-119.312  1.00 91.11           C  
ANISOU 2447  CD2 LEU A 336    11006  12263  11348   -125   -920    791       C  
ATOM   2448  N   PRO A 337     -56.187 -24.062-118.667  1.00 84.75           N  
ANISOU 2448  N   PRO A 337    10384  11079  10735     49  -1075    787       N  
ATOM   2449  CA  PRO A 337     -57.582 -23.693-118.916  1.00 84.63           C  
ANISOU 2449  CA  PRO A 337    10412  10977  10765     46  -1094    816       C  
ATOM   2450  C   PRO A 337     -58.190 -22.896-117.766  1.00 85.61           C  
ANISOU 2450  C   PRO A 337    10544  11026  10956      0  -1085    825       C  
ATOM   2451  O   PRO A 337     -59.169 -22.173-117.964  1.00 85.10           O  
ANISOU 2451  O   PRO A 337    10508  10901  10925    -12  -1092    850       O  
ATOM   2452  CB  PRO A 337     -58.282 -25.045-119.081  1.00 83.03           C  
ANISOU 2452  CB  PRO A 337    10232  10753  10561    110  -1142    786       C  
ATOM   2453  CG  PRO A 337     -57.206 -25.976-119.512  1.00 82.00           C  
ANISOU 2453  CG  PRO A 337    10080  10707  10367    158  -1151    753       C  
ATOM   2454  CD  PRO A 337     -56.001 -25.523-118.746  1.00 83.18           C  
ANISOU 2454  CD  PRO A 337    10186  10911  10506    123  -1115    740       C  
ATOM   2455  N   SER A 338     -57.586 -23.011-116.586  1.00 87.61           N  
ANISOU 2455  N   SER A 338    10774  11289  11225    -17  -1071    801       N  
ATOM   2456  CA  SER A 338     -58.009 -22.253-115.416  1.00 90.37           C  
ANISOU 2456  CA  SER A 338    11124  11579  11631    -59  -1060    804       C  
ATOM   2457  C   SER A 338     -57.889 -20.737-115.618  1.00 92.97           C  
ANISOU 2457  C   SER A 338    11463  11889  11972   -114  -1035    843       C  
ATOM   2458  O   SER A 338     -58.363 -19.961-114.785  1.00 95.22           O  
ANISOU 2458  O   SER A 338    11756  12117  12305   -142  -1033    847       O  
ATOM   2459  CB  SER A 338     -57.212 -22.681-114.186  1.00 89.43           C  
ANISOU 2459  CB  SER A 338    10978  11483  11518    -67  -1051    770       C  
ATOM   2460  OG  SER A 338     -55.907 -22.132-114.215  1.00 89.67           O  
ANISOU 2460  OG  SER A 338    10976  11578  11517    -99  -1017    774       O  
ATOM   2461  N   VAL A 339     -57.248 -20.321-116.711  1.00 93.06           N  
ANISOU 2461  N   VAL A 339    11476  11947  11935   -130  -1020    872       N  
ATOM   2462  CA  VAL A 339     -57.189 -18.906-117.064  1.00 93.70           C  
ANISOU 2462  CA  VAL A 339    11585  11999  12015   -188  -1006    917       C  
ATOM   2463  C   VAL A 339     -58.531 -18.482-117.667  1.00 96.18           C  
ANISOU 2463  C   VAL A 339    11951  12236  12356   -165  -1039    938       C  
ATOM   2464  O   VAL A 339     -58.962 -17.335-117.495  1.00 95.83           O  
ANISOU 2464  O   VAL A 339    11943  12126  12339   -195  -1048    960       O  
ATOM   2465  CB  VAL A 339     -56.017 -18.596-118.017  1.00 92.50           C  
ANISOU 2465  CB  VAL A 339    11420  11933  11792   -229   -978    942       C  
ATOM   2466  CG1 VAL A 339     -56.003 -17.128-118.405  1.00 92.74           C  
ANISOU 2466  CG1 VAL A 339    11498  11922  11816   -301   -971    995       C  
ATOM   2467  CG2 VAL A 339     -54.697 -18.954-117.358  1.00 94.03           C  
ANISOU 2467  CG2 VAL A 339    11554  12213  11960   -249   -947    912       C  
ATOM   2468  N   GLU A 340     -59.192 -19.415-118.355  1.00 98.79           N  
ANISOU 2468  N   GLU A 340    12286  12573  12677   -106  -1064    925       N  
ATOM   2469  CA  GLU A 340     -60.532 -19.168-118.888  1.00100.96           C  
ANISOU 2469  CA  GLU A 340    12601  12782  12976    -74  -1099    934       C  
ATOM   2470  C   GLU A 340     -61.568 -19.245-117.774  1.00 99.60           C  
ANISOU 2470  C   GLU A 340    12421  12554  12867    -58  -1118    902       C  
ATOM   2471  O   GLU A 340     -62.522 -18.464-117.762  1.00100.82           O  
ANISOU 2471  O   GLU A 340    12603  12649  13054    -50  -1141    905       O  
ATOM   2472  CB  GLU A 340     -60.902 -20.144-120.010  1.00104.57           C  
ANISOU 2472  CB  GLU A 340    13063  13267  13399    -20  -1121    930       C  
ATOM   2473  CG  GLU A 340     -62.009 -19.609-120.912  1.00111.89           C  
ANISOU 2473  CG  GLU A 340    14037  14140  14334      3  -1153    951       C  
ATOM   2474  CD  GLU A 340     -63.171 -20.575-121.095  1.00117.71           C  
ANISOU 2474  CD  GLU A 340    14771  14860  15090     62  -1189    921       C  
ATOM   2475  OE1 GLU A 340     -62.946 -21.705-121.581  1.00120.16           O  
ANISOU 2475  OE1 GLU A 340    15069  15215  15369     94  -1195    907       O  
ATOM   2476  OE2 GLU A 340     -64.321 -20.194-120.772  1.00119.16           O  
ANISOU 2476  OE2 GLU A 340    14966  14990  15318     76  -1214    908       O  
ATOM   2477  N   THR A 341     -61.369 -20.188-116.849  1.00 96.76           N  
ANISOU 2477  N   THR A 341    12026  12219  12519    -51  -1111    867       N  
ATOM   2478  CA  THR A 341     -62.237 -20.356-115.681  1.00 93.78           C  
ANISOU 2478  CA  THR A 341    11635  11805  12192    -48  -1122    835       C  
ATOM   2479  C   THR A 341     -62.138 -19.131-114.786  1.00 92.86           C  
ANISOU 2479  C   THR A 341    11519  11653  12111    -86  -1109    838       C  
ATOM   2480  O   THR A 341     -63.107 -18.748-114.129  1.00 92.86           O  
ANISOU 2480  O   THR A 341    11517  11614  12151    -79  -1124    817       O  
ATOM   2481  CB  THR A 341     -61.836 -21.580-114.835  1.00 93.90           C  
ANISOU 2481  CB  THR A 341    11624  11851  12201    -46  -1119    803       C  
ATOM   2482  OG1 THR A 341     -61.349 -22.628-115.680  1.00 96.02           O  
ANISOU 2482  OG1 THR A 341    11897  12164  12423    -13  -1129    801       O  
ATOM   2483  CG2 THR A 341     -63.022 -22.090-114.038  1.00 94.36           C  
ANISOU 2483  CG2 THR A 341    11675  11881  12293    -41  -1140    772       C  
ATOM   2484  N   LEU A 342     -60.954 -18.524-114.779  1.00 92.12           N  
ANISOU 2484  N   LEU A 342    11426  11579  11997   -126  -1081    861       N  
ATOM   2485  CA  LEU A 342     -60.643 -17.405-113.902  1.00 92.37           C  
ANISOU 2485  CA  LEU A 342    11461  11578  12056   -169  -1069    866       C  
ATOM   2486  C   LEU A 342     -61.478 -16.165-114.198  1.00 92.37           C  
ANISOU 2486  C   LEU A 342    11508  11509  12079   -166  -1097    882       C  
ATOM   2487  O   LEU A 342     -61.851 -15.437-113.283  1.00 93.22           O  
ANISOU 2487  O   LEU A 342    11619  11574  12225   -173  -1106    865       O  
ATOM   2488  CB  LEU A 342     -59.150 -17.080-113.970  1.00 92.82           C  
ANISOU 2488  CB  LEU A 342    11508  11682  12077   -220  -1035    888       C  
ATOM   2489  CG  LEU A 342     -58.446 -16.593-112.703  1.00 91.96           C  
ANISOU 2489  CG  LEU A 342    11378  11572  11991   -263  -1013    875       C  
ATOM   2490  CD1 LEU A 342     -58.821 -17.425-111.480  1.00 89.97           C  
ANISOU 2490  CD1 LEU A 342    11091  11318  11772   -237  -1015    830       C  
ATOM   2491  CD2 LEU A 342     -56.947 -16.619-112.954  1.00 91.39           C  
ANISOU 2491  CD2 LEU A 342    11280  11573  11870   -306   -979    889       C  
ATOM   2492  N   GLY A 343     -61.772 -15.927-115.472  1.00 93.08           N  
ANISOU 2492  N   GLY A 343    11637  11587  12142   -150  -1116    911       N  
ATOM   2493  CA  GLY A 343     -62.666 -14.841-115.850  1.00 94.86           C  
ANISOU 2493  CA  GLY A 343    11917  11740  12383   -133  -1157    921       C  
ATOM   2494  C   GLY A 343     -64.023 -15.014-115.194  1.00 95.13           C  
ANISOU 2494  C   GLY A 343    11931  11748  12465    -81  -1186    872       C  
ATOM   2495  O   GLY A 343     -64.580 -14.074-114.628  1.00 97.88           O  
ANISOU 2495  O   GLY A 343    12299  12046  12845    -70  -1211    855       O  
ATOM   2496  N   CYS A 344     -64.528 -16.240-115.230  1.00 93.96           N  
ANISOU 2496  N   CYS A 344    11741  11640  12316    -50  -1183    846       N  
ATOM   2497  CA  CYS A 344     -65.901 -16.526-114.832  1.00 95.58           C  
ANISOU 2497  CA  CYS A 344    11922  11838  12553     -7  -1210    800       C  
ATOM   2498  C   CYS A 344     -66.140 -16.747-113.338  1.00 95.63           C  
ANISOU 2498  C   CYS A 344    11881  11859  12593    -21  -1196    757       C  
ATOM   2499  O   CYS A 344     -67.285 -17.009-112.940  1.00 97.42           O  
ANISOU 2499  O   CYS A 344    12077  12096  12839      4  -1215    715       O  
ATOM   2500  CB  CYS A 344     -66.412 -17.747-115.592  1.00 95.88           C  
ANISOU 2500  CB  CYS A 344    11945  11911  12570     21  -1219    793       C  
ATOM   2501  SG  CYS A 344     -65.767 -17.850-117.269  1.00101.05           S  
ANISOU 2501  SG  CYS A 344    12645  12574  13173     29  -1222    845       S  
ATOM   2502  N   THR A 345     -65.092 -16.656-112.514  1.00 91.55           N  
ANISOU 2502  N   THR A 345    11353  11351  12079    -64  -1164    765       N  
ATOM   2503  CA  THR A 345     -65.248 -16.970-111.089  1.00 87.21           C  
ANISOU 2503  CA  THR A 345    10761  10820  11556    -81  -1149    726       C  
ATOM   2504  C   THR A 345     -66.203 -15.988-110.424  1.00 85.86           C  
ANISOU 2504  C   THR A 345    10583  10618  11419    -59  -1173    690       C  
ATOM   2505  O   THR A 345     -66.153 -14.783-110.689  1.00 86.52           O  
ANISOU 2505  O   THR A 345    10707  10652  11511    -48  -1194    703       O  
ATOM   2506  CB  THR A 345     -63.916 -17.056-110.307  1.00 86.83           C  
ANISOU 2506  CB  THR A 345    10701  10786  11502   -126  -1112    738       C  
ATOM   2507  OG1 THR A 345     -63.706 -15.863-109.545  1.00 88.20           O  
ANISOU 2507  OG1 THR A 345    10884  10926  11703   -144  -1111    733       O  
ATOM   2508  CG2 THR A 345     -62.745 -17.282-111.222  1.00 85.91           C  
ANISOU 2508  CG2 THR A 345    10603  10692  11347   -143  -1095    779       C  
ATOM   2509  N   SER A 346     -67.076 -16.525-109.578  1.00 83.00           N  
ANISOU 2509  N   SER A 346    10175  10289  11072    -53  -1174    644       N  
ATOM   2510  CA  SER A 346     -68.115 -15.750-108.918  1.00 81.89           C  
ANISOU 2510  CA  SER A 346    10013  10143  10959    -23  -1198    595       C  
ATOM   2511  C   SER A 346     -67.981 -15.794-107.399  1.00 82.99           C  
ANISOU 2511  C   SER A 346    10110  10306  11114    -54  -1174    562       C  
ATOM   2512  O   SER A 346     -68.569 -14.962-106.702  1.00 84.60           O  
ANISOU 2512  O   SER A 346    10298  10505  11339    -31  -1191    520       O  
ATOM   2513  CB  SER A 346     -69.477 -16.297-109.311  1.00 80.13           C  
ANISOU 2513  CB  SER A 346     9757   9957  10730     10  -1222    558       C  
ATOM   2514  OG  SER A 346     -69.525 -17.694-109.078  1.00 78.62           O  
ANISOU 2514  OG  SER A 346     9535   9814  10520    -25  -1200    556       O  
ATOM   2515  N   VAL A 347     -67.229 -16.777-106.895  1.00 81.58           N  
ANISOU 2515  N   VAL A 347     9918  10155  10922   -100  -1140    576       N  
ATOM   2516  CA  VAL A 347     -67.032 -16.977-105.455  1.00 79.70           C  
ANISOU 2516  CA  VAL A 347     9646   9941  10693   -135  -1116    549       C  
ATOM   2517  C   VAL A 347     -65.567 -17.281-105.135  1.00 80.96           C  
ANISOU 2517  C   VAL A 347     9824  10092  10843   -173  -1087    583       C  
ATOM   2518  O   VAL A 347     -64.896 -17.989-105.888  1.00 82.72           O  
ANISOU 2518  O   VAL A 347    10068  10320  11042   -180  -1080    615       O  
ATOM   2519  CB  VAL A 347     -67.886 -18.137-104.910  1.00 77.93           C  
ANISOU 2519  CB  VAL A 347     9382   9774  10453   -157  -1112    517       C  
ATOM   2520  CG1 VAL A 347     -67.861 -18.145-103.396  1.00 78.29           C  
ANISOU 2520  CG1 VAL A 347     9394   9846  10505   -191  -1092    485       C  
ATOM   2521  CG2 VAL A 347     -69.322 -18.029-105.376  1.00 79.23           C  
ANISOU 2521  CG2 VAL A 347     9519   9966  10617   -123  -1140    482       C  
ATOM   2522  N   ILE A 348     -65.076 -16.743-104.019  1.00 80.53           N  
ANISOU 2522  N   ILE A 348     9759  10031  10807   -194  -1071    569       N  
ATOM   2523  CA  ILE A 348     -63.740 -17.061-103.520  1.00 78.40           C  
ANISOU 2523  CA  ILE A 348     9495   9763  10527   -229  -1045    589       C  
ATOM   2524  C   ILE A 348     -63.823 -17.510-102.062  1.00 78.80           C  
ANISOU 2524  C   ILE A 348     9516   9840  10582   -256  -1030    555       C  
ATOM   2525  O   ILE A 348     -64.230 -16.740-101.191  1.00 78.11           O  
ANISOU 2525  O   ILE A 348     9409   9749  10517   -254  -1031    524       O  
ATOM   2526  CB  ILE A 348     -62.776 -15.866-103.665  1.00 77.84           C  
ANISOU 2526  CB  ILE A 348     9451   9654  10470   -237  -1040    613       C  
ATOM   2527  CG1 ILE A 348     -62.538 -15.551-105.142  1.00 79.04           C  
ANISOU 2527  CG1 ILE A 348     9639   9785  10605   -225  -1052    655       C  
ATOM   2528  CG2 ILE A 348     -61.444 -16.163-102.995  1.00 77.37           C  
ANISOU 2528  CG2 ILE A 348     9385   9610  10402   -274  -1012    622       C  
ATOM   2529  CD1 ILE A 348     -61.860 -14.217-105.395  1.00 81.09           C  
ANISOU 2529  CD1 ILE A 348     9936  10001  10872   -242  -1058    682       C  
ATOM   2530  N   CYS A 349     -63.457 -18.767-101.815  1.00 80.38           N  
ANISOU 2530  N   CYS A 349     9719  10066  10755   -279  -1021    558       N  
ATOM   2531  CA  CYS A 349     -63.338 -19.299-100.454  1.00 82.60           C  
ANISOU 2531  CA  CYS A 349     9985  10368  11030   -312  -1009    534       C  
ATOM   2532  C   CYS A 349     -61.909 -19.230 -99.951  1.00 83.62           C  
ANISOU 2532  C   CYS A 349    10126  10488  11159   -326   -993    545       C  
ATOM   2533  O   CYS A 349     -61.107 -20.135-100.210  1.00 83.88           O  
ANISOU 2533  O   CYS A 349    10177  10528  11162   -328   -994    559       O  
ATOM   2534  CB  CYS A 349     -63.796 -20.745-100.383  1.00 83.15           C  
ANISOU 2534  CB  CYS A 349    10064  10462  11065   -334  -1020    530       C  
ATOM   2535  SG  CYS A 349     -65.571 -20.938-100.253  1.00 88.54           S  
ANISOU 2535  SG  CYS A 349    10715  11182  11743   -346  -1032    498       S  
ATOM   2536  N   SER A 350     -61.603 -18.163 -99.221  1.00 83.97           N  
ANISOU 2536  N   SER A 350    10157  10517  11230   -331   -981    534       N  
ATOM   2537  CA  SER A 350     -60.274 -17.970 -98.676  1.00 83.92           C  
ANISOU 2537  CA  SER A 350    10154  10505  11224   -347   -966    540       C  
ATOM   2538  C   SER A 350     -60.187 -18.382 -97.207  1.00 82.37           C  
ANISOU 2538  C   SER A 350     9946  10324  11025   -371   -957    510       C  
ATOM   2539  O   SER A 350     -61.096 -18.117 -96.415  1.00 81.34           O  
ANISOU 2539  O   SER A 350     9796  10201  10907   -378   -957    482       O  
ATOM   2540  CB  SER A 350     -59.855 -16.513 -98.837  1.00 86.67           C  
ANISOU 2540  CB  SER A 350    10505  10823  11602   -346   -962    550       C  
ATOM   2541  OG  SER A 350     -58.466 -16.364 -98.591  1.00 91.48           O  
ANISOU 2541  OG  SER A 350    11115  11437  12204   -367   -946    561       O  
ATOM   2542  N   ASP A 351     -59.089 -19.040 -96.856  1.00 80.64           N  
ANISOU 2542  N   ASP A 351     9738  10115  10786   -381   -952    513       N  
ATOM   2543  CA  ASP A 351     -58.774 -19.307 -95.466  1.00 80.46           C  
ANISOU 2543  CA  ASP A 351     9712  10099  10759   -402   -947    488       C  
ATOM   2544  C   ASP A 351     -58.232 -18.028 -94.838  1.00 80.67           C  
ANISOU 2544  C   ASP A 351     9719  10112  10820   -408   -931    479       C  
ATOM   2545  O   ASP A 351     -57.659 -17.177 -95.536  1.00 78.46           O  
ANISOU 2545  O   ASP A 351     9438   9816  10554   -402   -927    498       O  
ATOM   2546  CB  ASP A 351     -57.730 -20.410 -95.361  1.00 82.88           C  
ANISOU 2546  CB  ASP A 351    10042  10417  11029   -399   -956    489       C  
ATOM   2547  CG  ASP A 351     -58.156 -21.683 -96.050  1.00 85.02           C  
ANISOU 2547  CG  ASP A 351    10344  10693  11263   -390   -981    499       C  
ATOM   2548  OD1 ASP A 351     -59.282 -22.145 -95.776  1.00 88.28           O  
ANISOU 2548  OD1 ASP A 351    10766  11107  11668   -411   -990    493       O  
ATOM   2549  OD2 ASP A 351     -57.365 -22.225 -96.858  1.00 85.42           O  
ANISOU 2549  OD2 ASP A 351    10411  10753  11291   -363   -993    509       O  
ATOM   2550  N   LYS A 352     -58.396 -17.903 -93.521  1.00 81.42           N  
ANISOU 2550  N   LYS A 352     9803  10210  10921   -424   -926    450       N  
ATOM   2551  CA  LYS A 352     -57.990 -16.683 -92.829  1.00 81.93           C  
ANISOU 2551  CA  LYS A 352     9852  10257  11018   -428   -917    437       C  
ATOM   2552  C   LYS A 352     -56.509 -16.606 -92.477  1.00 81.91           C  
ANISOU 2552  C   LYS A 352     9852  10256  11014   -439   -908    440       C  
ATOM   2553  O   LYS A 352     -55.797 -15.759 -93.018  1.00 83.17           O  
ANISOU 2553  O   LYS A 352    10010  10403  11188   -443   -904    457       O  
ATOM   2554  CB  LYS A 352     -58.837 -16.419 -91.580  1.00 81.69           C  
ANISOU 2554  CB  LYS A 352     9802  10236  10998   -436   -914    399       C  
ATOM   2555  CG  LYS A 352     -58.559 -15.047 -90.971  1.00 82.37           C  
ANISOU 2555  CG  LYS A 352     9877  10298  11120   -431   -914    382       C  
ATOM   2556  CD  LYS A 352     -58.969 -14.930 -89.509  1.00 83.15           C  
ANISOU 2556  CD  LYS A 352     9955  10416  11220   -439   -908    340       C  
ATOM   2557  CE  LYS A 352     -58.029 -15.672 -88.563  1.00 83.84           C  
ANISOU 2557  CE  LYS A 352    10052  10516  11288   -464   -898    335       C  
ATOM   2558  NZ  LYS A 352     -56.680 -15.052 -88.406  1.00 85.24           N  
ANISOU 2558  NZ  LYS A 352    10234  10669  11482   -467   -895    342       N  
ATOM   2559  N   THR A 353     -56.054 -17.486 -91.583  1.00 81.67           N  
ANISOU 2559  N   THR A 353     9827  10243  10960   -447   -908    422       N  
ATOM   2560  CA  THR A 353     -54.801 -17.250 -90.842  1.00 83.56           C  
ANISOU 2560  CA  THR A 353    10059  10486  11201   -455   -902    409       C  
ATOM   2561  C   THR A 353     -53.541 -17.060 -91.708  1.00 85.37           C  
ANISOU 2561  C   THR A 353    10280  10731  11423   -452   -897    426       C  
ATOM   2562  O   THR A 353     -52.695 -16.207 -91.401  1.00 87.65           O  
ANISOU 2562  O   THR A 353    10552  11020  11728   -469   -887    422       O  
ATOM   2563  CB  THR A 353     -54.545 -18.288 -89.719  1.00 82.41           C  
ANISOU 2563  CB  THR A 353     9930  10355  11026   -459   -910    384       C  
ATOM   2564  OG1 THR A 353     -55.782 -18.670 -89.111  1.00 83.64           O  
ANISOU 2564  OG1 THR A 353    10094  10510  11174   -474   -914    373       O  
ATOM   2565  CG2 THR A 353     -53.657 -17.694 -88.639  1.00 81.37           C  
ANISOU 2565  CG2 THR A 353     9784  10222  10909   -468   -903    361       C  
ATOM   2566  N   GLY A 354     -53.412 -17.819 -92.788  1.00 83.33           N  
ANISOU 2566  N   GLY A 354    10032  10492  11137   -435   -904    444       N  
ATOM   2567  CA  GLY A 354     -52.247 -17.628 -93.643  1.00 83.52           C  
ANISOU 2567  CA  GLY A 354    10039  10549  11146   -434   -897    456       C  
ATOM   2568  C   GLY A 354     -52.434 -16.535 -94.680  1.00 82.46           C  
ANISOU 2568  C   GLY A 354     9900  10399  11030   -453   -886    490       C  
ATOM   2569  O   GLY A 354     -51.494 -15.812 -95.027  1.00 81.13           O  
ANISOU 2569  O   GLY A 354     9715  10249  10859   -480   -874    500       O  
ATOM   2570  N   THR A 355     -53.673 -16.402 -95.141  1.00 82.71           N  
ANISOU 2570  N   THR A 355     9950  10398  11076   -444   -894    505       N  
ATOM   2571  CA  THR A 355     -53.961 -15.833 -96.458  1.00 82.25           C  
ANISOU 2571  CA  THR A 355     9903  10329  11019   -447   -895    539       C  
ATOM   2572  C   THR A 355     -54.606 -14.441 -96.419  1.00 79.52           C  
ANISOU 2572  C   THR A 355     9572   9931  10711   -461   -901    550       C  
ATOM   2573  O   THR A 355     -54.220 -13.564 -97.188  1.00 77.29           O  
ANISOU 2573  O   THR A 355     9302   9633  10428   -485   -902    578       O  
ATOM   2574  CB  THR A 355     -54.778 -16.856 -97.293  1.00 83.50           C  
ANISOU 2574  CB  THR A 355    10074  10494  11155   -415   -908    548       C  
ATOM   2575  OG1 THR A 355     -54.069 -18.106 -97.328  1.00 83.38           O  
ANISOU 2575  OG1 THR A 355    10056  10522  11103   -396   -912    535       O  
ATOM   2576  CG2 THR A 355     -54.993 -16.385 -98.714  1.00 83.85           C  
ANISOU 2576  CG2 THR A 355    10131  10533  11195   -414   -910    584       C  
ATOM   2577  N   LEU A 356     -55.577 -14.251 -95.529  1.00 78.48           N  
ANISOU 2577  N   LEU A 356     9440   9772  10605   -447   -911    524       N  
ATOM   2578  CA  LEU A 356     -56.161 -12.933 -95.286  1.00 78.64           C  
ANISOU 2578  CA  LEU A 356     9475   9743  10659   -448   -926    519       C  
ATOM   2579  C   LEU A 356     -55.320 -12.166 -94.271  1.00 79.66           C  
ANISOU 2579  C   LEU A 356     9600   9860  10806   -475   -922    504       C  
ATOM   2580  O   LEU A 356     -55.215 -10.941 -94.340  1.00 80.72           O  
ANISOU 2580  O   LEU A 356     9759   9950  10960   -490   -937    513       O  
ATOM   2581  CB  LEU A 356     -57.600 -13.052 -94.770  1.00 78.13           C  
ANISOU 2581  CB  LEU A 356     9403   9673  10609   -414   -940    487       C  
ATOM   2582  CG  LEU A 356     -58.699 -13.635 -95.667  1.00 77.81           C  
ANISOU 2582  CG  LEU A 356     9365   9643  10557   -387   -950    493       C  
ATOM   2583  CD1 LEU A 356     -59.910 -14.054 -94.845  1.00 76.40           C  
ANISOU 2583  CD1 LEU A 356     9160   9487  10379   -370   -954    452       C  
ATOM   2584  CD2 LEU A 356     -59.106 -12.651 -96.754  1.00 78.14           C  
ANISOU 2584  CD2 LEU A 356     9436   9641  10610   -370   -974    515       C  
ATOM   2585  N   THR A 357     -54.735 -12.892 -93.322  1.00 79.97           N  
ANISOU 2585  N   THR A 357     9615   9933  10835   -481   -906    481       N  
ATOM   2586  CA  THR A 357     -53.909 -12.282 -92.285  1.00 80.72           C  
ANISOU 2586  CA  THR A 357     9702  10022  10946   -505   -901    463       C  
ATOM   2587  C   THR A 357     -52.471 -12.745 -92.418  1.00 82.39           C  
ANISOU 2587  C   THR A 357     9895  10278  11130   -530   -884    470       C  
ATOM   2588  O   THR A 357     -52.214 -13.882 -92.827  1.00 81.43           O  
ANISOU 2588  O   THR A 357     9762  10198  10977   -514   -877    471       O  
ATOM   2589  CB  THR A 357     -54.392 -12.644 -90.873  1.00 79.95           C  
ANISOU 2589  CB  THR A 357     9588   9930  10856   -489   -900    421       C  
ATOM   2590  OG1 THR A 357     -54.025 -13.992 -90.585  1.00 78.68           O  
ANISOU 2590  OG1 THR A 357     9417   9812  10663   -485   -890    412       O  
ATOM   2591  CG2 THR A 357     -55.903 -12.486 -90.749  1.00 80.16           C  
ANISOU 2591  CG2 THR A 357     9618   9942  10896   -460   -914    403       C  
ATOM   2592  N   THR A 358     -51.550 -11.861 -92.031  1.00 84.81           N  
ANISOU 2592  N   THR A 358    10197  10578  11447   -567   -881    469       N  
ATOM   2593  CA  THR A 358     -50.102 -12.037 -92.222  1.00 87.03           C  
ANISOU 2593  CA  THR A 358    10451  10912  11701   -599   -864    472       C  
ATOM   2594  C   THR A 358     -49.464 -13.265 -91.563  1.00 88.31           C  
ANISOU 2594  C   THR A 358    10584  11129  11837   -572   -857    438       C  
ATOM   2595  O   THR A 358     -48.388 -13.699 -91.981  1.00 87.31           O  
ANISOU 2595  O   THR A 358    10431  11065  11679   -579   -848    434       O  
ATOM   2596  CB  THR A 358     -49.328 -10.813 -91.702  1.00 87.27           C  
ANISOU 2596  CB  THR A 358    10483  10924  11750   -650   -866    471       C  
ATOM   2597  OG1 THR A 358     -49.754 -10.509 -90.368  1.00 86.90           O  
ANISOU 2597  OG1 THR A 358    10441  10840  11734   -633   -876    438       O  
ATOM   2598  CG2 THR A 358     -49.564  -9.613 -92.593  1.00 89.44           C  
ANISOU 2598  CG2 THR A 358    10798  11150  12034   -689   -879    512       C  
ATOM   2599  N   ASN A 359     -50.120 -13.805 -90.535  1.00 89.66           N  
ANISOU 2599  N   ASN A 359    10763  11283  12019   -542   -865    411       N  
ATOM   2600  CA  ASN A 359     -49.543 -14.853 -89.677  1.00 91.74           C  
ANISOU 2600  CA  ASN A 359    11015  11581  12258   -520   -868    376       C  
ATOM   2601  C   ASN A 359     -48.318 -14.381 -88.871  1.00 94.54           C  
ANISOU 2601  C   ASN A 359    11344  11959  12616   -541   -863    351       C  
ATOM   2602  O   ASN A 359     -47.571 -15.183 -88.300  1.00 96.01           O  
ANISOU 2602  O   ASN A 359    11518  12183  12777   -520   -869    320       O  
ATOM   2603  CB  ASN A 359     -49.240 -16.137 -90.464  1.00 90.13           C  
ANISOU 2603  CB  ASN A 359    10811  11421  12010   -488   -875    377       C  
ATOM   2604  CG  ASN A 359     -49.065 -17.342 -89.560  1.00 89.87           C  
ANISOU 2604  CG  ASN A 359    10793  11401  11950   -455   -894    343       C  
ATOM   2605  OD1 ASN A 359     -49.748 -17.474 -88.540  1.00 89.77           O  
ANISOU 2605  OD1 ASN A 359    10801  11356  11949   -456   -900    330       O  
ATOM   2606  ND2 ASN A 359     -48.139 -18.222 -89.921  1.00 89.22           N  
ANISOU 2606  ND2 ASN A 359    10703  11367  11827   -425   -907    325       N  
ATOM   2607  N   GLN A 360     -48.127 -13.067 -88.832  1.00 96.57           N  
ANISOU 2607  N   GLN A 360    11598  12191  12902   -583   -857    363       N  
ATOM   2608  CA  GLN A 360     -47.155 -12.445 -87.953  1.00 98.94           C  
ANISOU 2608  CA  GLN A 360    11877  12501  13212   -611   -855    339       C  
ATOM   2609  C   GLN A 360     -47.762 -12.341 -86.552  1.00 99.22           C  
ANISOU 2609  C   GLN A 360    11927  12496  13273   -592   -864    310       C  
ATOM   2610  O   GLN A 360     -48.357 -11.321 -86.196  1.00100.40           O  
ANISOU 2610  O   GLN A 360    12094  12594  13457   -605   -871    313       O  
ATOM   2611  CB  GLN A 360     -46.776 -11.061 -88.492  1.00103.26           C  
ANISOU 2611  CB  GLN A 360    12428  13028  13776   -671   -852    368       C  
ATOM   2612  CG  GLN A 360     -46.077 -11.088 -89.841  1.00105.22           C  
ANISOU 2612  CG  GLN A 360    12658  13330  13990   -704   -838    397       C  
ATOM   2613  CD  GLN A 360     -44.859 -11.991 -89.831  1.00108.56           C  
ANISOU 2613  CD  GLN A 360    13028  13846  14370   -693   -827    366       C  
ATOM   2614  OE1 GLN A 360     -43.855 -11.700 -89.175  1.00110.53           O  
ANISOU 2614  OE1 GLN A 360    13247  14133  14616   -719   -823    339       O  
ATOM   2615  NE2 GLN A 360     -44.946 -13.101 -90.553  1.00109.85           N  
ANISOU 2615  NE2 GLN A 360    13184  14052  14500   -649   -826    365       N  
ATOM   2616  N   MET A 361     -47.617 -13.402 -85.762  1.00 99.15           N  
ANISOU 2616  N   MET A 361    11917  12512  13244   -560   -869    279       N  
ATOM   2617  CA  MET A 361     -48.304 -13.493 -84.471  1.00 99.20           C  
ANISOU 2617  CA  MET A 361    11939  12489  13263   -544   -876    253       C  
ATOM   2618  C   MET A 361     -47.488 -12.996 -83.280  1.00 99.59           C  
ANISOU 2618  C   MET A 361    11974  12540  13324   -555   -879    220       C  
ATOM   2619  O   MET A 361     -46.255 -13.108 -83.260  1.00101.81           O  
ANISOU 2619  O   MET A 361    12231  12862  13590   -563   -878    206       O  
ATOM   2620  CB  MET A 361     -48.783 -14.921 -84.216  1.00100.29           C  
ANISOU 2620  CB  MET A 361    12098  12640  13365   -512   -886    244       C  
ATOM   2621  CG  MET A 361     -49.936 -15.355 -85.101  1.00102.84           C  
ANISOU 2621  CG  MET A 361    12441  12952  13683   -503   -886    272       C  
ATOM   2622  SD  MET A 361     -50.765 -16.788 -84.391  1.00107.93           S  
ANISOU 2622  SD  MET A 361    13122  13598  14288   -487   -900    259       S  
ATOM   2623  CE  MET A 361     -52.398 -16.655 -85.128  1.00108.07           C  
ANISOU 2623  CE  MET A 361    13145  13598  14316   -493   -894    284       C  
ATOM   2624  N   SER A 362     -48.202 -12.453 -82.292  1.00 97.27           N  
ANISOU 2624  N   SER A 362    11691  12210  13054   -554   -883    203       N  
ATOM   2625  CA  SER A 362     -47.616 -11.937 -81.047  1.00 94.59           C  
ANISOU 2625  CA  SER A 362    11343  11865  12729   -561   -888    169       C  
ATOM   2626  C   SER A 362     -48.684 -11.806 -79.955  1.00 93.14           C  
ANISOU 2626  C   SER A 362    11175  11658  12556   -545   -892    146       C  
ATOM   2627  O   SER A 362     -49.785 -11.321 -80.217  1.00 94.72           O  
ANISOU 2627  O   SER A 362    11383  11833  12773   -539   -894    155       O  
ATOM   2628  CB  SER A 362     -46.965 -10.575 -81.294  1.00 93.57           C  
ANISOU 2628  CB  SER A 362    11203  11716  12630   -599   -890    178       C  
ATOM   2629  OG  SER A 362     -47.857  -9.695 -81.962  1.00 91.98           O  
ANISOU 2629  OG  SER A 362    11022  11468  12455   -607   -896    204       O  
ATOM   2630  N   VAL A 363     -48.371 -12.246 -78.739  1.00 90.68           N  
ANISOU 2630  N   VAL A 363    10865  11359  12229   -535   -897    113       N  
ATOM   2631  CA  VAL A 363     -49.263 -12.013 -77.599  1.00 88.47           C  
ANISOU 2631  CA  VAL A 363    10593  11068  11954   -526   -898     87       C  
ATOM   2632  C   VAL A 363     -49.173 -10.544 -77.228  1.00 88.48           C  
ANISOU 2632  C   VAL A 363    10583  11035  11998   -532   -907     71       C  
ATOM   2633  O   VAL A 363     -48.086 -10.041 -76.946  1.00 92.53           O  
ANISOU 2633  O   VAL A 363    11087  11543  12524   -547   -913     61       O  
ATOM   2634  CB  VAL A 363     -48.881 -12.860 -76.367  1.00 87.79           C  
ANISOU 2634  CB  VAL A 363    10519  11003  11835   -519   -904     57       C  
ATOM   2635  CG1 VAL A 363     -49.708 -12.451 -75.153  1.00 85.18           C  
ANISOU 2635  CG1 VAL A 363    10188  10668  11506   -516   -903     26       C  
ATOM   2636  CG2 VAL A 363     -49.050 -14.343 -76.669  1.00 89.44           C  
ANISOU 2636  CG2 VAL A 363    10755  11232  11995   -513   -908     71       C  
ATOM   2637  N   CYS A 364     -50.302  -9.851 -77.235  1.00 86.58           N  
ANISOU 2637  N   CYS A 364    10345  10773  11776   -520   -912     65       N  
ATOM   2638  CA  CYS A 364     -50.294  -8.442 -76.881  1.00 86.46           C  
ANISOU 2638  CA  CYS A 364    10333  10717  11800   -517   -932     47       C  
ATOM   2639  C   CYS A 364     -51.128  -8.154 -75.627  1.00 86.73           C  
ANISOU 2639  C   CYS A 364    10360  10759  11833   -489   -938      0       C  
ATOM   2640  O   CYS A 364     -51.011  -7.089 -75.026  1.00 87.96           O  
ANISOU 2640  O   CYS A 364    10520  10883  12015   -479   -960    -27       O  
ATOM   2641  CB  CYS A 364     -50.751  -7.598 -78.063  1.00 85.77           C  
ANISOU 2641  CB  CYS A 364    10262  10590  11737   -518   -946     75       C  
ATOM   2642  SG  CYS A 364     -52.509  -7.769 -78.388  1.00 85.52           S  
ANISOU 2642  SG  CYS A 364    10227  10569  11697   -478   -948     66       S  
ATOM   2643  N   LYS A 365     -51.962  -9.112 -75.234  1.00 87.05           N  
ANISOU 2643  N   LYS A 365    10392  10845  11838   -479   -922    -10       N  
ATOM   2644  CA  LYS A 365     -52.739  -9.003 -73.999  1.00 86.84           C  
ANISOU 2644  CA  LYS A 365    10352  10847  11797   -461   -922    -58       C  
ATOM   2645  C   LYS A 365     -52.776 -10.318 -73.246  1.00 84.57           C  
ANISOU 2645  C   LYS A 365    10067  10608  11457   -480   -902    -62       C  
ATOM   2646  O   LYS A 365     -52.709 -11.392 -73.847  1.00 82.90           O  
ANISOU 2646  O   LYS A 365     9870  10409  11218   -499   -892    -29       O  
ATOM   2647  CB  LYS A 365     -54.170  -8.549 -74.284  1.00 89.48           C  
ANISOU 2647  CB  LYS A 365    10668  11196  12132   -432   -927    -77       C  
ATOM   2648  CG  LYS A 365     -54.339  -7.049 -74.421  1.00 92.53           C  
ANISOU 2648  CG  LYS A 365    11061  11533  12563   -397   -962   -100       C  
ATOM   2649  CD  LYS A 365     -55.812  -6.695 -74.498  1.00 96.06           C  
ANISOU 2649  CD  LYS A 365    11485  12011  13002   -354   -973   -136       C  
ATOM   2650  CE  LYS A 365     -56.004  -5.202 -74.699  1.00100.19           C  
ANISOU 2650  CE  LYS A 365    12027  12473  13564   -308  -1022   -162       C  
ATOM   2651  NZ  LYS A 365     -57.412  -4.886 -75.070  1.00104.77           N  
ANISOU 2651  NZ  LYS A 365    12586  13082  14137   -256  -1039   -196       N  
ATOM   2652  N   MET A 366     -52.884 -10.218 -71.925  1.00 83.93           N  
ANISOU 2652  N   MET A 366     9980  10550  11360   -475   -902   -102       N  
ATOM   2653  CA  MET A 366     -53.042 -11.385 -71.061  1.00 83.73           C  
ANISOU 2653  CA  MET A 366     9966  10568  11277   -499   -888   -108       C  
ATOM   2654  C   MET A 366     -53.729 -11.012 -69.754  1.00 84.24           C  
ANISOU 2654  C   MET A 366    10010  10674  11321   -492   -885   -159       C  
ATOM   2655  O   MET A 366     -53.588  -9.888 -69.273  1.00 82.88           O  
ANISOU 2655  O   MET A 366     9821  10484  11183   -461   -899   -194       O  
ATOM   2656  CB  MET A 366     -51.694 -12.047 -70.770  1.00 81.50           C  
ANISOU 2656  CB  MET A 366     9715  10267  10984   -511   -896    -95       C  
ATOM   2657  CG  MET A 366     -50.703 -11.148 -70.064  1.00 80.69           C  
ANISOU 2657  CG  MET A 366     9606  10138  10915   -495   -910   -124       C  
ATOM   2658  SD  MET A 366     -49.205 -12.045 -69.662  1.00 81.29           S  
ANISOU 2658  SD  MET A 366     9711  10207  10967   -501   -922   -120       S  
ATOM   2659  CE  MET A 366     -48.140 -10.715 -69.098  1.00 81.11           C  
ANISOU 2659  CE  MET A 366     9667  10156  10996   -488   -938   -152       C  
ATOM   2660  N   PHE A 367     -54.480 -11.955 -69.191  1.00 86.55           N  
ANISOU 2660  N   PHE A 367    10307  11024  11553   -523   -868   -163       N  
ATOM   2661  CA  PHE A 367     -55.016 -11.778 -67.841  1.00 90.22           C  
ANISOU 2661  CA  PHE A 367    10753  11543  11983   -526   -861   -211       C  
ATOM   2662  C   PHE A 367     -54.868 -12.991 -66.908  1.00 91.19           C  
ANISOU 2662  C   PHE A 367    10914  11696  12035   -576   -853   -203       C  
ATOM   2663  O   PHE A 367     -54.714 -14.132 -67.358  1.00 89.86           O  
ANISOU 2663  O   PHE A 367    10789  11518  11833   -612   -854   -162       O  
ATOM   2664  CB  PHE A 367     -56.457 -11.218 -67.858  1.00 90.79           C  
ANISOU 2664  CB  PHE A 367    10771  11679  12046   -510   -851   -249       C  
ATOM   2665  CG  PHE A 367     -57.506 -12.191 -68.335  1.00 90.59           C  
ANISOU 2665  CG  PHE A 367    10737  11712  11968   -555   -830   -228       C  
ATOM   2666  CD1 PHE A 367     -57.893 -13.274 -67.544  1.00 90.20           C  
ANISOU 2666  CD1 PHE A 367    10705  11724  11842   -618   -812   -225       C  
ATOM   2667  CD2 PHE A 367     -58.139 -12.000 -69.556  1.00 90.09           C  
ANISOU 2667  CD2 PHE A 367    10654  11646  11930   -539   -831   -213       C  
ATOM   2668  CE1 PHE A 367     -58.863 -14.160 -67.978  1.00 89.20           C  
ANISOU 2668  CE1 PHE A 367    10575  11653  11664   -671   -796   -204       C  
ATOM   2669  CE2 PHE A 367     -59.114 -12.883 -69.993  1.00 90.13           C  
ANISOU 2669  CE2 PHE A 367    10648  11708  11887   -582   -814   -197       C  
ATOM   2670  CZ  PHE A 367     -59.477 -13.961 -69.202  1.00 89.54           C  
ANISOU 2670  CZ  PHE A 367    10590  11695  11735   -652   -795   -192       C  
ATOM   2671  N   ILE A 368     -54.890 -12.715 -65.609  1.00 92.03           N  
ANISOU 2671  N   ILE A 368    11014  11835  12119   -575   -852   -245       N  
ATOM   2672  CA  ILE A 368     -54.903 -13.743 -64.578  1.00 95.21           C  
ANISOU 2672  CA  ILE A 368    11456  12273  12445   -626   -846   -243       C  
ATOM   2673  C   ILE A 368     -55.929 -13.343 -63.523  1.00100.57           C  
ANISOU 2673  C   ILE A 368    12090  13039  13082   -637   -827   -294       C  
ATOM   2674  O   ILE A 368     -56.384 -12.198 -63.505  1.00105.13           O  
ANISOU 2674  O   ILE A 368    12608  13637  13697   -588   -826   -338       O  
ATOM   2675  CB  ILE A 368     -53.515 -13.931 -63.926  1.00 92.83           C  
ANISOU 2675  CB  ILE A 368    11203  11917  12150   -614   -869   -242       C  
ATOM   2676  CG1 ILE A 368     -52.834 -12.581 -63.697  1.00 91.22           C  
ANISOU 2676  CG1 ILE A 368    10964  11678  12016   -555   -882   -278       C  
ATOM   2677  CG2 ILE A 368     -52.637 -14.819 -64.790  1.00 91.94           C  
ANISOU 2677  CG2 ILE A 368    11144  11747  12041   -619   -888   -194       C  
ATOM   2678  CD1 ILE A 368     -51.785 -12.605 -62.608  1.00 91.87           C  
ANISOU 2678  CD1 ILE A 368    11077  11738  12090   -546   -899   -299       C  
ATOM   2679  N   ILE A 369     -56.297 -14.280 -62.652  1.00103.79           N  
ANISOU 2679  N   ILE A 369    12527  13500  13405   -701   -816   -291       N  
ATOM   2680  CA  ILE A 369     -57.255 -13.999 -61.586  1.00107.46           C  
ANISOU 2680  CA  ILE A 369    12946  14067  13815   -721   -793   -342       C  
ATOM   2681  C   ILE A 369     -56.612 -13.093 -60.533  1.00111.01           C  
ANISOU 2681  C   ILE A 369    13383  14504  14291   -670   -806   -390       C  
ATOM   2682  O   ILE A 369     -55.483 -13.338 -60.104  1.00110.93           O  
ANISOU 2682  O   ILE A 369    13428  14429  14289   -664   -826   -376       O  
ATOM   2683  CB  ILE A 369     -57.784 -15.300 -60.938  1.00108.43           C  
ANISOU 2683  CB  ILE A 369    13115  14252  13832   -822   -779   -318       C  
ATOM   2684  CG1 ILE A 369     -58.467 -16.202 -61.976  1.00107.39           C  
ANISOU 2684  CG1 ILE A 369    12999  14132  13671   -878   -771   -271       C  
ATOM   2685  CG2 ILE A 369     -58.736 -14.995 -59.788  1.00111.06           C  
ANISOU 2685  CG2 ILE A 369    13392  14706  14098   -850   -752   -374       C  
ATOM   2686  CD1 ILE A 369     -59.783 -15.684 -62.519  1.00106.38           C  
ANISOU 2686  CD1 ILE A 369    12779  14094  13545   -874   -744   -301       C  
ATOM   2687  N   ASP A 370     -57.341 -12.050 -60.133  1.00116.45           N  
ANISOU 2687  N   ASP A 370    13998  15256  14990   -627   -798   -453       N  
ATOM   2688  CA  ASP A 370     -56.873 -11.059 -59.157  1.00121.52           C  
ANISOU 2688  CA  ASP A 370    14622  15890  15658   -570   -813   -508       C  
ATOM   2689  C   ASP A 370     -57.472 -11.278 -57.761  1.00123.87           C  
ANISOU 2689  C   ASP A 370    14901  16294  15870   -606   -793   -552       C  
ATOM   2690  O   ASP A 370     -56.742 -11.514 -56.800  1.00126.29           O  
ANISOU 2690  O   ASP A 370    15250  16580  16152   -618   -801   -554       O  
ATOM   2691  CB  ASP A 370     -57.190  -9.644 -59.668  1.00123.37           C  
ANISOU 2691  CB  ASP A 370    14798  16111  15965   -484   -831   -554       C  
ATOM   2692  CG  ASP A 370     -56.652  -8.538 -58.765  1.00124.84           C  
ANISOU 2692  CG  ASP A 370    14973  16273  16186   -420   -858   -611       C  
ATOM   2693  OD1 ASP A 370     -55.623  -8.736 -58.075  1.00123.58           O  
ANISOU 2693  OD1 ASP A 370    14859  16067  16027   -430   -868   -600       O  
ATOM   2694  OD2 ASP A 370     -57.265  -7.448 -58.773  1.00125.16           O  
ANISOU 2694  OD2 ASP A 370    14962  16338  16252   -354   -874   -669       O  
ATOM   2695  N   LYS A 371     -58.797 -11.198 -57.661  1.00127.95           N  
ANISOU 2695  N   LYS A 371    15349  16929  16335   -622   -767   -590       N  
ATOM   2696  CA  LYS A 371     -59.493 -11.332 -56.382  1.00134.36           C  
ANISOU 2696  CA  LYS A 371    16127  17865  17057   -660   -743   -639       C  
ATOM   2697  C   LYS A 371     -60.876 -11.970 -56.573  1.00135.42           C  
ANISOU 2697  C   LYS A 371    16211  18133  17108   -734   -705   -644       C  
ATOM   2698  O   LYS A 371     -61.699 -11.474 -57.348  1.00133.72           O  
ANISOU 2698  O   LYS A 371    15927  17961  16917   -696   -702   -672       O  
ATOM   2699  CB  LYS A 371     -59.600  -9.959 -55.702  1.00139.40           C  
ANISOU 2699  CB  LYS A 371    16702  18534  17728   -565   -759   -726       C  
ATOM   2700  CG  LYS A 371     -60.378  -9.936 -54.394  1.00145.71           C  
ANISOU 2700  CG  LYS A 371    17450  19479  18434   -589   -734   -791       C  
ATOM   2701  CD  LYS A 371     -60.671  -8.504 -53.958  1.00146.57           C  
ANISOU 2701  CD  LYS A 371    17485  19624  18578   -477   -758   -887       C  
ATOM   2702  CE  LYS A 371     -61.821  -8.435 -52.960  1.00147.19           C  
ANISOU 2702  CE  LYS A 371    17480  19887  18557   -493   -728   -965       C  
ATOM   2703  NZ  LYS A 371     -61.498  -9.052 -51.642  1.00148.07           N  
ANISOU 2703  NZ  LYS A 371    17627  20046  18588   -562   -707   -961       N  
ATOM   2704  N   VAL A 372     -61.112 -13.076 -55.868  1.00136.90           N  
ANISOU 2704  N   VAL A 372    16437  18383  17194   -843   -681   -616       N  
ATOM   2705  CA  VAL A 372     -62.387 -13.801 -55.930  1.00139.11           C  
ANISOU 2705  CA  VAL A 372    16676  18799  17379   -939   -644   -616       C  
ATOM   2706  C   VAL A 372     -63.053 -13.795 -54.557  1.00143.01           C  
ANISOU 2706  C   VAL A 372    17123  19444  17769   -988   -615   -673       C  
ATOM   2707  O   VAL A 372     -62.454 -14.233 -53.573  1.00144.29           O  
ANISOU 2707  O   VAL A 372    17352  19587  17884  -1033   -618   -656       O  
ATOM   2708  CB  VAL A 372     -62.200 -15.262 -56.422  1.00136.03           C  
ANISOU 2708  CB  VAL A 372    16385  18357  16943  -1050   -644   -523       C  
ATOM   2709  CG1 VAL A 372     -63.488 -16.067 -56.293  1.00134.03           C  
ANISOU 2709  CG1 VAL A 372    16099  18251  16576  -1173   -606   -521       C  
ATOM   2710  CG2 VAL A 372     -61.722 -15.284 -57.863  1.00134.15           C  
ANISOU 2710  CG2 VAL A 372    16175  17996  16797  -1003   -668   -474       C  
ATOM   2711  N   ASP A 373     -64.286 -13.291 -54.499  1.00148.34           N  
ANISOU 2711  N   ASP A 373    17681  20274  18405   -977   -588   -745       N  
ATOM   2712  CA  ASP A 373     -65.078 -13.297 -53.266  1.00151.43           C  
ANISOU 2712  CA  ASP A 373    18009  20842  18685  -1031   -554   -807       C  
ATOM   2713  C   ASP A 373     -66.541 -13.639 -53.547  1.00148.80           C  
ANISOU 2713  C   ASP A 373    17580  20689  18267  -1105   -514   -837       C  
ATOM   2714  O   ASP A 373     -67.353 -12.753 -53.824  1.00148.39           O  
ANISOU 2714  O   ASP A 373    17412  20734  18234  -1022   -511   -920       O  
ATOM   2715  CB  ASP A 373     -64.965 -11.951 -52.536  1.00156.00           C  
ANISOU 2715  CB  ASP A 373    18518  21451  19303   -903   -571   -903       C  
ATOM   2716  CG  ASP A 373     -65.273 -12.064 -51.050  1.00161.00           C  
ANISOU 2716  CG  ASP A 373    19125  22222  19826   -957   -544   -951       C  
ATOM   2717  OD1 ASP A 373     -66.445 -12.311 -50.693  1.00163.22           O  
ANISOU 2717  OD1 ASP A 373    19320  22693  20002  -1027   -503   -996       O  
ATOM   2718  OD2 ASP A 373     -64.338 -11.899 -50.234  1.00162.11           O  
ANISOU 2718  OD2 ASP A 373    19325  22286  19980   -932   -563   -947       O  
ATOM   2719  N   GLY A 374     -66.863 -14.931 -53.472  1.00145.86           N  
ANISOU 2719  N   GLY A 374    17261  20359  17796  -1262   -488   -772       N  
ATOM   2720  CA  GLY A 374     -68.209 -15.429 -53.763  1.00145.90           C  
ANISOU 2720  CA  GLY A 374    17187  20536  17712  -1361   -448   -789       C  
ATOM   2721  C   GLY A 374     -68.614 -15.238 -55.215  1.00144.20           C  
ANISOU 2721  C   GLY A 374    16932  20285  17573  -1307   -459   -782       C  
ATOM   2722  O   GLY A 374     -68.070 -15.887 -56.114  1.00141.05           O  
ANISOU 2722  O   GLY A 374    16626  19744  17221  -1332   -480   -696       O  
ATOM   2723  N   ASP A 375     -69.573 -14.342 -55.438  1.00145.81           N  
ANISOU 2723  N   ASP A 375    16997  20620  17784  -1226   -450   -877       N  
ATOM   2724  CA  ASP A 375     -70.017 -13.984 -56.785  1.00146.62           C  
ANISOU 2724  CA  ASP A 375    17050  20696  17960  -1154   -465   -886       C  
ATOM   2725  C   ASP A 375     -69.152 -12.891 -57.414  1.00144.51           C  
ANISOU 2725  C   ASP A 375    16809  20258  17838   -986   -516   -895       C  
ATOM   2726  O   ASP A 375     -69.309 -12.573 -58.595  1.00146.01           O  
ANISOU 2726  O   ASP A 375    16985  20389  18101   -920   -537   -889       O  
ATOM   2727  CB  ASP A 375     -71.492 -13.558 -56.780  1.00154.28           C  
ANISOU 2727  CB  ASP A 375    17861  21892  18865  -1143   -438   -990       C  
ATOM   2728  CG  ASP A 375     -72.453 -14.743 -56.837  1.00159.39           C  
ANISOU 2728  CG  ASP A 375    18484  22686  19391  -1321   -392   -959       C  
ATOM   2729  OD1 ASP A 375     -72.130 -15.818 -56.284  1.00161.15           O  
ANISOU 2729  OD1 ASP A 375    18800  22892  19538  -1469   -374   -883       O  
ATOM   2730  OD2 ASP A 375     -73.542 -14.594 -57.434  1.00161.67           O  
ANISOU 2730  OD2 ASP A 375    18662  23107  19656  -1313   -379  -1014       O  
ATOM   2731  N   PHE A 376     -68.244 -12.321 -56.622  1.00141.99           N  
ANISOU 2731  N   PHE A 376    16531  19862  17556   -922   -537   -909       N  
ATOM   2732  CA  PHE A 376     -67.326 -11.283 -57.097  1.00136.71           C  
ANISOU 2732  CA  PHE A 376    15897  19029  17018   -778   -587   -914       C  
ATOM   2733  C   PHE A 376     -66.071 -11.879 -57.726  1.00134.24           C  
ANISOU 2733  C   PHE A 376    15714  18516  16772   -804   -608   -805       C  
ATOM   2734  O   PHE A 376     -65.466 -12.803 -57.177  1.00132.08           O  
ANISOU 2734  O   PHE A 376    15524  18205  16454   -897   -597   -744       O  
ATOM   2735  CB  PHE A 376     -66.941 -10.335 -55.955  1.00135.52           C  
ANISOU 2735  CB  PHE A 376    15725  18892  16874   -695   -604   -987       C  
ATOM   2736  CG  PHE A 376     -65.932  -9.289 -56.344  1.00131.39           C  
ANISOU 2736  CG  PHE A 376    15247  18196  16476   -565   -659   -988       C  
ATOM   2737  CD1 PHE A 376     -66.319  -8.160 -57.060  1.00130.59           C  
ANISOU 2737  CD1 PHE A 376    15093  18079  16445   -439   -697  -1048       C  
ATOM   2738  CD2 PHE A 376     -64.596  -9.427 -55.989  1.00130.63           C  
ANISOU 2738  CD2 PHE A 376    15252  17956  16424   -572   -676   -930       C  
ATOM   2739  CE1 PHE A 376     -65.392  -7.194 -57.419  1.00128.51           C  
ANISOU 2739  CE1 PHE A 376    14883  17655  16290   -335   -751  -1044       C  
ATOM   2740  CE2 PHE A 376     -63.664  -8.465 -56.347  1.00129.61           C  
ANISOU 2740  CE2 PHE A 376    15163  17678  16404   -467   -725   -931       C  
ATOM   2741  CZ  PHE A 376     -64.063  -7.346 -57.061  1.00128.34           C  
ANISOU 2741  CZ  PHE A 376    14955  17499  16309   -355   -762   -984       C  
ATOM   2742  N   CYS A 377     -65.688 -11.335 -58.879  1.00134.08           N  
ANISOU 2742  N   CYS A 377    15712  18375  16857   -719   -641   -785       N  
ATOM   2743  CA  CYS A 377     -64.462 -11.734 -59.564  1.00130.63           C  
ANISOU 2743  CA  CYS A 377    15384  17757  16491   -725   -664   -694       C  
ATOM   2744  C   CYS A 377     -63.852 -10.565 -60.339  1.00127.81           C  
ANISOU 2744  C   CYS A 377    15032  17276  16252   -599   -708   -706       C  
ATOM   2745  O   CYS A 377     -64.503  -9.982 -61.211  1.00128.36           O  
ANISOU 2745  O   CYS A 377    15051  17361  16357   -539   -721   -735       O  
ATOM   2746  CB  CYS A 377     -64.733 -12.910 -60.503  1.00130.46           C  
ANISOU 2746  CB  CYS A 377    15401  17723  16443   -817   -648   -618       C  
ATOM   2747  SG  CYS A 377     -63.234 -13.751 -61.051  1.00132.18           S  
ANISOU 2747  SG  CYS A 377    15758  17753  16711   -848   -672   -511       S  
ATOM   2748  N   SER A 378     -62.609 -10.223 -59.998  1.00122.31           N  
ANISOU 2748  N   SER A 378    14400  16461  15610   -564   -733   -686       N  
ATOM   2749  CA  SER A 378     -61.846  -9.198 -60.711  1.00119.34           C  
ANISOU 2749  CA  SER A 378    14047  15954  15341   -468   -776   -683       C  
ATOM   2750  C   SER A 378     -60.578  -9.815 -61.309  1.00119.12           C  
ANISOU 2750  C   SER A 378    14111  15789  15359   -502   -785   -594       C  
ATOM   2751  O   SER A 378     -60.160 -10.899 -60.895  1.00121.99           O  
ANISOU 2751  O   SER A 378    14527  16150  15674   -580   -768   -548       O  
ATOM   2752  CB  SER A 378     -61.486  -8.050 -59.774  1.00119.13           C  
ANISOU 2752  CB  SER A 378    14004  15917  15342   -387   -805   -752       C  
ATOM   2753  OG  SER A 378     -60.589  -8.485 -58.768  1.00121.20           O  
ANISOU 2753  OG  SER A 378    14316  16151  15580   -428   -797   -731       O  
ATOM   2754  N   LEU A 379     -59.970  -9.129 -62.277  1.00115.62           N  
ANISOU 2754  N   LEU A 379    13690  15236  15003   -443   -817   -573       N  
ATOM   2755  CA  LEU A 379     -58.801  -9.664 -62.985  1.00110.26           C  
ANISOU 2755  CA  LEU A 379    13084  14442  14365   -470   -825   -496       C  
ATOM   2756  C   LEU A 379     -57.573  -8.750 -62.949  1.00110.93           C  
ANISOU 2756  C   LEU A 379    13202  14419  14526   -416   -860   -496       C  
ATOM   2757  O   LEU A 379     -57.684  -7.546 -62.708  1.00113.07           O  
ANISOU 2757  O   LEU A 379    13447  14679  14834   -348   -887   -549       O  
ATOM   2758  CB  LEU A 379     -59.160  -9.994 -64.439  1.00105.24           C  
ANISOU 2758  CB  LEU A 379    12452  13782  13753   -479   -823   -450       C  
ATOM   2759  CG  LEU A 379     -60.289 -10.990 -64.698  1.00102.38           C  
ANISOU 2759  CG  LEU A 379    12064  13514  13320   -543   -791   -438       C  
ATOM   2760  CD1 LEU A 379     -60.415 -11.241 -66.187  1.00100.95           C  
ANISOU 2760  CD1 LEU A 379    11895  13286  13174   -543   -796   -389       C  
ATOM   2761  CD2 LEU A 379     -60.056 -12.299 -63.964  1.00102.43           C  
ANISOU 2761  CD2 LEU A 379    12118  13548  13251   -635   -770   -402       C  
ATOM   2762  N   ASN A 380     -56.403  -9.347 -63.167  1.00109.58           N  
ANISOU 2762  N   ASN A 380    13089  14172  14371   -447   -863   -441       N  
ATOM   2763  CA  ASN A 380     -55.169  -8.605 -63.413  1.00107.96           C  
ANISOU 2763  CA  ASN A 380    12914  13868  14238   -411   -893   -430       C  
ATOM   2764  C   ASN A 380     -54.853  -8.645 -64.899  1.00105.47           C  
ANISOU 2764  C   ASN A 380    12616  13489  13968   -413   -900   -376       C  
ATOM   2765  O   ASN A 380     -54.222  -9.586 -65.378  1.00105.02           O  
ANISOU 2765  O   ASN A 380    12594  13406  13901   -451   -891   -325       O  
ATOM   2766  CB  ASN A 380     -54.001  -9.213 -62.632  1.00109.17           C  
ANISOU 2766  CB  ASN A 380    13111  13991  14374   -439   -895   -414       C  
ATOM   2767  CG  ASN A 380     -53.935  -8.736 -61.197  1.00110.03           C  
ANISOU 2767  CG  ASN A 380    13209  14131  14463   -420   -901   -470       C  
ATOM   2768  OD1 ASN A 380     -53.635  -9.514 -60.288  1.00109.24           O  
ANISOU 2768  OD1 ASN A 380    13136  14057  14311   -454   -892   -469       O  
ATOM   2769  ND2 ASN A 380     -54.201  -7.452 -60.986  1.00112.11           N  
ANISOU 2769  ND2 ASN A 380    13439  14389  14766   -362   -923   -522       N  
ATOM   2770  N   GLU A 381     -55.318  -7.640 -65.632  1.00103.64           N  
ANISOU 2770  N   GLU A 381    12363  13233  13781   -369   -919   -391       N  
ATOM   2771  CA  GLU A 381     -55.055  -7.561 -67.066  1.00101.29           C  
ANISOU 2771  CA  GLU A 381    12083  12876  13525   -371   -928   -342       C  
ATOM   2772  C   GLU A 381     -53.700  -6.931 -67.323  1.00 97.06           C  
ANISOU 2772  C   GLU A 381    11581  12254  13044   -367   -952   -321       C  
ATOM   2773  O   GLU A 381     -53.259  -6.063 -66.574  1.00 99.64           O  
ANISOU 2773  O   GLU A 381    11910  12554  13394   -342   -975   -357       O  
ATOM   2774  CB  GLU A 381     -56.141  -6.757 -67.777  1.00104.28           C  
ANISOU 2774  CB  GLU A 381    12434  13263  13923   -326   -944   -365       C  
ATOM   2775  CG  GLU A 381     -57.264  -7.590 -68.359  1.00108.15           C  
ANISOU 2775  CG  GLU A 381    12897  13821  14372   -346   -918   -353       C  
ATOM   2776  CD  GLU A 381     -58.554  -6.802 -68.480  1.00115.88           C  
ANISOU 2776  CD  GLU A 381    13830  14847  15349   -290   -935   -410       C  
ATOM   2777  OE1 GLU A 381     -58.913  -6.387 -69.608  1.00119.75           O  
ANISOU 2777  OE1 GLU A 381    14324  15303  15869   -262   -954   -396       O  
ATOM   2778  OE2 GLU A 381     -59.208  -6.587 -67.436  1.00119.87           O  
ANISOU 2778  OE2 GLU A 381    14295  15430  15820   -269   -931   -473       O  
ATOM   2779  N   PHE A 382     -53.040  -7.379 -68.383  1.00 92.22           N  
ANISOU 2779  N   PHE A 382    10989  11601  12446   -395   -947   -265       N  
ATOM   2780  CA  PHE A 382     -51.768  -6.805 -68.797  1.00 88.01           C  
ANISOU 2780  CA  PHE A 382    10479  11001  11958   -403   -966   -242       C  
ATOM   2781  C   PHE A 382     -51.707  -6.649 -70.311  1.00 86.48           C  
ANISOU 2781  C   PHE A 382    10296  10769  11791   -414   -970   -195       C  
ATOM   2782  O   PHE A 382     -52.404  -7.341 -71.055  1.00 86.21           O  
ANISOU 2782  O   PHE A 382    10256  10761  11736   -420   -953   -170       O  
ATOM   2783  CB  PHE A 382     -50.601  -7.682 -68.350  1.00 86.20           C  
ANISOU 2783  CB  PHE A 382    10264  10777  11709   -433   -955   -227       C  
ATOM   2784  CG  PHE A 382     -50.583  -7.990 -66.883  1.00 83.87           C  
ANISOU 2784  CG  PHE A 382     9968  10518  11381   -428   -951   -267       C  
ATOM   2785  CD1 PHE A 382     -49.910  -7.164 -66.000  1.00 84.01           C  
ANISOU 2785  CD1 PHE A 382     9986  10512  11422   -413   -972   -303       C  
ATOM   2786  CD2 PHE A 382     -51.202  -9.129 -66.393  1.00 82.76           C  
ANISOU 2786  CD2 PHE A 382     9830  10432  11180   -446   -929   -266       C  
ATOM   2787  CE1 PHE A 382     -49.871  -7.460 -64.648  1.00 84.20           C  
ANISOU 2787  CE1 PHE A 382    10011  10569  11412   -408   -969   -340       C  
ATOM   2788  CE2 PHE A 382     -51.169  -9.431 -65.045  1.00 82.47           C  
ANISOU 2788  CE2 PHE A 382     9800  10429  11106   -449   -927   -300       C  
ATOM   2789  CZ  PHE A 382     -50.504  -8.595 -64.170  1.00 82.96           C  
ANISOU 2789  CZ  PHE A 382     9859  10469  11193   -426   -946   -338       C  
ATOM   2790  N   SER A 383     -50.861  -5.736 -70.761  1.00 85.10           N  
ANISOU 2790  N   SER A 383    10140  10535  11658   -422   -994   -181       N  
ATOM   2791  CA  SER A 383     -50.609  -5.589 -72.179  1.00 85.59           C  
ANISOU 2791  CA  SER A 383    10216  10563  11739   -444   -997   -132       C  
ATOM   2792  C   SER A 383     -49.117  -5.680 -72.434  1.00 84.87           C  
ANISOU 2792  C   SER A 383    10131  10457  11656   -487   -994   -105       C  
ATOM   2793  O   SER A 383     -48.304  -5.220 -71.630  1.00 85.05           O  
ANISOU 2793  O   SER A 383    10155  10467  11692   -495  -1007   -129       O  
ATOM   2794  CB  SER A 383     -51.185  -4.276 -72.717  1.00 87.78           C  
ANISOU 2794  CB  SER A 383    10516  10784  12051   -420  -1036   -138       C  
ATOM   2795  OG  SER A 383     -50.645  -3.154 -72.039  1.00 91.20           O  
ANISOU 2795  OG  SER A 383    10969  11168  12511   -415  -1071   -167       O  
ATOM   2796  N   ILE A 384     -48.767  -6.289 -73.559  1.00 83.50           N  
ANISOU 2796  N   ILE A 384     9957  10294  11474   -512   -978    -60       N  
ATOM   2797  CA  ILE A 384     -47.380  -6.517 -73.912  1.00 82.16           C  
ANISOU 2797  CA  ILE A 384     9781  10133  11303   -551   -971    -40       C  
ATOM   2798  C   ILE A 384     -47.042  -5.700 -75.151  1.00 82.18           C  
ANISOU 2798  C   ILE A 384     9797  10099  11327   -587   -982     -1       C  
ATOM   2799  O   ILE A 384     -47.666  -5.875 -76.201  1.00 82.23           O  
ANISOU 2799  O   ILE A 384     9812  10101  11330   -585   -976     30       O  
ATOM   2800  CB  ILE A 384     -47.115  -8.023 -74.153  1.00 81.68           C  
ANISOU 2800  CB  ILE A 384     9707  10126  11201   -549   -946    -26       C  
ATOM   2801  CG1 ILE A 384     -47.305  -8.823 -72.857  1.00 81.22           C  
ANISOU 2801  CG1 ILE A 384     9649  10096  11112   -525   -941    -61       C  
ATOM   2802  CG2 ILE A 384     -45.718  -8.258 -74.712  1.00 82.29           C  
ANISOU 2802  CG2 ILE A 384     9767  10226  11270   -579   -942    -11       C  
ATOM   2803  CD1 ILE A 384     -48.735  -9.236 -72.572  1.00 80.24           C  
ANISOU 2803  CD1 ILE A 384     9532   9986  10969   -504   -933    -68       C  
ATOM   2804  N   THR A 385     -46.075  -4.791 -75.018  1.00 82.05           N  
ANISOU 2804  N   THR A 385     9786  10057  11330   -626  -1000     -3       N  
ATOM   2805  CA  THR A 385     -45.571  -4.028 -76.163  1.00 82.55           C  
ANISOU 2805  CA  THR A 385     9868  10091  11404   -681  -1011     37       C  
ATOM   2806  C   THR A 385     -44.598  -4.867 -76.978  1.00 83.55           C  
ANISOU 2806  C   THR A 385     9961  10281  11502   -717   -981     64       C  
ATOM   2807  O   THR A 385     -44.037  -5.847 -76.474  1.00 82.99           O  
ANISOU 2807  O   THR A 385     9856  10268  11408   -700   -962     41       O  
ATOM   2808  CB  THR A 385     -44.861  -2.733 -75.739  1.00 83.02           C  
ANISOU 2808  CB  THR A 385     9952  10102  11489   -724  -1045     27       C  
ATOM   2809  OG1 THR A 385     -44.019  -2.994 -74.610  1.00 84.20           O  
ANISOU 2809  OG1 THR A 385    10070  10286  11634   -724  -1039    -11       O  
ATOM   2810  CG2 THR A 385     -45.867  -1.654 -75.388  1.00 83.56           C  
ANISOU 2810  CG2 THR A 385    10070  10092  11585   -690  -1089      9       C  
ATOM   2811  N   GLY A 386     -44.396  -4.474 -78.234  1.00 85.32           N  
ANISOU 2811  N   GLY A 386    10197  10496  11723   -764   -981    108       N  
ATOM   2812  CA  GLY A 386     -43.527  -5.216 -79.149  1.00 88.86           C  
ANISOU 2812  CA  GLY A 386    10607  11014  12138   -796   -953    131       C  
ATOM   2813  C   GLY A 386     -44.352  -6.284 -79.830  1.00 90.59           C  
ANISOU 2813  C   GLY A 386    10824  11255  12339   -750   -934    148       C  
ATOM   2814  O   GLY A 386     -44.958  -7.116 -79.163  1.00 91.28           O  
ANISOU 2814  O   GLY A 386    10908  11353  12420   -695   -929    124       O  
ATOM   2815  N   SER A 387     -44.383  -6.261 -81.158  1.00 92.53           N  
ANISOU 2815  N   SER A 387    11075  11508  12571   -778   -926    191       N  
ATOM   2816  CA  SER A 387     -45.347  -7.064 -81.903  1.00 92.20           C  
ANISOU 2816  CA  SER A 387    11042  11471  12518   -737   -915    211       C  
ATOM   2817  C   SER A 387     -44.710  -8.042 -82.885  1.00 93.07           C  
ANISOU 2817  C   SER A 387    11119  11653  12588   -744   -892    229       C  
ATOM   2818  O   SER A 387     -45.420  -8.772 -83.582  1.00 94.05           O  
ANISOU 2818  O   SER A 387    11250  11783  12699   -712   -884    247       O  
ATOM   2819  CB  SER A 387     -46.336  -6.152 -82.628  1.00 93.80           C  
ANISOU 2819  CB  SER A 387    11293  11603  12742   -743   -936    243       C  
ATOM   2820  OG  SER A 387     -45.644  -5.238 -83.459  1.00 97.00           O  
ANISOU 2820  OG  SER A 387    11717  11993  13145   -814   -945    279       O  
ATOM   2821  N   THR A 388     -43.380  -8.058 -82.936  1.00 94.54           N  
ANISOU 2821  N   THR A 388    11266  11899  12753   -783   -882    218       N  
ATOM   2822  CA  THR A 388     -42.649  -9.018 -83.774  1.00 94.88           C  
ANISOU 2822  CA  THR A 388    11268  12029  12753   -779   -863    220       C  
ATOM   2823  C   THR A 388     -42.339 -10.301 -82.983  1.00 96.69           C  
ANISOU 2823  C   THR A 388    11473  12304  12959   -715   -865    173       C  
ATOM   2824  O   THR A 388     -43.032 -10.611 -82.009  1.00 99.09           O  
ANISOU 2824  O   THR A 388    11804  12567  13279   -673   -876    154       O  
ATOM   2825  CB  THR A 388     -41.369  -8.399 -84.360  1.00 92.71           C  
ANISOU 2825  CB  THR A 388    10954  11813  12456   -857   -853    228       C  
ATOM   2826  OG1 THR A 388     -40.404  -8.219 -83.319  1.00 92.34           O  
ANISOU 2826  OG1 THR A 388    10874  11799  12410   -870   -857    184       O  
ATOM   2827  CG2 THR A 388     -41.682  -7.056 -85.008  1.00 92.65           C  
ANISOU 2827  CG2 THR A 388    10991  11744  12468   -930   -861    277       C  
ATOM   2828  N   TYR A 389     -41.321 -11.056 -83.394  1.00 95.50           N  
ANISOU 2828  N   TYR A 389    11277  12241  12766   -706   -858    153       N  
ATOM   2829  CA  TYR A 389     -40.972 -12.274 -82.658  1.00 93.26           C  
ANISOU 2829  CA  TYR A 389    10984  11994  12456   -638   -872    105       C  
ATOM   2830  C   TYR A 389     -39.851 -12.057 -81.642  1.00 91.50           C  
ANISOU 2830  C   TYR A 389    10724  11810  12229   -645   -880     56       C  
ATOM   2831  O   TYR A 389     -39.556 -12.946 -80.841  1.00 89.89           O  
ANISOU 2831  O   TYR A 389    10523  11625  12006   -588   -899     12       O  
ATOM   2832  CB  TYR A 389     -40.661 -13.439 -83.609  1.00 93.93           C  
ANISOU 2832  CB  TYR A 389    11050  12145  12491   -596   -874     99       C  
ATOM   2833  CG  TYR A 389     -41.897 -14.067 -84.233  1.00 95.24           C  
ANISOU 2833  CG  TYR A 389    11263  12264  12657   -565   -877    134       C  
ATOM   2834  CD1 TYR A 389     -42.890 -14.653 -83.439  1.00 94.93           C  
ANISOU 2834  CD1 TYR A 389    11275  12164  12628   -526   -892    131       C  
ATOM   2835  CD2 TYR A 389     -42.075 -14.077 -85.614  1.00 96.45           C  
ANISOU 2835  CD2 TYR A 389    11409  12439  12796   -580   -863    170       C  
ATOM   2836  CE1 TYR A 389     -44.021 -15.227 -84.004  1.00 94.58           C  
ANISOU 2836  CE1 TYR A 389    11270  12085  12581   -506   -894    162       C  
ATOM   2837  CE2 TYR A 389     -43.204 -14.648 -86.190  1.00 97.74           C  
ANISOU 2837  CE2 TYR A 389    11615  12561  12960   -551   -868    200       C  
ATOM   2838  CZ  TYR A 389     -44.176 -15.221 -85.383  1.00 96.04           C  
ANISOU 2838  CZ  TYR A 389    11446  12288  12755   -516   -883    195       C  
ATOM   2839  OH  TYR A 389     -45.296 -15.791 -85.961  1.00 93.66           O  
ANISOU 2839  OH  TYR A 389    11182  11954  12451   -496   -887    223       O  
ATOM   2840  N   ALA A 390     -39.260 -10.860 -81.668  1.00 90.98           N  
ANISOU 2840  N   ALA A 390    10634  11752  12182   -717   -870     63       N  
ATOM   2841  CA  ALA A 390     -38.111 -10.509 -80.826  1.00 90.01           C  
ANISOU 2841  CA  ALA A 390    10468  11675  12055   -738   -876     17       C  
ATOM   2842  C   ALA A 390     -38.500 -10.388 -79.366  1.00 91.07           C  
ANISOU 2842  C   ALA A 390    10637  11745  12220   -707   -894     -7       C  
ATOM   2843  O   ALA A 390     -39.587  -9.890 -79.061  1.00 92.91           O  
ANISOU 2843  O   ALA A 390    10920  11891  12489   -709   -897     18       O  
ATOM   2844  CB  ALA A 390     -37.485  -9.210 -81.300  1.00 89.44           C  
ANISOU 2844  CB  ALA A 390    10371  11620  11991   -838   -863     40       C  
ATOM   2845  N   PRO A 391     -37.622 -10.855 -78.457  1.00 91.72           N  
ANISOU 2845  N   PRO A 391    10690  11874  12283   -674   -909    -64       N  
ATOM   2846  CA  PRO A 391     -37.836 -10.677 -77.021  1.00 92.65           C  
ANISOU 2846  CA  PRO A 391    10836  11939  12426   -651   -927    -92       C  
ATOM   2847  C   PRO A 391     -37.527  -9.248 -76.619  1.00 94.63           C  
ANISOU 2847  C   PRO A 391    11078  12161  12713   -722   -925    -88       C  
ATOM   2848  O   PRO A 391     -36.624  -9.019 -75.818  1.00 99.71           O  
ANISOU 2848  O   PRO A 391    11692  12837  13356   -729   -936   -131       O  
ATOM   2849  CB  PRO A 391     -36.819 -11.633 -76.385  1.00 91.59           C  
ANISOU 2849  CB  PRO A 391    10671  11875  12252   -595   -947   -155       C  
ATOM   2850  CG  PRO A 391     -35.761 -11.804 -77.411  1.00 92.68           C  
ANISOU 2850  CG  PRO A 391    10742  12117  12354   -612   -938   -169       C  
ATOM   2851  CD  PRO A 391     -36.461 -11.719 -78.737  1.00 92.16           C  
ANISOU 2851  CD  PRO A 391    10689  12037  12289   -641   -916   -111       C  
ATOM   2852  N   GLU A 392     -38.262  -8.296 -77.184  1.00 95.15           N  
ANISOU 2852  N   GLU A 392    11176  12165  12811   -771   -918    -39       N  
ATOM   2853  CA  GLU A 392     -38.009  -6.883 -76.944  1.00 96.06           C  
ANISOU 2853  CA  GLU A 392    11298  12240  12957   -843   -926    -29       C  
ATOM   2854  C   GLU A 392     -39.324  -6.140 -76.725  1.00 93.29           C  
ANISOU 2854  C   GLU A 392    11015  11782  12649   -837   -939      0       C  
ATOM   2855  O   GLU A 392     -39.995  -5.743 -77.679  1.00 92.97           O  
ANISOU 2855  O   GLU A 392    11004  11703  12616   -860   -936     45       O  
ATOM   2856  CB  GLU A 392     -37.197  -6.283 -78.103  1.00103.05           C  
ANISOU 2856  CB  GLU A 392    12151  13178  13824   -932   -912      0       C  
ATOM   2857  CG  GLU A 392     -35.714  -6.669 -78.097  1.00113.49           C  
ANISOU 2857  CG  GLU A 392    13392  14620  15105   -953   -903    -44       C  
ATOM   2858  CD  GLU A 392     -35.059  -6.642 -79.479  1.00121.54           C  
ANISOU 2858  CD  GLU A 392    14366  15728  16085  -1017   -880    -20       C  
ATOM   2859  OE1 GLU A 392     -35.589  -5.952 -80.381  1.00124.24           O  
ANISOU 2859  OE1 GLU A 392    14746  16024  16436  -1077   -874     38       O  
ATOM   2860  OE2 GLU A 392     -34.006  -7.311 -79.664  1.00121.61           O  
ANISOU 2860  OE2 GLU A 392    14299  15858  16048  -1007   -870    -63       O  
ATOM   2861  N   GLY A 393     -39.692  -5.974 -75.456  1.00 92.23           N  
ANISOU 2861  N   GLY A 393    10902  11604  12537   -799   -956    -32       N  
ATOM   2862  CA  GLY A 393     -40.933  -5.293 -75.081  1.00 92.43           C  
ANISOU 2862  CA  GLY A 393    10981  11540  12596   -779   -972    -22       C  
ATOM   2863  C   GLY A 393     -41.171  -5.160 -73.583  1.00 92.38           C  
ANISOU 2863  C   GLY A 393    10987  11508  12606   -738   -989    -68       C  
ATOM   2864  O   GLY A 393     -40.387  -5.647 -72.763  1.00 92.38           O  
ANISOU 2864  O   GLY A 393    10958  11549  12590   -723   -989   -106       O  
ATOM   2865  N   GLU A 394     -42.261  -4.488 -73.230  1.00 92.43           N  
ANISOU 2865  N   GLU A 394    11034  11446  12638   -715  -1007    -68       N  
ATOM   2866  CA  GLU A 394     -42.643  -4.320 -71.836  1.00 93.32           C  
ANISOU 2866  CA  GLU A 394    11157  11537  12762   -672  -1022   -113       C  
ATOM   2867  C   GLU A 394     -43.980  -4.995 -71.574  1.00 93.00           C  
ANISOU 2867  C   GLU A 394    11129  11496  12709   -614  -1011   -118       C  
ATOM   2868  O   GLU A 394     -44.853  -5.029 -72.443  1.00 95.06           O  
ANISOU 2868  O   GLU A 394    11403  11741  12971   -607  -1006    -88       O  
ATOM   2869  CB  GLU A 394     -42.778  -2.839 -71.479  1.00 97.18           C  
ANISOU 2869  CB  GLU A 394    11680  11954  13287   -692  -1059   -122       C  
ATOM   2870  CG  GLU A 394     -41.810  -1.898 -72.179  1.00102.42           C  
ANISOU 2870  CG  GLU A 394    12352  12598  13964   -773  -1076    -96       C  
ATOM   2871  CD  GLU A 394     -41.900  -0.475 -71.652  1.00106.29           C  
ANISOU 2871  CD  GLU A 394    12890  13007  14487   -790  -1124   -111       C  
ATOM   2872  OE1 GLU A 394     -41.436  -0.223 -70.510  1.00105.69           O  
ANISOU 2872  OE1 GLU A 394    12807  12931  14420   -780  -1139   -154       O  
ATOM   2873  OE2 GLU A 394     -42.430   0.392 -72.388  1.00107.88           O  
ANISOU 2873  OE2 GLU A 394    13143  13142  14703   -810  -1153    -81       O  
ATOM   2874  N   VAL A 395     -44.134  -5.532 -70.371  1.00 90.52           N  
ANISOU 2874  N   VAL A 395    10810  11202  12379   -576  -1009   -156       N  
ATOM   2875  CA  VAL A 395     -45.440  -5.913 -69.870  1.00 88.04           C  
ANISOU 2875  CA  VAL A 395    10507  10891  12051   -533  -1003   -170       C  
ATOM   2876  C   VAL A 395     -45.943  -4.687 -69.131  1.00 88.93           C  
ANISOU 2876  C   VAL A 395    10634  10960  12193   -514  -1031   -203       C  
ATOM   2877  O   VAL A 395     -45.264  -4.181 -68.242  1.00 91.13           O  
ANISOU 2877  O   VAL A 395    10912  11227  12483   -517  -1048   -235       O  
ATOM   2878  CB  VAL A 395     -45.349  -7.123 -68.922  1.00 87.08           C  
ANISOU 2878  CB  VAL A 395    10381  10816  11888   -510   -989   -193       C  
ATOM   2879  CG1 VAL A 395     -46.637  -7.310 -68.134  1.00 86.27           C  
ANISOU 2879  CG1 VAL A 395    10287  10725  11766   -480   -984   -216       C  
ATOM   2880  CG2 VAL A 395     -45.012  -8.380 -69.709  1.00 86.86           C  
ANISOU 2880  CG2 VAL A 395    10351  10824  11826   -517   -972   -164       C  
ATOM   2881  N   LEU A 396     -47.104  -4.184 -69.526  1.00 89.90           N  
ANISOU 2881  N   LEU A 396    10770  11058  12327   -491  -1041   -201       N  
ATOM   2882  CA  LEU A 396     -47.695  -3.029 -68.858  1.00 91.96           C  
ANISOU 2882  CA  LEU A 396    11047  11280  12611   -458  -1076   -241       C  
ATOM   2883  C   LEU A 396     -48.992  -3.437 -68.166  1.00 96.79           C  
ANISOU 2883  C   LEU A 396    11643  11936  13196   -407  -1065   -277       C  
ATOM   2884  O   LEU A 396     -49.664  -4.388 -68.587  1.00 97.93           O  
ANISOU 2884  O   LEU A 396    11772  12123  13311   -406  -1035   -258       O  
ATOM   2885  CB  LEU A 396     -47.981  -1.899 -69.851  1.00 89.29           C  
ANISOU 2885  CB  LEU A 396    10743  10874  12306   -464  -1111   -220       C  
ATOM   2886  CG  LEU A 396     -47.075  -1.708 -71.064  1.00 88.25           C  
ANISOU 2886  CG  LEU A 396    10628  10714  12187   -528  -1111   -164       C  
ATOM   2887  CD1 LEU A 396     -47.887  -1.166 -72.223  1.00 89.80           C  
ANISOU 2887  CD1 LEU A 396    10857  10866  12394   -522  -1132   -134       C  
ATOM   2888  CD2 LEU A 396     -45.912  -0.790 -70.758  1.00 88.81           C  
ANISOU 2888  CD2 LEU A 396    10719  10745  12281   -575  -1141   -168       C  
ATOM   2889  N   LYS A 397     -49.320  -2.722 -67.092  1.00100.06           N  
ANISOU 2889  N   LYS A 397    12058  12344  13616   -369  -1090   -332       N  
ATOM   2890  CA  LYS A 397     -50.624  -2.809 -66.439  1.00 99.88           C  
ANISOU 2890  CA  LYS A 397    12013  12370  13566   -319  -1086   -377       C  
ATOM   2891  C   LYS A 397     -51.068  -1.374 -66.202  1.00102.52           C  
ANISOU 2891  C   LYS A 397    12366  12655  13931   -269  -1140   -423       C  
ATOM   2892  O   LYS A 397     -50.339  -0.585 -65.590  1.00105.22           O  
ANISOU 2892  O   LYS A 397    12729  12951  14297   -268  -1173   -445       O  
ATOM   2893  CB  LYS A 397     -50.511  -3.570 -65.123  1.00 96.81           C  
ANISOU 2893  CB  LYS A 397    11603  12042  13137   -319  -1061   -409       C  
ATOM   2894  CG  LYS A 397     -51.811  -3.722 -64.363  1.00 96.02           C  
ANISOU 2894  CG  LYS A 397    11472  12012  12997   -280  -1051   -458       C  
ATOM   2895  CD  LYS A 397     -51.518  -4.264 -62.978  1.00 98.27           C  
ANISOU 2895  CD  LYS A 397    11748  12345  13243   -287  -1034   -489       C  
ATOM   2896  CE  LYS A 397     -52.793  -4.552 -62.205  1.00101.66           C  
ANISOU 2896  CE  LYS A 397    12142  12864  13618   -264  -1016   -535       C  
ATOM   2897  NZ  LYS A 397     -52.494  -4.747 -60.757  1.00103.98           N  
ANISOU 2897  NZ  LYS A 397    12434  13196  13878   -264  -1011   -574       N  
ATOM   2898  N   ASN A 398     -52.249  -1.033 -66.707  1.00103.99           N  
ANISOU 2898  N   ASN A 398    12547  12848  14115   -225  -1155   -440       N  
ATOM   2899  CA  ASN A 398     -52.729   0.355 -66.714  1.00107.13           C  
ANISOU 2899  CA  ASN A 398    12975  13187  14540   -167  -1221   -483       C  
ATOM   2900  C   ASN A 398     -51.722   1.298 -67.368  1.00106.78           C  
ANISOU 2900  C   ASN A 398    12994  13034  14541   -203  -1266   -446       C  
ATOM   2901  O   ASN A 398     -51.356   2.325 -66.800  1.00107.53           O  
ANISOU 2901  O   ASN A 398    13125  13071  14659   -185  -1318   -479       O  
ATOM   2902  CB  ASN A 398     -53.087   0.837 -65.300  1.00109.32           C  
ANISOU 2902  CB  ASN A 398    13234  13498  14804   -109  -1243   -563       C  
ATOM   2903  CG  ASN A 398     -54.120  -0.043 -64.624  1.00110.59           C  
ANISOU 2903  CG  ASN A 398    13331  13778  14910    -85  -1198   -602       C  
ATOM   2904  OD1 ASN A 398     -55.215  -0.259 -65.150  1.00112.43           O  
ANISOU 2904  OD1 ASN A 398    13536  14060  15123    -58  -1189   -613       O  
ATOM   2905  ND2 ASN A 398     -53.777  -0.552 -63.445  1.00110.08           N  
ANISOU 2905  ND2 ASN A 398    13242  13765  14816   -100  -1170   -625       N  
ATOM   2906  N   ASP A 399     -51.269   0.916 -68.560  1.00110.09           N  
ANISOU 2906  N   ASP A 399    13428  13431  14968   -260  -1245   -376       N  
ATOM   2907  CA  ASP A 399     -50.292   1.679 -69.357  1.00113.14           C  
ANISOU 2907  CA  ASP A 399    13870  13728  15386   -316  -1278   -329       C  
ATOM   2908  C   ASP A 399     -48.962   1.984 -68.658  1.00112.53           C  
ANISOU 2908  C   ASP A 399    13804  13626  15324   -365  -1286   -330       C  
ATOM   2909  O   ASP A 399     -48.081   2.608 -69.254  1.00115.20           O  
ANISOU 2909  O   ASP A 399    14184  13903  15682   -426  -1310   -292       O  
ATOM   2910  CB  ASP A 399     -50.917   2.957 -69.925  1.00116.09           C  
ANISOU 2910  CB  ASP A 399    14310  14016  15783   -277  -1353   -342       C  
ATOM   2911  CG  ASP A 399     -52.079   2.669 -70.850  1.00120.67           C  
ANISOU 2911  CG  ASP A 399    14881  14616  16349   -237  -1348   -333       C  
ATOM   2912  OD1 ASP A 399     -51.925   1.815 -71.753  1.00123.98           O  
ANISOU 2912  OD1 ASP A 399    15281  15065  16758   -283  -1300   -276       O  
ATOM   2913  OD2 ASP A 399     -53.147   3.294 -70.673  1.00123.66           O  
ANISOU 2913  OD2 ASP A 399    15271  14985  16727   -155  -1395   -388       O  
ATOM   2914  N   LYS A 400     -48.822   1.553 -67.405  1.00108.10           N  
ANISOU 2914  N   LYS A 400    13205  13118  14748   -343  -1265   -373       N  
ATOM   2915  CA  LYS A 400     -47.562   1.694 -66.687  1.00104.83           C  
ANISOU 2915  CA  LYS A 400    12791  12693  14343   -386  -1268   -378       C  
ATOM   2916  C   LYS A 400     -46.844   0.348 -66.660  1.00101.24           C  
ANISOU 2916  C   LYS A 400    12290  12312  13864   -426  -1205   -350       C  
ATOM   2917  O   LYS A 400     -47.469  -0.679 -66.367  1.00101.32           O  
ANISOU 2917  O   LYS A 400    12266  12389  13842   -399  -1166   -359       O  
ATOM   2918  CB  LYS A 400     -47.783   2.247 -65.276  1.00107.41           C  
ANISOU 2918  CB  LYS A 400    13119  13019  14672   -330  -1299   -450       C  
ATOM   2919  CG  LYS A 400     -48.610   3.524 -65.261  1.00114.26           C  
ANISOU 2919  CG  LYS A 400    14034  13820  15559   -270  -1369   -490       C  
ATOM   2920  CD  LYS A 400     -48.213   4.496 -64.161  1.00117.18           C  
ANISOU 2920  CD  LYS A 400    14432  14144  15945   -246  -1424   -544       C  
ATOM   2921  CE  LYS A 400     -48.946   5.819 -64.351  1.00120.46           C  
ANISOU 2921  CE  LYS A 400    14913  14476  16379   -186  -1509   -580       C  
ATOM   2922  NZ  LYS A 400     -48.517   6.886 -63.401  1.00120.23           N  
ANISOU 2922  NZ  LYS A 400    14927  14383  16368   -164  -1576   -630       N  
ATOM   2923  N   PRO A 401     -45.537   0.343 -67.003  1.00 96.29           N  
ANISOU 2923  N   PRO A 401    11664  11674  13246   -494  -1200   -319       N  
ATOM   2924  CA  PRO A 401     -44.722  -0.875 -67.007  1.00 94.05           C  
ANISOU 2924  CA  PRO A 401    11339  11457  12936   -524  -1152   -300       C  
ATOM   2925  C   PRO A 401     -44.657  -1.548 -65.636  1.00 94.28           C  
ANISOU 2925  C   PRO A 401    11344  11536  12942   -487  -1137   -346       C  
ATOM   2926  O   PRO A 401     -44.534  -0.868 -64.617  1.00 94.96           O  
ANISOU 2926  O   PRO A 401    11439  11601  13040   -467  -1166   -390       O  
ATOM   2927  CB  PRO A 401     -43.342  -0.371 -67.425  1.00 92.52           C  
ANISOU 2927  CB  PRO A 401    11148  11243  12758   -596  -1165   -278       C  
ATOM   2928  CG  PRO A 401     -43.626   0.844 -68.234  1.00 92.77           C  
ANISOU 2928  CG  PRO A 401    11232  11198  12818   -623  -1206   -253       C  
ATOM   2929  CD  PRO A 401     -44.806   1.488 -67.574  1.00 93.89           C  
ANISOU 2929  CD  PRO A 401    11403  11297  12971   -550  -1242   -296       C  
ATOM   2930  N   ILE A 402     -44.760  -2.873 -65.631  1.00 94.69           N  
ANISOU 2930  N   ILE A 402    11372  11649  12957   -480  -1098   -335       N  
ATOM   2931  CA  ILE A 402     -44.736  -3.669 -64.409  1.00 96.80           C  
ANISOU 2931  CA  ILE A 402    11627  11962  13190   -452  -1084   -371       C  
ATOM   2932  C   ILE A 402     -43.757  -4.836 -64.568  1.00 97.46           C  
ANISOU 2932  C   ILE A 402    11696  12087  13245   -474  -1062   -354       C  
ATOM   2933  O   ILE A 402     -43.401  -5.205 -65.691  1.00 98.34           O  
ANISOU 2933  O   ILE A 402    11800  12206  13356   -501  -1050   -314       O  
ATOM   2934  CB  ILE A 402     -46.157  -4.175 -64.047  1.00100.20           C  
ANISOU 2934  CB  ILE A 402    12055  12426  13588   -413  -1066   -384       C  
ATOM   2935  CG1 ILE A 402     -46.315  -4.276 -62.525  1.00107.72           C  
ANISOU 2935  CG1 ILE A 402    13005  13407  14515   -384  -1070   -437       C  
ATOM   2936  CG2 ILE A 402     -46.490  -5.500 -64.738  1.00 96.50           C  
ANISOU 2936  CG2 ILE A 402    11582  11998  13082   -427  -1032   -345       C  
ATOM   2937  CD1 ILE A 402     -47.703  -3.922 -62.015  1.00113.28           C  
ANISOU 2937  CD1 ILE A 402    13701  14134  15204   -343  -1071   -472       C  
ATOM   2938  N   ARG A 403     -43.308  -5.410 -63.456  1.00 96.78           N  
ANISOU 2938  N   ARG A 403    11610  12030  13132   -457  -1063   -387       N  
ATOM   2939  CA  ARG A 403     -42.439  -6.574 -63.536  1.00 96.15           C  
ANISOU 2939  CA  ARG A 403    11525  11989  13019   -462  -1054   -379       C  
ATOM   2940  C   ARG A 403     -43.244  -7.848 -63.359  1.00 96.99           C  
ANISOU 2940  C   ARG A 403    11652  12125  13073   -443  -1035   -368       C  
ATOM   2941  O   ARG A 403     -43.748  -8.118 -62.269  1.00 98.44           O  
ANISOU 2941  O   ARG A 403    11853  12322  13227   -424  -1036   -395       O  
ATOM   2942  CB  ARG A 403     -41.330  -6.505 -62.497  1.00 97.22           C  
ANISOU 2942  CB  ARG A 403    11654  12134  13151   -454  -1074   -422       C  
ATOM   2943  CG  ARG A 403     -40.165  -7.418 -62.828  1.00 99.15           C  
ANISOU 2943  CG  ARG A 403    11884  12416  13370   -457  -1076   -421       C  
ATOM   2944  CD  ARG A 403     -39.096  -7.365 -61.759  1.00 99.05           C  
ANISOU 2944  CD  ARG A 403    11863  12418  13352   -443  -1099   -470       C  
ATOM   2945  NE  ARG A 403     -37.772  -7.355 -62.364  1.00100.54           N  
ANISOU 2945  NE  ARG A 403    12012  12640  13547   -464  -1107   -477       N  
ATOM   2946  CZ  ARG A 403     -37.118  -6.247 -62.696  1.00103.05           C  
ANISOU 2946  CZ  ARG A 403    12298  12950  13904   -509  -1113   -479       C  
ATOM   2947  NH1 ARG A 403     -37.665  -5.058 -62.471  1.00104.92           N  
ANISOU 2947  NH1 ARG A 403    12549  13133  14180   -530  -1121   -476       N  
ATOM   2948  NH2 ARG A 403     -35.915  -6.324 -63.248  1.00104.07           N  
ANISOU 2948  NH2 ARG A 403    12383  13129  14029   -535  -1116   -489       N  
ATOM   2949  N   SER A 404     -43.352  -8.631 -64.433  1.00 97.70           N  
ANISOU 2949  N   SER A 404    11745  12229  13147   -454  -1021   -329       N  
ATOM   2950  CA  SER A 404     -44.142  -9.869 -64.438  1.00 97.98           C  
ANISOU 2950  CA  SER A 404    11809  12287  13131   -447  -1008   -311       C  
ATOM   2951  C   SER A 404     -43.928 -10.710 -63.182  1.00 97.80           C  
ANISOU 2951  C   SER A 404    11818  12282  13057   -431  -1020   -340       C  
ATOM   2952  O   SER A 404     -44.883 -11.257 -62.629  1.00 96.51           O  
ANISOU 2952  O   SER A 404    11682  12134  12853   -435  -1011   -338       O  
ATOM   2953  CB  SER A 404     -43.827 -10.718 -65.678  1.00 98.90           C  
ANISOU 2953  CB  SER A 404    11927  12414  13233   -454  -1002   -274       C  
ATOM   2954  OG  SER A 404     -44.084 -10.017 -66.884  1.00 99.20           O  
ANISOU 2954  OG  SER A 404    11942  12437  13311   -473   -990   -243       O  
ATOM   2955  N   GLY A 405     -42.671 -10.779 -62.737  1.00 98.93           N  
ANISOU 2955  N   GLY A 405    11959  12428  13201   -417  -1042   -367       N  
ATOM   2956  CA  GLY A 405     -42.249 -11.628 -61.621  1.00100.77           C  
ANISOU 2956  CA  GLY A 405    12231  12672  13383   -397  -1064   -395       C  
ATOM   2957  C   GLY A 405     -42.897 -11.387 -60.267  1.00101.98           C  
ANISOU 2957  C   GLY A 405    12403  12827  13516   -394  -1063   -423       C  
ATOM   2958  O   GLY A 405     -42.860 -12.261 -59.397  1.00102.94           O  
ANISOU 2958  O   GLY A 405    12573  12958  13581   -387  -1078   -435       O  
ATOM   2959  N   GLN A 406     -43.494 -10.213 -60.081  1.00101.26           N  
ANISOU 2959  N   GLN A 406    12280  12727  13464   -399  -1050   -435       N  
ATOM   2960  CA  GLN A 406     -44.126  -9.880 -58.807  1.00102.40           C  
ANISOU 2960  CA  GLN A 406    12432  12884  13588   -391  -1049   -468       C  
ATOM   2961  C   GLN A 406     -45.457 -10.606 -58.635  1.00102.27           C  
ANISOU 2961  C   GLN A 406    12438  12901  13515   -410  -1026   -451       C  
ATOM   2962  O   GLN A 406     -45.871 -10.894 -57.510  1.00105.28           O  
ANISOU 2962  O   GLN A 406    12842  13309  13848   -414  -1025   -474       O  
ATOM   2963  CB  GLN A 406     -44.308  -8.362 -58.660  1.00105.03           C  
ANISOU 2963  CB  GLN A 406    12727  13199  13980   -379  -1052   -495       C  
ATOM   2964  CG  GLN A 406     -43.104  -7.515 -59.084  1.00108.00           C  
ANISOU 2964  CG  GLN A 406    13079  13540  14414   -380  -1073   -502       C  
ATOM   2965  CD  GLN A 406     -41.856  -7.702 -58.220  1.00108.53           C  
ANISOU 2965  CD  GLN A 406    13152  13610  14472   -368  -1097   -537       C  
ATOM   2966  OE1 GLN A 406     -41.369  -6.747 -57.607  1.00107.02           O  
ANISOU 2966  OE1 GLN A 406    12947  13402  14314   -360  -1117   -572       O  
ATOM   2967  NE2 GLN A 406     -41.321  -8.927 -58.184  1.00108.20           N  
ANISOU 2967  NE2 GLN A 406    13135  13589  14385   -362  -1102   -530       N  
ATOM   2968  N   PHE A 407     -46.109 -10.910 -59.755  1.00 99.75           N  
ANISOU 2968  N   PHE A 407    12113  12585  13199   -428  -1008   -411       N  
ATOM   2969  CA  PHE A 407     -47.393 -11.607 -59.760  1.00 98.03           C  
ANISOU 2969  CA  PHE A 407    11912  12407  12929   -457   -985   -392       C  
ATOM   2970  C   PHE A 407     -47.208 -13.119 -59.807  1.00 96.77           C  
ANISOU 2970  C   PHE A 407    11815  12248  12704   -481   -995   -361       C  
ATOM   2971  O   PHE A 407     -46.614 -13.641 -60.748  1.00 96.20           O  
ANISOU 2971  O   PHE A 407    11757  12152  12643   -476  -1006   -333       O  
ATOM   2972  CB  PHE A 407     -48.216 -11.173 -60.970  1.00 97.73           C  
ANISOU 2972  CB  PHE A 407    11837  12369  12925   -462   -966   -367       C  
ATOM   2973  CG  PHE A 407     -48.645  -9.736 -60.936  1.00 96.89           C  
ANISOU 2973  CG  PHE A 407    11683  12258  12871   -435   -965   -398       C  
ATOM   2974  CD1 PHE A 407     -47.828  -8.741 -61.457  1.00 96.94           C  
ANISOU 2974  CD1 PHE A 407    11672  12214  12945   -416   -983   -401       C  
ATOM   2975  CD2 PHE A 407     -49.883  -9.381 -60.405  1.00 96.44           C  
ANISOU 2975  CD2 PHE A 407    11601  12249  12791   -430   -951   -427       C  
ATOM   2976  CE1 PHE A 407     -48.229  -7.416 -61.436  1.00 97.87           C  
ANISOU 2976  CE1 PHE A 407    11762  12314  13107   -390   -995   -429       C  
ATOM   2977  CE2 PHE A 407     -50.292  -8.060 -60.380  1.00 96.23           C  
ANISOU 2977  CE2 PHE A 407    11537  12214  12809   -393   -961   -464       C  
ATOM   2978  CZ  PHE A 407     -49.464  -7.075 -60.897  1.00 98.44           C  
ANISOU 2978  CZ  PHE A 407    11815  12428  13158   -372   -987   -463       C  
ATOM   2979  N   ASP A 408     -47.732 -13.821 -58.808  1.00 96.97           N  
ANISOU 2979  N   ASP A 408    11882  12304  12657   -508   -994   -367       N  
ATOM   2980  CA  ASP A 408     -47.573 -15.277 -58.735  1.00 98.35           C  
ANISOU 2980  CA  ASP A 408    12138  12469  12761   -536  -1015   -338       C  
ATOM   2981  C   ASP A 408     -48.328 -16.033 -59.828  1.00 96.92           C  
ANISOU 2981  C   ASP A 408    11972  12292  12559   -571  -1003   -291       C  
ATOM   2982  O   ASP A 408     -47.905 -17.111 -60.248  1.00 96.34           O  
ANISOU 2982  O   ASP A 408    11961  12190  12451   -575  -1031   -263       O  
ATOM   2983  CB  ASP A 408     -47.961 -15.804 -57.353  1.00101.59           C  
ANISOU 2983  CB  ASP A 408    12599  12907  13090   -569  -1020   -353       C  
ATOM   2984  CG  ASP A 408     -46.836 -15.681 -56.346  1.00104.59           C  
ANISOU 2984  CG  ASP A 408    13005  13263  13469   -532  -1053   -389       C  
ATOM   2985  OD1 ASP A 408     -46.381 -14.544 -56.076  1.00106.62           O  
ANISOU 2985  OD1 ASP A 408    13204  13517  13787   -493  -1049   -427       O  
ATOM   2986  OD2 ASP A 408     -46.406 -16.728 -55.820  1.00105.93           O  
ANISOU 2986  OD2 ASP A 408    13260  13413  13575   -541  -1088   -382       O  
ATOM   2987  N   GLY A 409     -49.445 -15.468 -60.279  1.00 96.53           N  
ANISOU 2987  N   GLY A 409    11868  12280  12528   -589   -967   -286       N  
ATOM   2988  CA  GLY A 409     -50.183 -16.019 -61.413  1.00 94.71           C  
ANISOU 2988  CA  GLY A 409    11640  12056  12289   -618   -954   -244       C  
ATOM   2989  C   GLY A 409     -49.385 -15.917 -62.702  1.00 92.97           C  
ANISOU 2989  C   GLY A 409    11407  11790  12128   -581   -966   -223       C  
ATOM   2990  O   GLY A 409     -49.327 -16.864 -63.487  1.00 92.06           O  
ANISOU 2990  O   GLY A 409    11332  11656  11988   -593   -980   -187       O  
ATOM   2991  N   LEU A 410     -48.757 -14.765 -62.911  1.00 92.32           N  
ANISOU 2991  N   LEU A 410    11270  11689  12117   -540   -965   -245       N  
ATOM   2992  CA  LEU A 410     -47.940 -14.543 -64.098  1.00 92.52           C  
ANISOU 2992  CA  LEU A 410    11276  11681  12195   -513   -973   -227       C  
ATOM   2993  C   LEU A 410     -46.730 -15.484 -64.191  1.00 93.64           C  
ANISOU 2993  C   LEU A 410    11465  11800  12313   -494  -1007   -223       C  
ATOM   2994  O   LEU A 410     -46.291 -15.824 -65.293  1.00 95.23           O  
ANISOU 2994  O   LEU A 410    11664  11990  12528   -482  -1015   -201       O  
ATOM   2995  CB  LEU A 410     -47.496 -13.080 -64.192  1.00 91.99           C  
ANISOU 2995  CB  LEU A 410    11150  11599  12201   -487   -968   -252       C  
ATOM   2996  CG  LEU A 410     -48.493 -12.056 -64.741  1.00 91.14           C  
ANISOU 2996  CG  LEU A 410    10996  11497  12135   -487   -947   -250       C  
ATOM   2997  CD1 LEU A 410     -47.747 -10.807 -65.178  1.00 91.63           C  
ANISOU 2997  CD1 LEU A 410    11025  11524  12267   -467   -957   -259       C  
ATOM   2998  CD2 LEU A 410     -49.289 -12.616 -65.909  1.00 91.09           C  
ANISOU 2998  CD2 LEU A 410    10992  11500  12118   -505   -932   -209       C  
ATOM   2999  N   VAL A 411     -46.193 -15.897 -63.044  1.00 91.59           N  
ANISOU 2999  N   VAL A 411    11247  11538  12015   -486  -1032   -250       N  
ATOM   3000  CA  VAL A 411     -45.103 -16.867 -63.030  1.00 88.62           C  
ANISOU 3000  CA  VAL A 411    10923  11142  11605   -458  -1075   -255       C  
ATOM   3001  C   VAL A 411     -45.615 -18.164 -63.642  1.00 88.75           C  
ANISOU 3001  C   VAL A 411    11005  11149  11566   -478  -1091   -217       C  
ATOM   3002  O   VAL A 411     -45.052 -18.664 -64.619  1.00 88.45           O  
ANISOU 3002  O   VAL A 411    10974  11099  11532   -452  -1110   -205       O  
ATOM   3003  CB  VAL A 411     -44.556 -17.114 -61.611  1.00 87.49           C  
ANISOU 3003  CB  VAL A 411    10825  10994  11423   -445  -1104   -291       C  
ATOM   3004  CG1 VAL A 411     -43.422 -18.124 -61.644  1.00 87.04           C  
ANISOU 3004  CG1 VAL A 411    10825  10916  11329   -403  -1159   -305       C  
ATOM   3005  CG2 VAL A 411     -44.074 -15.811 -60.995  1.00 88.00           C  
ANISOU 3005  CG2 VAL A 411    10825  11066  11542   -426  -1091   -331       C  
ATOM   3006  N   GLU A 412     -46.708 -18.678 -63.086  1.00 89.11           N  
ANISOU 3006  N   GLU A 412    11095  11204  11556   -529  -1082   -199       N  
ATOM   3007  CA  GLU A 412     -47.303 -19.923 -63.560  1.00 89.67           C  
ANISOU 3007  CA  GLU A 412    11240  11263  11566   -563  -1100   -160       C  
ATOM   3008  C   GLU A 412     -47.797 -19.824 -65.000  1.00 88.79           C  
ANISOU 3008  C   GLU A 412    11087  11157  11492   -567  -1077   -128       C  
ATOM   3009  O   GLU A 412     -47.658 -20.789 -65.755  1.00 90.52           O  
ANISOU 3009  O   GLU A 412    11357  11353  11682   -561  -1106   -104       O  
ATOM   3010  CB  GLU A 412     -48.432 -20.377 -62.639  1.00 91.21           C  
ANISOU 3010  CB  GLU A 412    11483  11481  11691   -634  -1090   -147       C  
ATOM   3011  CG  GLU A 412     -49.026 -21.731 -62.997  1.00 91.46           C  
ANISOU 3011  CG  GLU A 412    11606  11495  11648   -684  -1116   -105       C  
ATOM   3012  CD  GLU A 412     -50.042 -22.204 -61.979  1.00 94.11           C  
ANISOU 3012  CD  GLU A 412    11994  11861  11902   -769  -1108    -93       C  
ATOM   3013  OE1 GLU A 412     -50.271 -21.485 -60.974  1.00 94.78           O  
ANISOU 3013  OE1 GLU A 412    12038  11985  11987   -782  -1080   -121       O  
ATOM   3014  OE2 GLU A 412     -50.604 -23.301 -62.185  1.00 93.52           O  
ANISOU 3014  OE2 GLU A 412    12001  11773  11758   -828  -1131    -55       O  
ATOM   3015  N   LEU A 413     -48.366 -18.675 -65.377  1.00 86.73           N  
ANISOU 3015  N   LEU A 413    10740  10922  11289   -572  -1031   -129       N  
ATOM   3016  CA  LEU A 413     -48.791 -18.455 -66.762  1.00 84.96           C  
ANISOU 3016  CA  LEU A 413    10475  10700  11104   -571  -1010   -101       C  
ATOM   3017  C   LEU A 413     -47.596 -18.658 -67.688  1.00 84.57           C  
ANISOU 3017  C   LEU A 413    10423  10627  11081   -523  -1035    -99       C  
ATOM   3018  O   LEU A 413     -47.693 -19.373 -68.690  1.00 83.30           O  
ANISOU 3018  O   LEU A 413    10286  10458  10906   -521  -1047    -71       O  
ATOM   3019  CB  LEU A 413     -49.401 -17.056 -66.964  1.00 84.23           C  
ANISOU 3019  CB  LEU A 413    10297  10630  11075   -570   -969   -112       C  
ATOM   3020  CG  LEU A 413     -49.947 -16.702 -68.368  1.00 84.23           C  
ANISOU 3020  CG  LEU A 413    10256  10631  11114   -569   -949    -83       C  
ATOM   3021  CD1 LEU A 413     -51.070 -15.672 -68.328  1.00 84.86           C  
ANISOU 3021  CD1 LEU A 413    10279  10739  11223   -579   -918    -95       C  
ATOM   3022  CD2 LEU A 413     -48.860 -16.256 -69.339  1.00 82.79           C  
ANISOU 3022  CD2 LEU A 413    10046  10424  10984   -532   -957    -78       C  
ATOM   3023  N   ALA A 414     -46.470 -18.041 -67.324  1.00 84.71           N  
ANISOU 3023  N   ALA A 414    10411  10642  11131   -485  -1045   -132       N  
ATOM   3024  CA  ALA A 414     -45.247 -18.088 -68.124  1.00 84.79           C  
ANISOU 3024  CA  ALA A 414    10400  10650  11163   -442  -1064   -142       C  
ATOM   3025  C   ALA A 414     -44.630 -19.480 -68.150  1.00 85.14           C  
ANISOU 3025  C   ALA A 414    10519  10682  11148   -411  -1116   -147       C  
ATOM   3026  O   ALA A 414     -44.037 -19.872 -69.156  1.00 85.40           O  
ANISOU 3026  O   ALA A 414    10544  10721  11181   -379  -1133   -144       O  
ATOM   3027  CB  ALA A 414     -44.240 -17.063 -67.628  1.00 84.31           C  
ANISOU 3027  CB  ALA A 414    10286  10599  11147   -420  -1061   -180       C  
ATOM   3028  N   THR A 415     -44.775 -20.218 -67.049  1.00 85.49           N  
ANISOU 3028  N   THR A 415    10639  10708  11134   -420  -1146   -156       N  
ATOM   3029  CA  THR A 415     -44.336 -21.613 -66.989  1.00 86.80           C  
ANISOU 3029  CA  THR A 415    10900  10847  11231   -392  -1209   -160       C  
ATOM   3030  C   THR A 415     -45.150 -22.497 -67.940  1.00 87.10           C  
ANISOU 3030  C   THR A 415    10986  10869  11238   -416  -1217   -116       C  
ATOM   3031  O   THR A 415     -44.582 -23.315 -68.662  1.00 88.84           O  
ANISOU 3031  O   THR A 415    11244  11077  11434   -372  -1261   -119       O  
ATOM   3032  CB  THR A 415     -44.386 -22.179 -65.557  1.00 86.94           C  
ANISOU 3032  CB  THR A 415    11003  10841  11187   -406  -1244   -175       C  
ATOM   3033  OG1 THR A 415     -43.566 -21.376 -64.703  1.00 86.98           O  
ANISOU 3033  OG1 THR A 415    10964  10861  11222   -377  -1240   -219       O  
ATOM   3034  CG2 THR A 415     -43.879 -23.621 -65.517  1.00 86.86           C  
ANISOU 3034  CG2 THR A 415    11108  10790  11102   -371  -1323   -180       C  
ATOM   3035  N   ILE A 416     -46.468 -22.328 -67.953  1.00 86.58           N  
ANISOU 3035  N   ILE A 416    10915  10809  11169   -483  -1178    -80       N  
ATOM   3036  CA  ILE A 416     -47.299 -23.077 -68.893  1.00 87.60           C  
ANISOU 3036  CA  ILE A 416    11081  10929  11274   -512  -1181    -39       C  
ATOM   3037  C   ILE A 416     -46.905 -22.769 -70.345  1.00 89.18           C  
ANISOU 3037  C   ILE A 416    11218  11140  11523   -471  -1169    -32       C  
ATOM   3038  O   ILE A 416     -46.747 -23.688 -71.148  1.00 91.91           O  
ANISOU 3038  O   ILE A 416    11611  11469  11840   -448  -1206    -19       O  
ATOM   3039  CB  ILE A 416     -48.811 -22.861 -68.659  1.00 86.03           C  
ANISOU 3039  CB  ILE A 416    10871  10751  11063   -592  -1137     -9       C  
ATOM   3040  CG1 ILE A 416     -49.218 -23.408 -67.289  1.00 85.10           C  
ANISOU 3040  CG1 ILE A 416    10830  10628  10875   -645  -1155    -11       C  
ATOM   3041  CG2 ILE A 416     -49.628 -23.543 -69.751  1.00 85.17           C  
ANISOU 3041  CG2 ILE A 416    10787  10637  10936   -622  -1139     31       C  
ATOM   3042  CD1 ILE A 416     -50.584 -22.950 -66.831  1.00 84.62           C  
ANISOU 3042  CD1 ILE A 416    10731  10615  10804   -721  -1103      0       C  
ATOM   3043  N   CYS A 417     -46.716 -21.489 -70.665  1.00 89.34           N  
ANISOU 3043  N   CYS A 417    11139  11190  11616   -462  -1122    -41       N  
ATOM   3044  CA  CYS A 417     -46.376 -21.071 -72.029  1.00 89.09           C  
ANISOU 3044  CA  CYS A 417    11046  11174  11629   -435  -1105    -31       C  
ATOM   3045  C   CYS A 417     -45.004 -21.553 -72.458  1.00 89.27           C  
ANISOU 3045  C   CYS A 417    11072  11205  11639   -371  -1146    -60       C  
ATOM   3046  O   CYS A 417     -44.754 -21.738 -73.642  1.00 90.41           O  
ANISOU 3046  O   CYS A 417    11195  11364  11790   -348  -1148    -50       O  
ATOM   3047  CB  CYS A 417     -46.451 -19.553 -72.175  1.00 89.98           C  
ANISOU 3047  CB  CYS A 417    11066  11307  11813   -448  -1054    -34       C  
ATOM   3048  SG  CYS A 417     -48.130 -18.895 -72.163  1.00 92.23           S  
ANISOU 3048  SG  CYS A 417    11327  11596  12119   -504  -1008     -6       S  
ATOM   3049  N   ALA A 418     -44.111 -21.749 -71.501  1.00 90.82           N  
ANISOU 3049  N   ALA A 418    11293  11400  11814   -339  -1180   -101       N  
ATOM   3050  CA  ALA A 418     -42.784 -22.242 -71.831  1.00 94.70           C  
ANISOU 3050  CA  ALA A 418    11782  11911  12286   -269  -1225   -141       C  
ATOM   3051  C   ALA A 418     -42.803 -23.732 -72.137  1.00 96.14           C  
ANISOU 3051  C   ALA A 418    12064  12065  12400   -233  -1290   -139       C  
ATOM   3052  O   ALA A 418     -42.162 -24.166 -73.087  1.00 99.30           O  
ANISOU 3052  O   ALA A 418    12451  12488  12789   -180  -1315   -155       O  
ATOM   3053  CB  ALA A 418     -41.791 -21.934 -70.723  1.00 96.35           C  
ANISOU 3053  CB  ALA A 418    11980  12132  12494   -239  -1244   -192       C  
ATOM   3054  N   LEU A 419     -43.548 -24.505 -71.347  1.00 95.96           N  
ANISOU 3054  N   LEU A 419    12141  11992  12327   -266  -1319   -120       N  
ATOM   3055  CA  LEU A 419     -43.518 -25.966 -71.452  1.00 97.48           C  
ANISOU 3055  CA  LEU A 419    12452  12141  12445   -236  -1396   -120       C  
ATOM   3056  C   LEU A 419     -44.459 -26.523 -72.521  1.00 97.99           C  
ANISOU 3056  C   LEU A 419    12545  12187  12496   -266  -1393    -72       C  
ATOM   3057  O   LEU A 419     -44.066 -27.388 -73.303  1.00 99.28           O  
ANISOU 3057  O   LEU A 419    12753  12340  12627   -212  -1446    -82       O  
ATOM   3058  CB  LEU A 419     -43.744 -26.622 -70.083  1.00 99.43           C  
ANISOU 3058  CB  LEU A 419    12810  12337  12629   -261  -1441   -123       C  
ATOM   3059  CG  LEU A 419     -42.630 -26.337 -69.054  1.00104.47           C  
ANISOU 3059  CG  LEU A 419    13440  12987  13267   -210  -1467   -179       C  
ATOM   3060  CD1 LEU A 419     -43.040 -26.694 -67.631  1.00105.17           C  
ANISOU 3060  CD1 LEU A 419    13623  13033  13303   -255  -1491   -173       C  
ATOM   3061  CD2 LEU A 419     -41.312 -27.021 -69.412  1.00106.51           C  
ANISOU 3061  CD2 LEU A 419    13719  13251  13495   -103  -1542   -236       C  
ATOM   3062  N   CYS A 420     -45.687 -26.015 -72.560  1.00 99.09           N  
ANISOU 3062  N   CYS A 420    12659  12330  12661   -347  -1334    -27       N  
ATOM   3063  CA  CYS A 420     -46.644 -26.335 -73.624  1.00100.38           C  
ANISOU 3063  CA  CYS A 420    12828  12487  12823   -381  -1319     16       C  
ATOM   3064  C   CYS A 420     -46.231 -25.778 -74.981  1.00102.38           C  
ANISOU 3064  C   CYS A 420    12990  12780  13130   -339  -1289     15       C  
ATOM   3065  O   CYS A 420     -47.051 -25.187 -75.698  1.00103.46           O  
ANISOU 3065  O   CYS A 420    13070  12934  13306   -378  -1237     48       O  
ATOM   3066  CB  CYS A 420     -48.005 -25.761 -73.276  1.00 99.68           C  
ANISOU 3066  CB  CYS A 420    12712  12408  12751   -471  -1259     53       C  
ATOM   3067  SG  CYS A 420     -49.180 -27.010 -72.786  1.00104.48           S  
ANISOU 3067  SG  CYS A 420    13448  12976  13274   -554  -1296     92       S  
ATOM   3068  N   ASN A 421     -44.968 -25.976 -75.340  1.00101.50           N  
ANISOU 3068  N   ASN A 421    12863  12689  13014   -259  -1325    -26       N  
ATOM   3069  CA  ASN A 421     -44.400 -25.304 -76.491  1.00101.60           C  
ANISOU 3069  CA  ASN A 421    12776  12755  13073   -226  -1292    -34       C  
ATOM   3070  C   ASN A 421     -43.418 -26.206 -77.230  1.00104.56           C  
ANISOU 3070  C   ASN A 421    13174  13148  13407   -140  -1353    -71       C  
ATOM   3071  O   ASN A 421     -42.479 -26.737 -76.629  1.00108.01           O  
ANISOU 3071  O   ASN A 421    13648  13585  13806    -79  -1411   -121       O  
ATOM   3072  CB  ASN A 421     -43.722 -24.010 -76.030  1.00 98.69           C  
ANISOU 3072  CB  ASN A 421    12310  12428  12758   -231  -1245    -59       C  
ATOM   3073  CG  ASN A 421     -43.651 -22.965 -77.119  1.00 97.26           C  
ANISOU 3073  CG  ASN A 421    12027  12292  12633   -245  -1188    -42       C  
ATOM   3074  OD1 ASN A 421     -42.810 -23.033 -78.012  1.00 98.17           O  
ANISOU 3074  OD1 ASN A 421    12100  12454  12746   -202  -1196    -62       O  
ATOM   3075  ND2 ASN A 421     -44.525 -21.977 -77.040  1.00 96.83           N  
ANISOU 3075  ND2 ASN A 421    11936  12228  12627   -306  -1133     -9       N  
ATOM   3076  N   ASP A 422     -43.648 -26.387 -78.529  1.00103.90           N  
ANISOU 3076  N   ASP A 422    13068  13080  13326   -129  -1346    -51       N  
ATOM   3077  CA  ASP A 422     -42.756 -27.184 -79.361  1.00106.03           C  
ANISOU 3077  CA  ASP A 422    13347  13380  13557    -41  -1401    -90       C  
ATOM   3078  C   ASP A 422     -41.844 -26.305 -80.207  1.00106.38           C  
ANISOU 3078  C   ASP A 422    13265  13515  13638    -15  -1357   -115       C  
ATOM   3079  O   ASP A 422     -41.127 -26.807 -81.072  1.00109.72           O  
ANISOU 3079  O   ASP A 422    13671  13986  14031     52  -1390   -149       O  
ATOM   3080  CB  ASP A 422     -43.554 -28.129 -80.259  1.00110.61           C  
ANISOU 3080  CB  ASP A 422    13998  13921  14105    -40  -1433    -56       C  
ATOM   3081  CG  ASP A 422     -44.360 -29.153 -79.473  1.00116.09           C  
ANISOU 3081  CG  ASP A 422    14831  14529  14748    -72  -1489    -33       C  
ATOM   3082  OD1 ASP A 422     -43.807 -29.785 -78.543  1.00118.23           O  
ANISOU 3082  OD1 ASP A 422    15180  14769  14973    -35  -1553    -69       O  
ATOM   3083  OD2 ASP A 422     -45.553 -29.335 -79.800  1.00119.24           O  
ANISOU 3083  OD2 ASP A 422    15263  14892  15147   -137  -1471     19       O  
ATOM   3084  N   SER A 423     -41.866 -24.998 -79.946  1.00105.55           N  
ANISOU 3084  N   SER A 423    13077  13436  13592    -73  -1287   -100       N  
ATOM   3085  CA  SER A 423     -41.092 -24.025 -80.718  1.00105.41           C  
ANISOU 3085  CA  SER A 423    12944  13500  13608    -75  -1240   -112       C  
ATOM   3086  C   SER A 423     -39.901 -23.504 -79.952  1.00104.76           C  
ANISOU 3086  C   SER A 423    12805  13469  13530    -55  -1241   -167       C  
ATOM   3087  O   SER A 423     -39.674 -23.873 -78.801  1.00107.32           O  
ANISOU 3087  O   SER A 423    13179  13762  13835    -33  -1279   -197       O  
ATOM   3088  CB  SER A 423     -41.958 -22.824 -81.088  1.00106.90           C  
ANISOU 3088  CB  SER A 423    13082  13675  13858   -159  -1166    -54       C  
ATOM   3089  OG  SER A 423     -43.168 -23.241 -81.685  1.00115.60           O  
ANISOU 3089  OG  SER A 423    14233  14729  14958   -182  -1162     -4       O  
ATOM   3090  N   SER A 424     -39.148 -22.637 -80.616  1.00103.43           N  
ANISOU 3090  N   SER A 424    12533  13381  13384    -70  -1201   -179       N  
ATOM   3091  CA  SER A 424     -38.130 -21.817 -79.984  1.00101.79           C  
ANISOU 3091  CA  SER A 424    12253  13228  13192    -80  -1184   -221       C  
ATOM   3092  C   SER A 424     -37.968 -20.554 -80.817  1.00104.40           C  
ANISOU 3092  C   SER A 424    12490  13611  13564   -150  -1118   -191       C  
ATOM   3093  O   SER A 424     -38.663 -20.366 -81.818  1.00109.10           O  
ANISOU 3093  O   SER A 424    13084  14195  14174   -183  -1089   -141       O  
ATOM   3094  CB  SER A 424     -36.807 -22.561 -79.922  1.00 99.67           C  
ANISOU 3094  CB  SER A 424    11962  13038  12869      8  -1239   -303       C  
ATOM   3095  OG  SER A 424     -36.227 -22.623 -81.206  1.00 99.26           O  
ANISOU 3095  OG  SER A 424    11840  13080  12794     30  -1230   -319       O  
ATOM   3096  N   LEU A 425     -37.058 -19.685 -80.398  1.00104.82           N  
ANISOU 3096  N   LEU A 425    12472  13719  13634   -178  -1098   -222       N  
ATOM   3097  CA  LEU A 425     -36.673 -18.538 -81.202  1.00104.53           C  
ANISOU 3097  CA  LEU A 425    12350  13743  13622   -249  -1045   -201       C  
ATOM   3098  C   LEU A 425     -35.296 -18.804 -81.782  1.00107.88           C  
ANISOU 3098  C   LEU A 425    12691  14300  13997   -213  -1057   -263       C  
ATOM   3099  O   LEU A 425     -34.613 -19.737 -81.363  1.00111.15           O  
ANISOU 3099  O   LEU A 425    13112  14753  14367   -127  -1108   -330       O  
ATOM   3100  CB  LEU A 425     -36.679 -17.261 -80.361  1.00101.73           C  
ANISOU 3100  CB  LEU A 425    11976  13356  13319   -322  -1014   -186       C  
ATOM   3101  CG  LEU A 425     -38.037 -16.573 -80.223  1.00 99.18           C  
ANISOU 3101  CG  LEU A 425    11704  12929  13048   -378   -987   -119       C  
ATOM   3102  CD1 LEU A 425     -38.048 -15.582 -79.069  1.00 97.19           C  
ANISOU 3102  CD1 LEU A 425    11453  12635  12839   -420   -977   -123       C  
ATOM   3103  CD2 LEU A 425     -38.387 -15.883 -81.529  1.00 99.26           C  
ANISOU 3103  CD2 LEU A 425    11688  12949  13075   -436   -949    -66       C  
ATOM   3104  N   ASP A 426     -34.897 -18.000 -82.758  1.00110.18           N  
ANISOU 3104  N   ASP A 426    12907  14665  14291   -277  -1013   -245       N  
ATOM   3105  CA  ASP A 426     -33.586 -18.133 -83.368  1.00112.28           C  
ANISOU 3105  CA  ASP A 426    13075  15079  14504   -258  -1015   -305       C  
ATOM   3106  C   ASP A 426     -33.128 -16.788 -83.907  1.00113.51           C  
ANISOU 3106  C   ASP A 426    13152  15297  14676   -374   -958   -277       C  
ATOM   3107  O   ASP A 426     -33.758 -16.226 -84.803  1.00114.67           O  
ANISOU 3107  O   ASP A 426    13310  15417  14842   -440   -922   -210       O  
ATOM   3108  CB  ASP A 426     -33.631 -19.176 -84.486  1.00115.33           C  
ANISOU 3108  CB  ASP A 426    13464  15514  14839   -188  -1036   -318       C  
ATOM   3109  CG  ASP A 426     -32.442 -19.089 -85.417  1.00121.88           C  
ANISOU 3109  CG  ASP A 426    14180  16512  15614   -190  -1021   -367       C  
ATOM   3110  OD1 ASP A 426     -31.297 -19.250 -84.940  1.00128.08           O  
ANISOU 3110  OD1 ASP A 426    14900  17399  16365   -151  -1044   -449       O  
ATOM   3111  OD2 ASP A 426     -32.655 -18.861 -86.630  1.00123.77           O  
ANISOU 3111  OD2 ASP A 426    14394  16790  15843   -232   -988   -327       O  
ATOM   3112  N   PHE A 427     -32.039 -16.263 -83.358  1.00114.31           N  
ANISOU 3112  N   PHE A 427    13182  15481  14768   -403   -954   -327       N  
ATOM   3113  CA  PHE A 427     -31.487 -15.027 -83.885  1.00116.44           C  
ANISOU 3113  CA  PHE A 427    13379  15821  15042   -524   -905   -303       C  
ATOM   3114  C   PHE A 427     -30.668 -15.288 -85.149  1.00120.91           C  
ANISOU 3114  C   PHE A 427    13853  16546  15540   -530   -889   -332       C  
ATOM   3115  O   PHE A 427     -29.561 -15.840 -85.092  1.00122.82           O  
ANISOU 3115  O   PHE A 427    14015  16924  15727   -474   -909   -418       O  
ATOM   3116  CB  PHE A 427     -30.661 -14.275 -82.837  1.00115.85           C  
ANISOU 3116  CB  PHE A 427    13260  15775  14982   -570   -905   -342       C  
ATOM   3117  CG  PHE A 427     -30.145 -12.951 -83.324  1.00116.31           C  
ANISOU 3117  CG  PHE A 427    13258  15891  15043   -711   -860   -310       C  
ATOM   3118  CD1 PHE A 427     -30.991 -11.851 -83.415  1.00114.77           C  
ANISOU 3118  CD1 PHE A 427    13125  15580  14902   -808   -836   -225       C  
ATOM   3119  CD2 PHE A 427     -28.819 -12.810 -83.723  1.00117.30           C  
ANISOU 3119  CD2 PHE A 427    13266  16190  15109   -749   -846   -367       C  
ATOM   3120  CE1 PHE A 427     -30.522 -10.634 -83.880  1.00115.23           C  
ANISOU 3120  CE1 PHE A 427    13145  15679  14956   -945   -804   -192       C  
ATOM   3121  CE2 PHE A 427     -28.344 -11.594 -84.189  1.00116.67           C  
ANISOU 3121  CE2 PHE A 427    13139  16166  15025   -896   -807   -333       C  
ATOM   3122  CZ  PHE A 427     -29.197 -10.504 -84.265  1.00116.85           C  
ANISOU 3122  CZ  PHE A 427    13239  16055  15102   -996   -788   -242       C  
ATOM   3123  N   ASN A 428     -31.237 -14.903 -86.289  1.00123.32           N  
ANISOU 3123  N   ASN A 428    14170  16837  15847   -593   -855   -263       N  
ATOM   3124  CA  ASN A 428     -30.525 -14.917 -87.562  1.00127.00           C  
ANISOU 3124  CA  ASN A 428    14549  17455  16249   -627   -828   -277       C  
ATOM   3125  C   ASN A 428     -29.507 -13.784 -87.567  1.00129.05           C  
ANISOU 3125  C   ASN A 428    14720  17820  16490   -753   -792   -285       C  
ATOM   3126  O   ASN A 428     -29.861 -12.612 -87.421  1.00131.43           O  
ANISOU 3126  O   ASN A 428    15058  18042  16836   -868   -767   -219       O  
ATOM   3127  CB  ASN A 428     -31.501 -14.766 -88.733  1.00127.13           C  
ANISOU 3127  CB  ASN A 428    14616  17412  16275   -664   -804   -194       C  
ATOM   3128  CG  ASN A 428     -30.842 -14.989 -90.083  1.00128.04           C  
ANISOU 3128  CG  ASN A 428    14648  17686  16315   -681   -781   -211       C  
ATOM   3129  OD1 ASN A 428     -29.754 -14.480 -90.357  1.00130.18           O  
ANISOU 3129  OD1 ASN A 428    14819  18103  16538   -754   -755   -244       O  
ATOM   3130  ND2 ASN A 428     -31.509 -15.747 -90.941  1.00129.53           N  
ANISOU 3130  ND2 ASN A 428    14873  17851  16488   -617   -790   -190       N  
ATOM   3131  N   GLU A 429     -28.242 -14.140 -87.737  1.00129.46           N  
ANISOU 3131  N   GLU A 429    14658  18055  16474   -732   -794   -371       N  
ATOM   3132  CA  GLU A 429     -27.169 -13.172 -87.588  1.00131.28           C  
ANISOU 3132  CA  GLU A 429    14795  18403  16680   -850   -765   -394       C  
ATOM   3133  C   GLU A 429     -26.984 -12.308 -88.830  1.00131.53           C  
ANISOU 3133  C   GLU A 429    14785  18514  16675   -997   -712   -335       C  
ATOM   3134  O   GLU A 429     -26.794 -11.097 -88.717  1.00134.31           O  
ANISOU 3134  O   GLU A 429    15137  18852  17043  -1142   -685   -289       O  
ATOM   3135  CB  GLU A 429     -25.867 -13.870 -87.193  1.00133.85           C  
ANISOU 3135  CB  GLU A 429    15007  18905  16943   -769   -790   -518       C  
ATOM   3136  CG  GLU A 429     -26.039 -14.844 -86.035  1.00133.85           C  
ANISOU 3136  CG  GLU A 429    15062  18825  16969   -615   -852   -577       C  
ATOM   3137  CD  GLU A 429     -24.820 -14.926 -85.140  1.00135.19           C  
ANISOU 3137  CD  GLU A 429    15142  19114  17109   -582   -876   -681       C  
ATOM   3138  OE1 GLU A 429     -24.256 -13.865 -84.794  1.00135.30           O  
ANISOU 3138  OE1 GLU A 429    15105  19171  17133   -703   -846   -675       O  
ATOM   3139  OE2 GLU A 429     -24.435 -16.054 -84.771  1.00137.31           O  
ANISOU 3139  OE2 GLU A 429    15398  19428  17342   -432   -931   -771       O  
ATOM   3140  N   THR A 430     -27.059 -12.927 -90.006  1.00131.48           N  
ANISOU 3140  N   THR A 430    14752  18586  16616   -961   -702   -335       N  
ATOM   3141  CA  THR A 430     -26.819 -12.225 -91.270  1.00133.06           C  
ANISOU 3141  CA  THR A 430    14907  18882  16766  -1096   -652   -286       C  
ATOM   3142  C   THR A 430     -27.999 -11.357 -91.708  1.00132.54           C  
ANISOU 3142  C   THR A 430    14961  18642  16756  -1190   -635   -162       C  
ATOM   3143  O   THR A 430     -27.801 -10.291 -92.291  1.00134.41           O  
ANISOU 3143  O   THR A 430    15191  18905  16973  -1346   -600   -104       O  
ATOM   3144  CB  THR A 430     -26.446 -13.193 -92.407  1.00134.71           C  
ANISOU 3144  CB  THR A 430    15040  19250  16893  -1022   -648   -335       C  
ATOM   3145  OG1 THR A 430     -27.445 -14.213 -92.512  1.00134.61           O  
ANISOU 3145  OG1 THR A 430    15115  19117  16911   -880   -684   -324       O  
ATOM   3146  CG2 THR A 430     -25.079 -13.834 -92.148  1.00136.17           C  
ANISOU 3146  CG2 THR A 430    15084  19649  17003   -953   -662   -466       C  
ATOM   3147  N   LYS A 431     -29.218 -11.822 -91.437  1.00132.06           N  
ANISOU 3147  N   LYS A 431    15009  18406  16759  -1095   -662   -124       N  
ATOM   3148  CA  LYS A 431     -30.429 -11.042 -91.709  1.00128.69           C  
ANISOU 3148  CA  LYS A 431    14700  17805  16392  -1161   -655    -19       C  
ATOM   3149  C   LYS A 431     -30.619  -9.966 -90.647  1.00125.59           C  
ANISOU 3149  C   LYS A 431    14363  17291  16064  -1236   -663     12       C  
ATOM   3150  O   LYS A 431     -31.140  -8.890 -90.936  1.00126.36           O  
ANISOU 3150  O   LYS A 431    14528  17293  16188  -1344   -654     91       O  
ATOM   3151  CB  LYS A 431     -31.668 -11.942 -91.778  1.00129.89           C  
ANISOU 3151  CB  LYS A 431    14938  17828  16584  -1035   -682      2       C  
ATOM   3152  CG  LYS A 431     -31.707 -12.855 -92.994  1.00135.15           C  
ANISOU 3152  CG  LYS A 431    15574  18582  17193   -974   -677     -8       C  
ATOM   3153  CD  LYS A 431     -33.006 -13.641 -93.068  1.00136.31           C  
ANISOU 3153  CD  LYS A 431    15818  18590  17383   -868   -704     21       C  
ATOM   3154  CE  LYS A 431     -32.913 -14.771 -94.083  1.00136.58           C  
ANISOU 3154  CE  LYS A 431    15817  18718  17357   -779   -712    -10       C  
ATOM   3155  NZ  LYS A 431     -34.140 -15.617 -94.080  1.00135.30           N  
ANISOU 3155  NZ  LYS A 431    15750  18424  17234   -678   -745     12       N  
ATOM   3156  N   GLY A 432     -30.196 -10.273 -89.422  1.00122.47           N  
ANISOU 3156  N   GLY A 432    13944  16898  15689  -1173   -687    -52       N  
ATOM   3157  CA  GLY A 432     -30.203  -9.313 -88.320  1.00119.65           C  
ANISOU 3157  CA  GLY A 432    13625  16448  15386  -1236   -697    -39       C  
ATOM   3158  C   GLY A 432     -31.401  -9.374 -87.387  1.00116.50           C  
ANISOU 3158  C   GLY A 432    13334  15859  15068  -1161   -727    -13       C  
ATOM   3159  O   GLY A 432     -31.433  -8.677 -86.373  1.00118.56           O  
ANISOU 3159  O   GLY A 432    13627  16043  15375  -1193   -741    -11       O  
ATOM   3160  N   VAL A 433     -32.380 -10.211 -87.713  1.00112.70           N  
ANISOU 3160  N   VAL A 433    12908  15310  14603  -1064   -738      4       N  
ATOM   3161  CA  VAL A 433     -33.631 -10.244 -86.959  1.00109.23           C  
ANISOU 3161  CA  VAL A 433    12569  14700  14232  -1006   -762     35       C  
ATOM   3162  C   VAL A 433     -33.912 -11.607 -86.312  1.00106.03           C  
ANISOU 3162  C   VAL A 433    12176  14282  13829   -864   -791    -16       C  
ATOM   3163  O   VAL A 433     -33.466 -12.642 -86.809  1.00104.23           O  
ANISOU 3163  O   VAL A 433    11902  14148  13549   -794   -797    -59       O  
ATOM   3164  CB  VAL A 433     -34.818  -9.767 -87.837  1.00110.24           C  
ANISOU 3164  CB  VAL A 433    12776  14723  14385  -1042   -754    119       C  
ATOM   3165  CG1 VAL A 433     -35.160 -10.792 -88.919  1.00109.18           C  
ANISOU 3165  CG1 VAL A 433    12634  14633  14214   -977   -748    124       C  
ATOM   3166  CG2 VAL A 433     -36.033  -9.408 -86.979  1.00109.98           C  
ANISOU 3166  CG2 VAL A 433    12836  14526  14424  -1012   -776    148       C  
ATOM   3167  N   TYR A 434     -34.638 -11.584 -85.192  1.00103.34           N  
ANISOU 3167  N   TYR A 434    11901  13823  13541   -824   -813    -14       N  
ATOM   3168  CA  TYR A 434     -35.083 -12.795 -84.498  1.00 99.67           C  
ANISOU 3168  CA  TYR A 434    11472  13320  13078   -705   -844    -50       C  
ATOM   3169  C   TYR A 434     -36.097 -13.550 -85.336  1.00 98.29           C  
ANISOU 3169  C   TYR A 434    11346  13100  12897   -656   -847    -13       C  
ATOM   3170  O   TYR A 434     -36.986 -12.944 -85.925  1.00100.02           O  
ANISOU 3170  O   TYR A 434    11608  13249  13145   -703   -830     50       O  
ATOM   3171  CB  TYR A 434     -35.728 -12.436 -83.166  1.00 96.86           C  
ANISOU 3171  CB  TYR A 434    11176  12848  12776   -695   -860    -46       C  
ATOM   3172  CG  TYR A 434     -34.761 -12.085 -82.070  1.00 95.14           C  
ANISOU 3172  CG  TYR A 434    10918  12667  12561   -707   -870   -100       C  
ATOM   3173  CD1 TYR A 434     -34.264 -13.064 -81.221  1.00 94.55           C  
ANISOU 3173  CD1 TYR A 434    10833  12626  12462   -618   -902   -167       C  
ATOM   3174  CD2 TYR A 434     -34.358 -10.771 -81.870  1.00 96.12           C  
ANISOU 3174  CD2 TYR A 434    11023  12787  12709   -806   -855    -84       C  
ATOM   3175  CE1 TYR A 434     -33.385 -12.744 -80.207  1.00 95.72           C  
ANISOU 3175  CE1 TYR A 434    10945  12810  12613   -625   -914   -219       C  
ATOM   3176  CE2 TYR A 434     -33.480 -10.437 -80.858  1.00 96.64           C  
ANISOU 3176  CE2 TYR A 434    11052  12887  12777   -819   -866   -134       C  
ATOM   3177  CZ  TYR A 434     -32.997 -11.429 -80.034  1.00 97.00           C  
ANISOU 3177  CZ  TYR A 434    11081  12973  12802   -726   -893   -203       C  
ATOM   3178  OH  TYR A 434     -32.124 -11.103 -79.031  1.00100.70           O  
ANISOU 3178  OH  TYR A 434    11511  13476  13272   -734   -907   -255       O  
ATOM   3179  N   GLU A 435     -35.976 -14.872 -85.371  1.00 97.32           N  
ANISOU 3179  N   GLU A 435    11224  13015  12738   -558   -874    -56       N  
ATOM   3180  CA  GLU A 435     -36.798 -15.680 -86.262  1.00 98.08           C  
ANISOU 3180  CA  GLU A 435    11361  13083  12819   -511   -881    -27       C  
ATOM   3181  C   GLU A 435     -37.475 -16.861 -85.588  1.00 99.02           C  
ANISOU 3181  C   GLU A 435    11550  13133  12937   -418   -922    -45       C  
ATOM   3182  O   GLU A 435     -36.921 -17.481 -84.674  1.00 98.81           O  
ANISOU 3182  O   GLU A 435    11526  13124  12893   -360   -956   -102       O  
ATOM   3183  CB  GLU A 435     -35.975 -16.173 -87.446  1.00100.28           C  
ANISOU 3183  CB  GLU A 435    11572  13491  13036   -493   -876    -53       C  
ATOM   3184  CG  GLU A 435     -35.846 -15.169 -88.580  1.00103.14           C  
ANISOU 3184  CG  GLU A 435    11896  13898  13393   -594   -832     -3       C  
ATOM   3185  CD  GLU A 435     -35.068 -15.726 -89.758  1.00105.79           C  
ANISOU 3185  CD  GLU A 435    12161  14374  13659   -573   -825    -33       C  
ATOM   3186  OE1 GLU A 435     -34.142 -16.541 -89.536  1.00106.57           O  
ANISOU 3186  OE1 GLU A 435    12206  14573  13709   -500   -850   -112       O  
ATOM   3187  OE2 GLU A 435     -35.383 -15.352 -90.908  1.00107.42           O  
ANISOU 3187  OE2 GLU A 435    12367  14593  13855   -626   -798     17       O  
ATOM   3188  N   LYS A 436     -38.678 -17.162 -86.077  1.00100.52           N  
ANISOU 3188  N   LYS A 436    11802  13247  13143   -410   -922      4       N  
ATOM   3189  CA  LYS A 436     -39.504 -18.269 -85.594  1.00100.06           C  
ANISOU 3189  CA  LYS A 436    11820  13118  13079   -343   -959      1       C  
ATOM   3190  C   LYS A 436     -38.870 -19.622 -85.892  1.00 99.12           C  
ANISOU 3190  C   LYS A 436    11702  13060  12899   -252  -1004    -52       C  
ATOM   3191  O   LYS A 436     -38.237 -19.801 -86.933  1.00100.97           O  
ANISOU 3191  O   LYS A 436    11884  13383  13096   -237   -999    -67       O  
ATOM   3192  CB  LYS A 436     -40.907 -18.166 -86.210  1.00100.24           C  
ANISOU 3192  CB  LYS A 436    11894  13061  13129   -367   -944     66       C  
ATOM   3193  CG  LYS A 436     -41.605 -19.487 -86.516  1.00101.58           C  
ANISOU 3193  CG  LYS A 436    12126  13200  13270   -304   -979     68       C  
ATOM   3194  CD  LYS A 436     -43.110 -19.311 -86.700  1.00102.40           C  
ANISOU 3194  CD  LYS A 436    12282  13217  13408   -335   -966    126       C  
ATOM   3195  CE  LYS A 436     -43.493 -18.682 -88.035  1.00101.50           C  
ANISOU 3195  CE  LYS A 436    12144  13113  13306   -372   -934    173       C  
ATOM   3196  NZ  LYS A 436     -43.422 -19.676 -89.143  1.00102.36           N  
ANISOU 3196  NZ  LYS A 436    12258  13261  13371   -324   -953    170       N  
ATOM   3197  N   VAL A 437     -39.027 -20.567 -84.971  1.00 97.35           N  
ANISOU 3197  N   VAL A 437    11540  12788  12657   -191  -1052    -82       N  
ATOM   3198  CA  VAL A 437     -38.593 -21.931 -85.235  1.00 98.68           C  
ANISOU 3198  CA  VAL A 437    11737  12991  12766    -96  -1110   -130       C  
ATOM   3199  C   VAL A 437     -39.786 -22.875 -85.368  1.00100.44           C  
ANISOU 3199  C   VAL A 437    12059  13121  12980    -71  -1142    -95       C  
ATOM   3200  O   VAL A 437     -39.980 -23.467 -86.435  1.00105.76           O  
ANISOU 3200  O   VAL A 437    12742  13813  13627    -40  -1155    -86       O  
ATOM   3201  CB  VAL A 437     -37.536 -22.426 -84.227  1.00 98.20           C  
ANISOU 3201  CB  VAL A 437    11672  12967  12672    -31  -1158   -208       C  
ATOM   3202  CG1 VAL A 437     -37.316 -23.928 -84.351  1.00 98.85           C  
ANISOU 3202  CG1 VAL A 437    11815  13050  12690     76  -1236   -256       C  
ATOM   3203  CG2 VAL A 437     -36.229 -21.694 -84.462  1.00 98.01           C  
ANISOU 3203  CG2 VAL A 437    11532  13068  12638    -46  -1131   -253       C  
ATOM   3204  N   GLY A 438     -40.597 -23.005 -84.322  1.00 96.99           N  
ANISOU 3204  N   GLY A 438    11696  12593  12564    -92  -1153    -74       N  
ATOM   3205  CA  GLY A 438     -41.758 -23.895 -84.398  1.00 98.83           C  
ANISOU 3205  CA  GLY A 438    12022  12743  12782    -85  -1182    -39       C  
ATOM   3206  C   GLY A 438     -42.926 -23.336 -85.200  1.00 98.19           C  
ANISOU 3206  C   GLY A 438    11936  12630  12740   -147  -1134     28       C  
ATOM   3207  O   GLY A 438     -42.758 -22.873 -86.332  1.00 96.45           O  
ANISOU 3207  O   GLY A 438    11659  12458  12528   -157  -1103     44       O  
ATOM   3208  N   GLU A 439     -44.116 -23.394 -84.610  1.00 99.19           N  
ANISOU 3208  N   GLU A 439    12122  12680  12885   -188  -1130     65       N  
ATOM   3209  CA  GLU A 439     -45.299 -22.780 -85.200  1.00101.18           C  
ANISOU 3209  CA  GLU A 439    12366  12902  13176   -244  -1087    121       C  
ATOM   3210  C   GLU A 439     -45.405 -21.299 -84.836  1.00 98.12           C  
ANISOU 3210  C   GLU A 439    11920  12514  12845   -301  -1033    137       C  
ATOM   3211  O   GLU A 439     -44.811 -20.844 -83.855  1.00 95.47           O  
ANISOU 3211  O   GLU A 439    11567  12185  12521   -307  -1030    109       O  
ATOM   3212  CB  GLU A 439     -46.569 -23.524 -84.762  1.00108.34           C  
ANISOU 3212  CB  GLU A 439    13353  13740  14068   -264  -1108    147       C  
ATOM   3213  CG  GLU A 439     -46.633 -24.987 -85.190  1.00116.36           C  
ANISOU 3213  CG  GLU A 439    14445  14739  15027   -218  -1168    140       C  
ATOM   3214  CD  GLU A 439     -46.356 -25.192 -86.674  1.00122.86           C  
ANISOU 3214  CD  GLU A 439    15239  15602  15838   -181  -1170    145       C  
ATOM   3215  OE1 GLU A 439     -47.040 -24.555 -87.515  1.00125.44           O  
ANISOU 3215  OE1 GLU A 439    15530  15932  16198   -216  -1128    184       O  
ATOM   3216  OE2 GLU A 439     -45.451 -25.998 -86.998  1.00125.10           O  
ANISOU 3216  OE2 GLU A 439    15537  15916  16077   -111  -1218    105       O  
ATOM   3217  N   ALA A 440     -46.172 -20.558 -85.632  1.00 97.17           N  
ANISOU 3217  N   ALA A 440    11777  12382  12758   -339   -997    179       N  
ATOM   3218  CA  ALA A 440     -46.427 -19.136 -85.379  1.00 95.73           C  
ANISOU 3218  CA  ALA A 440    11557  12187  12629   -390   -957    197       C  
ATOM   3219  C   ALA A 440     -47.040 -18.872 -83.996  1.00 93.61           C  
ANISOU 3219  C   ALA A 440    11312  11876  12380   -411   -956    188       C  
ATOM   3220  O   ALA A 440     -46.543 -18.030 -83.252  1.00 94.27           O  
ANISOU 3220  O   ALA A 440    11368  11961  12488   -428   -944    170       O  
ATOM   3221  CB  ALA A 440     -47.294 -18.543 -86.483  1.00 96.05           C  
ANISOU 3221  CB  ALA A 440    11587  12211  12694   -416   -933    241       C  
ATOM   3222  N   THR A 441     -48.099 -19.603 -83.657  1.00 91.39           N  
ANISOU 3222  N   THR A 441    11080  11560  12081   -413   -969    198       N  
ATOM   3223  CA  THR A 441     -48.761 -19.469 -82.360  1.00 91.43           C  
ANISOU 3223  CA  THR A 441    11107  11537  12093   -437   -967    188       C  
ATOM   3224  C   THR A 441     -47.821 -19.743 -81.190  1.00 91.90           C  
ANISOU 3224  C   THR A 441    11181  11604  12134   -420   -988    149       C  
ATOM   3225  O   THR A 441     -47.857 -19.051 -80.178  1.00 90.70           O  
ANISOU 3225  O   THR A 441    11015  11442  12003   -439   -975    134       O  
ATOM   3226  CB  THR A 441     -49.978 -20.408 -82.270  1.00 93.25           C  
ANISOU 3226  CB  THR A 441    11391  11746  12292   -452   -981    205       C  
ATOM   3227  OG1 THR A 441     -51.006 -19.919 -83.137  1.00 96.68           O  
ANISOU 3227  OG1 THR A 441    11803  12176  12751   -470   -957    235       O  
ATOM   3228  CG2 THR A 441     -50.525 -20.487 -80.841  1.00 92.83           C  
ANISOU 3228  CG2 THR A 441    11364  11680  12227   -480   -982    190       C  
ATOM   3229  N   GLU A 442     -46.973 -20.752 -81.337  1.00 94.97           N  
ANISOU 3229  N   GLU A 442    11596  12008  12479   -379  -1025    129       N  
ATOM   3230  CA  GLU A 442     -46.110 -21.171 -80.242  1.00 96.37           C  
ANISOU 3230  CA  GLU A 442    11796  12187  12630   -353  -1056     88       C  
ATOM   3231  C   GLU A 442     -44.860 -20.311 -80.096  1.00 94.72           C  
ANISOU 3231  C   GLU A 442    11522  12021  12446   -342  -1042     56       C  
ATOM   3232  O   GLU A 442     -44.443 -20.010 -78.975  1.00 96.05           O  
ANISOU 3232  O   GLU A 442    11688  12184  12619   -344  -1047     28       O  
ATOM   3233  CB  GLU A 442     -45.744 -22.642 -80.379  1.00 99.48           C  
ANISOU 3233  CB  GLU A 442    12258  12576  12961   -305  -1114     71       C  
ATOM   3234  CG  GLU A 442     -46.840 -23.593 -79.946  1.00104.67           C  
ANISOU 3234  CG  GLU A 442    13003  13183  13581   -330  -1140     93       C  
ATOM   3235  CD  GLU A 442     -46.428 -25.041 -80.100  1.00112.33           C  
ANISOU 3235  CD  GLU A 442    14057  14135  14487   -280  -1211     77       C  
ATOM   3236  OE1 GLU A 442     -45.675 -25.349 -81.058  1.00114.81           O  
ANISOU 3236  OE1 GLU A 442    14352  14481  14790   -224  -1231     59       O  
ATOM   3237  OE2 GLU A 442     -46.857 -25.870 -79.264  1.00115.67           O  
ANISOU 3237  OE2 GLU A 442    14568  14514  14865   -297  -1250     79       O  
ATOM   3238  N   THR A 443     -44.263 -19.913 -81.217  1.00 90.13           N  
ANISOU 3238  N   THR A 443    10885  11482  11875   -335  -1026     61       N  
ATOM   3239  CA  THR A 443     -43.170 -18.952 -81.169  1.00 88.19           C  
ANISOU 3239  CA  THR A 443    10571  11283  11653   -346  -1007     38       C  
ATOM   3240  C   THR A 443     -43.645 -17.703 -80.419  1.00 86.85           C  
ANISOU 3240  C   THR A 443    10386  11078  11534   -398   -976     51       C  
ATOM   3241  O   THR A 443     -42.929 -17.179 -79.562  1.00 87.47           O  
ANISOU 3241  O   THR A 443    10441  11168  11625   -403   -976     20       O  
ATOM   3242  CB  THR A 443     -42.665 -18.588 -82.577  1.00 88.36           C  
ANISOU 3242  CB  THR A 443    10537  11359  11675   -353   -986     52       C  
ATOM   3243  OG1 THR A 443     -42.217 -19.775 -83.236  1.00 90.41           O  
ANISOU 3243  OG1 THR A 443    10810  11657  11883   -295  -1020     31       O  
ATOM   3244  CG2 THR A 443     -41.506 -17.614 -82.504  1.00 87.56           C  
ANISOU 3244  CG2 THR A 443    10365  11313  11588   -380   -967     28       C  
ATOM   3245  N   ALA A 444     -44.868 -17.264 -80.719  1.00 84.19           N  
ANISOU 3245  N   ALA A 444    10063  10699  11225   -429   -954     91       N  
ATOM   3246  CA  ALA A 444     -45.461 -16.089 -80.080  1.00 83.67           C  
ANISOU 3246  CA  ALA A 444     9987  10598  11205   -466   -933     99       C  
ATOM   3247  C   ALA A 444     -45.623 -16.267 -78.573  1.00 83.98           C  
ANISOU 3247  C   ALA A 444    10052  10617  11237   -460   -945     69       C  
ATOM   3248  O   ALA A 444     -45.680 -15.280 -77.826  1.00 84.91           O  
ANISOU 3248  O   ALA A 444    10154  10718  11388   -481   -934     58       O  
ATOM   3249  CB  ALA A 444     -46.795 -15.755 -80.716  1.00 83.88           C  
ANISOU 3249  CB  ALA A 444    10025  10592  11252   -485   -917    137       C  
ATOM   3250  N   LEU A 445     -45.700 -17.525 -78.137  1.00 82.31           N  
ANISOU 3250  N   LEU A 445     9889  10404  10979   -434   -972     57       N  
ATOM   3251  CA  LEU A 445     -45.707 -17.848 -76.712  1.00 80.49           C  
ANISOU 3251  CA  LEU A 445     9692  10159  10730   -430   -989     29       C  
ATOM   3252  C   LEU A 445     -44.301 -17.874 -76.134  1.00 80.82           C  
ANISOU 3252  C   LEU A 445     9718  10226  10761   -401  -1010    -13       C  
ATOM   3253  O   LEU A 445     -44.090 -17.382 -75.031  1.00 82.74           O  
ANISOU 3253  O   LEU A 445     9958  10462  11017   -408  -1010    -38       O  
ATOM   3254  CB  LEU A 445     -46.418 -19.169 -76.440  1.00 78.42           C  
ANISOU 3254  CB  LEU A 445     9503   9878  10415   -425  -1016     38       C  
ATOM   3255  CG  LEU A 445     -47.934 -19.120 -76.550  1.00 77.38           C  
ANISOU 3255  CG  LEU A 445     9385   9727  10286   -464   -995     70       C  
ATOM   3256  CD1 LEU A 445     -48.527 -20.495 -76.314  1.00 77.79           C  
ANISOU 3256  CD1 LEU A 445     9514   9764  10277   -472  -1025     81       C  
ATOM   3257  CD2 LEU A 445     -48.494 -18.115 -75.561  1.00 77.59           C  
ANISOU 3257  CD2 LEU A 445     9385   9750  10342   -491   -969     58       C  
ATOM   3258  N   THR A 446     -43.347 -18.441 -76.873  1.00 79.82           N  
ANISOU 3258  N   THR A 446     9578  10137  10610   -366  -1030    -28       N  
ATOM   3259  CA  THR A 446     -41.939 -18.383 -76.476  1.00 79.52           C  
ANISOU 3259  CA  THR A 446     9507  10142  10562   -336  -1049    -77       C  
ATOM   3260  C   THR A 446     -41.535 -16.926 -76.262  1.00 79.22           C  
ANISOU 3260  C   THR A 446     9406  10118  10576   -378  -1015    -81       C  
ATOM   3261  O   THR A 446     -40.941 -16.586 -75.231  1.00 79.96           O  
ANISOU 3261  O   THR A 446     9489  10214  10675   -375  -1024   -116       O  
ATOM   3262  CB  THR A 446     -41.005 -19.042 -77.519  1.00 79.74           C  
ANISOU 3262  CB  THR A 446     9510  10229  10557   -291  -1069    -96       C  
ATOM   3263  OG1 THR A 446     -41.314 -20.436 -77.631  1.00 80.71           O  
ANISOU 3263  OG1 THR A 446     9707  10331  10628   -245  -1114    -99       O  
ATOM   3264  CG2 THR A 446     -39.544 -18.896 -77.115  1.00 79.12           C  
ANISOU 3264  CG2 THR A 446     9382  10213  10466   -261  -1087   -156       C  
ATOM   3265  N   THR A 447     -41.891 -16.072 -77.224  1.00 77.52           N  
ANISOU 3265  N   THR A 447     9156   9902  10395   -418   -982    -43       N  
ATOM   3266  CA  THR A 447     -41.503 -14.663 -77.196  1.00 77.60           C  
ANISOU 3266  CA  THR A 447     9118   9916  10450   -466   -958    -41       C  
ATOM   3267  C   THR A 447     -42.048 -13.954 -75.960  1.00 76.86           C  
ANISOU 3267  C   THR A 447     9043   9772  10387   -482   -956    -49       C  
ATOM   3268  O   THR A 447     -41.385 -13.081 -75.403  1.00 76.29           O  
ANISOU 3268  O   THR A 447     8942   9705  10338   -504   -954    -71       O  
ATOM   3269  CB  THR A 447     -41.928 -13.910 -78.480  1.00 78.12           C  
ANISOU 3269  CB  THR A 447     9163   9976  10540   -508   -931      6       C  
ATOM   3270  OG1 THR A 447     -41.297 -14.500 -79.623  1.00 78.01           O  
ANISOU 3270  OG1 THR A 447     9123  10022  10494   -495   -931      8       O  
ATOM   3271  CG2 THR A 447     -41.523 -12.438 -78.409  1.00 78.59           C  
ANISOU 3271  CG2 THR A 447     9191  10028  10640   -565   -917     11       C  
ATOM   3272  N   LEU A 448     -43.248 -14.341 -75.537  1.00 76.88           N  
ANISOU 3272  N   LEU A 448     9091   9733  10384   -474   -956    -34       N  
ATOM   3273  CA  LEU A 448     -43.885 -13.735 -74.364  1.00 77.78           C  
ANISOU 3273  CA  LEU A 448     9220   9811  10520   -485   -953    -47       C  
ATOM   3274  C   LEU A 448     -43.173 -14.111 -73.063  1.00 77.53           C  
ANISOU 3274  C   LEU A 448     9201   9789  10467   -462   -975    -92       C  
ATOM   3275  O   LEU A 448     -43.075 -13.297 -72.148  1.00 76.57           O  
ANISOU 3275  O   LEU A 448     9068   9652  10369   -473   -974   -113       O  
ATOM   3276  CB  LEU A 448     -45.376 -14.107 -74.299  1.00 77.61           C  
ANISOU 3276  CB  LEU A 448     9235   9763  10490   -487   -946    -24       C  
ATOM   3277  CG  LEU A 448     -46.188 -13.806 -73.028  1.00 77.11           C  
ANISOU 3277  CG  LEU A 448     9187   9680  10427   -492   -943    -43       C  
ATOM   3278  CD1 LEU A 448     -46.373 -12.315 -72.766  1.00 75.80           C  
ANISOU 3278  CD1 LEU A 448     8993   9494  10314   -505   -934    -53       C  
ATOM   3279  CD2 LEU A 448     -47.532 -14.505 -73.119  1.00 76.86           C  
ANISOU 3279  CD2 LEU A 448     9186   9648  10368   -499   -936    -23       C  
ATOM   3280  N   VAL A 449     -42.681 -15.346 -73.001  1.00 78.50           N  
ANISOU 3280  N   VAL A 449     9351   9933  10541   -427  -1001   -107       N  
ATOM   3281  CA  VAL A 449     -41.962 -15.857 -71.837  1.00 80.00           C  
ANISOU 3281  CA  VAL A 449     9563  10130  10702   -397  -1031   -152       C  
ATOM   3282  C   VAL A 449     -40.606 -15.149 -71.718  1.00 80.83           C  
ANISOU 3282  C   VAL A 449     9610  10273  10827   -394  -1034   -188       C  
ATOM   3283  O   VAL A 449     -40.076 -14.966 -70.611  1.00 80.75           O  
ANISOU 3283  O   VAL A 449     9601  10263  10816   -383  -1050   -226       O  
ATOM   3284  CB  VAL A 449     -41.793 -17.395 -71.914  1.00 80.48           C  
ANISOU 3284  CB  VAL A 449     9682  10196  10701   -353  -1070   -160       C  
ATOM   3285  CG1 VAL A 449     -40.942 -17.909 -70.765  1.00 82.68           C  
ANISOU 3285  CG1 VAL A 449     9989  10479  10944   -314  -1111   -210       C  
ATOM   3286  CG2 VAL A 449     -43.147 -18.090 -71.893  1.00 79.81           C  
ANISOU 3286  CG2 VAL A 449     9659  10073  10589   -371  -1069   -123       C  
ATOM   3287  N   GLU A 450     -40.070 -14.741 -72.868  1.00 81.36           N  
ANISOU 3287  N   GLU A 450     9626  10377  10910   -410  -1019   -176       N  
ATOM   3288  CA  GLU A 450     -38.829 -13.971 -72.940  1.00 82.41           C  
ANISOU 3288  CA  GLU A 450     9694  10558  11059   -428  -1016   -205       C  
ATOM   3289  C   GLU A 450     -38.981 -12.543 -72.427  1.00 82.24           C  
ANISOU 3289  C   GLU A 450     9654  10502  11088   -479   -998   -199       C  
ATOM   3290  O   GLU A 450     -38.131 -12.053 -71.692  1.00 81.60           O  
ANISOU 3290  O   GLU A 450     9546  10440  11016   -486  -1008   -237       O  
ATOM   3291  CB  GLU A 450     -38.304 -13.954 -74.375  1.00 82.86           C  
ANISOU 3291  CB  GLU A 450     9703  10671  11108   -444  -1002   -190       C  
ATOM   3292  CG  GLU A 450     -37.619 -15.241 -74.784  1.00 84.92           C  
ANISOU 3292  CG  GLU A 450     9962  10990  11314   -382  -1030   -222       C  
ATOM   3293  CD  GLU A 450     -36.517 -15.625 -73.817  1.00 87.40           C  
ANISOU 3293  CD  GLU A 450    10262  11344  11600   -336  -1065   -289       C  
ATOM   3294  OE1 GLU A 450     -35.728 -14.731 -73.439  1.00 88.35           O  
ANISOU 3294  OE1 GLU A 450    10328  11497  11742   -369  -1056   -315       O  
ATOM   3295  OE2 GLU A 450     -36.448 -16.811 -73.425  1.00 88.37           O  
ANISOU 3295  OE2 GLU A 450    10434  11462  11679   -269  -1107   -317       O  
ATOM   3296  N   LYS A 451     -40.068 -11.891 -72.833  1.00 83.26           N  
ANISOU 3296  N   LYS A 451     9801  10583  11250   -511   -978   -155       N  
ATOM   3297  CA  LYS A 451     -40.360 -10.515 -72.455  1.00 82.71           C  
ANISOU 3297  CA  LYS A 451     9727  10471  11228   -552   -970   -149       C  
ATOM   3298  C   LYS A 451     -40.730 -10.432 -70.991  1.00 83.85           C  
ANISOU 3298  C   LYS A 451     9898  10583  11377   -529   -983   -180       C  
ATOM   3299  O   LYS A 451     -40.361  -9.473 -70.321  1.00 86.05           O  
ANISOU 3299  O   LYS A 451    10165  10846  11684   -548   -990   -201       O  
ATOM   3300  CB  LYS A 451     -41.504  -9.951 -73.293  1.00 81.51           C  
ANISOU 3300  CB  LYS A 451     9593  10274  11102   -576   -955   -101       C  
ATOM   3301  CG  LYS A 451     -41.170  -9.758 -74.758  1.00 83.13           C  
ANISOU 3301  CG  LYS A 451     9775  10504  11307   -610   -942    -65       C  
ATOM   3302  CD  LYS A 451     -42.414  -9.347 -75.523  1.00 85.62           C  
ANISOU 3302  CD  LYS A 451    10118  10769  11642   -621   -932    -21       C  
ATOM   3303  CE  LYS A 451     -42.126  -9.113 -76.997  1.00 86.77           C  
ANISOU 3303  CE  LYS A 451    10247  10934  11784   -659   -920     18       C  
ATOM   3304  NZ  LYS A 451     -43.311  -8.541 -77.688  1.00 85.70           N  
ANISOU 3304  NZ  LYS A 451    10145  10743  11672   -667   -918     57       N  
ATOM   3305  N   MET A 452     -41.454 -11.437 -70.502  1.00 84.57           N  
ANISOU 3305  N   MET A 452    10029  10667  11436   -493   -988   -182       N  
ATOM   3306  CA  MET A 452     -41.952 -11.435 -69.126  1.00 86.08           C  
ANISOU 3306  CA  MET A 452    10250  10835  11621   -477   -996   -208       C  
ATOM   3307  C   MET A 452     -40.827 -11.580 -68.122  1.00 88.88           C  
ANISOU 3307  C   MET A 452    10598  11211  11962   -457  -1019   -256       C  
ATOM   3308  O   MET A 452     -40.781 -10.836 -67.137  1.00 91.25           O  
ANISOU 3308  O   MET A 452    10895  11493  12283   -461  -1025   -282       O  
ATOM   3309  CB  MET A 452     -42.974 -12.547 -68.903  1.00 85.10           C  
ANISOU 3309  CB  MET A 452    10174  10706  11455   -459   -996   -194       C  
ATOM   3310  CG  MET A 452     -44.341 -12.267 -69.498  1.00 85.05           C  
ANISOU 3310  CG  MET A 452    10172  10680  11463   -476   -974   -159       C  
ATOM   3311  SD  MET A 452     -45.439 -13.690 -69.411  1.00 83.70           S  
ANISOU 3311  SD  MET A 452    10053  10515  11232   -472   -973   -139       S  
ATOM   3312  CE  MET A 452     -45.928 -13.604 -67.688  1.00 84.04           C  
ANISOU 3312  CE  MET A 452    10119  10559  11252   -473   -977   -175       C  
ATOM   3313  N   ASN A 453     -39.922 -12.527 -68.386  1.00 89.88           N  
ANISOU 3313  N   ASN A 453    10720  11376  12052   -430  -1037   -272       N  
ATOM   3314  CA  ASN A 453     -38.838 -12.884 -67.461  1.00 91.22           C  
ANISOU 3314  CA  ASN A 453    10888  11572  12199   -398  -1066   -324       C  
ATOM   3315  C   ASN A 453     -39.329 -12.979 -66.005  1.00 92.12           C  
ANISOU 3315  C   ASN A 453    11048  11654  12299   -383  -1079   -345       C  
ATOM   3316  O   ASN A 453     -38.973 -12.158 -65.145  1.00 92.94           O  
ANISOU 3316  O   ASN A 453    11134  11751  12428   -390  -1083   -375       O  
ATOM   3317  CB  ASN A 453     -37.649 -11.918 -67.604  1.00 89.89           C  
ANISOU 3317  CB  ASN A 453    10653  11438  12061   -423  -1065   -350       C  
ATOM   3318  CG  ASN A 453     -36.391 -12.427 -66.922  1.00 89.31           C  
ANISOU 3318  CG  ASN A 453    10563  11411  11957   -382  -1098   -410       C  
ATOM   3319  OD1 ASN A 453     -36.302 -13.596 -66.529  1.00 88.67           O  
ANISOU 3319  OD1 ASN A 453    10525  11335  11828   -328  -1128   -431       O  
ATOM   3320  ND2 ASN A 453     -35.405 -11.546 -66.781  1.00 89.15           N  
ANISOU 3320  ND2 ASN A 453    10485  11424  11961   -409  -1099   -440       N  
ATOM   3321  N   VAL A 454     -40.160 -13.984 -65.750  1.00 91.26           N  
ANISOU 3321  N   VAL A 454    11000  11527  12147   -369  -1086   -329       N  
ATOM   3322  CA  VAL A 454     -40.789 -14.157 -64.441  1.00 91.47           C  
ANISOU 3322  CA  VAL A 454    11073  11530  12148   -366  -1093   -342       C  
ATOM   3323  C   VAL A 454     -39.806 -14.505 -63.314  1.00 92.06           C  
ANISOU 3323  C   VAL A 454    11169  11612  12195   -331  -1130   -393       C  
ATOM   3324  O   VAL A 454     -40.134 -14.343 -62.137  1.00 93.00           O  
ANISOU 3324  O   VAL A 454    11315  11717  12302   -333  -1134   -410       O  
ATOM   3325  CB  VAL A 454     -41.941 -15.191 -64.489  1.00 91.42           C  
ANISOU 3325  CB  VAL A 454    11132  11510  12094   -376  -1091   -308       C  
ATOM   3326  CG1 VAL A 454     -43.161 -14.597 -65.183  1.00 91.32           C  
ANISOU 3326  CG1 VAL A 454    11095  11490  12111   -413  -1052   -270       C  
ATOM   3327  CG2 VAL A 454     -41.494 -16.477 -65.171  1.00 90.80           C  
ANISOU 3327  CG2 VAL A 454    11093  11436  11969   -348  -1122   -300       C  
ATOM   3328  N   PHE A 455     -38.607 -14.965 -63.668  1.00 92.20           N  
ANISOU 3328  N   PHE A 455    11172  11660  12200   -295  -1159   -420       N  
ATOM   3329  CA  PHE A 455     -37.648 -15.410 -62.660  1.00 92.91           C  
ANISOU 3329  CA  PHE A 455    11284  11760  12256   -251  -1203   -474       C  
ATOM   3330  C   PHE A 455     -36.457 -14.478 -62.457  1.00 95.07           C  
ANISOU 3330  C   PHE A 455    11483  12069  12568   -246  -1206   -519       C  
ATOM   3331  O   PHE A 455     -35.518 -14.817 -61.731  1.00 98.59           O  
ANISOU 3331  O   PHE A 455    11936  12534  12989   -203  -1245   -571       O  
ATOM   3332  CB  PHE A 455     -37.196 -16.850 -62.937  1.00 93.24           C  
ANISOU 3332  CB  PHE A 455    11382  11809  12234   -198  -1251   -486       C  
ATOM   3333  CG  PHE A 455     -38.225 -17.881 -62.566  1.00 94.43           C  
ANISOU 3333  CG  PHE A 455    11633  11914  12329   -204  -1267   -454       C  
ATOM   3334  CD1 PHE A 455     -38.504 -18.160 -61.231  1.00 95.74           C  
ANISOU 3334  CD1 PHE A 455    11866  12051  12456   -205  -1288   -467       C  
ATOM   3335  CD2 PHE A 455     -38.932 -18.562 -63.545  1.00 95.18           C  
ANISOU 3335  CD2 PHE A 455    11759  11998  12405   -217  -1261   -410       C  
ATOM   3336  CE1 PHE A 455     -39.465 -19.102 -60.885  1.00 96.08           C  
ANISOU 3336  CE1 PHE A 455    12006  12058  12439   -228  -1302   -433       C  
ATOM   3337  CE2 PHE A 455     -39.895 -19.504 -63.204  1.00 94.96           C  
ANISOU 3337  CE2 PHE A 455    11826  11930  12321   -237  -1277   -378       C  
ATOM   3338  CZ  PHE A 455     -40.160 -19.777 -61.873  1.00 94.43           C  
ANISOU 3338  CZ  PHE A 455    11827  11838  12212   -247  -1297   -388       C  
ATOM   3339  N   ASN A 456     -36.516 -13.298 -63.077  1.00 94.64           N  
ANISOU 3339  N   ASN A 456    11364  12021  12571   -294  -1169   -500       N  
ATOM   3340  CA  ASN A 456     -35.488 -12.256 -62.923  1.00 93.56           C  
ANISOU 3340  CA  ASN A 456    11159  11914  12474   -312  -1169   -536       C  
ATOM   3341  C   ASN A 456     -34.074 -12.721 -63.257  1.00 94.03           C  
ANISOU 3341  C   ASN A 456    11172  12043  12508   -278  -1196   -583       C  
ATOM   3342  O   ASN A 456     -33.140 -12.557 -62.473  1.00 94.98           O  
ANISOU 3342  O   ASN A 456    11271  12192  12625   -257  -1222   -638       O  
ATOM   3343  CB  ASN A 456     -35.552 -11.643 -61.527  1.00 92.18           C  
ANISOU 3343  CB  ASN A 456    11000  11710  12312   -310  -1179   -565       C  
ATOM   3344  CG  ASN A 456     -36.866 -10.951 -61.269  1.00 93.88           C  
ANISOU 3344  CG  ASN A 456    11240  11874  12556   -343  -1151   -530       C  
ATOM   3345  OD1 ASN A 456     -37.433 -10.307 -62.157  1.00 94.12           O  
ANISOU 3345  OD1 ASN A 456    11248  11889  12620   -381  -1123   -491       O  
ATOM   3346  ND2 ASN A 456     -37.369 -11.086 -60.052  1.00 96.59           N  
ANISOU 3346  ND2 ASN A 456    11627  12193  12878   -325  -1161   -547       N  
ATOM   3347  N   THR A 457     -33.940 -13.309 -64.437  1.00 94.16           N  
ANISOU 3347  N   THR A 457    11173  12096  12507   -270  -1192   -566       N  
ATOM   3348  CA  THR A 457     -32.678 -13.833 -64.916  1.00 95.56           C  
ANISOU 3348  CA  THR A 457    11299  12355  12652   -232  -1217   -615       C  
ATOM   3349  C   THR A 457     -31.846 -12.686 -65.488  1.00 97.51           C  
ANISOU 3349  C   THR A 457    11448  12663  12936   -293  -1191   -625       C  
ATOM   3350  O   THR A 457     -32.393 -11.777 -66.119  1.00 97.38           O  
ANISOU 3350  O   THR A 457    11416  12622  12962   -364  -1152   -574       O  
ATOM   3351  CB  THR A 457     -32.933 -14.920 -65.983  1.00 94.90           C  
ANISOU 3351  CB  THR A 457    11238  12288  12530   -197  -1225   -594       C  
ATOM   3352  OG1 THR A 457     -33.694 -15.986 -65.399  1.00 92.89           O  
ANISOU 3352  OG1 THR A 457    11086  11972  12236   -152  -1255   -583       O  
ATOM   3353  CG2 THR A 457     -31.629 -15.479 -66.535  1.00 96.97           C  
ANISOU 3353  CG2 THR A 457    11441  12648  12754   -146  -1255   -654       C  
ATOM   3354  N   GLU A 458     -30.535 -12.718 -65.241  1.00 99.28           N  
ANISOU 3354  N   GLU A 458    11613  12968  13142   -270  -1216   -692       N  
ATOM   3355  CA  GLU A 458     -29.618 -11.752 -65.840  1.00101.00           C  
ANISOU 3355  CA  GLU A 458    11731  13262  13379   -337  -1193   -707       C  
ATOM   3356  C   GLU A 458     -29.524 -12.004 -67.339  1.00101.12           C  
ANISOU 3356  C   GLU A 458    11703  13339  13377   -358  -1169   -681       C  
ATOM   3357  O   GLU A 458     -28.934 -12.996 -67.775  1.00102.47           O  
ANISOU 3357  O   GLU A 458    11851  13583  13498   -293  -1193   -722       O  
ATOM   3358  CB  GLU A 458     -28.231 -11.834 -65.198  1.00103.77           C  
ANISOU 3358  CB  GLU A 458    12021  13701  13705   -303  -1228   -794       C  
ATOM   3359  CG  GLU A 458     -28.038 -10.961 -63.963  1.00105.44           C  
ANISOU 3359  CG  GLU A 458    12236  13874  13950   -329  -1236   -816       C  
ATOM   3360  CD  GLU A 458     -27.679  -9.519 -64.284  1.00107.46           C  
ANISOU 3360  CD  GLU A 458    12429  14150  14250   -440  -1205   -798       C  
ATOM   3361  OE1 GLU A 458     -28.508  -8.815 -64.898  1.00110.27           O  
ANISOU 3361  OE1 GLU A 458    12807  14446  14641   -509  -1171   -728       O  
ATOM   3362  OE2 GLU A 458     -26.568  -9.081 -63.911  1.00107.84           O  
ANISOU 3362  OE2 GLU A 458    12408  14270  14293   -461  -1219   -855       O  
ATOM   3363  N   VAL A 459     -30.128 -11.114 -68.122  1.00 99.41           N  
ANISOU 3363  N   VAL A 459    11481  13090  13199   -444  -1127   -615       N  
ATOM   3364  CA  VAL A 459     -30.183 -11.287 -69.574  1.00 97.82           C  
ANISOU 3364  CA  VAL A 459    11246  12937  12982   -471  -1101   -580       C  
ATOM   3365  C   VAL A 459     -29.564 -10.110 -70.327  1.00 97.55           C  
ANISOU 3365  C   VAL A 459    11137  12961  12965   -580  -1069   -564       C  
ATOM   3366  O   VAL A 459     -29.323 -10.188 -71.537  1.00 96.48           O  
ANISOU 3366  O   VAL A 459    10957  12894  12807   -612  -1047   -547       O  
ATOM   3367  CB  VAL A 459     -31.625 -11.574 -70.083  1.00 97.42           C  
ANISOU 3367  CB  VAL A 459    11272  12794  12946   -467  -1083   -508       C  
ATOM   3368  CG1 VAL A 459     -32.223 -12.780 -69.369  1.00 96.77           C  
ANISOU 3368  CG1 VAL A 459    11268  12660  12837   -375  -1116   -521       C  
ATOM   3369  CG2 VAL A 459     -32.530 -10.360 -69.931  1.00 97.95           C  
ANISOU 3369  CG2 VAL A 459    11374  12770  13071   -540  -1058   -451       C  
ATOM   3370  N   ARG A 460     -29.290  -9.033 -69.593  1.00 97.15           N  
ANISOU 3370  N   ARG A 460    11077  12884  12949   -640  -1070   -571       N  
ATOM   3371  CA  ARG A 460     -28.826  -7.776 -70.180  1.00 98.42           C  
ANISOU 3371  CA  ARG A 460    11191  13075  13128   -761  -1046   -545       C  
ATOM   3372  C   ARG A 460     -27.432  -7.842 -70.799  1.00100.88           C  
ANISOU 3372  C   ARG A 460    11392  13543  13392   -798  -1039   -594       C  
ATOM   3373  O   ARG A 460     -27.068  -6.979 -71.595  1.00101.41           O  
ANISOU 3373  O   ARG A 460    11418  13653  13458   -910  -1014   -565       O  
ATOM   3374  CB  ARG A 460     -28.881  -6.654 -69.145  1.00 97.93           C  
ANISOU 3374  CB  ARG A 460    11157  12938  13112   -809  -1059   -546       C  
ATOM   3375  CG  ARG A 460     -27.988  -6.864 -67.937  1.00 98.25           C  
ANISOU 3375  CG  ARG A 460    11165  13022  13141   -763  -1090   -625       C  
ATOM   3376  CD  ARG A 460     -27.878  -5.585 -67.132  1.00 98.32           C  
ANISOU 3376  CD  ARG A 460    11190  12974  13194   -833  -1101   -624       C  
ATOM   3377  NE  ARG A 460     -29.091  -5.325 -66.367  1.00 97.55           N  
ANISOU 3377  NE  ARG A 460    11184  12740  13137   -798  -1111   -592       N  
ATOM   3378  CZ  ARG A 460     -29.515  -4.114 -66.026  1.00 97.82           C  
ANISOU 3378  CZ  ARG A 460    11261  12688  13217   -859  -1118   -564       C  
ATOM   3379  NH1 ARG A 460     -28.830  -3.034 -66.390  1.00 97.78           N  
ANISOU 3379  NH1 ARG A 460    11224  12705  13222   -968  -1119   -555       N  
ATOM   3380  NH2 ARG A 460     -30.634  -3.984 -65.325  1.00 97.67           N  
ANISOU 3380  NH2 ARG A 460    11318  12564  13227   -813  -1128   -546       N  
ATOM   3381  N   ASN A 461     -26.663  -8.860 -70.419  1.00104.80           N  
ANISOU 3381  N   ASN A 461    11844  14128  13845   -706  -1065   -672       N  
ATOM   3382  CA  ASN A 461     -25.301  -9.057 -70.916  1.00105.82           C  
ANISOU 3382  CA  ASN A 461    11856  14428  13920   -720  -1064   -738       C  
ATOM   3383  C   ASN A 461     -25.174 -10.189 -71.933  1.00106.72           C  
ANISOU 3383  C   ASN A 461    11938  14630  13980   -650  -1063   -757       C  
ATOM   3384  O   ASN A 461     -24.085 -10.447 -72.447  1.00107.75           O  
ANISOU 3384  O   ASN A 461    11965  14918  14058   -650  -1062   -818       O  
ATOM   3385  CB  ASN A 461     -24.350  -9.297 -69.747  1.00107.42           C  
ANISOU 3385  CB  ASN A 461    12019  14688  14108   -661  -1103   -831       C  
ATOM   3386  CG  ASN A 461     -24.076  -8.036 -68.951  1.00110.88           C  
ANISOU 3386  CG  ASN A 461    12452  15088  14587   -754  -1101   -827       C  
ATOM   3387  OD1 ASN A 461     -24.076  -6.928 -69.494  1.00112.67           O  
ANISOU 3387  OD1 ASN A 461    12665  15309  14835   -883  -1072   -776       O  
ATOM   3388  ND2 ASN A 461     -23.827  -8.199 -67.654  1.00111.64           N  
ANISOU 3388  ND2 ASN A 461    12567  15156  14693   -689  -1139   -881       N  
ATOM   3389  N   LEU A 462     -26.292 -10.855 -72.218  1.00107.36           N  
ANISOU 3389  N   LEU A 462    12105  14614  14071   -592  -1064   -707       N  
ATOM   3390  CA  LEU A 462     -26.336 -11.953 -73.184  1.00105.72           C  
ANISOU 3390  CA  LEU A 462    11885  14466  13815   -521  -1068   -717       C  
ATOM   3391  C   LEU A 462     -26.244 -11.449 -74.620  1.00107.71           C  
ANISOU 3391  C   LEU A 462    12081  14790  14053   -616  -1022   -672       C  
ATOM   3392  O   LEU A 462     -26.686 -10.341 -74.931  1.00109.94           O  
ANISOU 3392  O   LEU A 462    12382  15014  14374   -730   -988   -601       O  
ATOM   3393  CB  LEU A 462     -27.614 -12.776 -73.003  1.00100.93           C  
ANISOU 3393  CB  LEU A 462    11396  13727  13224   -442  -1086   -673       C  
ATOM   3394  CG  LEU A 462     -27.802 -13.492 -71.668  1.00 98.79           C  
ANISOU 3394  CG  LEU A 462    11197  13385  12953   -344  -1135   -712       C  
ATOM   3395  CD1 LEU A 462     -29.205 -14.054 -71.590  1.00 98.45           C  
ANISOU 3395  CD1 LEU A 462    11268  13210  12928   -308  -1140   -650       C  
ATOM   3396  CD2 LEU A 462     -26.780 -14.601 -71.481  1.00 99.69           C  
ANISOU 3396  CD2 LEU A 462    11272  13600  13002   -232  -1188   -809       C  
ATOM   3397  N   SER A 463     -25.655 -12.268 -75.485  1.00107.77           N  
ANISOU 3397  N   SER A 463    12023  14924  13999   -565  -1026   -716       N  
ATOM   3398  CA  SER A 463     -25.568 -11.967 -76.907  1.00107.95           C  
ANISOU 3398  CA  SER A 463    11992  15027  13996   -643   -984   -678       C  
ATOM   3399  C   SER A 463     -26.919 -12.242 -77.526  1.00106.25           C  
ANISOU 3399  C   SER A 463    11874  14687  13808   -629   -972   -593       C  
ATOM   3400  O   SER A 463     -27.654 -13.091 -77.028  1.00106.68           O  
ANISOU 3400  O   SER A 463    12011  14646  13875   -529  -1004   -592       O  
ATOM   3401  CB  SER A 463     -24.530 -12.869 -77.556  1.00111.66           C  
ANISOU 3401  CB  SER A 463    12359  15679  14387   -572   -998   -765       C  
ATOM   3402  OG  SER A 463     -24.768 -14.222 -77.210  1.00111.13           O  
ANISOU 3402  OG  SER A 463    12346  15580  14299   -415  -1052   -811       O  
ATOM   3403  N   LYS A 464     -27.241 -11.533 -78.610  1.00105.94           N  
ANISOU 3403  N   LYS A 464    11827  14651  13775   -732   -928   -524       N  
ATOM   3404  CA  LYS A 464     -28.544 -11.677 -79.281  1.00104.18           C  
ANISOU 3404  CA  LYS A 464    11690  14313  13578   -728   -915   -441       C  
ATOM   3405  C   LYS A 464     -28.928 -13.145 -79.464  1.00104.33           C  
ANISOU 3405  C   LYS A 464    11745  14326  13568   -592   -947   -468       C  
ATOM   3406  O   LYS A 464     -30.076 -13.525 -79.235  1.00102.73           O  
ANISOU 3406  O   LYS A 464    11638  13994  13397   -548   -958   -424       O  
ATOM   3407  CB  LYS A 464     -28.558 -10.968 -80.641  1.00102.22           C  
ANISOU 3407  CB  LYS A 464    11410  14112  13315   -840   -871   -382       C  
ATOM   3408  CG  LYS A 464     -28.675  -9.450 -80.612  1.00 99.82           C  
ANISOU 3408  CG  LYS A 464    11125  13750  13050   -985   -847   -321       C  
ATOM   3409  CD  LYS A 464     -30.066  -8.981 -80.215  1.00 98.65           C  
ANISOU 3409  CD  LYS A 464    11095  13413  12971   -987   -853   -249       C  
ATOM   3410  CE  LYS A 464     -30.574  -7.859 -81.110  1.00 99.72           C  
ANISOU 3410  CE  LYS A 464    11270  13494  13124  -1107   -829   -164       C  
ATOM   3411  NZ  LYS A 464     -29.536  -6.843 -81.443  1.00100.90           N  
ANISOU 3411  NZ  LYS A 464    11357  13732  13246  -1245   -811   -163       N  
ATOM   3412  N   VAL A 465     -27.945 -13.954 -79.857  1.00106.06           N  
ANISOU 3412  N   VAL A 465    11884  14690  13721   -526   -964   -545       N  
ATOM   3413  CA  VAL A 465     -28.118 -15.388 -80.091  1.00105.67           C  
ANISOU 3413  CA  VAL A 465    11866  14650  13632   -391  -1007   -584       C  
ATOM   3414  C   VAL A 465     -28.473 -16.137 -78.799  1.00106.30           C  
ANISOU 3414  C   VAL A 465    12033  14627  13728   -289  -1061   -614       C  
ATOM   3415  O   VAL A 465     -29.439 -16.902 -78.759  1.00106.27           O  
ANISOU 3415  O   VAL A 465    12126  14519  13732   -229  -1085   -581       O  
ATOM   3416  CB  VAL A 465     -26.846 -16.010 -80.706  1.00104.62           C  
ANISOU 3416  CB  VAL A 465    11619  14709  13419   -335  -1022   -677       C  
ATOM   3417  CG1 VAL A 465     -27.206 -17.229 -81.537  1.00104.84           C  
ANISOU 3417  CG1 VAL A 465    11680  14748  13406   -230  -1051   -687       C  
ATOM   3418  CG2 VAL A 465     -26.096 -14.991 -81.555  1.00104.56           C  
ANISOU 3418  CG2 VAL A 465    11499  14836  13390   -464   -966   -668       C  
ATOM   3419  N   GLU A 466     -27.688 -15.894 -77.752  1.00108.42           N  
ANISOU 3419  N   GLU A 466    12268  14928  13997   -280  -1081   -673       N  
ATOM   3420  CA  GLU A 466     -27.842 -16.542 -76.447  1.00109.86           C  
ANISOU 3420  CA  GLU A 466    12527  15029  14186   -189  -1136   -710       C  
ATOM   3421  C   GLU A 466     -29.082 -16.032 -75.705  1.00106.02           C  
ANISOU 3421  C   GLU A 466    12142  14373  13765   -237  -1120   -631       C  
ATOM   3422  O   GLU A 466     -29.577 -16.683 -74.783  1.00103.81           O  
ANISOU 3422  O   GLU A 466    11950  14003  13488   -170  -1160   -638       O  
ATOM   3423  CB  GLU A 466     -26.593 -16.263 -75.610  1.00116.00           C  
ANISOU 3423  CB  GLU A 466    13226  15901  14946   -178  -1156   -796       C  
ATOM   3424  CG  GLU A 466     -26.031 -17.434 -74.818  1.00122.42           C  
ANISOU 3424  CG  GLU A 466    14064  16735  15712    -35  -1233   -889       C  
ATOM   3425  CD  GLU A 466     -24.703 -17.093 -74.143  1.00128.54           C  
ANISOU 3425  CD  GLU A 466    14743  17629  16466    -26  -1251   -982       C  
ATOM   3426  OE1 GLU A 466     -24.219 -15.948 -74.297  1.00129.88           O  
ANISOU 3426  OE1 GLU A 466    14825  17867  16657   -141  -1200   -972       O  
ATOM   3427  OE2 GLU A 466     -24.135 -17.969 -73.452  1.00131.33           O  
ANISOU 3427  OE2 GLU A 466    15112  18008  16779     93  -1320  -1068       O  
ATOM   3428  N   ARG A 467     -29.568 -14.862 -76.116  1.00104.07           N  
ANISOU 3428  N   ARG A 467    11886  14090  13566   -352  -1066   -559       N  
ATOM   3429  CA  ARG A 467     -30.730 -14.216 -75.511  1.00100.78           C  
ANISOU 3429  CA  ARG A 467    11551  13528  13210   -400  -1049   -490       C  
ATOM   3430  C   ARG A 467     -32.027 -14.906 -75.923  1.00 99.47           C  
ANISOU 3430  C   ARG A 467    11474  13269  13050   -365  -1052   -434       C  
ATOM   3431  O   ARG A 467     -32.896 -15.146 -75.085  1.00 99.87           O  
ANISOU 3431  O   ARG A 467    11607  13216  13122   -340  -1067   -414       O  
ATOM   3432  CB  ARG A 467     -30.773 -12.727 -75.901  1.00 98.34           C  
ANISOU 3432  CB  ARG A 467    11207  13213  12943   -529  -1002   -438       C  
ATOM   3433  CG  ARG A 467     -31.990 -11.952 -75.412  1.00 95.23           C  
ANISOU 3433  CG  ARG A 467    10894  12677  12611   -574   -988   -372       C  
ATOM   3434  CD  ARG A 467     -31.876 -11.610 -73.936  1.00 96.02           C  
ANISOU 3434  CD  ARG A 467    11017  12728  12738   -561  -1010   -404       C  
ATOM   3435  NE  ARG A 467     -33.140 -11.145 -73.363  1.00 95.95           N  
ANISOU 3435  NE  ARG A 467    11089  12591  12777   -575  -1005   -355       N  
ATOM   3436  CZ  ARG A 467     -34.073 -11.941 -72.849  1.00 95.16           C  
ANISOU 3436  CZ  ARG A 467    11060  12420  12674   -510  -1021   -346       C  
ATOM   3437  NH1 ARG A 467     -33.897 -13.253 -72.837  1.00 95.36           N  
ANISOU 3437  NH1 ARG A 467    11101  12476  12653   -429  -1048   -378       N  
ATOM   3438  NH2 ARG A 467     -35.188 -11.428 -72.348  1.00 94.42           N  
ANISOU 3438  NH2 ARG A 467    11024  12230  12619   -528  -1013   -308       N  
ATOM   3439  N   ALA A 468     -32.129 -15.233 -77.210  1.00 96.96           N  
ANISOU 3439  N   ALA A 468    11134  12996  12708   -367  -1037   -411       N  
ATOM   3440  CA  ALA A 468     -33.363 -15.716 -77.841  1.00 95.77           C  
ANISOU 3440  CA  ALA A 468    11056  12766  12565   -354  -1031   -350       C  
ATOM   3441  C   ALA A 468     -34.245 -16.654 -77.006  1.00 95.80           C  
ANISOU 3441  C   ALA A 468    11161  12671  12567   -285  -1068   -346       C  
ATOM   3442  O   ALA A 468     -35.471 -16.585 -77.082  1.00 97.26           O  
ANISOU 3442  O   ALA A 468    11408  12765  12780   -308  -1054   -286       O  
ATOM   3443  CB  ALA A 468     -33.046 -16.352 -79.188  1.00 95.81           C  
ANISOU 3443  CB  ALA A 468    11022  12857  12525   -326  -1029   -356       C  
ATOM   3444  N   ASN A 469     -33.632 -17.532 -76.221  1.00 95.08           N  
ANISOU 3444  N   ASN A 469    11088  12599  12438   -204  -1119   -411       N  
ATOM   3445  CA  ASN A 469     -34.397 -18.525 -75.471  1.00 93.53           C  
ANISOU 3445  CA  ASN A 469    10998  12313  12225   -145  -1162   -407       C  
ATOM   3446  C   ASN A 469     -34.033 -18.588 -73.990  1.00 94.22           C  
ANISOU 3446  C   ASN A 469    11115  12373  12309   -117  -1195   -451       C  
ATOM   3447  O   ASN A 469     -34.524 -19.458 -73.265  1.00 96.09           O  
ANISOU 3447  O   ASN A 469    11444  12542  12521    -71  -1237   -454       O  
ATOM   3448  CB  ASN A 469     -34.242 -19.904 -76.114  1.00 93.68           C  
ANISOU 3448  CB  ASN A 469    11052  12358  12184    -58  -1211   -434       C  
ATOM   3449  CG  ASN A 469     -34.501 -19.882 -77.604  1.00 92.92           C  
ANISOU 3449  CG  ASN A 469    10919  12299  12084    -79  -1181   -397       C  
ATOM   3450  OD1 ASN A 469     -35.639 -19.978 -78.050  1.00 93.10           O  
ANISOU 3450  OD1 ASN A 469    10995  12251  12125   -108  -1163   -333       O  
ATOM   3451  ND2 ASN A 469     -33.439 -19.757 -78.383  1.00 93.95           N  
ANISOU 3451  ND2 ASN A 469    10956  12550  12189    -67  -1174   -440       N  
ATOM   3452  N   ALA A 470     -33.190 -17.652 -73.553  1.00 93.12           N  
ANISOU 3452  N   ALA A 470    10902  12285  12193   -151  -1177   -483       N  
ATOM   3453  CA  ALA A 470     -32.701 -17.577 -72.175  1.00 91.92           C  
ANISOU 3453  CA  ALA A 470    10764  12119  12039   -126  -1207   -531       C  
ATOM   3454  C   ALA A 470     -33.777 -17.828 -71.109  1.00 92.87           C  
ANISOU 3454  C   ALA A 470    10988  12125  12170   -125  -1220   -499       C  
ATOM   3455  O   ALA A 470     -33.660 -18.765 -70.316  1.00 93.53           O  
ANISOU 3455  O   ALA A 470    11140  12182  12213    -58  -1274   -534       O  
ATOM   3456  CB  ALA A 470     -32.019 -16.237 -71.942  1.00 90.30           C  
ANISOU 3456  CB  ALA A 470    10473  11961  11875   -197  -1171   -544       C  
ATOM   3457  N   CYS A 471     -34.825 -17.006 -71.107  1.00 92.89           N  
ANISOU 3457  N   CYS A 471    11006  12065  12222   -198  -1173   -435       N  
ATOM   3458  CA  CYS A 471     -35.873 -17.081 -70.091  1.00 93.99           C  
ANISOU 3458  CA  CYS A 471    11226  12115  12371   -208  -1176   -408       C  
ATOM   3459  C   CYS A 471     -36.699 -18.354 -70.183  1.00 95.01           C  
ANISOU 3459  C   CYS A 471    11449  12195  12455   -173  -1206   -385       C  
ATOM   3460  O   CYS A 471     -37.186 -18.859 -69.166  1.00 95.68           O  
ANISOU 3460  O   CYS A 471    11611  12226  12516   -161  -1231   -386       O  
ATOM   3461  CB  CYS A 471     -36.792 -15.869 -70.191  1.00 95.88           C  
ANISOU 3461  CB  CYS A 471    11448  12311  12669   -286  -1123   -355       C  
ATOM   3462  SG  CYS A 471     -35.968 -14.299 -69.853  1.00102.16           S  
ANISOU 3462  SG  CYS A 471    12163  13137  13517   -341  -1098   -376       S  
ATOM   3463  N   ASN A 472     -36.869 -18.854 -71.405  1.00 95.28           N  
ANISOU 3463  N   ASN A 472    11479  12248  12475   -162  -1203   -362       N  
ATOM   3464  CA  ASN A 472     -37.552 -20.117 -71.640  1.00 95.82           C  
ANISOU 3464  CA  ASN A 472    11637  12274  12496   -129  -1239   -342       C  
ATOM   3465  C   ASN A 472     -36.757 -21.282 -71.075  1.00 97.99           C  
ANISOU 3465  C   ASN A 472    11970  12554  12707    -45  -1315   -401       C  
ATOM   3466  O   ASN A 472     -37.295 -22.122 -70.352  1.00101.35           O  
ANISOU 3466  O   ASN A 472    12499  12916  13093    -31  -1356   -393       O  
ATOM   3467  CB  ASN A 472     -37.799 -20.328 -73.132  1.00 97.01           C  
ANISOU 3467  CB  ASN A 472    11762  12449  12646   -132  -1222   -311       C  
ATOM   3468  CG  ASN A 472     -39.074 -19.666 -73.613  1.00 98.69           C  
ANISOU 3468  CG  ASN A 472    11974  12621  12903   -204  -1167   -241       C  
ATOM   3469  OD1 ASN A 472     -40.078 -20.336 -73.853  1.00101.66           O  
ANISOU 3469  OD1 ASN A 472    12414  12951  13261   -211  -1173   -204       O  
ATOM   3470  ND2 ASN A 472     -39.043 -18.346 -73.757  1.00 97.83           N  
ANISOU 3470  ND2 ASN A 472    11794  12527  12848   -258  -1118   -226       N  
ATOM   3471  N   SER A 473     -35.467 -21.319 -71.389  1.00 98.40           N  
ANISOU 3471  N   SER A 473    11957  12686  12744      9  -1338   -462       N  
ATOM   3472  CA  SER A 473     -34.613 -22.417 -70.957  1.00 99.09           C  
ANISOU 3472  CA  SER A 473    12094  12788  12768    106  -1420   -531       C  
ATOM   3473  C   SER A 473     -34.352 -22.441 -69.446  1.00 98.79           C  
ANISOU 3473  C   SER A 473    12105  12712  12716    123  -1454   -564       C  
ATOM   3474  O   SER A 473     -33.866 -23.443 -68.924  1.00102.44           O  
ANISOU 3474  O   SER A 473    12642  13160  13121    203  -1533   -613       O  
ATOM   3475  CB  SER A 473     -33.306 -22.459 -71.764  1.00100.42           C  
ANISOU 3475  CB  SER A 473    12165  13070  12916    167  -1436   -597       C  
ATOM   3476  OG  SER A 473     -32.741 -21.169 -71.912  1.00103.08           O  
ANISOU 3476  OG  SER A 473    12381  13481  13304    108  -1375   -605       O  
ATOM   3477  N   VAL A 474     -34.680 -21.358 -68.743  1.00 96.35           N  
ANISOU 3477  N   VAL A 474    11762  12385  12459     53  -1402   -541       N  
ATOM   3478  CA  VAL A 474     -34.615 -21.376 -67.279  1.00 97.37           C  
ANISOU 3478  CA  VAL A 474    11947  12472  12575     61  -1430   -564       C  
ATOM   3479  C   VAL A 474     -35.775 -22.201 -66.712  1.00 99.38           C  
ANISOU 3479  C   VAL A 474    12333  12633  12792     43  -1454   -518       C  
ATOM   3480  O   VAL A 474     -35.578 -22.992 -65.782  1.00102.83           O  
ANISOU 3480  O   VAL A 474    12862  13031  13176     86  -1518   -546       O  
ATOM   3481  CB  VAL A 474     -34.582 -19.960 -66.655  1.00 95.98           C  
ANISOU 3481  CB  VAL A 474    11696  12307  12462     -2  -1373   -560       C  
ATOM   3482  CG1 VAL A 474     -34.527 -20.026 -65.132  1.00 93.50           C  
ANISOU 3482  CG1 VAL A 474    11442  11951  12130     10  -1404   -586       C  
ATOM   3483  CG2 VAL A 474     -33.382 -19.186 -67.167  1.00 97.22           C  
ANISOU 3483  CG2 VAL A 474    11731  12559  12647      2  -1355   -605       C  
ATOM   3484  N   ILE A 475     -36.970 -22.028 -67.283  1.00 98.76           N  
ANISOU 3484  N   ILE A 475    12265  12522  12736    -22  -1406   -448       N  
ATOM   3485  CA  ILE A 475     -38.157 -22.775 -66.854  1.00 97.95           C  
ANISOU 3485  CA  ILE A 475    12276  12346  12595    -58  -1420   -400       C  
ATOM   3486  C   ILE A 475     -37.964 -24.251 -67.169  1.00101.82           C  
ANISOU 3486  C   ILE A 475    12868  12805  13010      4  -1501   -413       C  
ATOM   3487  O   ILE A 475     -38.322 -25.111 -66.363  1.00105.60           O  
ANISOU 3487  O   ILE A 475    13468  13223  13430      4  -1553   -407       O  
ATOM   3488  CB  ILE A 475     -39.465 -22.227 -67.484  1.00 95.25           C  
ANISOU 3488  CB  ILE A 475    11908  11990  12293   -139  -1351   -331       C  
ATOM   3489  CG1 ILE A 475     -39.822 -20.875 -66.857  1.00 93.23           C  
ANISOU 3489  CG1 ILE A 475    11584  11742  12095   -195  -1289   -322       C  
ATOM   3490  CG2 ILE A 475     -40.623 -23.202 -67.298  1.00 93.28           C  
ANISOU 3490  CG2 ILE A 475    11770  11680  11989   -175  -1372   -285       C  
ATOM   3491  CD1 ILE A 475     -40.897 -20.100 -67.580  1.00 90.95           C  
ANISOU 3491  CD1 ILE A 475    11247  11454  11856   -258  -1224   -270       C  
ATOM   3492  N   ARG A 476     -37.368 -24.537 -68.325  1.00104.30           N  
ANISOU 3492  N   ARG A 476    13140  13164  13323     56  -1517   -434       N  
ATOM   3493  CA  ARG A 476     -37.087 -25.919 -68.719  1.00109.86           C  
ANISOU 3493  CA  ARG A 476    13939  13844  13957    131  -1603   -456       C  
ATOM   3494  C   ARG A 476     -36.145 -26.646 -67.745  1.00112.28           C  
ANISOU 3494  C   ARG A 476    14321  14135  14205    216  -1695   -525       C  
ATOM   3495  O   ARG A 476     -36.252 -27.856 -67.551  1.00112.19           O  
ANISOU 3495  O   ARG A 476    14443  14061  14123    258  -1780   -530       O  
ATOM   3496  CB  ARG A 476     -36.590 -25.982 -70.167  1.00110.50           C  
ANISOU 3496  CB  ARG A 476    13943  13991  14049    176  -1598   -473       C  
ATOM   3497  CG  ARG A 476     -37.732 -26.071 -71.171  1.00111.40           C  
ANISOU 3497  CG  ARG A 476    14068  14079  14178    117  -1557   -400       C  
ATOM   3498  CD  ARG A 476     -37.255 -26.151 -72.610  1.00112.72           C  
ANISOU 3498  CD  ARG A 476    14163  14312  14351    161  -1552   -416       C  
ATOM   3499  NE  ARG A 476     -37.222 -24.840 -73.255  1.00116.21           N  
ANISOU 3499  NE  ARG A 476    14470  14819  14863    104  -1462   -395       N  
ATOM   3500  CZ  ARG A 476     -36.125 -24.255 -73.735  1.00121.02           C  
ANISOU 3500  CZ  ARG A 476    14967  15525  15490    134  -1444   -442       C  
ATOM   3501  NH1 ARG A 476     -34.947 -24.864 -73.655  1.00123.72           N  
ANISOU 3501  NH1 ARG A 476    15300  15921  15784    229  -1508   -522       N  
ATOM   3502  NH2 ARG A 476     -36.206 -23.057 -74.306  1.00121.97           N  
ANISOU 3502  NH2 ARG A 476    14983  15689  15668     66  -1365   -412       N  
ATOM   3503  N   GLN A 477     -35.254 -25.892 -67.111  1.00116.85           N  
ANISOU 3503  N   GLN A 477    14821  14765  14811    238  -1682   -577       N  
ATOM   3504  CA  GLN A 477     -34.368 -26.435 -66.086  1.00120.50           C  
ANISOU 3504  CA  GLN A 477    15346  15216  15223    317  -1764   -645       C  
ATOM   3505  C   GLN A 477     -35.044 -26.521 -64.718  1.00120.92           C  
ANISOU 3505  C   GLN A 477    15501  15187  15253    263  -1773   -614       C  
ATOM   3506  O   GLN A 477     -34.379 -26.784 -63.714  1.00122.02           O  
ANISOU 3506  O   GLN A 477    15691  15313  15357    315  -1832   -665       O  
ATOM   3507  CB  GLN A 477     -33.100 -25.591 -65.983  1.00124.32           C  
ANISOU 3507  CB  GLN A 477    15694  15797  15741    360  -1747   -718       C  
ATOM   3508  CG  GLN A 477     -32.148 -25.739 -67.159  1.00129.16           C  
ANISOU 3508  CG  GLN A 477    16216  16508  16349    433  -1762   -774       C  
ATOM   3509  CD  GLN A 477     -30.998 -24.749 -67.105  1.00134.68           C  
ANISOU 3509  CD  GLN A 477    16766  17319  17086    445  -1728   -837       C  
ATOM   3510  OE1 GLN A 477     -30.910 -23.922 -66.194  1.00135.54           O  
ANISOU 3510  OE1 GLN A 477    16843  17424  17230    401  -1695   -837       O  
ATOM   3511  NE2 GLN A 477     -30.109 -24.827 -68.089  1.00139.25           N  
ANISOU 3511  NE2 GLN A 477    17251  18004  17653    503  -1737   -892       N  
ATOM   3512  N   LEU A 478     -36.357 -26.300 -64.683  1.00121.04           N  
ANISOU 3512  N   LEU A 478    15546  15157  15285    161  -1716   -534       N  
ATOM   3513  CA  LEU A 478     -37.122 -26.366 -63.436  1.00122.66           C  
ANISOU 3513  CA  LEU A 478    15842  15300  15463     97  -1716   -501       C  
ATOM   3514  C   LEU A 478     -38.048 -27.569 -63.362  1.00124.35           C  
ANISOU 3514  C   LEU A 478    16213  15432  15601     61  -1767   -451       C  
ATOM   3515  O   LEU A 478     -38.347 -28.046 -62.264  1.00122.99           O  
ANISOU 3515  O   LEU A 478    16153  15203  15371     34  -1806   -442       O  
ATOM   3516  CB  LEU A 478     -37.912 -25.080 -63.205  1.00123.50           C  
ANISOU 3516  CB  LEU A 478    15855  15431  15639      1  -1611   -459       C  
ATOM   3517  CG  LEU A 478     -37.136 -23.898 -62.626  1.00126.21           C  
ANISOU 3517  CG  LEU A 478    16088  15825  16038     14  -1575   -504       C  
ATOM   3518  CD1 LEU A 478     -37.855 -22.597 -62.951  1.00127.06           C  
ANISOU 3518  CD1 LEU A 478    16089  15962  16224    -63  -1476   -463       C  
ATOM   3519  CD2 LEU A 478     -36.928 -24.049 -61.124  1.00126.44           C  
ANISOU 3519  CD2 LEU A 478    16190  15821  16027     22  -1614   -531       C  
ATOM   3520  N   MET A 479     -38.519 -28.034 -64.521  1.00128.77           N  
ANISOU 3520  N   MET A 479    16782  15986  16159     54  -1765   -417       N  
ATOM   3521  CA  MET A 479     -39.176 -29.355 -64.629  1.00134.19           C  
ANISOU 3521  CA  MET A 479    17629  16592  16765     36  -1836   -381       C  
ATOM   3522  C   MET A 479     -38.954 -30.125 -65.937  1.00133.10           C  
ANISOU 3522  C   MET A 479    17510  16452  16610     99  -1883   -388       C  
ATOM   3523  O   MET A 479     -39.048 -29.572 -67.039  1.00135.13           O  
ANISOU 3523  O   MET A 479    17652  16764  16924     95  -1822   -376       O  
ATOM   3524  CB  MET A 479     -40.673 -29.340 -64.255  1.00135.71           C  
ANISOU 3524  CB  MET A 479    17871  16748  16941    -95  -1786   -301       C  
ATOM   3525  CG  MET A 479     -41.362 -27.992 -64.173  1.00135.78           C  
ANISOU 3525  CG  MET A 479    17746  16815  17028   -175  -1668   -272       C  
ATOM   3526  SD  MET A 479     -42.629 -28.087 -62.892  1.00140.98           S  
ANISOU 3526  SD  MET A 479    18490  17441  17634   -299  -1644   -220       S  
ATOM   3527  CE  MET A 479     -41.636 -27.966 -61.402  1.00138.42           C  
ANISOU 3527  CE  MET A 479    18204  17105  17283   -249  -1690   -278       C  
ATOM   3528  N   LYS A 480     -38.668 -31.416 -65.775  1.00128.59           N  
ANISOU 3528  N   LYS A 480    17092  15811  15953    158  -1999   -408       N  
ATOM   3529  CA  LYS A 480     -38.442 -32.343 -66.875  1.00127.72           C  
ANISOU 3529  CA  LYS A 480    17033  15684  15809    230  -2069   -423       C  
ATOM   3530  C   LYS A 480     -39.737 -32.619 -67.642  1.00125.89           C  
ANISOU 3530  C   LYS A 480    16834  15420  15577    134  -2032   -341       C  
ATOM   3531  O   LYS A 480     -40.740 -33.040 -67.061  1.00124.92           O  
ANISOU 3531  O   LYS A 480    16821  15231  15410     35  -2038   -282       O  
ATOM   3532  CB  LYS A 480     -37.849 -33.652 -66.330  1.00129.62           C  
ANISOU 3532  CB  LYS A 480    17453  15844  15952    317  -2216   -468       C  
ATOM   3533  CG  LYS A 480     -37.362 -34.646 -67.378  1.00129.89           C  
ANISOU 3533  CG  LYS A 480    17544  15863  15943    426  -2311   -507       C  
ATOM   3534  CD  LYS A 480     -36.811 -35.900 -66.714  1.00129.13           C  
ANISOU 3534  CD  LYS A 480    17642  15675  15746    515  -2468   -554       C  
ATOM   3535  CE  LYS A 480     -36.355 -36.933 -67.733  1.00128.11           C  
ANISOU 3535  CE  LYS A 480    17581  15525  15567    634  -2576   -600       C  
ATOM   3536  NZ  LYS A 480     -35.927 -38.193 -67.063  1.00126.52           N  
ANISOU 3536  NZ  LYS A 480    17594  15215  15260    718  -2742   -641       N  
ATOM   3537  N   LYS A 481     -39.700 -32.364 -68.946  1.00124.08           N  
ANISOU 3537  N   LYS A 481    16506  15245  15394    161  -1993   -341       N  
ATOM   3538  CA  LYS A 481     -40.815 -32.660 -69.838  1.00123.65           C  
ANISOU 3538  CA  LYS A 481    16474  15166  15341     89  -1965   -273       C  
ATOM   3539  C   LYS A 481     -40.839 -34.161 -70.106  1.00125.34           C  
ANISOU 3539  C   LYS A 481    16864  15293  15465    134  -2090   -276       C  
ATOM   3540  O   LYS A 481     -39.986 -34.682 -70.825  1.00127.57           O  
ANISOU 3540  O   LYS A 481    17152  15590  15729    252  -2159   -333       O  
ATOM   3541  CB  LYS A 481     -40.662 -31.867 -71.141  1.00123.08           C  
ANISOU 3541  CB  LYS A 481    16240  15180  15344    110  -1888   -276       C  
ATOM   3542  CG  LYS A 481     -41.888 -31.831 -72.037  1.00120.73           C  
ANISOU 3542  CG  LYS A 481    15929  14874  15068     25  -1833   -204       C  
ATOM   3543  CD  LYS A 481     -41.756 -30.736 -73.088  1.00121.57           C  
ANISOU 3543  CD  LYS A 481    15864  15070  15258     29  -1740   -204       C  
ATOM   3544  CE  LYS A 481     -42.527 -31.093 -74.351  1.00125.77           C  
ANISOU 3544  CE  LYS A 481    16400  15594  15792      6  -1728   -160       C  
ATOM   3545  NZ  LYS A 481     -42.922 -29.910 -75.167  1.00126.12           N  
ANISOU 3545  NZ  LYS A 481    16298  15704  15917    -38  -1621   -130       N  
ATOM   3546  N   GLU A 482     -41.813 -34.848 -69.509  1.00127.18           N  
ANISOU 3546  N   GLU A 482    17244  15441  15638     38  -2122   -217       N  
ATOM   3547  CA  GLU A 482     -41.917 -36.310 -69.596  1.00128.05           C  
ANISOU 3547  CA  GLU A 482    17552  15449  15652     62  -2252   -212       C  
ATOM   3548  C   GLU A 482     -42.502 -36.766 -70.931  1.00125.93           C  
ANISOU 3548  C   GLU A 482    17289  15172  15386     54  -2255   -179       C  
ATOM   3549  O   GLU A 482     -41.895 -37.568 -71.642  1.00127.72           O  
ANISOU 3549  O   GLU A 482    17576  15374  15578    162  -2349   -222       O  
ATOM   3550  CB  GLU A 482     -42.743 -36.874 -68.431  1.00131.20           C  
ANISOU 3550  CB  GLU A 482    18113  15761  15976    -55  -2287   -157       C  
ATOM   3551  CG  GLU A 482     -42.277 -36.449 -67.040  1.00136.31           C  
ANISOU 3551  CG  GLU A 482    18766  16411  16614    -58  -2284   -183       C  
ATOM   3552  CD  GLU A 482     -41.102 -37.257 -66.510  1.00137.84           C  
ANISOU 3552  CD  GLU A 482    19084  16546  16740     70  -2421   -255       C  
ATOM   3553  OE1 GLU A 482     -41.159 -37.680 -65.335  1.00137.57           O  
ANISOU 3553  OE1 GLU A 482    19185  16444  16638     30  -2477   -246       O  
ATOM   3554  OE2 GLU A 482     -40.121 -37.472 -67.256  1.00139.35           O  
ANISOU 3554  OE2 GLU A 482    19240  16763  16943    212  -2475   -324       O  
ATOM   3555  N   PHE A 483     -43.684 -36.254 -71.261  1.00122.98           N  
ANISOU 3555  N   PHE A 483    16850  14822  15051    -69  -2157   -109       N  
ATOM   3556  CA  PHE A 483     -44.322 -36.532 -72.549  1.00121.44           C  
ANISOU 3556  CA  PHE A 483    16641  14630  14870    -87  -2143    -74       C  
ATOM   3557  C   PHE A 483     -45.340 -35.453 -72.915  1.00119.20           C  
ANISOU 3557  C   PHE A 483    16211  14415  14662   -194  -2005    -20       C  
ATOM   3558  O   PHE A 483     -45.645 -34.570 -72.104  1.00119.11           O  
ANISOU 3558  O   PHE A 483    16128  14441  14685   -261  -1926     -6       O  
ATOM   3559  CB  PHE A 483     -44.967 -37.924 -72.563  1.00121.00           C  
ANISOU 3559  CB  PHE A 483    16791  14463  14718   -133  -2250    -36       C  
ATOM   3560  CG  PHE A 483     -45.941 -38.159 -71.446  1.00120.02           C  
ANISOU 3560  CG  PHE A 483    16774  14288  14541   -282  -2245     24       C  
ATOM   3561  CD1 PHE A 483     -45.501 -38.610 -70.205  1.00119.46           C  
ANISOU 3561  CD1 PHE A 483    16829  14156  14402   -279  -2319      7       C  
ATOM   3562  CD2 PHE A 483     -47.302 -37.943 -71.638  1.00118.52           C  
ANISOU 3562  CD2 PHE A 483    16555  14116  14360   -428  -2167     97       C  
ATOM   3563  CE1 PHE A 483     -46.398 -38.836 -69.174  1.00119.17           C  
ANISOU 3563  CE1 PHE A 483    16891  14079  14306   -425  -2313     64       C  
ATOM   3564  CE2 PHE A 483     -48.202 -38.165 -70.609  1.00119.53           C  
ANISOU 3564  CE2 PHE A 483    16771  14214  14429   -572  -2158    149       C  
ATOM   3565  CZ  PHE A 483     -47.751 -38.615 -69.376  1.00118.93           C  
ANISOU 3565  CZ  PHE A 483    16824  14080  14283   -575  -2230    135       C  
ATOM   3566  N   THR A 484     -45.862 -35.536 -74.136  1.00114.94           N  
ANISOU 3566  N   THR A 484    15633  13890  14146   -202  -1981      6       N  
ATOM   3567  CA  THR A 484     -46.760 -34.520 -74.660  1.00112.10           C  
ANISOU 3567  CA  THR A 484    15134  13598  13860   -282  -1860     49       C  
ATOM   3568  C   THR A 484     -48.049 -35.142 -75.167  1.00111.46           C  
ANISOU 3568  C   THR A 484    15124  13480  13746   -380  -1864    112       C  
ATOM   3569  O   THR A 484     -48.024 -36.030 -76.019  1.00114.18           O  
ANISOU 3569  O   THR A 484    15544  13783  14056   -340  -1933    113       O  
ATOM   3570  CB  THR A 484     -46.099 -33.742 -75.814  1.00111.66           C  
ANISOU 3570  CB  THR A 484    14925  13619  13879   -195  -1809     17       C  
ATOM   3571  OG1 THR A 484     -44.750 -33.407 -75.462  1.00110.72           O  
ANISOU 3571  OG1 THR A 484    14758  13536  13775    -93  -1828    -50       O  
ATOM   3572  CG2 THR A 484     -46.881 -32.472 -76.136  1.00110.86           C  
ANISOU 3572  CG2 THR A 484    14676  13585  13858   -269  -1684     54       C  
ATOM   3573  N   LEU A 485     -49.175 -34.680 -74.637  1.00110.47           N  
ANISOU 3573  N   LEU A 485    14969  13375  13627   -507  -1791    159       N  
ATOM   3574  CA  LEU A 485     -50.468 -35.082 -75.169  1.00112.26           C  
ANISOU 3574  CA  LEU A 485    15228  13592  13833   -609  -1777    216       C  
ATOM   3575  C   LEU A 485     -50.798 -34.103 -76.284  1.00113.57           C  
ANISOU 3575  C   LEU A 485    15232  13833  14087   -593  -1685    222       C  
ATOM   3576  O   LEU A 485     -51.147 -32.952 -76.014  1.00114.88           O  
ANISOU 3576  O   LEU A 485    15272  14064  14312   -628  -1591    225       O  
ATOM   3577  CB  LEU A 485     -51.552 -35.083 -74.081  1.00109.54           C  
ANISOU 3577  CB  LEU A 485    14925  13251  13444   -756  -1744    258       C  
ATOM   3578  CG  LEU A 485     -51.305 -35.835 -72.764  1.00108.92           C  
ANISOU 3578  CG  LEU A 485    14998  13108  13277   -795  -1819    258       C  
ATOM   3579  CD1 LEU A 485     -52.589 -35.894 -71.952  1.00108.84           C  
ANISOU 3579  CD1 LEU A 485    15019  13119  13215   -961  -1779    307       C  
ATOM   3580  CD2 LEU A 485     -50.750 -37.237 -72.971  1.00107.98           C  
ANISOU 3580  CD2 LEU A 485    15065  12883  13079   -743  -1957    251       C  
ATOM   3581  N   GLU A 486     -50.659 -34.558 -77.532  1.00114.03           N  
ANISOU 3581  N   GLU A 486    15297  13878  14150   -534  -1718    221       N  
ATOM   3582  CA  GLU A 486     -50.740 -33.664 -78.690  1.00112.29           C  
ANISOU 3582  CA  GLU A 486    14930  13723  14009   -498  -1642    221       C  
ATOM   3583  C   GLU A 486     -52.158 -33.164 -78.957  1.00108.20           C  
ANISOU 3583  C   GLU A 486    14349  13242  13518   -606  -1565    268       C  
ATOM   3584  O   GLU A 486     -53.132 -33.780 -78.527  1.00106.62           O  
ANISOU 3584  O   GLU A 486    14230  13016  13263   -707  -1582    304       O  
ATOM   3585  CB  GLU A 486     -50.100 -34.289 -79.946  1.00119.05           C  
ANISOU 3585  CB  GLU A 486    15809  14563  14859   -397  -1701    200       C  
ATOM   3586  CG  GLU A 486     -51.039 -35.057 -80.876  1.00130.15           C  
ANISOU 3586  CG  GLU A 486    17275  15937  16236   -440  -1729    240       C  
ATOM   3587  CD  GLU A 486     -50.778 -36.558 -80.929  1.00138.60           C  
ANISOU 3587  CD  GLU A 486    18523  16917  17219   -407  -1857    233       C  
ATOM   3588  OE1 GLU A 486     -49.742 -37.022 -80.394  1.00141.90           O  
ANISOU 3588  OE1 GLU A 486    19013  17302  17601   -328  -1932    189       O  
ATOM   3589  OE2 GLU A 486     -51.616 -37.277 -81.526  1.00139.34           O  
ANISOU 3589  OE2 GLU A 486    18688  16974  17280   -459  -1889    270       O  
ATOM   3590  N   PHE A 487     -52.249 -32.036 -79.655  1.00106.18           N  
ANISOU 3590  N   PHE A 487    13950  13050  13341   -583  -1484    266       N  
ATOM   3591  CA  PHE A 487     -53.518 -31.408 -80.006  1.00105.43           C  
ANISOU 3591  CA  PHE A 487    13779  13000  13280   -662  -1411    299       C  
ATOM   3592  C   PHE A 487     -54.435 -32.343 -80.800  1.00106.20           C  
ANISOU 3592  C   PHE A 487    13944  13069  13335   -710  -1445    335       C  
ATOM   3593  O   PHE A 487     -53.977 -33.094 -81.657  1.00105.83           O  
ANISOU 3593  O   PHE A 487    13954  12985  13270   -649  -1505    331       O  
ATOM   3594  CB  PHE A 487     -53.240 -30.133 -80.807  1.00105.69           C  
ANISOU 3594  CB  PHE A 487    13668  13089  13401   -606  -1340    287       C  
ATOM   3595  CG  PHE A 487     -54.473 -29.382 -81.221  1.00106.08           C  
ANISOU 3595  CG  PHE A 487    13632  13183  13488   -667  -1271    312       C  
ATOM   3596  CD1 PHE A 487     -55.141 -29.702 -82.400  1.00106.95           C  
ANISOU 3596  CD1 PHE A 487    13740  13294  13600   -674  -1273    337       C  
ATOM   3597  CD2 PHE A 487     -54.955 -28.337 -80.446  1.00107.54           C  
ANISOU 3597  CD2 PHE A 487    13740  13412  13707   -709  -1208    305       C  
ATOM   3598  CE1 PHE A 487     -56.277 -29.009 -82.787  1.00107.29           C  
ANISOU 3598  CE1 PHE A 487    13706  13381  13677   -721  -1215    353       C  
ATOM   3599  CE2 PHE A 487     -56.087 -27.636 -80.828  1.00108.52           C  
ANISOU 3599  CE2 PHE A 487    13786  13581  13863   -751  -1152    318       C  
ATOM   3600  CZ  PHE A 487     -56.751 -27.974 -81.999  1.00108.47           C  
ANISOU 3600  CZ  PHE A 487    13778  13577  13858   -757  -1156    342       C  
ATOM   3601  N   SER A 488     -55.729 -32.285 -80.497  1.00109.35           N  
ANISOU 3601  N   SER A 488    14334  13495  13718   -820  -1409    365       N  
ATOM   3602  CA  SER A 488     -56.763 -32.994 -81.253  1.00111.05           C  
ANISOU 3602  CA  SER A 488    14591  13701  13900   -882  -1427    399       C  
ATOM   3603  C   SER A 488     -57.980 -32.090 -81.437  1.00112.92           C  
ANISOU 3603  C   SER A 488    14709  14015  14177   -947  -1342    411       C  
ATOM   3604  O   SER A 488     -58.412 -31.429 -80.487  1.00115.06           O  
ANISOU 3604  O   SER A 488    14927  14335  14453  -1000  -1291    403       O  
ATOM   3605  CB  SER A 488     -57.178 -34.263 -80.517  1.00112.00           C  
ANISOU 3605  CB  SER A 488    14865  13767  13923   -974  -1498    423       C  
ATOM   3606  OG  SER A 488     -57.752 -33.946 -79.259  1.00111.77           O  
ANISOU 3606  OG  SER A 488    14824  13775  13866  -1071  -1459    428       O  
ATOM   3607  N   ARG A 489     -58.538 -32.073 -82.646  1.00113.44           N  
ANISOU 3607  N   ARG A 489    14737  14096  14267   -937  -1330    425       N  
ATOM   3608  CA  ARG A 489     -59.654 -31.176 -82.982  1.00114.65           C  
ANISOU 3608  CA  ARG A 489    14774  14324  14463   -977  -1256    429       C  
ATOM   3609  C   ARG A 489     -60.868 -31.276 -82.054  1.00113.86           C  
ANISOU 3609  C   ARG A 489    14671  14276  14313  -1104  -1230    437       C  
ATOM   3610  O   ARG A 489     -61.599 -30.300 -81.893  1.00114.54           O  
ANISOU 3610  O   ARG A 489    14646  14438  14434  -1124  -1165    421       O  
ATOM   3611  CB  ARG A 489     -60.111 -31.380 -84.429  1.00119.86           C  
ANISOU 3611  CB  ARG A 489    15417  14982  15141   -954  -1263    445       C  
ATOM   3612  CG  ARG A 489     -59.126 -30.892 -85.480  1.00128.60           C  
ANISOU 3612  CG  ARG A 489    16480  16073  16309   -834  -1261    433       C  
ATOM   3613  CD  ARG A 489     -59.789 -30.725 -86.843  1.00133.05           C  
ANISOU 3613  CD  ARG A 489    16994  16656  16902   -818  -1245    448       C  
ATOM   3614  NE  ARG A 489     -60.678 -31.839 -87.175  1.00138.40           N  
ANISOU 3614  NE  ARG A 489    17748  17315  17521   -888  -1288    473       N  
ATOM   3615  CZ  ARG A 489     -60.288 -32.985 -87.728  1.00144.13           C  
ANISOU 3615  CZ  ARG A 489    18579  17979  18203   -865  -1362    485       C  
ATOM   3616  NH1 ARG A 489     -59.010 -33.194 -88.027  1.00145.38           N  
ANISOU 3616  NH1 ARG A 489    18772  18097  18368   -766  -1401    469       N  
ATOM   3617  NH2 ARG A 489     -61.184 -33.929 -87.984  1.00149.78           N  
ANISOU 3617  NH2 ARG A 489    19365  18678  18865   -941  -1400    510       N  
ATOM   3618  N   ASP A 490     -61.081 -32.445 -81.452  1.00113.29           N  
ANISOU 3618  N   ASP A 490    14722  14167  14155  -1189  -1285    459       N  
ATOM   3619  CA  ASP A 490     -62.251 -32.672 -80.599  1.00112.45           C  
ANISOU 3619  CA  ASP A 490    14620  14120  13985  -1328  -1263    469       C  
ATOM   3620  C   ASP A 490     -62.204 -31.887 -79.285  1.00109.75           C  
ANISOU 3620  C   ASP A 490    14221  13832  13645  -1352  -1215    444       C  
ATOM   3621  O   ASP A 490     -63.168 -31.208 -78.935  1.00110.46           O  
ANISOU 3621  O   ASP A 490    14211  14017  13740  -1407  -1153    428       O  
ATOM   3622  CB  ASP A 490     -62.491 -34.173 -80.346  1.00115.64           C  
ANISOU 3622  CB  ASP A 490    15186  14463  14286  -1428  -1342    506       C  
ATOM   3623  CG  ASP A 490     -61.342 -34.844 -79.596  1.00116.93           C  
ANISOU 3623  CG  ASP A 490    15483  14535  14408  -1396  -1413    507       C  
ATOM   3624  OD1 ASP A 490     -60.345 -35.230 -80.248  1.00114.18           O  
ANISOU 3624  OD1 ASP A 490    15193  14109  14079  -1290  -1471    502       O  
ATOM   3625  OD2 ASP A 490     -61.450 -35.001 -78.357  1.00116.78           O  
ANISOU 3625  OD2 ASP A 490    15510  14527  14332  -1477  -1414    510       O  
ATOM   3626  N   ARG A 491     -61.086 -31.967 -78.570  1.00106.65           N  
ANISOU 3626  N   ARG A 491    13888  13384  13249  -1303  -1245    434       N  
ATOM   3627  CA  ARG A 491     -60.946 -31.252 -77.305  1.00106.45           C  
ANISOU 3627  CA  ARG A 491    13817  13402  13226  -1318  -1204    408       C  
ATOM   3628  C   ARG A 491     -60.429 -29.830 -77.505  1.00108.21           C  
ANISOU 3628  C   ARG A 491    13908  13656  13548  -1211  -1148    372       C  
ATOM   3629  O   ARG A 491     -60.657 -28.956 -76.658  1.00111.26           O  
ANISOU 3629  O   ARG A 491    14218  14103  13951  -1223  -1097    345       O  
ATOM   3630  CB  ARG A 491     -60.056 -32.030 -76.326  1.00104.87           C  
ANISOU 3630  CB  ARG A 491    13750  13129  12965  -1327  -1267    414       C  
ATOM   3631  CG  ARG A 491     -58.577 -32.111 -76.679  1.00101.22           C  
ANISOU 3631  CG  ARG A 491    13331  12586  12543  -1196  -1316    398       C  
ATOM   3632  CD  ARG A 491     -57.944 -33.272 -75.934  1.00 99.98           C  
ANISOU 3632  CD  ARG A 491    13339  12344  12302  -1217  -1404    409       C  
ATOM   3633  NE  ARG A 491     -56.539 -33.066 -75.589  1.00 97.27           N  
ANISOU 3633  NE  ARG A 491    13012  11956  11987  -1105  -1434    376       N  
ATOM   3634  CZ  ARG A 491     -55.512 -33.416 -76.356  1.00 96.25           C  
ANISOU 3634  CZ  ARG A 491    12920  11770  11879   -993  -1488    361       C  
ATOM   3635  NH1 ARG A 491     -55.717 -33.966 -77.543  1.00 95.50           N  
ANISOU 3635  NH1 ARG A 491    12850  11650  11784   -973  -1519    378       N  
ATOM   3636  NH2 ARG A 491     -54.272 -33.201 -75.940  1.00 95.90           N  
ANISOU 3636  NH2 ARG A 491    12881  11703  11855   -899  -1512    324       N  
ATOM   3637  N   LYS A 492     -59.754 -29.611 -78.637  1.00105.51           N  
ANISOU 3637  N   LYS A 492    13545  13275  13268  -1110  -1159    371       N  
ATOM   3638  CA  LYS A 492     -59.080 -28.348 -78.950  1.00100.77           C  
ANISOU 3638  CA  LYS A 492    12842  12688  12758  -1010  -1117    343       C  
ATOM   3639  C   LYS A 492     -58.171 -27.893 -77.807  1.00 98.46           C  
ANISOU 3639  C   LYS A 492    12550  12385  12473   -980  -1114    317       C  
ATOM   3640  O   LYS A 492     -58.429 -26.889 -77.139  1.00 98.99           O  
ANISOU 3640  O   LYS A 492    12536  12504  12570   -985  -1064    292       O  
ATOM   3641  CB  LYS A 492     -60.081 -27.266 -79.376  1.00101.16           C  
ANISOU 3641  CB  LYS A 492    12767  12812  12858  -1015  -1053    330       C  
ATOM   3642  CG  LYS A 492     -60.394 -27.305 -80.862  1.00104.65           C  
ANISOU 3642  CG  LYS A 492    13183  13246  13331   -980  -1056    347       C  
ATOM   3643  CD  LYS A 492     -61.744 -26.680 -81.178  1.00110.10           C  
ANISOU 3643  CD  LYS A 492    13782  14013  14036  -1016  -1010    338       C  
ATOM   3644  CE  LYS A 492     -62.042 -26.700 -82.676  1.00113.28           C  
ANISOU 3644  CE  LYS A 492    14164  14406  14472   -978  -1015    355       C  
ATOM   3645  NZ  LYS A 492     -62.470 -28.032 -83.202  1.00112.58           N  
ANISOU 3645  NZ  LYS A 492    14159  14292  14323  -1033  -1059    387       N  
ATOM   3646  N   SER A 493     -57.116 -28.672 -77.588  1.00 96.18           N  
ANISOU 3646  N   SER A 493    12358  12031  12155   -945  -1174    318       N  
ATOM   3647  CA  SER A 493     -56.104 -28.382 -76.578  1.00 96.21           C  
ANISOU 3647  CA  SER A 493    12375  12018  12163   -907  -1183    291       C  
ATOM   3648  C   SER A 493     -54.998 -29.429 -76.599  1.00 96.06           C  
ANISOU 3648  C   SER A 493    12471  11923  12103   -857  -1263    289       C  
ATOM   3649  O   SER A 493     -55.175 -30.526 -77.115  1.00 97.19           O  
ANISOU 3649  O   SER A 493    12708  12023  12196   -873  -1319    312       O  
ATOM   3650  CB  SER A 493     -56.723 -28.319 -75.182  1.00 96.48           C  
ANISOU 3650  CB  SER A 493    12421  12087  12150   -994  -1162    286       C  
ATOM   3651  OG  SER A 493     -57.417 -29.512 -74.893  1.00 99.42           O  
ANISOU 3651  OG  SER A 493    12899  12443  12432  -1090  -1202    317       O  
ATOM   3652  N   MET A 494     -53.852 -29.066 -76.044  1.00 97.40           N  
ANISOU 3652  N   MET A 494    12633  12079  12293   -790  -1274    257       N  
ATOM   3653  CA  MET A 494     -52.743 -29.984 -75.873  1.00100.74           C  
ANISOU 3653  CA  MET A 494    13161  12441  12674   -731  -1354    242       C  
ATOM   3654  C   MET A 494     -52.220 -29.820 -74.454  1.00102.71           C  
ANISOU 3654  C   MET A 494    13437  12684  12901   -737  -1363    217       C  
ATOM   3655  O   MET A 494     -52.478 -28.802 -73.807  1.00105.26           O  
ANISOU 3655  O   MET A 494    13675  13055  13261   -762  -1300    206       O  
ATOM   3656  CB  MET A 494     -51.631 -29.690 -76.882  1.00103.90           C  
ANISOU 3656  CB  MET A 494    13508  12842  13126   -617  -1364    216       C  
ATOM   3657  CG  MET A 494     -50.952 -28.338 -76.688  1.00108.42           C  
ANISOU 3657  CG  MET A 494    13959  13461  13773   -571  -1305    185       C  
ATOM   3658  SD  MET A 494     -49.166 -28.349 -76.952  1.00113.03           S  
ANISOU 3658  SD  MET A 494    14530  14042  14371   -450  -1347    135       S  
ATOM   3659  CE  MET A 494     -48.624 -29.356 -75.574  1.00113.74           C  
ANISOU 3659  CE  MET A 494    14754  14078  14382   -445  -1428    111       C  
ATOM   3660  N   SER A 495     -51.494 -30.818 -73.965  1.00102.97           N  
ANISOU 3660  N   SER A 495    13595  12657  12872   -710  -1446    206       N  
ATOM   3661  CA  SER A 495     -50.889 -30.725 -72.642  1.00101.58           C  
ANISOU 3661  CA  SER A 495    13453  12469  12672   -705  -1463    180       C  
ATOM   3662  C   SER A 495     -49.540 -31.422 -72.585  1.00101.28           C  
ANISOU 3662  C   SER A 495    13498  12377  12606   -603  -1551    142       C  
ATOM   3663  O   SER A 495     -49.178 -32.180 -73.490  1.00101.71           O  
ANISOU 3663  O   SER A 495    13605  12397  12643   -546  -1610    139       O  
ATOM   3664  CB  SER A 495     -51.832 -31.258 -71.558  1.00101.14           C  
ANISOU 3664  CB  SER A 495    13487  12402  12538   -825  -1472    210       C  
ATOM   3665  OG  SER A 495     -52.157 -32.613 -71.774  1.00103.40           O  
ANISOU 3665  OG  SER A 495    13922  12623  12742   -868  -1551    241       O  
ATOM   3666  N   VAL A 496     -48.794 -31.133 -71.524  1.00100.48           N  
ANISOU 3666  N   VAL A 496    13402  12275  12501   -574  -1562    108       N  
ATOM   3667  CA  VAL A 496     -47.506 -31.762 -71.284  1.00104.43           C  
ANISOU 3667  CA  VAL A 496    13977  12731  12967   -474  -1649     62       C  
ATOM   3668  C   VAL A 496     -47.431 -32.250 -69.840  1.00109.14           C  
ANISOU 3668  C   VAL A 496    14690  13283  13494   -512  -1698     59       C  
ATOM   3669  O   VAL A 496     -47.863 -31.555 -68.918  1.00111.45           O  
ANISOU 3669  O   VAL A 496    14937  13608  13797   -578  -1639     66       O  
ATOM   3670  CB  VAL A 496     -46.328 -30.810 -71.587  1.00103.41           C  
ANISOU 3670  CB  VAL A 496    13720  12657  12914   -371  -1618      9       C  
ATOM   3671  CG1 VAL A 496     -46.049 -30.753 -73.079  1.00102.93           C  
ANISOU 3671  CG1 VAL A 496    13591  12624  12892   -309  -1610      3       C  
ATOM   3672  CG2 VAL A 496     -46.604 -29.414 -71.051  1.00106.23           C  
ANISOU 3672  CG2 VAL A 496    13949  13075  13339   -415  -1520      9       C  
ATOM   3673  N   TYR A 497     -46.901 -33.455 -69.656  1.00110.72           N  
ANISOU 3673  N   TYR A 497    15045  13406  13617   -469  -1811     46       N  
ATOM   3674  CA  TYR A 497     -46.704 -34.014 -68.330  1.00113.41           C  
ANISOU 3674  CA  TYR A 497    15516  13693  13882   -495  -1874     40       C  
ATOM   3675  C   TYR A 497     -45.293 -33.672 -67.884  1.00116.42           C  
ANISOU 3675  C   TYR A 497    15862  14085  14286   -372  -1905    -30       C  
ATOM   3676  O   TYR A 497     -44.349 -33.798 -68.665  1.00118.01           O  
ANISOU 3676  O   TYR A 497    16032  14294  14510   -255  -1943    -77       O  
ATOM   3677  CB  TYR A 497     -46.892 -35.524 -68.376  1.00116.38           C  
ANISOU 3677  CB  TYR A 497    16095  13968  14154   -514  -1992     63       C  
ATOM   3678  CG  TYR A 497     -47.039 -36.190 -67.027  1.00119.93           C  
ANISOU 3678  CG  TYR A 497    16706  14352  14508   -583  -2056     79       C  
ATOM   3679  CD1 TYR A 497     -48.293 -36.346 -66.440  1.00120.01           C  
ANISOU 3679  CD1 TYR A 497    16768  14364  14467   -746  -2020    142       C  
ATOM   3680  CD2 TYR A 497     -45.927 -36.685 -66.345  1.00122.02           C  
ANISOU 3680  CD2 TYR A 497    17073  14560  14729   -488  -2155     29       C  
ATOM   3681  CE1 TYR A 497     -48.436 -36.961 -65.206  1.00121.63           C  
ANISOU 3681  CE1 TYR A 497    17125  14513  14575   -822  -2078    161       C  
ATOM   3682  CE2 TYR A 497     -46.058 -37.302 -65.109  1.00122.79           C  
ANISOU 3682  CE2 TYR A 497    17328  14591  14733   -554  -2218     46       C  
ATOM   3683  CZ  TYR A 497     -47.314 -37.438 -64.543  1.00122.95           C  
ANISOU 3683  CZ  TYR A 497    17402  14613  14701   -725  -2178    115       C  
ATOM   3684  OH  TYR A 497     -47.449 -38.050 -63.317  1.00124.96           O  
ANISOU 3684  OH  TYR A 497    17816  14805  14854   -801  -2239    135       O  
ATOM   3685  N   CYS A 498     -45.149 -33.239 -66.634  1.00119.94           N  
ANISOU 3685  N   CYS A 498    16308  14538  14723   -400  -1887    -42       N  
ATOM   3686  CA  CYS A 498     -43.846 -32.827 -66.115  1.00124.22           C  
ANISOU 3686  CA  CYS A 498    16808  15098  15289   -292  -1910   -112       C  
ATOM   3687  C   CYS A 498     -43.573 -33.274 -64.688  1.00128.60           C  
ANISOU 3687  C   CYS A 498    17488  15601  15772   -305  -1974   -125       C  
ATOM   3688  O   CYS A 498     -44.478 -33.322 -63.856  1.00131.34           O  
ANISOU 3688  O   CYS A 498    17891  15935  16077   -422  -1949    -79       O  
ATOM   3689  CB  CYS A 498     -43.695 -31.310 -66.193  1.00126.15           C  
ANISOU 3689  CB  CYS A 498    16856  15436  15637   -288  -1797   -129       C  
ATOM   3690  SG  CYS A 498     -43.301 -30.688 -67.839  1.00131.32           S  
ANISOU 3690  SG  CYS A 498    17357  16157  16380   -218  -1747   -145       S  
ATOM   3691  N   SER A 499     -42.309 -33.593 -64.425  1.00132.70           N  
ANISOU 3691  N   SER A 499    18046  16098  16273   -182  -2056   -192       N  
ATOM   3692  CA  SER A 499     -41.816 -33.874 -63.080  1.00136.25           C  
ANISOU 3692  CA  SER A 499    18598  16505  16664   -168  -2118   -219       C  
ATOM   3693  C   SER A 499     -40.748 -32.838 -62.736  1.00138.22           C  
ANISOU 3693  C   SER A 499    18705  16826  16984    -81  -2079   -287       C  
ATOM   3694  O   SER A 499     -39.937 -32.495 -63.597  1.00142.49           O  
ANISOU 3694  O   SER A 499    19137  17420  17580     14  -2072   -335       O  
ATOM   3695  CB  SER A 499     -41.221 -35.281 -63.012  1.00136.62           C  
ANISOU 3695  CB  SER A 499    18840  16453  16614    -90  -2273   -246       C  
ATOM   3696  OG  SER A 499     -40.237 -35.473 -64.015  1.00134.20           O  
ANISOU 3696  OG  SER A 499    18485  16169  16335     52  -2321   -309       O  
ATOM   3697  N   PRO A 500     -40.735 -32.340 -61.483  1.00138.85           N  
ANISOU 3697  N   PRO A 500    18784  16913  17058   -120  -2054   -293       N  
ATOM   3698  CA  PRO A 500     -39.738 -31.339 -61.077  1.00142.05           C  
ANISOU 3698  CA  PRO A 500    19059  17384  17528    -46  -2020   -357       C  
ATOM   3699  C   PRO A 500     -38.298 -31.831 -61.243  1.00143.75           C  
ANISOU 3699  C   PRO A 500    19297  17594  17725    106  -2119   -442       C  
ATOM   3700  O   PRO A 500     -37.973 -32.941 -60.822  1.00142.98           O  
ANISOU 3700  O   PRO A 500    19365  17418  17540    154  -2236   -461       O  
ATOM   3701  CB  PRO A 500     -40.060 -31.099 -59.597  1.00141.31           C  
ANISOU 3701  CB  PRO A 500    19018  17273  17400   -115  -2007   -345       C  
ATOM   3702  CG  PRO A 500     -40.818 -32.308 -59.171  1.00141.39           C  
ANISOU 3702  CG  PRO A 500    19226  17193  17301   -190  -2079   -293       C  
ATOM   3703  CD  PRO A 500     -41.630 -32.693 -60.370  1.00138.69           C  
ANISOU 3703  CD  PRO A 500    18884  16845  16964   -238  -2059   -241       C  
ATOM   3704  N   ALA A 501     -37.459 -31.004 -61.864  1.00148.14           N  
ANISOU 3704  N   ALA A 501    19689  18236  18359    179  -2075   -494       N  
ATOM   3705  CA  ALA A 501     -36.075 -31.361 -62.169  1.00157.30           C  
ANISOU 3705  CA  ALA A 501    20835  19423  19507    327  -2156   -585       C  
ATOM   3706  C   ALA A 501     -35.282 -31.623 -60.899  1.00169.76           C  
ANISOU 3706  C   ALA A 501    22493  20972  21036    389  -2235   -642       C  
ATOM   3707  O   ALA A 501     -35.432 -30.901 -59.908  1.00170.47           O  
ANISOU 3707  O   ALA A 501    22550  21071  21147    333  -2184   -633       O  
ATOM   3708  CB  ALA A 501     -35.411 -30.269 -62.993  1.00155.46           C  
ANISOU 3708  CB  ALA A 501    20396  19304  19365    363  -2076   -623       C  
ATOM   3709  N   LYS A 502     -34.442 -32.660 -60.946  1.00185.02           N  
ANISOU 3709  N   LYS A 502    24531  22867  22899    511  -2364   -706       N  
ATOM   3710  CA  LYS A 502     -33.657 -33.128 -59.795  1.00191.83           C  
ANISOU 3710  CA  LYS A 502    25499  23686  23698    589  -2466   -767       C  
ATOM   3711  C   LYS A 502     -34.507 -33.151 -58.517  1.00196.38           C  
ANISOU 3711  C   LYS A 502    26191  24187  24235    474  -2454   -704       C  
ATOM   3712  O   LYS A 502     -35.336 -34.059 -58.330  1.00197.71           O  
ANISOU 3712  O   LYS A 502    26532  24260  24329    408  -2505   -643       O  
ATOM   3713  CB  LYS A 502     -32.381 -32.291 -59.606  1.00191.43           C  
ANISOU 3713  CB  LYS A 502    25291  23740  23701    683  -2447   -862       C  
ATOM   3714  CG  LYS A 502     -31.548 -32.093 -60.869  1.00190.38           C  
ANISOU 3714  CG  LYS A 502    25014  23711  23610    777  -2438   -925       C  
ATOM   3715  CD  LYS A 502     -30.327 -31.213 -60.621  1.00190.14           C  
ANISOU 3715  CD  LYS A 502    24823  23794  23627    848  -2414  -1015       C  
ATOM   3716  CE  LYS A 502     -30.695 -29.788 -60.221  1.00189.27           C  
ANISOU 3716  CE  LYS A 502    24576  23733  23604    733  -2279   -971       C  
ATOM   3717  NZ  LYS A 502     -31.433 -29.049 -61.284  1.00190.01           N  
ANISOU 3717  NZ  LYS A 502    24553  23871  23771    639  -2163   -903       N  
ATOM   3718  N   SER A 503     -34.310 -32.148 -57.655  1.00198.51           N  
ANISOU 3718  N   SER A 503    26366  24506  24551    445  -2386   -718       N  
ATOM   3719  CA  SER A 503     -35.089 -32.019 -56.422  1.00197.25           C  
ANISOU 3719  CA  SER A 503    26291  24297  24358    336  -2361   -664       C  
ATOM   3720  C   SER A 503     -35.381 -30.561 -56.055  1.00193.25           C  
ANISOU 3720  C   SER A 503    25613  23870  23940    261  -2227   -648       C  
ATOM   3721  O   SER A 503     -34.776 -29.631 -56.597  1.00192.45           O  
ANISOU 3721  O   SER A 503    25339  23856  23925    303  -2167   -689       O  
ATOM   3722  CB  SER A 503     -34.384 -32.731 -55.265  1.00196.94           C  
ANISOU 3722  CB  SER A 503    26403  24190  24232    407  -2483   -714       C  
ATOM   3723  OG  SER A 503     -35.288 -33.001 -54.209  1.00196.05           O  
ANISOU 3723  OG  SER A 503    26425  24008  24054    291  -2483   -648       O  
ATOM   3724  N   ALA A 507     -40.661 -32.291 -52.106  1.00191.64           N  
ANISOU 3724  N   ALA A 507    25977  23454  23381   -369  -2181   -316       N  
ATOM   3725  CA  ALA A 507     -40.827 -32.840 -53.448  1.00188.14           C  
ANISOU 3725  CA  ALA A 507    25541  22989  22952   -350  -2201   -295       C  
ATOM   3726  C   ALA A 507     -42.207 -32.517 -54.018  1.00187.13           C  
ANISOU 3726  C   ALA A 507    25340  22912  22846   -485  -2097   -223       C  
ATOM   3727  O   ALA A 507     -43.156 -33.292 -53.853  1.00188.60           O  
ANISOU 3727  O   ALA A 507    25653  23059  22945   -604  -2116   -159       O  
ATOM   3728  CB  ALA A 507     -40.578 -34.345 -53.446  1.00185.83           C  
ANISOU 3728  CB  ALA A 507    25479  22579  22549   -324  -2348   -286       C  
ATOM   3729  N   VAL A 508     -42.305 -31.364 -54.681  1.00186.69           N  
ANISOU 3729  N   VAL A 508    25082  22945  22904   -468  -1990   -237       N  
ATOM   3730  CA  VAL A 508     -43.541 -30.940 -55.352  1.00183.84           C  
ANISOU 3730  CA  VAL A 508    24630  22641  22578   -573  -1891   -181       C  
ATOM   3731  C   VAL A 508     -43.947 -31.949 -56.431  1.00183.85           C  
ANISOU 3731  C   VAL A 508    24718  22590  22543   -593  -1939   -140       C  
ATOM   3732  O   VAL A 508     -43.181 -32.224 -57.355  1.00187.82           O  
ANISOU 3732  O   VAL A 508    25212  23070  23081   -487  -1987   -171       O  
ATOM   3733  CB  VAL A 508     -43.438 -29.507 -55.942  1.00178.72           C  
ANISOU 3733  CB  VAL A 508    23760  22083  22059   -533  -1785   -209       C  
ATOM   3734  CG1 VAL A 508     -43.699 -28.466 -54.864  1.00175.71           C  
ANISOU 3734  CG1 VAL A 508    23295  21763  21701   -574  -1713   -223       C  
ATOM   3735  CG2 VAL A 508     -42.087 -29.268 -56.612  1.00173.88           C  
ANISOU 3735  CG2 VAL A 508    23079  21470  21515   -388  -1819   -272       C  
ATOM   3736  N   GLY A 509     -45.147 -32.509 -56.292  1.00177.11           N  
ANISOU 3736  N   GLY A 509    23950  21726  21616   -732  -1928    -73       N  
ATOM   3737  CA  GLY A 509     -45.624 -33.576 -57.177  1.00164.38           C  
ANISOU 3737  CA  GLY A 509    22447  20056  19953   -770  -1983    -28       C  
ATOM   3738  C   GLY A 509     -45.677 -33.205 -58.647  1.00154.76           C  
ANISOU 3738  C   GLY A 509    21100  18874  18827   -719  -1937    -30       C  
ATOM   3739  O   GLY A 509     -45.616 -32.026 -59.002  1.00155.62           O  
ANISOU 3739  O   GLY A 509    21025  19063  19037   -685  -1843    -54       O  
ATOM   3740  N   ASN A 510     -45.791 -34.222 -59.499  1.00147.76           N  
ANISOU 3740  N   ASN A 510    20319  17923  17899   -714  -2008     -5       N  
ATOM   3741  CA  ASN A 510     -45.894 -34.040 -60.950  1.00137.86           C  
ANISOU 3741  CA  ASN A 510    18965  16696  16718   -671  -1974     -3       C  
ATOM   3742  C   ASN A 510     -47.092 -33.191 -61.363  1.00131.22           C  
ANISOU 3742  C   ASN A 510    17981  15944  15932   -773  -1848     37       C  
ATOM   3743  O   ASN A 510     -48.090 -33.113 -60.644  1.00130.48           O  
ANISOU 3743  O   ASN A 510    17903  15881  15792   -901  -1804     75       O  
ATOM   3744  CB  ASN A 510     -45.939 -35.395 -61.661  1.00138.24           C  
ANISOU 3744  CB  ASN A 510    19177  16652  16695   -663  -2082     20       C  
ATOM   3745  CG  ASN A 510     -44.644 -36.170 -61.526  1.00138.70           C  
ANISOU 3745  CG  ASN A 510    19357  16628  16713   -525  -2214    -35       C  
ATOM   3746  OD1 ASN A 510     -43.718 -35.747 -60.832  1.00141.77           O  
ANISOU 3746  OD1 ASN A 510    19714  17030  17120   -443  -2227    -91       O  
ATOM   3747  ND2 ASN A 510     -44.572 -37.314 -62.191  1.00138.94           N  
ANISOU 3747  ND2 ASN A 510    19529  16576  16685   -495  -2319    -26       N  
ATOM   3748  N   LYS A 511     -46.981 -32.548 -62.521  1.00123.78           N  
ANISOU 3748  N   LYS A 511    16897  15048  15083   -713  -1794     23       N  
ATOM   3749  CA  LYS A 511     -48.011 -31.627 -62.987  1.00119.10           C  
ANISOU 3749  CA  LYS A 511    16158  14540  14553   -784  -1680     51       C  
ATOM   3750  C   LYS A 511     -48.247 -31.761 -64.486  1.00115.55           C  
ANISOU 3750  C   LYS A 511    15662  14093  14147   -759  -1670     67       C  
ATOM   3751  O   LYS A 511     -47.366 -32.194 -65.235  1.00114.14           O  
ANISOU 3751  O   LYS A 511    15510  13876  13982   -655  -1731     42       O  
ATOM   3752  CB  LYS A 511     -47.632 -30.173 -62.654  1.00119.25           C  
ANISOU 3752  CB  LYS A 511    16010  14633  14665   -738  -1596      9       C  
ATOM   3753  CG  LYS A 511     -47.320 -29.879 -61.190  1.00119.34           C  
ANISOU 3753  CG  LYS A 511    16046  14649  14645   -750  -1599    -15       C  
ATOM   3754  CD  LYS A 511     -48.569 -29.838 -60.321  1.00120.14           C  
ANISOU 3754  CD  LYS A 511    16168  14792  14688   -889  -1552     22       C  
ATOM   3755  CE  LYS A 511     -48.203 -29.642 -58.858  1.00123.03           C  
ANISOU 3755  CE  LYS A 511    16572  15159  15015   -897  -1563     -2       C  
ATOM   3756  NZ  LYS A 511     -49.400 -29.510 -57.981  1.00126.50           N  
ANISOU 3756  NZ  LYS A 511    17012  15658  15393  -1032  -1510     27       N  
ATOM   3757  N   MET A 512     -49.451 -31.395 -64.911  1.00113.38           N  
ANISOU 3757  N   MET A 512    15316  13872  13891   -850  -1595    107       N  
ATOM   3758  CA  MET A 512     -49.755 -31.238 -66.328  1.00112.46           C  
ANISOU 3758  CA  MET A 512    15122  13775  13831   -826  -1565    120       C  
ATOM   3759  C   MET A 512     -50.083 -29.786 -66.629  1.00111.16           C  
ANISOU 3759  C   MET A 512    14772  13698  13765   -820  -1457    107       C  
ATOM   3760  O   MET A 512     -50.674 -29.090 -65.801  1.00112.38           O  
ANISOU 3760  O   MET A 512    14870  13906  13923   -880  -1398    106       O  
ATOM   3761  CB  MET A 512     -50.937 -32.101 -66.737  1.00113.19           C  
ANISOU 3761  CB  MET A 512    15294  13851  13858   -936  -1578    177       C  
ATOM   3762  CG  MET A 512     -50.625 -33.571 -66.878  1.00114.92           C  
ANISOU 3762  CG  MET A 512    15701  13970  13990   -931  -1695    193       C  
ATOM   3763  SD  MET A 512     -52.140 -34.427 -67.322  1.00118.22           S  
ANISOU 3763  SD  MET A 512    16198  14382  14335  -1084  -1698    263       S  
ATOM   3764  CE  MET A 512     -51.723 -36.080 -66.797  1.00120.56           C  
ANISOU 3764  CE  MET A 512    16755  14548  14504  -1104  -1848    282       C  
ATOM   3765  N   PHE A 513     -49.697 -29.335 -67.819  1.00106.51           N  
ANISOU 3765  N   PHE A 513    14094  13123  13251   -744  -1437     96       N  
ATOM   3766  CA  PHE A 513     -50.001 -27.980 -68.255  1.00100.91           C  
ANISOU 3766  CA  PHE A 513    13224  12484  12633   -735  -1346     87       C  
ATOM   3767  C   PHE A 513     -50.765 -28.019 -69.566  1.00 97.91           C  
ANISOU 3767  C   PHE A 513    12802  12120  12279   -754  -1319    119       C  
ATOM   3768  O   PHE A 513     -50.329 -28.632 -70.532  1.00 97.47           O  
ANISOU 3768  O   PHE A 513    12782  12029  12222   -703  -1363    123       O  
ATOM   3769  CB  PHE A 513     -48.723 -27.143 -68.358  1.00 98.89           C  
ANISOU 3769  CB  PHE A 513    12886  12239  12449   -632  -1339     40       C  
ATOM   3770  CG  PHE A 513     -47.889 -27.179 -67.113  1.00 96.77           C  
ANISOU 3770  CG  PHE A 513    12663  11952  12153   -604  -1374      4       C  
ATOM   3771  CD1 PHE A 513     -48.426 -26.788 -65.895  1.00 96.05           C  
ANISOU 3771  CD1 PHE A 513    12571  11883  12039   -668  -1343      4       C  
ATOM   3772  CD2 PHE A 513     -46.578 -27.621 -67.152  1.00 95.99           C  
ANISOU 3772  CD2 PHE A 513    12606  11820  12045   -510  -1441    -33       C  
ATOM   3773  CE1 PHE A 513     -47.673 -26.832 -64.737  1.00 96.30           C  
ANISOU 3773  CE1 PHE A 513    12648  11897  12044   -642  -1377    -28       C  
ATOM   3774  CE2 PHE A 513     -45.816 -27.664 -65.998  1.00 97.13           C  
ANISOU 3774  CE2 PHE A 513    12793  11948  12162   -480  -1477    -70       C  
ATOM   3775  CZ  PHE A 513     -46.363 -27.268 -64.788  1.00 96.84           C  
ANISOU 3775  CZ  PHE A 513    12761  11926  12107   -548  -1445    -64       C  
ATOM   3776  N   VAL A 514     -51.922 -27.374 -69.567  1.00 94.68           N  
ANISOU 3776  N   VAL A 514    12317  11766  11888   -824  -1251    136       N  
ATOM   3777  CA  VAL A 514     -52.836 -27.413 -70.687  1.00 94.84           C  
ANISOU 3777  CA  VAL A 514    12300  11808  11925   -855  -1224    166       C  
ATOM   3778  C   VAL A 514     -52.931 -26.023 -71.286  1.00 94.96           C  
ANISOU 3778  C   VAL A 514    12170  11874  12036   -814  -1155    150       C  
ATOM   3779  O   VAL A 514     -52.995 -25.026 -70.560  1.00 96.24           O  
ANISOU 3779  O   VAL A 514    12261  12074  12230   -814  -1112    125       O  
ATOM   3780  CB  VAL A 514     -54.245 -27.867 -70.228  1.00 98.31           C  
ANISOU 3780  CB  VAL A 514    12772  12281  12297   -978  -1206    197       C  
ATOM   3781  CG1 VAL A 514     -55.285 -27.700 -71.334  1.00 98.36           C  
ANISOU 3781  CG1 VAL A 514    12715  12327  12329  -1009  -1168    219       C  
ATOM   3782  CG2 VAL A 514     -54.219 -29.306 -69.731  1.00 99.94           C  
ANISOU 3782  CG2 VAL A 514    13142  12428  12401  -1035  -1283    222       C  
ATOM   3783  N   LYS A 515     -52.917 -25.964 -72.614  1.00 94.85           N  
ANISOU 3783  N   LYS A 515    12120  11854  12062   -776  -1151    163       N  
ATOM   3784  CA  LYS A 515     -53.323 -24.764 -73.341  1.00 93.74           C  
ANISOU 3784  CA  LYS A 515    11859  11757  11998   -757  -1090    159       C  
ATOM   3785  C   LYS A 515     -54.285 -25.163 -74.446  1.00 90.90           C  
ANISOU 3785  C   LYS A 515    11497  11406  11631   -788  -1084    192       C  
ATOM   3786  O   LYS A 515     -54.164 -26.244 -75.016  1.00 91.17           O  
ANISOU 3786  O   LYS A 515    11611  11402  11626   -788  -1131    213       O  
ATOM   3787  CB  LYS A 515     -52.114 -23.989 -73.890  1.00 95.00           C  
ANISOU 3787  CB  LYS A 515    11961  11907  12226   -669  -1086    137       C  
ATOM   3788  CG  LYS A 515     -51.396 -24.606 -75.080  1.00 96.97           C  
ANISOU 3788  CG  LYS A 515    12237  12128  12478   -614  -1123    146       C  
ATOM   3789  CD  LYS A 515     -50.256 -23.707 -75.530  1.00 99.96           C  
ANISOU 3789  CD  LYS A 515    12542  12519  12919   -545  -1109    121       C  
ATOM   3790  CE  LYS A 515     -50.110 -23.694 -77.046  1.00104.12           C  
ANISOU 3790  CE  LYS A 515    13036  13050  13472   -511  -1105    138       C  
ATOM   3791  NZ  LYS A 515     -49.507 -24.936 -77.609  1.00107.17           N  
ANISOU 3791  NZ  LYS A 515    13495  13412  13811   -469  -1165    137       N  
ATOM   3792  N   GLY A 516     -55.252 -24.303 -74.731  1.00 88.76           N  
ANISOU 3792  N   GLY A 516    11140  11186  11398   -811  -1031    191       N  
ATOM   3793  CA  GLY A 516     -56.209 -24.575 -75.792  1.00 87.98           C  
ANISOU 3793  CA  GLY A 516    11028  11103  11297   -837  -1022    217       C  
ATOM   3794  C   GLY A 516     -57.253 -23.492 -75.892  1.00 88.42           C  
ANISOU 3794  C   GLY A 516    10982  11221  11391   -852   -967    203       C  
ATOM   3795  O   GLY A 516     -57.093 -22.405 -75.326  1.00 87.81           O  
ANISOU 3795  O   GLY A 516    10842  11164  11355   -825   -939    173       O  
ATOM   3796  N   ALA A 517     -58.319 -23.793 -76.628  1.00 90.14           N  
ANISOU 3796  N   ALA A 517    11187  11466  11594   -889   -959    222       N  
ATOM   3797  CA  ALA A 517     -59.466 -22.901 -76.756  1.00 93.11           C  
ANISOU 3797  CA  ALA A 517    11470  11910  11995   -902   -915    202       C  
ATOM   3798  C   ALA A 517     -60.039 -22.604 -75.371  1.00 94.89           C  
ANISOU 3798  C   ALA A 517    11669  12199  12185   -953   -891    171       C  
ATOM   3799  O   ALA A 517     -60.145 -23.511 -74.545  1.00 96.11           O  
ANISOU 3799  O   ALA A 517    11890  12360  12267  -1023   -906    181       O  
ATOM   3800  CB  ALA A 517     -60.527 -23.530 -77.650  1.00 93.86           C  
ANISOU 3800  CB  ALA A 517    11567  12030  12063   -946   -917    225       C  
ATOM   3801  N   PRO A 518     -60.390 -21.333 -75.105  1.00 96.06           N  
ANISOU 3801  N   PRO A 518    11727  12392  12378   -917   -857    131       N  
ATOM   3802  CA  PRO A 518     -60.942 -20.959 -73.806  1.00 99.73           C  
ANISOU 3802  CA  PRO A 518    12155  12928  12809   -954   -834     92       C  
ATOM   3803  C   PRO A 518     -62.241 -21.700 -73.485  1.00104.51           C  
ANISOU 3803  C   PRO A 518    12756  13619  13334  -1054   -820     93       C  
ATOM   3804  O   PRO A 518     -62.343 -22.321 -72.421  1.00107.02           O  
ANISOU 3804  O   PRO A 518    13116  13966  13581  -1127   -822     93       O  
ATOM   3805  CB  PRO A 518     -61.199 -19.457 -73.955  1.00 99.94           C  
ANISOU 3805  CB  PRO A 518    12085  12982  12904   -882   -811     48       C  
ATOM   3806  CG  PRO A 518     -60.243 -19.020 -75.009  1.00 99.17           C  
ANISOU 3806  CG  PRO A 518    11998  12800  12878   -808   -828     70       C  
ATOM   3807  CD  PRO A 518     -60.218 -20.161 -75.979  1.00 97.16           C  
ANISOU 3807  CD  PRO A 518    11802  12514  12600   -836   -847    118       C  
ATOM   3808  N   GLU A 519     -63.206 -21.649 -74.408  1.00106.98           N  
ANISOU 3808  N   GLU A 519    13020  13974  13652  -1060   -809     93       N  
ATOM   3809  CA  GLU A 519     -64.510 -22.319 -74.259  1.00107.13           C  
ANISOU 3809  CA  GLU A 519    13021  14088  13594  -1159   -794     90       C  
ATOM   3810  C   GLU A 519     -64.356 -23.762 -73.778  1.00104.24           C  
ANISOU 3810  C   GLU A 519    12766  13697  13141  -1263   -820    135       C  
ATOM   3811  O   GLU A 519     -65.032 -24.183 -72.841  1.00103.10           O  
ANISOU 3811  O   GLU A 519    12625  13631  12917  -1361   -806    126       O  
ATOM   3812  CB  GLU A 519     -65.298 -22.298 -75.583  1.00111.49           C  
ANISOU 3812  CB  GLU A 519    13530  14659  14170  -1145   -793     97       C  
ATOM   3813  CG  GLU A 519     -65.184 -21.011 -76.406  1.00114.71           C  
ANISOU 3813  CG  GLU A 519    13866  15046  14670  -1029   -787     70       C  
ATOM   3814  CD  GLU A 519     -64.071 -21.051 -77.453  1.00111.53           C  
ANISOU 3814  CD  GLU A 519    13520  14527  14329   -962   -814    113       C  
ATOM   3815  OE1 GLU A 519     -64.146 -21.894 -78.376  1.00109.47           O  
ANISOU 3815  OE1 GLU A 519    13303  14233  14054   -984   -832    153       O  
ATOM   3816  OE2 GLU A 519     -63.130 -20.229 -77.363  1.00107.17           O  
ANISOU 3816  OE2 GLU A 519    12963  13919  13835   -890   -817    104       O  
ATOM   3817  N   GLY A 520     -63.448 -24.497 -74.418  1.00102.51           N  
ANISOU 3817  N   GLY A 520    12642  13370  12934  -1241   -862    181       N  
ATOM   3818  CA  GLY A 520     -63.204 -25.902 -74.109  1.00104.45           C  
ANISOU 3818  CA  GLY A 520    13015  13568  13100  -1324   -905    225       C  
ATOM   3819  C   GLY A 520     -62.575 -26.210 -72.757  1.00105.03           C  
ANISOU 3819  C   GLY A 520    13158  13622  13125  -1358   -920    223       C  
ATOM   3820  O   GLY A 520     -63.069 -27.074 -72.029  1.00104.99           O  
ANISOU 3820  O   GLY A 520    13217  13645  13026  -1471   -931    241       O  
ATOM   3821  N   VAL A 521     -61.484 -25.517 -72.425  1.00104.97           N  
ANISOU 3821  N   VAL A 521    13140  13565  13175  -1266   -922    203       N  
ATOM   3822  CA  VAL A 521     -60.697 -25.834 -71.223  1.00103.72           C  
ANISOU 3822  CA  VAL A 521    13058  13373  12977  -1281   -945    201       C  
ATOM   3823  C   VAL A 521     -61.284 -25.273 -69.927  1.00107.36           C  
ANISOU 3823  C   VAL A 521    13461  13927  13401  -1332   -904    165       C  
ATOM   3824  O   VAL A 521     -61.104 -25.871 -68.865  1.00109.43           O  
ANISOU 3824  O   VAL A 521    13800  14185  13591  -1396   -922    172       O  
ATOM   3825  CB  VAL A 521     -59.208 -25.424 -71.341  1.00100.57           C  
ANISOU 3825  CB  VAL A 521    12677  12888  12647  -1167   -970    192       C  
ATOM   3826  CG1 VAL A 521     -58.562 -26.073 -72.553  1.00 99.80           C  
ANISOU 3826  CG1 VAL A 521    12638  12709  12571  -1117  -1014    223       C  
ATOM   3827  CG2 VAL A 521     -59.053 -23.915 -71.392  1.00 99.14           C  
ANISOU 3827  CG2 VAL A 521    12375  12738  12553  -1085   -926    150       C  
ATOM   3828  N   ILE A 522     -61.976 -24.135 -70.018  1.00107.99           N  
ANISOU 3828  N   ILE A 522    13412  14090  13527  -1300   -854    122       N  
ATOM   3829  CA  ILE A 522     -62.568 -23.486 -68.842  1.00109.36           C  
ANISOU 3829  CA  ILE A 522    13515  14366  13669  -1332   -815     75       C  
ATOM   3830  C   ILE A 522     -63.605 -24.393 -68.173  1.00111.77           C  
ANISOU 3830  C   ILE A 522    13850  14760  13857  -1477   -805     88       C  
ATOM   3831  O   ILE A 522     -63.695 -24.438 -66.941  1.00113.07           O  
ANISOU 3831  O   ILE A 522    14025  14975  13959  -1534   -793     71       O  
ATOM   3832  CB  ILE A 522     -63.150 -22.092 -69.185  1.00109.08           C  
ANISOU 3832  CB  ILE A 522    13339  14400  13704  -1255   -774     20       C  
ATOM   3833  CG1 ILE A 522     -62.012 -21.105 -69.446  1.00110.79           C  
ANISOU 3833  CG1 ILE A 522    13540  14533  14022  -1131   -785      6       C  
ATOM   3834  CG2 ILE A 522     -64.013 -21.555 -68.053  1.00109.85           C  
ANISOU 3834  CG2 ILE A 522    13357  14627  13753  -1296   -736    -34       C  
ATOM   3835  CD1 ILE A 522     -62.422 -19.865 -70.211  1.00112.46           C  
ANISOU 3835  CD1 ILE A 522    13648  14768  14311  -1046   -766    -30       C  
ATOM   3836  N   ASP A 523     -64.359 -25.129 -68.991  1.00113.63           N  
ANISOU 3836  N   ASP A 523    14101  15012  14058  -1543   -811    118       N  
ATOM   3837  CA  ASP A 523     -65.312 -26.125 -68.498  1.00115.62           C  
ANISOU 3837  CA  ASP A 523    14395  15340  14192  -1700   -808    140       C  
ATOM   3838  C   ASP A 523     -64.596 -27.273 -67.790  1.00116.40           C  
ANISOU 3838  C   ASP A 523    14658  15353  14215  -1772   -860    189       C  
ATOM   3839  O   ASP A 523     -65.094 -27.800 -66.797  1.00122.75           O  
ANISOU 3839  O   ASP A 523    15501  16221  14917  -1895   -854    196       O  
ATOM   3840  CB  ASP A 523     -66.170 -26.681 -69.636  1.00116.71           C  
ANISOU 3840  CB  ASP A 523    14525  15501  14317  -1750   -812    166       C  
ATOM   3841  CG  ASP A 523     -66.985 -25.610 -70.345  1.00118.21           C  
ANISOU 3841  CG  ASP A 523    14560  15782  14571  -1682   -767    115       C  
ATOM   3842  OD1 ASP A 523     -67.103 -24.475 -69.833  1.00114.14           O  
ANISOU 3842  OD1 ASP A 523    13940  15333  14092  -1617   -731     55       O  
ATOM   3843  OD2 ASP A 523     -67.516 -25.918 -71.432  1.00123.04           O  
ANISOU 3843  OD2 ASP A 523    15160  16395  15194  -1691   -773    132       O  
ATOM   3844  N   ARG A 524     -63.425 -27.647 -68.294  1.00113.01           N  
ANISOU 3844  N   ARG A 524    14323  14781  13831  -1693   -914    220       N  
ATOM   3845  CA  ARG A 524     -62.646 -28.725 -67.694  1.00114.50           C  
ANISOU 3845  CA  ARG A 524    14676  14873  13953  -1738   -977    259       C  
ATOM   3846  C   ARG A 524     -61.827 -28.300 -66.464  1.00119.93           C  
ANISOU 3846  C   ARG A 524    15382  15546  14640  -1700   -978    233       C  
ATOM   3847  O   ARG A 524     -61.082 -29.109 -65.902  1.00121.52           O  
ANISOU 3847  O   ARG A 524    15719  15662  14789  -1720  -1036    259       O  
ATOM   3848  CB  ARG A 524     -61.747 -29.365 -68.742  1.00111.87           C  
ANISOU 3848  CB  ARG A 524    14438  14407  13661  -1663  -1041    293       C  
ATOM   3849  CG  ARG A 524     -62.508 -30.160 -69.782  1.00111.92           C  
ANISOU 3849  CG  ARG A 524    14476  14410  13638  -1726  -1060    331       C  
ATOM   3850  CD  ARG A 524     -61.550 -30.825 -70.749  1.00111.56           C  
ANISOU 3850  CD  ARG A 524    14529  14232  13625  -1644  -1130    358       C  
ATOM   3851  NE  ARG A 524     -61.192 -29.947 -71.859  1.00109.71           N  
ANISOU 3851  NE  ARG A 524    14190  13990  13504  -1515  -1104    336       N  
ATOM   3852  CZ  ARG A 524     -60.029 -29.988 -72.498  1.00108.12           C  
ANISOU 3852  CZ  ARG A 524    14024  13696  13358  -1400  -1144    336       C  
ATOM   3853  NH1 ARG A 524     -59.091 -30.848 -72.128  1.00106.70           N  
ANISOU 3853  NH1 ARG A 524    13978  13425  13136  -1383  -1216    350       N  
ATOM   3854  NH2 ARG A 524     -59.801 -29.156 -73.502  1.00108.60           N  
ANISOU 3854  NH2 ARG A 524    13986  13762  13513  -1301  -1115    319       N  
ATOM   3855  N   CYS A 525     -61.971 -27.038 -66.054  1.00123.05           N  
ANISOU 3855  N   CYS A 525    15643  16020  15090  -1642   -921    180       N  
ATOM   3856  CA  CYS A 525     -61.360 -26.534 -64.825  1.00122.88           C  
ANISOU 3856  CA  CYS A 525    15620  16003  15063  -1614   -914    148       C  
ATOM   3857  C   CYS A 525     -62.327 -26.674 -63.658  1.00125.17           C  
ANISOU 3857  C   CYS A 525    15895  16415  15249  -1743   -880    136       C  
ATOM   3858  O   CYS A 525     -63.489 -26.268 -63.756  1.00125.79           O  
ANISOU 3858  O   CYS A 525    15863  16619  15310  -1792   -828    110       O  
ATOM   3859  CB  CYS A 525     -60.973 -25.062 -64.966  1.00123.54           C  
ANISOU 3859  CB  CYS A 525    15575  16104  15260  -1483   -877     94       C  
ATOM   3860  SG  CYS A 525     -59.806 -24.675 -66.289  1.00127.34           S  
ANISOU 3860  SG  CYS A 525    16053  16466  15864  -1337   -907    102       S  
ATOM   3861  N   ASN A 526     -61.838 -27.246 -62.559  1.00127.18           N  
ANISOU 3861  N   ASN A 526    16256  16634  15429  -1795   -911    151       N  
ATOM   3862  CA  ASN A 526     -62.606 -27.362 -61.315  1.00126.69           C  
ANISOU 3862  CA  ASN A 526    16187  16687  15260  -1919   -880    139       C  
ATOM   3863  C   ASN A 526     -62.207 -26.331 -60.260  1.00126.75           C  
ANISOU 3863  C   ASN A 526    16123  16739  15296  -1851   -849     82       C  
ATOM   3864  O   ASN A 526     -62.932 -26.120 -59.285  1.00128.07           O  
ANISOU 3864  O   ASN A 526    16240  17030  15390  -1931   -808     54       O  
ATOM   3865  CB  ASN A 526     -62.477 -28.770 -60.735  1.00126.45           C  
ANISOU 3865  CB  ASN A 526    16340  16596  15107  -2048   -938    199       C  
ATOM   3866  CG  ASN A 526     -63.398 -29.761 -61.408  1.00128.30           C  
ANISOU 3866  CG  ASN A 526    16628  16851  15269  -2178   -951    247       C  
ATOM   3867  OD1 ASN A 526     -64.587 -29.498 -61.590  1.00130.40           O  
ANISOU 3867  OD1 ASN A 526    16782  17253  15508  -2251   -894    230       O  
ATOM   3868  ND2 ASN A 526     -62.856 -30.913 -61.775  1.00129.41           N  
ANISOU 3868  ND2 ASN A 526    16937  16857  15374  -2204  -1032    305       N  
ATOM   3869  N   TYR A 527     -61.053 -25.698 -60.463  1.00124.85           N  
ANISOU 3869  N   TYR A 527    15875  16403  15159  -1707   -869     63       N  
ATOM   3870  CA  TYR A 527     -60.537 -24.684 -59.548  1.00121.02           C  
ANISOU 3870  CA  TYR A 527    15328  15940  14713  -1630   -849      9       C  
ATOM   3871  C   TYR A 527     -59.975 -23.504 -60.336  1.00118.40           C  
ANISOU 3871  C   TYR A 527    14895  15570  14520  -1478   -837    -26       C  
ATOM   3872  O   TYR A 527     -59.834 -23.579 -61.559  1.00118.76           O  
ANISOU 3872  O   TYR A 527    14936  15560  14627  -1432   -850     -4       O  
ATOM   3873  CB  TYR A 527     -59.436 -25.268 -58.656  1.00121.31           C  
ANISOU 3873  CB  TYR A 527    15500  15881  14711  -1627   -903     28       C  
ATOM   3874  CG  TYR A 527     -59.685 -26.679 -58.163  1.00124.57           C  
ANISOU 3874  CG  TYR A 527    16066  16272  14992  -1767   -945     83       C  
ATOM   3875  CD1 TYR A 527     -60.418 -26.917 -56.998  1.00126.14           C  
ANISOU 3875  CD1 TYR A 527    16279  16571  15075  -1894   -920     80       C  
ATOM   3876  CD2 TYR A 527     -59.179 -27.779 -58.860  1.00125.10           C  
ANISOU 3876  CD2 TYR A 527    16270  16217  15042  -1776  -1014    137       C  
ATOM   3877  CE1 TYR A 527     -60.645 -28.211 -56.545  1.00127.06           C  
ANISOU 3877  CE1 TYR A 527    16551  16663  15064  -2036   -964    137       C  
ATOM   3878  CE2 TYR A 527     -59.401 -29.075 -58.417  1.00126.51           C  
ANISOU 3878  CE2 TYR A 527    16608  16363  15097  -1906  -1065    190       C  
ATOM   3879  CZ  TYR A 527     -60.132 -29.287 -57.260  1.00127.51           C  
ANISOU 3879  CZ  TYR A 527    16754  16584  15109  -2041  -1039    193       C  
ATOM   3880  OH  TYR A 527     -60.348 -30.574 -56.822  1.00128.49           O  
ANISOU 3880  OH  TYR A 527    17048  16669  15102  -2183  -1094    250       O  
ATOM   3881  N   VAL A 528     -59.675 -22.413 -59.632  1.00115.67           N  
ANISOU 3881  N   VAL A 528    14473  15256  14219  -1405   -814    -81       N  
ATOM   3882  CA  VAL A 528     -58.929 -21.286 -60.204  1.00112.57           C  
ANISOU 3882  CA  VAL A 528    14010  14808  13951  -1267   -814   -113       C  
ATOM   3883  C   VAL A 528     -57.707 -20.962 -59.347  1.00110.38           C  
ANISOU 3883  C   VAL A 528    13774  14466  13700  -1203   -841   -132       C  
ATOM   3884  O   VAL A 528     -57.761 -21.040 -58.121  1.00112.55           O  
ANISOU 3884  O   VAL A 528    14070  14782  13909  -1245   -837   -150       O  
ATOM   3885  CB  VAL A 528     -59.785 -20.003 -60.404  1.00111.56           C  
ANISOU 3885  CB  VAL A 528    13733  14777  13874  -1219   -766   -170       C  
ATOM   3886  CG1 VAL A 528     -60.871 -20.224 -61.447  1.00110.06           C  
ANISOU 3886  CG1 VAL A 528    13495  14643  13678  -1258   -745   -156       C  
ATOM   3887  CG2 VAL A 528     -60.375 -19.505 -59.091  1.00112.86           C  
ANISOU 3887  CG2 VAL A 528    13841  15057  13981  -1249   -734   -225       C  
ATOM   3888  N   ARG A 529     -56.605 -20.615 -60.002  1.00107.65           N  
ANISOU 3888  N   ARG A 529    13435  14021  13443  -1106   -868   -129       N  
ATOM   3889  CA  ARG A 529     -55.410 -20.170 -59.305  1.00104.48           C  
ANISOU 3889  CA  ARG A 529    13055  13564  13079  -1036   -892   -155       C  
ATOM   3890  C   ARG A 529     -55.474 -18.666 -59.078  1.00105.60           C  
ANISOU 3890  C   ARG A 529    13081  13745  13294   -963   -861   -212       C  
ATOM   3891  O   ARG A 529     -55.634 -17.880 -60.023  1.00101.90           O  
ANISOU 3891  O   ARG A 529    12539  13273  12903   -909   -847   -222       O  
ATOM   3892  CB  ARG A 529     -54.144 -20.542 -60.086  1.00102.15           C  
ANISOU 3892  CB  ARG A 529    12819  13157  12836   -972   -939   -129       C  
ATOM   3893  CG  ARG A 529     -52.830 -20.207 -59.383  1.00 97.65           C  
ANISOU 3893  CG  ARG A 529    12274  12532  12296   -903   -970   -157       C  
ATOM   3894  CD  ARG A 529     -52.355 -21.322 -58.463  1.00 95.36           C  
ANISOU 3894  CD  ARG A 529    12109  12204  11916   -944  -1016   -142       C  
ATOM   3895  NE  ARG A 529     -51.903 -22.497 -59.206  1.00 92.07           N  
ANISOU 3895  NE  ARG A 529    11792  11715  11474   -948  -1068   -100       N  
ATOM   3896  CZ  ARG A 529     -52.591 -23.630 -59.331  1.00 90.67           C  
ANISOU 3896  CZ  ARG A 529    11701  11536  11212  -1034  -1086    -56       C  
ATOM   3897  NH1 ARG A 529     -53.775 -23.770 -58.759  1.00 90.85           N  
ANISOU 3897  NH1 ARG A 529    11717  11636  11164  -1135  -1051    -47       N  
ATOM   3898  NH2 ARG A 529     -52.088 -24.633 -60.027  1.00 90.32           N  
ANISOU 3898  NH2 ARG A 529    11751  11417  11150  -1021  -1142    -25       N  
ATOM   3899  N   VAL A 530     -55.368 -18.284 -57.809  1.00109.97           N  
ANISOU 3899  N   VAL A 530    13628  14336  13819   -964   -856   -251       N  
ATOM   3900  CA  VAL A 530     -55.242 -16.884 -57.420  1.00113.53           C  
ANISOU 3900  CA  VAL A 530    13990  14810  14336   -887   -840   -310       C  
ATOM   3901  C   VAL A 530     -53.909 -16.736 -56.692  1.00115.06           C  
ANISOU 3901  C   VAL A 530    14232  14933  14553   -838   -874   -324       C  
ATOM   3902  O   VAL A 530     -53.799 -17.065 -55.508  1.00116.12           O  
ANISOU 3902  O   VAL A 530    14408  15089  14621   -870   -881   -336       O  
ATOM   3903  CB  VAL A 530     -56.411 -16.411 -56.525  1.00112.75           C  
ANISOU 3903  CB  VAL A 530    13821  14837  14182   -922   -802   -358       C  
ATOM   3904  CG1 VAL A 530     -56.559 -14.897 -56.608  1.00111.10           C  
ANISOU 3904  CG1 VAL A 530    13509  14651  14054   -830   -791   -419       C  
ATOM   3905  CG2 VAL A 530     -57.714 -17.090 -56.927  1.00112.71           C  
ANISOU 3905  CG2 VAL A 530    13798  14918  14105  -1010   -773   -337       C  
ATOM   3906  N   GLY A 531     -52.897 -16.260 -57.419  1.00115.61           N  
ANISOU 3906  N   GLY A 531    14292  14921  14710   -765   -896   -321       N  
ATOM   3907  CA  GLY A 531     -51.528 -16.199 -56.910  1.00119.33           C  
ANISOU 3907  CA  GLY A 531    14806  15325  15207   -717   -933   -333       C  
ATOM   3908  C   GLY A 531     -50.941 -17.594 -56.781  1.00123.24           C  
ANISOU 3908  C   GLY A 531    15414  15773  15637   -751   -971   -295       C  
ATOM   3909  O   GLY A 531     -50.639 -18.244 -57.789  1.00126.23           O  
ANISOU 3909  O   GLY A 531    15829  16106  16028   -748   -991   -258       O  
ATOM   3910  N   THR A 532     -50.773 -18.045 -55.536  1.00122.39           N  
ANISOU 3910  N   THR A 532    15368  15675  15460   -779   -988   -307       N  
ATOM   3911  CA  THR A 532     -50.411 -19.435 -55.235  1.00117.54           C  
ANISOU 3911  CA  THR A 532    14879  15017  14762   -821  -1033   -272       C  
ATOM   3912  C   THR A 532     -51.545 -20.150 -54.511  1.00116.54           C  
ANISOU 3912  C   THR A 532    14800  14954  14524   -928  -1016   -252       C  
ATOM   3913  O   THR A 532     -51.357 -21.239 -53.977  1.00118.80           O  
ANISOU 3913  O   THR A 532    15204  15209  14725   -977  -1056   -226       O  
ATOM   3914  CB  THR A 532     -49.137 -19.534 -54.376  1.00116.34           C  
ANISOU 3914  CB  THR A 532    14786  14812  14606   -770  -1080   -298       C  
ATOM   3915  OG1 THR A 532     -49.069 -18.414 -53.487  1.00116.96           O  
ANISOU 3915  OG1 THR A 532    14794  14929  14716   -738  -1057   -349       O  
ATOM   3916  CG2 THR A 532     -47.905 -19.555 -55.256  1.00117.15           C  
ANISOU 3916  CG2 THR A 532    14890  14843  14777   -690  -1118   -300       C  
ATOM   3917  N   THR A 533     -52.720 -19.529 -54.503  1.00115.83           N  
ANISOU 3917  N   THR A 533    14620  14957  14432   -964   -961   -267       N  
ATOM   3918  CA  THR A 533     -53.892 -20.086 -53.844  1.00118.34           C  
ANISOU 3918  CA  THR A 533    14958  15362  14642  -1074   -935   -255       C  
ATOM   3919  C   THR A 533     -54.794 -20.763 -54.853  1.00118.22           C  
ANISOU 3919  C   THR A 533    14948  15369  14600  -1142   -921   -210       C  
ATOM   3920  O   THR A 533     -54.956 -20.277 -55.971  1.00118.37           O  
ANISOU 3920  O   THR A 533    14897  15381  14696  -1096   -905   -209       O  
ATOM   3921  CB  THR A 533     -54.709 -18.983 -53.157  1.00121.25           C  
ANISOU 3921  CB  THR A 533    15212  15844  15014  -1070   -882   -312       C  
ATOM   3922  OG1 THR A 533     -53.815 -18.033 -52.567  1.00125.07           O  
ANISOU 3922  OG1 THR A 533    15663  16296  15561   -978   -894   -360       O  
ATOM   3923  CG2 THR A 533     -55.636 -19.569 -52.087  1.00123.88           C  
ANISOU 3923  CG2 THR A 533    15573  16276  15216  -1184   -861   -310       C  
ATOM   3924  N   ARG A 534     -55.382 -21.883 -54.451  1.00118.64           N  
ANISOU 3924  N   ARG A 534    15091  15447  14539  -1257   -930   -171       N  
ATOM   3925  CA  ARG A 534     -56.404 -22.532 -55.252  1.00120.23           C  
ANISOU 3925  CA  ARG A 534    15294  15687  14698  -1342   -914   -131       C  
ATOM   3926  C   ARG A 534     -57.788 -22.220 -54.680  1.00122.10           C  
ANISOU 3926  C   ARG A 534    15447  16078  14868  -1430   -853   -157       C  
ATOM   3927  O   ARG A 534     -57.995 -22.278 -53.468  1.00126.09           O  
ANISOU 3927  O   ARG A 534    15970  16644  15293  -1486   -843   -174       O  
ATOM   3928  CB  ARG A 534     -56.159 -24.037 -55.320  1.00121.88           C  
ANISOU 3928  CB  ARG A 534    15667  15817  14822  -1420   -972    -69       C  
ATOM   3929  CG  ARG A 534     -56.704 -24.676 -56.586  1.00122.96           C  
ANISOU 3929  CG  ARG A 534    15819  15938  14961  -1459   -977    -24       C  
ATOM   3930  CD  ARG A 534     -56.293 -26.132 -56.716  1.00123.01           C  
ANISOU 3930  CD  ARG A 534    16001  15844  14893  -1514  -1051     33       C  
ATOM   3931  NE  ARG A 534     -57.081 -27.002 -55.850  1.00125.40           N  
ANISOU 3931  NE  ARG A 534    16394  16196  15057  -1667  -1056     65       N  
ATOM   3932  CZ  ARG A 534     -57.025 -28.331 -55.860  1.00127.74           C  
ANISOU 3932  CZ  ARG A 534    16855  16417  15261  -1750  -1121    120       C  
ATOM   3933  NH1 ARG A 534     -56.214 -28.971 -56.694  1.00126.54           N  
ANISOU 3933  NH1 ARG A 534    16795  16141  15143  -1683  -1190    145       N  
ATOM   3934  NH2 ARG A 534     -57.789 -29.024 -55.027  1.00132.38           N  
ANISOU 3934  NH2 ARG A 534    17521  17060  15718  -1903  -1121    150       N  
ATOM   3935  N   VAL A 535     -58.723 -21.878 -55.564  1.00122.72           N  
ANISOU 3935  N   VAL A 535    15429  16223  14975  -1438   -814   -163       N  
ATOM   3936  CA  VAL A 535     -60.074 -21.455 -55.184  1.00123.69           C  
ANISOU 3936  CA  VAL A 535    15443  16508  15043  -1502   -755   -201       C  
ATOM   3937  C   VAL A 535     -61.104 -22.193 -56.056  1.00128.03           C  
ANISOU 3937  C   VAL A 535    15991  17108  15546  -1598   -741   -163       C  
ATOM   3938  O   VAL A 535     -60.934 -22.266 -57.274  1.00131.52           O  
ANISOU 3938  O   VAL A 535    16432  17479  16058  -1551   -756   -138       O  
ATOM   3939  CB  VAL A 535     -60.222 -19.914 -55.309  1.00121.23           C  
ANISOU 3939  CB  VAL A 535    14983  16249  14829  -1382   -722   -276       C  
ATOM   3940  CG1 VAL A 535     -61.677 -19.483 -55.430  1.00123.75           C  
ANISOU 3940  CG1 VAL A 535    15176  16730  15113  -1422   -670   -319       C  
ATOM   3941  CG2 VAL A 535     -59.560 -19.214 -54.131  1.00120.67           C  
ANISOU 3941  CG2 VAL A 535    14903  16176  14767  -1324   -727   -323       C  
ATOM   3942  N   PRO A 536     -62.164 -22.759 -55.435  1.00129.33           N  
ANISOU 3942  N   PRO A 536    16153  17397  15586  -1739   -711   -158       N  
ATOM   3943  CA  PRO A 536     -63.204 -23.506 -56.166  1.00126.64           C  
ANISOU 3943  CA  PRO A 536    15811  17117  15188  -1849   -697   -123       C  
ATOM   3944  C   PRO A 536     -63.848 -22.711 -57.304  1.00123.80           C  
ANISOU 3944  C   PRO A 536    15314  16807  14915  -1774   -666   -158       C  
ATOM   3945  O   PRO A 536     -64.316 -21.591 -57.087  1.00122.94           O  
ANISOU 3945  O   PRO A 536    15069  16798  14841  -1707   -627   -230       O  
ATOM   3946  CB  PRO A 536     -64.243 -23.805 -55.084  1.00129.98           C  
ANISOU 3946  CB  PRO A 536    16208  17706  15470  -1995   -656   -140       C  
ATOM   3947  CG  PRO A 536     -63.469 -23.817 -53.810  1.00132.19           C  
ANISOU 3947  CG  PRO A 536    16562  17951  15711  -1993   -676   -145       C  
ATOM   3948  CD  PRO A 536     -62.383 -22.794 -53.976  1.00130.20           C  
ANISOU 3948  CD  PRO A 536    16275  17599  15597  -1812   -693   -183       C  
ATOM   3949  N   MET A 537     -63.862 -23.305 -58.498  1.00123.43           N  
ANISOU 3949  N   MET A 537    15311  16687  14897  -1782   -688   -108       N  
ATOM   3950  CA  MET A 537     -64.424 -22.690 -59.713  1.00123.69           C  
ANISOU 3950  CA  MET A 537    15236  16749  15011  -1715   -667   -131       C  
ATOM   3951  C   MET A 537     -65.951 -22.545 -59.663  1.00124.76           C  
ANISOU 3951  C   MET A 537    15252  17072  15077  -1797   -615   -171       C  
ATOM   3952  O   MET A 537     -66.689 -23.535 -59.695  1.00126.12           O  
ANISOU 3952  O   MET A 537    15465  17304  15151  -1940   -609   -134       O  
ATOM   3953  CB  MET A 537     -63.987 -23.479 -60.961  1.00122.56           C  
ANISOU 3953  CB  MET A 537    15182  16475  14907  -1709   -710    -64       C  
ATOM   3954  CG  MET A 537     -64.731 -23.152 -62.251  1.00123.14           C  
ANISOU 3954  CG  MET A 537    15165  16584  15036  -1676   -691    -73       C  
ATOM   3955  SD  MET A 537     -64.252 -21.593 -63.016  1.00123.18           S  
ANISOU 3955  SD  MET A 537    15061  16546  15196  -1486   -684   -125       S  
ATOM   3956  CE  MET A 537     -62.770 -22.087 -63.886  1.00122.51           C  
ANISOU 3956  CE  MET A 537    15098  16264  15187  -1416   -741    -62       C  
ATOM   3957  N   THR A 538     -66.412 -21.300 -59.594  1.00124.75           N  
ANISOU 3957  N   THR A 538    15106  17165  15126  -1704   -581   -251       N  
ATOM   3958  CA  THR A 538     -67.838 -21.003 -59.529  1.00126.52           C  
ANISOU 3958  CA  THR A 538    15196  17583  15290  -1755   -533   -310       C  
ATOM   3959  C   THR A 538     -68.367 -20.548 -60.893  1.00128.67           C  
ANISOU 3959  C   THR A 538    15388  17860  15641  -1681   -532   -327       C  
ATOM   3960  O   THR A 538     -67.596 -20.362 -61.835  1.00129.90           O  
ANISOU 3960  O   THR A 538    15587  17868  15900  -1587   -564   -295       O  
ATOM   3961  CB  THR A 538     -68.139 -19.927 -58.465  1.00126.05           C  
ANISOU 3961  CB  THR A 538    15024  17650  15217  -1698   -503   -403       C  
ATOM   3962  OG1 THR A 538     -67.484 -18.706 -58.819  1.00124.94           O  
ANISOU 3962  OG1 THR A 538    14840  17423  15206  -1523   -522   -444       O  
ATOM   3963  CG2 THR A 538     -67.666 -20.372 -57.082  1.00126.74           C  
ANISOU 3963  CG2 THR A 538    15190  17743  15220  -1776   -503   -388       C  
ATOM   3964  N   GLY A 539     -69.685 -20.383 -60.987  1.00131.47           N  
ANISOU 3964  N   GLY A 539    15621  18389  15940  -1726   -494   -380       N  
ATOM   3965  CA  GLY A 539     -70.341 -19.867 -62.191  1.00130.76           C  
ANISOU 3965  CA  GLY A 539    15440  18328  15915  -1652   -492   -411       C  
ATOM   3966  C   GLY A 539     -70.101 -18.388 -62.475  1.00130.35           C  
ANISOU 3966  C   GLY A 539    15303  18248  15976  -1467   -504   -482       C  
ATOM   3967  O   GLY A 539     -70.016 -17.998 -63.640  1.00131.48           O  
ANISOU 3967  O   GLY A 539    15435  18313  16208  -1378   -525   -475       O  
ATOM   3968  N   PRO A 540     -70.025 -17.549 -61.418  1.00129.70           N  
ANISOU 3968  N   PRO A 540    15164  18229  15885  -1410   -493   -551       N  
ATOM   3969  CA  PRO A 540     -69.646 -16.136 -61.563  1.00128.60           C  
ANISOU 3969  CA  PRO A 540    14970  18040  15852  -1236   -516   -614       C  
ATOM   3970  C   PRO A 540     -68.209 -15.908 -62.033  1.00126.68           C  
ANISOU 3970  C   PRO A 540    14833  17579  15720  -1153   -557   -555       C  
ATOM   3971  O   PRO A 540     -67.965 -14.971 -62.795  1.00126.23           O  
ANISOU 3971  O   PRO A 540    14751  17449  15762  -1028   -583   -577       O  
ATOM   3972  CB  PRO A 540     -69.827 -15.569 -60.149  1.00130.95           C  
ANISOU 3972  CB  PRO A 540    15206  18454  16092  -1226   -497   -691       C  
ATOM   3973  CG  PRO A 540     -69.939 -16.753 -59.251  1.00132.82           C  
ANISOU 3973  CG  PRO A 540    15500  18757  16207  -1395   -468   -646       C  
ATOM   3974  CD  PRO A 540     -70.586 -17.810 -60.084  1.00131.82           C  
ANISOU 3974  CD  PRO A 540    15393  18658  16032  -1511   -457   -590       C  
ATOM   3975  N   VAL A 541     -67.275 -16.741 -61.573  1.00124.89           N  
ANISOU 3975  N   VAL A 541    14723  17256  15470  -1221   -566   -485       N  
ATOM   3976  CA  VAL A 541     -65.882 -16.693 -62.041  1.00122.62           C  
ANISOU 3976  CA  VAL A 541    14535  16776  15276  -1155   -604   -428       C  
ATOM   3977  C   VAL A 541     -65.795 -17.149 -63.505  1.00121.68           C  
ANISOU 3977  C   VAL A 541    14454  16569  15208  -1151   -621   -369       C  
ATOM   3978  O   VAL A 541     -65.163 -16.484 -64.330  1.00122.75           O  
ANISOU 3978  O   VAL A 541    14596  16598  15443  -1049   -646   -362       O  
ATOM   3979  CB  VAL A 541     -64.938 -17.524 -61.135  1.00121.91           C  
ANISOU 3979  CB  VAL A 541    14560  16619  15141  -1224   -615   -377       C  
ATOM   3980  CG1 VAL A 541     -63.557 -17.671 -61.754  1.00119.45           C  
ANISOU 3980  CG1 VAL A 541    14347  16124  14913  -1167   -655   -318       C  
ATOM   3981  CG2 VAL A 541     -64.815 -16.877 -59.765  1.00125.26           C  
ANISOU 3981  CG2 VAL A 541    14949  17105  15536  -1201   -604   -437       C  
ATOM   3982  N   LYS A 542     -66.446 -18.271 -63.813  1.00119.16           N  
ANISOU 3982  N   LYS A 542    14162  16298  14815  -1266   -609   -327       N  
ATOM   3983  CA  LYS A 542     -66.535 -18.799 -65.176  1.00114.96           C  
ANISOU 3983  CA  LYS A 542    13661  15702  14316  -1273   -624   -275       C  
ATOM   3984  C   LYS A 542     -67.057 -17.761 -66.159  1.00112.19           C  
ANISOU 3984  C   LYS A 542    13214  15370  14042  -1167   -624   -321       C  
ATOM   3985  O   LYS A 542     -66.496 -17.589 -67.233  1.00111.48           O  
ANISOU 3985  O   LYS A 542    13157  15166  14033  -1100   -649   -286       O  
ATOM   3986  CB  LYS A 542     -67.436 -20.034 -65.211  1.00116.42           C  
ANISOU 3986  CB  LYS A 542    13868  15971  14394  -1422   -608   -241       C  
ATOM   3987  CG  LYS A 542     -67.403 -20.809 -66.517  1.00115.42           C  
ANISOU 3987  CG  LYS A 542    13801  15763  14290  -1444   -630   -176       C  
ATOM   3988  CD  LYS A 542     -68.201 -22.092 -66.382  1.00118.70           C  
ANISOU 3988  CD  LYS A 542    14258  16252  14591  -1607   -622   -139       C  
ATOM   3989  CE  LYS A 542     -67.438 -23.271 -66.958  1.00119.02           C  
ANISOU 3989  CE  LYS A 542    14446  16147  14627  -1652   -666    -51       C  
ATOM   3990  NZ  LYS A 542     -68.023 -24.578 -66.547  1.00120.73           N  
ANISOU 3990  NZ  LYS A 542    14738  16413  14719  -1824   -670     -7       N  
ATOM   3991  N   GLU A 543     -68.128 -17.073 -65.784  1.00113.16           N  
ANISOU 3991  N   GLU A 543    13219  15639  14134  -1148   -600   -401       N  
ATOM   3992  CA  GLU A 543     -68.721 -16.064 -66.646  1.00115.29           C  
ANISOU 3992  CA  GLU A 543    13400  15935  14468  -1041   -609   -455       C  
ATOM   3993  C   GLU A 543     -67.822 -14.845 -66.789  1.00111.61           C  
ANISOU 3993  C   GLU A 543    12944  15354  14108   -902   -641   -476       C  
ATOM   3994  O   GLU A 543     -67.726 -14.277 -67.876  1.00110.08           O  
ANISOU 3994  O   GLU A 543    12746  15087  13990   -820   -666   -471       O  
ATOM   3995  CB  GLU A 543     -70.121 -15.681 -66.162  1.00124.35           C  
ANISOU 3995  CB  GLU A 543    14416  17282  15546  -1052   -582   -547       C  
ATOM   3996  CG  GLU A 543     -71.196 -16.672 -66.602  1.00133.81           C  
ANISOU 3996  CG  GLU A 543    15584  18593  16664  -1170   -557   -531       C  
ATOM   3997  CD  GLU A 543     -72.554 -16.424 -65.962  1.00140.97           C  
ANISOU 3997  CD  GLU A 543    16353  19724  17481  -1202   -523   -626       C  
ATOM   3998  OE1 GLU A 543     -72.624 -16.269 -64.721  1.00145.05           O  
ANISOU 3998  OE1 GLU A 543    16840  20334  17938  -1231   -502   -669       O  
ATOM   3999  OE2 GLU A 543     -73.562 -16.402 -66.703  1.00142.72           O  
ANISOU 3999  OE2 GLU A 543    16496  20040  17689  -1200   -518   -660       O  
ATOM   4000  N   LYS A 544     -67.151 -14.467 -65.700  1.00110.44           N  
ANISOU 4000  N   LYS A 544    12815  15188  13959   -883   -643   -495       N  
ATOM   4001  CA  LYS A 544     -66.226 -13.322 -65.696  1.00108.67           C  
ANISOU 4001  CA  LYS A 544    12607  14854  13828   -765   -676   -514       C  
ATOM   4002  C   LYS A 544     -65.045 -13.504 -66.649  1.00107.55           C  
ANISOU 4002  C   LYS A 544    12557  14540  13764   -742   -702   -435       C  
ATOM   4003  O   LYS A 544     -64.679 -12.571 -67.372  1.00107.13           O  
ANISOU 4003  O   LYS A 544    12503  14407  13794   -649   -730   -443       O  
ATOM   4004  CB  LYS A 544     -65.707 -13.025 -64.280  1.00107.34           C  
ANISOU 4004  CB  LYS A 544    12446  14701  13635   -762   -672   -546       C  
ATOM   4005  CG  LYS A 544     -64.708 -11.875 -64.198  1.00104.77           C  
ANISOU 4005  CG  LYS A 544    12144  14261  13401   -653   -708   -564       C  
ATOM   4006  CD  LYS A 544     -65.306 -10.576 -64.721  1.00106.34           C  
ANISOU 4006  CD  LYS A 544    12273  14477  13654   -538   -735   -634       C  
ATOM   4007  CE  LYS A 544     -64.269  -9.473 -64.840  1.00106.30           C  
ANISOU 4007  CE  LYS A 544    12310  14337  13742   -442   -778   -637       C  
ATOM   4008  NZ  LYS A 544     -64.907  -8.178 -65.207  1.00107.20           N  
ANISOU 4008  NZ  LYS A 544    12368  14466  13896   -329   -816   -712       N  
ATOM   4009  N   ILE A 545     -64.452 -14.699 -66.624  1.00104.83           N  
ANISOU 4009  N   ILE A 545    12296  14146  13387   -828   -696   -363       N  
ATOM   4010  CA  ILE A 545     -63.345 -15.062 -67.508  1.00 99.50           C  
ANISOU 4010  CA  ILE A 545    11705  13329  12770   -814   -719   -292       C  
ATOM   4011  C   ILE A 545     -63.741 -14.890 -68.979  1.00 99.80           C  
ANISOU 4011  C   ILE A 545    11724  13339  12856   -777   -728   -274       C  
ATOM   4012  O   ILE A 545     -63.026 -14.236 -69.747  1.00100.19           O  
ANISOU 4012  O   ILE A 545    11791  13290  12984   -706   -752   -258       O  
ATOM   4013  CB  ILE A 545     -62.875 -16.507 -67.250  1.00 96.84           C  
ANISOU 4013  CB  ILE A 545    11459  12962  12372   -912   -718   -228       C  
ATOM   4014  CG1 ILE A 545     -62.208 -16.612 -65.883  1.00 96.31           C  
ANISOU 4014  CG1 ILE A 545    11430  12891  12270   -934   -719   -239       C  
ATOM   4015  CG2 ILE A 545     -61.910 -16.969 -68.331  1.00 95.94           C  
ANISOU 4015  CG2 ILE A 545    11420  12724  12309   -893   -744   -163       C  
ATOM   4016  CD1 ILE A 545     -62.041 -18.042 -65.415  1.00 98.31           C  
ANISOU 4016  CD1 ILE A 545    11774  13139  12439  -1041   -722   -188       C  
ATOM   4017  N   LEU A 546     -64.891 -15.455 -69.349  1.00 98.35           N  
ANISOU 4017  N   LEU A 546    11502  13246  12619   -831   -711   -278       N  
ATOM   4018  CA  LEU A 546     -65.387 -15.415 -70.725  1.00 94.71           C  
ANISOU 4018  CA  LEU A 546    11021  12769  12192   -805   -719   -262       C  
ATOM   4019  C   LEU A 546     -65.788 -14.007 -71.141  1.00 94.58           C  
ANISOU 4019  C   LEU A 546    10936  12761  12237   -694   -736   -322       C  
ATOM   4020  O   LEU A 546     -65.724 -13.669 -72.321  1.00 93.18           O  
ANISOU 4020  O   LEU A 546    10767  12519  12116   -644   -756   -302       O  
ATOM   4021  CB  LEU A 546     -66.550 -16.391 -70.908  1.00 93.95           C  
ANISOU 4021  CB  LEU A 546    10899  12779  12017   -898   -697   -256       C  
ATOM   4022  CG  LEU A 546     -66.285 -17.865 -70.572  1.00 93.66           C  
ANISOU 4022  CG  LEU A 546    10946  12730  11909  -1018   -691   -193       C  
ATOM   4023  CD1 LEU A 546     -67.576 -18.594 -70.232  1.00 94.49           C  
ANISOU 4023  CD1 LEU A 546    11008  12979  11915  -1126   -664   -210       C  
ATOM   4024  CD2 LEU A 546     -65.545 -18.575 -71.695  1.00 93.71           C  
ANISOU 4024  CD2 LEU A 546    11038  12614  11950  -1018   -716   -119       C  
ATOM   4025  N   SER A 547     -66.183 -13.191 -70.162  1.00 97.04           N  
ANISOU 4025  N   SER A 547    11187  13147  12535   -656   -733   -397       N  
ATOM   4026  CA  SER A 547     -66.489 -11.775 -70.384  1.00100.65           C  
ANISOU 4026  CA  SER A 547    11592  13602  13047   -540   -762   -463       C  
ATOM   4027  C   SER A 547     -65.356 -11.082 -71.130  1.00 98.99           C  
ANISOU 4027  C   SER A 547    11447  13234  12929   -473   -797   -423       C  
ATOM   4028  O   SER A 547     -65.572 -10.426 -72.152  1.00 98.97           O  
ANISOU 4028  O   SER A 547    11441  13188  12975   -408   -825   -427       O  
ATOM   4029  CB  SER A 547     -66.714 -11.041 -69.053  1.00103.86           C  
ANISOU 4029  CB  SER A 547    11947  14087  13428   -505   -761   -544       C  
ATOM   4030  OG  SER A 547     -67.616 -11.725 -68.203  1.00108.99           O  
ANISOU 4030  OG  SER A 547    12538  14890  13982   -583   -723   -578       O  
ATOM   4031  N   VAL A 548     -64.147 -11.228 -70.601  1.00 97.57           N  
ANISOU 4031  N   VAL A 548    11329  12974  12766   -493   -798   -385       N  
ATOM   4032  CA  VAL A 548     -62.986 -10.576 -71.179  1.00 96.90           C  
ANISOU 4032  CA  VAL A 548    11301  12755  12760   -444   -827   -350       C  
ATOM   4033  C   VAL A 548     -62.597 -11.308 -72.465  1.00 98.84           C  
ANISOU 4033  C   VAL A 548    11595  12934  13025   -475   -826   -274       C  
ATOM   4034  O   VAL A 548     -62.259 -10.660 -73.461  1.00101.89           O  
ANISOU 4034  O   VAL A 548    12001  13242  13468   -427   -851   -254       O  
ATOM   4035  CB  VAL A 548     -61.802 -10.478 -70.182  1.00 94.12           C  
ANISOU 4035  CB  VAL A 548    10991  12351  12418   -453   -829   -342       C  
ATOM   4036  CG1 VAL A 548     -60.831  -9.390 -70.609  1.00 91.50           C  
ANISOU 4036  CG1 VAL A 548    10693  11905  12164   -391   -865   -334       C  
ATOM   4037  CG2 VAL A 548     -62.298 -10.173 -68.781  1.00 92.67           C  
ANISOU 4037  CG2 VAL A 548    10760  12258  12190   -448   -820   -412       C  
ATOM   4038  N   ILE A 549     -62.673 -12.645 -72.446  1.00 97.93           N  
ANISOU 4038  N   ILE A 549    11502  12850  12856   -556   -801   -232       N  
ATOM   4039  CA  ILE A 549     -62.356 -13.480 -73.624  1.00 95.25           C  
ANISOU 4039  CA  ILE A 549    11209  12456  12525   -585   -802   -164       C  
ATOM   4040  C   ILE A 549     -63.163 -13.017 -74.833  1.00 93.70           C  
ANISOU 4040  C   ILE A 549    10980  12265  12357   -542   -814   -170       C  
ATOM   4041  O   ILE A 549     -62.628 -12.897 -75.936  1.00 92.42           O  
ANISOU 4041  O   ILE A 549    10851  12023  12238   -518   -829   -128       O  
ATOM   4042  CB  ILE A 549     -62.632 -14.991 -73.391  1.00 94.74           C  
ANISOU 4042  CB  ILE A 549    11173  12435  12385   -679   -782   -129       C  
ATOM   4043  CG1 ILE A 549     -61.894 -15.524 -72.153  1.00 92.39           C  
ANISOU 4043  CG1 ILE A 549    10919  12132  12050   -723   -777   -124       C  
ATOM   4044  CG2 ILE A 549     -62.299 -15.802 -74.643  1.00 92.77           C  
ANISOU 4044  CG2 ILE A 549    10974  12126  12147   -696   -791    -65       C  
ATOM   4045  CD1 ILE A 549     -60.553 -16.152 -72.430  1.00 91.11           C  
ANISOU 4045  CD1 ILE A 549    10838  11873  11905   -729   -794    -69       C  
ATOM   4046  N   LYS A 550     -64.447 -12.754 -74.607  1.00 92.99           N  
ANISOU 4046  N   LYS A 550    10820  12275  12235   -532   -807   -227       N  
ATOM   4047  CA  LYS A 550     -65.326 -12.231 -75.637  1.00 94.80           C  
ANISOU 4047  CA  LYS A 550    11011  12522  12487   -480   -824   -248       C  
ATOM   4048  C   LYS A 550     -64.965 -10.785 -75.979  1.00 96.34           C  
ANISOU 4048  C   LYS A 550    11213  12640  12750   -383   -863   -274       C  
ATOM   4049  O   LYS A 550     -64.903 -10.419 -77.154  1.00 94.80           O  
ANISOU 4049  O   LYS A 550    11042  12381  12597   -345   -886   -248       O  
ATOM   4050  CB  LYS A 550     -66.781 -12.339 -75.188  1.00 96.43           C  
ANISOU 4050  CB  LYS A 550    11132  12872  12632   -493   -808   -315       C  
ATOM   4051  CG  LYS A 550     -67.793 -11.775 -76.168  1.00 98.65           C  
ANISOU 4051  CG  LYS A 550    11365  13187  12931   -429   -830   -352       C  
ATOM   4052  CD  LYS A 550     -69.203 -12.107 -75.727  1.00102.74           C  
ANISOU 4052  CD  LYS A 550    11791  13869  13377   -459   -809   -416       C  
ATOM   4053  CE  LYS A 550     -70.208 -11.735 -76.801  1.00106.19           C  
ANISOU 4053  CE  LYS A 550    12180  14341  13825   -400   -832   -450       C  
ATOM   4054  NZ  LYS A 550     -71.504 -12.428 -76.568  1.00109.96           N  
ANISOU 4054  NZ  LYS A 550    12571  14983  14222   -461   -803   -494       N  
ATOM   4055  N   GLU A 551     -64.720  -9.974 -74.950  1.00 99.87           N  
ANISOU 4055  N   GLU A 551    11648  13091  13207   -347   -874   -322       N  
ATOM   4056  CA  GLU A 551     -64.356  -8.566 -75.129  1.00102.41           C  
ANISOU 4056  CA  GLU A 551    11988  13333  13589   -260   -920   -349       C  
ATOM   4057  C   GLU A 551     -63.183  -8.432 -76.103  1.00101.21           C  
ANISOU 4057  C   GLU A 551    11912  13052  13492   -266   -935   -274       C  
ATOM   4058  O   GLU A 551     -63.184  -7.555 -76.970  1.00101.79           O  
ANISOU 4058  O   GLU A 551    12009  13058  13607   -212   -974   -272       O  
ATOM   4059  CB  GLU A 551     -64.024  -7.927 -73.774  1.00106.08           C  
ANISOU 4059  CB  GLU A 551    12443  13812  14052   -237   -927   -401       C  
ATOM   4060  CG  GLU A 551     -63.582  -6.467 -73.830  1.00115.57           C  
ANISOU 4060  CG  GLU A 551    13675  14923  15311   -154   -982   -429       C  
ATOM   4061  CD  GLU A 551     -62.875  -6.007 -72.556  1.00123.89           C  
ANISOU 4061  CD  GLU A 551    14739  15963  16370   -149   -986   -458       C  
ATOM   4062  OE1 GLU A 551     -63.252  -6.470 -71.455  1.00129.41           O  
ANISOU 4062  OE1 GLU A 551    15391  16759  17018   -174   -956   -497       O  
ATOM   4063  OE2 GLU A 551     -61.938  -5.177 -72.647  1.00124.50           O  
ANISOU 4063  OE2 GLU A 551    14871  15935  16498   -124  -1021   -442       O  
ATOM   4064  N   TRP A 552     -62.211  -9.336 -75.967  1.00 99.21           N  
ANISOU 4064  N   TRP A 552    11695  12768  13229   -332   -907   -216       N  
ATOM   4065  CA  TRP A 552     -60.959  -9.302 -76.726  1.00 96.27           C  
ANISOU 4065  CA  TRP A 552    11384  12294  12899   -345   -916   -151       C  
ATOM   4066  C   TRP A 552     -61.089  -9.759 -78.180  1.00 94.61           C  
ANISOU 4066  C   TRP A 552    11193  12057  12696   -354   -916   -100       C  
ATOM   4067  O   TRP A 552     -60.551  -9.116 -79.082  1.00 94.08           O  
ANISOU 4067  O   TRP A 552    11161  11914  12671   -332   -939    -70       O  
ATOM   4068  CB  TRP A 552     -59.889 -10.118 -75.998  1.00 94.85           C  
ANISOU 4068  CB  TRP A 552    11232  12104  12702   -400   -892   -121       C  
ATOM   4069  CG  TRP A 552     -59.357  -9.444 -74.765  1.00 95.64           C  
ANISOU 4069  CG  TRP A 552    11330  12196  12812   -384   -900   -160       C  
ATOM   4070  CD1 TRP A 552     -59.809  -8.287 -74.204  1.00 96.13           C  
ANISOU 4070  CD1 TRP A 552    11368  12265  12891   -329   -925   -220       C  
ATOM   4071  CD2 TRP A 552     -58.289  -9.903 -73.926  1.00 97.36           C  
ANISOU 4071  CD2 TRP A 552    11572  12398  13019   -419   -888   -146       C  
ATOM   4072  NE1 TRP A 552     -59.082  -7.986 -73.081  1.00 97.81           N  
ANISOU 4072  NE1 TRP A 552    11589  12466  13107   -331   -927   -242       N  
ATOM   4073  CE2 TRP A 552     -58.145  -8.964 -72.883  1.00 98.26           C  
ANISOU 4073  CE2 TRP A 552    11675  12510  13148   -387   -903   -197       C  
ATOM   4074  CE3 TRP A 552     -57.436 -11.016 -73.957  1.00 97.75           C  
ANISOU 4074  CE3 TRP A 552    11657  12434  13047   -467   -872   -100       C  
ATOM   4075  CZ2 TRP A 552     -57.184  -9.101 -71.878  1.00 99.68           C  
ANISOU 4075  CZ2 TRP A 552    11873  12677  13323   -406   -899   -201       C  
ATOM   4076  CZ3 TRP A 552     -56.479 -11.152 -72.959  1.00 97.91           C  
ANISOU 4076  CZ3 TRP A 552    11697  12442  13061   -481   -871   -107       C  
ATOM   4077  CH2 TRP A 552     -56.363 -10.198 -71.933  1.00 99.49           C  
ANISOU 4077  CH2 TRP A 552    11880  12641  13278   -453   -882   -155       C  
ATOM   4078  N   GLY A 553     -61.800 -10.863 -78.399  1.00 93.33           N  
ANISOU 4078  N   GLY A 553    11010  11958  12490   -392   -891    -88       N  
ATOM   4079  CA  GLY A 553     -62.015 -11.400 -79.745  1.00 92.92           C  
ANISOU 4079  CA  GLY A 553    10974  11889  12440   -402   -891    -43       C  
ATOM   4080  C   GLY A 553     -62.976 -10.589 -80.601  1.00 94.65           C  
ANISOU 4080  C   GLY A 553    11172  12111  12680   -343   -918    -68       C  
ATOM   4081  O   GLY A 553     -63.006 -10.743 -81.823  1.00 93.29           O  
ANISOU 4081  O   GLY A 553    11021  11904  12521   -338   -926    -29       O  
ATOM   4082  N   THR A 554     -63.759  -9.725 -79.956  1.00 97.38           N  
ANISOU 4082  N   THR A 554    11475  12498  13025   -293   -936   -138       N  
ATOM   4083  CA  THR A 554     -64.758  -8.890 -80.629  1.00 97.25           C  
ANISOU 4083  CA  THR A 554    11436  12490  13022   -223   -972   -180       C  
ATOM   4084  C   THR A 554     -64.269  -7.452 -80.806  1.00 98.77           C  
ANISOU 4084  C   THR A 554    11673  12589  13266   -157  -1023   -192       C  
ATOM   4085  O   THR A 554     -64.791  -6.713 -81.642  1.00 98.02           O  
ANISOU 4085  O   THR A 554    11592  12461  13190    -98  -1065   -207       O  
ATOM   4086  CB  THR A 554     -66.071  -8.862 -79.829  1.00 96.94           C  
ANISOU 4086  CB  THR A 554    11317  12574  12941   -199   -968   -263       C  
ATOM   4087  OG1 THR A 554     -66.369 -10.179 -79.358  1.00 96.12           O  
ANISOU 4087  OG1 THR A 554    11181  12557  12781   -282   -920   -249       O  
ATOM   4088  CG2 THR A 554     -67.219  -8.372 -80.687  1.00 99.46           C  
ANISOU 4088  CG2 THR A 554    11604  12924  13261   -133  -1002   -304       C  
ATOM   4089  N   GLY A 555     -63.263  -7.072 -80.021  1.00101.15           N  
ANISOU 4089  N   GLY A 555    12002  12844  13586   -171  -1023   -186       N  
ATOM   4090  CA  GLY A 555     -62.721  -5.712 -80.022  1.00104.99           C  
ANISOU 4090  CA  GLY A 555    12537  13238  14115   -123  -1074   -198       C  
ATOM   4091  C   GLY A 555     -61.972  -5.275 -81.271  1.00106.58           C  
ANISOU 4091  C   GLY A 555    12809  13333  14351   -132  -1099   -132       C  
ATOM   4092  O   GLY A 555     -62.022  -5.935 -82.314  1.00104.84           O  
ANISOU 4092  O   GLY A 555    12597  13112  14125   -158  -1082    -83       O  
ATOM   4093  N   ARG A 556     -61.271  -4.148 -81.149  1.00109.76           N  
ANISOU 4093  N   ARG A 556    13266  13649  14787   -115  -1141   -132       N  
ATOM   4094  CA  ARG A 556     -60.556  -3.517 -82.260  1.00113.09           C  
ANISOU 4094  CA  ARG A 556    13763  13967  15236   -130  -1172    -74       C  
ATOM   4095  C   ARG A 556     -59.528  -4.405 -82.950  1.00110.09           C  
ANISOU 4095  C   ARG A 556    13396  13578  14852   -210  -1126      5       C  
ATOM   4096  O   ARG A 556     -59.192  -4.176 -84.110  1.00111.21           O  
ANISOU 4096  O   ARG A 556    13584  13665  15004   -227  -1140     56       O  
ATOM   4097  CB  ARG A 556     -59.867  -2.236 -81.788  1.00122.05           C  
ANISOU 4097  CB  ARG A 556    14956  15017  16400   -118  -1223    -87       C  
ATOM   4098  CG  ARG A 556     -60.633  -0.966 -82.107  1.00136.67           C  
ANISOU 4098  CG  ARG A 556    16856  16807  18264    -37  -1304   -130       C  
ATOM   4099  CD  ARG A 556     -59.765   0.262 -81.880  1.00148.66           C  
ANISOU 4099  CD  ARG A 556    18456  18217  19809    -46  -1360   -123       C  
ATOM   4100  NE  ARG A 556     -60.182   1.386 -82.718  1.00159.47           N  
ANISOU 4100  NE  ARG A 556    19909  19491  21188      3  -1445   -126       N  
ATOM   4101  CZ  ARG A 556     -59.732   1.615 -83.951  1.00164.19           C  
ANISOU 4101  CZ  ARG A 556    20578  20014  21790    -42  -1462    -55       C  
ATOM   4102  NH1 ARG A 556     -58.842   0.798 -84.509  1.00162.26           N  
ANISOU 4102  NH1 ARG A 556    20321  19789  21540   -134  -1397     20       N  
ATOM   4103  NH2 ARG A 556     -60.174   2.668 -84.629  1.00168.29           N  
ANISOU 4103  NH2 ARG A 556    21185  20442  22313      7  -1547    -63       N  
ATOM   4104  N   ASP A 557     -59.028  -5.410 -82.242  1.00107.51           N  
ANISOU 4104  N   ASP A 557    13031  13307  14508   -255  -1074     13       N  
ATOM   4105  CA  ASP A 557     -57.922  -6.209 -82.755  1.00106.29           C  
ANISOU 4105  CA  ASP A 557    12889  13147  14348   -319  -1038     77       C  
ATOM   4106  C   ASP A 557     -58.220  -7.704 -82.885  1.00101.56           C  
ANISOU 4106  C   ASP A 557    12253  12619  13714   -343   -993     93       C  
ATOM   4107  O   ASP A 557     -57.338  -8.492 -83.246  1.00100.56           O  
ANISOU 4107  O   ASP A 557    12135  12496  13578   -386   -968    136       O  
ATOM   4108  CB  ASP A 557     -56.662  -5.948 -81.925  1.00110.92           C  
ANISOU 4108  CB  ASP A 557    13488  13711  14947   -355  -1032     81       C  
ATOM   4109  CG  ASP A 557     -55.997  -4.629 -82.283  1.00114.36           C  
ANISOU 4109  CG  ASP A 557    13978  14060  15412   -363  -1074     96       C  
ATOM   4110  OD1 ASP A 557     -55.419  -4.540 -83.393  1.00114.62           O  
ANISOU 4110  OD1 ASP A 557    14043  14058  15446   -399  -1075    150       O  
ATOM   4111  OD2 ASP A 557     -56.055  -3.684 -81.462  1.00115.84           O  
ANISOU 4111  OD2 ASP A 557    14180  14216  15617   -336  -1108     55       O  
ATOM   4112  N   THR A 558     -59.469  -8.075 -82.606  1.00 97.34           N  
ANISOU 4112  N   THR A 558    11680  12145  13159   -316   -989     54       N  
ATOM   4113  CA  THR A 558     -59.962  -9.442 -82.789  1.00 93.94           C  
ANISOU 4113  CA  THR A 558    11222  11778  12691   -343   -956     68       C  
ATOM   4114  C   THR A 558     -58.921 -10.495 -82.384  1.00 92.52           C  
ANISOU 4114  C   THR A 558    11052  11608  12491   -396   -925    100       C  
ATOM   4115  O   THR A 558     -58.461 -11.289 -83.206  1.00 93.06           O  
ANISOU 4115  O   THR A 558    11140  11671  12549   -421   -913    145       O  
ATOM   4116  CB  THR A 558     -60.461  -9.673 -84.235  1.00 94.07           C  
ANISOU 4116  CB  THR A 558    11250  11784  12707   -334   -963    101       C  
ATOM   4117  OG1 THR A 558     -59.417  -9.382 -85.169  1.00 94.03           O  
ANISOU 4117  OG1 THR A 558    11290  11714  12723   -350   -970    155       O  
ATOM   4118  CG2 THR A 558     -61.632  -8.767 -84.548  1.00 96.10           C  
ANISOU 4118  CG2 THR A 558    11495  12043  12976   -273   -999     59       C  
ATOM   4119  N   LEU A 559     -58.556 -10.478 -81.106  1.00 90.94           N  
ANISOU 4119  N   LEU A 559    10843  11426  12285   -407   -916     70       N  
ATOM   4120  CA  LEU A 559     -57.520 -11.355 -80.569  1.00 89.96           C  
ANISOU 4120  CA  LEU A 559    10734  11306  12141   -446   -897     91       C  
ATOM   4121  C   LEU A 559     -57.943 -12.822 -80.500  1.00 93.76           C  
ANISOU 4121  C   LEU A 559    11215  11837  12572   -480   -878    103       C  
ATOM   4122  O   LEU A 559     -59.091 -13.135 -80.160  1.00 95.16           O  
ANISOU 4122  O   LEU A 559    11366  12068  12721   -486   -871     78       O  
ATOM   4123  CB  LEU A 559     -57.109 -10.887 -79.171  1.00 87.47           C  
ANISOU 4123  CB  LEU A 559    10410  10994  11829   -445   -898     52       C  
ATOM   4124  CG  LEU A 559     -56.599  -9.464 -78.947  1.00 85.83           C  
ANISOU 4124  CG  LEU A 559    10211  10734  11666   -419   -923     33       C  
ATOM   4125  CD1 LEU A 559     -56.270  -9.255 -77.479  1.00 84.90           C  
ANISOU 4125  CD1 LEU A 559    10083  10631  11543   -419   -921     -7       C  
ATOM   4126  CD2 LEU A 559     -55.383  -9.170 -79.806  1.00 86.05           C  
ANISOU 4126  CD2 LEU A 559    10269  10706  11719   -437   -929     79       C  
ATOM   4127  N   ARG A 560     -57.009 -13.720 -80.812  1.00 97.43           N  
ANISOU 4127  N   ARG A 560    11710  12287  13021   -503   -873    139       N  
ATOM   4128  CA  ARG A 560     -57.249 -15.161 -80.674  1.00102.30           C  
ANISOU 4128  CA  ARG A 560    12347  12936  13587   -536   -866    153       C  
ATOM   4129  C   ARG A 560     -56.777 -15.672 -79.307  1.00 99.46           C  
ANISOU 4129  C   ARG A 560    12003  12590  13196   -560   -864    133       C  
ATOM   4130  O   ARG A 560     -55.608 -16.029 -79.136  1.00 98.77           O  
ANISOU 4130  O   ARG A 560    11943  12478  13105   -560   -872    144       O  
ATOM   4131  CB  ARG A 560     -56.574 -15.950 -81.803  1.00108.55           C  
ANISOU 4131  CB  ARG A 560    13170  13704  14370   -537   -874    196       C  
ATOM   4132  CG  ARG A 560     -57.057 -17.389 -81.904  1.00116.10           C  
ANISOU 4132  CG  ARG A 560    14157  14683  15273   -568   -878    212       C  
ATOM   4133  CD  ARG A 560     -55.892 -18.366 -81.943  1.00125.13           C  
ANISOU 4133  CD  ARG A 560    15347  15806  16391   -568   -895    230       C  
ATOM   4134  NE  ARG A 560     -56.307 -19.699 -81.502  1.00133.87           N  
ANISOU 4134  NE  ARG A 560    16500  16924  17437   -604   -909    235       N  
ATOM   4135  CZ  ARG A 560     -55.477 -20.681 -81.149  1.00137.81           C  
ANISOU 4135  CZ  ARG A 560    17055  17407  17900   -606   -934    239       C  
ATOM   4136  NH1 ARG A 560     -54.158 -20.500 -81.174  1.00138.19           N  
ANISOU 4136  NH1 ARG A 560    17106  17436  17964   -569   -944    232       N  
ATOM   4137  NH2 ARG A 560     -55.972 -21.853 -80.764  1.00137.33           N  
ANISOU 4137  NH2 ARG A 560    17049  17348  17779   -647   -954    247       N  
ATOM   4138  N   CYS A 561     -57.703 -15.713 -78.350  1.00 96.82           N  
ANISOU 4138  N   CYS A 561    11648  12303  12833   -580   -854    102       N  
ATOM   4139  CA  CYS A 561     -57.399 -16.075 -76.966  1.00 93.99           C  
ANISOU 4139  CA  CYS A 561    11305  11963  12442   -606   -852     80       C  
ATOM   4140  C   CYS A 561     -57.119 -17.554 -76.766  1.00 91.90           C  
ANISOU 4140  C   CYS A 561    11099  11698  12120   -648   -861    106       C  
ATOM   4141  O   CYS A 561     -57.667 -18.398 -77.462  1.00 93.83           O  
ANISOU 4141  O   CYS A 561    11364  11952  12335   -673   -866    132       O  
ATOM   4142  CB  CYS A 561     -58.550 -15.666 -76.055  1.00 95.90           C  
ANISOU 4142  CB  CYS A 561    11504  12269  12663   -618   -837     36       C  
ATOM   4143  SG  CYS A 561     -58.888 -13.894 -76.064  1.00 99.83           S  
ANISOU 4143  SG  CYS A 561    11944  12763  13222   -555   -841     -8       S  
ATOM   4144  N   LEU A 562     -56.251 -17.848 -75.808  1.00 90.70           N  
ANISOU 4144  N   LEU A 562    10980  11532  11950   -654   -871     97       N  
ATOM   4145  CA  LEU A 562     -55.997 -19.207 -75.347  1.00 91.72           C  
ANISOU 4145  CA  LEU A 562    11178  11655  12016   -693   -891    113       C  
ATOM   4146  C   LEU A 562     -56.118 -19.191 -73.829  1.00 94.07           C  
ANISOU 4146  C   LEU A 562    11483  11981  12278   -723   -885     84       C  
ATOM   4147  O   LEU A 562     -55.662 -18.247 -73.176  1.00 97.01           O  
ANISOU 4147  O   LEU A 562    11821  12351  12684   -693   -877     53       O  
ATOM   4148  CB  LEU A 562     -54.577 -19.648 -75.715  1.00 90.51           C  
ANISOU 4148  CB  LEU A 562    11068  11450  11870   -657   -919    127       C  
ATOM   4149  CG  LEU A 562     -54.134 -19.817 -77.166  1.00 89.36           C  
ANISOU 4149  CG  LEU A 562    10923  11279  11748   -624   -929    154       C  
ATOM   4150  CD1 LEU A 562     -52.678 -19.413 -77.327  1.00 88.85           C  
ANISOU 4150  CD1 LEU A 562    10850  11191  11717   -578   -939    145       C  
ATOM   4151  CD2 LEU A 562     -54.336 -21.255 -77.606  1.00 89.86           C  
ANISOU 4151  CD2 LEU A 562    11055  11331  11756   -646   -958    181       C  
ATOM   4152  N   ALA A 563     -56.720 -20.224 -73.253  1.00 92.54           N  
ANISOU 4152  N   ALA A 563    11336  11812  12011   -787   -892     93       N  
ATOM   4153  CA  ALA A 563     -56.703 -20.346 -71.800  1.00 91.92           C  
ANISOU 4153  CA  ALA A 563    11278  11758  11888   -821   -891     70       C  
ATOM   4154  C   ALA A 563     -55.649 -21.358 -71.360  1.00 91.51           C  
ANISOU 4154  C   ALA A 563    11321  11652  11796   -825   -932     85       C  
ATOM   4155  O   ALA A 563     -55.537 -22.454 -71.920  1.00 91.58           O  
ANISOU 4155  O   ALA A 563    11399  11627  11767   -842   -964    118       O  
ATOM   4156  CB  ALA A 563     -58.080 -20.698 -71.259  1.00 92.64           C  
ANISOU 4156  CB  ALA A 563    11356  11926  11916   -900   -869     64       C  
ATOM   4157  N   LEU A 564     -54.865 -20.972 -70.364  1.00 90.71           N  
ANISOU 4157  N   LEU A 564    11224  11539  11701   -801   -938     58       N  
ATOM   4158  CA  LEU A 564     -53.785 -21.808 -69.870  1.00 91.58           C  
ANISOU 4158  CA  LEU A 564    11419  11598  11775   -790   -982     62       C  
ATOM   4159  C   LEU A 564     -54.140 -22.332 -68.481  1.00 94.32           C  
ANISOU 4159  C   LEU A 564    11821  11968  12048   -853   -990     55       C  
ATOM   4160  O   LEU A 564     -54.488 -21.555 -67.579  1.00 94.08           O  
ANISOU 4160  O   LEU A 564    11739  11982  12022   -864   -959     24       O  
ATOM   4161  CB  LEU A 564     -52.483 -21.008 -69.843  1.00 91.96           C  
ANISOU 4161  CB  LEU A 564    11435  11618  11887   -714   -988     36       C  
ATOM   4162  CG  LEU A 564     -52.174 -20.245 -71.137  1.00 92.30           C  
ANISOU 4162  CG  LEU A 564    11413  11652  12004   -664   -973     42       C  
ATOM   4163  CD1 LEU A 564     -51.663 -18.837 -70.868  1.00 91.37           C  
ANISOU 4163  CD1 LEU A 564    11223  11539  11953   -625   -951     11       C  
ATOM   4164  CD2 LEU A 564     -51.208 -21.027 -72.013  1.00 92.78           C  
ANISOU 4164  CD2 LEU A 564    11517  11674  12059   -626  -1011     58       C  
ATOM   4165  N   ALA A 565     -54.063 -23.654 -68.321  1.00 95.60           N  
ANISOU 4165  N   ALA A 565    12093  12096  12135   -894  -1035     81       N  
ATOM   4166  CA  ALA A 565     -54.472 -24.322 -67.087  1.00 96.14           C  
ANISOU 4166  CA  ALA A 565    12232  12179  12115   -972  -1048     85       C  
ATOM   4167  C   ALA A 565     -53.497 -25.421 -66.685  1.00 98.28           C  
ANISOU 4167  C   ALA A 565    12634  12375  12332   -960  -1119     95       C  
ATOM   4168  O   ALA A 565     -52.740 -25.922 -67.519  1.00 97.33           O  
ANISOU 4168  O   ALA A 565    12555  12198  12227   -903  -1162    103       O  
ATOM   4169  CB  ALA A 565     -55.869 -24.899 -67.250  1.00 96.11           C  
ANISOU 4169  CB  ALA A 565    12240  12225  12049  -1074  -1030    114       C  
ATOM   4170  N   THR A 566     -53.514 -25.785 -65.401  1.00102.46           N  
ANISOU 4170  N   THR A 566    13229  12907  12792  -1010  -1136     89       N  
ATOM   4171  CA  THR A 566     -52.735 -26.928 -64.908  1.00104.74           C  
ANISOU 4171  CA  THR A 566    13662  13120  13011  -1008  -1214     99       C  
ATOM   4172  C   THR A 566     -53.637 -27.967 -64.248  1.00108.11           C  
ANISOU 4172  C   THR A 566    14199  13551  13324  -1134  -1237    136       C  
ATOM   4173  O   THR A 566     -54.603 -27.617 -63.563  1.00108.31           O  
ANISOU 4173  O   THR A 566    14180  13653  13317  -1218  -1186    136       O  
ATOM   4174  CB  THR A 566     -51.626 -26.536 -63.896  1.00101.75           C  
ANISOU 4174  CB  THR A 566    13293  12721  12645   -945  -1234     58       C  
ATOM   4175  OG1 THR A 566     -52.198 -26.322 -62.604  1.00101.61           O  
ANISOU 4175  OG1 THR A 566    13279  12749  12576  -1018  -1208     51       O  
ATOM   4176  CG2 THR A 566     -50.894 -25.287 -64.323  1.00100.68           C  
ANISOU 4176  CG2 THR A 566    13032  12602  12617   -849  -1198     20       C  
ATOM   4177  N   ARG A 567     -53.327 -29.241 -64.474  1.00111.77           N  
ANISOU 4177  N   ARG A 567    14807  13935  13723  -1147  -1316    165       N  
ATOM   4178  CA  ARG A 567     -53.869 -30.300 -63.646  1.00115.18           C  
ANISOU 4178  CA  ARG A 567    15380  14348  14036  -1264  -1359    199       C  
ATOM   4179  C   ARG A 567     -52.900 -30.437 -62.488  1.00117.32           C  
ANISOU 4179  C   ARG A 567    15730  14573  14273  -1226  -1407    174       C  
ATOM   4180  O   ARG A 567     -51.756 -30.869 -62.668  1.00117.10           O  
ANISOU 4180  O   ARG A 567    15774  14463  14254  -1129  -1479    156       O  
ATOM   4181  CB  ARG A 567     -54.013 -31.624 -64.406  1.00117.88           C  
ANISOU 4181  CB  ARG A 567    15857  14613  14317  -1298  -1434    242       C  
ATOM   4182  CG  ARG A 567     -54.713 -32.706 -63.591  1.00123.83           C  
ANISOU 4182  CG  ARG A 567    16764  15348  14939  -1444  -1478    286       C  
ATOM   4183  CD  ARG A 567     -55.075 -33.942 -64.404  1.00126.47           C  
ANISOU 4183  CD  ARG A 567    17226  15612  15212  -1497  -1547    333       C  
ATOM   4184  NE  ARG A 567     -56.023 -34.795 -63.679  1.00127.57           N  
ANISOU 4184  NE  ARG A 567    17485  15759  15225  -1670  -1568    380       N  
ATOM   4185  CZ  ARG A 567     -56.779 -35.741 -64.235  1.00127.27           C  
ANISOU 4185  CZ  ARG A 567    17540  15696  15121  -1771  -1605    429       C  
ATOM   4186  NH1 ARG A 567     -56.716 -35.989 -65.536  1.00126.40           N  
ANISOU 4186  NH1 ARG A 567    17418  15546  15059  -1709  -1627    435       N  
ATOM   4187  NH2 ARG A 567     -57.610 -36.446 -63.486  1.00129.03           N  
ANISOU 4187  NH2 ARG A 567    17867  15933  15222  -1942  -1620    472       N  
ATOM   4188  N   ASP A 568     -53.361 -30.029 -61.309  1.00119.33           N  
ANISOU 4188  N   ASP A 568    15962  14888  14489  -1296  -1366    166       N  
ATOM   4189  CA  ASP A 568     -52.556 -30.077 -60.095  1.00119.68           C  
ANISOU 4189  CA  ASP A 568    16075  14899  14497  -1270  -1404    141       C  
ATOM   4190  C   ASP A 568     -52.261 -31.512 -59.675  1.00123.82           C  
ANISOU 4190  C   ASP A 568    16811  15326  14909  -1315  -1510    173       C  
ATOM   4191  O   ASP A 568     -51.119 -31.845 -59.354  1.00124.41           O  
ANISOU 4191  O   ASP A 568    16969  15322  14977  -1226  -1583    148       O  
ATOM   4192  CB  ASP A 568     -53.250 -29.307 -58.975  1.00116.04           C  
ANISOU 4192  CB  ASP A 568    15537  14536  14014  -1342  -1333    125       C  
ATOM   4193  CG  ASP A 568     -53.209 -27.814 -59.194  1.00112.92           C  
ANISOU 4193  CG  ASP A 568    14955  14215  13734  -1264  -1252     79       C  
ATOM   4194  OD1 ASP A 568     -52.098 -27.272 -59.373  1.00112.07           O  
ANISOU 4194  OD1 ASP A 568    14808  14067  13705  -1144  -1267     43       O  
ATOM   4195  OD2 ASP A 568     -54.283 -27.181 -59.186  1.00111.14           O  
ANISOU 4195  OD2 ASP A 568    14624  14087  13516  -1323  -1178     76       O  
ATOM   4196  N   THR A 569     -53.290 -32.356 -59.691  1.00126.88           N  
ANISOU 4196  N   THR A 569    17286  15717  15203  -1453  -1521    226       N  
ATOM   4197  CA  THR A 569     -53.117 -33.778 -59.425  1.00129.34           C  
ANISOU 4197  CA  THR A 569    17817  15925  15402  -1508  -1630    264       C  
ATOM   4198  C   THR A 569     -53.376 -34.583 -60.698  1.00128.93           C  
ANISOU 4198  C   THR A 569    17823  15817  15346  -1513  -1676    299       C  
ATOM   4199  O   THR A 569     -54.526 -34.884 -61.032  1.00129.06           O  
ANISOU 4199  O   THR A 569    17837  15878  15320  -1638  -1644    341       O  
ATOM   4200  CB  THR A 569     -54.019 -34.270 -58.278  1.00132.45           C  
ANISOU 4200  CB  THR A 569    18304  16353  15666  -1683  -1627    304       C  
ATOM   4201  OG1 THR A 569     -54.092 -33.265 -57.260  1.00134.48           O  
ANISOU 4201  OG1 THR A 569    18451  16703  15943  -1688  -1552    269       O  
ATOM   4202  CG2 THR A 569     -53.460 -35.559 -57.680  1.00133.75           C  
ANISOU 4202  CG2 THR A 569    18710  16389  15717  -1710  -1755    330       C  
ATOM   4203  N   PRO A 570     -52.298 -34.918 -61.424  1.00128.33           N  
ANISOU 4203  N   PRO A 570    17792  15653  15314  -1374  -1749    275       N  
ATOM   4204  CA  PRO A 570     -52.394 -35.725 -62.630  1.00129.18           C  
ANISOU 4204  CA  PRO A 570    17965  15698  15416  -1358  -1805    300       C  
ATOM   4205  C   PRO A 570     -52.450 -37.215 -62.309  1.00130.31           C  
ANISOU 4205  C   PRO A 570    18352  15729  15429  -1432  -1928    341       C  
ATOM   4206  O   PRO A 570     -51.904 -37.635 -61.286  1.00133.01           O  
ANISOU 4206  O   PRO A 570    18821  16013  15703  -1431  -1996    334       O  
ATOM   4207  CB  PRO A 570     -51.096 -35.395 -63.364  1.00128.95           C  
ANISOU 4207  CB  PRO A 570    17878  15634  15480  -1169  -1834    245       C  
ATOM   4208  CG  PRO A 570     -50.123 -35.088 -62.282  1.00128.14           C  
ANISOU 4208  CG  PRO A 570    17793  15517  15375  -1100  -1859    201       C  
ATOM   4209  CD  PRO A 570     -50.914 -34.482 -61.158  1.00127.13           C  
ANISOU 4209  CD  PRO A 570    17615  15468  15221  -1218  -1780    215       C  
ATOM   4210  N   PRO A 571     -53.105 -38.013 -63.174  1.00130.08           N  
ANISOU 4210  N   PRO A 571    18395  15665  15363  -1497  -1963    385       N  
ATOM   4211  CA  PRO A 571     -53.122 -39.465 -63.016  1.00134.11           C  
ANISOU 4211  CA  PRO A 571    19151  16052  15750  -1561  -2095    425       C  
ATOM   4212  C   PRO A 571     -51.723 -40.066 -63.086  1.00138.29           C  
ANISOU 4212  C   PRO A 571    19808  16461  16276  -1396  -2223    381       C  
ATOM   4213  O   PRO A 571     -50.803 -39.431 -63.605  1.00136.81           O  
ANISOU 4213  O   PRO A 571    19500  16292  16187  -1233  -2205    323       O  
ATOM   4214  CB  PRO A 571     -53.955 -39.942 -64.215  1.00132.65           C  
ANISOU 4214  CB  PRO A 571    18969  15866  15566  -1620  -2094    465       C  
ATOM   4215  CG  PRO A 571     -53.925 -38.816 -65.189  1.00128.90           C  
ANISOU 4215  CG  PRO A 571    18262  15484  15228  -1521  -1990    430       C  
ATOM   4216  CD  PRO A 571     -53.912 -37.590 -64.329  1.00129.28           C  
ANISOU 4216  CD  PRO A 571    18155  15635  15328  -1519  -1885    400       C  
ATOM   4217  N   LYS A 572     -51.572 -41.277 -62.554  1.00147.15           N  
ANISOU 4217  N   LYS A 572    21171  17463  17277  -1443  -2354    407       N  
ATOM   4218  CA  LYS A 572     -50.314 -42.015 -62.631  1.00153.72           C  
ANISOU 4218  CA  LYS A 572    22150  18170  18085  -1286  -2498    363       C  
ATOM   4219  C   LYS A 572     -49.816 -42.114 -64.071  1.00156.98           C  
ANISOU 4219  C   LYS A 572    22504  18566  18573  -1141  -2525    328       C  
ATOM   4220  O   LYS A 572     -50.604 -42.264 -65.009  1.00155.80           O  
ANISOU 4220  O   LYS A 572    22320  18436  18438  -1202  -2494    364       O  
ATOM   4221  CB  LYS A 572     -50.469 -43.417 -62.036  1.00156.60           C  
ANISOU 4221  CB  LYS A 572    22807  18396  18298  -1380  -2645    408       C  
ATOM   4222  CG  LYS A 572     -49.964 -43.572 -60.611  1.00155.81           C  
ANISOU 4222  CG  LYS A 572    22828  18249  18121  -1392  -2701    398       C  
ATOM   4223  CD  LYS A 572     -50.119 -45.016 -60.155  1.00158.76           C  
ANISOU 4223  CD  LYS A 572    23510  18470  18338  -1484  -2861    446       C  
ATOM   4224  CE  LYS A 572     -48.995 -45.441 -59.224  1.00159.93           C  
ANISOU 4224  CE  LYS A 572    23820  18516  18428  -1377  -2986    402       C  
ATOM   4225  NZ  LYS A 572     -49.055 -44.752 -57.907  1.00160.82           N  
ANISOU 4225  NZ  LYS A 572    23878  18698  18525  -1446  -2911    403       N  
ATOM   4226  N   ARG A 573     -48.498 -42.029 -64.227  1.00162.26           N  
ANISOU 4226  N   ARG A 573    23159  19207  19286   -949  -2585    253       N  
ATOM   4227  CA  ARG A 573     -47.835 -42.080 -65.529  1.00161.91           C  
ANISOU 4227  CA  ARG A 573    23050  19160  19309   -792  -2614    206       C  
ATOM   4228  C   ARG A 573     -48.233 -43.311 -66.352  1.00163.72           C  
ANISOU 4228  C   ARG A 573    23448  19288  19468   -817  -2723    240       C  
ATOM   4229  O   ARG A 573     -48.167 -43.289 -67.585  1.00162.11           O  
ANISOU 4229  O   ARG A 573    23168  19106  19321   -741  -2714    224       O  
ATOM   4230  CB  ARG A 573     -46.321 -42.037 -65.324  1.00160.18           C  
ANISOU 4230  CB  ARG A 573    22833  18917  19110   -596  -2689    117       C  
ATOM   4231  CG  ARG A 573     -45.539 -41.513 -66.510  1.00160.47           C  
ANISOU 4231  CG  ARG A 573    22703  19020  19248   -433  -2659     53       C  
ATOM   4232  CD  ARG A 573     -44.124 -41.162 -66.093  1.00162.21           C  
ANISOU 4232  CD  ARG A 573    22874  19260  19496   -266  -2695    -37       C  
ATOM   4233  NE  ARG A 573     -43.269 -40.910 -67.249  1.00166.56           N  
ANISOU 4233  NE  ARG A 573    23299  19866  20118   -107  -2695   -104       N  
ATOM   4234  CZ  ARG A 573     -41.984 -40.575 -67.178  1.00169.42           C  
ANISOU 4234  CZ  ARG A 573    23587  20271  20513     50  -2721   -193       C  
ATOM   4235  NH1 ARG A 573     -41.384 -40.445 -66.000  1.00172.41           N  
ANISOU 4235  NH1 ARG A 573    24006  20636  20866     76  -2752   -227       N  
ATOM   4236  NH2 ARG A 573     -41.295 -40.370 -68.294  1.00170.46           N  
ANISOU 4236  NH2 ARG A 573    23599  20466  20699    177  -2715   -250       N  
ATOM   4237  N   GLU A 574     -48.650 -44.370 -65.656  1.00167.53           N  
ANISOU 4237  N   GLU A 574    24167  19661  19824   -927  -2828    288       N  
ATOM   4238  CA  GLU A 574     -49.111 -45.610 -66.284  1.00170.30           C  
ANISOU 4238  CA  GLU A 574    24712  19901  20092   -976  -2944    328       C  
ATOM   4239  C   GLU A 574     -50.620 -45.839 -66.118  1.00168.58           C  
ANISOU 4239  C   GLU A 574    24538  19699  19815  -1218  -2889    424       C  
ATOM   4240  O   GLU A 574     -51.077 -46.978 -65.990  1.00172.78           O  
ANISOU 4240  O   GLU A 574    25297  20118  20232  -1321  -3002    474       O  
ATOM   4241  CB  GLU A 574     -48.307 -46.820 -65.777  1.00176.18           C  
ANISOU 4241  CB  GLU A 574    25729  20485  20726   -900  -3142    303       C  
ATOM   4242  CG  GLU A 574     -48.282 -47.010 -64.263  1.00183.62           C  
ANISOU 4242  CG  GLU A 574    26809  21379  21577   -990  -3181    325       C  
ATOM   4243  CD  GLU A 574     -47.175 -46.228 -63.571  1.00187.83           C  
ANISOU 4243  CD  GLU A 574    27235  21964  22168   -847  -3153    248       C  
ATOM   4244  OE1 GLU A 574     -46.438 -45.479 -64.251  1.00187.25           O  
ANISOU 4244  OE1 GLU A 574    26968  21973  22205   -688  -3096    179       O  
ATOM   4245  OE2 GLU A 574     -47.040 -46.365 -62.335  1.00192.34           O  
ANISOU 4245  OE2 GLU A 574    27917  22494  22667   -900  -3191    257       O  
ATOM   4246  N   GLU A 575     -51.384 -44.750 -66.122  1.00162.86           N  
ANISOU 4246  N   GLU A 575    23597  19117  19165  -1307  -2720    445       N  
ATOM   4247  CA  GLU A 575     -52.844 -44.819 -66.134  1.00160.27           C  
ANISOU 4247  CA  GLU A 575    23259  18840  18795  -1522  -2649    523       C  
ATOM   4248  C   GLU A 575     -53.394 -44.150 -67.386  1.00154.92           C  
ANISOU 4248  C   GLU A 575    22378  18261  18222  -1504  -2540    522       C  
ATOM   4249  O   GLU A 575     -54.609 -43.988 -67.535  1.00152.85           O  
ANISOU 4249  O   GLU A 575    22054  18072  17949  -1662  -2459    573       O  
ATOM   4250  CB  GLU A 575     -53.429 -44.141 -64.897  1.00164.25           C  
ANISOU 4250  CB  GLU A 575    23695  19436  19275  -1662  -2547    547       C  
ATOM   4251  CG  GLU A 575     -53.410 -44.991 -63.638  1.00173.45           C  
ANISOU 4251  CG  GLU A 575    25093  20507  20299  -1770  -2647    581       C  
ATOM   4252  CD  GLU A 575     -54.054 -44.297 -62.448  1.00179.27           C  
ANISOU 4252  CD  GLU A 575    25750  21355  21010  -1915  -2538    605       C  
ATOM   4253  OE1 GLU A 575     -54.572 -43.167 -62.607  1.00176.87           O  
ANISOU 4253  OE1 GLU A 575    25208  21197  20794  -1932  -2387    593       O  
ATOM   4254  OE2 GLU A 575     -54.045 -44.887 -61.346  1.00185.67           O  
ANISOU 4254  OE2 GLU A 575    26738  22102  21704  -2010  -2607    633       O  
ATOM   4255  N   MET A 576     -52.487 -43.763 -68.281  1.00150.42           N  
ANISOU 4255  N   MET A 576    21702  17700  17748  -1311  -2541    461       N  
ATOM   4256  CA  MET A 576     -52.839 -43.005 -69.476  1.00149.27           C  
ANISOU 4256  CA  MET A 576    21354  17649  17711  -1271  -2437    452       C  
ATOM   4257  C   MET A 576     -52.345 -43.694 -70.738  1.00151.30           C  
ANISOU 4257  C   MET A 576    21670  17835  17980  -1146  -2530    429       C  
ATOM   4258  O   MET A 576     -51.179 -44.071 -70.825  1.00150.13           O  
ANISOU 4258  O   MET A 576    21594  17620  17828   -987  -2628    374       O  
ATOM   4259  CB  MET A 576     -52.234 -41.603 -69.413  1.00144.19           C  
ANISOU 4259  CB  MET A 576    20481  17116  17186  -1162  -2322    398       C  
ATOM   4260  CG  MET A 576     -52.577 -40.801 -68.169  1.00140.85           C  
ANISOU 4260  CG  MET A 576    19982  16769  16762  -1255  -2231    407       C  
ATOM   4261  SD  MET A 576     -51.380 -39.487 -67.893  1.00133.72           S  
ANISOU 4261  SD  MET A 576    18895  15938  15973  -1089  -2161    330       S  
ATOM   4262  CE  MET A 576     -51.615 -38.518 -69.379  1.00134.91           C  
ANISOU 4262  CE  MET A 576    18820  16185  16253  -1024  -2053    317       C  
ATOM   4263  N   VAL A 577     -53.234 -43.846 -71.716  1.00155.13           N  
ANISOU 4263  N   VAL A 577    22120  18342  18478  -1212  -2499    467       N  
ATOM   4264  CA  VAL A 577     -52.856 -44.398 -73.016  1.00157.98           C  
ANISOU 4264  CA  VAL A 577    22513  18652  18859  -1095  -2572    444       C  
ATOM   4265  C   VAL A 577     -52.239 -43.289 -73.892  1.00159.21           C  
ANISOU 4265  C   VAL A 577    22437  18909  19145   -944  -2476    389       C  
ATOM   4266  O   VAL A 577     -52.931 -42.377 -74.358  1.00159.56           O  
ANISOU 4266  O   VAL A 577    22302  19058  19265   -993  -2348    407       O  
ATOM   4267  CB  VAL A 577     -54.027 -45.187 -73.680  1.00159.41           C  
ANISOU 4267  CB  VAL A 577    22786  18796  18985  -1231  -2601    508       C  
ATOM   4268  CG1 VAL A 577     -55.247 -44.308 -73.949  1.00155.64           C  
ANISOU 4268  CG1 VAL A 577    22122  18448  18563  -1361  -2447    547       C  
ATOM   4269  CG2 VAL A 577     -53.564 -45.909 -74.940  1.00161.35           C  
ANISOU 4269  CG2 VAL A 577    23098  18970  19235  -1102  -2700    482       C  
ATOM   4270  N   LEU A 578     -50.924 -43.373 -74.089  1.00159.14           N  
ANISOU 4270  N   LEU A 578    22436  18871  19156   -762  -2544    320       N  
ATOM   4271  CA  LEU A 578     -50.133 -42.274 -74.660  1.00156.25           C  
ANISOU 4271  CA  LEU A 578    21860  18607  18902   -623  -2458    262       C  
ATOM   4272  C   LEU A 578     -50.081 -42.248 -76.192  1.00156.60           C  
ANISOU 4272  C   LEU A 578    21819  18680  18999   -538  -2447    247       C  
ATOM   4273  O   LEU A 578     -49.391 -41.408 -76.775  1.00157.96           O  
ANISOU 4273  O   LEU A 578    21826  18935  19255   -426  -2384    201       O  
ATOM   4274  CB  LEU A 578     -48.704 -42.292 -74.093  1.00158.17           C  
ANISOU 4274  CB  LEU A 578    22129  18827  19138   -472  -2526    188       C  
ATOM   4275  CG  LEU A 578     -48.474 -42.644 -72.615  1.00163.38           C  
ANISOU 4275  CG  LEU A 578    22927  19424  19724   -517  -2586    190       C  
ATOM   4276  CD1 LEU A 578     -46.995 -42.855 -72.314  1.00162.74           C  
ANISOU 4276  CD1 LEU A 578    22888  19314  19631   -339  -2680    104       C  
ATOM   4277  CD2 LEU A 578     -49.066 -41.597 -71.683  1.00165.91           C  
ANISOU 4277  CD2 LEU A 578    23128  19827  20081   -638  -2454    221       C  
ATOM   4278  N   ASP A 579     -50.803 -43.160 -76.839  1.00156.47           N  
ANISOU 4278  N   ASP A 579    21918  18599  18931   -595  -2510    287       N  
ATOM   4279  CA  ASP A 579     -50.820 -43.229 -78.300  1.00154.14           C  
ANISOU 4279  CA  ASP A 579    21560  18328  18678   -520  -2508    275       C  
ATOM   4280  C   ASP A 579     -52.236 -43.161 -78.874  1.00155.30           C  
ANISOU 4280  C   ASP A 579    21669  18501  18836   -665  -2440    344       C  
ATOM   4281  O   ASP A 579     -52.411 -43.019 -80.088  1.00157.63           O  
ANISOU 4281  O   ASP A 579    21883  18831  19177   -619  -2412    341       O  
ATOM   4282  CB  ASP A 579     -50.095 -44.486 -78.797  1.00154.51           C  
ANISOU 4282  CB  ASP A 579    21781  18269  18655   -398  -2674    235       C  
ATOM   4283  CG  ASP A 579     -50.947 -45.740 -78.689  1.00156.61           C  
ANISOU 4283  CG  ASP A 579    22270  18414  18820   -514  -2781    291       C  
ATOM   4284  OD1 ASP A 579     -51.468 -46.026 -77.592  1.00158.00           O  
ANISOU 4284  OD1 ASP A 579    22558  18542  18932   -650  -2798    337       O  
ATOM   4285  OD2 ASP A 579     -51.091 -46.446 -79.708  1.00159.88           O  
ANISOU 4285  OD2 ASP A 579    22750  18782  19213   -474  -2852    291       O  
ATOM   4286  N   ASP A 580     -53.237 -43.275 -78.003  1.00153.90           N  
ANISOU 4286  N   ASP A 580    21550  18312  18610   -839  -2414    402       N  
ATOM   4287  CA  ASP A 580     -54.633 -43.148 -78.417  1.00155.44           C  
ANISOU 4287  CA  ASP A 580    21696  18553  18811   -988  -2342    462       C  
ATOM   4288  C   ASP A 580     -55.130 -41.715 -78.223  1.00153.45           C  
ANISOU 4288  C   ASP A 580    21222  18433  18646  -1035  -2179    466       C  
ATOM   4289  O   ASP A 580     -55.327 -41.257 -77.095  1.00153.39           O  
ANISOU 4289  O   ASP A 580    21191  18461  18627  -1113  -2130    475       O  
ATOM   4290  CB  ASP A 580     -55.527 -44.151 -77.682  1.00159.15           C  
ANISOU 4290  CB  ASP A 580    22354  18946  19166  -1164  -2410    521       C  
ATOM   4291  CG  ASP A 580     -56.926 -44.234 -78.277  1.00163.74           C  
ANISOU 4291  CG  ASP A 580    22901  19570  19741  -1310  -2358    577       C  
ATOM   4292  OD1 ASP A 580     -57.708 -43.273 -78.110  1.00165.59           O  
ANISOU 4292  OD1 ASP A 580    22971  19920  20025  -1394  -2228    592       O  
ATOM   4293  OD2 ASP A 580     -57.246 -45.264 -78.907  1.00164.77           O  
ANISOU 4293  OD2 ASP A 580    23170  19619  19814  -1339  -2453    600       O  
ATOM   4294  N   SER A 581     -55.335 -41.029 -79.344  1.00151.43           N  
ANISOU 4294  N   SER A 581    20812  18249  18474   -985  -2104    459       N  
ATOM   4295  CA  SER A 581     -55.670 -39.604 -79.371  1.00147.91           C  
ANISOU 4295  CA  SER A 581    20154  17921  18120   -995  -1962    453       C  
ATOM   4296  C   SER A 581     -56.979 -39.251 -78.662  1.00145.12           C  
ANISOU 4296  C   SER A 581    19760  17630  17747  -1167  -1884    495       C  
ATOM   4297  O   SER A 581     -57.074 -38.212 -78.010  1.00139.69           O  
ANISOU 4297  O   SER A 581    18950  17021  17105  -1184  -1794    483       O  
ATOM   4298  CB  SER A 581     -55.704 -39.108 -80.823  1.00147.33           C  
ANISOU 4298  CB  SER A 581    19956  17896  18124   -915  -1916    443       C  
ATOM   4299  OG  SER A 581     -56.274 -37.815 -80.924  1.00145.11           O  
ANISOU 4299  OG  SER A 581    19493  17719  17922   -945  -1789    446       O  
ATOM   4300  N   SER A 582     -57.974 -40.126 -78.790  1.00148.28           N  
ANISOU 4300  N   SER A 582    20262  18000  18075  -1292  -1924    541       N  
ATOM   4301  CA  SER A 582     -59.343 -39.833 -78.359  1.00149.55           C  
ANISOU 4301  CA  SER A 582    20366  18243  18213  -1459  -1848    576       C  
ATOM   4302  C   SER A 582     -59.523 -39.797 -76.848  1.00147.24           C  
ANISOU 4302  C   SER A 582    20117  17967  17860  -1566  -1834    586       C  
ATOM   4303  O   SER A 582     -60.395 -39.091 -76.342  1.00147.53           O  
ANISOU 4303  O   SER A 582    20042  18107  17903  -1663  -1741    593       O  
ATOM   4304  CB  SER A 582     -60.321 -40.839 -78.968  1.00152.76           C  
ANISOU 4304  CB  SER A 582    20871  18615  18553  -1571  -1899    621       C  
ATOM   4305  OG  SER A 582     -60.090 -42.141 -78.459  1.00160.10           O  
ANISOU 4305  OG  SER A 582    22025  19429  19376  -1626  -2023    646       O  
ATOM   4306  N   ARG A 583     -58.704 -40.560 -76.134  1.00147.22           N  
ANISOU 4306  N   ARG A 583    20277  17866  17793  -1544  -1931    584       N  
ATOM   4307  CA  ARG A 583     -58.836 -40.659 -74.684  1.00149.90           C  
ANISOU 4307  CA  ARG A 583    20684  18209  18060  -1649  -1932    597       C  
ATOM   4308  C   ARG A 583     -58.064 -39.565 -73.943  1.00148.54           C  
ANISOU 4308  C   ARG A 583    20394  18089  17954  -1559  -1867    552       C  
ATOM   4309  O   ARG A 583     -58.055 -39.541 -72.711  1.00153.08           O  
ANISOU 4309  O   ARG A 583    21013  18670  18477  -1628  -1864    556       O  
ATOM   4310  CB  ARG A 583     -58.423 -42.055 -74.186  1.00156.30           C  
ANISOU 4310  CB  ARG A 583    21748  18881  18757  -1685  -2077    620       C  
ATOM   4311  CG  ARG A 583     -59.230 -43.205 -74.782  1.00162.79           C  
ANISOU 4311  CG  ARG A 583    22712  19642  19499  -1796  -2153    670       C  
ATOM   4312  CD  ARG A 583     -59.309 -44.406 -73.848  1.00166.44           C  
ANISOU 4312  CD  ARG A 583    23417  19997  19822  -1920  -2268    711       C  
ATOM   4313  NE  ARG A 583     -60.462 -44.331 -72.948  1.00169.13           N  
ANISOU 4313  NE  ARG A 583    23747  20420  20091  -2134  -2204    755       N  
ATOM   4314  CZ  ARG A 583     -60.422 -43.896 -71.689  1.00170.87           C  
ANISOU 4314  CZ  ARG A 583    23949  20690  20283  -2193  -2159    752       C  
ATOM   4315  NH1 ARG A 583     -59.279 -43.493 -71.147  1.00172.63           N  
ANISOU 4315  NH1 ARG A 583    24165  20880  20544  -2054  -2173    708       N  
ATOM   4316  NH2 ARG A 583     -61.532 -43.866 -70.963  1.00168.96           N  
ANISOU 4316  NH2 ARG A 583    23689  20537  19968  -2393  -2100    789       N  
ATOM   4317  N   PHE A 584     -57.439 -38.654 -74.694  1.00144.11           N  
ANISOU 4317  N   PHE A 584    19686  17566  17503  -1414  -1815    511       N  
ATOM   4318  CA  PHE A 584     -56.614 -37.583 -74.117  1.00135.32           C  
ANISOU 4318  CA  PHE A 584    18459  16496  16458  -1320  -1759    466       C  
ATOM   4319  C   PHE A 584     -57.386 -36.594 -73.247  1.00133.67           C  
ANISOU 4319  C   PHE A 584    18126  16396  16265  -1411  -1651    466       C  
ATOM   4320  O   PHE A 584     -56.925 -36.248 -72.161  1.00134.63           O  
ANISOU 4320  O   PHE A 584    18250  16526  16378  -1406  -1641    447       O  
ATOM   4321  CB  PHE A 584     -55.854 -36.814 -75.203  1.00131.57           C  
ANISOU 4321  CB  PHE A 584    17853  16045  16091  -1163  -1725    427       C  
ATOM   4322  CG  PHE A 584     -54.599 -37.491 -75.677  1.00128.17           C  
ANISOU 4322  CG  PHE A 584    17516  15527  15653  -1027  -1825    397       C  
ATOM   4323  CD1 PHE A 584     -53.839 -38.275 -74.820  1.00127.87           C  
ANISOU 4323  CD1 PHE A 584    17632  15407  15546  -1004  -1921    384       C  
ATOM   4324  CD2 PHE A 584     -54.156 -37.308 -76.980  1.00126.80           C  
ANISOU 4324  CD2 PHE A 584    17273  15362  15543   -915  -1823    377       C  
ATOM   4325  CE1 PHE A 584     -52.680 -38.888 -75.266  1.00128.77           C  
ANISOU 4325  CE1 PHE A 584    17824  15451  15649   -865  -2019    345       C  
ATOM   4326  CE2 PHE A 584     -52.994 -37.913 -77.431  1.00125.70           C  
ANISOU 4326  CE2 PHE A 584    17206  15160  15392   -783  -1914    340       C  
ATOM   4327  CZ  PHE A 584     -52.254 -38.702 -76.572  1.00127.58           C  
ANISOU 4327  CZ  PHE A 584    17593  15321  15560   -753  -2013    320       C  
ATOM   4328  N   MET A 585     -58.547 -36.142 -73.725  1.00130.54           N  
ANISOU 4328  N   MET A 585    17620  16085  15891  -1488  -1575    483       N  
ATOM   4329  CA  MET A 585     -59.366 -35.167 -72.997  1.00130.93           C  
ANISOU 4329  CA  MET A 585    17538  16252  15954  -1564  -1474    473       C  
ATOM   4330  C   MET A 585     -59.679 -35.603 -71.566  1.00137.94           C  
ANISOU 4330  C   MET A 585    18517  17148  16742  -1690  -1489    489       C  
ATOM   4331  O   MET A 585     -59.694 -34.779 -70.652  1.00141.64           O  
ANISOU 4331  O   MET A 585    18903  17686  17227  -1698  -1428    464       O  
ATOM   4332  CB  MET A 585     -60.650 -34.849 -73.765  1.00128.14           C  
ANISOU 4332  CB  MET A 585    17078  15988  15620  -1634  -1410    486       C  
ATOM   4333  CG  MET A 585     -61.828 -34.438 -72.893  1.00128.20           C  
ANISOU 4333  CG  MET A 585    17011  16114  15583  -1770  -1338    487       C  
ATOM   4334  SD  MET A 585     -63.076 -33.437 -73.723  1.00133.75           S  
ANISOU 4334  SD  MET A 585    17516  16952  16350  -1783  -1240    467       S  
ATOM   4335  CE  MET A 585     -63.397 -34.378 -75.219  1.00131.59           C  
ANISOU 4335  CE  MET A 585    17309  16616  16070  -1788  -1295    504       C  
ATOM   4336  N   GLU A 586     -59.920 -36.899 -71.383  1.00147.63           N  
ANISOU 4336  N   GLU A 586    19923  18304  17865  -1790  -1573    532       N  
ATOM   4337  CA  GLU A 586     -60.138 -37.480 -70.057  1.00153.10           C  
ANISOU 4337  CA  GLU A 586    20736  18988  18447  -1919  -1603    555       C  
ATOM   4338  C   GLU A 586     -58.976 -37.162 -69.119  1.00145.78           C  
ANISOU 4338  C   GLU A 586    19838  18018  17534  -1826  -1625    522       C  
ATOM   4339  O   GLU A 586     -59.190 -36.854 -67.951  1.00147.14           O  
ANISOU 4339  O   GLU A 586    19999  18243  17664  -1898  -1590    518       O  
ATOM   4340  CB  GLU A 586     -60.335 -38.998 -70.155  1.00168.24           C  
ANISOU 4340  CB  GLU A 586    22872  20800  20251  -2019  -1716    607       C  
ATOM   4341  CG  GLU A 586     -61.626 -39.440 -70.838  1.00178.01           C  
ANISOU 4341  CG  GLU A 586    24101  22087  21448  -2154  -1698    646       C  
ATOM   4342  CD  GLU A 586     -62.791 -39.587 -69.875  1.00183.87           C  
ANISOU 4342  CD  GLU A 586    24847  22926  22087  -2363  -1655    675       C  
ATOM   4343  OE1 GLU A 586     -62.708 -40.432 -68.956  1.00187.43           O  
ANISOU 4343  OE1 GLU A 586    25471  23316  22426  -2469  -1723    708       O  
ATOM   4344  OE2 GLU A 586     -63.800 -38.870 -70.049  1.00187.36           O  
ANISOU 4344  OE2 GLU A 586    25123  23510  22556  -2423  -1555    663       O  
ATOM   4345  N   TYR A 587     -57.752 -37.223 -69.644  1.00140.77           N  
ANISOU 4345  N   TYR A 587    19234  17296  16955  -1665  -1682    495       N  
ATOM   4346  CA  TYR A 587     -56.550 -36.931 -68.858  1.00139.65           C  
ANISOU 4346  CA  TYR A 587    19114  17115  16832  -1561  -1708    456       C  
ATOM   4347  C   TYR A 587     -56.325 -35.427 -68.647  1.00135.51           C  
ANISOU 4347  C   TYR A 587    18388  16686  16410  -1486  -1602    411       C  
ATOM   4348  O   TYR A 587     -55.405 -35.026 -67.926  1.00134.71           O  
ANISOU 4348  O   TYR A 587    18281  16570  16330  -1410  -1610    376       O  
ATOM   4349  CB  TYR A 587     -55.305 -37.565 -69.498  1.00143.62           C  
ANISOU 4349  CB  TYR A 587    19715  17502  17349  -1414  -1812    434       C  
ATOM   4350  CG  TYR A 587     -55.475 -38.999 -69.958  1.00149.67           C  
ANISOU 4350  CG  TYR A 587    20675  18163  18027  -1459  -1927    472       C  
ATOM   4351  CD1 TYR A 587     -56.008 -39.971 -69.111  1.00155.85           C  
ANISOU 4351  CD1 TYR A 587    21636  18894  18685  -1605  -1990    517       C  
ATOM   4352  CD2 TYR A 587     -55.081 -39.388 -71.238  1.00151.98           C  
ANISOU 4352  CD2 TYR A 587    20981  18405  18356  -1356  -1976    462       C  
ATOM   4353  CE1 TYR A 587     -56.161 -41.283 -69.532  1.00161.83           C  
ANISOU 4353  CE1 TYR A 587    22584  19543  19357  -1650  -2105    553       C  
ATOM   4354  CE2 TYR A 587     -55.225 -40.700 -71.667  1.00156.40           C  
ANISOU 4354  CE2 TYR A 587    21726  18863  18834  -1390  -2090    493       C  
ATOM   4355  CZ  TYR A 587     -55.767 -41.643 -70.812  1.00161.78           C  
ANISOU 4355  CZ  TYR A 587    22588  19484  19394  -1538  -2157    539       C  
ATOM   4356  OH  TYR A 587     -55.916 -42.949 -71.227  1.00164.70           O  
ANISOU 4356  OH  TYR A 587    23156  19742  19679  -1577  -2279    572       O  
ATOM   4357  N   GLU A 588     -57.167 -34.603 -69.271  1.00128.53           N  
ANISOU 4357  N   GLU A 588    17346  15898  15588  -1508  -1510    409       N  
ATOM   4358  CA  GLU A 588     -57.079 -33.149 -69.145  1.00120.34           C  
ANISOU 4358  CA  GLU A 588    16126  14950  14648  -1443  -1415    368       C  
ATOM   4359  C   GLU A 588     -58.303 -32.559 -68.447  1.00119.30           C  
ANISOU 4359  C   GLU A 588    15901  14937  14490  -1562  -1331    369       C  
ATOM   4360  O   GLU A 588     -58.881 -31.581 -68.922  1.00118.46           O  
ANISOU 4360  O   GLU A 588    15641  14916  14453  -1543  -1253    350       O  
ATOM   4361  CB  GLU A 588     -56.894 -32.503 -70.519  1.00116.46           C  
ANISOU 4361  CB  GLU A 588    15517  14472  14261  -1337  -1382    352       C  
ATOM   4362  CG  GLU A 588     -55.511 -32.679 -71.126  1.00116.13           C  
ANISOU 4362  CG  GLU A 588    15511  14348  14263  -1194  -1441    330       C  
ATOM   4363  CD  GLU A 588     -55.442 -32.250 -72.582  1.00115.29           C  
ANISOU 4363  CD  GLU A 588    15311  14255  14239  -1114  -1416    325       C  
ATOM   4364  OE1 GLU A 588     -56.390 -31.603 -73.073  1.00115.52           O  
ANISOU 4364  OE1 GLU A 588    15230  14354  14306  -1153  -1346    333       O  
ATOM   4365  OE2 GLU A 588     -54.433 -32.562 -73.247  1.00116.39           O  
ANISOU 4365  OE2 GLU A 588    15484  14338  14401  -1008  -1468    310       O  
ATOM   4366  N   THR A 589     -58.692 -33.168 -67.327  1.00120.25           N  
ANISOU 4366  N   THR A 589    16119  15064  14506  -1682  -1352    390       N  
ATOM   4367  CA  THR A 589     -59.783 -32.678 -66.474  1.00121.70           C  
ANISOU 4367  CA  THR A 589    16221  15373  14646  -1801  -1276    384       C  
ATOM   4368  C   THR A 589     -59.324 -32.590 -65.030  1.00123.37           C  
ANISOU 4368  C   THR A 589    16482  15585  14808  -1822  -1284    370       C  
ATOM   4369  O   THR A 589     -58.238 -33.056 -64.701  1.00125.59           O  
ANISOU 4369  O   THR A 589    16879  15762  15077  -1759  -1356    370       O  
ATOM   4370  CB  THR A 589     -61.026 -33.579 -66.538  1.00123.78           C  
ANISOU 4370  CB  THR A 589    16546  15677  14805  -1974  -1283    430       C  
ATOM   4371  OG1 THR A 589     -60.683 -34.826 -67.155  1.00126.89           O  
ANISOU 4371  OG1 THR A 589    17108  15948  15155  -1985  -1380    473       O  
ATOM   4372  CG2 THR A 589     -62.124 -32.908 -67.338  1.00124.25           C  
ANISOU 4372  CG2 THR A 589    16444  15852  14913  -1995  -1204    417       C  
ATOM   4373  N   ASP A 590     -60.160 -32.006 -64.171  1.00125.47           N  
ANISOU 4373  N   ASP A 590    16658  15973  15040  -1908  -1213    353       N  
ATOM   4374  CA  ASP A 590     -59.766 -31.646 -62.800  1.00127.83           C  
ANISOU 4374  CA  ASP A 590    16967  16294  15307  -1914  -1203    328       C  
ATOM   4375  C   ASP A 590     -58.705 -30.529 -62.848  1.00126.85           C  
ANISOU 4375  C   ASP A 590    16746  16147  15304  -1742  -1183    276       C  
ATOM   4376  O   ASP A 590     -57.832 -30.425 -61.974  1.00125.84           O  
ANISOU 4376  O   ASP A 590    16666  15976  15170  -1695  -1210    258       O  
ATOM   4377  CB  ASP A 590     -59.272 -32.880 -62.022  1.00130.17           C  
ANISOU 4377  CB  ASP A 590    17475  16489  15491  -1984  -1295    368       C  
ATOM   4378  CG  ASP A 590     -59.472 -32.756 -60.518  1.00133.41           C  
ANISOU 4378  CG  ASP A 590    17906  16962  15819  -2072  -1273    359       C  
ATOM   4379  OD1 ASP A 590     -60.417 -32.064 -60.078  1.00134.19           O  
ANISOU 4379  OD1 ASP A 590    17876  17205  15904  -2141  -1188    337       O  
ATOM   4380  OD2 ASP A 590     -58.682 -33.371 -59.771  1.00135.12           O  
ANISOU 4380  OD2 ASP A 590    18271  17086  15979  -2068  -1346    371       O  
ATOM   4381  N   LEU A 591     -58.810 -29.694 -63.885  1.00123.88           N  
ANISOU 4381  N   LEU A 591    16235  15799  15032  -1656  -1138    254       N  
ATOM   4382  CA  LEU A 591     -57.843 -28.635 -64.169  1.00117.22           C  
ANISOU 4382  CA  LEU A 591    15300  14931  14306  -1502  -1121    211       C  
ATOM   4383  C   LEU A 591     -58.032 -27.420 -63.274  1.00114.78           C  
ANISOU 4383  C   LEU A 591    14869  14713  14028  -1484  -1056    162       C  
ATOM   4384  O   LEU A 591     -59.071 -27.254 -62.635  1.00117.49           O  
ANISOU 4384  O   LEU A 591    15165  15161  14314  -1579  -1010    154       O  
ATOM   4385  CB  LEU A 591     -57.934 -28.197 -65.637  1.00113.18           C  
ANISOU 4385  CB  LEU A 591    14700  14415  13887  -1428  -1101    210       C  
ATOM   4386  CG  LEU A 591     -57.483 -29.134 -66.760  1.00111.32           C  
ANISOU 4386  CG  LEU A 591    14557  14084  13654  -1396  -1165    245       C  
ATOM   4387  CD1 LEU A 591     -57.667 -28.458 -68.107  1.00110.55           C  
ANISOU 4387  CD1 LEU A 591    14347  14006  13650  -1325  -1128    238       C  
ATOM   4388  CD2 LEU A 591     -56.035 -29.559 -66.595  1.00110.86           C  
ANISOU 4388  CD2 LEU A 591    14597  13921  13604  -1305  -1236    237       C  
ATOM   4389  N   THR A 592     -57.013 -26.573 -63.238  1.00108.94           N  
ANISOU 4389  N   THR A 592    14079  13938  13376  -1362  -1054    126       N  
ATOM   4390  CA  THR A 592     -57.088 -25.321 -62.519  1.00106.27           C  
ANISOU 4390  CA  THR A 592    13624  13671  13080  -1325  -1000     75       C  
ATOM   4391  C   THR A 592     -56.791 -24.196 -63.492  1.00103.66           C  
ANISOU 4391  C   THR A 592    13177  13337  12872  -1214   -971     49       C  
ATOM   4392  O   THR A 592     -55.696 -24.130 -64.052  1.00104.22           O  
ANISOU 4392  O   THR A 592    13267  13328  13003  -1125  -1003     49       O  
ATOM   4393  CB  THR A 592     -56.090 -25.283 -61.348  1.00107.11           C  
ANISOU 4393  CB  THR A 592    13790  13736  13170  -1292  -1030     54       C  
ATOM   4394  OG1 THR A 592     -56.347 -26.384 -60.469  1.00109.91           O  
ANISOU 4394  OG1 THR A 592    14272  14084  13404  -1400  -1065     84       O  
ATOM   4395  CG2 THR A 592     -56.220 -23.986 -60.570  1.00106.23           C  
ANISOU 4395  CG2 THR A 592    13561  13700  13099  -1256   -977      0       C  
ATOM   4396  N   PHE A 593     -57.776 -23.325 -63.699  1.00100.46           N  
ANISOU 4396  N   PHE A 593    12651  13023  12495  -1221   -914     23       N  
ATOM   4397  CA  PHE A 593     -57.600 -22.140 -64.529  1.00 97.02           C  
ANISOU 4397  CA  PHE A 593    12109  12586  12169  -1122   -889     -3       C  
ATOM   4398  C   PHE A 593     -56.489 -21.273 -63.959  1.00 95.73           C  
ANISOU 4398  C   PHE A 593    11924  12383  12065  -1035   -896    -38       C  
ATOM   4399  O   PHE A 593     -56.427 -21.055 -62.751  1.00 96.03           O  
ANISOU 4399  O   PHE A 593    11965  12452  12069  -1051   -890    -66       O  
ATOM   4400  CB  PHE A 593     -58.894 -21.332 -64.609  1.00 96.92           C  
ANISOU 4400  CB  PHE A 593    11979  12682  12163  -1142   -836    -36       C  
ATOM   4401  CG  PHE A 593     -58.779 -20.086 -65.441  1.00 97.12           C  
ANISOU 4401  CG  PHE A 593    11908  12698  12293  -1042   -819    -63       C  
ATOM   4402  CD1 PHE A 593     -58.997 -20.129 -66.816  1.00 97.57           C  
ANISOU 4402  CD1 PHE A 593    11948  12730  12394  -1019   -821    -39       C  
ATOM   4403  CD2 PHE A 593     -58.446 -18.869 -64.855  1.00 95.99           C  
ANISOU 4403  CD2 PHE A 593    11701  12567  12202   -974   -806   -113       C  
ATOM   4404  CE1 PHE A 593     -58.887 -18.980 -67.588  1.00 96.98           C  
ANISOU 4404  CE1 PHE A 593    11797  12640  12409   -933   -811    -60       C  
ATOM   4405  CE2 PHE A 593     -58.335 -17.718 -65.621  1.00 95.55           C  
ANISOU 4405  CE2 PHE A 593    11574  12493  12238   -889   -800   -135       C  
ATOM   4406  CZ  PHE A 593     -58.557 -17.773 -66.988  1.00 95.74           C  
ANISOU 4406  CZ  PHE A 593    11585  12490  12301   -871   -802   -107       C  
ATOM   4407  N   VAL A 594     -55.607 -20.793 -64.830  1.00 93.60           N  
ANISOU 4407  N   VAL A 594    11634  12049  11880   -949   -910    -38       N  
ATOM   4408  CA  VAL A 594     -54.511 -19.931 -64.400  1.00 91.30           C  
ANISOU 4408  CA  VAL A 594    11318  11722  11649   -871   -917    -71       C  
ATOM   4409  C   VAL A 594     -54.631 -18.563 -65.056  1.00 90.31           C  
ANISOU 4409  C   VAL A 594    11089  11608  11614   -809   -889    -96       C  
ATOM   4410  O   VAL A 594     -54.585 -17.543 -64.374  1.00 90.30           O  
ANISOU 4410  O   VAL A 594    11035  11631  11644   -778   -874   -138       O  
ATOM   4411  CB  VAL A 594     -53.130 -20.557 -64.687  1.00 90.07           C  
ANISOU 4411  CB  VAL A 594    11237  11479  11503   -827   -967    -54       C  
ATOM   4412  CG1 VAL A 594     -52.017 -19.683 -64.132  1.00 88.48           C  
ANISOU 4412  CG1 VAL A 594    11005  11254  11356   -758   -973    -93       C  
ATOM   4413  CG2 VAL A 594     -53.047 -21.951 -64.085  1.00 90.65           C  
ANISOU 4413  CG2 VAL A 594    11431  11528  11482   -883  -1008    -30       C  
ATOM   4414  N   GLY A 595     -54.799 -18.548 -66.374  1.00 90.11           N  
ANISOU 4414  N   GLY A 595    11044  11565  11628   -791   -887    -71       N  
ATOM   4415  CA  GLY A 595     -54.902 -17.292 -67.114  1.00 90.87           C  
ANISOU 4415  CA  GLY A 595    11058  11660  11806   -735   -868    -89       C  
ATOM   4416  C   GLY A 595     -55.273 -17.431 -68.582  1.00 90.93           C  
ANISOU 4416  C   GLY A 595    11052  11654  11841   -728   -865    -56       C  
ATOM   4417  O   GLY A 595     -55.707 -18.501 -69.036  1.00 92.02           O  
ANISOU 4417  O   GLY A 595    11233  11797  11932   -773   -872    -22       O  
ATOM   4418  N   VAL A 596     -55.098 -16.336 -69.322  1.00 88.17           N  
ANISOU 4418  N   VAL A 596    10649  11284  11565   -675   -860    -66       N  
ATOM   4419  CA  VAL A 596     -55.412 -16.280 -70.752  1.00 85.26           C  
ANISOU 4419  CA  VAL A 596    10263  10901  11229   -661   -857    -37       C  
ATOM   4420  C   VAL A 596     -54.430 -15.357 -71.482  1.00 83.31           C  
ANISOU 4420  C   VAL A 596     9997  10598  11056   -607   -867    -34       C  
ATOM   4421  O   VAL A 596     -54.058 -14.302 -70.965  1.00 82.59           O  
ANISOU 4421  O   VAL A 596     9879  10498  11004   -578   -868    -65       O  
ATOM   4422  CB  VAL A 596     -56.868 -15.807 -70.987  1.00 84.89           C  
ANISOU 4422  CB  VAL A 596    10159  10915  11180   -670   -835    -56       C  
ATOM   4423  CG1 VAL A 596     -57.081 -15.315 -72.416  1.00 84.09           C  
ANISOU 4423  CG1 VAL A 596    10031  10787  11129   -636   -837    -37       C  
ATOM   4424  CG2 VAL A 596     -57.849 -16.916 -70.645  1.00 84.91           C  
ANISOU 4424  CG2 VAL A 596    10180  10977  11102   -741   -824    -46       C  
ATOM   4425  N   VAL A 597     -54.005 -15.770 -72.672  1.00 80.41           N  
ANISOU 4425  N   VAL A 597     9649  10200  10703   -599   -875      2       N  
ATOM   4426  CA  VAL A 597     -53.170 -14.931 -73.519  1.00 78.86           C  
ANISOU 4426  CA  VAL A 597     9432   9963  10567   -563   -881     11       C  
ATOM   4427  C   VAL A 597     -53.937 -14.586 -74.778  1.00 78.41           C  
ANISOU 4427  C   VAL A 597     9351   9905  10535   -555   -873     32       C  
ATOM   4428  O   VAL A 597     -54.416 -15.474 -75.477  1.00 78.20           O  
ANISOU 4428  O   VAL A 597     9343   9889  10480   -572   -872     59       O  
ATOM   4429  CB  VAL A 597     -51.822 -15.598 -73.884  1.00 78.70           C  
ANISOU 4429  CB  VAL A 597     9445   9915  10541   -553   -899     29       C  
ATOM   4430  CG1 VAL A 597     -50.897 -15.638 -72.676  1.00 78.73           C  
ANISOU 4430  CG1 VAL A 597     9464   9914  10533   -547   -912      0       C  
ATOM   4431  CG2 VAL A 597     -52.030 -16.996 -74.446  1.00 78.78           C  
ANISOU 4431  CG2 VAL A 597     9500   9928  10501   -569   -910     59       C  
ATOM   4432  N   GLY A 598     -54.070 -13.292 -75.046  1.00 79.04           N  
ANISOU 4432  N   GLY A 598     9398   9967  10664   -529   -874     18       N  
ATOM   4433  CA  GLY A 598     -54.749 -12.811 -76.243  1.00 79.62           C  
ANISOU 4433  CA  GLY A 598     9455  10032  10764   -515   -874     36       C  
ATOM   4434  C   GLY A 598     -53.751 -12.504 -77.338  1.00 80.32           C  
ANISOU 4434  C   GLY A 598     9555  10076  10885   -508   -882     70       C  
ATOM   4435  O   GLY A 598     -52.873 -11.655 -77.169  1.00 81.03           O  
ANISOU 4435  O   GLY A 598     9643  10136  11007   -502   -890     63       O  
ATOM   4436  N   MET A 599     -53.893 -13.190 -78.466  1.00 81.31           N  
ANISOU 4436  N   MET A 599     9691  10203  10998   -513   -879    106       N  
ATOM   4437  CA  MET A 599     -52.928 -13.100 -79.554  1.00 82.70           C  
ANISOU 4437  CA  MET A 599     9875  10354  11191   -512   -883    138       C  
ATOM   4438  C   MET A 599     -53.373 -12.211 -80.686  1.00 84.05           C  
ANISOU 4438  C   MET A 599    10039  10499  11395   -503   -887    158       C  
ATOM   4439  O   MET A 599     -54.555 -12.157 -81.023  1.00 86.99           O  
ANISOU 4439  O   MET A 599    10405  10879  11765   -491   -888    157       O  
ATOM   4440  CB  MET A 599     -52.680 -14.469 -80.133  1.00 84.26           C  
ANISOU 4440  CB  MET A 599    10095  10569  11350   -519   -883    163       C  
ATOM   4441  CG  MET A 599     -51.974 -15.381 -79.181  1.00 87.63           C  
ANISOU 4441  CG  MET A 599    10543  11008  11741   -524   -891    147       C  
ATOM   4442  SD  MET A 599     -50.839 -16.315 -80.189  1.00 92.79           S  
ANISOU 4442  SD  MET A 599    11216  11668  12372   -510   -904    170       S  
ATOM   4443  CE  MET A 599     -50.034 -17.214 -78.871  1.00 95.57           C  
ANISOU 4443  CE  MET A 599    11600  12027  12683   -504   -925    138       C  
ATOM   4444  N   LEU A 600     -52.402 -11.555 -81.304  1.00 84.17           N  
ANISOU 4444  N   LEU A 600    10057  10488  11433   -511   -892    177       N  
ATOM   4445  CA  LEU A 600     -52.666 -10.671 -82.423  1.00 85.25           C  
ANISOU 4445  CA  LEU A 600    10201  10592  11595   -510   -902    203       C  
ATOM   4446  C   LEU A 600     -52.075 -11.247 -83.703  1.00 86.49           C  
ANISOU 4446  C   LEU A 600    10363  10760  11736   -523   -894    244       C  
ATOM   4447  O   LEU A 600     -50.895 -11.602 -83.750  1.00 87.64           O  
ANISOU 4447  O   LEU A 600    10502  10926  11868   -540   -887    250       O  
ATOM   4448  CB  LEU A 600     -52.084  -9.291 -82.136  1.00 85.14           C  
ANISOU 4448  CB  LEU A 600    10196  10536  11616   -521   -919    194       C  
ATOM   4449  CG  LEU A 600     -52.121  -8.249 -83.239  1.00 85.74           C  
ANISOU 4449  CG  LEU A 600    10297  10564  11714   -531   -938    224       C  
ATOM   4450  CD1 LEU A 600     -53.488  -7.582 -83.293  1.00 86.51           C  
ANISOU 4450  CD1 LEU A 600    10407  10632  11828   -491   -963    206       C  
ATOM   4451  CD2 LEU A 600     -51.018  -7.239 -82.972  1.00 87.38           C  
ANISOU 4451  CD2 LEU A 600    10517  10740  11941   -567   -951    226       C  
ATOM   4452  N   ASP A 601     -52.915 -11.364 -84.726  1.00 87.67           N  
ANISOU 4452  N   ASP A 601    10521  10905  11884   -512   -896    267       N  
ATOM   4453  CA  ASP A 601     -52.476 -11.723 -86.070  1.00 89.33           C  
ANISOU 4453  CA  ASP A 601    10737  11122  12080   -522   -891    307       C  
ATOM   4454  C   ASP A 601     -53.279 -10.886 -87.058  1.00 91.26           C  
ANISOU 4454  C   ASP A 601    11000  11330  12344   -515   -905    328       C  
ATOM   4455  O   ASP A 601     -54.426 -11.228 -87.387  1.00 92.39           O  
ANISOU 4455  O   ASP A 601    11144  11477  12483   -490   -909    327       O  
ATOM   4456  CB  ASP A 601     -52.653 -13.215 -86.333  1.00 90.18           C  
ANISOU 4456  CB  ASP A 601    10844  11269  12150   -510   -883    312       C  
ATOM   4457  CG  ASP A 601     -52.604 -13.563 -87.812  1.00 91.96           C  
ANISOU 4457  CG  ASP A 601    11076  11501  12361   -508   -882    349       C  
ATOM   4458  OD1 ASP A 601     -51.876 -12.894 -88.587  1.00 90.03           O  
ANISOU 4458  OD1 ASP A 601    10831  11252  12124   -527   -880    372       O  
ATOM   4459  OD2 ASP A 601     -53.317 -14.515 -88.195  1.00 93.97           O  
ANISOU 4459  OD2 ASP A 601    11338  11770  12594   -493   -884    355       O  
ATOM   4460  N   PRO A 602     -52.669  -9.787 -87.538  1.00 91.08           N  
ANISOU 4460  N   PRO A 602    10994  11272  12338   -541   -916    349       N  
ATOM   4461  CA  PRO A 602     -53.373  -8.708 -88.220  1.00 90.79           C  
ANISOU 4461  CA  PRO A 602    10991  11181  12322   -533   -943    363       C  
ATOM   4462  C   PRO A 602     -53.641  -8.998 -89.690  1.00 91.59           C  
ANISOU 4462  C   PRO A 602    11107  11285  12408   -533   -943    404       C  
ATOM   4463  O   PRO A 602     -52.805  -9.622 -90.355  1.00 91.90           O  
ANISOU 4463  O   PRO A 602    11134  11360  12421   -559   -922    430       O  
ATOM   4464  CB  PRO A 602     -52.409  -7.535 -88.085  1.00 92.56           C  
ANISOU 4464  CB  PRO A 602    11239  11366  12562   -576   -958    373       C  
ATOM   4465  CG  PRO A 602     -51.049  -8.161 -88.000  1.00 92.79           C  
ANISOU 4465  CG  PRO A 602    11237  11448  12569   -616   -929    382       C  
ATOM   4466  CD  PRO A 602     -51.208  -9.582 -87.540  1.00 90.77           C  
ANISOU 4466  CD  PRO A 602    10947  11248  12292   -584   -906    360       C  
ATOM   4467  N   PRO A 603     -54.808  -8.552 -90.194  1.00 92.46           N  
ANISOU 4467  N   PRO A 603    11239  11360  12529   -499   -968    403       N  
ATOM   4468  CA  PRO A 603     -55.157  -8.664 -91.614  1.00 93.46           C  
ANISOU 4468  CA  PRO A 603    11388  11480  12642   -496   -974    441       C  
ATOM   4469  C   PRO A 603     -54.101  -8.011 -92.505  1.00 95.93           C  
ANISOU 4469  C   PRO A 603    11732  11770  12944   -550   -976    488       C  
ATOM   4470  O   PRO A 603     -53.580  -6.940 -92.173  1.00 97.36           O  
ANISOU 4470  O   PRO A 603    11943  11909  13140   -583   -995    491       O  
ATOM   4471  CB  PRO A 603     -56.473  -7.888 -91.710  1.00 92.26           C  
ANISOU 4471  CB  PRO A 603    11261  11282  12510   -447  -1013    420       C  
ATOM   4472  CG  PRO A 603     -57.066  -7.980 -90.346  1.00 91.09           C  
ANISOU 4472  CG  PRO A 603    11080  11155  12375   -416  -1013    364       C  
ATOM   4473  CD  PRO A 603     -55.899  -7.950 -89.404  1.00 91.52           C  
ANISOU 4473  CD  PRO A 603    11123  11218  12433   -455   -994    359       C  
ATOM   4474  N   ARG A 604     -53.774  -8.667 -93.612  1.00 97.23           N  
ANISOU 4474  N   ARG A 604    11891  11970  13081   -565   -958    523       N  
ATOM   4475  CA  ARG A 604     -52.836  -8.109 -94.580  1.00101.58           C  
ANISOU 4475  CA  ARG A 604    12468  12517  13611   -624   -956    569       C  
ATOM   4476  C   ARG A 604     -53.436  -6.835 -95.137  1.00104.40           C  
ANISOU 4476  C   ARG A 604    12894  12791  13981   -629  -1000    590       C  
ATOM   4477  O   ARG A 604     -54.640  -6.779 -95.379  1.00106.88           O  
ANISOU 4477  O   ARG A 604    13227  13072  14308   -573  -1026    579       O  
ATOM   4478  CB  ARG A 604     -52.569  -9.113 -95.696  1.00102.26           C  
ANISOU 4478  CB  ARG A 604    12532  12662  13659   -626   -931    595       C  
ATOM   4479  CG  ARG A 604     -51.875 -10.377 -95.215  1.00100.39           C  
ANISOU 4479  CG  ARG A 604    12238  12502  13402   -616   -899    571       C  
ATOM   4480  CD  ARG A 604     -52.153 -11.538 -96.144  1.00 98.35           C  
ANISOU 4480  CD  ARG A 604    11967  12287  13114   -584   -889    582       C  
ATOM   4481  NE  ARG A 604     -51.159 -12.589 -95.994  1.00 96.16           N  
ANISOU 4481  NE  ARG A 604    11647  12084  12805   -581   -867    565       N  
ATOM   4482  CZ  ARG A 604     -50.004 -12.609 -96.643  1.00 96.69           C  
ANISOU 4482  CZ  ARG A 604    11691  12209  12836   -616   -851    578       C  
ATOM   4483  NH1 ARG A 604     -49.701 -11.631 -97.484  1.00 97.32           N  
ANISOU 4483  NH1 ARG A 604    11791  12278  12906   -669   -849    617       N  
ATOM   4484  NH2 ARG A 604     -49.152 -13.605 -96.449  1.00 98.30           N  
ANISOU 4484  NH2 ARG A 604    11854  12484  13008   -598   -839    551       N  
ATOM   4485  N   LYS A 605     -52.607  -5.812 -95.325  1.00107.89           N  
ANISOU 4485  N   LYS A 605    13376  13199  14416   -696  -1014    619       N  
ATOM   4486  CA  LYS A 605     -53.111  -4.460 -95.608  1.00111.46           C  
ANISOU 4486  CA  LYS A 605    13914  13553  14881   -702  -1071    635       C  
ATOM   4487  C   LYS A 605     -53.919  -4.315 -96.907  1.00110.34           C  
ANISOU 4487  C   LYS A 605    13822  13375  14725   -679  -1098    666       C  
ATOM   4488  O   LYS A 605     -54.934  -3.609 -96.937  1.00106.43           O  
ANISOU 4488  O   LYS A 605    13381  12807  14249   -628  -1152    651       O  
ATOM   4489  CB  LYS A 605     -51.983  -3.426 -95.522  1.00117.85           C  
ANISOU 4489  CB  LYS A 605    14765  14331  15680   -795  -1084    663       C  
ATOM   4490  CG  LYS A 605     -50.773  -3.693 -96.412  1.00124.81           C  
ANISOU 4490  CG  LYS A 605    15627  15279  16513   -885  -1045    711       C  
ATOM   4491  CD  LYS A 605     -49.542  -2.902 -95.972  1.00130.93           C  
ANISOU 4491  CD  LYS A 605    16414  16056  17277   -982  -1044    724       C  
ATOM   4492  CE  LYS A 605     -49.852  -1.453 -95.588  1.00133.88           C  
ANISOU 4492  CE  LYS A 605    16885  16309  17674  -1003  -1111    729       C  
ATOM   4493  NZ  LYS A 605     -50.534  -0.667 -96.657  1.00134.44           N  
ANISOU 4493  NZ  LYS A 605    17057  16292  17730  -1009  -1165    771       N  
ATOM   4494  N   GLU A 606     -53.475  -5.005 -97.956  1.00112.74           N  
ANISOU 4494  N   GLU A 606    14106  13736  14992   -710  -1064    704       N  
ATOM   4495  CA  GLU A 606     -54.140  -4.981 -99.265  1.00115.40           C  
ANISOU 4495  CA  GLU A 606    14486  14049  15309   -692  -1085    738       C  
ATOM   4496  C   GLU A 606     -55.475  -5.732 -99.258  1.00113.66           C  
ANISOU 4496  C   GLU A 606    14237  13837  15108   -595  -1091    702       C  
ATOM   4497  O   GLU A 606     -56.348  -5.460-100.086  1.00114.77           O  
ANISOU 4497  O   GLU A 606    14424  13936  15247   -558  -1126    713       O  
ATOM   4498  CB  GLU A 606     -53.240  -5.571-100.363  1.00118.20           C  
ANISOU 4498  CB  GLU A 606    14819  14477  15614   -751  -1043    783       C  
ATOM   4499  CG  GLU A 606     -51.739  -5.462-100.129  1.00122.14           C  
ANISOU 4499  CG  GLU A 606    15287  15033  16086   -842  -1008    799       C  
ATOM   4500  CD  GLU A 606     -51.186  -6.627 -99.328  1.00124.82           C  
ANISOU 4500  CD  GLU A 606    15532  15464  16428   -818   -960    757       C  
ATOM   4501  OE1 GLU A 606     -50.348  -6.386 -98.431  1.00129.68           O  
ANISOU 4501  OE1 GLU A 606    16122  16099  17051   -857   -948    739       O  
ATOM   4502  OE2 GLU A 606     -51.594  -7.780 -99.588  1.00124.96           O  
ANISOU 4502  OE2 GLU A 606    15506  15530  16440   -760   -941    742       O  
ATOM   4503  N   VAL A 607     -55.615  -6.682 -98.332  1.00110.97           N  
ANISOU 4503  N   VAL A 607    13825  13553  14784   -559  -1059    658       N  
ATOM   4504  CA  VAL A 607     -56.827  -7.497 -98.199  1.00108.87           C  
ANISOU 4504  CA  VAL A 607    13523  13309  14530   -484  -1059    622       C  
ATOM   4505  C   VAL A 607     -58.079  -6.628 -98.108  1.00108.22           C  
ANISOU 4505  C   VAL A 607    13483  13162  14473   -424  -1115    594       C  
ATOM   4506  O   VAL A 607     -59.048  -6.859 -98.832  1.00109.69           O  
ANISOU 4506  O   VAL A 607    13676  13346  14655   -377  -1133    590       O  
ATOM   4507  CB  VAL A 607     -56.719  -8.485 -97.008  1.00108.65           C  
ANISOU 4507  CB  VAL A 607    13427  13343  14511   -470  -1023    581       C  
ATOM   4508  CG1 VAL A 607     -58.088  -8.975 -96.540  1.00107.13           C  
ANISOU 4508  CG1 VAL A 607    13205  13163  14333   -406  -1033    535       C  
ATOM   4509  CG2 VAL A 607     -55.817  -9.656 -97.379  1.00107.19           C  
ANISOU 4509  CG2 VAL A 607    13202  13229  14295   -498   -980    601       C  
ATOM   4510  N   MET A 608     -58.036  -5.621 -97.238  1.00107.87           N  
ANISOU 4510  N   MET A 608    13466  13066  14452   -422  -1146    569       N  
ATOM   4511  CA  MET A 608     -59.117  -4.645 -97.089  1.00108.46           C  
ANISOU 4511  CA  MET A 608    13586  13075  14546   -358  -1210    532       C  
ATOM   4512  C   MET A 608     -59.651  -4.129 -98.429  1.00105.18           C  
ANISOU 4512  C   MET A 608    13242  12604  14116   -338  -1257    564       C  
ATOM   4513  O   MET A 608     -60.860  -4.107 -98.660  1.00100.73           O  
ANISOU 4513  O   MET A 608    12679  12035  13559   -262  -1291    528       O  
ATOM   4514  CB  MET A 608     -58.637  -3.475 -96.224  1.00114.42           C  
ANISOU 4514  CB  MET A 608    14386  13767  15320   -377  -1246    518       C  
ATOM   4515  CG  MET A 608     -59.263  -3.397 -94.838  1.00117.13           C  
ANISOU 4515  CG  MET A 608    14685  14127  15689   -318  -1255    444       C  
ATOM   4516  SD  MET A 608     -60.884  -2.590 -94.861  1.00124.56           S  
ANISOU 4516  SD  MET A 608    15658  15024  16644   -205  -1334    380       S  
ATOM   4517  CE  MET A 608     -60.477  -0.909 -95.352  1.00122.00           C  
ANISOU 4517  CE  MET A 608    15472  14561  16320   -221  -1422    410       C  
ATOM   4518  N   GLY A 609     -58.729  -3.737 -99.306  1.00107.02           N  
ANISOU 4518  N   GLY A 609    13533  12805  14324   -411  -1257    628       N  
ATOM   4519  CA  GLY A 609     -59.053  -3.182-100.620  1.00107.32           C  
ANISOU 4519  CA  GLY A 609    13653  12784  14340   -410  -1302    669       C  
ATOM   4520  C   GLY A 609     -59.353  -4.220-101.682  1.00105.54           C  
ANISOU 4520  C   GLY A 609    13393  12616  14091   -397  -1269    692       C  
ATOM   4521  O   GLY A 609     -60.189  -3.990-102.552  1.00106.52           O  
ANISOU 4521  O   GLY A 609    13562  12704  14207   -351  -1311    697       O  
ATOM   4522  N   SER A 610     -58.664  -5.357-101.618  1.00105.04           N  
ANISOU 4522  N   SER A 610    13254  12641  14015   -434  -1199    705       N  
ATOM   4523  CA  SER A 610     -58.927  -6.481-102.519  1.00105.30           C  
ANISOU 4523  CA  SER A 610    13248  12734  14026   -416  -1168    720       C  
ATOM   4524  C   SER A 610     -60.329  -7.058-102.302  1.00106.97           C  
ANISOU 4524  C   SER A 610    13419  12965  14258   -329  -1182    668       C  
ATOM   4525  O   SER A 610     -60.985  -7.492-103.259  1.00107.67           O  
ANISOU 4525  O   SER A 610    13511  13064  14332   -296  -1190    677       O  
ATOM   4526  CB  SER A 610     -57.869  -7.570-102.349  1.00104.08           C  
ANISOU 4526  CB  SER A 610    13025  12666  13852   -464  -1102    733       C  
ATOM   4527  OG  SER A 610     -56.611  -7.132-102.831  1.00104.15           O  
ANISOU 4527  OG  SER A 610    13061  12680  13831   -547  -1086    781       O  
ATOM   4528  N   ILE A 611     -60.772  -7.064-101.043  1.00106.30           N  
ANISOU 4528  N   ILE A 611    13293  12893  14202   -296  -1182    612       N  
ATOM   4529  CA  ILE A 611     -62.153  -7.392-100.684  1.00105.31           C  
ANISOU 4529  CA  ILE A 611    13127  12792  14092   -220  -1200    553       C  
ATOM   4530  C   ILE A 611     -63.123  -6.447-101.394  1.00106.37           C  
ANISOU 4530  C   ILE A 611    13322  12862  14229   -159  -1269    540       C  
ATOM   4531  O   ILE A 611     -64.100  -6.896-101.994  1.00107.25           O  
ANISOU 4531  O   ILE A 611    13416  12998  14334   -110  -1281    523       O  
ATOM   4532  CB  ILE A 611     -62.362  -7.330 -99.149  1.00106.08           C  
ANISOU 4532  CB  ILE A 611    13177  12913  14214   -204  -1193    494       C  
ATOM   4533  CG1 ILE A 611     -61.839  -8.607 -98.473  1.00104.77           C  
ANISOU 4533  CG1 ILE A 611    12941  12824  14040   -243  -1130    493       C  
ATOM   4534  CG2 ILE A 611     -63.817  -7.036 -98.779  1.00106.71           C  
ANISOU 4534  CG2 ILE A 611    13234  13002  14306   -123  -1233    425       C  
ATOM   4535  CD1 ILE A 611     -62.604  -9.869 -98.806  1.00104.98           C  
ANISOU 4535  CD1 ILE A 611    12919  12915  14050   -224  -1108    482       C  
ATOM   4536  N   GLN A 612     -62.832  -5.146-101.333  1.00106.03           N  
ANISOU 4536  N   GLN A 612    13358  12734  14193   -164  -1319    548       N  
ATOM   4537  CA  GLN A 612     -63.655  -4.125-101.978  1.00106.23           C  
ANISOU 4537  CA  GLN A 612    13462  12681  14217   -103  -1400    536       C  
ATOM   4538  C   GLN A 612     -63.708  -4.301-103.493  1.00103.12           C  
ANISOU 4538  C   GLN A 612    13115  12269  13794   -112  -1409    590       C  
ATOM   4539  O   GLN A 612     -64.765  -4.127-104.101  1.00104.46           O  
ANISOU 4539  O   GLN A 612    13307  12421  13961    -39  -1458    564       O  
ATOM   4540  CB  GLN A 612     -63.163  -2.717-101.610  1.00111.36           C  
ANISOU 4540  CB  GLN A 612    14204  13232  14873   -120  -1457    542       C  
ATOM   4541  CG  GLN A 612     -63.916  -1.567-102.278  1.00115.45           C  
ANISOU 4541  CG  GLN A 612    14828  13651  15385    -55  -1556    531       C  
ATOM   4542  CD  GLN A 612     -65.423  -1.647-102.089  1.00117.49           C  
ANISOU 4542  CD  GLN A 612    15044  13940  15657     65  -1597    446       C  
ATOM   4543  OE1 GLN A 612     -65.917  -1.808-100.971  1.00119.40           O  
ANISOU 4543  OE1 GLN A 612    15210  14235  15919    111  -1588    375       O  
ATOM   4544  NE2 GLN A 612     -66.161  -1.532-103.188  1.00118.00           N  
ANISOU 4544  NE2 GLN A 612    15152  13977  15704    117  -1644    450       N  
ATOM   4545  N   LEU A 613     -62.569  -4.642-104.091  1.00100.03           N  
ANISOU 4545  N   LEU A 613    12737  11891  13378   -199  -1364    659       N  
ATOM   4546  CA  LEU A 613     -62.492  -4.943-105.520  1.00 99.49           C  
ANISOU 4546  CA  LEU A 613    12703  11821  13275   -217  -1362    713       C  
ATOM   4547  C   LEU A 613     -63.465  -6.045-105.923  1.00101.06           C  
ANISOU 4547  C   LEU A 613    12835  12086  13475   -156  -1344    685       C  
ATOM   4548  O   LEU A 613     -64.153  -5.930-106.942  1.00102.19           O  
ANISOU 4548  O   LEU A 613    13019  12205  13604   -114  -1382    693       O  
ATOM   4549  CB  LEU A 613     -61.074  -5.362-105.908  1.00 97.93           C  
ANISOU 4549  CB  LEU A 613    12497  11663  13047   -318  -1302    778       C  
ATOM   4550  CG  LEU A 613     -60.233  -4.458-106.803  1.00 96.65           C  
ANISOU 4550  CG  LEU A 613    12433  11442  12847   -396  -1324    847       C  
ATOM   4551  CD1 LEU A 613     -58.784  -4.920-106.785  1.00 97.13           C  
ANISOU 4551  CD1 LEU A 613    12452  11571  12879   -495  -1256    888       C  
ATOM   4552  CD2 LEU A 613     -60.776  -4.475-108.219  1.00 96.40           C  
ANISOU 4552  CD2 LEU A 613    12455  11389  12784   -373  -1353    879       C  
ATOM   4553  N   CYS A 614     -63.514  -7.102-105.112  1.00100.61           N  
ANISOU 4553  N   CYS A 614    12683  12111  13432   -154  -1291    652       N  
ATOM   4554  CA  CYS A 614     -64.353  -8.268-105.380  1.00100.41           C  
ANISOU 4554  CA  CYS A 614    12592  12154  13403   -114  -1271    627       C  
ATOM   4555  C   CYS A 614     -65.838  -7.943-105.405  1.00100.79           C  
ANISOU 4555  C   CYS A 614    12635  12194  13465    -25  -1324    567       C  
ATOM   4556  O   CYS A 614     -66.584  -8.535-106.180  1.00100.14           O  
ANISOU 4556  O   CYS A 614    12536  12140  13371      8  -1330    562       O  
ATOM   4557  CB  CYS A 614     -64.074  -9.375-104.369  1.00100.61           C  
ANISOU 4557  CB  CYS A 614    12531  12257  13436   -139  -1212    604       C  
ATOM   4558  SG  CYS A 614     -62.517 -10.239-104.660  1.00100.74           S  
ANISOU 4558  SG  CYS A 614    12536  12315  13426   -219  -1151    662       S  
ATOM   4559  N   ARG A 615     -66.260  -7.010-104.554  1.00103.71           N  
ANISOU 4559  N   ARG A 615    13016  12530  13857     13  -1365    518       N  
ATOM   4560  CA  ARG A 615     -67.621  -6.489-104.608  1.00107.59           C  
ANISOU 4560  CA  ARG A 615    13509  13011  14356    108  -1428    453       C  
ATOM   4561  C   ARG A 615     -67.869  -5.902-105.990  1.00109.28           C  
ANISOU 4561  C   ARG A 615    13813  13156  14552    138  -1485    486       C  
ATOM   4562  O   ARG A 615     -68.795  -6.316-106.690  1.00111.80           O  
ANISOU 4562  O   ARG A 615    14112  13504  14862    190  -1503    465       O  
ATOM   4563  CB  ARG A 615     -67.853  -5.425-103.536  1.00109.93           C  
ANISOU 4563  CB  ARG A 615    13820  13273  14675    149  -1473    396       C  
ATOM   4564  CG  ARG A 615     -67.913  -5.965-102.122  1.00113.02           C  
ANISOU 4564  CG  ARG A 615    14117  13744  15082    137  -1426    346       C  
ATOM   4565  CD  ARG A 615     -68.206  -4.857-101.124  1.00117.12           C  
ANISOU 4565  CD  ARG A 615    14651  14229  15619    190  -1477    283       C  
ATOM   4566  NE  ARG A 615     -68.273  -5.377 -99.761  1.00120.94           N  
ANISOU 4566  NE  ARG A 615    15043  14794  16112    176  -1430    235       N  
ATOM   4567  CZ  ARG A 615     -69.338  -5.981 -99.237  1.00125.11           C  
ANISOU 4567  CZ  ARG A 615    15478  15423  16635    215  -1417    166       C  
ATOM   4568  NH1 ARG A 615     -70.446  -6.145 -99.954  1.00129.65           N  
ANISOU 4568  NH1 ARG A 615    16031  16031  17197    276  -1447    132       N  
ATOM   4569  NH2 ARG A 615     -69.296  -6.424 -97.988  1.00125.36           N  
ANISOU 4569  NH2 ARG A 615    15437  15525  16669    189  -1373    131       N  
ATOM   4570  N   ASP A 616     -67.012  -4.964-106.386  1.00108.38           N  
ANISOU 4570  N   ASP A 616    13799  12951  14427     97  -1514    541       N  
ATOM   4571  CA  ASP A 616     -67.113  -4.297-107.679  1.00109.48           C  
ANISOU 4571  CA  ASP A 616    14044  13010  14541    111  -1572    582       C  
ATOM   4572  C   ASP A 616     -67.039  -5.288-108.836  1.00107.86           C  
ANISOU 4572  C   ASP A 616    13819  12852  14310     87  -1532    629       C  
ATOM   4573  O   ASP A 616     -67.733  -5.141-109.843  1.00109.07           O  
ANISOU 4573  O   ASP A 616    14016  12978  14447    137  -1578    631       O  
ATOM   4574  CB  ASP A 616     -66.026  -3.234-107.796  1.00112.44           C  
ANISOU 4574  CB  ASP A 616    14528  13290  14901     40  -1597    643       C  
ATOM   4575  CG  ASP A 616     -66.104  -2.203-106.682  1.00115.71           C  
ANISOU 4575  CG  ASP A 616    14974  13649  15341     69  -1647    595       C  
ATOM   4576  OD1 ASP A 616     -67.231  -1.844-106.276  1.00118.35           O  
ANISOU 4576  OD1 ASP A 616    15296  13978  15692    173  -1705    516       O  
ATOM   4577  OD2 ASP A 616     -65.040  -1.753-106.210  1.00117.45           O  
ANISOU 4577  OD2 ASP A 616    15228  13836  15561    -10  -1631    632       O  
ATOM   4578  N   ALA A 617     -66.208  -6.309-108.664  1.00106.09           N  
ANISOU 4578  N   ALA A 617    13529  12697  14080     16  -1450    662       N  
ATOM   4579  CA  ALA A 617     -66.084  -7.397-109.627  1.00103.86           C  
ANISOU 4579  CA  ALA A 617    13217  12471  13774     -3  -1409    699       C  
ATOM   4580  C   ALA A 617     -67.339  -8.274-109.698  1.00100.30           C  
ANISOU 4580  C   ALA A 617    12694  12082  13333     66  -1411    644       C  
ATOM   4581  O   ALA A 617     -67.598  -8.912-110.718  1.00 99.79           O  
ANISOU 4581  O   ALA A 617    12628  12039  13247     76  -1407    665       O  
ATOM   4582  CB  ALA A 617     -64.865  -8.243-109.293  1.00104.53           C  
ANISOU 4582  CB  ALA A 617    13251  12615  13849    -85  -1331    735       C  
ATOM   4583  N   GLY A 618     -68.113  -8.303-108.618  1.00 96.96           N  
ANISOU 4583  N   GLY A 618    12209  11692  12937    109  -1418    573       N  
ATOM   4584  CA  GLY A 618     -69.305  -9.144-108.551  1.00 95.93           C  
ANISOU 4584  CA  GLY A 618    12000  11636  12811    161  -1416    516       C  
ATOM   4585  C   GLY A 618     -69.003 -10.544-108.050  1.00 93.63           C  
ANISOU 4585  C   GLY A 618    11628  11430  12517    108  -1345    520       C  
ATOM   4586  O   GLY A 618     -69.746 -11.495-108.323  1.00 93.00           O  
ANISOU 4586  O   GLY A 618    11496  11409  12428    123  -1335    499       O  
ATOM   4587  N   ILE A 619     -67.909 -10.657-107.303  1.00 92.10           N  
ANISOU 4587  N   ILE A 619    11427  11237  12328     45  -1301    546       N  
ATOM   4588  CA  ILE A 619     -67.437 -11.929-106.762  1.00 89.60           C  
ANISOU 4588  CA  ILE A 619    11051  10988  12005     -5  -1242    553       C  
ATOM   4589  C   ILE A 619     -67.656 -11.989-105.240  1.00 89.45           C  
ANISOU 4589  C   ILE A 619    10974  11006  12005    -13  -1224    501       C  
ATOM   4590  O   ILE A 619     -67.214 -11.103-104.495  1.00 89.51           O  
ANISOU 4590  O   ILE A 619    10999  10979  12030    -19  -1231    492       O  
ATOM   4591  CB  ILE A 619     -65.948 -12.160-107.123  1.00 87.82           C  
ANISOU 4591  CB  ILE A 619    10857  10749  11762    -69  -1205    619       C  
ATOM   4592  CG1 ILE A 619     -65.750 -12.074-108.642  1.00 86.13           C  
ANISOU 4592  CG1 ILE A 619    10696  10507  11521    -64  -1221    669       C  
ATOM   4593  CG2 ILE A 619     -65.455 -13.495-106.580  1.00 86.95           C  
ANISOU 4593  CG2 ILE A 619    10694  10702  11642   -108  -1155    620       C  
ATOM   4594  CD1 ILE A 619     -64.331 -11.797-109.078  1.00 84.35           C  
ANISOU 4594  CD1 ILE A 619    10511  10263  11272   -124  -1197    729       C  
ATOM   4595  N   ARG A 620     -68.353 -13.033-104.792  1.00 88.55           N  
ANISOU 4595  N   ARG A 620    10795  10965  11885    -18  -1204    466       N  
ATOM   4596  CA  ARG A 620     -68.612 -13.256-103.368  1.00 88.04           C  
ANISOU 4596  CA  ARG A 620    10672  10950  11828    -36  -1183    418       C  
ATOM   4597  C   ARG A 620     -67.371 -13.828-102.704  1.00 87.26           C  
ANISOU 4597  C   ARG A 620    10576  10854  11726   -100  -1138    452       C  
ATOM   4598  O   ARG A 620     -66.646 -14.619-103.310  1.00 87.31           O  
ANISOU 4598  O   ARG A 620    10600  10859  11713   -131  -1117    498       O  
ATOM   4599  CB  ARG A 620     -69.794 -14.210-103.181  1.00 88.17           C  
ANISOU 4599  CB  ARG A 620    10623  11047  11827    -34  -1178    374       C  
ATOM   4600  CG  ARG A 620     -70.419 -14.186-101.793  1.00 88.12           C  
ANISOU 4600  CG  ARG A 620    10552  11104  11823    -42  -1167    311       C  
ATOM   4601  CD  ARG A 620     -71.896 -14.548-101.857  1.00 89.40           C  
ANISOU 4601  CD  ARG A 620    10652  11347  11969    -18  -1183    251       C  
ATOM   4602  NE  ARG A 620     -72.115 -15.941-102.254  1.00 90.53           N  
ANISOU 4602  NE  ARG A 620    10779  11533  12082    -69  -1162    275       N  
ATOM   4603  CZ  ARG A 620     -72.186 -16.969-101.406  1.00 90.80           C  
ANISOU 4603  CZ  ARG A 620    10779  11627  12093   -138  -1130    268       C  
ATOM   4604  NH1 ARG A 620     -72.060 -16.779-100.096  1.00 90.64           N  
ANISOU 4604  NH1 ARG A 620    10728  11636  12072   -165  -1109    239       N  
ATOM   4605  NH2 ARG A 620     -72.387 -18.196-101.866  1.00 89.21           N  
ANISOU 4605  NH2 ARG A 620    10581  11451  11864   -183  -1123    292       N  
ATOM   4606  N   VAL A 621     -67.121 -13.419-101.464  1.00 86.21           N  
ANISOU 4606  N   VAL A 621    10422  10725  11606   -114  -1126    425       N  
ATOM   4607  CA  VAL A 621     -65.959 -13.912-100.725  1.00 84.44           C  
ANISOU 4607  CA  VAL A 621    10198  10505  11379   -169  -1088    449       C  
ATOM   4608  C   VAL A 621     -66.391 -14.594 -99.423  1.00 84.88           C  
ANISOU 4608  C   VAL A 621    10200  10622  11427   -195  -1066    407       C  
ATOM   4609  O   VAL A 621     -67.087 -13.996 -98.596  1.00 87.54           O  
ANISOU 4609  O   VAL A 621    10504  10980  11774   -174  -1076    355       O  
ATOM   4610  CB  VAL A 621     -64.919 -12.795-100.482  1.00 82.61           C  
ANISOU 4610  CB  VAL A 621    10006  10215  11166   -178  -1091    469       C  
ATOM   4611  CG1 VAL A 621     -63.875 -13.228 -99.467  1.00 81.93           C  
ANISOU 4611  CG1 VAL A 621     9906  10145  11079   -227  -1055    476       C  
ATOM   4612  CG2 VAL A 621     -64.247 -12.413-101.791  1.00 82.30           C  
ANISOU 4612  CG2 VAL A 621    10022  10126  11118   -181  -1102    525       C  
ATOM   4613  N   ILE A 622     -65.994 -15.855 -99.264  1.00 82.23           N  
ANISOU 4613  N   ILE A 622     9859  10315  11066   -239  -1040    426       N  
ATOM   4614  CA  ILE A 622     -66.325 -16.613 -98.068  1.00 80.27           C  
ANISOU 4614  CA  ILE A 622     9576  10121  10801   -278  -1021    396       C  
ATOM   4615  C   ILE A 622     -65.059 -16.938 -97.282  1.00 81.03           C  
ANISOU 4615  C   ILE A 622     9691  10203  10894   -316   -998    415       C  
ATOM   4616  O   ILE A 622     -64.198 -17.681 -97.756  1.00 81.05           O  
ANISOU 4616  O   ILE A 622     9723  10190  10880   -332   -991    453       O  
ATOM   4617  CB  ILE A 622     -67.070 -17.925 -98.392  1.00 79.07           C  
ANISOU 4617  CB  ILE A 622     9412  10016  10615   -305  -1021    396       C  
ATOM   4618  CG1 ILE A 622     -68.083 -17.732 -99.528  1.00 78.34           C  
ANISOU 4618  CG1 ILE A 622     9310   9931  10524   -265  -1047    388       C  
ATOM   4619  CG2 ILE A 622     -67.740 -18.465 -97.136  1.00 79.48           C  
ANISOU 4619  CG2 ILE A 622     9423  10131  10643   -351  -1008    356       C  
ATOM   4620  CD1 ILE A 622     -68.679 -19.021-100.070  1.00 76.40           C  
ANISOU 4620  CD1 ILE A 622     9064   9720  10244   -293  -1051    398       C  
ATOM   4621  N   MET A 623     -64.950 -16.372 -96.081  1.00 81.99           N  
ANISOU 4621  N   MET A 623     9792  10331  11029   -323   -989    385       N  
ATOM   4622  CA  MET A 623     -63.854 -16.694 -95.170  1.00 82.51           C  
ANISOU 4622  CA  MET A 623     9870  10390  11089   -358   -968    394       C  
ATOM   4623  C   MET A 623     -64.108 -18.001 -94.418  1.00 82.55           C  
ANISOU 4623  C   MET A 623     9869  10439  11057   -405   -958    385       C  
ATOM   4624  O   MET A 623     -65.155 -18.166 -93.780  1.00 82.68           O  
ANISOU 4624  O   MET A 623     9851  10505  11059   -422   -956    349       O  
ATOM   4625  CB  MET A 623     -63.636 -15.565 -94.158  1.00 83.84           C  
ANISOU 4625  CB  MET A 623    10023  10545  11284   -348   -966    364       C  
ATOM   4626  CG  MET A 623     -62.595 -15.891 -93.089  1.00 85.02           C  
ANISOU 4626  CG  MET A 623    10179  10694  11428   -383   -946    366       C  
ATOM   4627  SD  MET A 623     -62.771 -14.965 -91.551  1.00 85.61           S  
ANISOU 4627  SD  MET A 623    10224  10781  11521   -380   -942    315       S  
ATOM   4628  CE  MET A 623     -62.150 -13.358 -92.055  1.00 85.20           C  
ANISOU 4628  CE  MET A 623    10198  10660  11514   -343   -963    326       C  
ATOM   4629  N   ILE A 624     -63.140 -18.915 -94.493  1.00 81.73           N  
ANISOU 4629  N   ILE A 624     9802  10320  10932   -426   -955    415       N  
ATOM   4630  CA  ILE A 624     -63.127 -20.108 -93.650  1.00 81.86           C  
ANISOU 4630  CA  ILE A 624     9834  10360  10909   -472   -954    410       C  
ATOM   4631  C   ILE A 624     -62.057 -19.944 -92.566  1.00 83.19           C  
ANISOU 4631  C   ILE A 624    10011  10514  11080   -483   -943    403       C  
ATOM   4632  O   ILE A 624     -60.899 -19.637 -92.867  1.00 84.27           O  
ANISOU 4632  O   ILE A 624    10163  10621  11232   -462   -941    421       O  
ATOM   4633  CB  ILE A 624     -62.898 -21.389 -94.469  1.00 81.70           C  
ANISOU 4633  CB  ILE A 624     9858  10329  10853   -480   -973    440       C  
ATOM   4634  CG1 ILE A 624     -63.939 -21.501 -95.583  1.00 84.30           C  
ANISOU 4634  CG1 ILE A 624    10177  10671  11181   -467   -984    446       C  
ATOM   4635  CG2 ILE A 624     -62.990 -22.614 -93.581  1.00 80.99           C  
ANISOU 4635  CG2 ILE A 624     9801  10253  10717   -533   -983    436       C  
ATOM   4636  CD1 ILE A 624     -63.666 -22.614 -96.576  1.00 86.29           C  
ANISOU 4636  CD1 ILE A 624    10475  10907  11404   -463  -1007    476       C  
ATOM   4637  N   THR A 625     -62.458 -20.137 -91.308  1.00 84.93           N  
ANISOU 4637  N   THR A 625    10220  10764  11284   -520   -934    376       N  
ATOM   4638  CA  THR A 625     -61.597 -19.871 -90.148  1.00 86.90           C  
ANISOU 4638  CA  THR A 625    10474  11005  11539   -529   -924    363       C  
ATOM   4639  C   THR A 625     -61.500 -21.005 -89.148  1.00 87.02           C  
ANISOU 4639  C   THR A 625    10522  11033  11505   -579   -930    359       C  
ATOM   4640  O   THR A 625     -62.294 -21.952 -89.165  1.00 87.36           O  
ANISOU 4640  O   THR A 625    10583  11100  11508   -620   -940    363       O  
ATOM   4641  CB  THR A 625     -62.068 -18.646 -89.334  1.00 89.37           C  
ANISOU 4641  CB  THR A 625    10738  11335  11880   -519   -910    325       C  
ATOM   4642  OG1 THR A 625     -63.276 -18.107 -89.894  1.00 90.99           O  
ANISOU 4642  OG1 THR A 625    10906  11566  12098   -499   -913    307       O  
ATOM   4643  CG2 THR A 625     -60.998 -17.588 -89.310  1.00 88.91           C  
ANISOU 4643  CG2 THR A 625    10681  11236  11863   -487   -907    329       C  
ATOM   4644  N   GLY A 626     -60.515 -20.880 -88.265  1.00 86.58           N  
ANISOU 4644  N   GLY A 626    10481  10962  11453   -578   -927    351       N  
ATOM   4645  CA  GLY A 626     -60.385 -21.767 -87.124  1.00 87.90           C  
ANISOU 4645  CA  GLY A 626    10684  11138  11575   -623   -935    343       C  
ATOM   4646  C   GLY A 626     -60.867 -21.039 -85.893  1.00 88.64           C  
ANISOU 4646  C   GLY A 626    10736  11266  11675   -645   -912    308       C  
ATOM   4647  O   GLY A 626     -61.084 -21.648 -84.843  1.00 89.91           O  
ANISOU 4647  O   GLY A 626    10919  11449  11794   -694   -914    297       O  
ATOM   4648  N   ASP A 627     -61.032 -19.725 -86.034  1.00 89.56           N  
ANISOU 4648  N   ASP A 627    10800  11387  11841   -607   -897    289       N  
ATOM   4649  CA  ASP A 627     -61.516 -18.876 -84.952  1.00 92.89           C  
ANISOU 4649  CA  ASP A 627    11177  11844  12273   -611   -880    248       C  
ATOM   4650  C   ASP A 627     -62.904 -19.290 -84.513  1.00 91.67           C  
ANISOU 4650  C   ASP A 627    10993  11760  12077   -657   -872    224       C  
ATOM   4651  O   ASP A 627     -63.667 -19.839 -85.308  1.00 91.71           O  
ANISOU 4651  O   ASP A 627    10997  11785  12063   -672   -878    237       O  
ATOM   4652  CB  ASP A 627     -61.555 -17.416 -85.403  1.00 97.38           C  
ANISOU 4652  CB  ASP A 627    11706  12395  12899   -554   -878    232       C  
ATOM   4653  CG  ASP A 627     -60.266 -16.681 -85.109  1.00102.17           C  
ANISOU 4653  CG  ASP A 627    12325  12953  13540   -529   -879    236       C  
ATOM   4654  OD1 ASP A 627     -59.884 -16.598 -83.912  1.00103.78           O  
ANISOU 4654  OD1 ASP A 627    12528  13165  13736   -544   -872    214       O  
ATOM   4655  OD2 ASP A 627     -59.641 -16.186 -86.076  1.00101.92           O  
ANISOU 4655  OD2 ASP A 627    12304  12879  13539   -501   -886    261       O  
ATOM   4656  N   ASN A 628     -63.233 -19.027 -83.252  1.00 89.63           N  
ANISOU 4656  N   ASN A 628    10706  11547  11799   -681   -858    187       N  
ATOM   4657  CA  ASN A 628     -64.607 -19.194 -82.805  1.00 90.17           C  
ANISOU 4657  CA  ASN A 628    10727  11705  11827   -724   -845    153       C  
ATOM   4658  C   ASN A 628     -65.525 -18.189 -83.512  1.00 90.65           C  
ANISOU 4658  C   ASN A 628    10721  11798  11922   -669   -845    120       C  
ATOM   4659  O   ASN A 628     -65.090 -17.096 -83.884  1.00 89.51           O  
ANISOU 4659  O   ASN A 628    10568  11607  11834   -599   -854    112       O  
ATOM   4660  CB  ASN A 628     -64.715 -19.089 -81.282  1.00 90.09           C  
ANISOU 4660  CB  ASN A 628    10697  11746  11784   -761   -828    117       C  
ATOM   4661  CG  ASN A 628     -64.175 -17.782 -80.741  1.00 90.36           C  
ANISOU 4661  CG  ASN A 628    10702  11759  11869   -697   -825     83       C  
ATOM   4662  OD1 ASN A 628     -64.520 -16.700 -81.218  1.00 91.43           O  
ANISOU 4662  OD1 ASN A 628    10794  11894  12049   -634   -831     56       O  
ATOM   4663  ND2 ASN A 628     -63.337 -17.876 -79.720  1.00 91.06           N  
ANISOU 4663  ND2 ASN A 628    10820  11827  11949   -713   -822     83       N  
ATOM   4664  N   LYS A 629     -66.788 -18.575 -83.694  1.00 91.67           N  
ANISOU 4664  N   LYS A 629    10809  12007  12014   -702   -840     99       N  
ATOM   4665  CA  LYS A 629     -67.755 -17.809 -84.487  1.00 90.31           C  
ANISOU 4665  CA  LYS A 629    10577  11870  11866   -647   -848     65       C  
ATOM   4666  C   LYS A 629     -67.689 -16.311 -84.242  1.00 89.79           C  
ANISOU 4666  C   LYS A 629    10474  11793  11850   -563   -857     18       C  
ATOM   4667  O   LYS A 629     -67.555 -15.536 -85.189  1.00 88.69           O  
ANISOU 4667  O   LYS A 629    10342  11597  11758   -494   -879     24       O  
ATOM   4668  CB  LYS A 629     -69.181 -18.315 -84.235  1.00 90.40           C  
ANISOU 4668  CB  LYS A 629    10526  12002  11817   -703   -835     26       C  
ATOM   4669  CG  LYS A 629     -70.240 -17.707 -85.148  1.00 88.78           C  
ANISOU 4669  CG  LYS A 629    10259  11841  11629   -645   -849    -11       C  
ATOM   4670  CD  LYS A 629     -71.514 -18.531 -85.126  1.00 88.16           C  
ANISOU 4670  CD  LYS A 629    10129  11880  11485   -719   -837    -35       C  
ATOM   4671  CE  LYS A 629     -72.655 -17.808 -85.810  1.00 88.32           C  
ANISOU 4671  CE  LYS A 629    10070  11968  11517   -653   -851    -94       C  
ATOM   4672  NZ  LYS A 629     -73.953 -18.420 -85.422  1.00 89.26           N  
ANISOU 4672  NZ  LYS A 629    10113  12237  11563   -729   -833   -139       N  
ATOM   4673  N   GLY A 630     -67.782 -15.920 -82.972  1.00 90.32           N  
ANISOU 4673  N   GLY A 630    10507  11910  11901   -570   -844    -27       N  
ATOM   4674  CA  GLY A 630     -67.822 -14.509 -82.584  1.00 91.91           C  
ANISOU 4674  CA  GLY A 630    10673  12107  12141   -489   -859    -81       C  
ATOM   4675  C   GLY A 630     -66.693 -13.694 -83.180  1.00 90.49           C  
ANISOU 4675  C   GLY A 630    10549  11804  12026   -431   -882    -47       C  
ATOM   4676  O   GLY A 630     -66.930 -12.675 -83.838  1.00 90.82           O  
ANISOU 4676  O   GLY A 630    10585  11813  12106   -358   -912    -66       O  
ATOM   4677  N   THR A 631     -65.470 -14.163 -82.943  1.00 88.45           N  
ANISOU 4677  N   THR A 631    10348  11484  11775   -467   -872      3       N  
ATOM   4678  CA  THR A 631     -64.254 -13.572 -83.486  1.00 88.14           C  
ANISOU 4678  CA  THR A 631    10361  11341  11786   -434   -888     42       C  
ATOM   4679  C   THR A 631     -64.234 -13.655 -85.015  1.00 89.89           C  
ANISOU 4679  C   THR A 631    10609  11516  12028   -415   -902     85       C  
ATOM   4680  O   THR A 631     -63.861 -12.689 -85.696  1.00 89.05           O  
ANISOU 4680  O   THR A 631    10524  11347  11964   -367   -925     95       O  
ATOM   4681  CB  THR A 631     -63.024 -14.287 -82.905  1.00 87.30           C  
ANISOU 4681  CB  THR A 631    10298  11200  11669   -481   -872     79       C  
ATOM   4682  OG1 THR A 631     -63.080 -14.218 -81.474  1.00 89.16           O  
ANISOU 4682  OG1 THR A 631    10512  11480  11883   -500   -860     40       O  
ATOM   4683  CG2 THR A 631     -61.734 -13.649 -83.388  1.00 87.21           C  
ANISOU 4683  CG2 THR A 631    10328  11102  11704   -455   -885    113       C  
ATOM   4684  N   ALA A 632     -64.655 -14.812 -85.535  1.00 91.73           N  
ANISOU 4684  N   ALA A 632    10845  11780  12226   -456   -892    111       N  
ATOM   4685  CA  ALA A 632     -64.759 -15.071 -86.980  1.00 88.95           C  
ANISOU 4685  CA  ALA A 632    10516  11396  11884   -441   -904    150       C  
ATOM   4686  C   ALA A 632     -65.627 -14.039 -87.691  1.00 86.21           C  
ANISOU 4686  C   ALA A 632    10141  11051  11562   -377   -929    119       C  
ATOM   4687  O   ALA A 632     -65.274 -13.573 -88.776  1.00 85.42           O  
ANISOU 4687  O   ALA A 632    10074  10888  11492   -343   -948    150       O  
ATOM   4688  CB  ALA A 632     -65.294 -16.475 -87.233  1.00 88.33           C  
ANISOU 4688  CB  ALA A 632    10441  11363  11757   -497   -894    169       C  
ATOM   4689  N   ILE A 633     -66.756 -13.694 -87.076  1.00 83.89           N  
ANISOU 4689  N   ILE A 633     9788  10833  11253   -359   -932     55       N  
ATOM   4690  CA  ILE A 633     -67.641 -12.665 -87.610  1.00 83.25           C  
ANISOU 4690  CA  ILE A 633     9679  10760  11192   -284   -965      9       C  
ATOM   4691  C   ILE A 633     -66.946 -11.308 -87.542  1.00 82.72           C  
ANISOU 4691  C   ILE A 633     9648  10610  11172   -226   -995      3       C  
ATOM   4692  O   ILE A 633     -66.913 -10.575 -88.530  1.00 81.75           O  
ANISOU 4692  O   ILE A 633     9560  10423  11077   -177  -1030     17       O  
ATOM   4693  CB  ILE A 633     -69.024 -12.662 -86.908  1.00 82.90           C  
ANISOU 4693  CB  ILE A 633     9551  10836  11110   -276   -962    -69       C  
ATOM   4694  CG1 ILE A 633     -69.832 -13.889 -87.351  1.00 82.59           C  
ANISOU 4694  CG1 ILE A 633     9483  10870  11026   -333   -942    -57       C  
ATOM   4695  CG2 ILE A 633     -69.808 -11.405 -87.243  1.00 82.40           C  
ANISOU 4695  CG2 ILE A 633     9460  10776  11069   -177  -1008   -132       C  
ATOM   4696  CD1 ILE A 633     -71.021 -14.239 -86.480  1.00 82.59           C  
ANISOU 4696  CD1 ILE A 633     9398  11010  10971   -367   -924   -124       C  
ATOM   4697  N   ALA A 634     -66.355 -11.008 -86.389  1.00 83.44           N  
ANISOU 4697  N   ALA A 634     9738  10697  11267   -238   -985    -13       N  
ATOM   4698  CA  ALA A 634     -65.696  -9.722 -86.154  1.00 85.21           C  
ANISOU 4698  CA  ALA A 634     9998  10845  11532   -192  -1016    -23       C  
ATOM   4699  C   ALA A 634     -64.601  -9.404 -87.181  1.00 85.92           C  
ANISOU 4699  C   ALA A 634    10161  10830  11654   -199  -1030     46       C  
ATOM   4700  O   ALA A 634     -64.518  -8.276 -87.679  1.00 87.52           O  
ANISOU 4700  O   ALA A 634    10403  10964  11886   -152  -1073     43       O  
ATOM   4701  CB  ALA A 634     -65.148  -9.658 -84.734  1.00 84.93           C  
ANISOU 4701  CB  ALA A 634     9950  10827  11491   -216   -998    -46       C  
ATOM   4702  N   ILE A 635     -63.774 -10.395 -87.504  1.00 84.89           N  
ANISOU 4702  N   ILE A 635    10051  10688  11513   -258   -997    106       N  
ATOM   4703  CA  ILE A 635     -62.730 -10.222 -88.518  1.00 84.11           C  
ANISOU 4703  CA  ILE A 635    10008  10513  11434   -272  -1002    169       C  
ATOM   4704  C   ILE A 635     -63.344  -9.939 -89.898  1.00 84.70           C  
ANISOU 4704  C   ILE A 635    10104  10562  11514   -237  -1030    186       C  
ATOM   4705  O   ILE A 635     -62.838  -9.103 -90.648  1.00 85.14           O  
ANISOU 4705  O   ILE A 635    10210  10546  11591   -224  -1057    215       O  
ATOM   4706  CB  ILE A 635     -61.762 -11.426 -88.543  1.00 82.62           C  
ANISOU 4706  CB  ILE A 635     9830  10334  11226   -332   -965    217       C  
ATOM   4707  CG1 ILE A 635     -61.134 -11.597 -87.164  1.00 82.63           C  
ANISOU 4707  CG1 ILE A 635     9820  10353  11222   -359   -946    197       C  
ATOM   4708  CG2 ILE A 635     -60.661 -11.237 -89.580  1.00 81.33           C  
ANISOU 4708  CG2 ILE A 635     9713  10113  11076   -346   -969    274       C  
ATOM   4709  CD1 ILE A 635     -60.704 -13.012 -86.854  1.00 84.55           C  
ANISOU 4709  CD1 ILE A 635    10064  10631  11430   -407   -918    219       C  
ATOM   4710  N   CYS A 636     -64.445 -10.622 -90.213  1.00 85.52           N  
ANISOU 4710  N   CYS A 636    10171  10727  11596   -227  -1026    167       N  
ATOM   4711  CA  CYS A 636     -65.184 -10.380 -91.452  1.00 86.28           C  
ANISOU 4711  CA  CYS A 636    10278  10808  11694   -186  -1055    172       C  
ATOM   4712  C   CYS A 636     -65.710  -8.948 -91.501  1.00 89.05           C  
ANISOU 4712  C   CYS A 636    10647  11119  12069   -114  -1109    129       C  
ATOM   4713  O   CYS A 636     -65.762  -8.344 -92.576  1.00 91.32           O  
ANISOU 4713  O   CYS A 636    10981  11345  12367    -82  -1145    151       O  
ATOM   4714  CB  CYS A 636     -66.348 -11.360 -91.603  1.00 85.12           C  
ANISOU 4714  CB  CYS A 636    10079  10746  11516   -191  -1041    148       C  
ATOM   4715  SG  CYS A 636     -65.915 -13.055 -92.047  1.00 81.92           S  
ANISOU 4715  SG  CYS A 636     9680  10365  11078   -263  -1001    207       S  
ATOM   4716  N   ARG A 637     -66.103  -8.412 -90.344  1.00 89.77           N  
ANISOU 4716  N   ARG A 637    10704  11242  12162    -85  -1119     64       N  
ATOM   4717  CA  ARG A 637     -66.528  -7.012 -90.257  1.00 91.02           C  
ANISOU 4717  CA  ARG A 637    10886  11356  12341     -8  -1181     14       C  
ATOM   4718  C   ARG A 637     -65.323  -6.119 -90.507  1.00 91.60           C  
ANISOU 4718  C   ARG A 637    11044  11316  12442    -23  -1205     63       C  
ATOM   4719  O   ARG A 637     -65.406  -5.182 -91.297  1.00 93.26           O  
ANISOU 4719  O   ARG A 637    11318  11450  12666     17  -1260     72       O  
ATOM   4720  CB  ARG A 637     -67.171  -6.678 -88.901  1.00 90.60           C  
ANISOU 4720  CB  ARG A 637    10772  11372  12278     28  -1186    -70       C  
ATOM   4721  CG  ARG A 637     -68.043  -7.781 -88.319  1.00 90.48           C  
ANISOU 4721  CG  ARG A 637    10666  11487  12224      1  -1141   -108       C  
ATOM   4722  CD  ARG A 637     -68.854  -7.325 -87.118  1.00 89.43           C  
ANISOU 4722  CD  ARG A 637    10466  11438  12074     46  -1152   -203       C  
ATOM   4723  NE  ARG A 637     -70.116  -6.737 -87.554  1.00 89.29           N  
ANISOU 4723  NE  ARG A 637    10415  11463  12048    136  -1202   -276       N  
ATOM   4724  CZ  ARG A 637     -71.307  -7.323 -87.465  1.00 88.28           C  
ANISOU 4724  CZ  ARG A 637    10199  11461  11880    142  -1187   -331       C  
ATOM   4725  NH1 ARG A 637     -71.444  -8.530 -86.933  1.00 86.81           N  
ANISOU 4725  NH1 ARG A 637     9957  11369  11657     55  -1124   -318       N  
ATOM   4726  NH2 ARG A 637     -72.373  -6.682 -87.906  1.00 90.25           N  
ANISOU 4726  NH2 ARG A 637    10420  11745  12123    236  -1240   -402       N  
ATOM   4727  N   ARG A 638     -64.205  -6.435 -89.851  1.00 92.10           N  
ANISOU 4727  N   ARG A 638    11111  11371  12510    -87  -1166     96       N  
ATOM   4728  CA  ARG A 638     -62.960  -5.682 -90.004  1.00 94.17           C  
ANISOU 4728  CA  ARG A 638    11444  11542  12794   -119  -1180    143       C  
ATOM   4729  C   ARG A 638     -62.518  -5.560 -91.455  1.00 93.30           C  
ANISOU 4729  C   ARG A 638    11394  11370  12683   -142  -1193    211       C  
ATOM   4730  O   ARG A 638     -62.271  -4.452 -91.931  1.00 94.79           O  
ANISOU 4730  O   ARG A 638    11656  11474  12885   -129  -1244    226       O  
ATOM   4731  CB  ARG A 638     -61.826  -6.310 -89.189  1.00 98.44           C  
ANISOU 4731  CB  ARG A 638    11965  12103  13332   -188  -1129    168       C  
ATOM   4732  CG  ARG A 638     -61.574  -5.672 -87.833  1.00103.35           C  
ANISOU 4732  CG  ARG A 638    12578  12720  13967   -178  -1139    122       C  
ATOM   4733  CD  ARG A 638     -60.388  -6.327 -87.141  1.00106.32           C  
ANISOU 4733  CD  ARG A 638    12940  13114  14339   -244  -1091    150       C  
ATOM   4734  NE  ARG A 638     -59.109  -5.709 -87.493  1.00110.42           N  
ANISOU 4734  NE  ARG A 638    13515  13563  14875   -288  -1100    198       N  
ATOM   4735  CZ  ARG A 638     -57.928  -6.096 -87.008  1.00115.29           C  
ANISOU 4735  CZ  ARG A 638    14125  14190  15490   -343  -1067    221       C  
ATOM   4736  NH1 ARG A 638     -57.852  -7.109 -86.152  1.00116.90           N  
ANISOU 4736  NH1 ARG A 638    14280  14459  15677   -356  -1027    203       N  
ATOM   4737  NH2 ARG A 638     -56.813  -5.473 -87.374  1.00117.02           N  
ANISOU 4737  NH2 ARG A 638    14387  14356  15718   -387  -1076    260       N  
ATOM   4738  N   ILE A 639     -62.423  -6.694 -92.151  1.00 90.98           N  
ANISOU 4738  N   ILE A 639    11077  11118  12370   -176  -1151    251       N  
ATOM   4739  CA  ILE A 639     -61.893  -6.711 -93.521  1.00 90.34           C  
ANISOU 4739  CA  ILE A 639    11047  10993  12283   -204  -1154    318       C  
ATOM   4740  C   ILE A 639     -62.901  -6.242 -94.586  1.00 90.03           C  
ANISOU 4740  C   ILE A 639    11040  10924  12241   -147  -1203    312       C  
ATOM   4741  O   ILE A 639     -62.533  -5.964 -95.729  1.00 89.93           O  
ANISOU 4741  O   ILE A 639    11085  10861  12222   -165  -1218    365       O  
ATOM   4742  CB  ILE A 639     -61.214  -8.057 -93.898  1.00 89.76           C  
ANISOU 4742  CB  ILE A 639    10945  10971  12188   -260  -1097    364       C  
ATOM   4743  CG1 ILE A 639     -62.214  -9.213 -93.913  1.00 91.22           C  
ANISOU 4743  CG1 ILE A 639    11075  11229  12355   -240  -1076    340       C  
ATOM   4744  CG2 ILE A 639     -60.061  -8.355 -92.950  1.00 88.49           C  
ANISOU 4744  CG2 ILE A 639    10767  10826  12028   -310  -1061    371       C  
ATOM   4745  CD1 ILE A 639     -61.682 -10.472 -94.569  1.00 91.82           C  
ANISOU 4745  CD1 ILE A 639    11142  11338  12406   -280  -1038    386       C  
ATOM   4746  N   GLY A 640     -64.169  -6.151 -94.206  1.00 90.26           N  
ANISOU 4746  N   GLY A 640    11031  10991  12271    -79  -1227    246       N  
ATOM   4747  CA  GLY A 640     -65.179  -5.620 -95.110  1.00 92.71           C  
ANISOU 4747  CA  GLY A 640    11370  11275  12580    -11  -1282    226       C  
ATOM   4748  C   GLY A 640     -66.069  -6.657 -95.765  1.00 92.74           C  
ANISOU 4748  C   GLY A 640    11322  11350  12564      2  -1261    221       C  
ATOM   4749  O   GLY A 640     -66.973  -6.302 -96.522  1.00 94.33           O  
ANISOU 4749  O   GLY A 640    11539  11540  12761     63  -1307    199       O  
ATOM   4750  N   ILE A 641     -65.813  -7.936 -95.489  1.00 90.59           N  
ANISOU 4750  N   ILE A 641    10995  11147  12277    -52  -1198    239       N  
ATOM   4751  CA  ILE A 641     -66.736  -8.998 -95.876  1.00 89.91           C  
ANISOU 4751  CA  ILE A 641    10855  11137  12169    -46  -1179    225       C  
ATOM   4752  C   ILE A 641     -68.144  -8.636 -95.387  1.00 92.20           C  
ANISOU 4752  C   ILE A 641    11090  11484  12454     22  -1211    139       C  
ATOM   4753  O   ILE A 641     -69.103  -8.689 -96.156  1.00 94.55           O  
ANISOU 4753  O   ILE A 641    11375  11804  12742     67  -1237    117       O  
ATOM   4754  CB  ILE A 641     -66.292 -10.380 -95.344  1.00 88.57           C  
ANISOU 4754  CB  ILE A 641    10642  11029  11980   -116  -1117    247       C  
ATOM   4755  CG1 ILE A 641     -65.126 -10.914 -96.178  1.00 88.34           C  
ANISOU 4755  CG1 ILE A 641    10656  10961  11945   -165  -1093    324       C  
ATOM   4756  CG2 ILE A 641     -67.442 -11.378 -95.377  1.00 88.29           C  
ANISOU 4756  CG2 ILE A 641    10546  11082  11919   -115  -1104    215       C  
ATOM   4757  CD1 ILE A 641     -64.748 -12.353 -95.883  1.00 87.55           C  
ANISOU 4757  CD1 ILE A 641    10528  10914  11821   -220  -1048    344       C  
ATOM   4758  N   PHE A 642     -68.255  -8.251 -94.118  1.00 92.51           N  
ANISOU 4758  N   PHE A 642    11095  11555  12498     33  -1210     84       N  
ATOM   4759  CA  PHE A 642     -69.497  -7.713 -93.590  1.00 94.30           C  
ANISOU 4759  CA  PHE A 642    11269  11841  12718    108  -1246     -7       C  
ATOM   4760  C   PHE A 642     -69.371  -6.213 -93.361  1.00100.48           C  
ANISOU 4760  C   PHE A 642    12107  12544  13524    178  -1311    -41       C  
ATOM   4761  O   PHE A 642     -68.267  -5.654 -93.417  1.00 99.98           O  
ANISOU 4761  O   PHE A 642    12119  12386  13482    149  -1320     10       O  
ATOM   4762  CB  PHE A 642     -69.878  -8.404 -92.283  1.00 91.94           C  
ANISOU 4762  CB  PHE A 642    10883  11654  12397     75  -1200    -56       C  
ATOM   4763  CG  PHE A 642     -70.165  -9.866 -92.432  1.00 91.28           C  
ANISOU 4763  CG  PHE A 642    10751  11649  12281      5  -1148    -32       C  
ATOM   4764  CD1 PHE A 642     -71.021 -10.326 -93.430  1.00 91.36           C  
ANISOU 4764  CD1 PHE A 642    10743  11694  12276     22  -1158    -34       C  
ATOM   4765  CD2 PHE A 642     -69.596 -10.787 -91.563  1.00 90.40           C  
ANISOU 4765  CD2 PHE A 642    10620  11574  12153    -75  -1094     -8       C  
ATOM   4766  CE1 PHE A 642     -71.290 -11.678 -93.569  1.00 90.10           C  
ANISOU 4766  CE1 PHE A 642    10547  11600  12085    -46  -1116    -10       C  
ATOM   4767  CE2 PHE A 642     -69.856 -12.142 -91.698  1.00 89.98           C  
ANISOU 4767  CE2 PHE A 642    10539  11582  12065   -142  -1056     15       C  
ATOM   4768  CZ  PHE A 642     -70.707 -12.587 -92.701  1.00 90.25           C  
ANISOU 4768  CZ  PHE A 642    10556  11647  12085   -130  -1067     15       C  
ATOM   4769  N   GLY A 643     -70.516  -5.570 -93.126  1.00107.08           N  
ANISOU 4769  N   GLY A 643    12909  13423  14354    269  -1362   -130       N  
ATOM   4770  CA  GLY A 643     -70.565  -4.185 -92.660  1.00111.71           C  
ANISOU 4770  CA  GLY A 643    13539  13948  14955    349  -1434   -184       C  
ATOM   4771  C   GLY A 643     -70.412  -4.137 -91.150  1.00115.06           C  
ANISOU 4771  C   GLY A 643    13908  14430  15377    337  -1407   -234       C  
ATOM   4772  O   GLY A 643     -70.649  -5.135 -90.461  1.00116.04           O  
ANISOU 4772  O   GLY A 643    13945  14664  15479    285  -1342   -248       O  
ATOM   4773  N   GLU A 644     -70.011  -2.980 -90.632  1.00117.61           N  
ANISOU 4773  N   GLU A 644    14289  14676  15721    380  -1460   -258       N  
ATOM   4774  CA  GLU A 644     -69.806  -2.810 -89.195  1.00120.04           C  
ANISOU 4774  CA  GLU A 644    14553  15028  16027    376  -1442   -306       C  
ATOM   4775  C   GLU A 644     -71.101  -2.996 -88.409  1.00120.89           C  
ANISOU 4775  C   GLU A 644    14547  15283  16102    437  -1441   -417       C  
ATOM   4776  O   GLU A 644     -71.075  -3.442 -87.263  1.00124.42           O  
ANISOU 4776  O   GLU A 644    14924  15816  16532    401  -1392   -446       O  
ATOM   4777  CB  GLU A 644     -69.195  -1.441 -88.891  1.00125.02           C  
ANISOU 4777  CB  GLU A 644    15278  15539  16685    420  -1513   -316       C  
ATOM   4778  CG  GLU A 644     -67.901  -1.140 -89.639  1.00133.28           C  
ANISOU 4778  CG  GLU A 644    16437  16447  17756    350  -1518   -210       C  
ATOM   4779  CD  GLU A 644     -66.684  -1.854 -89.072  1.00138.36           C  
ANISOU 4779  CD  GLU A 644    17066  17097  18406    238  -1439   -144       C  
ATOM   4780  OE1 GLU A 644     -66.847  -2.774 -88.236  1.00139.33           O  
ANISOU 4780  OE1 GLU A 644    17098  17325  18514    205  -1374   -166       O  
ATOM   4781  OE2 GLU A 644     -65.553  -1.491 -89.472  1.00142.40           O  
ANISOU 4781  OE2 GLU A 644    17659  17509  18935    180  -1443    -71       O  
ATOM   4782  N   ASN A 645     -72.227  -2.658 -89.031  1.00120.53           N  
ANISOU 4782  N   ASN A 645    14481  15271  16042    529  -1495   -480       N  
ATOM   4783  CA  ASN A 645     -73.535  -2.830 -88.416  1.00120.16           C  
ANISOU 4783  CA  ASN A 645    14314  15383  15957    590  -1496   -593       C  
ATOM   4784  C   ASN A 645     -74.280  -4.034 -88.943  1.00120.36           C  
ANISOU 4784  C   ASN A 645    14257  15522  15950    540  -1442   -584       C  
ATOM   4785  O   ASN A 645     -75.120  -4.597 -88.246  1.00123.92           O  
ANISOU 4785  O   ASN A 645    14593  16129  16361    530  -1405   -653       O  
ATOM   4786  CB  ASN A 645     -74.394  -1.592 -88.639  1.00123.75           C  
ANISOU 4786  CB  ASN A 645    14788  15819  16409    741  -1603   -692       C  
ATOM   4787  CG  ASN A 645     -74.247  -0.576 -87.534  1.00129.54           C  
ANISOU 4787  CG  ASN A 645    15535  16536  17148    810  -1652   -764       C  
ATOM   4788  OD1 ASN A 645     -73.992  -0.926 -86.380  1.00133.02           O  
ANISOU 4788  OD1 ASN A 645    15914  17049  17577    760  -1597   -780       O  
ATOM   4789  ND2 ASN A 645     -74.417   0.696 -87.877  1.00133.64           N  
ANISOU 4789  ND2 ASN A 645    16141  16954  17682    927  -1762   -810       N  
ATOM   4790  N   GLU A 646     -73.959  -4.420 -90.175  1.00119.12           N  
ANISOU 4790  N   GLU A 646    14161  15289  15809    505  -1437   -500       N  
ATOM   4791  CA  GLU A 646     -74.719  -5.414 -90.931  1.00119.10           C  
ANISOU 4791  CA  GLU A 646    14099  15370  15781    475  -1406   -492       C  
ATOM   4792  C   GLU A 646     -75.216  -6.588 -90.096  1.00116.66           C  
ANISOU 4792  C   GLU A 646    13675  15222  15429    394  -1329   -517       C  
ATOM   4793  O   GLU A 646     -74.484  -7.130 -89.280  1.00115.15           O  
ANISOU 4793  O   GLU A 646    13480  15036  15234    307  -1272   -477       O  
ATOM   4794  CB  GLU A 646     -73.888  -5.927 -92.111  1.00119.98           C  
ANISOU 4794  CB  GLU A 646    14295  15374  15914    409  -1386   -374       C  
ATOM   4795  CG  GLU A 646     -74.705  -6.637 -93.179  1.00121.55           C  
ANISOU 4795  CG  GLU A 646    14462  15625  16094    410  -1383   -369       C  
ATOM   4796  CD  GLU A 646     -73.853  -7.404 -94.169  1.00119.18           C  
ANISOU 4796  CD  GLU A 646    14228  15247  15807    329  -1347   -254       C  
ATOM   4797  OE1 GLU A 646     -72.743  -6.931 -94.496  1.00117.20           O  
ANISOU 4797  OE1 GLU A 646    14073  14871  15586    312  -1357   -184       O  
ATOM   4798  OE2 GLU A 646     -74.307  -8.478 -94.625  1.00118.42           O  
ANISOU 4798  OE2 GLU A 646    14086  15219  15688    281  -1310   -237       O  
ATOM   4799  N   GLU A 647     -76.470  -6.967 -90.309  1.00120.93           N  
ANISOU 4799  N   GLU A 647    14123  15892  15931    420  -1331   -586       N  
ATOM   4800  CA  GLU A 647     -77.028  -8.167 -89.703  1.00126.10           C  
ANISOU 4800  CA  GLU A 647    14674  16701  16536    325  -1260   -602       C  
ATOM   4801  C   GLU A 647     -76.381  -9.397 -90.350  1.00126.72           C  
ANISOU 4801  C   GLU A 647    14798  16730  16617    207  -1205   -487       C  
ATOM   4802  O   GLU A 647     -76.252  -9.471 -91.577  1.00128.30           O  
ANISOU 4802  O   GLU A 647    15055  16851  16839    222  -1227   -435       O  
ATOM   4803  CB  GLU A 647     -78.549  -8.194 -89.876  1.00131.07           C  
ANISOU 4803  CB  GLU A 647    15192  17486  17121    382  -1282   -707       C  
ATOM   4804  CG  GLU A 647     -79.304  -8.725 -88.668  1.00137.10           C  
ANISOU 4804  CG  GLU A 647    15827  18442  17823    329  -1233   -784       C  
ATOM   4805  CD  GLU A 647     -78.827 -10.098 -88.237  1.00140.70           C  
ANISOU 4805  CD  GLU A 647    16279  18927  18251    165  -1149   -701       C  
ATOM   4806  OE1 GLU A 647     -78.952 -11.048 -89.042  1.00144.06           O  
ANISOU 4806  OE1 GLU A 647    16716  19353  18668     95  -1126   -643       O  
ATOM   4807  OE2 GLU A 647     -78.316 -10.220 -87.100  1.00141.86           O  
ANISOU 4807  OE2 GLU A 647    16421  19093  18386    110  -1112   -695       O  
ATOM   4808  N   VAL A 648     -75.967 -10.352 -89.520  1.00125.29           N  
ANISOU 4808  N   VAL A 648    14597  16596  16412     94  -1140   -450       N  
ATOM   4809  CA  VAL A 648     -75.142 -11.470 -89.978  1.00121.28           C  
ANISOU 4809  CA  VAL A 648    14148  16024  15907     -9  -1096   -342       C  
ATOM   4810  C   VAL A 648     -75.673 -12.850 -89.558  1.00122.62           C  
ANISOU 4810  C   VAL A 648    14256  16314  16018   -123  -1042   -337       C  
ATOM   4811  O   VAL A 648     -75.264 -13.869 -90.117  1.00122.35           O  
ANISOU 4811  O   VAL A 648    14267  16240  15978   -199  -1019   -259       O  
ATOM   4812  CB  VAL A 648     -73.686 -11.305 -89.492  1.00117.98           C  
ANISOU 4812  CB  VAL A 648    13811  15491  15523    -41  -1080   -275       C  
ATOM   4813  CG1 VAL A 648     -72.829 -12.461 -89.961  1.00118.99           C  
ANISOU 4813  CG1 VAL A 648    13997  15561  15650   -135  -1042   -175       C  
ATOM   4814  CG2 VAL A 648     -73.091 -10.001 -89.994  1.00118.24           C  
ANISOU 4814  CG2 VAL A 648    13918  15398  15610     50  -1134   -267       C  
ATOM   4815  N   ALA A 649     -76.591 -12.871 -88.592  1.00124.41           N  
ANISOU 4815  N   ALA A 649    14384  16689  16196   -137  -1027   -421       N  
ATOM   4816  CA  ALA A 649     -77.086 -14.109 -87.963  1.00123.24           C  
ANISOU 4816  CA  ALA A 649    14179  16665  15981   -263   -975   -419       C  
ATOM   4817  C   ALA A 649     -77.282 -15.319 -88.882  1.00122.50           C  
ANISOU 4817  C   ALA A 649    14109  16569  15866   -344   -961   -356       C  
ATOM   4818  O   ALA A 649     -76.985 -16.444 -88.482  1.00121.69           O  
ANISOU 4818  O   ALA A 649    14031  16477  15726   -463   -924   -303       O  
ATOM   4819  CB  ALA A 649     -78.361 -13.831 -87.181  1.00127.33           C  
ANISOU 4819  CB  ALA A 649    14568  17368  16443   -248   -971   -535       C  
ATOM   4820  N   ASP A 650     -77.780 -15.089 -90.097  1.00124.41           N  
ANISOU 4820  N   ASP A 650    14350  16791  16129   -279   -996   -364       N  
ATOM   4821  CA  ASP A 650     -78.023 -16.178 -91.057  1.00125.27           C  
ANISOU 4821  CA  ASP A 650    14481  16895  16219   -345   -989   -310       C  
ATOM   4822  C   ASP A 650     -77.025 -16.200 -92.232  1.00119.30           C  
ANISOU 4822  C   ASP A 650    13835  15972  15518   -312  -1010   -220       C  
ATOM   4823  O   ASP A 650     -77.289 -16.796 -93.280  1.00116.34           O  
ANISOU 4823  O   ASP A 650    13480  15583  15141   -325  -1021   -188       O  
ATOM   4824  CB  ASP A 650     -79.479 -16.144 -91.559  1.00132.17           C  
ANISOU 4824  CB  ASP A 650    15256  17900  17059   -316  -1008   -389       C  
ATOM   4825  CG  ASP A 650     -79.746 -15.004 -92.543  1.00138.48           C  
ANISOU 4825  CG  ASP A 650    16062  18645  17908   -168  -1067   -427       C  
ATOM   4826  OD1 ASP A 650     -79.172 -13.899 -92.380  1.00140.90           O  
ANISOU 4826  OD1 ASP A 650    16409  18867  18260    -76  -1095   -438       O  
ATOM   4827  OD2 ASP A 650     -80.542 -15.218 -93.484  1.00139.48           O  
ANISOU 4827  OD2 ASP A 650    16160  18812  18024   -146  -1089   -446       O  
ATOM   4828  N   ARG A 651     -75.879 -15.551 -92.042  1.00114.50           N  
ANISOU 4828  N   ARG A 651    13297  15249  14957   -273  -1016   -183       N  
ATOM   4829  CA  ARG A 651     -74.858 -15.449 -93.084  1.00110.52           C  
ANISOU 4829  CA  ARG A 651    12892  14600  14501   -243  -1033   -104       C  
ATOM   4830  C   ARG A 651     -73.470 -15.886 -92.600  1.00106.18           C  
ANISOU 4830  C   ARG A 651    12414  13966  13962   -302  -1005    -32       C  
ATOM   4831  O   ARG A 651     -72.505 -15.860 -93.366  1.00105.12           O  
ANISOU 4831  O   ARG A 651    12355  13724  13860   -287  -1014     32       O  
ATOM   4832  CB  ARG A 651     -74.824 -14.030 -93.661  1.00114.42           C  
ANISOU 4832  CB  ARG A 651    13407  15026  15042   -122  -1082   -131       C  
ATOM   4833  CG  ARG A 651     -75.960 -13.737 -94.634  1.00118.00           C  
ANISOU 4833  CG  ARG A 651    13822  15521  15491    -53  -1122   -178       C  
ATOM   4834  CD  ARG A 651     -76.361 -12.261 -94.680  1.00120.56           C  
ANISOU 4834  CD  ARG A 651    14138  15827  15840     71  -1178   -249       C  
ATOM   4835  NE  ARG A 651     -75.284 -11.348 -95.084  1.00120.21           N  
ANISOU 4835  NE  ARG A 651    14195  15634  15845    120  -1208   -199       N  
ATOM   4836  CZ  ARG A 651     -74.737 -11.293 -96.299  1.00120.84           C  
ANISOU 4836  CZ  ARG A 651    14355  15608  15948    132  -1227   -130       C  
ATOM   4837  NH1 ARG A 651     -75.133 -12.116 -97.267  1.00122.41           N  
ANISOU 4837  NH1 ARG A 651    14551  15827  16133    109  -1221   -101       N  
ATOM   4838  NH2 ARG A 651     -73.775 -10.416 -96.548  1.00119.18           N  
ANISOU 4838  NH2 ARG A 651    14232  15276  15774    163  -1252    -88       N  
ATOM   4839  N   ALA A 652     -73.380 -16.285 -91.330  1.00101.74           N  
ANISOU 4839  N   ALA A 652    11826  13460  13369   -367   -974    -47       N  
ATOM   4840  CA  ALA A 652     -72.167 -16.903 -90.786  1.00 97.02           C  
ANISOU 4840  CA  ALA A 652    11293  12798  12770   -430   -949     14       C  
ATOM   4841  C   ALA A 652     -72.498 -18.095 -89.888  1.00 94.81           C  
ANISOU 4841  C   ALA A 652    10995  12600  12428   -541   -919     15       C  
ATOM   4842  O   ALA A 652     -73.346 -17.997 -88.998  1.00 94.26           O  
ANISOU 4842  O   ALA A 652    10852  12640  12320   -567   -904    -45       O  
ATOM   4843  CB  ALA A 652     -71.329 -15.886 -90.036  1.00 96.86           C  
ANISOU 4843  CB  ALA A 652    11289  12725  12787   -386   -951      3       C  
ATOM   4844  N   TYR A 653     -71.817 -19.213 -90.134  1.00 92.04           N  
ANISOU 4844  N   TYR A 653    10715  12196  12061   -605   -913     82       N  
ATOM   4845  CA  TYR A 653     -72.083 -20.473 -89.440  1.00 91.32           C  
ANISOU 4845  CA  TYR A 653    10633  12160  11903   -719   -896     96       C  
ATOM   4846  C   TYR A 653     -70.798 -21.138 -88.969  1.00 90.15           C  
ANISOU 4846  C   TYR A 653    10572  11928  11750   -759   -893    152       C  
ATOM   4847  O   TYR A 653     -69.759 -20.995 -89.608  1.00 90.99           O  
ANISOU 4847  O   TYR A 653    10736  11937  11898   -709   -906    194       O  
ATOM   4848  CB  TYR A 653     -72.820 -21.441 -90.375  1.00 91.05           C  
ANISOU 4848  CB  TYR A 653    10606  12152  11837   -765   -909    116       C  
ATOM   4849  CG  TYR A 653     -74.207 -20.993 -90.766  1.00 91.67           C  
ANISOU 4849  CG  TYR A 653    10591  12333  11905   -740   -913     53       C  
ATOM   4850  CD1 TYR A 653     -74.411 -20.167 -91.872  1.00 91.96           C  
ANISOU 4850  CD1 TYR A 653    10611  12337  11991   -637   -937     40       C  
ATOM   4851  CD2 TYR A 653     -75.318 -21.400 -90.035  1.00 91.90           C  
ANISOU 4851  CD2 TYR A 653    10547  12499  11870   -821   -895      5       C  
ATOM   4852  CE1 TYR A 653     -75.682 -19.752 -92.232  1.00 92.72           C  
ANISOU 4852  CE1 TYR A 653    10623  12529  12076   -604   -947    -24       C  
ATOM   4853  CE2 TYR A 653     -76.592 -20.991 -90.387  1.00 93.48           C  
ANISOU 4853  CE2 TYR A 653    10652  12809  12057   -793   -900    -61       C  
ATOM   4854  CZ  TYR A 653     -76.767 -20.168 -91.484  1.00 94.19           C  
ANISOU 4854  CZ  TYR A 653    10728  12859  12200   -679   -928    -78       C  
ATOM   4855  OH  TYR A 653     -78.032 -19.764 -91.831  1.00 97.31           O  
ANISOU 4855  OH  TYR A 653    11028  13364  12580   -642   -940   -151       O  
ATOM   4856  N   THR A 654     -70.871 -21.866 -87.855  1.00 89.14           N  
ANISOU 4856  N   THR A 654    10455  11846  11567   -849   -878    151       N  
ATOM   4857  CA  THR A 654     -69.791 -22.778 -87.479  1.00 88.32           C  
ANISOU 4857  CA  THR A 654    10446  11667  11444   -896   -886    205       C  
ATOM   4858  C   THR A 654     -70.039 -24.123 -88.135  1.00 90.05           C  
ANISOU 4858  C   THR A 654    10726  11871  11617   -963   -909    247       C  
ATOM   4859  O   THR A 654     -71.165 -24.418 -88.533  1.00 92.93           O  
ANISOU 4859  O   THR A 654    11049  12305  11952  -1003   -910    231       O  
ATOM   4860  CB  THR A 654     -69.671 -22.986 -85.959  1.00 87.52           C  
ANISOU 4860  CB  THR A 654    10348  11606  11297   -964   -868    189       C  
ATOM   4861  OG1 THR A 654     -70.814 -23.693 -85.467  1.00 87.54           O  
ANISOU 4861  OG1 THR A 654    10321  11713  11226  -1069   -858    170       O  
ATOM   4862  CG2 THR A 654     -69.546 -21.663 -85.250  1.00 88.69           C  
ANISOU 4862  CG2 THR A 654    10432  11779  11486   -899   -848    139       C  
ATOM   4863  N   GLY A 655     -68.993 -24.936 -88.244  1.00 90.66           N  
ANISOU 4863  N   GLY A 655    10900  11858  11686   -973   -933    297       N  
ATOM   4864  CA  GLY A 655     -69.114 -26.272 -88.823  1.00 92.20           C  
ANISOU 4864  CA  GLY A 655    11172  12024  11835  -1032   -967    338       C  
ATOM   4865  C   GLY A 655     -70.114 -27.124 -88.068  1.00 94.99           C  
ANISOU 4865  C   GLY A 655    11529  12454  12107  -1160   -965    331       C  
ATOM   4866  O   GLY A 655     -70.817 -27.938 -88.665  1.00 94.20           O  
ANISOU 4866  O   GLY A 655    11450  12372  11969  -1217   -985    347       O  
ATOM   4867  N   ARG A 656     -70.176 -26.920 -86.753  1.00 99.11           N  
ANISOU 4867  N   ARG A 656    12030  13027  12600  -1210   -941    308       N  
ATOM   4868  CA  ARG A 656     -71.119 -27.624 -85.886  1.00103.45           C  
ANISOU 4868  CA  ARG A 656    12575  13666  13064  -1345   -933    298       C  
ATOM   4869  C   ARG A 656     -72.571 -27.245 -86.178  1.00100.20           C  
ANISOU 4869  C   ARG A 656    12049  13383  12636  -1373   -907    252       C  
ATOM   4870  O   ARG A 656     -73.406 -28.127 -86.369  1.00100.71           O  
ANISOU 4870  O   ARG A 656    12128  13498  12639  -1474   -918    263       O  
ATOM   4871  CB  ARG A 656     -70.783 -27.383 -84.407  1.00110.00           C  
ANISOU 4871  CB  ARG A 656    13403  14523  13866  -1382   -911    281       C  
ATOM   4872  CG  ARG A 656     -71.847 -27.857 -83.426  1.00117.68           C  
ANISOU 4872  CG  ARG A 656    14346  15617  14747  -1522   -890    261       C  
ATOM   4873  CD  ARG A 656     -71.886 -29.375 -83.313  1.00124.17           C  
ANISOU 4873  CD  ARG A 656    15292  16400  15485  -1651   -931    315       C  
ATOM   4874  NE  ARG A 656     -73.210 -29.860 -82.921  1.00133.48           N  
ANISOU 4874  NE  ARG A 656    16428  17710  16577  -1794   -913    299       N  
ATOM   4875  CZ  ARG A 656     -73.719 -29.778 -81.692  1.00138.93           C  
ANISOU 4875  CZ  ARG A 656    17076  18509  17202  -1889   -880    271       C  
ATOM   4876  NH1 ARG A 656     -73.023 -29.217 -80.706  1.00142.06           N  
ANISOU 4876  NH1 ARG A 656    17470  18891  17613  -1849   -862    256       N  
ATOM   4877  NH2 ARG A 656     -74.935 -30.254 -81.448  1.00139.17           N  
ANISOU 4877  NH2 ARG A 656    17060  18669  17147  -2027   -864    256       N  
ATOM   4878  N   GLU A 657     -72.858 -25.940 -86.201  1.00 97.40           N  
ANISOU 4878  N   GLU A 657    11587  13082  12336  -1282   -878    197       N  
ATOM   4879  CA  GLU A 657     -74.192 -25.422 -86.517  1.00 94.98           C  
ANISOU 4879  CA  GLU A 657    11164  12902  12022  -1280   -859    139       C  
ATOM   4880  C   GLU A 657     -74.608 -25.873 -87.902  1.00 93.61           C  
ANISOU 4880  C   GLU A 657    11004  12703  11860  -1267   -886    161       C  
ATOM   4881  O   GLU A 657     -75.756 -26.268 -88.118  1.00 95.88           O  
ANISOU 4881  O   GLU A 657    11239  13091  12099  -1336   -883    138       O  
ATOM   4882  CB  GLU A 657     -74.211 -23.897 -86.494  1.00 95.15           C  
ANISOU 4882  CB  GLU A 657    11093  12947  12110  -1154   -842     80       C  
ATOM   4883  CG  GLU A 657     -73.997 -23.258 -85.137  1.00 99.85           C  
ANISOU 4883  CG  GLU A 657    11652  13589  12697  -1154   -816     41       C  
ATOM   4884  CD  GLU A 657     -73.638 -21.786 -85.244  1.00102.25           C  
ANISOU 4884  CD  GLU A 657    11906  13862  13079  -1014   -815      0       C  
ATOM   4885  OE1 GLU A 657     -73.458 -21.296 -86.378  1.00103.34           O  
ANISOU 4885  OE1 GLU A 657    12052  13934  13277   -923   -836     10       O  
ATOM   4886  OE2 GLU A 657     -73.529 -21.113 -84.196  1.00104.53           O  
ANISOU 4886  OE2 GLU A 657    12156  14192  13367   -997   -797    -41       O  
ATOM   4887  N   PHE A 658     -73.657 -25.803 -88.832  1.00 89.60           N  
ANISOU 4887  N   PHE A 658    10562  12067  11412  -1179   -911    204       N  
ATOM   4888  CA  PHE A 658     -73.879 -26.141 -90.228  1.00 86.28           C  
ANISOU 4888  CA  PHE A 658    10162  11607  11010  -1146   -938    227       C  
ATOM   4889  C   PHE A 658     -74.253 -27.608 -90.368  1.00 89.08           C  
ANISOU 4889  C   PHE A 658    10588  11964  11294  -1267   -964    267       C  
ATOM   4890  O   PHE A 658     -75.038 -27.965 -91.244  1.00 91.14           O  
ANISOU 4890  O   PHE A 658    10829  12255  11542  -1284   -979    265       O  
ATOM   4891  CB  PHE A 658     -72.628 -25.823 -91.043  1.00 81.44           C  
ANISOU 4891  CB  PHE A 658     9613  10863  10465  -1039   -958    267       C  
ATOM   4892  CG  PHE A 658     -72.777 -26.052 -92.515  1.00 78.87           C  
ANISOU 4892  CG  PHE A 658     9306  10496  10163   -992   -984    290       C  
ATOM   4893  CD1 PHE A 658     -73.252 -25.047 -93.341  1.00 78.84           C  
ANISOU 4893  CD1 PHE A 658     9233  10514  10209   -902   -981    258       C  
ATOM   4894  CD2 PHE A 658     -72.415 -27.264 -93.085  1.00 78.56           C  
ANISOU 4894  CD2 PHE A 658     9362  10390  10095  -1032  -1019    341       C  
ATOM   4895  CE1 PHE A 658     -73.381 -25.248 -94.709  1.00 78.11           C  
ANISOU 4895  CE1 PHE A 658     9160  10383  10135   -858  -1006    280       C  
ATOM   4896  CE2 PHE A 658     -72.541 -27.474 -94.450  1.00 78.15           C  
ANISOU 4896  CE2 PHE A 658     9326  10302  10062   -985  -1044    360       C  
ATOM   4897  CZ  PHE A 658     -73.023 -26.465 -95.265  1.00 77.60           C  
ANISOU 4897  CZ  PHE A 658     9182  10259  10041   -901  -1035    331       C  
ATOM   4898  N   ASP A 659     -73.699 -28.449 -89.494  1.00 91.59           N  
ANISOU 4898  N   ASP A 659    10994  12244  11562  -1351   -975    301       N  
ATOM   4899  CA  ASP A 659     -73.964 -29.892 -89.516  1.00 93.24           C  
ANISOU 4899  CA  ASP A 659    11294  12436  11694  -1475  -1010    343       C  
ATOM   4900  C   ASP A 659     -75.323 -30.269 -88.954  1.00 94.20           C  
ANISOU 4900  C   ASP A 659    11356  12698  11737  -1613   -991    314       C  
ATOM   4901  O   ASP A 659     -75.793 -31.379 -89.187  1.00 95.84           O  
ANISOU 4901  O   ASP A 659    11626  12906  11881  -1721  -1022    345       O  
ATOM   4902  CB  ASP A 659     -72.876 -30.663 -88.766  1.00 95.09           C  
ANISOU 4902  CB  ASP A 659    11657  12573  11897  -1513  -1039    388       C  
ATOM   4903  CG  ASP A 659     -71.699 -31.025 -89.651  1.00 96.72           C  
ANISOU 4903  CG  ASP A 659    11962  12640  12145  -1420  -1084    430       C  
ATOM   4904  OD1 ASP A 659     -71.869 -31.075 -90.892  1.00 97.75           O  
ANISOU 4904  OD1 ASP A 659    12086  12746  12306  -1366  -1101    438       O  
ATOM   4905  OD2 ASP A 659     -70.599 -31.262 -89.104  1.00 97.81           O  
ANISOU 4905  OD2 ASP A 659    12180  12699  12282  -1399  -1103    451       O  
ATOM   4906  N   ASP A 660     -75.939 -29.353 -88.207  1.00 94.69           N  
ANISOU 4906  N   ASP A 660    11297  12882  11798  -1611   -943    254       N  
ATOM   4907  CA  ASP A 660     -77.250 -29.585 -87.609  1.00 95.98           C  
ANISOU 4907  CA  ASP A 660    11378  13208  11881  -1739   -917    213       C  
ATOM   4908  C   ASP A 660     -78.383 -29.006 -88.433  1.00 96.14           C  
ANISOU 4908  C   ASP A 660    11271  13336  11920  -1696   -904    156       C  
ATOM   4909  O   ASP A 660     -79.536 -29.012 -87.996  1.00 99.61           O  
ANISOU 4909  O   ASP A 660    11612  13936  12297  -1783   -878    105       O  
ATOM   4910  CB  ASP A 660     -77.300 -29.031 -86.193  1.00100.14           C  
ANISOU 4910  CB  ASP A 660    11846  13823  12379  -1772   -875    173       C  
ATOM   4911  CG  ASP A 660     -76.440 -29.819 -85.239  1.00106.90           C  
ANISOU 4911  CG  ASP A 660    12829  14599  13187  -1855   -891    227       C  
ATOM   4912  OD1 ASP A 660     -75.752 -30.761 -85.698  1.00109.99           O  
ANISOU 4912  OD1 ASP A 660    13356  14860  13573  -1874   -939    292       O  
ATOM   4913  OD2 ASP A 660     -76.449 -29.500 -84.029  1.00112.73           O  
ANISOU 4913  OD2 ASP A 660    13533  15406  13892  -1896   -859    200       O  
ATOM   4914  N   LEU A 661     -78.053 -28.507 -89.621  1.00 92.83           N  
ANISOU 4914  N   LEU A 661    10853  12836  11582  -1561   -923    161       N  
ATOM   4915  CA  LEU A 661     -79.059 -28.060 -90.575  1.00 90.07           C  
ANISOU 4915  CA  LEU A 661    10405  12566  11252  -1511   -923    113       C  
ATOM   4916  C   LEU A 661     -79.378 -29.202 -91.514  1.00 88.09           C  
ANISOU 4916  C   LEU A 661    10221  12279  10969  -1581   -961    159       C  
ATOM   4917  O   LEU A 661     -78.480 -29.959 -91.880  1.00 86.24           O  
ANISOU 4917  O   LEU A 661    10117  11907  10743  -1585   -996    228       O  
ATOM   4918  CB  LEU A 661     -78.558 -26.868 -91.387  1.00 89.71           C  
ANISOU 4918  CB  LEU A 661    10330  12448  11305  -1330   -929     95       C  
ATOM   4919  CG  LEU A 661     -77.895 -25.712 -90.644  1.00 89.39           C  
ANISOU 4919  CG  LEU A 661    10260  12389  11314  -1238   -906     67       C  
ATOM   4920  CD1 LEU A 661     -77.428 -24.688 -91.663  1.00 89.00           C  
ANISOU 4920  CD1 LEU A 661    10206  12253  11354  -1078   -923     63       C  
ATOM   4921  CD2 LEU A 661     -78.820 -25.084 -89.607  1.00 89.91           C  
ANISOU 4921  CD2 LEU A 661    10202  12619  11341  -1265   -871    -15       C  
ATOM   4922  N   PRO A 662     -80.659 -29.338 -91.901  1.00 88.25           N  
ANISOU 4922  N   PRO A 662    10153  12427  10951  -1635   -957    115       N  
ATOM   4923  CA  PRO A 662     -81.051 -30.344 -92.882  1.00 88.76           C  
ANISOU 4923  CA  PRO A 662    10272  12462  10988  -1695   -995    152       C  
ATOM   4924  C   PRO A 662     -80.419 -30.016 -94.227  1.00 87.70           C  
ANISOU 4924  C   PRO A 662    10183  12199  10939  -1546  -1026    178       C  
ATOM   4925  O   PRO A 662     -80.140 -28.848 -94.497  1.00 87.63           O  
ANISOU 4925  O   PRO A 662    10118  12174  11002  -1404  -1013    146       O  
ATOM   4926  CB  PRO A 662     -82.573 -30.194 -92.958  1.00 89.61           C  
ANISOU 4926  CB  PRO A 662    10239  12758  11048  -1754   -976     79       C  
ATOM   4927  CG  PRO A 662     -82.964 -29.478 -91.711  1.00 89.88           C  
ANISOU 4927  CG  PRO A 662    10165  12929  11052  -1776   -928     14       C  
ATOM   4928  CD  PRO A 662     -81.817 -28.567 -91.420  1.00 88.97           C  
ANISOU 4928  CD  PRO A 662    10082  12705  11016  -1640   -920     23       C  
ATOM   4929  N   LEU A 663     -80.194 -31.036 -95.053  1.00 87.06           N  
ANISOU 4929  N   LEU A 663    10205  12026  10845  -1579  -1071    236       N  
ATOM   4930  CA  LEU A 663     -79.502 -30.868 -96.331  1.00 86.23           C  
ANISOU 4930  CA  LEU A 663    10155  11797  10811  -1448  -1102    267       C  
ATOM   4931  C   LEU A 663     -79.917 -29.619 -97.106  1.00 86.84           C  
ANISOU 4931  C   LEU A 663    10124  11914  10954  -1309  -1087    214       C  
ATOM   4932  O   LEU A 663     -79.060 -28.898 -97.619  1.00 87.98           O  
ANISOU 4932  O   LEU A 663    10293  11966  11169  -1181  -1091    228       O  
ATOM   4933  CB  LEU A 663     -79.695 -32.097 -97.214  1.00 87.73           C  
ANISOU 4933  CB  LEU A 663    10433  11934  10965  -1511  -1152    312       C  
ATOM   4934  CG  LEU A 663     -78.968 -33.390 -96.846  1.00 89.73           C  
ANISOU 4934  CG  LEU A 663    10841  12085  11168  -1605  -1194    379       C  
ATOM   4935  CD1 LEU A 663     -79.573 -34.547 -97.627  1.00 91.07           C  
ANISOU 4935  CD1 LEU A 663    11072  12241  11287  -1690  -1245    405       C  
ATOM   4936  CD2 LEU A 663     -77.468 -33.292 -97.106  1.00 88.85           C  
ANISOU 4936  CD2 LEU A 663    10824  11823  11110  -1490  -1214    421       C  
ATOM   4937  N   ALA A 664     -81.224 -29.367 -97.181  1.00 87.28           N  
ANISOU 4937  N   ALA A 664    10065  12112  10983  -1339  -1075    150       N  
ATOM   4938  CA  ALA A 664     -81.765 -28.263 -97.969  1.00 85.51           C  
ANISOU 4938  CA  ALA A 664     9744  11932  10813  -1208  -1074     92       C  
ATOM   4939  C   ALA A 664     -81.457 -26.912 -97.360  1.00 85.01           C  
ANISOU 4939  C   ALA A 664     9618  11883  10796  -1105  -1047     47       C  
ATOM   4940  O   ALA A 664     -81.181 -25.958 -98.072  1.00 84.56           O  
ANISOU 4940  O   ALA A 664     9552  11772  10805   -967  -1058     35       O  
ATOM   4941  CB  ALA A 664     -83.255 -28.428 -98.154  1.00 86.87           C  
ANISOU 4941  CB  ALA A 664     9808  12263  10935  -1269  -1074     29       C  
ATOM   4942  N   GLU A 665     -81.501 -26.831 -96.039  1.00 87.58           N  
ANISOU 4942  N   GLU A 665     9908  12280  11085  -1174  -1014     23       N  
ATOM   4943  CA  GLU A 665     -81.125 -25.602 -95.351  1.00 90.69           C  
ANISOU 4943  CA  GLU A 665    10255  12681  11521  -1081   -992    -17       C  
ATOM   4944  C   GLU A 665     -79.615 -25.373 -95.401  1.00 90.34           C  
ANISOU 4944  C   GLU A 665    10318  12470  11535  -1013   -997     48       C  
ATOM   4945  O   GLU A 665     -79.166 -24.230 -95.487  1.00 91.48           O  
ANISOU 4945  O   GLU A 665    10447  12571  11739   -894   -996     28       O  
ATOM   4946  CB  GLU A 665     -81.630 -25.611 -93.910  1.00 93.30           C  
ANISOU 4946  CB  GLU A 665    10513  13146  11790  -1176   -954    -64       C  
ATOM   4947  CG  GLU A 665     -83.146 -25.576 -93.810  1.00 96.77           C  
ANISOU 4947  CG  GLU A 665    10817  13779  12172  -1226   -944   -149       C  
ATOM   4948  CD  GLU A 665     -83.641 -25.624 -92.383  1.00 99.86           C  
ANISOU 4948  CD  GLU A 665    11132  14318  12492  -1330   -904   -197       C  
ATOM   4949  OE1 GLU A 665     -84.726 -26.199 -92.153  1.00103.40           O  
ANISOU 4949  OE1 GLU A 665    11504  14921  12861  -1448   -891   -235       O  
ATOM   4950  OE2 GLU A 665     -82.945 -25.092 -91.494  1.00101.04           O  
ANISOU 4950  OE2 GLU A 665    11296  14434  12659  -1299   -885   -197       O  
ATOM   4951  N   GLN A 666     -78.848 -26.465 -95.344  1.00 89.19           N  
ANISOU 4951  N   GLN A 666    10284  12235  11367  -1090  -1008    122       N  
ATOM   4952  CA  GLN A 666     -77.403 -26.440 -95.558  1.00 86.69           C  
ANISOU 4952  CA  GLN A 666    10072  11768  11098  -1029  -1019    184       C  
ATOM   4953  C   GLN A 666     -77.074 -25.838 -96.905  1.00 85.29           C  
ANISOU 4953  C   GLN A 666     9909  11512  10985   -903  -1041    197       C  
ATOM   4954  O   GLN A 666     -76.191 -24.993 -97.014  1.00 85.73           O  
ANISOU 4954  O   GLN A 666     9983  11492  11095   -810  -1037    207       O  
ATOM   4955  CB  GLN A 666     -76.837 -27.851 -95.539  1.00 86.89           C  
ANISOU 4955  CB  GLN A 666    10214  11720  11080  -1122  -1042    252       C  
ATOM   4956  CG  GLN A 666     -76.279 -28.307 -94.212  1.00 87.57           C  
ANISOU 4956  CG  GLN A 666    10349  11797  11125  -1207  -1029    270       C  
ATOM   4957  CD  GLN A 666     -75.507 -29.609 -94.340  1.00 88.92           C  
ANISOU 4957  CD  GLN A 666    10657  11864  11262  -1266  -1069    338       C  
ATOM   4958  OE1 GLN A 666     -75.487 -30.243 -95.401  1.00 87.42           O  
ANISOU 4958  OE1 GLN A 666    10522  11619  11073  -1253  -1105    368       O  
ATOM   4959  NE2 GLN A 666     -74.861 -30.015 -93.252  1.00 91.29           N  
ANISOU 4959  NE2 GLN A 666    11019  12135  11530  -1325  -1067    359       N  
ATOM   4960  N   ARG A 667     -77.788 -26.290 -97.928  1.00 84.91           N  
ANISOU 4960  N   ARG A 667     9853  11482  10925   -907  -1065    197       N  
ATOM   4961  CA  ARG A 667     -77.617 -25.782 -99.281  1.00 86.41           C  
ANISOU 4961  CA  ARG A 667    10055  11608  11166   -795  -1088    208       C  
ATOM   4962  C   ARG A 667     -77.993 -24.305 -99.384  1.00 87.99           C  
ANISOU 4962  C   ARG A 667    10174  11843  11412   -686  -1082    149       C  
ATOM   4963  O   ARG A 667     -77.280 -23.505-100.001  1.00 86.77           O  
ANISOU 4963  O   ARG A 667    10053  11604  11312   -586  -1092    168       O  
ATOM   4964  CB  ARG A 667     -78.465 -26.595-100.247  1.00 85.92           C  
ANISOU 4964  CB  ARG A 667     9993  11575  11075   -831  -1116    211       C  
ATOM   4965  CG  ARG A 667     -78.350 -26.118-101.670  1.00 85.38           C  
ANISOU 4965  CG  ARG A 667     9940  11446  11054   -719  -1142    222       C  
ATOM   4966  CD  ARG A 667     -79.270 -26.900-102.567  1.00 88.41           C  
ANISOU 4966  CD  ARG A 667    10315  11868  11406   -754  -1170    218       C  
ATOM   4967  NE  ARG A 667     -79.143 -26.424-103.936  1.00 91.09           N  
ANISOU 4967  NE  ARG A 667    10672  12147  11789   -644  -1195    229       N  
ATOM   4968  CZ  ARG A 667     -80.035 -25.659-104.552  1.00 91.97           C  
ANISOU 4968  CZ  ARG A 667    10713  12313  11918   -574  -1207    177       C  
ATOM   4969  NH1 ARG A 667     -81.145 -25.286-103.925  1.00 94.21           N  
ANISOU 4969  NH1 ARG A 667    10891  12723  12179   -596  -1196    103       N  
ATOM   4970  NH2 ARG A 667     -79.817 -25.278-105.802  1.00 91.98           N  
ANISOU 4970  NH2 ARG A 667    10747  12246  11953   -479  -1233    196       N  
ATOM   4971  N   GLU A 668     -79.125 -23.959 -98.779  1.00 90.75           N  
ANISOU 4971  N   GLU A 668    10422  12324  11735   -708  -1070     76       N  
ATOM   4972  CA  GLU A 668     -79.595 -22.584 -98.749  1.00 91.47           C  
ANISOU 4972  CA  GLU A 668    10434  12459  11860   -602  -1073      6       C  
ATOM   4973  C   GLU A 668     -78.574 -21.708 -98.041  1.00 90.59           C  
ANISOU 4973  C   GLU A 668    10352  12278  11788   -550  -1059     16       C  
ATOM   4974  O   GLU A 668     -78.210 -20.649 -98.548  1.00 90.72           O  
ANISOU 4974  O   GLU A 668    10383  12228  11856   -440  -1078     10       O  
ATOM   4975  CB  GLU A 668     -80.978 -22.497 -98.092  1.00 93.32           C  
ANISOU 4975  CB  GLU A 668    10545  12866  12045   -643  -1062    -82       C  
ATOM   4976  CG  GLU A 668     -82.108 -22.902 -99.034  1.00 94.90           C  
ANISOU 4976  CG  GLU A 668    10695  13140  12220   -649  -1086   -113       C  
ATOM   4977  CD  GLU A 668     -83.456 -23.081 -98.351  1.00 96.93           C  
ANISOU 4977  CD  GLU A 668    10827  13589  12413   -721  -1070   -198       C  
ATOM   4978  OE1 GLU A 668     -83.536 -23.009 -97.103  1.00 97.73           O  
ANISOU 4978  OE1 GLU A 668    10881  13771  12480   -780  -1038   -229       O  
ATOM   4979  OE2 GLU A 668     -84.446 -23.302 -99.079  1.00 97.62           O  
ANISOU 4979  OE2 GLU A 668    10857  13754  12479   -720  -1090   -236       O  
ATOM   4980  N   ALA A 669     -78.089 -22.179 -96.893  1.00 90.52           N  
ANISOU 4980  N   ALA A 669    10361  12279  11753   -633  -1030     34       N  
ATOM   4981  CA  ALA A 669     -77.064 -21.476 -96.125  1.00 89.99           C  
ANISOU 4981  CA  ALA A 669    10324  12147  11720   -598  -1015     45       C  
ATOM   4982  C   ALA A 669     -75.850 -21.114 -96.978  1.00 89.69           C  
ANISOU 4982  C   ALA A 669    10374  11965  11737   -524  -1032    107       C  
ATOM   4983  O   ALA A 669     -75.291 -20.029 -96.822  1.00 90.66           O  
ANISOU 4983  O   ALA A 669    10503  12038  11903   -449  -1034     98       O  
ATOM   4984  CB  ALA A 669     -76.643 -22.291 -94.911  1.00 88.35           C  
ANISOU 4984  CB  ALA A 669    10141  11957  11468   -708   -987     68       C  
ATOM   4985  N   CYS A 670     -75.466 -22.005 -97.891  1.00 88.92           N  
ANISOU 4985  N   CYS A 670    10344  11806  11635   -546  -1045    167       N  
ATOM   4986  CA  CYS A 670     -74.301 -21.775 -98.749  1.00 89.44           C  
ANISOU 4986  CA  CYS A 670    10488  11752  11742   -486  -1057    225       C  
ATOM   4987  C   CYS A 670     -74.496 -20.668 -99.776  1.00 92.27           C  
ANISOU 4987  C   CYS A 670    10836  12077  12143   -380  -1081    210       C  
ATOM   4988  O   CYS A 670     -73.520 -20.129-100.310  1.00 91.14           O  
ANISOU 4988  O   CYS A 670    10748  11845  12035   -328  -1088    249       O  
ATOM   4989  CB  CYS A 670     -73.877 -23.059 -99.442  1.00 87.36           C  
ANISOU 4989  CB  CYS A 670    10296  11441  11455   -532  -1070    283       C  
ATOM   4990  SG  CYS A 670     -72.906 -24.101 -98.347  1.00 87.54           S  
ANISOU 4990  SG  CYS A 670    10383  11434  11444   -621  -1056    322       S  
ATOM   4991  N   ARG A 671     -75.757 -20.336-100.042  1.00 96.55           N  
ANISOU 4991  N   ARG A 671    11309  12697  12677   -352  -1097    152       N  
ATOM   4992  CA  ARG A 671     -76.096 -19.305-101.014  1.00 97.76           C  
ANISOU 4992  CA  ARG A 671    11458  12823  12864   -248  -1131    130       C  
ATOM   4993  C   ARG A 671     -75.778 -17.907-100.485  1.00 96.06           C  
ANISOU 4993  C   ARG A 671    11236  12577  12683   -176  -1138     99       C  
ATOM   4994  O   ARG A 671     -75.470 -17.010-101.261  1.00 98.98           O  
ANISOU 4994  O   ARG A 671    11647  12872  13086    -97  -1167    112       O  
ATOM   4995  CB  ARG A 671     -77.572 -19.398-101.409  1.00 99.17           C  
ANISOU 4995  CB  ARG A 671    11560  13100  13017   -233  -1151     68       C  
ATOM   4996  CG  ARG A 671     -77.891 -18.798-102.765  1.00102.13           C  
ANISOU 4996  CG  ARG A 671    11955  13432  13417   -139  -1194     65       C  
ATOM   4997  CD  ARG A 671     -79.178 -17.996-102.707  1.00106.28           C  
ANISOU 4997  CD  ARG A 671    12395  14049  13937    -69  -1223    -29       C  
ATOM   4998  NE  ARG A 671     -79.859 -17.952-103.999  1.00109.55           N  
ANISOU 4998  NE  ARG A 671    12811  14460  14353     -9  -1263    -40       N  
ATOM   4999  CZ  ARG A 671     -80.948 -18.658-104.302  1.00111.50           C  
ANISOU 4999  CZ  ARG A 671    12993  14805  14564    -40  -1269    -78       C  
ATOM   5000  NH1 ARG A 671     -81.499 -19.472-103.404  1.00113.50           N  
ANISOU 5000  NH1 ARG A 671    13177  15171  14775   -139  -1237   -107       N  
ATOM   5001  NH2 ARG A 671     -81.495 -18.545-105.504  1.00111.19           N  
ANISOU 5001  NH2 ARG A 671    12961  14755  14530     22  -1309    -88       N  
ATOM   5002  N   ARG A 672     -75.831 -17.731 -99.172  1.00 93.33           N  
ANISOU 5002  N   ARG A 672    10847  12286  12328   -207  -1115     61       N  
ATOM   5003  CA  ARG A 672     -75.715 -16.402 -98.589  1.00 95.37           C  
ANISOU 5003  CA  ARG A 672    11091  12527  12614   -136  -1129     18       C  
ATOM   5004  C   ARG A 672     -74.520 -16.216 -97.652  1.00 96.75           C  
ANISOU 5004  C   ARG A 672    11306  12646  12805   -167  -1102     51       C  
ATOM   5005  O   ARG A 672     -74.126 -15.078 -97.359  1.00 96.96           O  
ANISOU 5005  O   ARG A 672    11350  12625  12863   -108  -1119     35       O  
ATOM   5006  CB  ARG A 672     -77.008 -16.051 -97.855  1.00 98.48           C  
ANISOU 5006  CB  ARG A 672    11382  13052  12982   -116  -1135    -81       C  
ATOM   5007  CG  ARG A 672     -77.421 -17.080 -96.818  1.00 98.76           C  
ANISOU 5007  CG  ARG A 672    11357  13198  12966   -225  -1092    -98       C  
ATOM   5008  CD  ARG A 672     -78.850 -16.871 -96.363  1.00100.24           C  
ANISOU 5008  CD  ARG A 672    11429  13539  13116   -212  -1098   -200       C  
ATOM   5009  NE  ARG A 672     -79.515 -18.157 -96.184  1.00102.97           N  
ANISOU 5009  NE  ARG A 672    11730  13987  13404   -327  -1070   -198       N  
ATOM   5010  CZ  ARG A 672     -79.475 -18.879 -95.068  1.00104.42           C  
ANISOU 5010  CZ  ARG A 672    11892  14237  13543   -436  -1030   -195       C  
ATOM   5011  NH1 ARG A 672     -78.804 -18.436 -94.012  1.00103.45           N  
ANISOU 5011  NH1 ARG A 672    11780  14093  13430   -438  -1011   -197       N  
ATOM   5012  NH2 ARG A 672     -80.111 -20.046 -95.007  1.00105.27           N  
ANISOU 5012  NH2 ARG A 672    11973  14431  13594   -549  -1012   -188       N  
ATOM   5013  N   ALA A 673     -73.957 -17.333 -97.188  1.00 96.23           N  
ANISOU 5013  N   ALA A 673    11262  12585  12717   -259  -1067     96       N  
ATOM   5014  CA  ALA A 673     -72.901 -17.329 -96.171  1.00 93.41           C  
ANISOU 5014  CA  ALA A 673    10933  12190  12365   -297  -1040    121       C  
ATOM   5015  C   ALA A 673     -71.570 -16.787 -96.673  1.00 92.37           C  
ANISOU 5015  C   ALA A 673    10879  11942  12275   -262  -1047    178       C  
ATOM   5016  O   ALA A 673     -71.087 -17.169 -97.739  1.00 91.84           O  
ANISOU 5016  O   ALA A 673    10862  11820  12213   -258  -1054    231       O  
ATOM   5017  CB  ALA A 673     -72.712 -18.720 -95.592  1.00 92.37           C  
ANISOU 5017  CB  ALA A 673    10813  12092  12191   -400  -1011    150       C  
ATOM   5018  N   CYS A 674     -70.984 -15.895 -95.885  1.00 91.79           N  
ANISOU 5018  N   CYS A 674    10811  11839  12225   -240  -1044    164       N  
ATOM   5019  CA  CYS A 674     -69.692 -15.306 -96.202  1.00 90.98           C  
ANISOU 5019  CA  CYS A 674    10774  11637  12156   -221  -1048    213       C  
ATOM   5020  C   CYS A 674     -68.630 -15.742 -95.204  1.00 90.39           C  
ANISOU 5020  C   CYS A 674    10718  11550  12076   -277  -1016    238       C  
ATOM   5021  O   CYS A 674     -67.451 -15.435 -95.382  1.00 91.61           O  
ANISOU 5021  O   CYS A 674    10919  11635  12251   -275  -1013    279       O  
ATOM   5022  CB  CYS A 674     -69.791 -13.782 -96.192  1.00 91.32           C  
ANISOU 5022  CB  CYS A 674    10823  11641  12232   -146  -1081    180       C  
ATOM   5023  SG  CYS A 674     -70.905 -13.097 -97.430  1.00 93.97           S  
ANISOU 5023  SG  CYS A 674    11156  11971  12574    -62  -1133    151       S  
ATOM   5024  N   CYS A 675     -69.046 -16.459 -94.160  1.00 88.99           N  
ANISOU 5024  N   CYS A 675    10502  11442  11867   -330   -994    211       N  
ATOM   5025  CA  CYS A 675     -68.154 -16.778 -93.050  1.00 88.57           C  
ANISOU 5025  CA  CYS A 675    10464  11380  11806   -376   -969    222       C  
ATOM   5026  C   CYS A 675     -68.438 -18.137 -92.423  1.00 87.12           C  
ANISOU 5026  C   CYS A 675    10274  11253  11571   -457   -950    226       C  
ATOM   5027  O   CYS A 675     -69.529 -18.365 -91.898  1.00 88.80           O  
ANISOU 5027  O   CYS A 675    10434  11550  11753   -485   -944    183       O  
ATOM   5028  CB  CYS A 675     -68.253 -15.685 -91.985  1.00 90.51           C  
ANISOU 5028  CB  CYS A 675    10675  11642  12070   -348   -969    171       C  
ATOM   5029  SG  CYS A 675     -67.333 -16.042 -90.477  1.00 94.98           S  
ANISOU 5029  SG  CYS A 675    11252  12212  12623   -404   -940    174       S  
ATOM   5030  N   PHE A 676     -67.447 -19.027 -92.468  1.00 83.70           N  
ANISOU 5030  N   PHE A 676     9898  10776  11126   -494   -945    275       N  
ATOM   5031  CA  PHE A 676     -67.546 -20.351 -91.846  1.00 81.71           C  
ANISOU 5031  CA  PHE A 676     9667  10556  10822   -572   -938    286       C  
ATOM   5032  C   PHE A 676     -66.450 -20.578 -90.803  1.00 82.62           C  
ANISOU 5032  C   PHE A 676     9818  10642  10930   -599   -928    298       C  
ATOM   5033  O   PHE A 676     -65.281 -20.737 -91.142  1.00 83.69           O  
ANISOU 5033  O   PHE A 676    10002  10715  11079   -579   -934    333       O  
ATOM   5034  CB  PHE A 676     -67.480 -21.452 -92.904  1.00 79.36           C  
ANISOU 5034  CB  PHE A 676     9417  10232  10501   -589   -957    329       C  
ATOM   5035  CG  PHE A 676     -68.743 -21.620 -93.696  1.00 78.51           C  
ANISOU 5035  CG  PHE A 676     9276  10172  10382   -591   -967    314       C  
ATOM   5036  CD1 PHE A 676     -69.846 -22.255 -93.144  1.00 78.00           C  
ANISOU 5036  CD1 PHE A 676     9177  10187  10269   -660   -962    287       C  
ATOM   5037  CD2 PHE A 676     -68.820 -21.167 -95.009  1.00 77.98           C  
ANISOU 5037  CD2 PHE A 676     9210  10073  10345   -528   -982    327       C  
ATOM   5038  CE1 PHE A 676     -71.007 -22.415 -93.881  1.00 77.85           C  
ANISOU 5038  CE1 PHE A 676     9120  10221  10237   -663   -972    269       C  
ATOM   5039  CE2 PHE A 676     -69.979 -21.327 -95.753  1.00 76.90           C  
ANISOU 5039  CE2 PHE A 676     9041   9980  10197   -524   -995    310       C  
ATOM   5040  CZ  PHE A 676     -71.074 -21.953 -95.186  1.00 77.15           C  
ANISOU 5040  CZ  PHE A 676     9033  10096  10184   -590   -990    279       C  
ATOM   5041  N   ALA A 677     -66.829 -20.602 -89.532  1.00 84.12           N  
ANISOU 5041  N   ALA A 677     9981  10885  11095   -643   -912    265       N  
ATOM   5042  CA  ALA A 677     -65.864 -20.794 -88.450  1.00 84.44           C  
ANISOU 5042  CA  ALA A 677    10056  10901  11126   -667   -905    271       C  
ATOM   5043  C   ALA A 677     -65.842 -22.233 -87.949  1.00 85.08           C  
ANISOU 5043  C   ALA A 677    10191  10990  11144   -748   -913    293       C  
ATOM   5044  O   ALA A 677     -66.882 -22.871 -87.820  1.00 85.20           O  
ANISOU 5044  O   ALA A 677    10194  11064  11114   -810   -913    284       O  
ATOM   5045  CB  ALA A 677     -66.167 -19.844 -87.304  1.00 85.19           C  
ANISOU 5045  CB  ALA A 677    10095  11041  11231   -660   -886    222       C  
ATOM   5046  N   ARG A 678     -64.643 -22.730 -87.664  1.00 87.31           N  
ANISOU 5046  N   ARG A 678    10538  11214  11420   -748   -926    320       N  
ATOM   5047  CA  ARG A 678     -64.440 -24.067 -87.087  1.00 89.61           C  
ANISOU 5047  CA  ARG A 678    10903  11495  11650   -816   -946    340       C  
ATOM   5048  C   ARG A 678     -65.129 -25.176 -87.879  1.00 90.81           C  
ANISOU 5048  C   ARG A 678    11093  11649  11760   -859   -972    365       C  
ATOM   5049  O   ARG A 678     -66.096 -25.782 -87.407  1.00 91.95           O  
ANISOU 5049  O   ARG A 678    11239  11847  11852   -942   -971    359       O  
ATOM   5050  CB  ARG A 678     -64.881 -24.111 -85.616  1.00 88.78           C  
ANISOU 5050  CB  ARG A 678    10784  11444  11505   -883   -929    314       C  
ATOM   5051  CG  ARG A 678     -64.293 -22.998 -84.781  1.00 88.60           C  
ANISOU 5051  CG  ARG A 678    10720  11420  11522   -840   -906    284       C  
ATOM   5052  CD  ARG A 678     -63.995 -23.445 -83.372  1.00 89.23           C  
ANISOU 5052  CD  ARG A 678    10835  11511  11557   -897   -905    277       C  
ATOM   5053  NE  ARG A 678     -63.215 -22.416 -82.703  1.00 91.88           N  
ANISOU 5053  NE  ARG A 678    11142  11831  11936   -845   -890    253       N  
ATOM   5054  CZ  ARG A 678     -62.828 -22.468 -81.435  1.00 95.00           C  
ANISOU 5054  CZ  ARG A 678    11554  12233  12307   -873   -885    238       C  
ATOM   5055  NH1 ARG A 678     -63.147 -23.512 -80.679  1.00 97.61           N  
ANISOU 5055  NH1 ARG A 678    11936  12585  12565   -957   -895    248       N  
ATOM   5056  NH2 ARG A 678     -62.122 -21.469 -80.920  1.00 95.63           N  
ANISOU 5056  NH2 ARG A 678    11605  12298  12432   -821   -873    216       N  
ATOM   5057  N   VAL A 679     -64.619 -25.440 -89.077  1.00 89.89           N  
ANISOU 5057  N   VAL A 679    11009  11481  11663   -808   -994    392       N  
ATOM   5058  CA  VAL A 679     -65.219 -26.437 -89.945  1.00 91.40           C  
ANISOU 5058  CA  VAL A 679    11238  11668  11819   -839  -1023    414       C  
ATOM   5059  C   VAL A 679     -64.372 -27.703 -90.020  1.00 97.09           C  
ANISOU 5059  C   VAL A 679    12066  12323  12498   -848  -1071    444       C  
ATOM   5060  O   VAL A 679     -63.155 -27.643 -89.889  1.00101.57           O  
ANISOU 5060  O   VAL A 679    12664  12845  13080   -796  -1082    447       O  
ATOM   5061  CB  VAL A 679     -65.477 -25.867 -91.351  1.00 88.57           C  
ANISOU 5061  CB  VAL A 679    10839  11307  11506   -774  -1019    419       C  
ATOM   5062  CG1 VAL A 679     -66.191 -24.534 -91.247  1.00 89.41           C  
ANISOU 5062  CG1 VAL A 679    10851  11466  11655   -747   -983    385       C  
ATOM   5063  CG2 VAL A 679     -64.185 -25.701 -92.124  1.00 87.45           C  
ANISOU 5063  CG2 VAL A 679    10726  11103  11396   -695  -1031    439       C  
ATOM   5064  N   GLU A 680     -65.025 -28.846 -90.212  1.00103.76           N  
ANISOU 5064  N   GLU A 680    12970  13165  13286   -914  -1105    461       N  
ATOM   5065  CA  GLU A 680     -64.339 -30.101 -90.507  1.00112.51           C  
ANISOU 5065  CA  GLU A 680    14191  14203  14351   -912  -1166    487       C  
ATOM   5066  C   GLU A 680     -63.561 -29.988 -91.818  1.00116.29           C  
ANISOU 5066  C   GLU A 680    14671  14643  14868   -811  -1182    496       C  
ATOM   5067  O   GLU A 680     -63.809 -29.061 -92.600  1.00118.87           O  
ANISOU 5067  O   GLU A 680    14920  14997  15247   -764  -1148    490       O  
ATOM   5068  CB  GLU A 680     -65.354 -31.244 -90.601  1.00119.92           C  
ANISOU 5068  CB  GLU A 680    15190  15148  15224  -1008  -1202    505       C  
ATOM   5069  CG  GLU A 680     -65.226 -32.299 -89.511  1.00128.70           C  
ANISOU 5069  CG  GLU A 680    16409  16229  16261  -1094  -1244    518       C  
ATOM   5070  CD  GLU A 680     -65.177 -31.706 -88.115  1.00133.43           C  
ANISOU 5070  CD  GLU A 680    16971  16869  16857  -1133  -1204    498       C  
ATOM   5071  OE1 GLU A 680     -66.216 -31.183 -87.654  1.00138.16           O  
ANISOU 5071  OE1 GLU A 680    17490  17552  17452  -1197  -1158    481       O  
ATOM   5072  OE2 GLU A 680     -64.099 -31.773 -87.481  1.00132.84           O  
ANISOU 5072  OE2 GLU A 680    16946  16747  16781  -1096  -1222    495       O  
ATOM   5073  N   PRO A 681     -62.612 -30.921 -92.069  1.00117.89           N  
ANISOU 5073  N   PRO A 681    14965  14784  15041   -775  -1238    506       N  
ATOM   5074  CA  PRO A 681     -61.950 -30.934 -93.386  1.00115.03           C  
ANISOU 5074  CA  PRO A 681    14603  14399  14703   -684  -1255    511       C  
ATOM   5075  C   PRO A 681     -62.946 -31.276 -94.498  1.00111.32           C  
ANISOU 5075  C   PRO A 681    14130  13939  14227   -699  -1266    527       C  
ATOM   5076  O   PRO A 681     -62.833 -30.768 -95.617  1.00109.53           O  
ANISOU 5076  O   PRO A 681    13857  13721  14037   -635  -1251    530       O  
ATOM   5077  CB  PRO A 681     -60.902 -32.044 -93.244  1.00115.12           C  
ANISOU 5077  CB  PRO A 681    14721  14352  14667   -650  -1324    509       C  
ATOM   5078  CG  PRO A 681     -61.415 -32.915 -92.140  1.00118.44           C  
ANISOU 5078  CG  PRO A 681    15224  14750  15026   -744  -1358    516       C  
ATOM   5079  CD  PRO A 681     -62.089 -31.978 -91.182  1.00116.73           C  
ANISOU 5079  CD  PRO A 681    14927  14589  14833   -808  -1292    509       C  
ATOM   5080  N   SER A 682     -63.929 -32.108 -94.157  1.00107.43           N  
ANISOU 5080  N   SER A 682    13686  13447  13685   -789  -1292    537       N  
ATOM   5081  CA  SER A 682     -64.969 -32.544 -95.077  1.00105.30           C  
ANISOU 5081  CA  SER A 682    13417  13189  13400   -820  -1307    550       C  
ATOM   5082  C   SER A 682     -66.021 -31.467 -95.366  1.00103.72           C  
ANISOU 5082  C   SER A 682    13101  13061  13244   -832  -1247    538       C  
ATOM   5083  O   SER A 682     -66.929 -31.682 -96.177  1.00107.85           O  
ANISOU 5083  O   SER A 682    13609  13605  13763   -851  -1254    544       O  
ATOM   5084  CB  SER A 682     -65.649 -33.795 -94.522  1.00106.77           C  
ANISOU 5084  CB  SER A 682    13698  13356  13511   -929  -1357    565       C  
ATOM   5085  OG  SER A 682     -66.093 -33.574 -93.194  1.00109.11           O  
ANISOU 5085  OG  SER A 682    13976  13693  13788  -1017  -1327    558       O  
ATOM   5086  N   HIS A 683     -65.910 -30.315 -94.710  1.00 97.33           N  
ANISOU 5086  N   HIS A 683    12212  12289  12477   -817  -1193    519       N  
ATOM   5087  CA  HIS A 683     -66.871 -29.245 -94.945  1.00 93.08           C  
ANISOU 5087  CA  HIS A 683    11571  11816  11979   -814  -1146    499       C  
ATOM   5088  C   HIS A 683     -66.585 -28.425 -96.201  1.00 88.85           C  
ANISOU 5088  C   HIS A 683    10991  11269  11498   -719  -1134    502       C  
ATOM   5089  O   HIS A 683     -67.508 -27.865 -96.784  1.00 87.39           O  
ANISOU 5089  O   HIS A 683    10745  11124  11335   -710  -1117    490       O  
ATOM   5090  CB  HIS A 683     -67.022 -28.343 -93.719  1.00 96.73           C  
ANISOU 5090  CB  HIS A 683    11969  12324  12456   -838  -1101    471       C  
ATOM   5091  CG  HIS A 683     -67.917 -28.909 -92.657  1.00101.36           C  
ANISOU 5091  CG  HIS A 683    12561  12962  12986   -949  -1099    461       C  
ATOM   5092  ND1 HIS A 683     -67.668 -28.751 -91.309  1.00102.63           N  
ANISOU 5092  ND1 HIS A 683    12722  13140  13130   -991  -1081    447       N  
ATOM   5093  CD2 HIS A 683     -69.057 -29.637 -92.743  1.00103.85           C  
ANISOU 5093  CD2 HIS A 683    12882  13322  13252  -1036  -1113    462       C  
ATOM   5094  CE1 HIS A 683     -68.616 -29.352 -90.612  1.00102.96           C  
ANISOU 5094  CE1 HIS A 683    12770  13237  13112  -1100  -1082    442       C  
ATOM   5095  NE2 HIS A 683     -69.470 -29.898 -91.459  1.00104.67           N  
ANISOU 5095  NE2 HIS A 683    12989  13474  13307  -1133  -1100    451       N  
ATOM   5096  N   LYS A 684     -65.320 -28.362 -96.619  1.00 86.29           N  
ANISOU 5096  N   LYS A 684    10698  10897  11192   -650  -1144    515       N  
ATOM   5097  CA  LYS A 684     -64.940 -27.618 -97.833  1.00 84.32           C  
ANISOU 5097  CA  LYS A 684    10415  10638  10985   -569  -1133    522       C  
ATOM   5098  C   LYS A 684     -65.500 -28.240 -99.106  1.00 83.82           C  
ANISOU 5098  C   LYS A 684    10373  10568  10906   -555  -1162    537       C  
ATOM   5099  O   LYS A 684     -65.973 -27.527 -99.987  1.00 83.59           O  
ANISOU 5099  O   LYS A 684    10297  10555  10908   -520  -1147    537       O  
ATOM   5100  CB  LYS A 684     -63.421 -27.456 -97.955  1.00 83.84           C  
ANISOU 5100  CB  LYS A 684    10375  10544  10935   -509  -1135    529       C  
ATOM   5101  CG  LYS A 684     -62.851 -26.227 -97.262  1.00 82.67           C  
ANISOU 5101  CG  LYS A 684    10176  10406  10829   -493  -1093    516       C  
ATOM   5102  CD  LYS A 684     -61.363 -26.086 -97.544  1.00 81.60           C  
ANISOU 5102  CD  LYS A 684    10053  10251  10699   -439  -1095    522       C  
ATOM   5103  CE  LYS A 684     -60.722 -25.003 -96.688  1.00 80.30           C  
ANISOU 5103  CE  LYS A 684     9848  10093  10568   -436  -1060    508       C  
ATOM   5104  NZ  LYS A 684     -59.238 -25.153 -96.611  1.00 79.70           N  
ANISOU 5104  NZ  LYS A 684     9789  10009  10483   -401  -1067    505       N  
ATOM   5105  N   SER A 685     -65.444 -29.566 -99.204  1.00 84.51           N  
ANISOU 5105  N   SER A 685    10537  10627  10943   -582  -1210    549       N  
ATOM   5106  CA  SER A 685     -66.051 -30.265-100.331  1.00 85.60           C  
ANISOU 5106  CA  SER A 685    10703  10758  11062   -577  -1244    561       C  
ATOM   5107  C   SER A 685     -67.560 -30.080-100.366  1.00 86.51           C  
ANISOU 5107  C   SER A 685    10768  10923  11178   -634  -1230    551       C  
ATOM   5108  O   SER A 685     -68.126 -29.845-101.436  1.00 86.73           O  
ANISOU 5108  O   SER A 685    10767  10964  11222   -603  -1231    553       O  
ATOM   5109  CB  SER A 685     -65.699 -31.743-100.321  1.00 87.71           C  
ANISOU 5109  CB  SER A 685    11076  10978  11272   -597  -1308    573       C  
ATOM   5110  OG  SER A 685     -64.601 -31.981-101.180  1.00 90.62           O  
ANISOU 5110  OG  SER A 685    11477  11314  11639   -510  -1334    578       O  
ATOM   5111  N   LYS A 686     -68.204 -30.183 -99.201  1.00 86.87           N  
ANISOU 5111  N   LYS A 686    10801  11004  11201   -718  -1217    537       N  
ATOM   5112  CA  LYS A 686     -69.637 -29.892 -99.082  1.00 86.82           C  
ANISOU 5112  CA  LYS A 686    10726  11068  11191   -774  -1197    515       C  
ATOM   5113  C   LYS A 686     -69.977 -28.479 -99.559  1.00 84.16           C  
ANISOU 5113  C   LYS A 686    10295  10767  10912   -706  -1158    493       C  
ATOM   5114  O   LYS A 686     -70.877 -28.300-100.375  1.00 84.76           O  
ANISOU 5114  O   LYS A 686    10332  10876  10996   -693  -1162    482       O  
ATOM   5115  CB  LYS A 686     -70.126 -30.086 -97.648  1.00 88.91           C  
ANISOU 5115  CB  LYS A 686    10981  11379  11419   -873  -1181    499       C  
ATOM   5116  CG  LYS A 686     -70.549 -31.501 -97.312  1.00 93.27           C  
ANISOU 5116  CG  LYS A 686    11616  11923  11900   -978  -1224    517       C  
ATOM   5117  CD  LYS A 686     -71.191 -31.537 -95.936  1.00 98.54           C  
ANISOU 5117  CD  LYS A 686    12257  12656  12527  -1086  -1200    499       C  
ATOM   5118  CE  LYS A 686     -71.056 -32.905 -95.287  1.00101.77           C  
ANISOU 5118  CE  LYS A 686    12783  13024  12860  -1188  -1248    527       C  
ATOM   5119  NZ  LYS A 686     -71.326 -32.813 -93.826  1.00103.68           N  
ANISOU 5119  NZ  LYS A 686    13008  13320  13065  -1280  -1220    513       N  
ATOM   5120  N   ILE A 687     -69.248 -27.486 -99.057  1.00 81.06           N  
ANISOU 5120  N   ILE A 687     9874  10366  10559   -661  -1127    485       N  
ATOM   5121  CA  ILE A 687     -69.492 -26.104 -99.434  1.00 79.53           C  
ANISOU 5121  CA  ILE A 687     9608  10193  10417   -597  -1101    464       C  
ATOM   5122  C   ILE A 687     -69.367 -25.952-100.949  1.00 80.66           C  
ANISOU 5122  C   ILE A 687     9762  10302  10579   -528  -1118    484       C  
ATOM   5123  O   ILE A 687     -70.280 -25.416-101.586  1.00 82.49           O  
ANISOU 5123  O   ILE A 687     9949  10565  10828   -502  -1118    467       O  
ATOM   5124  CB  ILE A 687     -68.610 -25.116 -98.632  1.00 78.64           C  
ANISOU 5124  CB  ILE A 687     9478  10063  10338   -567  -1072    456       C  
ATOM   5125  CG1 ILE A 687     -69.135 -25.028 -97.198  1.00 79.83           C  
ANISOU 5125  CG1 ILE A 687     9593  10268  10471   -630  -1052    424       C  
ATOM   5126  CG2 ILE A 687     -68.624 -23.720 -99.241  1.00 76.90           C  
ANISOU 5126  CG2 ILE A 687     9212   9836  10169   -492  -1059    446       C  
ATOM   5127  CD1 ILE A 687     -68.152 -24.483 -96.185  1.00 80.27           C  
ANISOU 5127  CD1 ILE A 687     9652  10301  10545   -621  -1031    421       C  
ATOM   5128  N   VAL A 688     -68.279 -26.462-101.531  1.00 80.59           N  
ANISOU 5128  N   VAL A 688     9815  10240  10565   -496  -1135    517       N  
ATOM   5129  CA  VAL A 688     -68.096 -26.395-102.993  1.00 81.23           C  
ANISOU 5129  CA  VAL A 688     9910  10296  10657   -434  -1151    538       C  
ATOM   5130  C   VAL A 688     -69.322 -26.970-103.709  1.00 83.75           C  
ANISOU 5130  C   VAL A 688    10223  10640  10956   -453  -1176    532       C  
ATOM   5131  O   VAL A 688     -69.947 -26.300-104.536  1.00 82.73           O  
ANISOU 5131  O   VAL A 688    10057  10526  10850   -412  -1174    524       O  
ATOM   5132  CB  VAL A 688     -66.780 -27.065-103.471  1.00 78.78           C  
ANISOU 5132  CB  VAL A 688     9663   9940  10328   -401  -1170    566       C  
ATOM   5133  CG1 VAL A 688     -66.869 -27.496-104.926  1.00 78.66           C  
ANISOU 5133  CG1 VAL A 688     9672   9911  10302   -358  -1198    583       C  
ATOM   5134  CG2 VAL A 688     -65.610 -26.114-103.306  1.00 77.24           C  
ANISOU 5134  CG2 VAL A 688     9453   9731  10163   -360  -1142    571       C  
ATOM   5135  N   GLU A 689     -69.674 -28.199-103.342  1.00 87.58           N  
ANISOU 5135  N   GLU A 689    10749  11130  11396   -519  -1202    534       N  
ATOM   5136  CA  GLU A 689     -70.800 -28.902-103.929  1.00 91.20           C  
ANISOU 5136  CA  GLU A 689    11209  11615  11828   -555  -1229    529       C  
ATOM   5137  C   GLU A 689     -72.070 -28.059-103.926  1.00 88.47           C  
ANISOU 5137  C   GLU A 689    10775  11337  11501   -559  -1208    493       C  
ATOM   5138  O   GLU A 689     -72.679 -27.879-104.980  1.00 90.14           O  
ANISOU 5138  O   GLU A 689    10966  11559  11723   -521  -1221    488       O  
ATOM   5139  CB  GLU A 689     -71.032 -30.226-103.206  1.00 98.95           C  
ANISOU 5139  CB  GLU A 689    12248  12594  12752   -649  -1258    536       C  
ATOM   5140  CG  GLU A 689     -71.651 -31.297-104.086  1.00111.44           C  
ANISOU 5140  CG  GLU A 689    13877  14167  14298   -675  -1305    547       C  
ATOM   5141  CD  GLU A 689     -71.218 -32.698-103.692  1.00121.56           C  
ANISOU 5141  CD  GLU A 689    15264  15397  15523   -733  -1354    569       C  
ATOM   5142  OE1 GLU A 689     -70.367 -32.828-102.778  1.00124.24           O  
ANISOU 5142  OE1 GLU A 689    15642  15709  15854   -744  -1352    575       O  
ATOM   5143  OE2 GLU A 689     -71.725 -33.670-104.304  1.00128.31           O  
ANISOU 5143  OE2 GLU A 689    16170  16238  16342   -766  -1401    580       O  
ATOM   5144  N   TYR A 690     -72.461 -27.541-102.759  1.00 85.09           N  
ANISOU 5144  N   TYR A 690    10293  10958  11075   -600  -1178    462       N  
ATOM   5145  CA  TYR A 690     -73.676 -26.728-102.657  1.00 83.76           C  
ANISOU 5145  CA  TYR A 690    10034  10868  10920   -596  -1162    414       C  
ATOM   5146  C   TYR A 690     -73.576 -25.493-103.535  1.00 84.03           C  
ANISOU 5146  C   TYR A 690    10040  10881  11006   -491  -1159    407       C  
ATOM   5147  O   TYR A 690     -74.498 -25.196-104.291  1.00 84.03           O  
ANISOU 5147  O   TYR A 690    10000  10914  11011   -460  -1173    383       O  
ATOM   5148  CB  TYR A 690     -73.979 -26.316-101.219  1.00 82.72           C  
ANISOU 5148  CB  TYR A 690     9850  10797  10780   -647  -1131    378       C  
ATOM   5149  CG  TYR A 690     -74.516 -27.414-100.328  1.00 83.88           C  
ANISOU 5149  CG  TYR A 690    10008  10995  10867   -768  -1134    375       C  
ATOM   5150  CD1 TYR A 690     -75.422 -28.365-100.802  1.00 84.84           C  
ANISOU 5150  CD1 TYR A 690    10137  11153  10945   -833  -1159    375       C  
ATOM   5151  CD2 TYR A 690     -74.138 -27.481 -98.988  1.00 84.80           C  
ANISOU 5151  CD2 TYR A 690    10131  11124  10964   -824  -1112    371       C  
ATOM   5152  CE1 TYR A 690     -75.913 -29.360 -99.966  1.00 84.95           C  
ANISOU 5152  CE1 TYR A 690    10169  11212  10895   -959  -1164    376       C  
ATOM   5153  CE2 TYR A 690     -74.623 -28.467 -98.149  1.00 84.21           C  
ANISOU 5153  CE2 TYR A 690    10075  11094  10826   -946  -1116    371       C  
ATOM   5154  CZ  TYR A 690     -75.507 -29.398 -98.638  1.00 84.64           C  
ANISOU 5154  CZ  TYR A 690    10140  11182  10834  -1017  -1142    375       C  
ATOM   5155  OH  TYR A 690     -75.975 -30.363 -97.785  1.00 86.31           O  
ANISOU 5155  OH  TYR A 690    10379  11437  10976  -1151  -1148    380       O  
ATOM   5156  N   LEU A 691     -72.448 -24.791-103.447  1.00 83.57           N  
ANISOU 5156  N   LEU A 691    10006  10766  10980   -441  -1145    428       N  
ATOM   5157  CA  LEU A 691     -72.182 -23.648-104.315  1.00 83.64           C  
ANISOU 5157  CA  LEU A 691    10009  10739  11029   -353  -1147    432       C  
ATOM   5158  C   LEU A 691     -72.394 -23.991-105.790  1.00 84.92           C  
ANISOU 5158  C   LEU A 691    10199  10879  11187   -314  -1175    454       C  
ATOM   5159  O   LEU A 691     -72.958 -23.202-106.551  1.00 85.85           O  
ANISOU 5159  O   LEU A 691    10292  11000  11325   -256  -1188    439       O  
ATOM   5160  CB  LEU A 691     -70.763 -23.136-104.091  1.00 81.77           C  
ANISOU 5160  CB  LEU A 691     9810  10443  10816   -328  -1130    463       C  
ATOM   5161  CG  LEU A 691     -70.600 -22.302-102.825  1.00 82.38           C  
ANISOU 5161  CG  LEU A 691     9853  10535  10913   -337  -1106    436       C  
ATOM   5162  CD1 LEU A 691     -69.130 -22.111-102.489  1.00 82.48           C  
ANISOU 5162  CD1 LEU A 691     9905  10494  10936   -333  -1089    468       C  
ATOM   5163  CD2 LEU A 691     -71.302 -20.962-102.977  1.00 82.88           C  
ANISOU 5163  CD2 LEU A 691     9870  10611  11006   -280  -1111    399       C  
ATOM   5164  N   GLN A 692     -71.959 -25.185-106.176  1.00 85.81           N  
ANISOU 5164  N   GLN A 692    10366  10968  11270   -342  -1191    487       N  
ATOM   5165  CA  GLN A 692     -72.074 -25.648-107.553  1.00 85.57           C  
ANISOU 5165  CA  GLN A 692    10367  10915  11230   -307  -1219    509       C  
ATOM   5166  C   GLN A 692     -73.497 -25.878-108.012  1.00 86.04           C  
ANISOU 5166  C   GLN A 692    10387  11025  11277   -318  -1240    478       C  
ATOM   5167  O   GLN A 692     -73.797 -25.659-109.184  1.00 88.79           O  
ANISOU 5167  O   GLN A 692    10739  11362  11633   -264  -1260    483       O  
ATOM   5168  CB  GLN A 692     -71.260 -26.911-107.763  1.00 84.69           C  
ANISOU 5168  CB  GLN A 692    10325  10767  11084   -329  -1239    543       C  
ATOM   5169  CG  GLN A 692     -69.794 -26.624-107.971  1.00 83.38           C  
ANISOU 5169  CG  GLN A 692    10196  10555  10929   -285  -1227    573       C  
ATOM   5170  CD  GLN A 692     -68.997 -27.887-108.072  1.00 83.41           C  
ANISOU 5170  CD  GLN A 692    10265  10529  10894   -296  -1253    594       C  
ATOM   5171  OE1 GLN A 692     -69.438 -28.949-107.625  1.00 84.61           O  
ANISOU 5171  OE1 GLN A 692    10447  10686  11014   -352  -1278    588       O  
ATOM   5172  NE2 GLN A 692     -67.811 -27.787-108.655  1.00 84.00           N  
ANISOU 5172  NE2 GLN A 692    10367  10579  10969   -244  -1251    615       N  
ATOM   5173  N   SER A 693     -74.363 -26.330-107.108  1.00 84.85           N  
ANISOU 5173  N   SER A 693    10198  10936  11103   -391  -1236    446       N  
ATOM   5174  CA  SER A 693     -75.769 -26.523-107.447  1.00 86.31           C  
ANISOU 5174  CA  SER A 693    10331  11189  11271   -411  -1253    409       C  
ATOM   5175  C   SER A 693     -76.470 -25.205-107.808  1.00 88.04           C  
ANISOU 5175  C   SER A 693    10484  11440  11524   -334  -1252    366       C  
ATOM   5176  O   SER A 693     -77.547 -25.221-108.402  1.00 90.11           O  
ANISOU 5176  O   SER A 693    10705  11752  11779   -321  -1273    333       O  
ATOM   5177  CB  SER A 693     -76.511 -27.233-106.323  1.00 85.89           C  
ANISOU 5177  CB  SER A 693    10245  11209  11178   -519  -1245    382       C  
ATOM   5178  OG  SER A 693     -76.547 -26.427-105.168  1.00 86.01           O  
ANISOU 5178  OG  SER A 693    10207  11266  11206   -528  -1212    349       O  
ATOM   5179  N   TYR A 694     -75.849 -24.078-107.458  1.00 88.02           N  
ANISOU 5179  N   TYR A 694    10477  11407  11557   -282  -1234    364       N  
ATOM   5180  CA  TYR A 694     -76.334 -22.759-107.857  1.00 88.31           C  
ANISOU 5180  CA  TYR A 694    10477  11450  11626   -197  -1246    329       C  
ATOM   5181  C   TYR A 694     -75.541 -22.202-109.035  1.00 90.17           C  
ANISOU 5181  C   TYR A 694    10776  11600  11885   -122  -1261    374       C  
ATOM   5182  O   TYR A 694     -75.624 -21.011-109.330  1.00 93.82           O  
ANISOU 5182  O   TYR A 694    11234  12039  12374    -52  -1274    358       O  
ATOM   5183  CB  TYR A 694     -76.246 -21.771-106.698  1.00 87.54           C  
ANISOU 5183  CB  TYR A 694    10340  11372  11548   -187  -1225    293       C  
ATOM   5184  CG  TYR A 694     -77.125 -22.088-105.521  1.00 88.78           C  
ANISOU 5184  CG  TYR A 694    10422  11630  11679   -253  -1208    238       C  
ATOM   5185  CD1 TYR A 694     -76.733 -23.021-104.577  1.00 90.69           C  
ANISOU 5185  CD1 TYR A 694    10677  11886  11892   -348  -1183    259       C  
ATOM   5186  CD2 TYR A 694     -78.332 -21.432-105.328  1.00 90.11           C  
ANISOU 5186  CD2 TYR A 694    10507  11885  11846   -219  -1221    162       C  
ATOM   5187  CE1 TYR A 694     -77.524 -23.314-103.482  1.00 91.75           C  
ANISOU 5187  CE1 TYR A 694    10746  12119  11994   -421  -1166    212       C  
ATOM   5188  CE2 TYR A 694     -79.133 -21.721-104.234  1.00 92.13           C  
ANISOU 5188  CE2 TYR A 694    10685  12252  12069   -286  -1202    108       C  
ATOM   5189  CZ  TYR A 694     -78.717 -22.664-103.313  1.00 91.84           C  
ANISOU 5189  CZ  TYR A 694    10665  12227  12001   -393  -1172    137       C  
ATOM   5190  OH  TYR A 694     -79.482 -22.969-102.216  1.00 93.70           O  
ANISOU 5190  OH  TYR A 694    10827  12576  12195   -472  -1150     88       O  
ATOM   5191  N   ASP A 695     -74.768 -23.058-109.698  1.00 91.14           N  
ANISOU 5191  N   ASP A 695    10958  11676  11993   -137  -1263    427       N  
ATOM   5192  CA  ASP A 695     -73.973 -22.672-110.876  1.00 93.50           C  
ANISOU 5192  CA  ASP A 695    11314  11908  12302    -78  -1274    473       C  
ATOM   5193  C   ASP A 695     -72.923 -21.596-110.593  1.00 92.73           C  
ANISOU 5193  C   ASP A 695    11241  11760  12230    -52  -1255    495       C  
ATOM   5194  O   ASP A 695     -72.569 -20.819-111.482  1.00 93.59           O  
ANISOU 5194  O   ASP A 695    11385  11825  12349      0  -1267    518       O  
ATOM   5195  CB  ASP A 695     -74.874 -22.227-112.040  1.00 96.96           C  
ANISOU 5195  CB  ASP A 695    11745  12349  12743    -14  -1309    456       C  
ATOM   5196  CG  ASP A 695     -76.018 -23.182-112.292  1.00101.20           C  
ANISOU 5196  CG  ASP A 695    12248  12946  13257    -42  -1329    426       C  
ATOM   5197  OD1 ASP A 695     -75.760 -24.394-112.457  1.00103.91           O  
ANISOU 5197  OD1 ASP A 695    12621  13285  13573    -89  -1331    453       O  
ATOM   5198  OD2 ASP A 695     -77.179 -22.716-112.324  1.00105.04           O  
ANISOU 5198  OD2 ASP A 695    12679  13483  13748    -15  -1348    372       O  
ATOM   5199  N   GLU A 696     -72.431 -21.553-109.359  1.00 91.67           N  
ANISOU 5199  N   GLU A 696    11093  11634  12102    -94  -1227    488       N  
ATOM   5200  CA  GLU A 696     -71.356 -20.637-108.994  1.00 90.61           C  
ANISOU 5200  CA  GLU A 696    10983  11455  11989    -82  -1208    510       C  
ATOM   5201  C   GLU A 696     -70.030 -21.181-109.501  1.00 90.16           C  
ANISOU 5201  C   GLU A 696    10978  11362  11917    -93  -1195    564       C  
ATOM   5202  O   GLU A 696     -69.845 -22.397-109.585  1.00 91.42           O  
ANISOU 5202  O   GLU A 696    11151  11534  12049   -121  -1197    576       O  
ATOM   5203  CB  GLU A 696     -71.297 -20.458-107.479  1.00 91.13           C  
ANISOU 5203  CB  GLU A 696    11014  11546  12065   -122  -1183    481       C  
ATOM   5204  CG  GLU A 696     -72.537 -19.830-106.867  1.00 92.95           C  
ANISOU 5204  CG  GLU A 696    11182  11826  12306   -106  -1194    418       C  
ATOM   5205  CD  GLU A 696     -72.492 -18.315-106.869  1.00 96.47           C  
ANISOU 5205  CD  GLU A 696    11633  12236  12783    -46  -1208    401       C  
ATOM   5206  OE1 GLU A 696     -72.883 -17.716-105.844  1.00101.04           O  
ANISOU 5206  OE1 GLU A 696    12170  12844  13373    -42  -1205    354       O  
ATOM   5207  OE2 GLU A 696     -72.060 -17.716-107.878  1.00 96.95           O  
ANISOU 5207  OE2 GLU A 696    11745  12238  12853     -3  -1227    435       O  
ATOM   5208  N   ILE A 697     -69.116 -20.285-109.854  1.00 89.83           N  
ANISOU 5208  N   ILE A 697    10965  11278  11886    -71  -1187    593       N  
ATOM   5209  CA  ILE A 697     -67.763 -20.687-110.243  1.00 90.64           C  
ANISOU 5209  CA  ILE A 697    11104  11366  11969    -82  -1171    636       C  
ATOM   5210  C   ILE A 697     -66.843 -20.324-109.080  1.00 89.03           C  
ANISOU 5210  C   ILE A 697    10892  11156  11778   -115  -1142    636       C  
ATOM   5211  O   ILE A 697     -66.569 -19.148-108.837  1.00 88.33           O  
ANISOU 5211  O   ILE A 697    10807  11043  11712   -109  -1135    638       O  
ATOM   5212  CB  ILE A 697     -67.313 -20.036-111.582  1.00 91.37           C  
ANISOU 5212  CB  ILE A 697    11234  11428  12053    -47  -1179    674       C  
ATOM   5213  CG1 ILE A 697     -68.352 -20.260-112.702  1.00 90.53           C  
ANISOU 5213  CG1 ILE A 697    11134  11323  11937     -8  -1212    670       C  
ATOM   5214  CG2 ILE A 697     -65.920 -20.508-111.997  1.00 90.16           C  
ANISOU 5214  CG2 ILE A 697    11104  11282  11870    -60  -1160    710       C  
ATOM   5215  CD1 ILE A 697     -68.796 -21.696-112.915  1.00 89.53           C  
ANISOU 5215  CD1 ILE A 697    11000  11228  11786    -16  -1224    660       C  
ATOM   5216  N   THR A 698     -66.388 -21.346-108.358  1.00 88.21           N  
ANISOU 5216  N   THR A 698    10785  11072  11657   -148  -1130    631       N  
ATOM   5217  CA  THR A 698     -65.813 -21.154-107.021  1.00 89.73           C  
ANISOU 5217  CA  THR A 698    10963  11268  11862   -181  -1107    618       C  
ATOM   5218  C   THR A 698     -64.317 -21.463-106.916  1.00 87.85           C  
ANISOU 5218  C   THR A 698    10744  11027  11607   -191  -1091    640       C  
ATOM   5219  O   THR A 698     -63.848 -22.526-107.334  1.00 87.20           O  
ANISOU 5219  O   THR A 698    10682  10956  11492   -186  -1101    649       O  
ATOM   5220  CB  THR A 698     -66.579 -21.969-105.954  1.00 91.31           C  
ANISOU 5220  CB  THR A 698    11141  11496  12054   -219  -1110    585       C  
ATOM   5221  OG1 THR A 698     -66.381 -23.369-106.184  1.00 94.35           O  
ANISOU 5221  OG1 THR A 698    11555  11888  12403   -235  -1125    595       O  
ATOM   5222  CG2 THR A 698     -68.069 -21.677-106.023  1.00 91.93           C  
ANISOU 5222  CG2 THR A 698    11185  11598  12143   -212  -1124    553       C  
ATOM   5223  N   ALA A 699     -63.579 -20.515-106.350  1.00 86.28           N  
ANISOU 5223  N   ALA A 699    10538  10816  11427   -202  -1069    643       N  
ATOM   5224  CA  ALA A 699     -62.150 -20.665-106.144  1.00 84.60           C  
ANISOU 5224  CA  ALA A 699    10331  10612  11199   -214  -1051    656       C  
ATOM   5225  C   ALA A 699     -61.903 -20.983-104.674  1.00 84.11           C  
ANISOU 5225  C   ALA A 699    10256  10557  11143   -243  -1041    631       C  
ATOM   5226  O   ALA A 699     -62.183 -20.165-103.793  1.00 84.36           O  
ANISOU 5226  O   ALA A 699    10270  10578  11205   -258  -1030    615       O  
ATOM   5227  CB  ALA A 699     -61.413 -19.405-106.571  1.00 82.89           C  
ANISOU 5227  CB  ALA A 699    10119  10381  10993   -217  -1036    681       C  
ATOM   5228  N   MET A 700     -61.410 -22.191-104.419  1.00 82.58           N  
ANISOU 5228  N   MET A 700    10077  10379  10919   -246  -1050    624       N  
ATOM   5229  CA  MET A 700     -61.190 -22.676-103.066  1.00 81.27           C  
ANISOU 5229  CA  MET A 700     9911  10216  10749   -274  -1047    601       C  
ATOM   5230  C   MET A 700     -59.707 -22.630-102.771  1.00 82.11           C  
ANISOU 5230  C   MET A 700    10017  10334  10845   -269  -1035    602       C  
ATOM   5231  O   MET A 700     -58.895 -22.978-103.634  1.00 84.08           O  
ANISOU 5231  O   MET A 700    10275  10603  11067   -242  -1040    612       O  
ATOM   5232  CB  MET A 700     -61.703 -24.113-102.937  1.00 81.33           C  
ANISOU 5232  CB  MET A 700     9950  10226  10723   -283  -1078    592       C  
ATOM   5233  CG  MET A 700     -61.637 -24.702-101.536  1.00 81.91           C  
ANISOU 5233  CG  MET A 700    10038  10299  10786   -321  -1082    571       C  
ATOM   5234  SD  MET A 700     -62.674 -23.831-100.345  1.00 82.29           S  
ANISOU 5234  SD  MET A 700    10043  10355  10866   -364  -1057    550       S  
ATOM   5235  CE  MET A 700     -64.234 -24.689-100.504  1.00 80.59           C  
ANISOU 5235  CE  MET A 700     9834  10158  10627   -398  -1080    542       C  
ATOM   5236  N   THR A 701     -59.353 -22.187-101.567  1.00 81.21           N  
ANISOU 5236  N   THR A 701     9889  10217  10748   -293  -1018    586       N  
ATOM   5237  CA  THR A 701     -57.966 -22.256-101.118  1.00 79.86           C  
ANISOU 5237  CA  THR A 701     9714  10063  10564   -291  -1010    578       C  
ATOM   5238  C   THR A 701     -57.795 -23.483-100.249  1.00 81.23           C  
ANISOU 5238  C   THR A 701     9917  10237  10709   -293  -1034    555       C  
ATOM   5239  O   THR A 701     -58.715 -23.872 -99.521  1.00 79.75           O  
ANISOU 5239  O   THR A 701     9743  10034  10523   -320  -1044    546       O  
ATOM   5240  CB  THR A 701     -57.495 -21.002-100.341  1.00 78.66           C  
ANISOU 5240  CB  THR A 701     9534   9906  10447   -315   -981    574       C  
ATOM   5241  OG1 THR A 701     -58.323 -20.784 -99.193  1.00 78.12           O  
ANISOU 5241  OG1 THR A 701     9460   9819  10402   -339   -979    555       O  
ATOM   5242  CG2 THR A 701     -57.528 -19.778-101.220  1.00 78.47           C  
ANISOU 5242  CG2 THR A 701     9498   9872  10443   -317   -967    599       C  
ATOM   5243  N   GLY A 702     -56.618 -24.096-100.355  1.00 84.47           N  
ANISOU 5243  N   GLY A 702    10337  10669  11087   -265  -1047    544       N  
ATOM   5244  CA  GLY A 702     -56.214 -25.212 -99.495  1.00 87.20           C  
ANISOU 5244  CA  GLY A 702    10722  11009  11399   -258  -1080    518       C  
ATOM   5245  C   GLY A 702     -54.703 -25.286 -99.367  1.00 87.60           C  
ANISOU 5245  C   GLY A 702    10758  11094  11428   -225  -1082    495       C  
ATOM   5246  O   GLY A 702     -53.981 -24.564-100.065  1.00 86.57           O  
ANISOU 5246  O   GLY A 702    10585  11002  11303   -213  -1056    502       O  
ATOM   5247  N   ASP A 703     -54.221 -26.150 -98.475  1.00 88.84           N  
ANISOU 5247  N   ASP A 703    10953  11244  11558   -212  -1115    467       N  
ATOM   5248  CA  ASP A 703     -52.779 -26.368 -98.336  1.00 91.28           C  
ANISOU 5248  CA  ASP A 703    11249  11594  11840   -169  -1127    434       C  
ATOM   5249  C   ASP A 703     -52.387 -27.734 -97.774  1.00 90.07           C  
ANISOU 5249  C   ASP A 703    11162  11423  11637   -130  -1190    401       C  
ATOM   5250  O   ASP A 703     -51.243 -28.159 -97.931  1.00 91.43           O  
ANISOU 5250  O   ASP A 703    11329  11636  11774    -72  -1215    364       O  
ATOM   5251  CB  ASP A 703     -52.135 -25.253 -97.506  1.00 95.49           C  
ANISOU 5251  CB  ASP A 703    11729  12146  12405   -198  -1084    427       C  
ATOM   5252  CG  ASP A 703     -52.485 -25.333 -96.032  1.00 98.81           C  
ANISOU 5252  CG  ASP A 703    12177  12527  12839   -232  -1090    416       C  
ATOM   5253  OD1 ASP A 703     -53.415 -26.090 -95.663  1.00100.11           O  
ANISOU 5253  OD1 ASP A 703    12396  12649  12991   -249  -1117    422       O  
ATOM   5254  OD2 ASP A 703     -51.819 -24.627 -95.240  1.00101.46           O  
ANISOU 5254  OD2 ASP A 703    12479  12876  13193   -246  -1066    401       O  
ATOM   5255  N   GLY A 704     -53.326 -28.408 -97.118  1.00 88.19           N  
ANISOU 5255  N   GLY A 704    10988  11127  11391   -163  -1219    410       N  
ATOM   5256  CA  GLY A 704     -53.053 -29.712 -96.510  1.00 89.13           C  
ANISOU 5256  CA  GLY A 704    11193  11213  11459   -137  -1289    383       C  
ATOM   5257  C   GLY A 704     -53.492 -30.891 -97.358  1.00 88.22           C  
ANISOU 5257  C   GLY A 704    11148  11069  11301   -106  -1349    387       C  
ATOM   5258  O   GLY A 704     -54.230 -30.724 -98.327  1.00 87.81           O  
ANISOU 5258  O   GLY A 704    11078  11021  11263   -117  -1332    415       O  
ATOM   5259  N   VAL A 705     -53.032 -32.085 -96.991  1.00 88.20           N  
ANISOU 5259  N   VAL A 705    11231  11034  11244    -66  -1426    358       N  
ATOM   5260  CA  VAL A 705     -53.470 -33.320 -97.641  1.00 89.52           C  
ANISOU 5260  CA  VAL A 705    11488  11159  11364    -40  -1499    360       C  
ATOM   5261  C   VAL A 705     -54.984 -33.453 -97.604  1.00 91.84           C  
ANISOU 5261  C   VAL A 705    11816  11408  11670   -129  -1490    405       C  
ATOM   5262  O   VAL A 705     -55.578 -34.056 -98.497  1.00 92.12           O  
ANISOU 5262  O   VAL A 705    11888  11425  11687   -122  -1522    419       O  
ATOM   5263  CB  VAL A 705     -52.871 -34.570 -96.970  1.00 89.55           C  
ANISOU 5263  CB  VAL A 705    11603  11116  11306      3  -1594    323       C  
ATOM   5264  CG1 VAL A 705     -51.873 -35.256 -97.887  1.00 89.32           C  
ANISOU 5264  CG1 VAL A 705    11589  11115  11231    120  -1655    276       C  
ATOM   5265  CG2 VAL A 705     -52.251 -34.214 -95.627  1.00 90.49           C  
ANISOU 5265  CG2 VAL A 705    11715  11235  11431    -11  -1581    303       C  
ATOM   5266  N   ASN A 706     -55.591 -32.885 -96.561  1.00 95.01           N  
ANISOU 5266  N   ASN A 706    12199  11800  12099   -210  -1448    423       N  
ATOM   5267  CA  ASN A 706     -57.042 -32.908 -96.357  1.00 96.49           C  
ANISOU 5267  CA  ASN A 706    12401  11965  12295   -303  -1431    458       C  
ATOM   5268  C   ASN A 706     -57.839 -32.092 -97.370  1.00 93.51           C  
ANISOU 5268  C   ASN A 706    11943  11622  11961   -315  -1377    482       C  
ATOM   5269  O   ASN A 706     -58.951 -32.461 -97.724  1.00 95.85           O  
ANISOU 5269  O   ASN A 706    12263  11905  12250   -361  -1387    503       O  
ATOM   5270  CB  ASN A 706     -57.387 -32.423 -94.944  1.00100.68           C  
ANISOU 5270  CB  ASN A 706    12918  12494  12839   -378  -1397    461       C  
ATOM   5271  CG  ASN A 706     -57.072 -33.453 -93.876  1.00102.42           C  
ANISOU 5271  CG  ASN A 706    13246  12664  13003   -398  -1462    449       C  
ATOM   5272  OD1 ASN A 706     -57.234 -34.659 -94.081  1.00102.68           O  
ANISOU 5272  OD1 ASN A 706    13384  12647  12980   -399  -1538    452       O  
ATOM   5273  ND2 ASN A 706     -56.631 -32.978 -92.718  1.00103.58           N  
ANISOU 5273  ND2 ASN A 706    13376  12818  13160   -415  -1438    436       N  
ATOM   5274  N   ASP A 707     -57.276 -30.979 -97.823  1.00 89.49           N  
ANISOU 5274  N   ASP A 707    11346  11159  11497   -276  -1322    479       N  
ATOM   5275  CA  ASP A 707     -57.964 -30.121 -98.773  1.00 89.20           C  
ANISOU 5275  CA  ASP A 707    11241  11148  11500   -283  -1275    501       C  
ATOM   5276  C   ASP A 707     -57.873 -30.641-100.210  1.00 89.68           C  
ANISOU 5276  C   ASP A 707    11318  11214  11541   -227  -1305    506       C  
ATOM   5277  O   ASP A 707     -58.486 -30.075-101.114  1.00 91.74           O  
ANISOU 5277  O   ASP A 707    11537  11492  11828   -228  -1276    525       O  
ATOM   5278  CB  ASP A 707     -57.398 -28.705 -98.710  1.00 89.20           C  
ANISOU 5278  CB  ASP A 707    11156  11186  11550   -272  -1212    500       C  
ATOM   5279  CG  ASP A 707     -57.240 -28.206 -97.300  1.00 90.14           C  
ANISOU 5279  CG  ASP A 707    11260  11302  11686   -312  -1188    488       C  
ATOM   5280  OD1 ASP A 707     -58.246 -27.794 -96.686  1.00 90.27           O  
ANISOU 5280  OD1 ASP A 707    11261  11314  11724   -369  -1164    496       O  
ATOM   5281  OD2 ASP A 707     -56.097 -28.217 -96.806  1.00 92.79           O  
ANISOU 5281  OD2 ASP A 707    11596  11647  12012   -282  -1194    466       O  
ATOM   5282  N   ALA A 708     -57.109 -31.708-100.426  1.00 88.07           N  
ANISOU 5282  N   ALA A 708    11176  10996  11287   -172  -1367    484       N  
ATOM   5283  CA  ALA A 708     -56.888 -32.221-101.777  1.00 87.77           C  
ANISOU 5283  CA  ALA A 708    11151  10970  11224   -107  -1399    481       C  
ATOM   5284  C   ALA A 708     -58.189 -32.523-102.537  1.00 87.80           C  
ANISOU 5284  C   ALA A 708    11176  10951  11230   -140  -1409    509       C  
ATOM   5285  O   ALA A 708     -58.356 -32.038-103.661  1.00 90.48           O  
ANISOU 5285  O   ALA A 708    11469  11320  11586   -114  -1384    522       O  
ATOM   5286  CB  ALA A 708     -55.957 -33.428-101.766  1.00 90.52           C  
ANISOU 5286  CB  ALA A 708    11575  11303  11513    -37  -1478    444       C  
ATOM   5287  N   PRO A 709     -59.120 -33.298-101.931  1.00 85.49           N  
ANISOU 5287  N   PRO A 709    10952  10611  10916   -203  -1446    519       N  
ATOM   5288  CA  PRO A 709     -60.365 -33.612-102.642  1.00 85.50           C  
ANISOU 5288  CA  PRO A 709    10968  10599  10916   -240  -1457    542       C  
ATOM   5289  C   PRO A 709     -61.215 -32.369-102.939  1.00 84.77           C  
ANISOU 5289  C   PRO A 709    10782  10545  10879   -274  -1385    561       C  
ATOM   5290  O   PRO A 709     -61.876 -32.304-103.976  1.00 83.50           O  
ANISOU 5290  O   PRO A 709    10605  10392  10726   -264  -1384    574       O  
ATOM   5291  CB  PRO A 709     -61.105 -34.518-101.653  1.00 86.13           C  
ANISOU 5291  CB  PRO A 709    11130  10633  10960   -323  -1500    548       C  
ATOM   5292  CG  PRO A 709     -60.586 -34.111-100.316  1.00 84.59           C  
ANISOU 5292  CG  PRO A 709    10924  10442  10774   -350  -1475    537       C  
ATOM   5293  CD  PRO A 709     -59.130 -33.870-100.572  1.00 84.37           C  
ANISOU 5293  CD  PRO A 709    10875  10432  10749   -255  -1476    512       C  
ATOM   5294  N   ALA A 710     -61.185 -31.403-102.022  1.00 84.71           N  
ANISOU 5294  N   ALA A 710    10720  10557  10908   -308  -1332    559       N  
ATOM   5295  CA  ALA A 710     -61.984 -30.185-102.111  1.00 82.44           C  
ANISOU 5295  CA  ALA A 710    10352  10300  10671   -335  -1272    569       C  
ATOM   5296  C   ALA A 710     -61.444 -29.234-103.164  1.00 80.28           C  
ANISOU 5296  C   ALA A 710    10023  10050  10427   -275  -1240    577       C  
ATOM   5297  O   ALA A 710     -62.211 -28.519-103.800  1.00 79.24           O  
ANISOU 5297  O   ALA A 710     9851   9932  10324   -278  -1215    589       O  
ATOM   5298  CB  ALA A 710     -62.047 -29.500-100.750  1.00 83.65           C  
ANISOU 5298  CB  ALA A 710    10472  10463  10847   -384  -1235    560       C  
ATOM   5299  N   LEU A 711     -60.123 -29.226-103.333  1.00 80.28           N  
ANISOU 5299  N   LEU A 711    10025  10062  10416   -223  -1242    568       N  
ATOM   5300  CA  LEU A 711     -59.476 -28.419-104.367  1.00 81.94           C  
ANISOU 5300  CA  LEU A 711    10188  10303  10641   -176  -1213    577       C  
ATOM   5301  C   LEU A 711     -59.714 -29.046-105.736  1.00 83.27           C  
ANISOU 5301  C   LEU A 711    10381  10475  10783   -135  -1244    585       C  
ATOM   5302  O   LEU A 711     -59.803 -28.346-106.757  1.00 82.53           O  
ANISOU 5302  O   LEU A 711    10251  10401  10703   -115  -1221    602       O  
ATOM   5303  CB  LEU A 711     -57.975 -28.259-104.092  1.00 81.49           C  
ANISOU 5303  CB  LEU A 711    10116  10275  10571   -142  -1204    558       C  
ATOM   5304  CG  LEU A 711     -57.560 -27.474-102.840  1.00 81.97           C  
ANISOU 5304  CG  LEU A 711    10145  10338  10661   -176  -1169    550       C  
ATOM   5305  CD1 LEU A 711     -56.048 -27.451-102.695  1.00 83.10           C  
ANISOU 5305  CD1 LEU A 711    10271  10518  10783   -138  -1167    526       C  
ATOM   5306  CD2 LEU A 711     -58.108 -26.055-102.842  1.00 81.98           C  
ANISOU 5306  CD2 LEU A 711    10093  10341  10713   -210  -1118    569       C  
ATOM   5307  N   LYS A 712     -59.828 -30.371-105.747  1.00 83.94           N  
ANISOU 5307  N   LYS A 712    10532  10535  10826   -123  -1303    574       N  
ATOM   5308  CA  LYS A 712     -60.231 -31.076-106.948  1.00 85.64           C  
ANISOU 5308  CA  LYS A 712    10779  10744  11015    -89  -1341    580       C  
ATOM   5309  C   LYS A 712     -61.671 -30.709-107.344  1.00 86.26           C  
ANISOU 5309  C   LYS A 712    10839  10812  11121   -131  -1326    601       C  
ATOM   5310  O   LYS A 712     -61.929 -30.425-108.509  1.00 86.92           O  
ANISOU 5310  O   LYS A 712    10904  10911  11210   -100  -1321    614       O  
ATOM   5311  CB  LYS A 712     -60.007 -32.582-106.805  1.00 86.64           C  
ANISOU 5311  CB  LYS A 712    10994  10837  11088    -67  -1418    560       C  
ATOM   5312  CG  LYS A 712     -58.568 -32.985-107.099  1.00 88.12           C  
ANISOU 5312  CG  LYS A 712    11191  11051  11237     15  -1445    530       C  
ATOM   5313  CD  LYS A 712     -58.017 -33.976-106.082  1.00 90.87           C  
ANISOU 5313  CD  LYS A 712    11614  11364  11548     23  -1503    501       C  
ATOM   5314  CE  LYS A 712     -58.072 -35.422-106.561  1.00 93.61           C  
ANISOU 5314  CE  LYS A 712    12059  11669  11838     67  -1596    484       C  
ATOM   5315  NZ  LYS A 712     -57.633 -36.368-105.489  1.00 95.04           N  
ANISOU 5315  NZ  LYS A 712    12331  11801  11979     68  -1663    459       N  
ATOM   5316  N   LYS A 713     -62.585 -30.655-106.376  1.00 88.45           N  
ANISOU 5316  N   LYS A 713    11116  11075  11415   -200  -1318    602       N  
ATOM   5317  CA  LYS A 713     -63.997 -30.372-106.663  1.00 89.92           C  
ANISOU 5317  CA  LYS A 713    11278  11266  11622   -240  -1309    612       C  
ATOM   5318  C   LYS A 713     -64.248 -28.955-107.150  1.00 90.27           C  
ANISOU 5318  C   LYS A 713    11251  11333  11711   -223  -1258    620       C  
ATOM   5319  O   LYS A 713     -65.119 -28.732-107.988  1.00 91.82           O  
ANISOU 5319  O   LYS A 713    11432  11537  11918   -215  -1261    627       O  
ATOM   5320  CB  LYS A 713     -64.883 -30.665-105.453  1.00 92.53           C  
ANISOU 5320  CB  LYS A 713    11617  11592  11948   -323  -1310    604       C  
ATOM   5321  CG  LYS A 713     -65.206 -32.140-105.271  1.00 99.16           C  
ANISOU 5321  CG  LYS A 713    12541  12400  12735   -361  -1373    603       C  
ATOM   5322  CD  LYS A 713     -66.129 -32.381-104.082  1.00104.07           C  
ANISOU 5322  CD  LYS A 713    13167  13029  13345   -460  -1370    598       C  
ATOM   5323  CE  LYS A 713     -67.552 -31.897-104.347  1.00106.86           C  
ANISOU 5323  CE  LYS A 713    13459  13425  13718   -503  -1345    595       C  
ATOM   5324  NZ  LYS A 713     -68.312 -32.791-105.270  1.00108.66           N  
ANISOU 5324  NZ  LYS A 713    13725  13642  13915   -516  -1391    602       N  
ATOM   5325  N   ALA A 714     -63.482 -28.002-106.630  1.00 90.57           N  
ANISOU 5325  N   ALA A 714    11255  11382  11776   -217  -1219    619       N  
ATOM   5326  CA  ALA A 714     -63.692 -26.592-106.949  1.00 91.91           C  
ANISOU 5326  CA  ALA A 714    11372  11563  11987   -207  -1179    628       C  
ATOM   5327  C   ALA A 714     -63.318 -26.290-108.394  1.00 92.39           C  
ANISOU 5327  C   ALA A 714    11431  11630  12040   -156  -1180    648       C  
ATOM   5328  O   ALA A 714     -62.536 -27.030-108.997  1.00 94.19           O  
ANISOU 5328  O   ALA A 714    11687  11866  12234   -122  -1201    651       O  
ATOM   5329  CB  ALA A 714     -62.888 -25.717-106.003  1.00 92.89           C  
ANISOU 5329  CB  ALA A 714    11468  11690  12134   -219  -1144    623       C  
ATOM   5330  N   GLU A 715     -63.875 -25.208-108.938  1.00 91.30           N  
ANISOU 5330  N   GLU A 715    11266  11491  11931   -148  -1162    659       N  
ATOM   5331  CA  GLU A 715     -63.533 -24.741-110.285  1.00 90.95           C  
ANISOU 5331  CA  GLU A 715    11224  11451  11879   -108  -1160    683       C  
ATOM   5332  C   GLU A 715     -62.077 -24.283-110.384  1.00 90.48           C  
ANISOU 5332  C   GLU A 715    11159  11411  11808   -100  -1135    695       C  
ATOM   5333  O   GLU A 715     -61.356 -24.689-111.294  1.00 91.79           O  
ANISOU 5333  O   GLU A 715    11335  11601  11938    -69  -1142    704       O  
ATOM   5334  CB  GLU A 715     -64.474 -23.625-110.737  1.00 92.09           C  
ANISOU 5334  CB  GLU A 715    11352  11581  12055   -103  -1154    690       C  
ATOM   5335  CG  GLU A 715     -65.820 -24.111-111.248  1.00 95.50           C  
ANISOU 5335  CG  GLU A 715    11787  12012  12486    -93  -1184    679       C  
ATOM   5336  CD  GLU A 715     -66.729 -24.619-110.144  1.00 98.85           C  
ANISOU 5336  CD  GLU A 715    12194  12445  12919   -134  -1191    649       C  
ATOM   5337  OE1 GLU A 715     -66.979 -23.869-109.172  1.00 99.93           O  
ANISOU 5337  OE1 GLU A 715    12301  12585  13083   -156  -1171    632       O  
ATOM   5338  OE2 GLU A 715     -67.201 -25.771-110.255  1.00100.10           O  
ANISOU 5338  OE2 GLU A 715    12372  12610  13051   -147  -1218    642       O  
ATOM   5339  N   ILE A 716     -61.648 -23.428-109.460  1.00 89.31           N  
ANISOU 5339  N   ILE A 716    10989  11258  11684   -128  -1107    692       N  
ATOM   5340  CA  ILE A 716     -60.238 -23.056-109.381  1.00 89.57           C  
ANISOU 5340  CA  ILE A 716    11010  11317  11703   -132  -1082    699       C  
ATOM   5341  C   ILE A 716     -59.682 -23.471-108.023  1.00 89.30           C  
ANISOU 5341  C   ILE A 716    10969  11287  11672   -152  -1078    673       C  
ATOM   5342  O   ILE A 716     -59.832 -22.762-107.016  1.00 89.15           O  
ANISOU 5342  O   ILE A 716    10935  11251  11687   -183  -1060    666       O  
ATOM   5343  CB  ILE A 716     -59.962 -21.550-109.660  1.00 90.42           C  
ANISOU 5343  CB  ILE A 716    11107  11417  11831   -153  -1055    724       C  
ATOM   5344  CG1 ILE A 716     -60.456 -21.135-111.043  1.00 89.75           C  
ANISOU 5344  CG1 ILE A 716    11039  11323  11736   -133  -1065    752       C  
ATOM   5345  CG2 ILE A 716     -58.471 -21.241-109.585  1.00 91.29           C  
ANISOU 5345  CG2 ILE A 716    11199  11568  11919   -170  -1029    729       C  
ATOM   5346  CD1 ILE A 716     -61.792 -20.438-111.008  1.00 91.01           C  
ANISOU 5346  CD1 ILE A 716    11207  11436  11933   -131  -1080    751       C  
ATOM   5347  N   GLY A 717     -59.056 -24.643-108.006  1.00 88.35           N  
ANISOU 5347  N   GLY A 717    10865  11188  11513   -127  -1100    656       N  
ATOM   5348  CA  GLY A 717     -58.295 -25.078-106.847  1.00 85.37           C  
ANISOU 5348  CA  GLY A 717    10489  10818  11129   -136  -1102    631       C  
ATOM   5349  C   GLY A 717     -57.082 -24.184-106.732  1.00 82.73           C  
ANISOU 5349  C   GLY A 717    10118  10519  10796   -145  -1066    633       C  
ATOM   5350  O   GLY A 717     -56.223 -24.175-107.617  1.00 81.37           O  
ANISOU 5350  O   GLY A 717     9931  10394  10591   -121  -1061    636       O  
ATOM   5351  N   ILE A 718     -57.041 -23.402-105.659  1.00 81.87           N  
ANISOU 5351  N   ILE A 718     9991  10393  10721   -183  -1043    629       N  
ATOM   5352  CA  ILE A 718     -55.886 -22.563-105.356  1.00 81.76           C  
ANISOU 5352  CA  ILE A 718     9945  10409  10710   -202  -1012    628       C  
ATOM   5353  C   ILE A 718     -55.134 -23.139-104.158  1.00 82.57           C  
ANISOU 5353  C   ILE A 718    10044  10524  10803   -200  -1019    594       C  
ATOM   5354  O   ILE A 718     -55.688 -23.237-103.054  1.00 82.60           O  
ANISOU 5354  O   ILE A 718    10061  10491  10831   -220  -1024    583       O  
ATOM   5355  CB  ILE A 718     -56.291 -21.096-105.102  1.00 80.61           C  
ANISOU 5355  CB  ILE A 718     9786  10230  10608   -244   -985    650       C  
ATOM   5356  CG1 ILE A 718     -56.906 -20.499-106.373  1.00 80.75           C  
ANISOU 5356  CG1 ILE A 718     9817  10235  10629   -240   -986    684       C  
ATOM   5357  CG2 ILE A 718     -55.086 -20.279-104.661  1.00 79.39           C  
ANISOU 5357  CG2 ILE A 718     9604  10103  10455   -275   -958    649       C  
ATOM   5358  CD1 ILE A 718     -57.688 -19.225-106.150  1.00 81.40           C  
ANISOU 5358  CD1 ILE A 718     9906  10266  10754   -265   -980    698       C  
ATOM   5359  N   ALA A 719     -53.883 -23.536-104.387  1.00 82.26           N  
ANISOU 5359  N   ALA A 719     9987  10542  10724   -173  -1021    574       N  
ATOM   5360  CA  ALA A 719     -53.045 -24.088-103.323  1.00 83.24           C  
ANISOU 5360  CA  ALA A 719    10109  10682  10833   -160  -1034    535       C  
ATOM   5361  C   ALA A 719     -52.076 -23.046-102.740  1.00 84.21           C  
ANISOU 5361  C   ALA A 719    10186  10838  10971   -195   -997    530       C  
ATOM   5362  O   ALA A 719     -51.690 -22.093-103.425  1.00 85.24           O  
ANISOU 5362  O   ALA A 719    10284  10999  11102   -223   -965    553       O  
ATOM   5363  CB  ALA A 719     -52.285 -25.306-103.824  1.00 82.35           C  
ANISOU 5363  CB  ALA A 719    10008  10616  10663    -95  -1073    502       C  
ATOM   5364  N   MET A 720     -51.700 -23.224-101.473  1.00 83.52           N  
ANISOU 5364  N   MET A 720    10100  10740  10891   -200  -1003    502       N  
ATOM   5365  CA  MET A 720     -50.678 -22.386-100.850  1.00 82.68           C  
ANISOU 5365  CA  MET A 720     9950  10670  10795   -229   -974    489       C  
ATOM   5366  C   MET A 720     -49.289 -22.839-101.271  1.00 82.46           C  
ANISOU 5366  C   MET A 720     9884  10732  10713   -191   -980    454       C  
ATOM   5367  O   MET A 720     -49.020 -24.044-101.351  1.00 82.69           O  
ANISOU 5367  O   MET A 720     9934  10780  10702   -129  -1021    419       O  
ATOM   5368  CB  MET A 720     -50.797 -22.410 -99.329  1.00 83.02           C  
ANISOU 5368  CB  MET A 720    10008  10672  10863   -244   -980    469       C  
ATOM   5369  CG  MET A 720     -52.099 -21.820 -98.822  1.00 85.64           C  
ANISOU 5369  CG  MET A 720    10360  10933  11244   -282   -970    495       C  
ATOM   5370  SD  MET A 720     -52.270 -20.082 -99.270  1.00 87.99           S  
ANISOU 5370  SD  MET A 720    10630  11219  11583   -334   -929    532       S  
ATOM   5371  CE  MET A 720     -53.939 -20.067 -99.917  1.00 88.03           C  
ANISOU 5371  CE  MET A 720    10667  11171  11610   -330   -940    560       C  
ATOM   5372  N   GLY A 721     -48.426 -21.863-101.549  1.00 81.66           N  
ANISOU 5372  N   GLY A 721     9729  10689  10607   -231   -942    460       N  
ATOM   5373  CA  GLY A 721     -47.031 -22.111-101.897  1.00 81.99           C  
ANISOU 5373  CA  GLY A 721     9715  10840  10594   -207   -939    420       C  
ATOM   5374  C   GLY A 721     -46.315 -22.809-100.762  1.00 83.41           C  
ANISOU 5374  C   GLY A 721     9893  11038  10762   -165   -968    363       C  
ATOM   5375  O   GLY A 721     -45.690 -23.855-100.958  1.00 84.65           O  
ANISOU 5375  O   GLY A 721    10045  11248  10868    -92  -1005    314       O  
ATOM   5376  N   SER A 722     -46.426 -22.230 -99.567  1.00 82.85           N  
ANISOU 5376  N   SER A 722     9828  10917  10734   -205   -956    366       N  
ATOM   5377  CA  SER A 722     -45.898 -22.827 -98.343  1.00 82.58           C  
ANISOU 5377  CA  SER A 722     9802  10880  10694   -170   -984    316       C  
ATOM   5378  C   SER A 722     -46.537 -24.188 -98.013  1.00 84.18           C  
ANISOU 5378  C   SER A 722    10079  11025  10881   -108  -1042    299       C  
ATOM   5379  O   SER A 722     -45.960 -24.983 -97.272  1.00 84.78           O  
ANISOU 5379  O   SER A 722    10174  11109  10930    -59  -1083    250       O  
ATOM   5380  CB  SER A 722     -46.123 -21.871 -97.184  1.00 80.61           C  
ANISOU 5380  CB  SER A 722     9553  10577  10498   -231   -959    331       C  
ATOM   5381  OG  SER A 722     -47.511 -21.675 -96.996  1.00 79.50           O  
ANISOU 5381  OG  SER A 722     9462  10343  10400   -257   -957    372       O  
ATOM   5382  N   GLY A 723     -47.723 -24.448 -98.566  1.00 87.10           N  
ANISOU 5382  N   GLY A 723    10495  11334  11264   -114  -1050    338       N  
ATOM   5383  CA  GLY A 723     -48.457 -25.711 -98.358  1.00 88.02           C  
ANISOU 5383  CA  GLY A 723    10689  11390  11362    -74  -1105    330       C  
ATOM   5384  C   GLY A 723     -47.809 -26.978 -98.905  1.00 87.88           C  
ANISOU 5384  C   GLY A 723    10695  11412  11281     12  -1163    285       C  
ATOM   5385  O   GLY A 723     -46.747 -26.921 -99.538  1.00 88.90           O  
ANISOU 5385  O   GLY A 723    10768  11633  11375     50  -1158    253       O  
ATOM   5386  N   THR A 724     -48.461 -28.118 -98.657  1.00 86.47           N  
ANISOU 5386  N   THR A 724    10602  11167  11083     41  -1222    281       N  
ATOM   5387  CA  THR A 724     -47.950 -29.444 -99.038  1.00 85.74           C  
ANISOU 5387  CA  THR A 724    10558  11091  10928    131  -1297    234       C  
ATOM   5388  C   THR A 724     -47.986 -29.667-100.539  1.00 87.08           C  
ANISOU 5388  C   THR A 724    10708  11306  11071    170  -1300    239       C  
ATOM   5389  O   THR A 724     -48.875 -29.149-101.228  1.00 88.36           O  
ANISOU 5389  O   THR A 724    10860  11447  11264    122  -1262    291       O  
ATOM   5390  CB  THR A 724     -48.783 -30.586 -98.426  1.00 84.66           C  
ANISOU 5390  CB  THR A 724    10536  10856  10775    135  -1364    238       C  
ATOM   5391  OG1 THR A 724     -49.995 -30.754 -99.176  1.00 82.23           O  
ANISOU 5391  OG1 THR A 724    10260  10502  10479    104  -1362    285       O  
ATOM   5392  CG2 THR A 724     -49.102 -30.323 -96.954  1.00 85.78           C  
ANISOU 5392  CG2 THR A 724    10705  10941  10945     76  -1354    248       C  
ATOM   5393  N   ALA A 725     -47.035 -30.461-101.033  1.00 87.16           N  
ANISOU 5393  N   ALA A 725    10714  11380  11021    262  -1349    181       N  
ATOM   5394  CA  ALA A 725     -46.973 -30.825-102.449  1.00 86.41           C  
ANISOU 5394  CA  ALA A 725    10604  11337  10889    313  -1362    175       C  
ATOM   5395  C   ALA A 725     -48.319 -31.351-102.941  1.00 85.66           C  
ANISOU 5395  C   ALA A 725    10587  11153  10807    295  -1387    221       C  
ATOM   5396  O   ALA A 725     -48.819 -30.906-103.974  1.00 84.71           O  
ANISOU 5396  O   ALA A 725    10436  11048  10699    272  -1351    259       O  
ATOM   5397  CB  ALA A 725     -45.880 -31.856-102.685  1.00 87.62           C  
ANISOU 5397  CB  ALA A 725    10763  11557  10969    430  -1434     93       C  
ATOM   5398  N   VAL A 726     -48.897 -32.278-102.172  1.00 85.28           N  
ANISOU 5398  N   VAL A 726    10640  11010  10752    299  -1450    219       N  
ATOM   5399  CA  VAL A 726     -50.195 -32.906-102.460  1.00 83.83           C  
ANISOU 5399  CA  VAL A 726    10539  10738  10574    271  -1483    259       C  
ATOM   5400  C   VAL A 726     -51.289 -31.899-102.832  1.00 82.61           C  
ANISOU 5400  C   VAL A 726    10344  10566  10478    184  -1409    325       C  
ATOM   5401  O   VAL A 726     -52.010 -32.093-103.817  1.00 81.60           O  
ANISOU 5401  O   VAL A 726    10229  10425  10347    185  -1414    350       O  
ATOM   5402  CB  VAL A 726     -50.675 -33.750-101.257  1.00 83.69           C  
ANISOU 5402  CB  VAL A 726    10628  10623  10545    248  -1544    257       C  
ATOM   5403  CG1 VAL A 726     -52.060 -34.329-101.509  1.00 84.61           C  
ANISOU 5403  CG1 VAL A 726    10823  10658  10664    199  -1571    301       C  
ATOM   5404  CG2 VAL A 726     -49.684 -34.860-100.956  1.00 84.66           C  
ANISOU 5404  CG2 VAL A 726    10815  10746  10603    346  -1636    190       C  
ATOM   5405  N   ALA A 727     -51.403 -30.839-102.030  1.00 81.75           N  
ANISOU 5405  N   ALA A 727    10187  10454  10418    114  -1347    348       N  
ATOM   5406  CA  ALA A 727     -52.389 -29.784-102.242  1.00 80.90           C  
ANISOU 5406  CA  ALA A 727    10042  10330  10366     39  -1283    401       C  
ATOM   5407  C   ALA A 727     -52.140 -29.046-103.550  1.00 82.21           C  
ANISOU 5407  C   ALA A 727    10142  10559  10535     51  -1241    417       C  
ATOM   5408  O   ALA A 727     -53.083 -28.755-104.291  1.00 83.49           O  
ANISOU 5408  O   ALA A 727    10305  10699  10718     26  -1224    455       O  
ATOM   5409  CB  ALA A 727     -52.377 -28.811-101.078  1.00 79.63           C  
ANISOU 5409  CB  ALA A 727     9846  10158  10250    -21  -1235    410       C  
ATOM   5410  N   LYS A 728     -50.870 -28.752-103.828  1.00 82.69           N  
ANISOU 5410  N   LYS A 728    10144  10701  10570     86  -1225    387       N  
ATOM   5411  CA  LYS A 728     -50.481 -28.106-105.076  1.00 82.97           C  
ANISOU 5411  CA  LYS A 728    10118  10810  10594     91  -1187    400       C  
ATOM   5412  C   LYS A 728     -50.747 -29.014-106.281  1.00 82.84           C  
ANISOU 5412  C   LYS A 728    10134  10805  10536    151  -1229    395       C  
ATOM   5413  O   LYS A 728     -51.295 -28.562-107.281  1.00 81.21           O  
ANISOU 5413  O   LYS A 728     9913  10602  10339    133  -1204    431       O  
ATOM   5414  CB  LYS A 728     -49.004 -27.710-105.056  1.00 85.05           C  
ANISOU 5414  CB  LYS A 728    10310  11177  10827    110  -1164    362       C  
ATOM   5415  CG  LYS A 728     -48.519 -26.922-103.855  1.00 85.69           C  
ANISOU 5415  CG  LYS A 728    10359  11258  10941     60  -1131    356       C  
ATOM   5416  CD  LYS A 728     -47.021 -27.161-103.709  1.00 88.09           C  
ANISOU 5416  CD  LYS A 728    10609  11663  11194    110  -1141    293       C  
ATOM   5417  CE  LYS A 728     -46.340 -26.148-102.799  1.00 89.41           C  
ANISOU 5417  CE  LYS A 728    10722  11858  11388     53  -1095    290       C  
ATOM   5418  NZ  LYS A 728     -45.975 -24.882-103.502  1.00 89.31           N  
ANISOU 5418  NZ  LYS A 728    10639  11910  11382    -14  -1030    323       N  
ATOM   5419  N   THR A 729     -50.364 -30.290-106.174  1.00 84.77           N  
ANISOU 5419  N   THR A 729    10427  11047  10733    227  -1300    346       N  
ATOM   5420  CA  THR A 729     -50.526 -31.264-107.267  1.00 87.97           C  
ANISOU 5420  CA  THR A 729    10869  11461  11092    297  -1353    331       C  
ATOM   5421  C   THR A 729     -51.997 -31.437-107.655  1.00 89.59           C  
ANISOU 5421  C   THR A 729    11130  11581  11327    258  -1362    381       C  
ATOM   5422  O   THR A 729     -52.307 -31.884-108.764  1.00 91.37           O  
ANISOU 5422  O   THR A 729    11371  11815  11526    296  -1385    385       O  
ATOM   5423  CB  THR A 729     -49.946 -32.662-106.916  1.00 89.05           C  
ANISOU 5423  CB  THR A 729    11072  11589  11172    388  -1445    267       C  
ATOM   5424  OG1 THR A 729     -48.798 -32.535-106.068  1.00 89.85           O  
ANISOU 5424  OG1 THR A 729    11137  11742  11259    412  -1444    219       O  
ATOM   5425  CG2 THR A 729     -49.545 -33.420-108.185  1.00 89.62           C  
ANISOU 5425  CG2 THR A 729    11146  11721  11184    482  -1490    231       C  
ATOM   5426  N   ALA A 730     -52.891 -31.067-106.739  1.00 89.47           N  
ANISOU 5426  N   ALA A 730    11138  11492  11361    184  -1343    415       N  
ATOM   5427  CA  ALA A 730     -54.326 -31.236-106.919  1.00 88.20           C  
ANISOU 5427  CA  ALA A 730    11023  11259  11227    140  -1351    455       C  
ATOM   5428  C   ALA A 730     -55.053 -29.933-107.252  1.00 88.26           C  
ANISOU 5428  C   ALA A 730    10977  11268  11288     77  -1282    503       C  
ATOM   5429  O   ALA A 730     -56.285 -29.902-107.263  1.00 90.81           O  
ANISOU 5429  O   ALA A 730    11325  11541  11638     36  -1282    531       O  
ATOM   5430  CB  ALA A 730     -54.927 -31.869-105.672  1.00 88.76           C  
ANISOU 5430  CB  ALA A 730    11164  11255  11305    101  -1388    454       C  
ATOM   5431  N   SER A 731     -54.304 -28.868-107.539  1.00 87.59           N  
ANISOU 5431  N   SER A 731    10823  11244  11213     69  -1228    509       N  
ATOM   5432  CA  SER A 731     -54.911 -27.555-107.791  1.00 88.01           C  
ANISOU 5432  CA  SER A 731    10837  11287  11313     11  -1171    552       C  
ATOM   5433  C   SER A 731     -54.530 -26.909-109.136  1.00 87.21           C  
ANISOU 5433  C   SER A 731    10697  11244  11195     23  -1142    572       C  
ATOM   5434  O   SER A 731     -53.568 -27.318-109.781  1.00 86.33           O  
ANISOU 5434  O   SER A 731    10566  11201  11034     70  -1152    547       O  
ATOM   5435  CB  SER A 731     -54.602 -26.611-106.628  1.00 89.63           C  
ANISOU 5435  CB  SER A 731    11010  11486  11556    -39  -1131    554       C  
ATOM   5436  OG  SER A 731     -53.278 -26.121-106.709  1.00 93.16           O  
ANISOU 5436  OG  SER A 731    11407  12004  11983    -31  -1105    538       O  
ATOM   5437  N   GLU A 732     -55.292 -25.896-109.543  1.00 88.19           N  
ANISOU 5437  N   GLU A 732    10810  11342  11355    -19  -1110    613       N  
ATOM   5438  CA  GLU A 732     -55.071 -25.208-110.822  1.00 90.95           C  
ANISOU 5438  CA  GLU A 732    11136  11734  11687    -20  -1084    640       C  
ATOM   5439  C   GLU A 732     -54.048 -24.086-110.741  1.00 92.11           C  
ANISOU 5439  C   GLU A 732    11234  11931  11829    -62  -1037    650       C  
ATOM   5440  O   GLU A 732     -53.490 -23.670-111.758  1.00 93.44           O  
ANISOU 5440  O   GLU A 732    11380  12159  11963    -67  -1017    665       O  
ATOM   5441  CB  GLU A 732     -56.381 -24.617-111.342  1.00 92.35           C  
ANISOU 5441  CB  GLU A 732    11335  11854  11900    -42  -1081    678       C  
ATOM   5442  CG  GLU A 732     -57.269 -25.601-112.070  1.00 94.17           C  
ANISOU 5442  CG  GLU A 732    11602  12060  12115     -1  -1123    676       C  
ATOM   5443  CD  GLU A 732     -57.618 -26.794-111.213  1.00 96.89           C  
ANISOU 5443  CD  GLU A 732    11982  12372  12460     14  -1165    646       C  
ATOM   5444  OE1 GLU A 732     -58.042 -26.603-110.047  1.00 95.73           O  
ANISOU 5444  OE1 GLU A 732    11837  12186  12347    -24  -1158    642       O  
ATOM   5445  OE2 GLU A 732     -57.477 -27.933-111.703  1.00100.79           O  
ANISOU 5445  OE2 GLU A 732    12504  12877  12913     63  -1208    626       O  
ATOM   5446  N   MET A 733     -53.819 -23.588-109.532  1.00 91.92           N  
ANISOU 5446  N   MET A 733    11198  11886  11838   -100  -1020    642       N  
ATOM   5447  CA  MET A 733     -53.010 -22.400-109.327  1.00 90.97           C  
ANISOU 5447  CA  MET A 733    11041  11798  11724   -155   -978    657       C  
ATOM   5448  C   MET A 733     -52.425 -22.409-107.917  1.00 88.39           C  
ANISOU 5448  C   MET A 733    10698  11470  11415   -168   -973    626       C  
ATOM   5449  O   MET A 733     -53.082 -22.835-106.961  1.00 85.61           O  
ANISOU 5449  O   MET A 733    10372  11059  11094   -161   -993    612       O  
ATOM   5450  CB  MET A 733     -53.883 -21.170-109.553  1.00 94.85           C  
ANISOU 5450  CB  MET A 733    11554  12227  12257   -204   -961    703       C  
ATOM   5451  CG  MET A 733     -53.198 -19.826-109.390  1.00102.49           C  
ANISOU 5451  CG  MET A 733    12502  13207  13230   -271   -926    726       C  
ATOM   5452  SD  MET A 733     -54.425 -18.507-109.215  1.00111.84           S  
ANISOU 5452  SD  MET A 733    13730  14287  14475   -310   -929    765       S  
ATOM   5453  CE  MET A 733     -55.445 -18.810-110.657  1.00111.82           C  
ANISOU 5453  CE  MET A 733    13763  14265  14457   -272   -952    791       C  
ATOM   5454  N   VAL A 734     -51.179 -21.956-107.798  1.00 87.11           N  
ANISOU 5454  N   VAL A 734    10490  11380  11228   -192   -946    613       N  
ATOM   5455  CA  VAL A 734     -50.513 -21.863-106.500  1.00 85.65           C  
ANISOU 5455  CA  VAL A 734    10283  11201  11058   -207   -940    582       C  
ATOM   5456  C   VAL A 734     -50.133 -20.425-106.205  1.00 85.12           C  
ANISOU 5456  C   VAL A 734    10193  11132  11014   -285   -900    609       C  
ATOM   5457  O   VAL A 734     -49.402 -19.811-106.980  1.00 87.65           O  
ANISOU 5457  O   VAL A 734    10483  11517  11300   -322   -874    626       O  
ATOM   5458  CB  VAL A 734     -49.239 -22.728-106.422  1.00 84.86           C  
ANISOU 5458  CB  VAL A 734    10144  11195  10902   -158   -953    527       C  
ATOM   5459  CG1 VAL A 734     -48.558 -22.530-105.078  1.00 83.78           C  
ANISOU 5459  CG1 VAL A 734     9986  11063  10783   -175   -947    496       C  
ATOM   5460  CG2 VAL A 734     -49.568 -24.199-106.624  1.00 85.65           C  
ANISOU 5460  CG2 VAL A 734    10281  11284  10975    -75  -1006    496       C  
ATOM   5461  N   LEU A 735     -50.641 -19.899-105.090  1.00 83.38           N  
ANISOU 5461  N   LEU A 735     9990  10840  10847   -312   -899    613       N  
ATOM   5462  CA  LEU A 735     -50.246 -18.585-104.598  1.00 82.40           C  
ANISOU 5462  CA  LEU A 735     9854  10705  10749   -382   -871    631       C  
ATOM   5463  C   LEU A 735     -48.842 -18.697-104.051  1.00 83.46           C  
ANISOU 5463  C   LEU A 735     9936  10921  10854   -392   -857    594       C  
ATOM   5464  O   LEU A 735     -48.622 -19.365-103.044  1.00 85.53           O  
ANISOU 5464  O   LEU A 735    10191  11181  11122   -358   -872    554       O  
ATOM   5465  CB  LEU A 735     -51.174 -18.110-103.484  1.00 80.62           C  
ANISOU 5465  CB  LEU A 735     9658  10388  10585   -394   -879    634       C  
ATOM   5466  CG  LEU A 735     -52.670 -18.005-103.746  1.00 80.10           C  
ANISOU 5466  CG  LEU A 735     9636  10245  10553   -379   -896    657       C  
ATOM   5467  CD1 LEU A 735     -53.357 -17.557-102.470  1.00 79.32           C  
ANISOU 5467  CD1 LEU A 735     9549  10083  10505   -390   -901    644       C  
ATOM   5468  CD2 LEU A 735     -52.971 -17.053-104.892  1.00 80.25           C  
ANISOU 5468  CD2 LEU A 735     9675  10246  10568   -408   -891    702       C  
ATOM   5469  N   ALA A 736     -47.893 -18.052-104.718  1.00 83.64           N  
ANISOU 5469  N   ALA A 736     9921  11018  10838   -441   -829    607       N  
ATOM   5470  CA  ALA A 736     -46.506 -18.122-104.308  1.00 84.80           C  
ANISOU 5470  CA  ALA A 736    10005  11264  10949   -454   -814    566       C  
ATOM   5471  C   ALA A 736     -46.304 -17.459-102.945  1.00 86.03           C  
ANISOU 5471  C   ALA A 736    10159  11377  11149   -493   -807    556       C  
ATOM   5472  O   ALA A 736     -45.521 -17.940-102.126  1.00 87.64           O  
ANISOU 5472  O   ALA A 736    10328  11628  11343   -468   -812    506       O  
ATOM   5473  CB  ALA A 736     -45.619 -17.488-105.362  1.00 86.64           C  
ANISOU 5473  CB  ALA A 736    10197  11596  11127   -517   -782    586       C  
ATOM   5474  N   ASP A 737     -47.033 -16.376-102.697  1.00 85.99           N  
ANISOU 5474  N   ASP A 737    10197  11281  11193   -546   -802    599       N  
ATOM   5475  CA  ASP A 737     -46.867 -15.610-101.468  1.00 87.30           C  
ANISOU 5475  CA  ASP A 737    10364  11403  11400   -586   -798    591       C  
ATOM   5476  C   ASP A 737     -48.021 -15.791-100.483  1.00 88.29           C  
ANISOU 5476  C   ASP A 737    10533  11427  11583   -547   -821    584       C  
ATOM   5477  O   ASP A 737     -48.199 -14.971 -99.576  1.00 89.07           O  
ANISOU 5477  O   ASP A 737    10647  11471  11724   -579   -820    586       O  
ATOM   5478  CB  ASP A 737     -46.681 -14.122-101.796  1.00 88.79           C  
ANISOU 5478  CB  ASP A 737    10570  11569  11595   -680   -782    637       C  
ATOM   5479  CG  ASP A 737     -47.943 -13.473-102.354  1.00 87.96           C  
ANISOU 5479  CG  ASP A 737    10535  11363  11521   -687   -799    686       C  
ATOM   5480  OD1 ASP A 737     -48.800 -14.188-102.910  1.00 88.37           O  
ANISOU 5480  OD1 ASP A 737    10606  11394  11574   -629   -813    690       O  
ATOM   5481  OD2 ASP A 737     -48.072 -12.237-102.239  1.00 88.01           O  
ANISOU 5481  OD2 ASP A 737    10579  11310  11549   -750   -803    718       O  
ATOM   5482  N   ASP A 738     -48.806 -16.852-100.678  1.00 88.95           N  
ANISOU 5482  N   ASP A 738    10638  11493  11666   -482   -841    574       N  
ATOM   5483  CA  ASP A 738     -49.955 -17.182 -99.810  1.00 90.12           C  
ANISOU 5483  CA  ASP A 738    10822  11562  11856   -451   -862    565       C  
ATOM   5484  C   ASP A 738     -50.928 -16.025 -99.527  1.00 90.77           C  
ANISOU 5484  C   ASP A 738    10936  11561  11988   -483   -862    592       C  
ATOM   5485  O   ASP A 738     -51.735 -16.104 -98.591  1.00 89.78           O  
ANISOU 5485  O   ASP A 738    10826  11387  11896   -467   -873    576       O  
ATOM   5486  CB  ASP A 738     -49.476 -17.780 -98.477  1.00 89.59           C  
ANISOU 5486  CB  ASP A 738    10741  11505  11792   -430   -869    520       C  
ATOM   5487  CG  ASP A 738     -48.579 -18.985 -98.663  1.00 90.51           C  
ANISOU 5487  CG  ASP A 738    10836  11695  11857   -381   -883    483       C  
ATOM   5488  OD1 ASP A 738     -48.772 -19.752 -99.636  1.00 89.30           O  
ANISOU 5488  OD1 ASP A 738    10692  11564  11673   -344   -897    487       O  
ATOM   5489  OD2 ASP A 738     -47.674 -19.163 -97.822  1.00 92.04           O  
ANISOU 5489  OD2 ASP A 738    11004  11924  12040   -376   -885    445       O  
ATOM   5490  N   ASN A 739     -50.846 -14.961-100.327  1.00 89.36           N  
ANISOU 5490  N   ASN A 739    10770  11371  11809   -527   -854    630       N  
ATOM   5491  CA  ASN A 739     -51.638 -13.762-100.095  1.00 88.48           C  
ANISOU 5491  CA  ASN A 739    10697  11179  11740   -552   -865    651       C  
ATOM   5492  C   ASN A 739     -52.990 -13.864-100.782  1.00 87.57           C  
ANISOU 5492  C   ASN A 739    10616  11016  11638   -515   -885    667       C  
ATOM   5493  O   ASN A 739     -53.062 -14.251-101.948  1.00 87.92           O  
ANISOU 5493  O   ASN A 739    10666  11084  11652   -504   -886    689       O  
ATOM   5494  CB  ASN A 739     -50.872 -12.527-100.576  1.00 89.51           C  
ANISOU 5494  CB  ASN A 739    10840  11310  11860   -624   -857    684       C  
ATOM   5495  CG  ASN A 739     -51.620 -11.221-100.330  1.00 91.56           C  
ANISOU 5495  CG  ASN A 739    11153  11475  12159   -645   -881    702       C  
ATOM   5496  OD1 ASN A 739     -52.650 -11.177 -99.653  1.00 91.91           O  
ANISOU 5496  OD1 ASN A 739    11213  11465  12242   -603   -901    681       O  
ATOM   5497  ND2 ASN A 739     -51.089 -10.139-100.884  1.00 93.53           N  
ANISOU 5497  ND2 ASN A 739    11434  11709  12393   -713   -884    740       N  
ATOM   5498  N   PHE A 740     -54.051 -13.522-100.046  1.00 86.26           N  
ANISOU 5498  N   PHE A 740    10469  10791  11513   -494   -903    651       N  
ATOM   5499  CA  PHE A 740     -55.421 -13.503-100.575  1.00 84.79           C  
ANISOU 5499  CA  PHE A 740    10309  10564  11342   -458   -926    657       C  
ATOM   5500  C   PHE A 740     -55.541 -12.549-101.754  1.00 87.33           C  
ANISOU 5500  C   PHE A 740    10672  10852  11656   -476   -940    699       C  
ATOM   5501  O   PHE A 740     -56.209 -12.863-102.738  1.00 88.29           O  
ANISOU 5501  O   PHE A 740    10809  10970  11765   -448   -952    714       O  
ATOM   5502  CB  PHE A 740     -56.424 -13.122 -99.480  1.00 82.73           C  
ANISOU 5502  CB  PHE A 740    10050  10261  11121   -436   -942    624       C  
ATOM   5503  CG  PHE A 740     -57.753 -12.654-100.003  1.00 81.92           C  
ANISOU 5503  CG  PHE A 740     9973  10116  11035   -402   -971    625       C  
ATOM   5504  CD1 PHE A 740     -58.782 -13.559-100.231  1.00 81.54           C  
ANISOU 5504  CD1 PHE A 740     9911  10087  10982   -364   -977    610       C  
ATOM   5505  CD2 PHE A 740     -57.983 -11.303-100.259  1.00 82.14           C  
ANISOU 5505  CD2 PHE A 740    10043  10084  11080   -406   -998    637       C  
ATOM   5506  CE1 PHE A 740     -60.014 -13.133-100.712  1.00 81.12           C  
ANISOU 5506  CE1 PHE A 740     9874  10006  10942   -328  -1005    603       C  
ATOM   5507  CE2 PHE A 740     -59.209 -10.871-100.744  1.00 82.16           C  
ANISOU 5507  CE2 PHE A 740    10071  10050  11096   -363  -1033    630       C  
ATOM   5508  CZ  PHE A 740     -60.226 -11.789-100.973  1.00 81.49           C  
ANISOU 5508  CZ  PHE A 740     9960   9995  11006   -322  -1034    610       C  
ATOM   5509  N   SER A 741     -54.890 -11.390-101.643  1.00 89.21           N  
ANISOU 5509  N   SER A 741    10934  11062  11898   -526   -943    717       N  
ATOM   5510  CA  SER A 741     -54.898 -10.384-102.702  1.00 91.46           C  
ANISOU 5510  CA  SER A 741    11274  11306  12169   -558   -962    761       C  
ATOM   5511  C   SER A 741     -54.308 -10.910-104.005  1.00 92.58           C  
ANISOU 5511  C   SER A 741    11409  11506  12260   -578   -943    796       C  
ATOM   5512  O   SER A 741     -54.693 -10.458-105.087  1.00 94.38           O  
ANISOU 5512  O   SER A 741    11684  11704  12471   -584   -962    831       O  
ATOM   5513  CB  SER A 741     -54.150  -9.131-102.261  1.00 93.08           C  
ANISOU 5513  CB  SER A 741    11510  11473  12379   -623   -970    776       C  
ATOM   5514  OG  SER A 741     -54.897  -8.427-101.289  1.00 95.07           O  
ANISOU 5514  OG  SER A 741    11787  11657  12677   -595  -1002    747       O  
ATOM   5515  N   THR A 742     -53.386 -11.865-103.899  1.00 91.92           N  
ANISOU 5515  N   THR A 742    11270  11507  12149   -584   -909    782       N  
ATOM   5516  CA  THR A 742     -52.815 -12.506-105.080  1.00 94.34           C  
ANISOU 5516  CA  THR A 742    11558  11885  12402   -590   -891    802       C  
ATOM   5517  C   THR A 742     -53.910 -13.168-105.915  1.00 93.49           C  
ANISOU 5517  C   THR A 742    11469  11761  12293   -529   -910    807       C  
ATOM   5518  O   THR A 742     -53.842 -13.143-107.147  1.00 96.71           O  
ANISOU 5518  O   THR A 742    11894  12188  12664   -538   -910    839       O  
ATOM   5519  CB  THR A 742     -51.711 -13.525-104.724  1.00 96.72           C  
ANISOU 5519  CB  THR A 742    11792  12282  12672   -585   -863    770       C  
ATOM   5520  OG1 THR A 742     -50.808 -12.941-103.778  1.00100.56           O  
ANISOU 5520  OG1 THR A 742    12258  12782  13167   -634   -848    757       O  
ATOM   5521  CG2 THR A 742     -50.921 -13.941-105.967  1.00 96.83           C  
ANISOU 5521  CG2 THR A 742    11783  12384  12622   -600   -844    787       C  
ATOM   5522  N   ILE A 743     -54.917 -13.737-105.246  1.00 90.50           N  
ANISOU 5522  N   ILE A 743    11085  11351  11950   -473   -925    775       N  
ATOM   5523  CA  ILE A 743     -56.070 -14.335-105.935  1.00 88.82           C  
ANISOU 5523  CA  ILE A 743    10886  11119  11739   -419   -946    775       C  
ATOM   5524  C   ILE A 743     -56.839 -13.287-106.728  1.00 88.04           C  
ANISOU 5524  C   ILE A 743    10843  10957  11649   -421   -974    806       C  
ATOM   5525  O   ILE A 743     -57.060 -13.457-107.927  1.00 88.44           O  
ANISOU 5525  O   ILE A 743    10914  11016  11673   -409   -981    831       O  
ATOM   5526  CB  ILE A 743     -57.036 -15.051-104.967  1.00 87.33           C  
ANISOU 5526  CB  ILE A 743    10680  10915  11583   -375   -957    734       C  
ATOM   5527  CG1 ILE A 743     -56.335 -16.231-104.294  1.00 85.77           C  
ANISOU 5527  CG1 ILE A 743    10446  10773  11369   -368   -940    706       C  
ATOM   5528  CG2 ILE A 743     -58.292 -15.516-105.700  1.00 85.53           C  
ANISOU 5528  CG2 ILE A 743    10468  10671  11358   -329   -980    734       C  
ATOM   5529  CD1 ILE A 743     -57.072 -16.770-103.093  1.00 85.75           C  
ANISOU 5529  CD1 ILE A 743    10432  10755  11393   -349   -948    669       C  
ATOM   5530  N   VAL A 744     -57.231 -12.209-106.050  1.00 86.98           N  
ANISOU 5530  N   VAL A 744    10738  10759  11551   -431   -994    799       N  
ATOM   5531  CA  VAL A 744     -57.976 -11.109-106.670  1.00 87.90           C  
ANISOU 5531  CA  VAL A 744    10919  10801  11676   -424  -1034    821       C  
ATOM   5532  C   VAL A 744     -57.207 -10.538-107.868  1.00 88.02           C  
ANISOU 5532  C   VAL A 744    10979  10819  11646   -479  -1032    877       C  
ATOM   5533  O   VAL A 744     -57.784 -10.324-108.940  1.00 87.80           O  
ANISOU 5533  O   VAL A 744    10995  10762  11601   -462  -1058    902       O  
ATOM   5534  CB  VAL A 744     -58.324 -10.008-105.635  1.00 87.79           C  
ANISOU 5534  CB  VAL A 744    10931  10720  11703   -424  -1062    799       C  
ATOM   5535  CG1 VAL A 744     -59.218  -8.934-106.241  1.00 87.05           C  
ANISOU 5535  CG1 VAL A 744    10911  10543  11617   -398  -1118    810       C  
ATOM   5536  CG2 VAL A 744     -59.001 -10.628-104.422  1.00 87.21           C  
ANISOU 5536  CG2 VAL A 744    10805  10664  11664   -379  -1056    743       C  
ATOM   5537  N   ALA A 745     -55.906 -10.324-107.683  1.00 87.89           N  
ANISOU 5537  N   ALA A 745    10945  10842  11604   -549  -1002    894       N  
ATOM   5538  CA  ALA A 745     -55.025  -9.888-108.761  1.00 90.93           C  
ANISOU 5538  CA  ALA A 745    11359  11255  11933   -619   -990    946       C  
ATOM   5539  C   ALA A 745     -55.064 -10.853-109.943  1.00 92.51           C  
ANISOU 5539  C   ALA A 745    11537  11518  12091   -592   -975    958       C  
ATOM   5540  O   ALA A 745     -55.067 -10.421-111.100  1.00 93.77           O  
ANISOU 5540  O   ALA A 745    11745  11668  12212   -619   -987   1001       O  
ATOM   5541  CB  ALA A 745     -53.602  -9.740-108.251  1.00 91.89           C  
ANISOU 5541  CB  ALA A 745    11441  11439  12032   -696   -953    948       C  
ATOM   5542  N   ALA A 746     -55.097 -12.151-109.634  1.00 93.08           N  
ANISOU 5542  N   ALA A 746    11545  11650  12168   -538   -955    920       N  
ATOM   5543  CA  ALA A 746     -55.142 -13.220-110.635  1.00 93.73           C  
ANISOU 5543  CA  ALA A 746    11604  11793  12213   -499   -946    921       C  
ATOM   5544  C   ALA A 746     -56.456 -13.227-111.406  1.00 93.52           C  
ANISOU 5544  C   ALA A 746    11622  11709  12200   -446   -982    931       C  
ATOM   5545  O   ALA A 746     -56.466 -13.449-112.616  1.00 94.05           O  
ANISOU 5545  O   ALA A 746    11705  11801  12226   -441   -984    957       O  
ATOM   5546  CB  ALA A 746     -54.909 -14.578-109.982  1.00 93.36           C  
ANISOU 5546  CB  ALA A 746    11493  11807  12170   -453   -929    874       C  
ATOM   5547  N   VAL A 747     -57.559 -12.988-110.702  1.00 92.81           N  
ANISOU 5547  N   VAL A 747    11549  11551  12164   -405  -1011    906       N  
ATOM   5548  CA  VAL A 747     -58.864 -12.910-111.345  1.00 93.72           C  
ANISOU 5548  CA  VAL A 747    11701  11614  12292   -351  -1049    907       C  
ATOM   5549  C   VAL A 747     -58.907 -11.703-112.275  1.00 98.31           C  
ANISOU 5549  C   VAL A 747    12359  12139  12852   -382  -1078    953       C  
ATOM   5550  O   VAL A 747     -59.511 -11.773-113.347  1.00102.69           O  
ANISOU 5550  O   VAL A 747    12948  12681  13388   -352  -1100    971       O  
ATOM   5551  CB  VAL A 747     -60.024 -12.877-110.328  1.00 91.97           C  
ANISOU 5551  CB  VAL A 747    11469  11349  12126   -302  -1074    861       C  
ATOM   5552  CG1 VAL A 747     -61.353 -12.638-111.027  1.00 91.87           C  
ANISOU 5552  CG1 VAL A 747    11491  11289  12124   -246  -1118    856       C  
ATOM   5553  CG2 VAL A 747     -60.088 -14.191-109.566  1.00 92.05           C  
ANISOU 5553  CG2 VAL A 747    11414  11412  12146   -278  -1051    821       C  
ATOM   5554  N   GLU A 748     -58.253 -10.610-111.880  1.00100.79           N  
ANISOU 5554  N   GLU A 748    12709  12419  13165   -445  -1080    975       N  
ATOM   5555  CA  GLU A 748     -58.152  -9.435-112.749  1.00102.38           C  
ANISOU 5555  CA  GLU A 748    13000  12562  13336   -492  -1111   1026       C  
ATOM   5556  C   GLU A 748     -57.339  -9.739-113.998  1.00102.22           C  
ANISOU 5556  C   GLU A 748    12982  12609  13247   -541  -1083   1072       C  
ATOM   5557  O   GLU A 748     -57.778  -9.444-115.107  1.00103.14           O  
ANISOU 5557  O   GLU A 748    13157  12695  13334   -534  -1111   1104       O  
ATOM   5558  CB  GLU A 748     -57.572  -8.223-112.020  1.00104.91           C  
ANISOU 5558  CB  GLU A 748    13365  12829  13666   -559  -1124   1040       C  
ATOM   5559  CG  GLU A 748     -57.602  -6.961-112.872  1.00107.56           C  
ANISOU 5559  CG  GLU A 748    13815  13084  13969   -608  -1172   1094       C  
ATOM   5560  CD  GLU A 748     -57.236  -5.702-112.113  1.00110.31           C  
ANISOU 5560  CD  GLU A 748    14225  13356  14330   -666  -1202   1104       C  
ATOM   5561  OE1 GLU A 748     -57.486  -5.631-110.892  1.00110.60           O  
ANISOU 5561  OE1 GLU A 748    14231  13371  14420   -631  -1207   1057       O  
ATOM   5562  OE2 GLU A 748     -56.702  -4.770-112.749  1.00114.28           O  
ANISOU 5562  OE2 GLU A 748    14814  13819  14787   -751  -1224   1160       O  
ATOM   5563  N   GLU A 749     -56.164 -10.334-113.812  1.00102.67           N  
ANISOU 5563  N   GLU A 749    12971  12764  13275   -586  -1030   1069       N  
ATOM   5564  CA  GLU A 749     -55.327 -10.745-114.934  1.00104.27           C  
ANISOU 5564  CA  GLU A 749    13156  13057  13405   -627   -998   1100       C  
ATOM   5565  C   GLU A 749     -56.024 -11.745-115.841  1.00103.21           C  
ANISOU 5565  C   GLU A 749    13006  12948  13258   -549  -1005   1091       C  
ATOM   5566  O   GLU A 749     -55.677 -11.867-117.013  1.00105.34           O  
ANISOU 5566  O   GLU A 749    13287  13267  13468   -572   -996   1122       O  
ATOM   5567  CB  GLU A 749     -53.998 -11.322-114.451  1.00107.17           C  
ANISOU 5567  CB  GLU A 749    13437  13536  13745   -668   -945   1080       C  
ATOM   5568  CG  GLU A 749     -52.852 -10.319-114.439  1.00112.53           C  
ANISOU 5568  CG  GLU A 749    14133  14241  14381   -787   -925   1117       C  
ATOM   5569  CD  GLU A 749     -52.451  -9.831-115.825  1.00114.30           C  
ANISOU 5569  CD  GLU A 749    14402  14497  14527   -860   -922   1175       C  
ATOM   5570  OE1 GLU A 749     -52.771 -10.508-116.828  1.00114.72           O  
ANISOU 5570  OE1 GLU A 749    14449  14589  14549   -813   -920   1179       O  
ATOM   5571  OE2 GLU A 749     -51.805  -8.765-115.912  1.00116.33           O  
ANISOU 5571  OE2 GLU A 749    14706  14742  14749   -969   -921   1217       O  
ATOM   5572  N   GLY A 750     -56.999 -12.463-115.290  1.00100.95           N  
ANISOU 5572  N   GLY A 750    12695  12634  13025   -464  -1022   1046       N  
ATOM   5573  CA  GLY A 750     -57.810 -13.395-116.064  1.00 98.64           C  
ANISOU 5573  CA  GLY A 750    12395  12355  12728   -390  -1037   1034       C  
ATOM   5574  C   GLY A 750     -58.779 -12.638-116.942  1.00 98.07           C  
ANISOU 5574  C   GLY A 750    12402  12203  12655   -372  -1083   1063       C  
ATOM   5575  O   GLY A 750     -58.885 -12.906-118.135  1.00 98.11           O  
ANISOU 5575  O   GLY A 750    12427  12230  12617   -359  -1088   1087       O  
ATOM   5576  N   ARG A 751     -59.477 -11.683-116.336  1.00 99.50           N  
ANISOU 5576  N   ARG A 751    12631  12293  12881   -364  -1120   1057       N  
ATOM   5577  CA  ARG A 751     -60.422 -10.826-117.040  1.00101.17           C  
ANISOU 5577  CA  ARG A 751    12928  12418  13094   -338  -1177   1077       C  
ATOM   5578  C   ARG A 751     -59.715  -9.930-118.040  1.00102.76           C  
ANISOU 5578  C   ARG A 751    13207  12604  13233   -416  -1183   1142       C  
ATOM   5579  O   ARG A 751     -60.219  -9.707-119.141  1.00105.45           O  
ANISOU 5579  O   ARG A 751    13608  12913  13545   -397  -1216   1170       O  
ATOM   5580  CB  ARG A 751     -61.190  -9.959-116.053  1.00101.37           C  
ANISOU 5580  CB  ARG A 751    12984  12356  13175   -310  -1220   1047       C  
ATOM   5581  CG  ARG A 751     -62.121 -10.724-115.135  1.00101.61           C  
ANISOU 5581  CG  ARG A 751    12946  12399  13260   -236  -1221    981       C  
ATOM   5582  CD  ARG A 751     -63.144  -9.762-114.573  1.00104.25           C  
ANISOU 5582  CD  ARG A 751    13322  12649  13636   -189  -1279    949       C  
ATOM   5583  NE  ARG A 751     -64.020 -10.385-113.591  1.00104.69           N  
ANISOU 5583  NE  ARG A 751    13307  12729  13739   -130  -1277    883       N  
ATOM   5584  CZ  ARG A 751     -64.891  -9.719-112.839  1.00105.69           C  
ANISOU 5584  CZ  ARG A 751    13441  12810  13903    -83  -1318    837       C  
ATOM   5585  NH1 ARG A 751     -65.005  -8.400-112.945  1.00104.22           N  
ANISOU 5585  NH1 ARG A 751    13341  12540  13718    -79  -1373    847       N  
ATOM   5586  NH2 ARG A 751     -65.644 -10.374-111.970  1.00109.00           N  
ANISOU 5586  NH2 ARG A 751    13787  13271  14355    -42  -1309    778       N  
ATOM   5587  N   ALA A 752     -58.550  -9.420-117.644  1.00103.23           N  
ANISOU 5587  N   ALA A 752    13265  12688  13270   -507  -1153   1167       N  
ATOM   5588  CA  ALA A 752     -57.721  -8.585-118.503  1.00104.95           C  
ANISOU 5588  CA  ALA A 752    13551  12906  13418   -607  -1152   1232       C  
ATOM   5589  C   ALA A 752     -57.236  -9.339-119.739  1.00106.76           C  
ANISOU 5589  C   ALA A 752    13752  13234  13579   -621  -1117   1257       C  
ATOM   5590  O   ALA A 752     -57.100  -8.743-120.808  1.00110.52           O  
ANISOU 5590  O   ALA A 752    14302  13694  13995   -673  -1134   1311       O  
ATOM   5591  CB  ALA A 752     -56.540  -8.028-117.726  1.00105.35           C  
ANISOU 5591  CB  ALA A 752    13586  12982  13457   -707  -1120   1245       C  
ATOM   5592  N   ILE A 753     -56.977 -10.640-119.591  1.00106.12           N  
ANISOU 5592  N   ILE A 753    13568  13250  13500   -575  -1074   1217       N  
ATOM   5593  CA  ILE A 753     -56.576 -11.477-120.725  1.00105.04           C  
ANISOU 5593  CA  ILE A 753    13397  13212  13300   -569  -1046   1228       C  
ATOM   5594  C   ILE A 753     -57.735 -11.632-121.696  1.00105.28           C  
ANISOU 5594  C   ILE A 753    13480  13189  13332   -496  -1090   1236       C  
ATOM   5595  O   ILE A 753     -57.580 -11.344-122.879  1.00108.84           O  
ANISOU 5595  O   ILE A 753    13979  13653  13719   -529  -1096   1281       O  
ATOM   5596  CB  ILE A 753     -56.001 -12.857-120.306  1.00103.92           C  
ANISOU 5596  CB  ILE A 753    13142  13182  13158   -527  -1002   1177       C  
ATOM   5597  CG1 ILE A 753     -54.601 -12.710-119.706  1.00103.51           C  
ANISOU 5597  CG1 ILE A 753    13035  13216  13077   -608   -954   1174       C  
ATOM   5598  CG2 ILE A 753     -55.907 -13.797-121.497  1.00103.13           C  
ANISOU 5598  CG2 ILE A 753    13015  13166  13003   -487   -991   1176       C  
ATOM   5599  CD1 ILE A 753     -53.704 -11.759-120.472  1.00107.53           C  
ANISOU 5599  CD1 ILE A 753    13582  13763  13509   -725   -936   1232       C  
ATOM   5600  N   TYR A 754     -58.894 -12.056-121.194  1.00105.84           N  
ANISOU 5600  N   TYR A 754    13540  13202  13470   -403  -1122   1193       N  
ATOM   5601  CA  TYR A 754     -60.058 -12.294-122.050  1.00109.06           C  
ANISOU 5601  CA  TYR A 754    13987  13567  13884   -327  -1165   1190       C  
ATOM   5602  C   TYR A 754     -60.423 -11.087-122.911  1.00111.97           C  
ANISOU 5602  C   TYR A 754    14469  13851  14222   -355  -1213   1241       C  
ATOM   5603  O   TYR A 754     -60.774 -11.247-124.081  1.00114.48           O  
ANISOU 5603  O   TYR A 754    14823  14172  14500   -331  -1232   1262       O  
ATOM   5604  CB  TYR A 754     -61.274 -12.754-121.245  1.00109.90           C  
ANISOU 5604  CB  TYR A 754    14064  13626  14066   -238  -1194   1133       C  
ATOM   5605  CG  TYR A 754     -62.464 -13.093-122.116  1.00110.77           C  
ANISOU 5605  CG  TYR A 754    14200  13706  14180   -159  -1236   1123       C  
ATOM   5606  CD1 TYR A 754     -62.598 -14.356-122.681  1.00110.11           C  
ANISOU 5606  CD1 TYR A 754    14066  13689  14080   -113  -1222   1104       C  
ATOM   5607  CD2 TYR A 754     -63.451 -12.143-122.387  1.00112.63           C  
ANISOU 5607  CD2 TYR A 754    14514  13847  14433   -127  -1297   1127       C  
ATOM   5608  CE1 TYR A 754     -63.683 -14.666-123.485  1.00112.52           C  
ANISOU 5608  CE1 TYR A 754    14393  13968  14388    -44  -1262   1094       C  
ATOM   5609  CE2 TYR A 754     -64.538 -12.444-123.194  1.00112.48           C  
ANISOU 5609  CE2 TYR A 754    14515  13806  14416    -52  -1339   1113       C  
ATOM   5610  CZ  TYR A 754     -64.651 -13.708-123.738  1.00112.09           C  
ANISOU 5610  CZ  TYR A 754    14410  13827  14352    -14  -1318   1098       C  
ATOM   5611  OH  TYR A 754     -65.727 -14.022-124.538  1.00112.48           O  
ANISOU 5611  OH  TYR A 754    14477  13857  14403     56  -1360   1083       O  
ATOM   5612  N   ASN A 755     -60.348  -9.890-122.333  1.00113.07           N  
ANISOU 5612  N   ASN A 755    14672  13910  14377   -403  -1239   1258       N  
ATOM   5613  CA  ASN A 755     -60.518  -8.664-123.108  1.00114.43           C  
ANISOU 5613  CA  ASN A 755    14972  13995  14511   -445  -1292   1312       C  
ATOM   5614  C   ASN A 755     -59.486  -8.513-124.216  1.00114.84           C  
ANISOU 5614  C   ASN A 755    15054  14112  14468   -543  -1261   1377       C  
ATOM   5615  O   ASN A 755     -59.832  -8.183-125.346  1.00116.91           O  
ANISOU 5615  O   ASN A 755    15395  14340  14683   -543  -1296   1415       O  
ATOM   5616  CB  ASN A 755     -60.509  -7.431-122.208  1.00114.79           C  
ANISOU 5616  CB  ASN A 755    15085  13942  14586   -484  -1330   1318       C  
ATOM   5617  CG  ASN A 755     -61.875  -6.793-122.090  1.00116.08           C  
ANISOU 5617  CG  ASN A 755    15323  13985  14796   -393  -1414   1289       C  
ATOM   5618  OD1 ASN A 755     -61.992  -5.571-122.029  1.00117.29           O  
ANISOU 5618  OD1 ASN A 755    15587  14035  14943   -421  -1474   1313       O  
ATOM   5619  ND2 ASN A 755     -62.921  -7.618-122.070  1.00115.22           N  
ANISOU 5619  ND2 ASN A 755    15156  13891  14730   -283  -1425   1235       N  
ATOM   5620  N   ASN A 756     -58.226  -8.771-123.888  1.00114.61           N  
ANISOU 5620  N   ASN A 756    14956  14182  14407   -625  -1196   1385       N  
ATOM   5621  CA  ASN A 756     -57.144  -8.641-124.852  1.00117.10           C  
ANISOU 5621  CA  ASN A 756    15281  14586  14625   -728  -1158   1439       C  
ATOM   5622  C   ASN A 756     -57.222  -9.671-125.975  1.00116.69           C  
ANISOU 5622  C   ASN A 756    15184  14624  14527   -678  -1136   1435       C  
ATOM   5623  O   ASN A 756     -56.667  -9.461-127.050  1.00120.30           O  
ANISOU 5623  O   ASN A 756    15674  15136  14897   -747  -1122   1483       O  
ATOM   5624  CB  ASN A 756     -55.788  -8.709-124.149  1.00120.32           C  
ANISOU 5624  CB  ASN A 756    15610  15095  15011   -820  -1094   1435       C  
ATOM   5625  CG  ASN A 756     -54.650  -8.218-125.023  1.00122.50           C  
ANISOU 5625  CG  ASN A 756    15909  15455  15179   -957  -1060   1496       C  
ATOM   5626  OD1 ASN A 756     -54.855  -7.442-125.957  1.00124.62           O  
ANISOU 5626  OD1 ASN A 756    16288  15668  15394  -1010  -1096   1555       O  
ATOM   5627  ND2 ASN A 756     -53.440  -8.669-124.722  1.00123.23           N  
ANISOU 5627  ND2 ASN A 756    15899  15687  15234  -1016   -994   1479       N  
ATOM   5628  N   MET A 757     -57.907 -10.781-125.721  1.00115.46           N  
ANISOU 5628  N   MET A 757    14957  14485  14425   -562  -1136   1376       N  
ATOM   5629  CA  MET A 757     -58.179 -11.765-126.762  1.00117.95           C  
ANISOU 5629  CA  MET A 757    15241  14864  14707   -497  -1130   1366       C  
ATOM   5630  C   MET A 757     -59.165 -11.165-127.754  1.00118.63           C  
ANISOU 5630  C   MET A 757    15437  14855  14779   -469  -1192   1401       C  
ATOM   5631  O   MET A 757     -58.886 -11.085-128.947  1.00121.90           O  
ANISOU 5631  O   MET A 757    15889  15309  15116   -503  -1189   1443       O  
ATOM   5632  CB  MET A 757     -58.779 -13.042-126.174  1.00121.31           C  
ANISOU 5632  CB  MET A 757    15581  15312  15198   -386  -1127   1297       C  
ATOM   5633  CG  MET A 757     -57.954 -13.721-125.094  1.00125.48           C  
ANISOU 5633  CG  MET A 757    16010  15918  15748   -395  -1079   1255       C  
ATOM   5634  SD  MET A 757     -56.689 -14.824-125.739  1.00130.51           S  
ANISOU 5634  SD  MET A 757    16555  16728  16303   -405  -1022   1240       S  
ATOM   5635  CE  MET A 757     -56.522 -15.974-124.375  1.00128.29           C  
ANISOU 5635  CE  MET A 757    16176  16482  16084   -342  -1005   1165       C  
ATOM   5636  N   LYS A 758     -60.310 -10.724-127.236  1.00117.11           N  
ANISOU 5636  N   LYS A 758    15294  14542  14658   -404  -1250   1380       N  
ATOM   5637  CA  LYS A 758     -61.395 -10.162-128.043  1.00116.49           C  
ANISOU 5637  CA  LYS A 758    15319  14364  14577   -354  -1320   1398       C  
ATOM   5638  C   LYS A 758     -60.999  -8.869-128.756  1.00119.55           C  
ANISOU 5638  C   LYS A 758    15835  14692  14895   -451  -1351   1472       C  
ATOM   5639  O   LYS A 758     -61.605  -8.505-129.763  1.00123.06           O  
ANISOU 5639  O   LYS A 758    16370  15079  15305   -428  -1402   1500       O  
ATOM   5640  CB  LYS A 758     -62.623  -9.923-127.166  1.00113.79           C  
ANISOU 5640  CB  LYS A 758    14989  13921  14325   -265  -1375   1346       C  
ATOM   5641  CG  LYS A 758     -63.136 -11.173-126.470  1.00111.03           C  
ANISOU 5641  CG  LYS A 758    14523  13623  14039   -180  -1352   1276       C  
ATOM   5642  CD  LYS A 758     -64.442 -11.654-127.066  1.00109.79           C  
ANISOU 5642  CD  LYS A 758    14373  13437  13904    -74  -1399   1244       C  
ATOM   5643  CE  LYS A 758     -65.607 -10.886-126.471  1.00109.69           C  
ANISOU 5643  CE  LYS A 758    14404  13320  13950    -13  -1466   1209       C  
ATOM   5644  NZ  LYS A 758     -66.904 -11.430-126.946  1.00112.03           N  
ANISOU 5644  NZ  LYS A 758    14688  13604  14271     90  -1509   1166       N  
ATOM   5645  N   GLN A 759     -59.995  -8.177-128.222  1.00120.87           N  
ANISOU 5645  N   GLN A 759    16016  14870  15039   -564  -1324   1504       N  
ATOM   5646  CA  GLN A 759     -59.422  -6.999-128.869  1.00120.27           C  
ANISOU 5646  CA  GLN A 759    16062  14751  14883   -685  -1346   1581       C  
ATOM   5647  C   GLN A 759     -58.773  -7.400-130.186  1.00120.75           C  
ANISOU 5647  C   GLN A 759    16116  14920  14843   -741  -1307   1625       C  
ATOM   5648  O   GLN A 759     -59.109  -6.866-131.238  1.00119.93           O  
ANISOU 5648  O   GLN A 759    16122  14763  14682   -759  -1352   1673       O  
ATOM   5649  CB  GLN A 759     -58.391  -6.327-127.959  1.00120.97           C  
ANISOU 5649  CB  GLN A 759    16146  14850  14966   -802  -1316   1600       C  
ATOM   5650  CG  GLN A 759     -58.985  -5.493-126.835  1.00121.47           C  
ANISOU 5650  CG  GLN A 759    16266  14779  15107   -772  -1374   1577       C  
ATOM   5651  CD  GLN A 759     -57.926  -4.825-125.978  1.00122.90           C  
ANISOU 5651  CD  GLN A 759    16446  14970  15278   -893  -1346   1598       C  
ATOM   5652  OE1 GLN A 759     -56.797  -4.612-126.419  1.00125.11           O  
ANISOU 5652  OE1 GLN A 759    16727  15330  15477  -1024  -1302   1649       O  
ATOM   5653  NE2 GLN A 759     -58.288  -4.486-124.748  1.00122.71           N  
ANISOU 5653  NE2 GLN A 759    16417  14873  15334   -852  -1372   1556       N  
ATOM   5654  N   PHE A 760     -57.850  -8.355-130.112  1.00122.30           N  
ANISOU 5654  N   PHE A 760    16182  15270  15014   -764  -1226   1603       N  
ATOM   5655  CA  PHE A 760     -57.185  -8.889-131.292  1.00125.31           C  
ANISOU 5655  CA  PHE A 760    16531  15781  15298   -804  -1182   1629       C  
ATOM   5656  C   PHE A 760     -58.160  -9.652-132.190  1.00124.07           C  
ANISOU 5656  C   PHE A 760    16376  15614  15148   -683  -1212   1608       C  
ATOM   5657  O   PHE A 760     -58.044  -9.601-133.412  1.00125.98           O  
ANISOU 5657  O   PHE A 760    16665  15894  15307   -712  -1214   1648       O  
ATOM   5658  CB  PHE A 760     -55.989  -9.771-130.897  1.00128.14           C  
ANISOU 5658  CB  PHE A 760    16741  16312  15632   -836  -1097   1594       C  
ATOM   5659  CG  PHE A 760     -55.540 -10.698-131.987  1.00134.21           C  
ANISOU 5659  CG  PHE A 760    17444  17226  16322   -819  -1057   1587       C  
ATOM   5660  CD1 PHE A 760     -54.893 -10.207-133.118  1.00139.33           C  
ANISOU 5660  CD1 PHE A 760    18140  17943  16854   -928  -1039   1648       C  
ATOM   5661  CD2 PHE A 760     -55.787 -12.060-131.899  1.00136.99           C  
ANISOU 5661  CD2 PHE A 760    17692  17644  16712   -696  -1040   1519       C  
ATOM   5662  CE1 PHE A 760     -54.497 -11.058-134.139  1.00142.36           C  
ANISOU 5662  CE1 PHE A 760    18459  18469  17160   -906  -1003   1637       C  
ATOM   5663  CE2 PHE A 760     -55.391 -12.918-132.914  1.00141.29           C  
ANISOU 5663  CE2 PHE A 760    18180  18319  17182   -670  -1011   1507       C  
ATOM   5664  CZ  PHE A 760     -54.745 -12.417-134.036  1.00142.54           C  
ANISOU 5664  CZ  PHE A 760    18377  18554  17225   -771   -991   1563       C  
ATOM   5665  N   ILE A 761     -59.113 -10.355-131.585  1.00122.69           N  
ANISOU 5665  N   ILE A 761    16153  15395  15068   -553  -1235   1544       N  
ATOM   5666  CA  ILE A 761     -60.110 -11.106-132.343  1.00122.73           C  
ANISOU 5666  CA  ILE A 761    16156  15387  15086   -437  -1267   1518       C  
ATOM   5667  C   ILE A 761     -60.977 -10.173-133.194  1.00128.98           C  
ANISOU 5667  C   ILE A 761    17091  16058  15857   -428  -1342   1562       C  
ATOM   5668  O   ILE A 761     -61.229 -10.466-134.363  1.00133.02           O  
ANISOU 5668  O   ILE A 761    17632  16594  16316   -400  -1355   1579       O  
ATOM   5669  CB  ILE A 761     -60.954 -12.029-131.435  1.00119.88           C  
ANISOU 5669  CB  ILE A 761    15714  15007  14829   -317  -1276   1441       C  
ATOM   5670  CG1 ILE A 761     -60.117 -13.242-131.016  1.00121.03           C  
ANISOU 5670  CG1 ILE A 761    15727  15286  14971   -308  -1209   1399       C  
ATOM   5671  CG2 ILE A 761     -62.216 -12.511-132.140  1.00116.97           C  
ANISOU 5671  CG2 ILE A 761    15370  14591  14483   -204  -1328   1418       C  
ATOM   5672  CD1 ILE A 761     -60.589 -13.923-129.746  1.00123.37           C  
ANISOU 5672  CD1 ILE A 761    15950  15562  15362   -238  -1208   1334       C  
ATOM   5673  N   ARG A 762     -61.405  -9.044-132.627  1.00133.75           N  
ANISOU 5673  N   ARG A 762    17789  16531  16496   -447  -1397   1577       N  
ATOM   5674  CA  ARG A 762     -62.184  -8.061-133.388  1.00135.82           C  
ANISOU 5674  CA  ARG A 762    18204  16668  16733   -436  -1481   1616       C  
ATOM   5675  C   ARG A 762     -61.383  -7.573-134.588  1.00139.73           C  
ANISOU 5675  C   ARG A 762    18780  17202  17108   -552  -1469   1697       C  
ATOM   5676  O   ARG A 762     -61.868  -7.606-135.718  1.00145.84           O  
ANISOU 5676  O   ARG A 762    19618  17958  17834   -519  -1504   1719       O  
ATOM   5677  CB  ARG A 762     -62.604  -6.868-132.524  1.00135.78           C  
ANISOU 5677  CB  ARG A 762    18292  16520  16776   -445  -1546   1617       C  
ATOM   5678  CG  ARG A 762     -63.737  -6.054-133.137  1.00138.29           C  
ANISOU 5678  CG  ARG A 762    18755  16696  17093   -379  -1652   1627       C  
ATOM   5679  CD  ARG A 762     -63.838  -4.626-132.622  1.00141.35           C  
ANISOU 5679  CD  ARG A 762    19279  16940  17485   -423  -1726   1653       C  
ATOM   5680  NE  ARG A 762     -63.500  -4.498-131.207  1.00143.03           N  
ANISOU 5680  NE  ARG A 762    19426  17153  17764   -442  -1699   1618       N  
ATOM   5681  CZ  ARG A 762     -62.501  -3.754-130.740  1.00145.96           C  
ANISOU 5681  CZ  ARG A 762    19837  17515  18104   -572  -1680   1664       C  
ATOM   5682  NH1 ARG A 762     -61.743  -3.051-131.572  1.00149.69           N  
ANISOU 5682  NH1 ARG A 762    20420  17979  18477   -703  -1685   1748       N  
ATOM   5683  NH2 ARG A 762     -62.263  -3.702-129.439  1.00145.58           N  
ANISOU 5683  NH2 ARG A 762    19724  17468  18121   -576  -1656   1626       N  
ATOM   5684  N   TYR A 763     -60.149  -7.146-134.329  1.00141.35           N  
ANISOU 5684  N   TYR A 763    18978  17469  17260   -692  -1418   1739       N  
ATOM   5685  CA  TYR A 763     -59.265  -6.608-135.359  1.00143.18           C  
ANISOU 5685  CA  TYR A 763    19281  17753  17365   -831  -1399   1819       C  
ATOM   5686  C   TYR A 763     -58.975  -7.593-136.492  1.00143.55           C  
ANISOU 5686  C   TYR A 763    19258  17941  17342   -812  -1351   1818       C  
ATOM   5687  O   TYR A 763     -58.940  -7.200-137.655  1.00151.15           O  
ANISOU 5687  O   TYR A 763    20314  18901  18214   -864  -1372   1876       O  
ATOM   5688  CB  TYR A 763     -57.962  -6.117-134.729  1.00144.68           C  
ANISOU 5688  CB  TYR A 763    19444  18010  17516   -985  -1343   1849       C  
ATOM   5689  CG  TYR A 763     -56.953  -5.581-135.714  1.00148.80           C  
ANISOU 5689  CG  TYR A 763    20025  18611  17901  -1150  -1313   1930       C  
ATOM   5690  CD1 TYR A 763     -57.143  -4.346-136.334  1.00152.16           C  
ANISOU 5690  CD1 TYR A 763    20638  18914  18262  -1240  -1384   2008       C  
ATOM   5691  CD2 TYR A 763     -55.800  -6.303-136.018  1.00149.27           C  
ANISOU 5691  CD2 TYR A 763    19956  18871  17888  -1220  -1219   1925       C  
ATOM   5692  CE1 TYR A 763     -56.217  -3.851-137.237  1.00156.80           C  
ANISOU 5692  CE1 TYR A 763    21284  19579  18714  -1408  -1356   2086       C  
ATOM   5693  CE2 TYR A 763     -54.867  -5.815-136.917  1.00154.42           C  
ANISOU 5693  CE2 TYR A 763    20651  19614  18404  -1380  -1187   1996       C  
ATOM   5694  CZ  TYR A 763     -55.080  -4.590-137.523  1.00158.13           C  
ANISOU 5694  CZ  TYR A 763    21310  19962  18810  -1481  -1254   2079       C  
ATOM   5695  OH  TYR A 763     -54.156  -4.101-138.418  1.00163.35           O  
ANISOU 5695  OH  TYR A 763    22018  20718  19328  -1656  -1222   2154       O  
ATOM   5696  N   LEU A 764     -58.773  -8.865-136.153  1.00140.83           N  
ANISOU 5696  N   LEU A 764    18757  17716  17036   -737  -1291   1753       N  
ATOM   5697  CA  LEU A 764     -58.515  -9.891-137.161  1.00138.73           C  
ANISOU 5697  CA  LEU A 764    18417  17584  16708   -702  -1251   1740       C  
ATOM   5698  C   LEU A 764     -59.759 -10.190-137.985  1.00137.37           C  
ANISOU 5698  C   LEU A 764    18302  17335  16555   -580  -1314   1729       C  
ATOM   5699  O   LEU A 764     -59.680 -10.299-139.205  1.00140.16           O  
ANISOU 5699  O   LEU A 764    18691  17737  16824   -594  -1315   1762       O  
ATOM   5700  CB  LEU A 764     -57.998 -11.184-136.523  1.00138.60           C  
ANISOU 5700  CB  LEU A 764    18229  17701  16728   -643  -1185   1667       C  
ATOM   5701  CG  LEU A 764     -57.516 -12.277-137.485  1.00138.01           C  
ANISOU 5701  CG  LEU A 764    18069  17787  16582   -610  -1141   1646       C  
ATOM   5702  CD1 LEU A 764     -56.018 -12.166-137.725  1.00139.69           C  
ANISOU 5702  CD1 LEU A 764    18222  18165  16687   -741  -1068   1670       C  
ATOM   5703  CD2 LEU A 764     -57.865 -13.658-136.956  1.00137.18           C  
ANISOU 5703  CD2 LEU A 764    17846  17721  16552   -473  -1132   1561       C  
ATOM   5704  N   ILE A 765     -60.902 -10.318-137.319  1.00136.58           N  
ANISOU 5704  N   ILE A 765    18207  17122  16563   -464  -1366   1681       N  
ATOM   5705  CA  ILE A 765     -62.136 -10.715-138.001  1.00141.72           C  
ANISOU 5705  CA  ILE A 765    18892  17711  17242   -338  -1425   1656       C  
ATOM   5706  C   ILE A 765     -62.736  -9.596-138.857  1.00144.76           C  
ANISOU 5706  C   ILE A 765    19446  17973  17581   -358  -1504   1714       C  
ATOM   5707  O   ILE A 765     -63.247  -9.864-139.946  1.00150.64           O  
ANISOU 5707  O   ILE A 765    20230  18717  18286   -304  -1533   1722       O  
ATOM   5708  CB  ILE A 765     -63.190 -11.310-137.031  1.00140.67           C  
ANISOU 5708  CB  ILE A 765    18695  17520  17233   -209  -1453   1578       C  
ATOM   5709  CG1 ILE A 765     -62.611 -12.505-136.254  1.00141.87           C  
ANISOU 5709  CG1 ILE A 765    18694  17789  17422   -188  -1383   1522       C  
ATOM   5710  CG2 ILE A 765     -64.457 -11.724-137.775  1.00139.34           C  
ANISOU 5710  CG2 ILE A 765    18555  17299  17086    -87  -1514   1549       C  
ATOM   5711  CD1 ILE A 765     -61.908 -13.561-137.092  1.00142.86           C  
ANISOU 5711  CD1 ILE A 765    18742  18060  17478   -184  -1331   1516       C  
ATOM   5712  N   SER A 766     -62.665  -8.354-138.381  1.00141.20           N  
ANISOU 5712  N   SER A 766    19102  17416  17132   -431  -1543   1752       N  
ATOM   5713  CA  SER A 766     -63.184  -7.221-139.149  1.00139.10           C  
ANISOU 5713  CA  SER A 766    19015  17019  16816   -454  -1629   1809       C  
ATOM   5714  C   SER A 766     -62.344  -6.954-140.401  1.00139.44           C  
ANISOU 5714  C   SER A 766    19125  17132  16723   -575  -1604   1889       C  
ATOM   5715  O   SER A 766     -62.895  -6.671-141.467  1.00140.45           O  
ANISOU 5715  O   SER A 766    19361  17204  16799   -550  -1661   1921       O  
ATOM   5716  CB  SER A 766     -63.297  -5.961-138.285  1.00139.87           C  
ANISOU 5716  CB  SER A 766    19218  16976  16946   -500  -1687   1827       C  
ATOM   5717  OG  SER A 766     -62.026  -5.391-138.030  1.00142.67           O  
ANISOU 5717  OG  SER A 766    19589  17378  17238   -666  -1637   1885       O  
ATOM   5718  N   SER A 767     -61.021  -7.064-140.269  1.00137.73           N  
ANISOU 5718  N   SER A 767    18840  17047  16445   -704  -1519   1918       N  
ATOM   5719  CA  SER A 767     -60.097  -6.813-141.379  1.00138.42           C  
ANISOU 5719  CA  SER A 767    18972  17229  16392   -839  -1483   1991       C  
ATOM   5720  C   SER A 767     -60.253  -7.843-142.491  1.00138.01           C  
ANISOU 5720  C   SER A 767    18857  17285  16293   -766  -1458   1973       C  
ATOM   5721  O   SER A 767     -60.150  -7.511-143.671  1.00141.93           O  
ANISOU 5721  O   SER A 767    19446  17795  16686   -822  -1474   2031       O  
ATOM   5722  CB  SER A 767     -58.649  -6.802-140.897  1.00137.73           C  
ANISOU 5722  CB  SER A 767    18795  17282  16252   -986  -1391   2010       C  
ATOM   5723  OG  SER A 767     -58.030  -8.056-141.122  1.00135.89           O  
ANISOU 5723  OG  SER A 767    18395  17239  15997   -954  -1307   1963       O  
ATOM   5724  N   ASN A 768     -60.487  -9.094-142.109  1.00135.03           N  
ANISOU 5724  N   ASN A 768    18330  16984  15990   -643  -1421   1893       N  
ATOM   5725  CA  ASN A 768     -60.736 -10.154-143.080  1.00134.91           C  
ANISOU 5725  CA  ASN A 768    18254  17060  15944   -553  -1407   1864       C  
ATOM   5726  C   ASN A 768     -62.086  -9.996-143.783  1.00136.04           C  
ANISOU 5726  C   ASN A 768    18504  17071  16112   -443  -1498   1863       C  
ATOM   5727  O   ASN A 768     -62.210 -10.318-144.965  1.00137.40           O  
ANISOU 5727  O   ASN A 768    18701  17289  16213   -421  -1505   1880       O  
ATOM   5728  CB  ASN A 768     -60.604 -11.535-142.432  1.00131.01           C  
ANISOU 5728  CB  ASN A 768    17584  16672  15519   -456  -1354   1778       C  
ATOM   5729  CG  ASN A 768     -59.162 -11.909-142.130  1.00130.42           C  
ANISOU 5729  CG  ASN A 768    17393  16771  15388   -551  -1261   1773       C  
ATOM   5730  OD1 ASN A 768     -58.890 -13.002-141.634  1.00128.82           O  
ANISOU 5730  OD1 ASN A 768    17055  16662  15225   -482  -1220   1706       O  
ATOM   5731  ND2 ASN A 768     -58.229 -11.006-142.430  1.00131.52           N  
ANISOU 5731  ND2 ASN A 768    17587  16954  15428   -711  -1233   1842       N  
ATOM   5732  N   VAL A 769     -63.086  -9.494-143.055  1.00135.35           N  
ANISOU 5732  N   VAL A 769    18475  16828  16122   -371  -1569   1839       N  
ATOM   5733  CA  VAL A 769     -64.383  -9.151-143.646  1.00137.01           C  
ANISOU 5733  CA  VAL A 769    18797  16904  16354   -270  -1666   1834       C  
ATOM   5734  C   VAL A 769     -64.200  -7.982-144.614  1.00142.91           C  
ANISOU 5734  C   VAL A 769    19725  17581  16993   -371  -1716   1924       C  
ATOM   5735  O   VAL A 769     -64.864  -7.913-145.649  1.00146.24           O  
ANISOU 5735  O   VAL A 769    20232  17956  17374   -316  -1773   1939       O  
ATOM   5736  CB  VAL A 769     -65.450  -8.830-142.574  1.00134.17           C  
ANISOU 5736  CB  VAL A 769    18451  16409  16117   -172  -1731   1779       C  
ATOM   5737  CG1 VAL A 769     -66.732  -8.307-143.206  1.00133.93           C  
ANISOU 5737  CG1 VAL A 769    18546  16241  16097    -73  -1840   1774       C  
ATOM   5738  CG2 VAL A 769     -65.763 -10.072-141.757  1.00132.98           C  
ANISOU 5738  CG2 VAL A 769    18132  16329  16066    -71  -1689   1692       C  
ATOM   5739  N   GLY A 770     -63.281  -7.081-144.275  1.00145.41           N  
ANISOU 5739  N   GLY A 770    20101  17891  17257   -523  -1695   1985       N  
ATOM   5740  CA  GLY A 770     -62.876  -6.005-145.173  1.00148.26           C  
ANISOU 5740  CA  GLY A 770    20631  18204  17495   -655  -1731   2081       C  
ATOM   5741  C   GLY A 770     -62.328  -6.543-146.475  1.00150.08           C  
ANISOU 5741  C   GLY A 770    20840  18574  17608   -703  -1681   2116       C  
ATOM   5742  O   GLY A 770     -62.694  -6.071-147.546  1.00153.91           O  
ANISOU 5742  O   GLY A 770    21461  18999  18016   -714  -1739   2166       O  
ATOM   5743  N   GLU A 771     -61.462  -7.548-146.378  1.00148.82           N  
ANISOU 5743  N   GLU A 771    20509  18602  17432   -723  -1578   2085       N  
ATOM   5744  CA  GLU A 771     -60.872  -8.188-147.550  1.00151.66           C  
ANISOU 5744  CA  GLU A 771    20820  19122  17680   -756  -1523   2104       C  
ATOM   5745  C   GLU A 771     -61.908  -8.919-148.408  1.00152.15           C  
ANISOU 5745  C   GLU A 771    20885  19161  17763   -599  -1568   2066       C  
ATOM   5746  O   GLU A 771     -61.758  -8.998-149.624  1.00154.36           O  
ANISOU 5746  O   GLU A 771    21209  19502  17937   -626  -1566   2103       O  
ATOM   5747  CB  GLU A 771     -59.744  -9.137-147.136  1.00151.15           C  
ANISOU 5747  CB  GLU A 771    20563  19264  17602   -791  -1411   2062       C  
ATOM   5748  CG  GLU A 771     -58.495  -8.429-146.626  1.00152.53           C  
ANISOU 5748  CG  GLU A 771    20731  19507  17713   -976  -1354   2109       C  
ATOM   5749  CD  GLU A 771     -57.524  -9.361-145.916  1.00152.52           C  
ANISOU 5749  CD  GLU A 771    20533  19687  17731   -979  -1257   2048       C  
ATOM   5750  OE1 GLU A 771     -57.961 -10.151-145.053  1.00150.94           O  
ANISOU 5750  OE1 GLU A 771    20231  19469  17650   -849  -1255   1970       O  
ATOM   5751  OE2 GLU A 771     -56.312  -9.293-146.208  1.00153.79           O  
ANISOU 5751  OE2 GLU A 771    20640  20012  17781  -1115  -1185   2075       O  
ATOM   5752  N   VAL A 772     -62.955  -9.442-147.773  1.00152.14           N  
ANISOU 5752  N   VAL A 772    20836  19077  17892   -440  -1609   1991       N  
ATOM   5753  CA  VAL A 772     -64.041 -10.126-148.487  1.00154.12           C  
ANISOU 5753  CA  VAL A 772    21087  19297  18174   -287  -1660   1948       C  
ATOM   5754  C   VAL A 772     -65.023  -9.135-149.119  1.00157.53           C  
ANISOU 5754  C   VAL A 772    21707  19556  18589   -258  -1770   1988       C  
ATOM   5755  O   VAL A 772     -65.471  -9.343-150.244  1.00162.07           O  
ANISOU 5755  O   VAL A 772    22334  20133  19110   -207  -1804   1999       O  
ATOM   5756  CB  VAL A 772     -64.794 -11.131-147.582  1.00154.18           C  
ANISOU 5756  CB  VAL A 772    20964  19295  18320   -137  -1661   1851       C  
ATOM   5757  CG1 VAL A 772     -66.031 -11.684-148.278  1.00153.08           C  
ANISOU 5757  CG1 VAL A 772    20842  19104  18216     12  -1726   1808       C  
ATOM   5758  CG2 VAL A 772     -63.876 -12.272-147.176  1.00156.26           C  
ANISOU 5758  CG2 VAL A 772    21053  19731  18587   -145  -1564   1807       C  
ATOM   5759  N   VAL A 773     -65.356  -8.066-148.397  1.00159.54           N  
ANISOU 5759  N   VAL A 773    22067  19664  18888   -284  -1830   2006       N  
ATOM   5760  CA  VAL A 773     -66.232  -7.016-148.930  1.00162.03           C  
ANISOU 5760  CA  VAL A 773    22576  19805  19181   -257  -1947   2041       C  
ATOM   5761  C   VAL A 773     -65.538  -6.256-150.069  1.00165.84           C  
ANISOU 5761  C   VAL A 773    23205  20297  19508   -404  -1954   2145       C  
ATOM   5762  O   VAL A 773     -66.183  -5.880-151.051  1.00168.95           O  
ANISOU 5762  O   VAL A 773    23734  20608  19850   -365  -2032   2173       O  
ATOM   5763  CB  VAL A 773     -66.728  -6.054-147.819  1.00163.01           C  
ANISOU 5763  CB  VAL A 773    22777  19769  19387   -242  -2017   2027       C  
ATOM   5764  CG1 VAL A 773     -67.506  -4.884-148.405  1.00164.81           C  
ANISOU 5764  CG1 VAL A 773    23225  19817  19577   -222  -2147   2066       C  
ATOM   5765  CG2 VAL A 773     -67.601  -6.799-146.819  1.00159.95           C  
ANISOU 5765  CG2 VAL A 773    22255  19372  19145    -88  -2021   1922       C  
ATOM   5766  N   CYS A 774     -64.225  -6.058-149.938  1.00166.34           N  
ANISOU 5766  N   CYS A 774    23238  20468  19494   -574  -1871   2199       N  
ATOM   5767  CA  CYS A 774     -63.403  -5.394-150.961  1.00169.24           C  
ANISOU 5767  CA  CYS A 774    23724  20877  19700   -743  -1860   2299       C  
ATOM   5768  C   CYS A 774     -63.453  -6.092-152.320  1.00166.60           C  
ANISOU 5768  C   CYS A 774    23373  20648  19280   -708  -1841   2307       C  
ATOM   5769  O   CYS A 774     -63.653  -5.446-153.349  1.00167.85           O  
ANISOU 5769  O   CYS A 774    23694  20741  19339   -754  -1901   2373       O  
ATOM   5770  CB  CYS A 774     -61.948  -5.278-150.485  1.00172.41           C  
ANISOU 5770  CB  CYS A 774    24047  21419  20042   -925  -1757   2336       C  
ATOM   5771  SG  CYS A 774     -60.715  -4.969-151.775  1.00179.97           S  
ANISOU 5771  SG  CYS A 774    25059  22530  20789  -1136  -1696   2437       S  
ATOM   5772  N   ILE A 775     -63.272  -7.409-152.311  1.00160.69           N  
ANISOU 5772  N   ILE A 775    22432  20055  18565   -625  -1763   2238       N  
ATOM   5773  CA  ILE A 775     -63.205  -8.194-153.540  1.00158.58           C  
ANISOU 5773  CA  ILE A 775    22125  19910  18216   -588  -1735   2236       C  
ATOM   5774  C   ILE A 775     -64.584  -8.537-154.110  1.00159.65           C  
ANISOU 5774  C   ILE A 775    22310  19939  18409   -409  -1824   2194       C  
ATOM   5775  O   ILE A 775     -64.785  -8.474-155.323  1.00164.62           O  
ANISOU 5775  O   ILE A 775    23027  20574  18947   -406  -1855   2230       O  
ATOM   5776  CB  ILE A 775     -62.306  -9.437-153.357  1.00154.36           C  
ANISOU 5776  CB  ILE A 775    21373  19597  17676   -583  -1620   2181       C  
ATOM   5777  CG1 ILE A 775     -60.838  -9.011-153.462  1.00155.06           C  
ANISOU 5777  CG1 ILE A 775    21444  19833  17639   -787  -1536   2244       C  
ATOM   5778  CG2 ILE A 775     -62.632 -10.522-154.378  1.00153.25           C  
ANISOU 5778  CG2 ILE A 775    21166  19553  17507   -467  -1612   2140       C  
ATOM   5779  CD1 ILE A 775     -59.847  -9.999-152.891  1.00155.24           C  
ANISOU 5779  CD1 ILE A 775    21255  20055  17671   -795  -1428   2183       C  
ATOM   5780  N   PHE A 776     -65.533  -8.885-153.246  1.00157.55           N  
ANISOU 5780  N   PHE A 776    21989  19582  18288   -263  -1864   2116       N  
ATOM   5781  CA  PHE A 776     -66.873  -9.254-153.701  1.00156.26           C  
ANISOU 5781  CA  PHE A 776    21855  19329  18185    -91  -1947   2065       C  
ATOM   5782  C   PHE A 776     -67.686  -8.062-154.203  1.00158.10           C  
ANISOU 5782  C   PHE A 776    22304  19376  18389    -81  -2067   2111       C  
ATOM   5783  O   PHE A 776     -68.745  -8.247-154.794  1.00158.39           O  
ANISOU 5783  O   PHE A 776    22387  19344  18450     49  -2142   2078       O  
ATOM   5784  CB  PHE A 776     -67.638 -10.019-152.619  1.00156.28           C  
ANISOU 5784  CB  PHE A 776    21726  19307  18345     50  -1951   1965       C  
ATOM   5785  CG  PHE A 776     -68.942 -10.603-153.091  1.00157.07           C  
ANISOU 5785  CG  PHE A 776    21821  19353  18503    222  -2020   1902       C  
ATOM   5786  CD1 PHE A 776     -68.961 -11.713-153.932  1.00157.11           C  
ANISOU 5786  CD1 PHE A 776    21744  19472  18479    286  -1989   1874       C  
ATOM   5787  CD2 PHE A 776     -70.153 -10.045-152.690  1.00157.41           C  
ANISOU 5787  CD2 PHE A 776    21940  19238  18630    322  -2120   1866       C  
ATOM   5788  CE1 PHE A 776     -70.164 -12.252-154.367  1.00157.77           C  
ANISOU 5788  CE1 PHE A 776    21823  19507  18615    438  -2055   1816       C  
ATOM   5789  CE2 PHE A 776     -71.358 -10.579-153.121  1.00157.52           C  
ANISOU 5789  CE2 PHE A 776    21941  19213  18694    477  -2184   1803       C  
ATOM   5790  CZ  PHE A 776     -71.364 -11.684-153.960  1.00157.85           C  
ANISOU 5790  CZ  PHE A 776    21902  19364  18706    530  -2150   1781       C  
ATOM   5791  N   LEU A 777     -67.198  -6.845-153.973  1.00161.20           N  
ANISOU 5791  N   LEU A 777    22833  19686  18727   -217  -2092   2185       N  
ATOM   5792  CA  LEU A 777     -67.785  -5.663-154.614  1.00165.25           C  
ANISOU 5792  CA  LEU A 777    23578  20028  19182   -230  -2212   2243       C  
ATOM   5793  C   LEU A 777     -67.262  -5.474-156.044  1.00169.23           C  
ANISOU 5793  C   LEU A 777    24186  20590  19523   -332  -2204   2328       C  
ATOM   5794  O   LEU A 777     -68.028  -5.144-156.951  1.00169.04           O  
ANISOU 5794  O   LEU A 777    24300  20469  19457   -268  -2296   2344       O  
ATOM   5795  CB  LEU A 777     -67.585  -4.397-153.770  1.00163.02           C  
ANISOU 5795  CB  LEU A 777    23422  19608  18908   -325  -2261   2285       C  
ATOM   5796  CG  LEU A 777     -68.666  -4.097-152.722  1.00159.37           C  
ANISOU 5796  CG  LEU A 777    22968  18996  18587   -183  -2346   2208       C  
ATOM   5797  CD1 LEU A 777     -68.162  -3.087-151.706  1.00160.76           C  
ANISOU 5797  CD1 LEU A 777    23215  19088  18777   -292  -2360   2242       C  
ATOM   5798  CD2 LEU A 777     -69.962  -3.606-153.352  1.00158.06           C  
ANISOU 5798  CD2 LEU A 777    22956  18671  18428    -46  -2487   2188       C  
ATOM   5799  N   THR A 778     -65.962  -5.697-156.236  1.00171.79           N  
ANISOU 5799  N   THR A 778    24438  21082  19752   -489  -2095   2376       N  
ATOM   5800  CA  THR A 778     -65.336  -5.655-157.560  1.00175.98           C  
ANISOU 5800  CA  THR A 778    25032  21711  20119   -598  -2066   2450       C  
ATOM   5801  C   THR A 778     -66.016  -6.625-158.534  1.00176.44           C  
ANISOU 5801  C   THR A 778    25037  21825  20177   -448  -2078   2402       C  
ATOM   5802  O   THR A 778     -66.298  -6.268-159.680  1.00180.52           O  
ANISOU 5802  O   THR A 778    25693  22299  20594   -459  -2134   2452       O  
ATOM   5803  CB  THR A 778     -63.816  -5.939-157.471  1.00176.79           C  
ANISOU 5803  CB  THR A 778    25013  22025  20133   -773  -1932   2484       C  
ATOM   5804  OG1 THR A 778     -63.169  -4.862-156.782  1.00177.21           O  
ANISOU 5804  OG1 THR A 778    25155  22017  20158   -939  -1934   2548       O  
ATOM   5805  CG2 THR A 778     -63.188  -6.085-158.855  1.00179.85           C  
ANISOU 5805  CG2 THR A 778    25430  22552  20350   -871  -1891   2544       C  
ATOM   5806  N   ALA A 779     -66.290  -7.841-158.071  1.00173.74           N  
ANISOU 5806  N   ALA A 779    24500  21569  19942   -311  -2029   2305       N  
ATOM   5807  CA  ALA A 779     -66.951  -8.842-158.900  1.00175.17           C  
ANISOU 5807  CA  ALA A 779    24619  21802  20134   -164  -2041   2251       C  
ATOM   5808  C   ALA A 779     -68.436  -8.531-159.096  1.00177.96           C  
ANISOU 5808  C   ALA A 779    25086  21969  20559     -8  -2170   2218       C  
ATOM   5809  O   ALA A 779     -68.883  -8.346-160.227  1.00182.96           O  
ANISOU 5809  O   ALA A 779    25835  22562  21116     22  -2231   2248       O  
ATOM   5810  CB  ALA A 779     -66.756 -10.235-158.321  1.00170.74           C  
ANISOU 5810  CB  ALA A 779    23827  21385  19660    -74  -1957   2160       C  
ATOM   5811  N   ALA A 780     -69.185  -8.448-157.997  1.00177.44           N  
ANISOU 5811  N   ALA A 780    24988  21795  20633     86  -2214   2156       N  
ATOM   5812  CA  ALA A 780     -70.649  -8.336-158.052  1.00177.91           C  
ANISOU 5812  CA  ALA A 780    25112  21706  20776    257  -2329   2098       C  
ATOM   5813  C   ALA A 780     -71.194  -6.976-158.510  1.00182.28           C  
ANISOU 5813  C   ALA A 780    25907  22075  21275    241  -2455   2155       C  
ATOM   5814  O   ALA A 780     -72.405  -6.823-158.689  1.00183.95           O  
ANISOU 5814  O   ALA A 780    26183  22167  21539    387  -2560   2106       O  
ATOM   5815  CB  ALA A 780     -71.271  -8.744-156.724  1.00174.12           C  
ANISOU 5815  CB  ALA A 780    24504  21194  20456    363  -2330   2005       C  
ATOM   5816  N   LEU A 781     -70.314  -5.993-158.691  1.00184.38           N  
ANISOU 5816  N   LEU A 781    26308  22316  21432     66  -2449   2254       N  
ATOM   5817  CA  LEU A 781     -70.709  -4.745-159.345  1.00188.06           C  
ANISOU 5817  CA  LEU A 781    27027  22611  21815     34  -2572   2322       C  
ATOM   5818  C   LEU A 781     -70.238  -4.721-160.798  1.00192.82           C  
ANISOU 5818  C   LEU A 781    27724  23279  22257    -53  -2560   2402       C  
ATOM   5819  O   LEU A 781     -71.018  -4.409-161.697  1.00196.62           O  
ANISOU 5819  O   LEU A 781    28348  23661  22695     23  -2661   2411       O  
ATOM   5820  CB  LEU A 781     -70.207  -3.511-158.585  1.00187.31           C  
ANISOU 5820  CB  LEU A 781    27061  22406  21702   -100  -2603   2382       C  
ATOM   5821  CG  LEU A 781     -70.871  -3.130-157.257  1.00184.04           C  
ANISOU 5821  CG  LEU A 781    26630  21868  21429     -6  -2660   2313       C  
ATOM   5822  CD1 LEU A 781     -70.263  -1.838-156.734  1.00184.12           C  
ANISOU 5822  CD1 LEU A 781    26799  21767  21390   -160  -2697   2389       C  
ATOM   5823  CD2 LEU A 781     -72.383  -2.995-157.379  1.00181.93           C  
ANISOU 5823  CD2 LEU A 781    26429  21459  21237    200  -2793   2236       C  
ATOM   5824  N   GLY A 782     -68.969  -5.060-161.019  1.00193.92           N  
ANISOU 5824  N   GLY A 782    27781  23593  22305   -210  -2439   2454       N  
ATOM   5825  CA  GLY A 782     -68.404  -5.134-162.366  1.00196.27           C  
ANISOU 5825  CA  GLY A 782    28140  23991  22442   -306  -2409   2526       C  
ATOM   5826  C   GLY A 782     -67.161  -4.289-162.573  1.00198.80           C  
ANISOU 5826  C   GLY A 782    28561  24359  22614   -554  -2363   2640       C  
ATOM   5827  O   GLY A 782     -66.566  -4.313-163.651  1.00203.49           O  
ANISOU 5827  O   GLY A 782    29199  25057  23059   -660  -2326   2705       O  
ATOM   5828  N   LEU A 783     -66.771  -3.550-161.534  1.00197.46           N  
ANISOU 5828  N   LEU A 783    28424  24119  22481   -649  -2364   2663       N  
ATOM   5829  CA  LEU A 783     -65.608  -2.654-161.559  1.00200.04           C  
ANISOU 5829  CA  LEU A 783    28853  24477  22677   -898  -2326   2771       C  
ATOM   5830  C   LEU A 783     -64.292  -3.380-161.892  1.00202.69           C  
ANISOU 5830  C   LEU A 783    29018  25081  22913  -1036  -2172   2791       C  
ATOM   5831  O   LEU A 783     -64.224  -4.610-161.803  1.00200.28           O  
ANISOU 5831  O   LEU A 783    28496  24931  22668   -929  -2089   2710       O  
ATOM   5832  CB  LEU A 783     -65.481  -1.931-160.210  1.00198.23           C  
ANISOU 5832  CB  LEU A 783    28646  24135  22535   -945  -2348   2768       C  
ATOM   5833  CG  LEU A 783     -66.623  -1.033-159.722  1.00196.91           C  
ANISOU 5833  CG  LEU A 783    28655  23706  22456   -831  -2503   2748       C  
ATOM   5834  CD1 LEU A 783     -66.571  -0.877-158.210  1.00194.67           C  
ANISOU 5834  CD1 LEU A 783    28285  23376  22304   -813  -2489   2698       C  
ATOM   5835  CD2 LEU A 783     -66.587   0.326-160.403  1.00200.02           C  
ANISOU 5835  CD2 LEU A 783    29347  23938  22714   -964  -2615   2859       C  
ATOM   5836  N   PRO A 784     -63.242  -2.623-162.283  1.00207.21           N  
ANISOU 5836  N   PRO A 784    29689  25713  23326  -1275  -2136   2897       N  
ATOM   5837  CA  PRO A 784     -61.930  -3.227-162.547  1.00208.25           C  
ANISOU 5837  CA  PRO A 784    29654  26115  23353  -1418  -1989   2912       C  
ATOM   5838  C   PRO A 784     -61.266  -3.751-161.273  1.00205.56           C  
ANISOU 5838  C   PRO A 784    29099  25888  23114  -1425  -1890   2848       C  
ATOM   5839  O   PRO A 784     -61.678  -3.382-160.171  1.00204.70           O  
ANISOU 5839  O   PRO A 784    29008  25635  23134  -1373  -1935   2819       O  
ATOM   5840  CB  PRO A 784     -61.119  -2.063-163.127  1.00212.45           C  
ANISOU 5840  CB  PRO A 784    30378  26642  23699  -1682  -1998   3044       C  
ATOM   5841  CG  PRO A 784     -61.778  -0.839-162.595  1.00213.61           C  
ANISOU 5841  CG  PRO A 784    30754  26511  23896  -1693  -2133   3087       C  
ATOM   5842  CD  PRO A 784     -63.239  -1.176-162.574  1.00211.50           C  
ANISOU 5842  CD  PRO A 784    30512  26080  23768  -1427  -2237   3007       C  
ATOM   5843  N   GLU A 785     -60.246  -4.595-161.434  1.00205.49           N  
ANISOU 5843  N   GLU A 785    28893  26138  23043  -1486  -1759   2823       N  
ATOM   5844  CA  GLU A 785     -59.551  -5.218-160.302  1.00201.18           C  
ANISOU 5844  CA  GLU A 785    28130  25722  22584  -1483  -1661   2755       C  
ATOM   5845  C   GLU A 785     -59.097  -4.191-159.258  1.00198.76           C  
ANISOU 5845  C   GLU A 785    27897  25321  22300  -1630  -1671   2803       C  
ATOM   5846  O   GLU A 785     -58.327  -3.275-159.562  1.00200.75           O  
ANISOU 5846  O   GLU A 785    28266  25596  22415  -1852  -1661   2899       O  
ATOM   5847  CB  GLU A 785     -58.387  -6.116-160.776  1.00204.09           C  
ANISOU 5847  CB  GLU A 785    28302  26395  22846  -1553  -1527   2731       C  
ATOM   5848  CG  GLU A 785     -57.109  -5.405-161.229  1.00212.73           C  
ANISOU 5848  CG  GLU A 785    29438  27637  23749  -1825  -1461   2824       C  
ATOM   5849  CD  GLU A 785     -57.122  -4.954-162.686  1.00218.90           C  
ANISOU 5849  CD  GLU A 785    30377  28437  24356  -1923  -1491   2910       C  
ATOM   5850  OE1 GLU A 785     -57.908  -5.498-163.491  1.00220.53           O  
ANISOU 5850  OE1 GLU A 785    30603  28616  24572  -1770  -1534   2881       O  
ATOM   5851  OE2 GLU A 785     -56.324  -4.055-163.034  1.00220.41           O  
ANISOU 5851  OE2 GLU A 785    30674  28676  24393  -2163  -1472   3009       O  
ATOM   5852  N   ALA A 786     -59.609  -4.333-158.038  1.00190.68           N  
ANISOU 5852  N   ALA A 786    26813  24189  21448  -1508  -1695   2735       N  
ATOM   5853  CA  ALA A 786     -59.291  -3.405-156.957  1.00185.24           C  
ANISOU 5853  CA  ALA A 786    26188  23395  20799  -1619  -1713   2768       C  
ATOM   5854  C   ALA A 786     -57.870  -3.618-156.443  1.00183.14           C  
ANISOU 5854  C   ALA A 786    25761  23343  20478  -1780  -1586   2769       C  
ATOM   5855  O   ALA A 786     -57.131  -2.654-156.238  1.00183.88           O  
ANISOU 5855  O   ALA A 786    25949  23427  20490  -1985  -1579   2847       O  
ATOM   5856  CB  ALA A 786     -60.300  -3.533-155.828  1.00181.29           C  
ANISOU 5856  CB  ALA A 786    25662  22725  20493  -1432  -1777   2688       C  
ATOM   5857  N   LEU A 787     -57.499  -4.883-156.244  1.00178.93           N  
ANISOU 5857  N   LEU A 787    24991  23004  19989  -1684  -1490   2680       N  
ATOM   5858  CA  LEU A 787     -56.157  -5.259-155.799  1.00177.48           C  
ANISOU 5858  CA  LEU A 787    24628  23051  19755  -1807  -1367   2662       C  
ATOM   5859  C   LEU A 787     -55.696  -6.547-156.475  1.00176.96           C  
ANISOU 5859  C   LEU A 787    24369  23231  19635  -1734  -1279   2596       C  
ATOM   5860  O   LEU A 787     -56.475  -7.489-156.630  1.00172.13           O  
ANISOU 5860  O   LEU A 787    23687  22602  19111  -1530  -1300   2522       O  
ATOM   5861  CB  LEU A 787     -56.119  -5.432-154.277  1.00174.77           C  
ANISOU 5861  CB  LEU A 787    24176  22663  19565  -1747  -1350   2597       C  
ATOM   5862  CG  LEU A 787     -56.255  -4.192-153.385  1.00176.36           C  
ANISOU 5862  CG  LEU A 787    24528  22665  19814  -1841  -1415   2651       C  
ATOM   5863  CD1 LEU A 787     -56.933  -4.540-152.067  1.00172.90           C  
ANISOU 5863  CD1 LEU A 787    24014  22110  19569  -1674  -1442   2566       C  
ATOM   5864  CD2 LEU A 787     -54.909  -3.522-153.149  1.00178.71           C  
ANISOU 5864  CD2 LEU A 787    24818  23085  19998  -2091  -1346   2713       C  
ATOM   5865  N   ILE A 788     -54.429  -6.574-156.882  1.00182.07           N  
ANISOU 5865  N   ILE A 788    24931  24111  20133  -1904  -1184   2621       N  
ATOM   5866  CA  ILE A 788     -53.815  -7.766-157.474  1.00185.01           C  
ANISOU 5866  CA  ILE A 788    25108  24747  20440  -1847  -1095   2552       C  
ATOM   5867  C   ILE A 788     -53.409  -8.735-156.344  1.00184.10           C  
ANISOU 5867  C   ILE A 788    24770  24736  20441  -1739  -1032   2442       C  
ATOM   5868  O   ILE A 788     -53.151  -8.290-155.222  1.00186.38           O  
ANISOU 5868  O   ILE A 788    25049  24962  20803  -1796  -1026   2443       O  
ATOM   5869  CB  ILE A 788     -52.620  -7.381-158.402  1.00188.04           C  
ANISOU 5869  CB  ILE A 788    25486  25356  20604  -2075  -1019   2617       C  
ATOM   5870  CG1 ILE A 788     -52.392  -8.420-159.509  1.00188.66           C  
ANISOU 5870  CG1 ILE A 788    25443  25651  20587  -1995   -969   2566       C  
ATOM   5871  CG2 ILE A 788     -51.335  -7.145-157.618  1.00187.84           C  
ANISOU 5871  CG2 ILE A 788    25341  25495  20533  -2244   -930   2614       C  
ATOM   5872  CD1 ILE A 788     -53.332  -8.298-160.690  1.00190.02           C  
ANISOU 5872  CD1 ILE A 788    25773  25710  20716  -1930  -1046   2611       C  
ATOM   5873  N   PRO A 789     -53.390 -10.060-156.617  1.00180.93           N  
ANISOU 5873  N   PRO A 789    24201  24481  20059  -1577   -994   2346       N  
ATOM   5874  CA  PRO A 789     -52.938 -11.055-155.634  1.00177.74           C  
ANISOU 5874  CA  PRO A 789    23592  24190  19749  -1474   -938   2239       C  
ATOM   5875  C   PRO A 789     -51.617 -10.741-154.917  1.00178.38           C  
ANISOU 5875  C   PRO A 789    23568  24432  19773  -1640   -854   2239       C  
ATOM   5876  O   PRO A 789     -51.452 -11.109-153.757  1.00176.63           O  
ANISOU 5876  O   PRO A 789    23244  24202  19664  -1579   -836   2177       O  
ATOM   5877  CB  PRO A 789     -52.790 -12.319-156.478  1.00176.34           C  
ANISOU 5877  CB  PRO A 789    23280  24200  19518  -1344   -904   2161       C  
ATOM   5878  CG  PRO A 789     -53.865 -12.186-157.498  1.00176.59           C  
ANISOU 5878  CG  PRO A 789    23460  24095  19539  -1271   -981   2203       C  
ATOM   5879  CD  PRO A 789     -54.032 -10.714-157.775  1.00179.44           C  
ANISOU 5879  CD  PRO A 789    24031  24310  19835  -1449  -1025   2327       C  
ATOM   5880  N   VAL A 790     -50.696 -10.067-155.599  1.00182.57           N  
ANISOU 5880  N   VAL A 790    24126  25110  20129  -1851   -804   2308       N  
ATOM   5881  CA  VAL A 790     -49.414  -9.681-155.008  1.00185.35           C  
ANISOU 5881  CA  VAL A 790    24384  25628  20411  -2031   -724   2314       C  
ATOM   5882  C   VAL A 790     -49.598  -8.576-153.965  1.00184.66           C  
ANISOU 5882  C   VAL A 790    24420  25332  20406  -2135   -765   2377       C  
ATOM   5883  O   VAL A 790     -48.844  -8.497-152.995  1.00185.79           O  
ANISOU 5883  O   VAL A 790    24466  25548  20578  -2201   -717   2349       O  
ATOM   5884  CB  VAL A 790     -48.411  -9.210-156.085  1.00192.90           C  
ANISOU 5884  CB  VAL A 790    25343  26805  21143  -2248   -660   2376       C  
ATOM   5885  CG1 VAL A 790     -47.012  -9.087-155.500  1.00194.51           C  
ANISOU 5885  CG1 VAL A 790    25397  27236  21270  -2409   -565   2353       C  
ATOM   5886  CG2 VAL A 790     -48.399 -10.161-157.274  1.00195.46           C  
ANISOU 5886  CG2 VAL A 790    25583  27306  21376  -2145   -636   2326       C  
ATOM   5887  N   GLN A 791     -50.603  -7.728-154.176  1.00185.22           N  
ANISOU 5887  N   GLN A 791    24709  25148  20515  -2141   -860   2457       N  
ATOM   5888  CA  GLN A 791     -50.904  -6.616-153.273  1.00185.57           C  
ANISOU 5888  CA  GLN A 791    24899  24972  20636  -2226   -918   2517       C  
ATOM   5889  C   GLN A 791     -51.705  -7.071-152.058  1.00178.63           C  
ANISOU 5889  C   GLN A 791    23974  23931  19965  -2029   -960   2441       C  
ATOM   5890  O   GLN A 791     -51.435  -6.641-150.936  1.00175.82           O  
ANISOU 5890  O   GLN A 791    23607  23515  19680  -2081   -956   2438       O  
ATOM   5891  CB  GLN A 791     -51.669  -5.513-154.013  1.00191.74           C  
ANISOU 5891  CB  GLN A 791    25943  25543  21367  -2301  -1015   2627       C  
ATOM   5892  CG  GLN A 791     -50.821  -4.685-154.968  1.00199.42           C  
ANISOU 5892  CG  GLN A 791    27009  26631  22129  -2558   -984   2730       C  
ATOM   5893  CD  GLN A 791     -51.648  -3.844-155.925  1.00202.17           C  
ANISOU 5893  CD  GLN A 791    27611  26787  22415  -2597  -1085   2828       C  
ATOM   5894  OE1 GLN A 791     -52.703  -4.269-156.403  1.00199.33           O  
ANISOU 5894  OE1 GLN A 791    27301  26314  22119  -2413  -1148   2802       O  
ATOM   5895  NE2 GLN A 791     -51.165  -2.643-156.216  1.00206.82           N  
ANISOU 5895  NE2 GLN A 791    28367  27340  22875  -2841  -1104   2941       N  
ATOM   5896  N   LEU A 792     -52.691  -7.936-152.294  1.00173.55           N  
ANISOU 5896  N   LEU A 792    23306  23219  19413  -1811  -1002   2380       N  
ATOM   5897  CA  LEU A 792     -53.534  -8.480-151.232  1.00166.69           C  
ANISOU 5897  CA  LEU A 792    22389  22210  18734  -1619  -1041   2304       C  
ATOM   5898  C   LEU A 792     -52.710  -9.267-150.217  1.00164.18           C  
ANISOU 5898  C   LEU A 792    21864  22045  18469  -1589   -963   2218       C  
ATOM   5899  O   LEU A 792     -52.918  -9.138-149.015  1.00162.92           O  
ANISOU 5899  O   LEU A 792    21690  21778  18434  -1552   -979   2191       O  
ATOM   5900  CB  LEU A 792     -54.641  -9.363-151.818  1.00162.66           C  
ANISOU 5900  CB  LEU A 792    21876  21638  18288  -1407  -1091   2253       C  
ATOM   5901  CG  LEU A 792     -55.723  -9.884-150.867  1.00157.58           C  
ANISOU 5901  CG  LEU A 792    21206  20831  17833  -1211  -1146   2181       C  
ATOM   5902  CD1 LEU A 792     -56.702  -8.781-150.491  1.00156.90           C  
ANISOU 5902  CD1 LEU A 792    21308  20485  17820  -1215  -1244   2235       C  
ATOM   5903  CD2 LEU A 792     -56.456 -11.061-151.489  1.00154.50           C  
ANISOU 5903  CD2 LEU A 792    20753  20467  17480  -1019  -1165   2114       C  
ATOM   5904  N   LEU A 793     -51.772 -10.073-150.708  1.00163.94           N  
ANISOU 5904  N   LEU A 793    21677  22269  18342  -1602   -881   2172       N  
ATOM   5905  CA  LEU A 793     -50.879 -10.833-149.837  1.00162.14           C  
ANISOU 5905  CA  LEU A 793    21251  22208  18144  -1576   -808   2086       C  
ATOM   5906  C   LEU A 793     -49.837  -9.952-149.148  1.00164.16           C  
ANISOU 5906  C   LEU A 793    21495  22525  18350  -1778   -760   2127       C  
ATOM   5907  O   LEU A 793     -49.180 -10.393-148.205  1.00165.39           O  
ANISOU 5907  O   LEU A 793    21510  22777  18553  -1761   -712   2061       O  
ATOM   5908  CB  LEU A 793     -50.186 -11.968-150.602  1.00162.29           C  
ANISOU 5908  CB  LEU A 793    21107  22488  18068  -1516   -744   2014       C  
ATOM   5909  CG  LEU A 793     -51.007 -13.127-151.178  1.00160.95           C  
ANISOU 5909  CG  LEU A 793    20901  22304  17947  -1299   -781   1947       C  
ATOM   5910  CD1 LEU A 793     -50.070 -14.223-151.660  1.00161.73           C  
ANISOU 5910  CD1 LEU A 793    20816  22682  17952  -1249   -713   1862       C  
ATOM   5911  CD2 LEU A 793     -52.010 -13.685-150.179  1.00157.65           C  
ANISOU 5911  CD2 LEU A 793    20478  21701  17719  -1117   -837   1890       C  
ATOM   5912  N   TRP A 794     -49.686  -8.715-149.616  1.00165.98           N  
ANISOU 5912  N   TRP A 794    21881  22697  18484  -1971   -777   2235       N  
ATOM   5913  CA  TRP A 794     -48.765  -7.774-148.983  1.00167.50           C  
ANISOU 5913  CA  TRP A 794    22087  22926  18627  -2179   -742   2284       C  
ATOM   5914  C   TRP A 794     -49.392  -7.113-147.757  1.00166.30           C  
ANISOU 5914  C   TRP A 794    22032  22529  18624  -2156   -805   2299       C  
ATOM   5915  O   TRP A 794     -48.797  -7.123-146.680  1.00167.04           O  
ANISOU 5915  O   TRP A 794    22032  22666  18771  -2186   -768   2262       O  
ATOM   5916  CB  TRP A 794     -48.263  -6.719-149.970  1.00170.66           C  
ANISOU 5916  CB  TRP A 794    22617  23374  18849  -2416   -735   2396       C  
ATOM   5917  CG  TRP A 794     -47.437  -5.648-149.313  1.00171.36           C  
ANISOU 5917  CG  TRP A 794    22750  23465  18890  -2641   -713   2457       C  
ATOM   5918  CD1 TRP A 794     -47.820  -4.364-149.048  1.00173.05           C  
ANISOU 5918  CD1 TRP A 794    23175  23457  19117  -2763   -787   2553       C  
ATOM   5919  CD2 TRP A 794     -46.098  -5.776-148.822  1.00171.26           C  
ANISOU 5919  CD2 TRP A 794    22569  23688  18812  -2766   -618   2420       C  
ATOM   5920  NE1 TRP A 794     -46.801  -3.681-148.431  1.00173.94           N  
ANISOU 5920  NE1 TRP A 794    23265  23648  19176  -2965   -742   2584       N  
ATOM   5921  CE2 TRP A 794     -45.731  -4.523-148.281  1.00173.34           C  
ANISOU 5921  CE2 TRP A 794    22953  23857  19050  -2973   -636   2503       C  
ATOM   5922  CE3 TRP A 794     -45.169  -6.824-148.793  1.00170.13           C  
ANISOU 5922  CE3 TRP A 794    22186  23829  18624  -2720   -525   2321       C  
ATOM   5923  CZ2 TRP A 794     -44.476  -4.289-147.714  1.00174.62           C  
ANISOU 5923  CZ2 TRP A 794    22998  24201  19146  -3141   -559   2492       C  
ATOM   5924  CZ3 TRP A 794     -43.921  -6.591-148.230  1.00171.94           C  
ANISOU 5924  CZ3 TRP A 794    22296  24244  18787  -2878   -450   2305       C  
ATOM   5925  CH2 TRP A 794     -43.588  -5.333-147.697  1.00174.11           C  
ANISOU 5925  CH2 TRP A 794    22690  24422  19040  -3090   -465   2392       C  
ATOM   5926  N   VAL A 795     -50.584  -6.538-147.922  1.00164.68           N  
ANISOU 5926  N   VAL A 795    22012  22074  18483  -2097   -903   2349       N  
ATOM   5927  CA  VAL A 795     -51.317  -5.954-146.793  1.00161.57           C  
ANISOU 5927  CA  VAL A 795    21711  21443  18235  -2047   -973   2353       C  
ATOM   5928  C   VAL A 795     -51.571  -7.004-145.718  1.00158.45           C  
ANISOU 5928  C   VAL A 795    21154  21057  17992  -1859   -954   2242       C  
ATOM   5929  O   VAL A 795     -51.479  -6.716-144.525  1.00158.58           O  
ANISOU 5929  O   VAL A 795    21152  21001  18099  -1868   -958   2224       O  
ATOM   5930  CB  VAL A 795     -52.661  -5.313-147.211  1.00160.34           C  
ANISOU 5930  CB  VAL A 795    21766  21030  18125  -1976  -1089   2404       C  
ATOM   5931  CG1 VAL A 795     -52.454  -3.879-147.659  1.00164.14           C  
ANISOU 5931  CG1 VAL A 795    22456  21413  18497  -2184  -1137   2522       C  
ATOM   5932  CG2 VAL A 795     -53.350  -6.123-148.299  1.00159.83           C  
ANISOU 5932  CG2 VAL A 795    21690  20993  18042  -1834  -1106   2378       C  
ATOM   5933  N   ASN A 796     -51.864  -8.225-146.160  1.00155.15           N  
ANISOU 5933  N   ASN A 796    20623  20730  17595  -1697   -935   2170       N  
ATOM   5934  CA  ASN A 796     -52.131  -9.350-145.274  1.00149.77           C  
ANISOU 5934  CA  ASN A 796    19796  20064  17045  -1515   -922   2066       C  
ATOM   5935  C   ASN A 796     -50.880  -9.858-144.557  1.00150.96           C  
ANISOU 5935  C   ASN A 796    19766  20415  17175  -1563   -834   2007       C  
ATOM   5936  O   ASN A 796     -50.975 -10.654-143.626  1.00150.14           O  
ANISOU 5936  O   ASN A 796    19552  20314  17179  -1438   -825   1926       O  
ATOM   5937  CB  ASN A 796     -52.783 -10.482-146.063  1.00146.14           C  
ANISOU 5937  CB  ASN A 796    19286  19642  16598  -1340   -936   2011       C  
ATOM   5938  CG  ASN A 796     -53.626 -11.386-145.196  1.00142.11           C  
ANISOU 5938  CG  ASN A 796    18709  19038  16248  -1142   -967   1927       C  
ATOM   5939  OD1 ASN A 796     -53.314 -12.563-145.026  1.00141.40           O  
ANISOU 5939  OD1 ASN A 796    18469  19076  16177  -1039   -928   1845       O  
ATOM   5940  ND2 ASN A 796     -54.702 -10.842-144.639  1.00140.51           N  
ANISOU 5940  ND2 ASN A 796    18618  18613  16155  -1088  -1041   1944       N  
ATOM   5941  N   LEU A 797     -49.711  -9.401-144.999  1.00154.87           N  
ANISOU 5941  N   LEU A 797    20231  21082  17527  -1747   -772   2047       N  
ATOM   5942  CA  LEU A 797     -48.455  -9.724-144.329  1.00158.07           C  
ANISOU 5942  CA  LEU A 797    20471  21687  17900  -1813   -691   1994       C  
ATOM   5943  C   LEU A 797     -48.016  -8.597-143.397  1.00161.15           C  
ANISOU 5943  C   LEU A 797    20922  21999  18306  -1974   -691   2046       C  
ATOM   5944  O   LEU A 797     -47.478  -8.857-142.321  1.00164.14           O  
ANISOU 5944  O   LEU A 797    21190  22430  18745  -1962   -657   1990       O  
ATOM   5945  CB  LEU A 797     -47.355 -10.050-145.348  1.00161.45           C  
ANISOU 5945  CB  LEU A 797    20794  22394  18154  -1908   -615   1986       C  
ATOM   5946  CG  LEU A 797     -45.880 -10.091-144.918  1.00163.88           C  
ANISOU 5946  CG  LEU A 797    20945  22943  18377  -2034   -527   1949       C  
ATOM   5947  CD1 LEU A 797     -45.595 -11.179-143.890  1.00160.72           C  
ANISOU 5947  CD1 LEU A 797    20372  22616  18077  -1878   -503   1830       C  
ATOM   5948  CD2 LEU A 797     -44.982 -10.264-146.135  1.00167.29           C  
ANISOU 5948  CD2 LEU A 797    21301  23638  18621  -2136   -463   1953       C  
ATOM   5949  N   VAL A 798     -48.242  -7.353-143.809  1.00164.02           N  
ANISOU 5949  N   VAL A 798    21468  22236  18615  -2123   -734   2152       N  
ATOM   5950  CA  VAL A 798     -47.846  -6.193-143.006  1.00165.21           C  
ANISOU 5950  CA  VAL A 798    21701  22298  18771  -2288   -745   2209       C  
ATOM   5951  C   VAL A 798     -48.774  -6.005-141.804  1.00160.93           C  
ANISOU 5951  C   VAL A 798    21219  21521  18406  -2166   -813   2186       C  
ATOM   5952  O   VAL A 798     -48.306  -5.724-140.701  1.00159.56           O  
ANISOU 5952  O   VAL A 798    21001  21337  18284  -2215   -796   2169       O  
ATOM   5953  CB  VAL A 798     -47.759  -4.897-143.848  1.00170.25           C  
ANISOU 5953  CB  VAL A 798    22533  22870  19283  -2496   -780   2333       C  
ATOM   5954  CG1 VAL A 798     -47.405  -3.698-142.979  1.00172.09           C  
ANISOU 5954  CG1 VAL A 798    22866  22993  19528  -2661   -803   2391       C  
ATOM   5955  CG2 VAL A 798     -46.721  -5.049-144.945  1.00174.13           C  
ANISOU 5955  CG2 VAL A 798    22950  23622  19588  -2641   -701   2354       C  
ATOM   5956  N   THR A 799     -50.078  -6.174-142.016  1.00157.80           N  
ANISOU 5956  N   THR A 799    20915  20944  18096  -2008   -889   2182       N  
ATOM   5957  CA  THR A 799     -51.046  -6.040-140.926  1.00154.76           C  
ANISOU 5957  CA  THR A 799    20579  20348  17874  -1883   -955   2152       C  
ATOM   5958  C   THR A 799     -50.900  -7.163-139.902  1.00152.99           C  
ANISOU 5958  C   THR A 799    20170  20203  17756  -1744   -910   2047       C  
ATOM   5959  O   THR A 799     -50.856  -6.902-138.702  1.00152.18           O  
ANISOU 5959  O   THR A 799    20051  20028  17741  -1742   -916   2025       O  
ATOM   5960  CB  THR A 799     -52.505  -5.953-141.422  1.00152.05           C  
ANISOU 5960  CB  THR A 799    20372  19806  17592  -1746  -1048   2166       C  
ATOM   5961  OG1 THR A 799     -52.811  -7.095-142.228  1.00150.96           O  
ANISOU 5961  OG1 THR A 799    20146  19768  17441  -1614  -1028   2118       O  
ATOM   5962  CG2 THR A 799     -52.715  -4.692-142.234  1.00152.96           C  
ANISOU 5962  CG2 THR A 799    20699  19802  17615  -1881  -1112   2272       C  
ATOM   5963  N   ASP A 800     -50.800  -8.402-140.384  1.00153.10           N  
ANISOU 5963  N   ASP A 800    20052  20364  17755  -1630   -869   1981       N  
ATOM   5964  CA  ASP A 800     -50.625  -9.572-139.517  1.00150.91           C  
ANISOU 5964  CA  ASP A 800    19605  20168  17564  -1495   -832   1879       C  
ATOM   5965  C   ASP A 800     -49.219  -9.676-138.916  1.00150.85           C  
ANISOU 5965  C   ASP A 800    19461  20349  17505  -1598   -753   1848       C  
ATOM   5966  O   ASP A 800     -48.964 -10.527-138.065  1.00150.55           O  
ANISOU 5966  O   ASP A 800    19293  20373  17536  -1502   -726   1766       O  
ATOM   5967  CB  ASP A 800     -50.970 -10.864-140.272  1.00149.38           C  
ANISOU 5967  CB  ASP A 800    19329  20064  17364  -1338   -825   1819       C  
ATOM   5968  CG  ASP A 800     -52.461 -11.008-140.554  1.00148.47           C  
ANISOU 5968  CG  ASP A 800    19315  19760  17335  -1197   -905   1822       C  
ATOM   5969  OD1 ASP A 800     -53.249 -10.114-140.179  1.00147.90           O  
ANISOU 5969  OD1 ASP A 800    19374  19492  17326  -1210   -967   1866       O  
ATOM   5970  OD2 ASP A 800     -52.852 -12.029-141.156  1.00148.49           O  
ANISOU 5970  OD2 ASP A 800    19264  19814  17340  -1068   -909   1775       O  
ATOM   5971  N   GLY A 801     -48.317  -8.802-139.353  1.00152.87           N  
ANISOU 5971  N   GLY A 801    19750  20695  17637  -1798   -718   1913       N  
ATOM   5972  CA  GLY A 801     -46.921  -8.855-138.937  1.00153.99           C  
ANISOU 5972  CA  GLY A 801    19756  21043  17708  -1913   -640   1884       C  
ATOM   5973  C   GLY A 801     -46.491  -7.764-137.979  1.00156.17           C  
ANISOU 5973  C   GLY A 801    20087  21244  18005  -2061   -643   1928       C  
ATOM   5974  O   GLY A 801     -45.597  -7.977-137.162  1.00157.06           O  
ANISOU 5974  O   GLY A 801    20075  21476  18124  -2095   -592   1878       O  
ATOM   5975  N   LEU A 802     -47.113  -6.592-138.076  1.00158.14           N  
ANISOU 5975  N   LEU A 802    20527  21294  18264  -2147   -707   2017       N  
ATOM   5976  CA  LEU A 802     -46.742  -5.466-137.219  1.00159.96           C  
ANISOU 5976  CA  LEU A 802    20833  21435  18509  -2294   -722   2065       C  
ATOM   5977  C   LEU A 802     -47.869  -4.970-136.298  1.00160.48           C  
ANISOU 5977  C   LEU A 802    21020  21230  18723  -2198   -808   2071       C  
ATOM   5978  O   LEU A 802     -47.782  -5.170-135.089  1.00161.18           O  
ANISOU 5978  O   LEU A 802    21037  21293  18910  -2142   -800   2017       O  
ATOM   5979  CB  LEU A 802     -46.104  -4.326-138.027  1.00162.52           C  
ANISOU 5979  CB  LEU A 802    21271  21795  18681  -2537   -717   2169       C  
ATOM   5980  CG  LEU A 802     -44.635  -4.500-138.418  1.00164.60           C  
ANISOU 5980  CG  LEU A 802    21393  22349  18798  -2697   -619   2159       C  
ATOM   5981  CD1 LEU A 802     -44.315  -3.718-139.681  1.00168.64           C  
ANISOU 5981  CD1 LEU A 802    22019  22912  19143  -2893   -618   2259       C  
ATOM   5982  CD2 LEU A 802     -43.709  -4.088-137.283  1.00165.41           C  
ANISOU 5982  CD2 LEU A 802    21424  22506  18915  -2810   -583   2142       C  
ATOM   5983  N   PRO A 803     -48.929  -4.338-136.851  1.00162.48           N  
ANISOU 5983  N   PRO A 803    21455  21289  18991  -2173   -892   2131       N  
ATOM   5984  CA  PRO A 803     -49.971  -3.847-135.940  1.00162.25           C  
ANISOU 5984  CA  PRO A 803    21531  21020  19096  -2078   -976   2125       C  
ATOM   5985  C   PRO A 803     -50.779  -4.945-135.242  1.00160.14           C  
ANISOU 5985  C   PRO A 803    21158  20718  18970  -1851   -981   2029       C  
ATOM   5986  O   PRO A 803     -51.268  -4.729-134.134  1.00160.13           O  
ANISOU 5986  O   PRO A 803    21173  20587  19080  -1786  -1018   2000       O  
ATOM   5987  CB  PRO A 803     -50.874  -3.008-136.849  1.00163.08           C  
ANISOU 5987  CB  PRO A 803    21845  20950  19166  -2095  -1066   2202       C  
ATOM   5988  CG  PRO A 803     -50.648  -3.547-138.214  1.00164.56           C  
ANISOU 5988  CG  PRO A 803    22002  21281  19240  -2112  -1028   2221       C  
ATOM   5989  CD  PRO A 803     -49.210  -3.966-138.250  1.00164.92           C  
ANISOU 5989  CD  PRO A 803    21886  21583  19191  -2234   -921   2203       C  
ATOM   5990  N   ALA A 804     -50.914  -6.106-135.878  1.00138.74           N  
ANISOU 5990  N   ALA A 804    23458  15773  13481   -239   -945   3748       N  
ATOM   5991  CA  ALA A 804     -51.628  -7.223-135.268  1.00137.99           C  
ANISOU 5991  CA  ALA A 804    23272  15695  13463    -90   -808   3673       C  
ATOM   5992  C   ALA A 804     -50.849  -7.784-134.091  1.00137.49           C  
ANISOU 5992  C   ALA A 804    23102  15721  13414    -71   -745   3753       C  
ATOM   5993  O   ALA A 804     -51.416  -8.009-133.023  1.00139.51           O  
ANISOU 5993  O   ALA A 804    23354  15956  13694     16   -735   3697       O  
ATOM   5994  CB  ALA A 804     -51.908  -8.315-136.285  1.00139.44           C  
ANISOU 5994  CB  ALA A 804    23378  15906  13694    -47   -647   3644       C  
ATOM   5995  N   THR A 805     -49.549  -7.996-134.290  1.00137.03           N  
ANISOU 5995  N   THR A 805    22948  15792  13326   -148   -704   3886       N  
ATOM   5996  CA  THR A 805     -48.686  -8.553-133.245  1.00137.94           C  
ANISOU 5996  CA  THR A 805    22942  16037  13431   -113   -638   3978       C  
ATOM   5997  C   THR A 805     -48.338  -7.528-132.164  1.00138.67           C  
ANISOU 5997  C   THR A 805    23082  16142  13463   -206   -793   4009       C  
ATOM   5998  O   THR A 805     -47.803  -7.885-131.111  1.00137.40           O  
ANISOU 5998  O   THR A 805    22828  16086  13290   -169   -757   4068       O  
ATOM   5999  CB  THR A 805     -47.392  -9.160-133.821  1.00137.51           C  
ANISOU 5999  CB  THR A 805    22743  16175  13329   -131   -536   4115       C  
ATOM   6000  OG1 THR A 805     -46.660  -8.152-134.526  1.00141.57           O  
ANISOU 6000  OG1 THR A 805    23269  16765  13755   -320   -658   4191       O  
ATOM   6001  CG2 THR A 805     -47.711 -10.313-134.765  1.00138.39           C  
ANISOU 6001  CG2 THR A 805    22833  16258  13489    -12   -367   4078       C  
ATOM   6002  N   ALA A 806     -48.649  -6.261-132.436  1.00139.15           N  
ANISOU 6002  N   ALA A 806    23308  16087  13472   -320   -966   3970       N  
ATOM   6003  CA  ALA A 806     -48.465  -5.181-131.468  1.00138.40           C  
ANISOU 6003  CA  ALA A 806    23330  15951  13302   -415  -1131   3976       C  
ATOM   6004  C   ALA A 806     -49.615  -5.121-130.467  1.00137.97           C  
ANISOU 6004  C   ALA A 806    23357  15777  13288   -258  -1162   3849       C  
ATOM   6005  O   ALA A 806     -49.426  -4.682-129.332  1.00144.74           O  
ANISOU 6005  O   ALA A 806    24250  16639  14102   -276  -1241   3855       O  
ATOM   6006  CB  ALA A 806     -48.313  -3.846-132.175  1.00138.04           C  
ANISOU 6006  CB  ALA A 806    23487  15802  13160   -598  -1306   3988       C  
ATOM   6007  N   LEU A 807     -50.799  -5.561-130.892  1.00133.07           N  
ANISOU 6007  N   LEU A 807    22752  15074  12731   -111  -1099   3735       N  
ATOM   6008  CA  LEU A 807     -51.979  -5.583-130.023  1.00128.66           C  
ANISOU 6008  CA  LEU A 807    22237  14458  12190     45  -1116   3613       C  
ATOM   6009  C   LEU A 807     -51.868  -6.605-128.889  1.00127.64           C  
ANISOU 6009  C   LEU A 807    21954  14429  12114    127   -993   3634       C  
ATOM   6010  O   LEU A 807     -52.572  -6.502-127.886  1.00128.06           O  
ANISOU 6010  O   LEU A 807    22029  14469  12159    226  -1027   3561       O  
ATOM   6011  CB  LEU A 807     -53.257  -5.830-130.829  1.00125.54           C  
ANISOU 6011  CB  LEU A 807    21866  14012  11819    155  -1075   3493       C  
ATOM   6012  CG  LEU A 807     -53.709  -4.797-131.860  1.00123.53           C  
ANISOU 6012  CG  LEU A 807    21783  13651  11499    139  -1202   3443       C  
ATOM   6013  CD1 LEU A 807     -54.940  -5.316-132.572  1.00124.43           C  
ANISOU 6013  CD1 LEU A 807    21854  13789  11635    255  -1126   3332       C  
ATOM   6014  CD2 LEU A 807     -53.999  -3.442-131.239  1.00124.49           C  
ANISOU 6014  CD2 LEU A 807    22127  13657  11516    174  -1399   3396       C  
ATOM   6015  N   GLY A 808     -50.985  -7.587-129.051  1.00126.13           N  
ANISOU 6015  N   GLY A 808    21616  14345  11962    104   -851   3738       N  
ATOM   6016  CA  GLY A 808     -50.687  -8.532-127.977  1.00129.73           C  
ANISOU 6016  CA  GLY A 808    21949  14894  12447    185   -736   3784       C  
ATOM   6017  C   GLY A 808     -49.900  -7.882-126.850  1.00131.75           C  
ANISOU 6017  C   GLY A 808    22193  15224  12642    127   -838   3852       C  
ATOM   6018  O   GLY A 808     -49.610  -8.517-125.833  1.00129.47           O  
ANISOU 6018  O   GLY A 808    21806  15024  12362    198   -765   3896       O  
ATOM   6019  N   PHE A 809     -49.564  -6.608-127.035  1.00133.93           N  
ANISOU 6019  N   PHE A 809    22588  15457  12841    -10  -1010   3861       N  
ATOM   6020  CA  PHE A 809     -48.755  -5.865-126.078  1.00135.57           C  
ANISOU 6020  CA  PHE A 809    22814  15733  12964   -120  -1126   3924       C  
ATOM   6021  C   PHE A 809     -49.459  -4.634-125.506  1.00136.19           C  
ANISOU 6021  C   PHE A 809    23111  15654  12979   -131  -1312   3821       C  
ATOM   6022  O   PHE A 809     -48.867  -3.905-124.709  1.00140.00           O  
ANISOU 6022  O   PHE A 809    23657  16162  13375   -241  -1427   3857       O  
ATOM   6023  CB  PHE A 809     -47.417  -5.468-126.710  1.00136.72           C  
ANISOU 6023  CB  PHE A 809    22916  16007  13025   -329  -1166   4059       C  
ATOM   6024  CG  PHE A 809     -46.497  -6.630-126.966  1.00139.02           C  
ANISOU 6024  CG  PHE A 809    22973  16515  13331   -285   -993   4179       C  
ATOM   6025  CD1 PHE A 809     -45.680  -7.127-125.955  1.00140.87           C  
ANISOU 6025  CD1 PHE A 809    23046  16951  13525   -251   -935   4273       C  
ATOM   6026  CD2 PHE A 809     -46.446  -7.230-128.217  1.00139.87           C  
ANISOU 6026  CD2 PHE A 809    23032  16634  13477   -253   -887   4199       C  
ATOM   6027  CE1 PHE A 809     -44.828  -8.195-126.189  1.00141.62           C  
ANISOU 6027  CE1 PHE A 809    22944  17256  13606   -162   -775   4386       C  
ATOM   6028  CE2 PHE A 809     -45.599  -8.303-128.455  1.00141.71           C  
ANISOU 6028  CE2 PHE A 809    23079  17063  13702   -172   -727   4306       C  
ATOM   6029  CZ  PHE A 809     -44.789  -8.786-127.440  1.00140.67           C  
ANISOU 6029  CZ  PHE A 809    22797  17133  13518   -113   -671   4401       C  
ATOM   6030  N   ASN A 810     -50.711  -4.401-125.901  1.00135.05           N  
ANISOU 6030  N   ASN A 810    23089  15362  12858     -8  -1342   3692       N  
ATOM   6031  CA  ASN A 810     -51.465  -3.260-125.367  1.00134.53           C  
ANISOU 6031  CA  ASN A 810    23251  15153  12711     46  -1514   3584       C  
ATOM   6032  C   ASN A 810     -51.974  -3.487-123.939  1.00135.19           C  
ANISOU 6032  C   ASN A 810    23286  15283  12795    190  -1507   3525       C  
ATOM   6033  O   ASN A 810     -52.415  -4.586-123.609  1.00133.71           O  
ANISOU 6033  O   ASN A 810    22918  15193  12690    310  -1359   3510       O  
ATOM   6034  CB  ASN A 810     -52.577  -2.787-126.322  1.00131.91           C  
ANISOU 6034  CB  ASN A 810    23073  14684  12362    150  -1567   3473       C  
ATOM   6035  CG  ASN A 810     -53.556  -3.878-126.691  1.00129.42           C  
ANISOU 6035  CG  ASN A 810    22595  14440  12138    307  -1411   3405       C  
ATOM   6036  OD1 ASN A 810     -53.926  -4.710-125.869  1.00132.17           O  
ANISOU 6036  OD1 ASN A 810    22797  14884  12534    404  -1311   3383       O  
ATOM   6037  ND2 ASN A 810     -54.002  -3.862-127.937  1.00127.24           N  
ANISOU 6037  ND2 ASN A 810    22353  14119  11870    314  -1394   3372       N  
ATOM   6038  N   PRO A 811     -51.887  -2.450-123.085  1.00140.93           N  
ANISOU 6038  N   PRO A 811    24191  15938  13418    166  -1667   3494       N  
ATOM   6039  CA  PRO A 811     -52.135  -2.574-121.645  1.00144.06           C  
ANISOU 6039  CA  PRO A 811    24539  16399  13798    273  -1675   3455       C  
ATOM   6040  C   PRO A 811     -53.556  -3.000-121.279  1.00140.75           C  
ANISOU 6040  C   PRO A 811    24071  16001  13406    523  -1622   3328       C  
ATOM   6041  O   PRO A 811     -54.493  -2.717-122.036  1.00135.26           O  
ANISOU 6041  O   PRO A 811    23469  15233  12690    628  -1651   3237       O  
ATOM   6042  CB  PRO A 811     -51.845  -1.161-121.119  1.00150.85           C  
ANISOU 6042  CB  PRO A 811    25680  17125  14511    184  -1885   3428       C  
ATOM   6043  CG  PRO A 811     -50.908  -0.578-122.119  1.00150.95           C  
ANISOU 6043  CG  PRO A 811    25807  17071  14475    -63  -1951   3518       C  
ATOM   6044  CD  PRO A 811     -51.427  -1.093-123.428  1.00147.05           C  
ANISOU 6044  CD  PRO A 811    25246  16558  14067      4  -1855   3504       C  
ATOM   6045  N   PRO A 812     -53.708  -3.676-120.117  1.00139.07           N  
ANISOU 6045  N   PRO A 812    23702  15914  13221    610  -1547   3327       N  
ATOM   6046  CA  PRO A 812     -54.971  -4.251-119.659  1.00136.35           C  
ANISOU 6046  CA  PRO A 812    23263  15652  12892    809  -1476   3227       C  
ATOM   6047  C   PRO A 812     -56.083  -3.223-119.671  1.00133.86           C  
ANISOU 6047  C   PRO A 812    23139  15262  12460    977  -1621   3084       C  
ATOM   6048  O   PRO A 812     -55.890  -2.106-119.194  1.00133.68           O  
ANISOU 6048  O   PRO A 812    23331  15133  12329    990  -1785   3051       O  
ATOM   6049  CB  PRO A 812     -54.666  -4.690-118.219  1.00138.96           C  
ANISOU 6049  CB  PRO A 812    23471  16100  13225    836  -1437   3264       C  
ATOM   6050  CG  PRO A 812     -53.409  -3.982-117.843  1.00142.19           C  
ANISOU 6050  CG  PRO A 812    23967  16471  13585    679  -1540   3348       C  
ATOM   6051  CD  PRO A 812     -52.642  -3.879-119.121  1.00141.12           C  
ANISOU 6051  CD  PRO A 812    23867  16272  13478    511  -1532   3428       C  
ATOM   6052  N   ASP A 813     -57.231  -3.616-120.219  1.00133.57           N  
ANISOU 6052  N   ASP A 813    23034  15292  12423   1107  -1560   3000       N  
ATOM   6053  CA  ASP A 813     -58.357  -2.711-120.445  1.00132.49           C  
ANISOU 6053  CA  ASP A 813    23055  15128  12154   1307  -1683   2866       C  
ATOM   6054  C   ASP A 813     -58.844  -2.025-119.165  1.00133.88           C  
ANISOU 6054  C   ASP A 813    23325  15340  12203   1490  -1799   2781       C  
ATOM   6055  O   ASP A 813     -58.537  -2.458-118.048  1.00132.07           O  
ANISOU 6055  O   ASP A 813    22980  15199  12002   1469  -1756   2814       O  
ATOM   6056  CB  ASP A 813     -59.503  -3.443-121.153  1.00130.21           C  
ANISOU 6056  CB  ASP A 813    22608  14991  11876   1398  -1574   2799       C  
ATOM   6057  CG  ASP A 813     -60.307  -2.531-122.065  1.00128.21           C  
ANISOU 6057  CG  ASP A 813    22523  14687  11503   1547  -1685   2704       C  
ATOM   6058  OD1 ASP A 813     -60.411  -1.320-121.779  1.00127.96           O  
ANISOU 6058  OD1 ASP A 813    22741  14538  11340   1682  -1855   2648       O  
ATOM   6059  OD2 ASP A 813     -60.845  -3.031-123.073  1.00128.54           O  
ANISOU 6059  OD2 ASP A 813    22465  14805  11570   1535  -1602   2684       O  
ATOM   6060  N   LEU A 814     -59.627  -0.968-119.352  1.00134.02           N  
ANISOU 6060  N   LEU A 814    23560  15294  12066   1692  -1942   2670       N  
ATOM   6061  CA  LEU A 814     -59.831   0.049-118.334  1.00137.02           C  
ANISOU 6061  CA  LEU A 814    24154  15615  12291   1862  -2100   2592       C  
ATOM   6062  C   LEU A 814     -60.777  -0.307-117.189  1.00138.75           C  
ANISOU 6062  C   LEU A 814    24204  16074  12438   2080  -2068   2509       C  
ATOM   6063  O   LEU A 814     -60.412  -0.162-116.021  1.00144.49           O  
ANISOU 6063  O   LEU A 814    24950  16809  13140   2084  -2108   2515       O  
ATOM   6064  CB  LEU A 814     -60.275   1.350-118.999  1.00139.71           C  
ANISOU 6064  CB  LEU A 814    24844  15772  12466   2028  -2270   2508       C  
ATOM   6065  CG  LEU A 814     -60.133   2.632-118.188  1.00144.89           C  
ANISOU 6065  CG  LEU A 814    25862  16241  12946   2147  -2465   2446       C  
ATOM   6066  CD1 LEU A 814     -58.669   2.995-117.983  1.00145.17           C  
ANISOU 6066  CD1 LEU A 814    26059  16066  13032   1826  -2524   2555       C  
ATOM   6067  CD2 LEU A 814     -60.871   3.739-118.914  1.00148.96           C  
ANISOU 6067  CD2 LEU A 814    26713  16610  13275   2391  -2606   2350       C  
ATOM   6068  N   ASP A 815     -61.983  -0.762-117.514  1.00137.44           N  
ANISOU 6068  N   ASP A 815    23866  16131  12225   2248  -1999   2433       N  
ATOM   6069  CA  ASP A 815     -62.997  -0.999-116.486  1.00139.12           C  
ANISOU 6069  CA  ASP A 815    23917  16616  12325   2466  -1983   2347       C  
ATOM   6070  C   ASP A 815     -63.272  -2.472-116.192  1.00136.81           C  
ANISOU 6070  C   ASP A 815    23261  16576  12142   2337  -1786   2397       C  
ATOM   6071  O   ASP A 815     -64.267  -2.802-115.543  1.00139.64           O  
ANISOU 6071  O   ASP A 815    23443  17215  12396   2486  -1752   2329       O  
ATOM   6072  CB  ASP A 815     -64.292  -0.259-116.836  1.00143.93           C  
ANISOU 6072  CB  ASP A 815    24614  17354  12718   2797  -2077   2210       C  
ATOM   6073  CG  ASP A 815     -64.335   1.145-116.256  1.00148.88           C  
ANISOU 6073  CG  ASP A 815    25594  17818  13154   3049  -2279   2125       C  
ATOM   6074  OD1 ASP A 815     -64.543   1.278-115.030  1.00152.42           O  
ANISOU 6074  OD1 ASP A 815    26021  18375  13516   3186  -2317   2080       O  
ATOM   6075  OD2 ASP A 815     -64.171   2.116-117.025  1.00150.38           O  
ANISOU 6075  OD2 ASP A 815    26103  17764  13269   3112  -2401   2104       O  
ATOM   6076  N   ILE A 816     -62.367  -3.343-116.639  1.00131.98           N  
ANISOU 6076  N   ILE A 816    22554  15868  11721   2061  -1660   2518       N  
ATOM   6077  CA  ILE A 816     -62.534  -4.803-116.546  1.00125.58           C  
ANISOU 6077  CA  ILE A 816    21465  15232  11014   1913  -1465   2578       C  
ATOM