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***  CELL CYCLE 19-FEB-15 4YC6  ***

elNémo ID: 21041915160580634

Job options:

ID        	=	 21041915160580634
JOBID     	=	 CELL CYCLE 19-FEB-15 4YC6
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    CELL CYCLE                              19-FEB-15   4YC6              
TITLE     CDK1/CKS1                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN-DEPENDENT KINASE 1;                                 
COMPND   3 CHAIN: A, C, E, G;                                                   
COMPND   4 SYNONYM: CDK1,CELL DIVISION CONTROL PROTEIN 2 HOMOLOG,CELL DIVISION  
COMPND   5 PROTEIN KINASE 1,P34 PROTEIN KINASE;                                 
COMPND   6 EC: 2.7.11.22,2.7.11.23;                                             
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CYCLIN-DEPENDENT KINASES REGULATORY SUBUNIT 1;             
COMPND  10 CHAIN: B, D, F, H;                                                   
COMPND  11 SYNONYM: CKS-1;                                                      
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CDK1, CDC2, CDC28A, CDKN1, P34CDC2;                            
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: CKS1B, CKS1, PNAS-143, PNAS-16;                                
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    CDK1, CYCLIN B1, CKS2, CELL CYCLE                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.R.BROWN,S.KOROLCHUK,M.P.MARTIN,W.STANLEY,R.MOUKHAMETZIANOV,         
AUTHOR   2 M.E.M.NOBLE,J.A.ENDICOTT                                             
REVDAT   2   30-AUG-17 4YC6    1       REMARK ATOM                              
REVDAT   1   20-MAY-15 4YC6    0                                                
JRNL        AUTH   N.R.BROWN,S.KOROLCHUK,M.P.MARTIN,W.A.STANLEY,                
JRNL        AUTH 2 R.MOUKHAMETZIANOV,M.E.NOBLE,J.A.ENDICOTT                     
JRNL        TITL   CDK1 STRUCTURES REVEAL CONSERVED AND UNIQUE FEATURES OF THE  
JRNL        TITL 2 ESSENTIAL CELL CYCLE CDK.                                    
JRNL        REF    NAT COMMUN                    V.   6  6769 2015              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   25864384                                                     
JRNL        DOI    10.1038/NCOMMS7769                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0103                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 75.09                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 50430                          
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) : 0.227                           
REMARK   3   R VALUE            (WORKING SET) : 0.225                           
REMARK   3   FREE R VALUE                     : 0.267                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1787                            
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3068                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 79.71                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3910                       
REMARK   3   BIN FREE R VALUE SET COUNT          : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11632                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 639                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 95.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.71000                                             
REMARK   3    B22 (A**2) : 4.54000                                              
REMARK   3    B33 (A**2) : -2.67000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -2.01000                                             
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): 0.357         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.912                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 11998 ; 0.016 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 11516 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 16234 ; 1.855 ; 1.970       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 26586 ; 3.625 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1418 ;10.050 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   564 ;40.943 ;23.830       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2168 ;19.959 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    72 ;19.758 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1752 ; 0.108 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 13234 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2734 ; 0.012 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5702 ; 2.296 ; 3.245       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  5701 ; 2.293 ; 3.244       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7110 ; 3.943 ; 4.843       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 11                                         
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 :   B     5        B    73                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.4780  20.3230  -8.3350              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3356 T22:   0.0852                                     
REMARK   3      T33:   0.6600 T12:   0.0919                                     
REMARK   3      T13:   0.0031 T23:  -0.0867                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1143 L22:   7.3283                                     
REMARK   3      L33:   6.2393 L12:   1.8715                                     
REMARK   3      L13:  -0.8600 L23:  -0.3091                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2966 S12:   0.5951 S13:   0.0656                       
REMARK   3      S21:  -0.1403 S22:  -0.0587 S23:   0.8259                       
REMARK   3      S31:  -0.0012 S32:  -0.2544 S33:  -0.2379                       
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 :   D     5        D    73                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.0260   7.1540  -6.9250              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3158 T22:   0.0342                                     
REMARK   3      T33:   0.5019 T12:   0.0330                                     
REMARK   3      T13:   0.0391 T23:   0.0570                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.4759 L22:   8.4019                                     
REMARK   3      L33:   7.1468 L12:   1.2593                                     
REMARK   3      L13:   1.9605 L23:  -0.3807                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0654 S12:   0.3388 S13:  -0.2120                       
REMARK   3      S21:  -0.2510 S22:  -0.2116 S23:  -0.7360                       
REMARK   3      S31:   0.0990 S32:   0.2930 S33:   0.2770                       
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 :   F     5        F    73                          
REMARK   3    ORIGIN FOR THE GROUP (A): -31.2120  11.7790 -37.2560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9955 T22:   0.2549                                     
REMARK   3      T33:   1.4835 T12:  -0.1209                                     
REMARK   3      T13:  -0.2194 T23:  -0.3377                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.7432 L22:   3.9140                                     
REMARK   3      L33:   8.1139 L12:  -2.1225                                     
REMARK   3      L13:   1.5170 L23:  -1.0161                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5183 S12:  -1.0175 S13:   1.0106                       
REMARK   3      S21:  -0.0305 S22:   0.1464 S23:   0.9561                       
REMARK   3      S31:   0.0344 S32:  -0.8990 S33:   0.3720                       
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 :   H     5        H    73                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.1610  10.1730 -35.9530              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8674 T22:   0.1083                                     
REMARK   3      T33:   0.4886 T12:  -0.1540                                     
REMARK   3      T13:   0.2374 T23:  -0.0451                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.9332 L22:   9.3506                                     
REMARK   3      L33:   7.7061 L12:   0.2738                                     
REMARK   3      L13:  -2.9644 L23:   0.4824                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5512 S12:  -0.4404 S13:  -0.3769                       
REMARK   3      S21:  -0.0244 S22:   0.4193 S23:  -0.6783                       
REMARK   3      S31:  -0.2555 S32:   0.6719 S33:   0.1318                       
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 :   G     1        G   290                          
REMARK   3    ORIGIN FOR THE GROUP (A): -16.3160  34.7910 -43.6500              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8946 T22:   0.0727                                     
REMARK   3      T33:   0.7128 T12:  -0.2148                                     
REMARK   3      T13:  -0.3032 T23:   0.1549                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3471 L22:   4.8951                                     
REMARK   3      L33:   1.9985 L12:  -0.7259                                     
REMARK   3      L13:  -0.9761 L23:   1.9935                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5106 S12:   0.0699 S13:   0.0055                       
REMARK   3      S21:  -1.9045 S22:   0.2754 S23:   0.8446                       
REMARK   3      S31:  -0.9919 S32:  -0.0415 S33:   0.2351                       
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 :   A     1        A    80                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.7860  34.9610 -21.5500              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7965 T22:   0.1603                                     
REMARK   3      T33:   0.8023 T12:   0.0650                                     
REMARK   3      T13:   0.1146 T23:  -0.0679                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6995 L22:   2.8678                                     
REMARK   3      L33:   9.9060 L12:  -1.4620                                     
REMARK   3      L13:   3.1806 L23:  -1.6392                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2701 S12:   0.9214 S13:  -0.4019                       
REMARK   3      S21:  -0.9453 S22:  -0.3280 S23:  -0.2686                       
REMARK   3      S31:   0.3662 S32:   0.7821 S33:   0.0578                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    81        A   289                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.9100  35.1360  -0.0770              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6513 T22:   0.0719                                     
REMARK   3      T33:   0.3965 T12:  -0.0102                                     
REMARK   3      T13:   0.0473 T23:  -0.1127                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6119 L22:   4.7014                                     
REMARK   3      L33:   1.5002 L12:   1.1687                                     
REMARK   3      L13:  -1.0431 L23:  -0.6080                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2198 S12:  -0.4867 S13:   0.3547                       
REMARK   3      S21:   0.5691 S22:  -0.2437 S23:   0.0959                       
REMARK   3      S31:  -0.3479 S32:   0.0928 S33:   0.0239                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C    80                          
REMARK   3    ORIGIN FOR THE GROUP (A): -39.1320  -9.7040 -16.8370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7187 T22:   0.3940                                     
REMARK   3      T33:   0.8816 T12:  -0.1461                                     
REMARK   3      T13:  -0.0068 T23:  -0.0291                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2846 L22:   0.9898                                     
REMARK   3      L33:   8.3134 L12:  -1.0554                                     
REMARK   3      L13:  -2.4246 L23:   2.8236                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2083 S12:   1.0148 S13:   0.2950                       
REMARK   3      S21:  -0.1197 S22:  -0.2151 S23:   0.1155                       
REMARK   3      S31:  -0.0458 S32:  -0.6613 S33:   0.4235                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    81        C   289                          
REMARK   3    ORIGIN FOR THE GROUP (A): -22.5080  -5.4760   4.3400              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6154 T22:   0.0576                                     
REMARK   3      T33:   0.3335 T12:  -0.0455                                     
REMARK   3      T13:   0.0458 T23:   0.0095                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9671 L22:   3.9647                                     
REMARK   3      L33:   1.2069 L12:   0.5212                                     
REMARK   3      L13:  -0.5636 L23:  -0.1709                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0589 S12:  -0.0841 S13:  -0.0693                       
REMARK   3      S21:   0.4888 S22:  -0.1924 S23:   0.1368                       
REMARK   3      S31:   0.1715 S32:  -0.2063 S33:   0.1334                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     1        E    80                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.9040 -18.3660 -21.8340              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2505 T22:   0.2427                                     
REMARK   3      T33:   0.8434 T12:  -0.1204                                     
REMARK   3      T13:  -0.0573 T23:  -0.1774                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6917 L22:   1.7213                                     
REMARK   3      L33:  11.4434 L12:  -2.0101                                     
REMARK   3      L13:  -5.5387 L23:  -0.4397                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3500 S12:  -0.6572 S13:   0.3437                       
REMARK   3      S21:  -0.0680 S22:   0.1345 S23:  -0.2117                       
REMARK   3      S31:   0.9980 S32:   0.6325 S33:   0.2155                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E    81        E   289                          
REMARK   3    ORIGIN FOR THE GROUP (A): -15.6030 -11.6130 -44.3300              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2465 T22:   0.0742                                     
REMARK   3      T33:   0.4541 T12:  -0.2590                                     
REMARK   3      T13:  -0.0258 T23:  -0.0676                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5911 L22:   5.3926                                     
REMARK   3      L33:   3.5665 L12:  -0.1960                                     
REMARK   3      L13:   2.5288 L23:   0.3100                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1360 S12:   0.0971 S13:  -0.0384                       
REMARK   3      S21:  -1.0008 S22:  -0.0168 S23:   0.4851                       
REMARK   3      S31:   0.6956 S32:  -0.1129 S33:  -0.1192                       
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 4YC6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-FEB-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000207190.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-DEC-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.2-8.4                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50462                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 75.090                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : 0.09400                            
REMARK 200  R SYM                      (I) : 0.08400                            
REMARK 200   FOR THE DATA SET  : 16.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.68                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 2.08000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.970                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16-18% PEG 10 000, 0.1M IMIDAZOLE PH     
REMARK 280  8.2 -8.4, PH 8.3, VAPOR DIFFUSION, TEMPERATURE 277K                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       73.76550            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.                         
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1450 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1440 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18180 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1460 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1460 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18130 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
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     ILE A   155                                                      
REMARK 465     PRO A   156                                                      
REMARK 465     ILE A   157                                                      
REMARK 465     ARG A   158                                                      
REMARK 465     LEU A   290                                                      
REMARK 465     ASP A   291                                                      
REMARK 465     ASN A   292                                                      
REMARK 465     GLN A   293                                                      
REMARK 465     ILE A   294                                                      
REMARK 465     LYS A   295                                                      
REMARK 465     LYS A   296                                                      
REMARK 465     MET A   297                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     LYS B     4                                                      
REMARK 465     LYS B    75                                                      
REMARK 465     LYS B    76                                                      
REMARK 465     PRO B    77                                                      
REMARK 465     LYS B    78                                                      
REMARK 465     LYS B    79                                                      
REMARK 465     HIS B    80                                                      
REMARK 465     HIS B    81                                                      
REMARK 465     HIS B    82                                                      
REMARK 465     HIS B    83                                                      
REMARK 465     HIS B    84                                                      
REMARK 465     HIS B    85                                                      
REMARK 465     ILE C   155                                                      
REMARK 465     PRO C   156                                                      
REMARK 465     ILE C   157                                                      
REMARK 465     ARG C   158                                                      
REMARK 465     LEU C   290                                                      
REMARK 465     ASP C   291                                                      
REMARK 465     ASN C   292                                                      
REMARK 465     GLN C   293                                                      
REMARK 465     ILE C   294                                                      
REMARK 465     LYS C   295                                                      
REMARK 465     LYS C   296                                                      
REMARK 465     MET C   297                                                      
REMARK 465     MET D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     HIS D     3                                                      
REMARK 465     LYS D     4                                                      
REMARK 465     LYS D    75                                                      
REMARK 465     LYS D    76                                                      
REMARK 465     PRO D    77                                                      
REMARK 465     LYS D    78                                                      
REMARK 465     LYS D    79                                                      
REMARK 465     HIS D    80                                                      
REMARK 465     HIS D    81                                                      
REMARK 465     HIS D    82                                                      
REMARK 465     HIS D    83                                                      
REMARK 465     HIS D    84                                                      
REMARK 465     HIS D    85                                                      
REMARK 465     ILE E   155                                                      
REMARK 465     PRO E   156                                                      
REMARK 465     ILE E   157                                                      
REMARK 465     ARG E   158                                                      
REMARK 465     LEU E   290                                                      
REMARK 465     ASP E   291                                                      
REMARK 465     ASN E   292                                                      
REMARK 465     GLN E   293                                                      
REMARK 465     ILE E   294                                                      
REMARK 465     LYS E   295                                                      
REMARK 465     LYS E   296                                                      
REMARK 465     MET E   297                                                      
REMARK 465     MET F     1                                                      
REMARK 465     SER F     2                                                      
REMARK 465     HIS F     3                                                      
REMARK 465     LYS F     4                                                      
REMARK 465     LYS F    75                                                      
REMARK 465     LYS F    76                                                      
REMARK 465     PRO F    77                                                      
REMARK 465     LYS F    78                                                      
REMARK 465     LYS F    79                                                      
REMARK 465     HIS F    80                                                      
REMARK 465     HIS F    81                                                      
REMARK 465     HIS F    82                                                      
REMARK 465     HIS F    83                                                      
REMARK 465     HIS F    84                                                      
REMARK 465     HIS F    85                                                      
REMARK 465     ILE G   155                                                      
REMARK 465     PRO G   156                                                      
REMARK 465     ILE G   157                                                      
REMARK 465     ARG G   158                                                      
REMARK 465     LEU G   290                                                      
REMARK 465     ASP G   291                                                      
REMARK 465     ASN G   292                                                      
REMARK 465     GLN G   293                                                      
REMARK 465     ILE G   294                                                      
REMARK 465     LYS G   295                                                      
REMARK 465     LYS G   296                                                      
REMARK 465     MET G   297                                                      
REMARK 465     MET H     1                                                      
REMARK 465     SER H     2                                                      
REMARK 465     HIS H     3                                                      
REMARK 465     LYS H     4                                                      
REMARK 465     LYS H    75                                                      
REMARK 465     LYS H    76                                                      
REMARK 465     PRO H    77                                                      
REMARK 465     LYS H    78                                                      
REMARK 465     LYS H    79                                                      
REMARK 465     HIS H    80                                                      
REMARK 465     HIS H    81                                                      
REMARK 465     HIS H    82                                                      
REMARK 465     HIS H    83                                                      
REMARK 465     HIS H    84                                                      
REMARK 465     HIS H    85                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ILE G   193     O    HOH G   301              1.68            
REMARK 500   O    TRP G   188     O    HOH G   302              1.75            
REMARK 500   O    PHE F    17     O    HOH F   101              1.92            
REMARK 500   N    MET C     1     O    HOH C   301              2.00            
REMARK 500   O    PHE G   194     O    HOH G   301              2.08            
REMARK 500   O    LYS G    24     O    HOH G   303              2.08            
REMARK 500   N    LEU G   197     O    HOH G   301              2.09            
REMARK 500   OD2  ASP A    73     O    SER G   233              2.10            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ASP B  27   CA    ASP B  27   C       0.162                       
REMARK 500    ASP D  27   CA    ASP D  27   C       0.161                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 123   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A 218   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG B  20   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ASP B  27   CB  -  CA  -  C   ANGL. DEV. =  12.5 DEGREES          
REMARK 500    ARG C 123   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG C 218   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG D  20   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500    ASP D  27   CB  -  CA  -  C   ANGL. DEV. =  12.9 DEGREES          
REMARK 500    ARG D  71   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG D  71   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ARG E 123   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG E 151   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG E 218   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG F  20   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ARG G 218   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG H  20   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    ARG H  71   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ILE A  10       35.31   -145.56                                   
REMARK 500    THR A  14      -40.65     50.20                                   
REMARK 500    TYR A  15      -80.16    -87.18                                   
REMARK 500    GLU A  42      -73.72    -39.13                                   
REMARK 500    VAL A  44      103.80    -36.62                                   
REMARK 500    HIS A  60      147.14   -173.14                                   
REMARK 500    GLN A  72     -155.08   -106.12                                   
REMARK 500    SER A  74       18.16     52.39                                   
REMARK 500    SER A 121      -68.97     40.74                                   
REMARK 500    ARG A 127      -55.74     89.41                                   
REMARK 500    ASP A 128       44.69    -95.97                                   
REMARK 500    PHE A 153      -91.09   -130.44                                   
REMARK 500    GLU A 163      -70.14    -70.89                                   
REMARK 500    SER A 182     -154.24   -154.89                                   
REMARK 500    LYS A 200      -17.50     73.93                                   
REMARK 500    HIS A 205       58.81   -102.73                                   
REMARK 500    SER A 248       67.32     71.71                                   
REMARK 500    ASN A 255       38.69     78.22                                   
REMARK 500    ASP A 257      170.02    -59.64                                   
REMARK 500    LYS B  26      -87.70    -61.33                                   
REMARK 500    ASP B  27      -40.90     10.70                                   
REMARK 500    ASP B  27       36.28    -67.57                                   
REMARK 500    ILE C  10       35.58   -146.50                                   
REMARK 500    THR C  14      -41.38     49.63                                   
REMARK 500    TYR C  15      -81.21    -86.75                                   
REMARK 500    GLU C  42      -74.28    -38.17                                   
REMARK 500    VAL C  44      102.58    -35.46                                   
REMARK 500    GLN C  72     -153.18   -104.33                                   
REMARK 500    SER C  74       18.59     51.30                                   
REMARK 500    SER C 121      -68.62     40.59                                   
REMARK 500    ARG C 127      -54.95     86.32                                   
REMARK 500    ASP C 128       44.39    -97.33                                   
REMARK 500    PHE C 153      -90.17   -132.96                                   
REMARK 500    GLU C 163      -70.23    -71.55                                   
REMARK 500    SER C 182     -156.23   -150.10                                   
REMARK 500    LYS C 200      -18.43     73.71                                   
REMARK 500    HIS C 205       61.96   -103.05                                   
REMARK 500    PHE C 241      150.53    -49.18                                   
REMARK 500    SER C 248       67.60     70.76                                   
REMARK 500    ASN C 255       38.80     78.14                                   
REMARK 500    ASP C 257      170.68    -59.54                                   
REMARK 500    LYS D  26      -87.61    -60.47                                   
REMARK 500    ASP D  27      -41.16     10.55                                   
REMARK 500    ASP D  27       35.80    -68.14                                   
REMARK 500    ILE E  10       34.92   -145.53                                   
REMARK 500    THR E  14      -41.28     49.95                                   
REMARK 500    TYR E  15      -80.38    -85.54                                   
REMARK 500    GLU E  42      -73.81    -39.52                                   
REMARK 500    VAL E  44      104.80    -36.27                                   
REMARK 500    HIS E  60      146.37   -174.44                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      90 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 HIS A  120     SER A  121                   91.42                    
REMARK 500 GLY A  247     SER A  248                   34.30                    
REMARK 500 LYS B   26     ASP B   27                  143.61                    
REMARK 500 ASP B   27     ILE B   28                  144.73                    
REMARK 500 HIS C  120     SER C  121                   90.21                    
REMARK 500 GLY C  247     SER C  248                   34.68                    
REMARK 500 LYS D   26     ASP D   27                  143.90                    
REMARK 500 ASP D   27     ILE D   28                  144.17                    
REMARK 500 HIS E  120     SER E  121                   89.67                    
REMARK 500 GLY E  247     SER E  248                   34.94                    
REMARK 500 LYS F   26     ASP F   27                  142.64                    
REMARK 500 ASP F   27     ILE F   28                  144.66                    
REMARK 500 HIS G  120     SER G  121                   88.94                    
REMARK 500 GLY G  247     SER G  248                   34.97                    
REMARK 500 LYS H   26     ASP H   27                  142.91                    
REMARK 500 ASP H   27     ILE H   28                  148.38                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH E 428        DISTANCE =  5.81 ANGSTROMS                       
DBREF  4YC6 A    1   297  UNP    P06493   CDK1_HUMAN       1    297             
DBREF  4YC6 B    1    79  UNP    P61024   CKS1_HUMAN       1     79             
DBREF  4YC6 C    1   297  UNP    P06493   CDK1_HUMAN       1    297             
DBREF  4YC6 D    1    79  UNP    P61024   CKS1_HUMAN       1     79             
DBREF  4YC6 E    1   297  UNP    P06493   CDK1_HUMAN       1    297             
DBREF  4YC6 F    1    79  UNP    P61024   CKS1_HUMAN       1     79             
DBREF  4YC6 G    1   297  UNP    P06493   CDK1_HUMAN       1    297             
DBREF  4YC6 H    1    79  UNP    P61024   CKS1_HUMAN       1     79             
SEQADV 4YC6 HIS B   80  UNP  P61024              EXPRESSION TAG                 
SEQADV 4YC6 HIS B   81  UNP  P61024              EXPRESSION TAG                 
SEQADV 4YC6 HIS B   82  UNP  P61024              EXPRESSION TAG                 
SEQADV 4YC6 HIS B   83  UNP  P61024              EXPRESSION TAG                 
SEQADV 4YC6 HIS B   84  UNP  P61024              EXPRESSION TAG                 
SEQADV 4YC6 HIS B   85  UNP  P61024              EXPRESSION TAG                 
SEQADV 4YC6 HIS D   80  UNP  P61024              EXPRESSION TAG                 
SEQADV 4YC6 HIS D   81  UNP  P61024              EXPRESSION TAG                 
SEQADV 4YC6 HIS D   82  UNP  P61024              EXPRESSION TAG                 
SEQADV 4YC6 HIS D   83  UNP  P61024              EXPRESSION TAG                 
SEQADV 4YC6 HIS D   84  UNP  P61024              EXPRESSION TAG                 
SEQADV 4YC6 HIS D   85  UNP  P61024              EXPRESSION TAG                 
SEQADV 4YC6 HIS F   80  UNP  P61024              EXPRESSION TAG                 
SEQADV 4YC6 HIS F   81  UNP  P61024              EXPRESSION TAG                 
SEQADV 4YC6 HIS F   82  UNP  P61024              EXPRESSION TAG                 
SEQADV 4YC6 HIS F   83  UNP  P61024              EXPRESSION TAG                 
SEQADV 4YC6 HIS F   84  UNP  P61024              EXPRESSION TAG                 
SEQADV 4YC6 HIS F   85  UNP  P61024              EXPRESSION TAG                 
SEQADV 4YC6 HIS H   80  UNP  P61024              EXPRESSION TAG                 
SEQADV 4YC6 HIS H   81  UNP  P61024              EXPRESSION TAG                 
SEQADV 4YC6 HIS H   82  UNP  P61024              EXPRESSION TAG                 
SEQADV 4YC6 HIS H   83  UNP  P61024              EXPRESSION TAG                 
SEQADV 4YC6 HIS H   84  UNP  P61024              EXPRESSION TAG                 
SEQADV 4YC6 HIS H   85  UNP  P61024              EXPRESSION TAG                 
SEQRES   1 A  297  MET GLU ASP TYR THR LYS ILE GLU LYS ILE GLY GLU GLY          
SEQRES   2 A  297  THR TYR GLY VAL VAL TYR LYS GLY ARG HIS LYS THR THR          
SEQRES   3 A  297  GLY GLN VAL VAL ALA MET LYS LYS ILE ARG LEU GLU SER          
SEQRES   4 A  297  GLU GLU GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE          
SEQRES   5 A  297  SER LEU LEU LYS GLU LEU ARG HIS PRO ASN ILE VAL SER          
SEQRES   6 A  297  LEU GLN ASP VAL LEU MET GLN ASP SER ARG LEU TYR LEU          
SEQRES   7 A  297  ILE PHE GLU PHE LEU SER MET ASP LEU LYS LYS TYR LEU          
SEQRES   8 A  297  ASP SER ILE PRO PRO GLY GLN TYR MET ASP SER SER LEU          
SEQRES   9 A  297  VAL LYS SER TYR LEU TYR GLN ILE LEU GLN GLY ILE VAL          
SEQRES  10 A  297  PHE CYS HIS SER ARG ARG VAL LEU HIS ARG ASP LEU LYS          
SEQRES  11 A  297  PRO GLN ASN LEU LEU ILE ASP ASP LYS GLY THR ILE LYS          
SEQRES  12 A  297  LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY ILE PRO          
SEQRES  13 A  297  ILE ARG VAL TYR THR HIS GLU VAL VAL THR LEU TRP TYR          
SEQRES  14 A  297  ARG SER PRO GLU VAL LEU LEU GLY SER ALA ARG TYR SER          
SEQRES  15 A  297  THR PRO VAL ASP ILE TRP SER ILE GLY THR ILE PHE ALA          
SEQRES  16 A  297  GLU LEU ALA THR LYS LYS PRO LEU PHE HIS GLY ASP SER          
SEQRES  17 A  297  GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG ALA LEU GLY          
SEQRES  18 A  297  THR PRO ASN ASN GLU VAL TRP PRO GLU VAL GLU SER LEU          
SEQRES  19 A  297  GLN ASP TYR LYS ASN THR PHE PRO LYS TRP LYS PRO GLY          
SEQRES  20 A  297  SER LEU ALA SER HIS VAL LYS ASN LEU ASP GLU ASN GLY          
SEQRES  21 A  297  LEU ASP LEU LEU SER LYS MET LEU ILE TYR ASP PRO ALA          
SEQRES  22 A  297  LYS ARG ILE SER GLY LYS MET ALA LEU ASN HIS PRO TYR          
SEQRES  23 A  297  PHE ASN ASP LEU ASP ASN GLN ILE LYS LYS MET                  
SEQRES   1 B   85  MET SER HIS LYS GLN ILE TYR TYR SER ASP LYS TYR ASP          
SEQRES   2 B   85  ASP GLU GLU PHE GLU TYR ARG HIS VAL MET LEU PRO LYS          
SEQRES   3 B   85  ASP ILE ALA LYS LEU VAL PRO LYS THR HIS LEU MET SER          
SEQRES   4 B   85  GLU SER GLU TRP ARG ASN LEU GLY VAL GLN GLN SER GLN          
SEQRES   5 B   85  GLY TRP VAL HIS TYR MET ILE HIS GLU PRO GLU PRO HIS          
SEQRES   6 B   85  ILE LEU LEU PHE ARG ARG PRO LEU PRO LYS LYS PRO LYS          
SEQRES   7 B   85  LYS HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 C  297  MET GLU ASP TYR THR LYS ILE GLU LYS ILE GLY GLU GLY          
SEQRES   2 C  297  THR TYR GLY VAL VAL TYR LYS GLY ARG HIS LYS THR THR          
SEQRES   3 C  297  GLY GLN VAL VAL ALA MET LYS LYS ILE ARG LEU GLU SER          
SEQRES   4 C  297  GLU GLU GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE          
SEQRES   5 C  297  SER LEU LEU LYS GLU LEU ARG HIS PRO ASN ILE VAL SER          
SEQRES   6 C  297  LEU GLN ASP VAL LEU MET GLN ASP SER ARG LEU TYR LEU          
SEQRES   7 C  297  ILE PHE GLU PHE LEU SER MET ASP LEU LYS LYS TYR LEU          
SEQRES   8 C  297  ASP SER ILE PRO PRO GLY GLN TYR MET ASP SER SER LEU          
SEQRES   9 C  297  VAL LYS SER TYR LEU TYR GLN ILE LEU GLN GLY ILE VAL          
SEQRES  10 C  297  PHE CYS HIS SER ARG ARG VAL LEU HIS ARG ASP LEU LYS          
SEQRES  11 C  297  PRO GLN ASN LEU LEU ILE ASP ASP LYS GLY THR ILE LYS          
SEQRES  12 C  297  LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY ILE PRO          
SEQRES  13 C  297  ILE ARG VAL TYR THR HIS GLU VAL VAL THR LEU TRP TYR          
SEQRES  14 C  297  ARG SER PRO GLU VAL LEU LEU GLY SER ALA ARG TYR SER          
SEQRES  15 C  297  THR PRO VAL ASP ILE TRP SER ILE GLY THR ILE PHE ALA          
SEQRES  16 C  297  GLU LEU ALA THR LYS LYS PRO LEU PHE HIS GLY ASP SER          
SEQRES  17 C  297  GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG ALA LEU GLY          
SEQRES  18 C  297  THR PRO ASN ASN GLU VAL TRP PRO GLU VAL GLU SER LEU          
SEQRES  19 C  297  GLN ASP TYR LYS ASN THR PHE PRO LYS TRP LYS PRO GLY          
SEQRES  20 C  297  SER LEU ALA SER HIS VAL LYS ASN LEU ASP GLU ASN GLY          
SEQRES  21 C  297  LEU ASP LEU LEU SER LYS MET LEU ILE TYR ASP PRO ALA          
SEQRES  22 C  297  LYS ARG ILE SER GLY LYS MET ALA LEU ASN HIS PRO TYR          
SEQRES  23 C  297  PHE ASN ASP LEU ASP ASN GLN ILE LYS LYS MET                  
SEQRES   1 D   85  MET SER HIS LYS GLN ILE TYR TYR SER ASP LYS TYR ASP          
SEQRES   2 D   85  ASP GLU GLU PHE GLU TYR ARG HIS VAL MET LEU PRO LYS          
SEQRES   3 D   85  ASP ILE ALA LYS LEU VAL PRO LYS THR HIS LEU MET SER          
SEQRES   4 D   85  GLU SER GLU TRP ARG ASN LEU GLY VAL GLN GLN SER GLN          
SEQRES   5 D   85  GLY TRP VAL HIS TYR MET ILE HIS GLU PRO GLU PRO HIS          
SEQRES   6 D   85  ILE LEU LEU PHE ARG ARG PRO LEU PRO LYS LYS PRO LYS          
SEQRES   7 D   85  LYS HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 E  297  MET GLU ASP TYR THR LYS ILE GLU LYS ILE GLY GLU GLY          
SEQRES   2 E  297  THR TYR GLY VAL VAL TYR LYS GLY ARG HIS LYS THR THR          
SEQRES   3 E  297  GLY GLN VAL VAL ALA MET LYS LYS ILE ARG LEU GLU SER          
SEQRES   4 E  297  GLU GLU GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE          
SEQRES   5 E  297  SER LEU LEU LYS GLU LEU ARG HIS PRO ASN ILE VAL SER          
SEQRES   6 E  297  LEU GLN ASP VAL LEU MET GLN ASP SER ARG LEU TYR LEU          
SEQRES   7 E  297  ILE PHE GLU PHE LEU SER MET ASP LEU LYS LYS TYR LEU          
SEQRES   8 E  297  ASP SER ILE PRO PRO GLY GLN TYR MET ASP SER SER LEU          
SEQRES   9 E  297  VAL LYS SER TYR LEU TYR GLN ILE LEU GLN GLY ILE VAL          
SEQRES  10 E  297  PHE CYS HIS SER ARG ARG VAL LEU HIS ARG ASP LEU LYS          
SEQRES  11 E  297  PRO GLN ASN LEU LEU ILE ASP ASP LYS GLY THR ILE LYS          
SEQRES  12 E  297  LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY ILE PRO          
SEQRES  13 E  297  ILE ARG VAL TYR THR HIS GLU VAL VAL THR LEU TRP TYR          
SEQRES  14 E  297  ARG SER PRO GLU VAL LEU LEU GLY SER ALA ARG TYR SER          
SEQRES  15 E  297  THR PRO VAL ASP ILE TRP SER ILE GLY THR ILE PHE ALA          
SEQRES  16 E  297  GLU LEU ALA THR LYS LYS PRO LEU PHE HIS GLY ASP SER          
SEQRES  17 E  297  GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG ALA LEU GLY          
SEQRES  18 E  297  THR PRO ASN ASN GLU VAL TRP PRO GLU VAL GLU SER LEU          
SEQRES  19 E  297  GLN ASP TYR LYS ASN THR PHE PRO LYS TRP LYS PRO GLY          
SEQRES  20 E  297  SER LEU ALA SER HIS VAL LYS ASN LEU ASP GLU ASN GLY          
SEQRES  21 E  297  LEU ASP LEU LEU SER LYS MET LEU ILE TYR ASP PRO ALA          
SEQRES  22 E  297  LYS ARG ILE SER GLY LYS MET ALA LEU ASN HIS PRO TYR          
SEQRES  23 E  297  PHE ASN ASP LEU ASP ASN GLN ILE LYS LYS MET                  
SEQRES   1 F   85  MET SER HIS LYS GLN ILE TYR TYR SER ASP LYS TYR ASP          
SEQRES   2 F   85  ASP GLU GLU PHE GLU TYR ARG HIS VAL MET LEU PRO LYS          
SEQRES   3 F   85  ASP ILE ALA LYS LEU VAL PRO LYS THR HIS LEU MET SER          
SEQRES   4 F   85  GLU SER GLU TRP ARG ASN LEU GLY VAL GLN GLN SER GLN          
SEQRES   5 F   85  GLY TRP VAL HIS TYR MET ILE HIS GLU PRO GLU PRO HIS          
SEQRES   6 F   85  ILE LEU LEU PHE ARG ARG PRO LEU PRO LYS LYS PRO LYS          
SEQRES   7 F   85  LYS HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 G  297  MET GLU ASP TYR THR LYS ILE GLU LYS ILE GLY GLU GLY          
SEQRES   2 G  297  THR TYR GLY VAL VAL TYR LYS GLY ARG HIS LYS THR THR          
SEQRES   3 G  297  GLY GLN VAL VAL ALA MET LYS LYS ILE ARG LEU GLU SER          
SEQRES   4 G  297  GLU GLU GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE          
SEQRES   5 G  297  SER LEU LEU LYS GLU LEU ARG HIS PRO ASN ILE VAL SER          
SEQRES   6 G  297  LEU GLN ASP VAL LEU MET GLN ASP SER ARG LEU TYR LEU          
SEQRES   7 G  297  ILE PHE GLU PHE LEU SER MET ASP LEU LYS LYS TYR LEU          
SEQRES   8 G  297  ASP SER ILE PRO PRO GLY GLN TYR MET ASP SER SER LEU          
SEQRES   9 G  297  VAL LYS SER TYR LEU TYR GLN ILE LEU GLN GLY ILE VAL          
SEQRES  10 G  297  PHE CYS HIS SER ARG ARG VAL LEU HIS ARG ASP LEU LYS          
SEQRES  11 G  297  PRO GLN ASN LEU LEU ILE ASP ASP LYS GLY THR ILE LYS          
SEQRES  12 G  297  LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY ILE PRO          
SEQRES  13 G  297  ILE ARG VAL TYR THR HIS GLU VAL VAL THR LEU TRP TYR          
SEQRES  14 G  297  ARG SER PRO GLU VAL LEU LEU GLY SER ALA ARG TYR SER          
SEQRES  15 G  297  THR PRO VAL ASP ILE TRP SER ILE GLY THR ILE PHE ALA          
SEQRES  16 G  297  GLU LEU ALA THR LYS LYS PRO LEU PHE HIS GLY ASP SER          
SEQRES  17 G  297  GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG ALA LEU GLY          
SEQRES  18 G  297  THR PRO ASN ASN GLU VAL TRP PRO GLU VAL GLU SER LEU          
SEQRES  19 G  297  GLN ASP TYR LYS ASN THR PHE PRO LYS TRP LYS PRO GLY          
SEQRES  20 G  297  SER LEU ALA SER HIS VAL LYS ASN LEU ASP GLU ASN GLY          
SEQRES  21 G  297  LEU ASP LEU LEU SER LYS MET LEU ILE TYR ASP PRO ALA          
SEQRES  22 G  297  LYS ARG ILE SER GLY LYS MET ALA LEU ASN HIS PRO TYR          
SEQRES  23 G  297  PHE ASN ASP LEU ASP ASN GLN ILE LYS LYS MET                  
SEQRES   1 H   85  MET SER HIS LYS GLN ILE TYR TYR SER ASP LYS TYR ASP          
SEQRES   2 H   85  ASP GLU GLU PHE GLU TYR ARG HIS VAL MET LEU PRO LYS          
SEQRES   3 H   85  ASP ILE ALA LYS LEU VAL PRO LYS THR HIS LEU MET SER          
SEQRES   4 H   85  GLU SER GLU TRP ARG ASN LEU GLY VAL GLN GLN SER GLN          
SEQRES   5 H   85  GLY TRP VAL HIS TYR MET ILE HIS GLU PRO GLU PRO HIS          
SEQRES   6 H   85  ILE LEU LEU PHE ARG ARG PRO LEU PRO LYS LYS PRO LYS          
SEQRES   7 H   85  LYS HIS HIS HIS HIS HIS HIS                                  
FORMUL   9  HOH   *639(H2 O)                                                    
HELIX    1 AA1 SER A   46  GLU A   57  1                                  12    
HELIX    2 AA2 LEU A   87  SER A   93  1                                   7    
HELIX    3 AA3 ASP A  101  ARG A  122  1                                  22    
HELIX    4 AA4 LYS A  130  GLN A  132  5                                   3    
HELIX    5 AA5 GLY A  148  PHE A  153  1                                   6    
HELIX    6 AA6 HIS A  162  VAL A  164  1                                   3    
HELIX    7 AA7 THR A  166  LEU A  167  1                                   2    
HELIX    8 AA8 TRP A  168  ARG A  170  5                                   3    
HELIX    9 AA9 SER A  171  LEU A  176  1                                   6    
HELIX   10 AB1 THR A  183  LYS A  200  1                                  18    
HELIX   11 AB2 SER A  208  GLY A  221  1                                  14    
HELIX   12 AB3 GLU A  230  LEU A  234  5                                   5    
HELIX   13 AB4 LEU A  249  VAL A  253  5                                   5    
HELIX   14 AB5 ASP A  257  LEU A  268  1                                  12    
HELIX   15 AB6 SER A  277  LEU A  282  1                                   6    
HELIX   16 AB7 PRO B   25  VAL B   32  5                                   8    
HELIX   17 AB8 SER B   39  ASN B   45  1                                   7    
HELIX   18 AB9 SER C   46  GLU C   57  1                                  12    
HELIX   19 AC1 LEU C   87  SER C   93  1                                   7    
HELIX   20 AC2 ASP C  101  ARG C  122  1                                  22    
HELIX   21 AC3 LYS C  130  GLN C  132  5                                   3    
HELIX   22 AC4 GLY C  148  PHE C  153  1                                   6    
HELIX   23 AC5 HIS C  162  VAL C  164  1                                   3    
HELIX   24 AC6 THR C  166  LEU C  167  1                                   2    
HELIX   25 AC7 TRP C  168  ARG C  170  5                                   3    
HELIX   26 AC8 SER C  171  LEU C  176  1                                   6    
HELIX   27 AC9 THR C  183  LYS C  200  1                                  18    
HELIX   28 AD1 SER C  208  GLY C  221  1                                  14    
HELIX   29 AD2 GLU C  230  LEU C  234  5                                   5    
HELIX   30 AD3 LEU C  249  VAL C  253  5                                   5    
HELIX   31 AD4 ASP C  257  LEU C  268  1                                  12    
HELIX   32 AD5 SER C  277  LEU C  282  1                                   6    
HELIX   33 AD6 PRO D   25  VAL D   32  5                                   8    
HELIX   34 AD7 SER D   39  LEU D   46  1                                   8    
HELIX   35 AD8 SER E   46  GLU E   57  1                                  12    
HELIX   36 AD9 LEU E   87  SER E   93  1                                   7    
HELIX   37 AE1 ASP E  101  ARG E  122  1                                  22    
HELIX   38 AE2 LYS E  130  GLN E  132  5                                   3    
HELIX   39 AE3 GLY E  148  PHE E  153  1                                   6    
HELIX   40 AE4 HIS E  162  VAL E  164  1                                   3    
HELIX   41 AE5 THR E  166  LEU E  167  1                                   2    
HELIX   42 AE6 TRP E  168  ARG E  170  5                                   3    
HELIX   43 AE7 SER E  171  LEU E  176  1                                   6    
HELIX   44 AE8 THR E  183  LYS E  200  1                                  18    
HELIX   45 AE9 SER E  208  GLY E  221  1                                  14    
HELIX   46 AF1 GLU E  230  LEU E  234  5                                   5    
HELIX   47 AF2 LEU E  249  VAL E  253  5                                   5    
HELIX   48 AF3 ASP E  257  LEU E  268  1                                  12    
HELIX   49 AF4 SER E  277  LEU E  282  1                                   6    
HELIX   50 AF5 PRO F   25  VAL F   32  5                                   8    
HELIX   51 AF6 SER F   39  LEU F   46  1                                   8    
HELIX   52 AF7 SER G   46  GLU G   57  1                                  12    
HELIX   53 AF8 LEU G   87  SER G   93  1                                   7    
HELIX   54 AF9 ASP G  101  ARG G  122  1                                  22    
HELIX   55 AG1 LYS G  130  GLN G  132  5                                   3    
HELIX   56 AG2 GLY G  148  PHE G  153  1                                   6    
HELIX   57 AG3 HIS G  162  VAL G  164  1                                   3    
HELIX   58 AG4 THR G  166  LEU G  167  1                                   2    
HELIX   59 AG5 TRP G  168  ARG G  170  5                                   3    
HELIX   60 AG6 SER G  171  LEU G  176  1                                   6    
HELIX   61 AG7 THR G  183  LYS G  200  1                                  18    
HELIX   62 AG8 SER G  208  GLY G  221  1                                  14    
HELIX   63 AG9 GLU G  230  LEU G  234  5                                   5    
HELIX   64 AH1 LEU G  249  VAL G  253  5                                   5    
HELIX   65 AH2 ASP G  257  LEU G  268  1                                  12    
HELIX   66 AH3 SER G  277  LEU G  282  1                                   6    
HELIX   67 AH4 PRO H   25  VAL H   32  5                                   8    
HELIX   68 AH5 SER H   39  LEU H   46  1                                   8    
SHEET    1 AA1 5 TYR A   4  LYS A   9  0                                        
SHEET    2 AA1 5 VAL A  17  HIS A  23 -1  O  LYS A  20   N  GLU A   8           
SHEET    3 AA1 5 VAL A  29  ARG A  36 -1  O  VAL A  30   N  GLY A  21           
SHEET    4 AA1 5 ARG A  75  GLU A  81 -1  O  LEU A  76   N  ILE A  35           
SHEET    5 AA1 5 LEU A  66  MET A  71 -1  N  ASP A  68   O  ILE A  79           
SHEET    1 AA2 2 GLU A  40  GLU A  41  0                                        
SHEET    2 AA2 2 ARG G 180  TYR G 181  1  O  TYR G 181   N  GLU A  40           
SHEET    1 AA3 3 MET A  85  ASP A  86  0                                        
SHEET    2 AA3 3 LEU A 134  ILE A 136 -1  O  ILE A 136   N  MET A  85           
SHEET    3 AA3 3 ILE A 142  LEU A 144 -1  O  LYS A 143   N  LEU A 135           
SHEET    1 AA4 2 ARG A 180  TYR A 181  0                                        
SHEET    2 AA4 2 GLU G  40  GLU G  41  1  O  GLU G  40   N  TYR A 181           
SHEET    1 AA5 3 TYR B   7  TYR B   8  0                                        
SHEET    2 AA5 3 PHE B  17  MET B  23 -1  O  MET B  23   N  TYR B   7           
SHEET    3 AA5 3 TYR B  12  ASP B  13 -1  N  TYR B  12   O  TYR B  19           
SHEET    1 AA6 4 TYR B   7  TYR B   8  0                                        
SHEET    2 AA6 4 PHE B  17  MET B  23 -1  O  MET B  23   N  TYR B   7           
SHEET    3 AA6 4 ILE B  66  PRO B  72 -1  O  ARG B  71   N  GLU B  18           
SHEET    4 AA6 4 VAL B  55  MET B  58 -1  N  VAL B  55   O  ARG B  70           
SHEET    1 AA7 5 TYR C   4  LYS C   9  0                                        
SHEET    2 AA7 5 VAL C  17  HIS C  23 -1  O  LYS C  20   N  GLU C   8           
SHEET    3 AA7 5 VAL C  29  ARG C  36 -1  O  VAL C  30   N  GLY C  21           
SHEET    4 AA7 5 ARG C  75  GLU C  81 -1  O  LEU C  76   N  ILE C  35           
SHEET    5 AA7 5 LEU C  66  MET C  71 -1  N  ASP C  68   O  ILE C  79           
SHEET    1 AA8 2 GLU C  40  GLU C  41  0                                        
SHEET    2 AA8 2 ARG E 180  TYR E 181  1  O  TYR E 181   N  GLU C  40           
SHEET    1 AA9 3 MET C  85  ASP C  86  0                                        
SHEET    2 AA9 3 LEU C 134  ILE C 136 -1  O  ILE C 136   N  MET C  85           
SHEET    3 AA9 3 ILE C 142  LEU C 144 -1  O  LYS C 143   N  LEU C 135           
SHEET    1 AB1 2 ARG C 180  TYR C 181  0                                        
SHEET    2 AB1 2 GLU E  40  GLU E  41  1  O  GLU E  40   N  TYR C 181           
SHEET    1 AB2 3 TYR D   7  TYR D   8  0                                        
SHEET    2 AB2 3 PHE D  17  MET D  23 -1  O  MET D  23   N  TYR D   7           
SHEET    3 AB2 3 TYR D  12  ASP D  13 -1  N  TYR D  12   O  TYR D  19           
SHEET    1 AB3 4 TYR D   7  TYR D   8  0                                        
SHEET    2 AB3 4 PHE D  17  MET D  23 -1  O  MET D  23   N  TYR D   7           
SHEET    3 AB3 4 ILE D  66  PRO D  72 -1  O  ARG D  71   N  GLU D  18           
SHEET    4 AB3 4 VAL D  55  MET D  58 -1  N  VAL D  55   O  ARG D  70           
SHEET    1 AB4 5 TYR E   4  LYS E   9  0                                        
SHEET    2 AB4 5 VAL E  17  HIS E  23 -1  O  LYS E  20   N  GLU E   8           
SHEET    3 AB4 5 VAL E  29  ARG E  36 -1  O  VAL E  30   N  GLY E  21           
SHEET    4 AB4 5 ARG E  75  GLU E  81 -1  O  LEU E  76   N  ILE E  35           
SHEET    5 AB4 5 LEU E  66  MET E  71 -1  N  ASP E  68   O  ILE E  79           
SHEET    1 AB5 3 MET E  85  ASP E  86  0                                        
SHEET    2 AB5 3 LEU E 134  ILE E 136 -1  O  ILE E 136   N  MET E  85           
SHEET    3 AB5 3 ILE E 142  LEU E 144 -1  O  LYS E 143   N  LEU E 135           
SHEET    1 AB6 3 TYR F   7  TYR F   8  0                                        
SHEET    2 AB6 3 PHE F  17  MET F  23 -1  O  MET F  23   N  TYR F   7           
SHEET    3 AB6 3 TYR F  12  ASP F  13 -1  N  TYR F  12   O  TYR F  19           
SHEET    1 AB7 4 TYR F   7  TYR F   8  0                                        
SHEET    2 AB7 4 PHE F  17  MET F  23 -1  O  MET F  23   N  TYR F   7           
SHEET    3 AB7 4 ILE F  66  PRO F  72 -1  O  ARG F  71   N  GLU F  18           
SHEET    4 AB7 4 VAL F  55  MET F  58 -1  N  VAL F  55   O  ARG F  70           
SHEET    1 AB8 5 TYR G   4  LYS G   9  0                                        
SHEET    2 AB8 5 VAL G  17  HIS G  23 -1  O  LYS G  20   N  GLU G   8           
SHEET    3 AB8 5 VAL G  29  ARG G  36 -1  O  VAL G  30   N  GLY G  21           
SHEET    4 AB8 5 ARG G  75  GLU G  81 -1  O  LEU G  76   N  ILE G  35           
SHEET    5 AB8 5 LEU G  66  MET G  71 -1  N  ASP G  68   O  ILE G  79           
SHEET    1 AB9 3 MET G  85  ASP G  86  0                                        
SHEET    2 AB9 3 LEU G 134  ILE G 136 -1  O  ILE G 136   N  MET G  85           
SHEET    3 AB9 3 ILE G 142  LEU G 144 -1  O  LYS G 143   N  LEU G 135           
SHEET    1 AC1 3 TYR H   7  TYR H   8  0                                        
SHEET    2 AC1 3 PHE H  17  MET H  23 -1  O  MET H  23   N  TYR H   7           
SHEET    3 AC1 3 TYR H  12  ASP H  13 -1  N  TYR H  12   O  TYR H  19           
SHEET    1 AC2 4 TYR H   7  TYR H   8  0                                        
SHEET    2 AC2 4 PHE H  17  MET H  23 -1  O  MET H  23   N  TYR H   7           
SHEET    3 AC2 4 ILE H  66  PRO H  72 -1  O  ARG H  71   N  GLU H  18           
SHEET    4 AC2 4 VAL H  55  MET H  58 -1  N  VAL H  55   O  ARG H  70           
CISPEP   1 PRO A  246    GLY A  247          0        28.93                     
CISPEP   2 PRO C  246    GLY C  247          0        28.06                     
CISPEP   3 PRO E  246    GLY E  247          0        28.18                     
CISPEP   4 PRO G  246    GLY G  247          0        28.93                     
CRYST1   66.817  147.531   87.297  90.00  92.06  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014966  0.000000  0.000538        0.00000                         
SCALE2      0.000000  0.006778  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011462        0.00000                         
ATOM      1  N   MET A   1      16.608  32.672 -27.872  1.00147.56           N  
ANISOU    1  N   MET A   1    20093  17530  18440   3063   2822  -1009       N  
ATOM      2  CA  MET A   1      17.363  31.409 -27.535  1.00152.23           C  
ANISOU    2  CA  MET A   1    20632  18161  19045   3648   2858  -1301       C  
ATOM      3  C   MET A   1      18.837  31.376 -27.949  1.00153.60           C  
ANISOU    3  C   MET A   1    20306  19233  18821   4058   3247  -1140       C  
ATOM      4  O   MET A   1      19.519  30.373 -27.704  1.00160.35           O  
ANISOU    4  O   MET A   1    21098  20183  19643   4629   3286  -1376       O  
ATOM      5  CB  MET A   1      16.661  30.149 -28.105  1.00160.38           C  
ANISOU    5  CB  MET A   1    22234  18735  19966   4150   2603  -1881       C  
ATOM      6  CG  MET A   1      16.318  29.088 -27.064  1.00163.41           C  
ANISOU    6  CG  MET A   1    22885  18393  20810   4231   2292  -2131       C  
ATOM      7  SD  MET A   1      14.707  29.362 -26.290  1.00164.68           S  
ANISOU    7  SD  MET A   1    23350  17741  21479   3528   1891  -2083       S  
ATOM      8  CE  MET A   1      14.871  30.965 -25.497  1.00152.61           C  
ANISOU    8  CE  MET A   1    21336  16482  20165   2868   2073  -1508       C  
ATOM      9  N   GLU A   2      19.330  32.429 -28.593  1.00148.15           N  
ANISOU    9  N   GLU A   2    19258  19225  17805   3799   3523   -727       N  
ATOM     10  CA  GLU A   2      20.769  32.605 -28.801  1.00148.15           C  
ANISOU   10  CA  GLU A   2    18623  20195  17470   4008   3905   -417       C  
ATOM     11  C   GLU A   2      21.503  32.581 -27.478  1.00141.35           C  
ANISOU   11  C   GLU A   2    17361  19323  17022   3824   3896   -209       C  
ATOM     12  O   GLU A   2      22.401  31.779 -27.276  1.00142.50           O  
ANISOU   12  O   GLU A   2    17231  19855  17057   4383   4029   -332       O  
ATOM     13  CB  GLU A   2      21.048  33.925 -29.516  1.00151.02           C  
ANISOU   13  CB  GLU A   2    18672  21182  17524   3505   4133    129       C  
ATOM     14  CG  GLU A   2      21.020  33.832 -31.030  1.00158.13           C  
ANISOU   14  CG  GLU A   2    19674  22656  17752   3930   4335     26       C  
ATOM     15  CD  GLU A   2      19.893  32.956 -31.562  1.00158.92           C  
ANISOU   15  CD  GLU A   2    20475  22118  17787   4372   4065   -607       C  
ATOM     16  OE1 GLU A   2      18.738  33.100 -31.080  1.00155.46           O  
ANISOU   16  OE1 GLU A   2    20472  20808  17785   3976   3716   -733       O  
ATOM     17  OE2 GLU A   2      20.158  32.127 -32.461  1.00164.79           O  
ANISOU   17  OE2 GLU A   2    21330  23260  18022   5120   4183   -982       O  
ATOM     18  N   ASP A   3      21.056  33.428 -26.564  1.00132.37           N  
ANISOU   18  N   ASP A   3    16237  17710  16346   3093   3706     66       N  
ATOM     19  CA  ASP A   3      21.699  33.579 -25.258  1.00126.79           C  
ANISOU   19  CA  ASP A   3    15158  16988  16025   2815   3660    297       C  
ATOM     20  C   ASP A   3      21.439  32.454 -24.243  1.00120.09           C  
ANISOU   20  C   ASP A   3    14545  15531  15553   3154   3430    -69       C  
ATOM     21  O   ASP A   3      22.077  32.441 -23.196  1.00118.37           O  
ANISOU   21  O   ASP A   3    13993  15391  15589   3039   3408     99       O  
ATOM     22  CB  ASP A   3      21.281  34.925 -24.636  1.00122.54           C  
ANISOU   22  CB  ASP A   3    14624  16125  15808   1945   3497    684       C  
ATOM     23  CG  ASP A   3      21.791  36.146 -25.420  1.00125.66           C  
ANISOU   23  CG  ASP A   3    14718  17133  15892   1484   3693   1191       C  
ATOM     24  OD1 ASP A   3      22.678  36.043 -26.301  1.00130.19           O  
ANISOU   24  OD1 ASP A   3    14898  18566  15999   1758   4012   1356       O  
ATOM     25  OD2 ASP A   3      21.291  37.244 -25.116  1.00123.00           O  
ANISOU   25  OD2 ASP A   3    14548  16411  15773    836   3508   1451       O  
ATOM     26  N   TYR A   4      20.533  31.519 -24.551  1.00116.25           N  
ANISOU   26  N   TYR A   4    14624  14457  15088   3537   3237   -537       N  
ATOM     27  CA  TYR A   4      20.050  30.498 -23.596  1.00111.14           C  
ANISOU   27  CA  TYR A   4    14305  13086  14835   3723   2948   -832       C  
ATOM     28  C   TYR A   4      20.004  29.066 -24.128  1.00113.28           C  
ANISOU   28  C   TYR A   4    14970  13139  14929   4502   2860  -1328       C  
ATOM     29  O   TYR A   4      19.475  28.827 -25.230  1.00115.17           O  
ANISOU   29  O   TYR A   4    15572  13319  14866   4741   2832  -1611       O  
ATOM     30  CB  TYR A   4      18.635  30.850 -23.166  1.00104.94           C  
ANISOU   30  CB  TYR A   4    13937  11538  14398   3190   2642   -870       C  
ATOM     31  CG  TYR A   4      18.535  32.153 -22.461  1.00100.90           C  
ANISOU   31  CG  TYR A   4    13179  11047  14108   2497   2632   -470       C  
ATOM     32  CD1 TYR A   4      18.782  32.244 -21.106  1.00 98.61           C  
ANISOU   32  CD1 TYR A   4    12691  10597  14178   2256   2529   -308       C  
ATOM     33  CD2 TYR A   4      18.209  33.304 -23.135  1.00100.61           C  
ANISOU   33  CD2 TYR A   4    13148  11172  13905   2104   2696   -256       C  
ATOM     34  CE1 TYR A   4      18.705  33.452 -20.428  1.00 95.34           C  
ANISOU   34  CE1 TYR A   4    12112  10166  13947   1654   2474      8       C  
ATOM     35  CE2 TYR A   4      18.114  34.526 -22.463  1.00 98.17           C  
ANISOU   35  CE2 TYR A   4    12704  10789  13807   1492   2627     85       C  
ATOM     36  CZ  TYR A   4      18.371  34.596 -21.103  1.00 95.31           C  
ANISOU   36  CZ  TYR A   4    12165  10252  13794   1276   2509    194       C  
ATOM     37  OH  TYR A   4      18.273  35.796 -20.422  1.00 93.69           O  
ANISOU   37  OH  TYR A   4    11893   9932  13771    714   2394    474       O  
ATOM     38  N   THR A   5      20.526  28.120 -23.350  1.00113.15           N  
ANISOU   38  N   THR A   5    14934  12962  15093   4905   2776  -1445       N  
ATOM     39  CA  THR A   5      20.330  26.693 -23.630  1.00116.17           C  
ANISOU   39  CA  THR A   5    15847  12871  15419   5595   2564  -1935       C  
ATOM     40  C   THR A   5      19.150  26.184 -22.827  1.00112.93           C  
ANISOU   40  C   THR A   5    15948  11464  15493   5235   2143  -2049       C  
ATOM     41  O   THR A   5      19.070  26.439 -21.634  1.00108.25           O  
ANISOU   41  O   THR A   5    15171  10670  15289   4813   2060  -1775       O  
ATOM     42  CB  THR A   5      21.520  25.837 -23.210  1.00119.09           C  
ANISOU   42  CB  THR A   5    15988  13541  15720   6305   2652  -1998       C  
ATOM     43  OG1 THR A   5      21.750  26.031 -21.812  1.00115.49           O  
ANISOU   43  OG1 THR A   5    15238  12948  15695   5923   2578  -1675       O  
ATOM     44  CG2 THR A   5      22.739  26.202 -23.980  1.00123.82           C  
ANISOU   44  CG2 THR A   5    16009  15238  15797   6740   3075  -1876       C  
ATOM     45  N   LYS A   6      18.241  25.458 -23.490  1.00116.43           N  
ANISOU   45  N   LYS A   6    17020  11332  15883   5391   1866  -2442       N  
ATOM     46  CA  LYS A   6      17.181  24.689 -22.809  1.00113.93           C  
ANISOU   46  CA  LYS A   6    17217  10081  15988   5127   1424  -2567       C  
ATOM     47  C   LYS A   6      17.938  23.568 -22.131  1.00114.92           C  
ANISOU   47  C   LYS A   6    17450   9969  16244   5678   1313  -2664       C  
ATOM     48  O   LYS A   6      18.750  22.916 -22.772  1.00117.80           O  
ANISOU   48  O   LYS A   6    17911  10570  16277   6456   1399  -2949       O  
ATOM     49  CB  LYS A   6      16.090  24.133 -23.783  1.00118.24           C  
ANISOU   49  CB  LYS A   6    18411  10102  16410   5150   1109  -2972       C  
ATOM     50  CG  LYS A   6      14.983  25.136 -24.179  1.00116.46           C  
ANISOU   50  CG  LYS A   6    18159   9905  16185   4487   1086  -2840       C  
ATOM     51  CD  LYS A   6      13.868  24.608 -25.118  1.00120.98           C  
ANISOU   51  CD  LYS A   6    19322  10012  16630   4458    738  -3221       C  
ATOM     52  CE  LYS A   6      13.127  25.777 -25.808  1.00119.72           C  
ANISOU   52  CE  LYS A   6    19013  10186  16288   4018    842  -3086       C  
ATOM     53  NZ  LYS A   6      11.700  25.591 -26.232  1.00119.71           N  
ANISOU   53  NZ  LYS A   6    19416   9725  16343   3648    455  -3262       N  
ATOM     54  N   ILE A   7      17.708  23.414 -20.827  1.00110.54           N  
ANISOU   54  N   ILE A   7    16845   9022  16132   5310   1143  -2405       N  
ATOM     55  CA  ILE A   7      18.211  22.270 -20.049  1.00113.18           C  
ANISOU   55  CA  ILE A   7    17385   8958  16660   5752    942  -2454       C  
ATOM     56  C   ILE A   7      17.087  21.238 -19.955  1.00115.46           C  
ANISOU   56  C   ILE A   7    18414   8244  17210   5587    438  -2658       C  
ATOM     57  O   ILE A   7      17.269  20.102 -20.397  1.00120.90           O  
ANISOU   57  O   ILE A   7    19649   8482  17804   6188    192  -3022       O  
ATOM     58  CB  ILE A   7      18.663  22.654 -18.629  1.00108.45           C  
ANISOU   58  CB  ILE A   7    16296   8546  16363   5449   1028  -2011       C  
ATOM     59  CG1 ILE A   7      19.662  23.817 -18.661  1.00106.61           C  
ANISOU   59  CG1 ILE A   7    15310   9279  15915   5404   1467  -1750       C  
ATOM     60  CG2 ILE A   7      19.269  21.458 -17.925  1.00112.16           C  
ANISOU   60  CG2 ILE A   7    16980   8658  16974   5997    830  -2052       C  
ATOM     61  CD1 ILE A   7      19.705  24.595 -17.367  1.00101.34           C  
ANISOU   61  CD1 ILE A   7    14199   8760  15543   4815   1505  -1321       C  
ATOM     62  N   GLU A   8      15.923  21.635 -19.415  1.00111.68           N  
ANISOU   62  N   GLU A   8    17961   7436  17035   4785    264  -2427       N  
ATOM     63  CA  GLU A   8      14.749  20.726 -19.337  1.00114.32           C  
ANISOU   63  CA  GLU A   8    18926   6890  17618   4472   -232  -2542       C  
ATOM     64  C   GLU A   8      13.360  21.372 -19.152  1.00108.58           C  
ANISOU   64  C   GLU A   8    18131   6049  17073   3615   -356  -2334       C  
ATOM     65  O   GLU A   8      13.255  22.422 -18.530  1.00102.20           O  
ANISOU   65  O   GLU A   8    16804   5683  16342   3201   -117  -2000       O  
ATOM     66  CB  GLU A   8      14.963  19.711 -18.205  1.00117.26           C  
ANISOU   66  CB  GLU A   8    19520   6711  18320   4564   -505  -2370       C  
ATOM     67  CG  GLU A   8      14.929  20.325 -16.811  1.00113.45           C  
ANISOU   67  CG  GLU A   8    18515   6474  18114   4059   -373  -1855       C  
ATOM     68  CD  GLU A   8      15.526  19.427 -15.747  1.00116.04           C  
ANISOU   68  CD  GLU A   8    18950   6475  18662   4332   -537  -1666       C  
ATOM     69  OE1 GLU A   8      16.035  18.342 -16.067  1.00121.14           O  
ANISOU   69  OE1 GLU A   8    20075   6690  19260   4959   -746  -1927       O  
ATOM     70  OE2 GLU A   8      15.497  19.848 -14.570  1.00114.90           O  
ANISOU   70  OE2 GLU A   8    18412   6528  18715   3949   -459  -1254       O  
ATOM     71  N   LYS A   9      12.325  20.688 -19.666  1.00111.74           N  
ANISOU   71  N   LYS A   9    19074   5850  17531   3388   -767  -2544       N  
ATOM     72  CA  LYS A   9      10.900  20.929 -19.345  1.00109.64           C  
ANISOU   72  CA  LYS A   9    18804   5370  17484   2587  -1007  -2324       C  
ATOM     73  C   LYS A   9      10.596  20.844 -17.846  1.00109.06           C  
ANISOU   73  C   LYS A   9    18492   5166  17777   2126  -1084  -1847       C  
ATOM     74  O   LYS A   9      11.107  19.979 -17.150  1.00111.77           O  
ANISOU   74  O   LYS A   9    19027   5139  18300   2335  -1230  -1754       O  
ATOM     75  CB  LYS A   9       9.959  19.953 -20.099  1.00114.37           C  
ANISOU   75  CB  LYS A   9    20070   5283  18100   2433  -1524  -2626       C  
ATOM     76  CG  LYS A   9       8.571  20.511 -20.428  1.00112.33           C  
ANISOU   76  CG  LYS A   9    19709   5120  17848   1753  -1669  -2540       C  
ATOM     77  CD  LYS A   9       7.453  19.471 -20.562  1.00117.74           C  
ANISOU   77  CD  LYS A   9    20926   5085  18724   1289  -2276  -2604       C  
ATOM     78  CE  LYS A   9       6.679  19.295 -19.251  1.00117.28           C  
ANISOU   78  CE  LYS A   9    20639   4874  19046    591  -2453  -2069       C  
ATOM     79  NZ  LYS A   9       5.530  18.358 -19.320  1.00124.17           N  
ANISOU   79  NZ  LYS A   9    21932   5129  20115    -10  -3051  -2018       N  
ATOM     80  N   ILE A  10       9.754  21.746 -17.347  1.00108.26           N  
ANISOU   80  N   ILE A  10    17981   5396  17754   1541   -991  -1542       N  
ATOM     81  CA  ILE A  10       9.346  21.756 -15.925  1.00109.13           C  
ANISOU   81  CA  ILE A  10    17819   5502  18141   1095  -1045  -1079       C  
ATOM     82  C   ILE A  10       7.895  22.213 -15.710  1.00113.32           C  
ANISOU   82  C   ILE A  10    18161   6157  18736    417  -1179   -853       C  
ATOM     83  O   ILE A  10       7.601  22.905 -14.729  1.00119.93           O  
ANISOU   83  O   ILE A  10    18552   7378  19635    133  -1024   -513       O  
ATOM     84  CB  ILE A  10      10.304  22.604 -15.030  1.00103.00           C  
ANISOU   84  CB  ILE A  10    16513   5273  17347   1274   -650   -850       C  
ATOM     85  CG1 ILE A  10      10.656  23.929 -15.678  1.00 98.02           C  
ANISOU   85  CG1 ILE A  10    15536   5246  16459   1388   -282   -969       C  
ATOM     86  CG2 ILE A  10      11.562  21.822 -14.700  1.00108.07           C  
ANISOU   86  CG2 ILE A  10    17287   5741  18032   1822   -630   -893       C  
ATOM     87  CD1 ILE A  10      11.378  24.881 -14.740  1.00 95.04           C  
ANISOU   87  CD1 ILE A  10    14649   5375  16087   1388     22   -714       C  
ATOM     88  N   GLY A  11       6.982  21.876 -16.621  1.00118.31           N  
ANISOU   88  N   GLY A  11    19100   6533  19318    187  -1466  -1050       N  
ATOM     89  CA  GLY A  11       5.547  22.068 -16.365  1.00120.15           C  
ANISOU   89  CA  GLY A  11    19148   6876  19627   -469  -1668   -796       C  
ATOM     90  C   GLY A  11       4.809  22.895 -17.383  1.00120.64           C  
ANISOU   90  C   GLY A  11    19102   7281  19455   -574  -1623   -991       C  
ATOM     91  O   GLY A  11       5.354  23.178 -18.456  1.00116.85           O  
ANISOU   91  O   GLY A  11    18794   6857  18743   -165  -1490  -1357       O  
ATOM     92  N   GLU A  12       3.567  23.269 -17.024  1.00125.64           N  
ANISOU   92  N   GLU A  12    19420   8196  20118  -1099  -1731   -718       N  
ATOM     93  CA  GLU A  12       2.686  24.153 -17.838  1.00129.04           C  
ANISOU   93  CA  GLU A  12    19664   9040  20324  -1227  -1706   -825       C  
ATOM     94  C   GLU A  12       1.847  25.194 -17.019  1.00127.16           C  
ANISOU   94  C   GLU A  12    18834   9433  20046  -1494  -1538   -471       C  
ATOM     95  O   GLU A  12       0.611  25.101 -16.922  1.00127.65           O  
ANISOU   95  O   GLU A  12    18702   9683  20114  -1938  -1769   -279       O  
ATOM     96  CB  GLU A  12       1.774  23.304 -18.740  1.00135.46           C  
ANISOU   96  CB  GLU A  12    20842   9493  21131  -1552  -2180  -1001       C  
ATOM     97  CG  GLU A  12       2.529  22.371 -19.688  1.00140.60           C  
ANISOU   97  CG  GLU A  12    22144   9538  21739  -1191  -2374  -1446       C  
ATOM     98  CD  GLU A  12       1.880  22.235 -21.048  1.00144.40           C  
ANISOU   98  CD  GLU A  12    22932   9931  22002  -1247  -2661  -1806       C  
ATOM     99  OE1 GLU A  12       1.614  21.082 -21.452  1.00144.88           O  
ANISOU   99  OE1 GLU A  12    23515   9380  22151  -1419  -3140  -1994       O  
ATOM    100  OE2 GLU A  12       1.651  23.298 -21.701  1.00142.06           O  
ANISOU  100  OE2 GLU A  12    22382  10158  21435  -1114  -2431  -1899       O  
ATOM    101  N   GLY A  13       2.540  26.203 -16.483  1.00123.80           N  
ANISOU  101  N   GLY A  13    18129   9357  19549  -1193  -1153   -408       N  
ATOM    102  CA  GLY A  13       1.951  27.194 -15.592  1.00121.47           C  
ANISOU  102  CA  GLY A  13    17350   9610  19193  -1306   -988   -130       C  
ATOM    103  C   GLY A  13       0.978  28.125 -16.297  1.00122.86           C  
ANISOU  103  C   GLY A  13    17356  10183  19140  -1339   -996   -202       C  
ATOM    104  O   GLY A  13       1.353  29.261 -16.638  1.00116.47           O  
ANISOU  104  O   GLY A  13    16495   9599  18156  -1031   -755   -327       O  
ATOM    105  N   THR A  14      -0.259  27.619 -16.511  1.00125.31           N  
ANISOU  105  N   THR A  14    17586  10573  19452  -1734  -1303    -96       N  
ATOM    106  CA  THR A  14      -1.476  28.342 -17.084  1.00122.12           C  
ANISOU  106  CA  THR A  14    16935  10637  18825  -1828  -1392    -95       C  
ATOM    107  C   THR A  14      -1.292  29.124 -18.396  1.00111.48           C  
ANISOU  107  C   THR A  14    15800   9316  17242  -1501  -1311   -427       C  
ATOM    108  O   THR A  14      -2.174  29.114 -19.254  1.00107.42           O  
ANISOU  108  O   THR A  14    15294   8935  16584  -1635  -1532   -516       O  
ATOM    109  CB  THR A  14      -2.237  29.279 -16.071  1.00123.53           C  
ANISOU  109  CB  THR A  14    16570  11479  18886  -1815  -1244    199       C  
ATOM    110  OG1 THR A  14      -1.358  30.301 -15.574  1.00118.98           O  
ANISOU  110  OG1 THR A  14    15970  10988  18248  -1395   -909    143       O  
ATOM    111  CG2 THR A  14      -2.886  28.497 -14.876  1.00125.07           C  
ANISOU  111  CG2 THR A  14    16427  11873  19218  -2243  -1380    617       C  
ATOM    112  N   TYR A  15      -0.164  29.815 -18.512  1.00102.43           N  
ANISOU  112  N   TYR A  15    14790   8089  16039  -1105  -1007   -566       N  
ATOM    113  CA  TYR A  15       0.220  30.503 -19.719  1.00 98.42           C  
ANISOU  113  CA  TYR A  15    14504   7587  15302   -807   -899   -821       C  
ATOM    114  C   TYR A  15       0.968  29.607 -20.666  1.00 97.32           C  
ANISOU  114  C   TYR A  15    14791   7031  15154   -703   -973  -1109       C  
ATOM    115  O   TYR A  15       0.362  29.042 -21.576  1.00102.03           O  
ANISOU  115  O   TYR A  15    15593   7518  15655   -824  -1247  -1286       O  
ATOM    116  CB  TYR A  15       1.014  31.754 -19.350  1.00 96.35           C  
ANISOU  116  CB  TYR A  15    14145   7495  14966   -502   -563   -765       C  
ATOM    117  CG  TYR A  15       0.166  32.649 -18.483  1.00 94.77           C  
ANISOU  117  CG  TYR A  15    13595   7692  14719   -520   -544   -551       C  
ATOM    118  CD1 TYR A  15      -1.092  33.122 -18.929  1.00 95.75           C  
ANISOU  118  CD1 TYR A  15    13571   8155  14654   -545   -701   -527       C  
ATOM    119  CD2 TYR A  15       0.559  32.954 -17.201  1.00 94.21           C  
ANISOU  119  CD2 TYR A  15    13330   7704  14762   -478   -396   -383       C  
ATOM    120  CE1 TYR A  15      -1.914  33.917 -18.145  1.00 95.17           C  
ANISOU  120  CE1 TYR A  15    13164   8508  14487   -463   -690   -354       C  
ATOM    121  CE2 TYR A  15      -0.250  33.758 -16.410  1.00 94.47           C  
ANISOU  121  CE2 TYR A  15    13064   8136  14692   -413   -391   -230       C  
ATOM    122  CZ  TYR A  15      -1.476  34.239 -16.895  1.00 93.85           C  
ANISOU  122  CZ  TYR A  15    12845   8403  14410   -377   -529   -222       C  
ATOM    123  OH  TYR A  15      -2.255  35.021 -16.096  1.00 93.19           O  
ANISOU  123  OH  TYR A  15    12459   8764  14184   -212   -518    -93       O  
ATOM    124  N   GLY A  16       2.254  29.400 -20.428  1.00 93.05           N  
ANISOU  124  N   GLY A  16    14381   6277  14696   -466   -762  -1166       N  
ATOM    125  CA  GLY A  16       3.057  28.659 -21.377  1.00 93.55           C  
ANISOU  125  CA  GLY A  16    14835   6033  14673   -222   -787  -1472       C  
ATOM    126  C   GLY A  16       3.341  27.197 -21.035  1.00 93.53           C  
ANISOU  126  C   GLY A  16    15104   5535  14898   -287  -1016  -1548       C  
ATOM    127  O   GLY A  16       2.667  26.574 -20.211  1.00 93.66           O  
ANISOU  127  O   GLY A  16    15042   5395  15149   -655  -1248  -1344       O  
ATOM    128  N   VAL A  17       4.340  26.685 -21.748  1.00 92.80           N  
ANISOU  128  N   VAL A  17    15341   5223  14692    102   -955  -1838       N  
ATOM    129  CA  VAL A  17       5.167  25.567 -21.350  1.00 94.26           C  
ANISOU  129  CA  VAL A  17    15783   4978  15052    293  -1028  -1922       C  
ATOM    130  C   VAL A  17       6.378  26.146 -20.607  1.00 89.89           C  
ANISOU  130  C   VAL A  17    14933   4680  14541    569   -625  -1752       C  
ATOM    131  O   VAL A  17       7.047  27.008 -21.142  1.00 91.18           O  
ANISOU  131  O   VAL A  17    14960   5209  14475    835   -317  -1803       O  
ATOM    132  CB  VAL A  17       5.724  24.848 -22.592  1.00100.17           C  
ANISOU  132  CB  VAL A  17    17018   5479  15563    725  -1130  -2373       C  
ATOM    133  CG1 VAL A  17       6.383  23.538 -22.188  1.00103.62           C  
ANISOU  133  CG1 VAL A  17    17819   5362  16189    946  -1318  -2491       C  
ATOM    134  CG2 VAL A  17       4.632  24.604 -23.641  1.00104.10           C  
ANISOU  134  CG2 VAL A  17    17798   5864  15890    517  -1486  -2612       C  
ATOM    135  N   VAL A  18       6.698  25.692 -19.403  1.00 87.32           N  
ANISOU  135  N   VAL A  18    14499   4189  14487    490   -636  -1526       N  
ATOM    136  CA  VAL A  18       7.816  26.261 -18.639  1.00 82.77           C  
ANISOU  136  CA  VAL A  18    13609   3892  13947    711   -294  -1355       C  
ATOM    137  C   VAL A  18       9.059  25.388 -18.747  1.00 85.44           C  
ANISOU  137  C   VAL A  18    14157   4021  14283   1192   -245  -1525       C  
ATOM    138  O   VAL A  18       8.985  24.207 -18.551  1.00 88.60           O  
ANISOU  138  O   VAL A  18    14889   3934  14840   1233   -524  -1594       O  
ATOM    139  CB  VAL A  18       7.458  26.407 -17.170  1.00 80.58           C  
ANISOU  139  CB  VAL A  18    13030   3668  13916    383   -312   -988       C  
ATOM    140  CG1 VAL A  18       8.555  27.133 -16.403  1.00 77.94           C  
ANISOU  140  CG1 VAL A  18    12365   3659  13588    570      4   -830       C  
ATOM    141  CG2 VAL A  18       6.170  27.192 -17.031  1.00 79.22           C  
ANISOU  141  CG2 VAL A  18    12639   3751  13710     -7   -376   -834       C  
ATOM    142  N   TYR A  19      10.200  25.998 -19.048  1.00 84.74           N  
ANISOU  142  N   TYR A  19    13863   4328  14006   1556     95  -1567       N  
ATOM    143  CA  TYR A  19      11.468  25.305 -19.243  1.00 88.35           C  
ANISOU  143  CA  TYR A  19    14420   4767  14379   2113    200  -1730       C  
ATOM    144  C   TYR A  19      12.533  25.806 -18.283  1.00 86.31           C  
ANISOU  144  C   TYR A  19    13717   4877  14198   2205    474  -1463       C  
ATOM    145  O   TYR A  19      12.474  26.922 -17.803  1.00 82.47           O  
ANISOU  145  O   TYR A  19    12865   4735  13733   1900    643  -1223       O  
ATOM    146  CB  TYR A  19      11.955  25.497 -20.680  1.00 91.61           C  
ANISOU  146  CB  TYR A  19    14946   5464  14398   2523    367  -2034       C  
ATOM    147  CG  TYR A  19      11.323  24.533 -21.666  1.00 97.48           C  
ANISOU  147  CG  TYR A  19    16256   5760  15022   2679     41  -2424       C  
ATOM    148  CD1 TYR A  19      11.756  23.196 -21.715  1.00103.43           C  
ANISOU  148  CD1 TYR A  19    17443   6040  15812   3118   -188  -2687       C  
ATOM    149  CD2 TYR A  19      10.306  24.949 -22.557  1.00 97.70           C  
ANISOU  149  CD2 TYR A  19    16422   5815  14883   2416    -77  -2546       C  
ATOM    150  CE1 TYR A  19      11.218  22.283 -22.610  1.00108.96           C  
ANISOU  150  CE1 TYR A  19    18743   6258  16396   3273   -551  -3087       C  
ATOM    151  CE2 TYR A  19       9.747  24.051 -23.465  1.00102.68           C  
ANISOU  151  CE2 TYR A  19    17590   6036  15387   2542   -424  -2929       C  
ATOM    152  CZ  TYR A  19      10.207  22.710 -23.490  1.00109.09           C  
ANISOU  152  CZ  TYR A  19    18872   6330  16245   2958   -674  -3214       C  
ATOM    153  OH  TYR A  19       9.681  21.752 -24.359  1.00114.11           O  
ANISOU  153  OH  TYR A  19    20136   6460  16759   3090  -1094  -3639       O  
ATOM    154  N   LYS A  20      13.514  24.963 -18.005  1.00 90.30           N  
ANISOU  154  N   LYS A  20    14279   5295  14733   2654    484  -1522       N  
ATOM    155  CA  LYS A  20      14.728  25.374 -17.309  1.00 89.66           C  
ANISOU  155  CA  LYS A  20    13749   5664  14652   2842    751  -1314       C  
ATOM    156  C   LYS A  20      15.778  25.687 -18.356  1.00 89.83           C  
ANISOU  156  C   LYS A  20    13601   6216  14313   3305   1049  -1472       C  
ATOM    157  O   LYS A  20      15.854  25.007 -19.371  1.00 93.07           O  
ANISOU  157  O   LYS A  20    14346   6508  14505   3736    998  -1801       O  
ATOM    158  CB  LYS A  20      15.229  24.254 -16.388  1.00 94.70           C  
ANISOU  158  CB  LYS A  20    14505   5975  15500   3122    586  -1254       C  
ATOM    159  CG  LYS A  20      16.090  24.757 -15.240  1.00 94.73           C  
ANISOU  159  CG  LYS A  20    14006   6385  15599   3083    763   -936       C  
ATOM    160  CD  LYS A  20      16.606  23.630 -14.363  1.00 99.30           C  
ANISOU  160  CD  LYS A  20    14711   6660  16356   3410    590   -858       C  
ATOM    161  CE  LYS A  20      17.615  24.165 -13.357  1.00 99.80           C  
ANISOU  161  CE  LYS A  20    14229   7243  16445   3441    779   -576       C  
ATOM    162  NZ  LYS A  20      18.257  23.083 -12.533  1.00103.99           N  
ANISOU  162  NZ  LYS A  20    14849   7555  17107   3850    625   -483       N  
ATOM    163  N   GLY A  21      16.565  26.722 -18.113  1.00 86.72           N  
ANISOU  163  N   GLY A  21    12690   6425  13834   3196   1341  -1230       N  
ATOM    164  CA  GLY A  21      17.612  27.103 -19.040  1.00 89.40           C  
ANISOU  164  CA  GLY A  21    12755   7401  13811   3555   1653  -1274       C  
ATOM    165  C   GLY A  21      18.792  27.798 -18.412  1.00 89.24           C  
ANISOU  165  C   GLY A  21    12132   8000  13774   3507   1897   -960       C  
ATOM    166  O   GLY A  21      18.768  28.131 -17.220  1.00 85.93           O  
ANISOU  166  O   GLY A  21    11520   7502  13626   3158   1817   -720       O  
ATOM    167  N   ARG A  22      19.828  28.005 -19.216  1.00 93.82           N  
ANISOU  167  N   ARG A  22    12397   9244  14006   3855   2182   -953       N  
ATOM    168  CA  ARG A  22      21.022  28.714 -18.776  1.00 96.33           C  
ANISOU  168  CA  ARG A  22    12072  10269  14260   3760   2415   -620       C  
ATOM    169  C   ARG A  22      21.486  29.802 -19.760  1.00 98.48           C  
ANISOU  169  C   ARG A  22    11999  11228  14191   3557   2702   -429       C  
ATOM    170  O   ARG A  22      21.521  29.584 -20.968  1.00100.85           O  
ANISOU  170  O   ARG A  22    12420  11763  14136   3914   2844   -612       O  
ATOM    171  CB  ARG A  22      22.158  27.711 -18.534  1.00102.24           C  
ANISOU  171  CB  ARG A  22    12606  11326  14913   4464   2486   -691       C  
ATOM    172  CG  ARG A  22      23.334  28.233 -17.702  1.00103.96           C  
ANISOU  172  CG  ARG A  22    12140  12197  15163   4338   2627   -328       C  
ATOM    173  CD  ARG A  22      23.880  27.197 -16.730  1.00106.72           C  
ANISOU  173  CD  ARG A  22    12452  12418  15678   4811   2492   -361       C  
ATOM    174  NE  ARG A  22      24.088  25.902 -17.364  1.00113.67           N  
ANISOU  174  NE  ARG A  22    13668  13152  16368   5685   2471   -721       N  
ATOM    175  CZ  ARG A  22      24.348  24.761 -16.719  1.00118.88           C  
ANISOU  175  CZ  ARG A  22    14533  13472  17162   6226   2282   -838       C  
ATOM    176  NH1 ARG A  22      24.428  24.737 -15.384  1.00117.57           N  
ANISOU  176  NH1 ARG A  22    14225  13127  17316   5962   2120   -592       N  
ATOM    177  NH2 ARG A  22      24.554  23.616 -17.411  1.00124.57           N  
ANISOU  177  NH2 ARG A  22    15638  14020  17670   7082   2232  -1209       N  
ATOM    178  N   HIS A  23      21.850  30.960 -19.203  1.00 97.82           N  
ANISOU  178  N   HIS A  23    11510  11451  14206   2971   2758    -49       N  
ATOM    179  CA  HIS A  23      22.440  32.086 -19.956  1.00101.91           C  
ANISOU  179  CA  HIS A  23    11641  12638  14440   2649   2998    259       C  
ATOM    180  C   HIS A  23      23.882  31.754 -20.344  1.00109.29           C  
ANISOU  180  C   HIS A  23    11996  14489  15041   3111   3290    384       C  
ATOM    181  O   HIS A  23      24.718  31.540 -19.467  1.00111.09           O  
ANISOU  181  O   HIS A  23    11823  14997  15387   3190   3286    525       O  
ATOM    182  CB  HIS A  23      22.408  33.362 -19.084  1.00100.02           C  
ANISOU  182  CB  HIS A  23    11214  12332  14454   1860   2875    616       C  
ATOM    183  CG  HIS A  23      22.486  34.670 -19.840  1.00101.74           C  
ANISOU  183  CG  HIS A  23    11309  12865  14480   1334   2980    930       C  
ATOM    184  ND1 HIS A  23      23.125  34.823 -21.055  1.00107.13           N  
ANISOU  184  ND1 HIS A  23    11728  14237  14738   1493   3269   1073       N  
ATOM    185  CD2 HIS A  23      22.043  35.905 -19.501  1.00 99.38           C  
ANISOU  185  CD2 HIS A  23    11127  12285  14347    654   2812   1158       C  
ATOM    186  CE1 HIS A  23      23.056  36.081 -21.444  1.00107.20           C  
ANISOU  186  CE1 HIS A  23    11701  14352  14677    880   3272   1416       C  
ATOM    187  NE2 HIS A  23      22.407  36.760 -20.517  1.00102.94           N  
ANISOU  187  NE2 HIS A  23    11420  13188  14504    376   2979   1457       N  
ATOM    188  N   LYS A  24      24.180  31.754 -21.640  1.00115.01           N  
ANISOU  188  N   LYS A  24    12632  15752  15314   3419   3546    355       N  
ATOM    189  CA  LYS A  24      25.509  31.352 -22.143  1.00124.16           C  
ANISOU  189  CA  LYS A  24    13212  17904  16056   3990   3862    446       C  
ATOM    190  C   LYS A  24      26.651  32.326 -21.837  1.00128.42           C  
ANISOU  190  C   LYS A  24    12954  19316  16523   3490   4037   1010       C  
ATOM    191  O   LYS A  24      27.816  31.931 -21.871  1.00134.73           O  
ANISOU  191  O   LYS A  24    13160  20965  17066   3937   4253   1127       O  
ATOM    192  CB  LYS A  24      25.469  31.127 -23.660  1.00128.87           C  
ANISOU  192  CB  LYS A  24    13930  18918  16115   4474   4100    264       C  
ATOM    193  CG  LYS A  24      24.466  30.078 -24.086  1.00127.84           C  
ANISOU  193  CG  LYS A  24    14573  18008  15990   5017   3902   -321       C  
ATOM    194  CD  LYS A  24      24.589  29.763 -25.559  1.00133.95           C  
ANISOU  194  CD  LYS A  24    15438  19296  16160   5616   4131   -548       C  
ATOM    195  CE  LYS A  24      23.540  28.750 -25.978  1.00134.00           C  
ANISOU  195  CE  LYS A  24    16272  18452  16188   6074   3854  -1151       C  
ATOM    196  NZ  LYS A  24      23.164  28.873 -27.408  1.00137.42           N  
ANISOU  196  NZ  LYS A  24    16949  19151  16111   6295   3975  -1334       N  
ATOM    197  N   THR A  25      26.317  33.596 -21.615  1.00126.85           N  
ANISOU  197  N   THR A  25    12749  18934  16514   2587   3929   1358       N  
ATOM    198  CA  THR A  25      27.271  34.611 -21.157  1.00130.29           C  
ANISOU  198  CA  THR A  25    12532  19993  16979   1924   3969   1908       C  
ATOM    199  C   THR A  25      27.481  34.460 -19.650  1.00126.37           C  
ANISOU  199  C   THR A  25    11927  19177  16909   1758   3709   1909       C  
ATOM    200  O   THR A  25      28.548  34.061 -19.199  1.00130.79           O  
ANISOU  200  O   THR A  25    11908  20384  17400   2020   3798   2038       O  
ATOM    201  CB  THR A  25      26.790  36.057 -21.499  1.00130.01           C  
ANISOU  201  CB  THR A  25    12658  19749  16990   1016   3876   2264       C  
ATOM    202  OG1 THR A  25      26.628  36.212 -22.917  1.00134.70           O  
ANISOU  202  OG1 THR A  25    13329  20704  17145   1169   4123   2312       O  
ATOM    203  CG2 THR A  25      27.786  37.113 -21.012  1.00133.45           C  
ANISOU  203  CG2 THR A  25    12478  20749  17477    246   3842   2846       C  
ATOM    204  N   THR A  26      26.440  34.738 -18.883  1.00119.49           N  
ANISOU  204  N   THR A  26    11605  17357  16440   1383   3392   1754       N  
ATOM    205  CA  THR A  26      26.548  34.838 -17.427  1.00116.97           C  
ANISOU  205  CA  THR A  26    11212  16734  16496   1096   3122   1802       C  
ATOM    206  C   THR A  26      26.444  33.497 -16.656  1.00116.54           C  
ANISOU  206  C   THR A  26    11312  16358  16607   1770   3031   1460       C  
ATOM    207  O   THR A  26      26.498  33.524 -15.413  1.00116.50           O  
ANISOU  207  O   THR A  26    11259  16118  16886   1569   2805   1503       O  
ATOM    208  CB  THR A  26      25.466  35.796 -16.823  1.00110.53           C  
ANISOU  208  CB  THR A  26    10905  15085  16004    417   2805   1798       C  
ATOM    209  OG1 THR A  26      24.174  35.157 -16.779  1.00104.15           O  
ANISOU  209  OG1 THR A  26    10745  13478  15349    727   2685   1394       O  
ATOM    210  CG2 THR A  26      25.379  37.106 -17.592  1.00111.56           C  
ANISOU  210  CG2 THR A  26    11063  15317  16004   -224   2823   2108       C  
ATOM    211  N   GLY A  27      26.185  32.369 -17.335  1.00116.67           N  
ANISOU  211  N   GLY A  27    11606  16259  16463   2523   3149   1116       N  
ATOM    212  CA  GLY A  27      25.929  31.086 -16.656  1.00114.74           C  
ANISOU  212  CA  GLY A  27    11662  15527  16404   3116   2997    800       C  
ATOM    213  C   GLY A  27      24.693  30.986 -15.747  1.00108.38           C  
ANISOU  213  C   GLY A  27    11430  13751  15997   2822   2675    643       C  
ATOM    214  O   GLY A  27      24.428  29.926 -15.158  1.00107.42           O  
ANISOU  214  O   GLY A  27    11582  13190  16040   3233   2523    443       O  
ATOM    215  N   GLN A  28      23.964  32.097 -15.600  1.00103.88           N  
ANISOU  215  N   GLN A  28    11027  12878  15564   2123   2562    762       N  
ATOM    216  CA  GLN A  28      22.733  32.192 -14.799  1.00 97.91           C  
ANISOU  216  CA  GLN A  28    10747  11335  15117   1818   2287    645       C  
ATOM    217  C   GLN A  28      21.738  31.094 -15.189  1.00 92.64           C  
ANISOU  217  C   GLN A  28    10631  10071  14494   2234   2207    303       C  
ATOM    218  O   GLN A  28      21.505  30.844 -16.372  1.00 91.92           O  
ANISOU  218  O   GLN A  28    10741   9996  14189   2486   2325    129       O  
ATOM    219  CB  GLN A  28      22.124  33.601 -15.005  1.00 99.09           C  
ANISOU  219  CB  GLN A  28    11022  11340  15285   1149   2224    784       C  
ATOM    220  CG  GLN A  28      20.626  33.786 -14.748  1.00 97.05           C  
ANISOU  220  CG  GLN A  28    11304  10361  15208    938   2013    612       C  
ATOM    221  CD  GLN A  28      20.327  34.478 -13.444  1.00 96.59           C  
ANISOU  221  CD  GLN A  28    11256  10073  15370    525   1781    714       C  
ATOM    222  OE1 GLN A  28      19.477  35.363 -13.386  1.00 91.37           O  
ANISOU  222  OE1 GLN A  28    10859   9101  14753    178   1650    708       O  
ATOM    223  NE2 GLN A  28      20.996  34.043 -12.368  1.00100.77           N  
ANISOU  223  NE2 GLN A  28    11518  10758  16011    624   1712    787       N  
ATOM    224  N   VAL A  29      21.128  30.497 -14.171  1.00 87.19           N  
ANISOU  224  N   VAL A  29    10187   8869  14070   2247   1981    235       N  
ATOM    225  CA  VAL A  29      20.095  29.491 -14.344  1.00 83.91           C  
ANISOU  225  CA  VAL A  29    10303   7821  13756   2483   1824    -21       C  
ATOM    226  C   VAL A  29      18.769  30.224 -14.393  1.00 77.91           C  
ANISOU  226  C   VAL A  29     9838   6674  13088   1986   1701    -41       C  
ATOM    227  O   VAL A  29      18.534  31.131 -13.581  1.00 75.56           O  
ANISOU  227  O   VAL A  29     9416   6387  12904   1550   1625    129       O  
ATOM    228  CB  VAL A  29      20.073  28.526 -13.167  1.00 84.19           C  
ANISOU  228  CB  VAL A  29    10426   7537  14024   2668   1627      6       C  
ATOM    229  CG1 VAL A  29      19.126  27.365 -13.444  1.00 84.83           C  
ANISOU  229  CG1 VAL A  29    11068   6958  14203   2896   1433   -223       C  
ATOM    230  CG2 VAL A  29      21.482  27.996 -12.892  1.00 89.29           C  
ANISOU  230  CG2 VAL A  29    10690   8653  14583   3146   1732     85       C  
ATOM    231  N   VAL A  30      17.903  29.848 -15.333  1.00 75.96           N  
ANISOU  231  N   VAL A  30     9984   6108  12769   2082   1658   -264       N  
ATOM    232  CA  VAL A  30      16.620  30.544 -15.529  1.00 71.12           C  
ANISOU  232  CA  VAL A  30     9618   5208  12196   1670   1548   -287       C  
ATOM    233  C   VAL A  30      15.404  29.660 -15.751  1.00 71.35           C  
ANISOU  233  C   VAL A  30    10089   4701  12317   1715   1333   -488       C  
ATOM    234  O   VAL A  30      15.495  28.461 -16.176  1.00 74.77           O  
ANISOU  234  O   VAL A  30    10777   4899  12734   2098   1258   -689       O  
ATOM    235  CB  VAL A  30      16.655  31.499 -16.726  1.00 70.57           C  
ANISOU  235  CB  VAL A  30     9522   5420  11870   1552   1712   -287       C  
ATOM    236  CG1 VAL A  30      17.594  32.631 -16.438  1.00 70.58           C  
ANISOU  236  CG1 VAL A  30     9120   5880  11817   1284   1850    -12       C  
ATOM    237  CG2 VAL A  30      17.032  30.801 -18.016  1.00 74.20           C  
ANISOU  237  CG2 VAL A  30    10098   6032  12060   2007   1846   -500       C  
ATOM    238  N   ALA A  31      14.251  30.267 -15.487  1.00 67.72           N  
ANISOU  238  N   ALA A  31     9734   4055  11938   1328   1205   -437       N  
ATOM    239  CA  ALA A  31      12.972  29.693 -15.840  1.00 67.84           C  
ANISOU  239  CA  ALA A  31    10096   3676  12002   1246    998   -581       C  
ATOM    240  C   ALA A  31      12.498  30.404 -17.102  1.00 68.11           C  
ANISOU  240  C   ALA A  31    10251   3819  11806   1185   1061   -702       C  
ATOM    241  O   ALA A  31      12.434  31.624 -17.104  1.00 65.39           O  
ANISOU  241  O   ALA A  31     9758   3695  11389    962   1150   -570       O  
ATOM    242  CB  ALA A  31      11.986  29.899 -14.697  1.00 65.41           C  
ANISOU  242  CB  ALA A  31     9743   3224  11883    900    830   -412       C  
ATOM    243  N   MET A  32      12.103  29.641 -18.125  1.00 71.21           N  
ANISOU  243  N   MET A  32    10958   4014  12083   1374    969   -949       N  
ATOM    244  CA  MET A  32      11.667  30.204 -19.367  1.00 73.42           C  
ANISOU  244  CA  MET A  32    11368   4419  12106   1361   1013  -1071       C  
ATOM    245  C   MET A  32      10.236  29.814 -19.695  1.00 74.94           C  
ANISOU  245  C   MET A  32    11851   4285  12335   1176    732  -1205       C  
ATOM    246  O   MET A  32       9.992  28.663 -19.950  1.00 79.46           O  
ANISOU  246  O   MET A  32    12708   4531  12951   1307    535  -1404       O  
ATOM    247  CB  MET A  32      12.570  29.693 -20.457  1.00 78.11           C  
ANISOU  247  CB  MET A  32    12054   5193  12428   1809   1162  -1279       C  
ATOM    248  CG  MET A  32      14.004  30.098 -20.256  1.00 80.58           C  
ANISOU  248  CG  MET A  32    11995   5968  12654   1986   1454  -1111       C  
ATOM    249  SD  MET A  32      15.225  29.214 -21.232  1.00 89.26           S  
ANISOU  249  SD  MET A  32    13107   7379  13426   2666   1644  -1345       S  
ATOM    250  CE  MET A  32      14.302  28.705 -22.687  1.00 92.95           C  
ANISOU  250  CE  MET A  32    14085   7620  13612   2864   1487  -1733       C  
ATOM    251  N   LYS A  33       9.295  30.761 -19.751  1.00 74.37           N  
ANISOU  251  N   LYS A  33    11726   4304  12226    887    685  -1104       N  
ATOM    252  CA  LYS A  33       7.936  30.482 -20.235  1.00 76.76           C  
ANISOU  252  CA  LYS A  33    12236   4426  12501    718    424  -1221       C  
ATOM    253  C   LYS A  33       7.892  30.671 -21.732  1.00 79.52           C  
ANISOU  253  C   LYS A  33    12790   4900  12524    894    457  -1427       C  
ATOM    254  O   LYS A  33       8.190  31.725 -22.198  1.00 80.88           O  
ANISOU  254  O   LYS A  33    12860   5366  12505    918    647  -1330       O  
ATOM    255  CB  LYS A  33       6.917  31.398 -19.578  1.00 76.37           C  
ANISOU  255  CB  LYS A  33    12001   4495  12521    416    354  -1019       C  
ATOM    256  CG  LYS A  33       6.085  30.734 -18.517  1.00 79.79           C  
ANISOU  256  CG  LYS A  33    12354   4765  13196    174    140   -902       C  
ATOM    257  CD  LYS A  33       5.597  31.710 -17.455  1.00 83.06           C  
ANISOU  257  CD  LYS A  33    12481   5414  13663     18    181   -669       C  
ATOM    258  CE  LYS A  33       4.596  31.058 -16.481  1.00 89.42           C  
ANISOU  258  CE  LYS A  33    13146   6193  14633   -235    -23   -509       C  
ATOM    259  NZ  LYS A  33       4.917  31.336 -15.035  1.00 90.98           N  
ANISOU  259  NZ  LYS A  33    13092   6527  14949   -260     69   -292       N  
ATOM    260  N   LYS A  34       7.512  29.676 -22.512  1.00 83.36           N  
ANISOU  260  N   LYS A  34    13594   5155  12923   1006    247  -1705       N  
ATOM    261  CA  LYS A  34       7.428  29.825 -23.970  1.00 87.21           C  
ANISOU  261  CA  LYS A  34    14294   5799  13040   1205    258  -1929       C  
ATOM    262  C   LYS A  34       5.944  30.073 -24.241  1.00 85.32           C  
ANISOU  262  C   LYS A  34    14118   5514  12784    893    -17  -1931       C  
ATOM    263  O   LYS A  34       5.123  29.289 -23.830  1.00 86.24           O  
ANISOU  263  O   LYS A  34    14323   5339  13102    661   -321  -1972       O  
ATOM    264  CB  LYS A  34       7.974  28.569 -24.662  1.00 95.04           C  
ANISOU  264  CB  LYS A  34    15633   6575  13900   1589    164  -2289       C  
ATOM    265  CG  LYS A  34       7.918  28.524 -26.189  1.00102.02           C  
ANISOU  265  CG  LYS A  34    16789   7629  14342   1872    146  -2588       C  
ATOM    266  CD  LYS A  34       8.280  27.133 -26.731  1.00111.26           C  
ANISOU  266  CD  LYS A  34    18397   8474  15402   2280    -51  -3015       C  
ATOM    267  CE  LYS A  34       7.063  26.212 -26.922  1.00116.91           C  
ANISOU  267  CE  LYS A  34    19521   8662  16236   2022   -573  -3259       C  
ATOM    268  NZ  LYS A  34       6.403  26.338 -28.264  1.00121.58           N  
ANISOU  268  NZ  LYS A  34    20366   9393  16434   2079   -739  -3530       N  
ATOM    269  N   ILE A  35       5.607  31.184 -24.904  1.00 83.44           N  
ANISOU  269  N   ILE A  35    13810   5591  12302    875     77  -1845       N  
ATOM    270  CA  ILE A  35       4.195  31.557 -25.190  1.00 82.06           C  
ANISOU  270  CA  ILE A  35    13637   5473  12067    640   -172  -1823       C  
ATOM    271  C   ILE A  35       3.942  31.893 -26.662  1.00 84.06           C  
ANISOU  271  C   ILE A  35    14093   5936  11907    806   -203  -1985       C  
ATOM    272  O   ILE A  35       4.674  32.676 -27.264  1.00 84.31           O  
ANISOU  272  O   ILE A  35    14114   6233  11686   1005     63  -1904       O  
ATOM    273  CB  ILE A  35       3.761  32.731 -24.337  1.00 78.90           C  
ANISOU  273  CB  ILE A  35    12941   5250  11786    465    -89  -1510       C  
ATOM    274  CG1 ILE A  35       3.655  32.307 -22.886  1.00 76.96           C  
ANISOU  274  CG1 ILE A  35    12492   4849  11900    270   -138  -1365       C  
ATOM    275  CG2 ILE A  35       2.391  33.250 -24.766  1.00 80.26           C  
ANISOU  275  CG2 ILE A  35    13084   5592  11817    345   -310  -1483       C  
ATOM    276  CD1 ILE A  35       3.813  33.458 -21.935  1.00 73.33           C  
ANISOU  276  CD1 ILE A  35    11781   4552  11527    237     33  -1105       C  
ATOM    277  N   ARG A  36       2.958  31.217 -27.247  1.00 87.16           N  
ANISOU  277  N   ARG A  36    14676   6220  12220    704   -550  -2203       N  
ATOM    278  CA  ARG A  36       2.667  31.275 -28.678  1.00 91.30           C  
ANISOU  278  CA  ARG A  36    15444   6919  12325    877   -654  -2425       C  
ATOM    279  C   ARG A  36       1.616  32.327 -28.756  1.00 91.77           C  
ANISOU  279  C   ARG A  36    15314   7247  12305    711   -735  -2208       C  
ATOM    280  O   ARG A  36       0.541  32.169 -28.187  1.00 90.59           O  
ANISOU  280  O   ARG A  36    15008   7060  12352    423   -994  -2134       O  
ATOM    281  CB  ARG A  36       2.109  29.955 -29.218  1.00 93.82           C  
ANISOU  281  CB  ARG A  36    16097   6940  12607    822  -1066  -2800       C  
ATOM    282  CG  ARG A  36       1.791  29.957 -30.696  1.00 97.29           C  
ANISOU  282  CG  ARG A  36    16815   7575  12575   1020  -1214  -3077       C  
ATOM    283  CD  ARG A  36       1.011  28.705 -31.087  1.00102.64           C  
ANISOU  283  CD  ARG A  36    17830   7902  13266    847  -1736  -3437       C  
ATOM    284  NE  ARG A  36       1.459  28.265 -32.401  1.00107.25           N  
ANISOU  284  NE  ARG A  36    18832   8529  13387   1258  -1793  -3854       N  
ATOM    285  CZ  ARG A  36       2.567  27.554 -32.618  1.00109.61           C  
ANISOU  285  CZ  ARG A  36    19417   8651  13579   1682  -1662  -4133       C  
ATOM    286  NH1 ARG A  36       3.362  27.130 -31.622  1.00107.63           N  
ANISOU  286  NH1 ARG A  36    19096   8123  13675   1734  -1493  -4041       N  
ATOM    287  NH2 ARG A  36       2.879  27.241 -33.855  1.00114.77           N  
ANISOU  287  NH2 ARG A  36    20430   9444  13733   2107  -1712  -4521       N  
ATOM    288  N   LEU A  37       1.915  33.396 -29.500  1.00 93.15           N  
ANISOU  288  N   LEU A  37    15502   7728  12162    908   -525  -2084       N  
ATOM    289  CA  LEU A  37       0.958  34.452 -29.623  1.00 91.96           C  
ANISOU  289  CA  LEU A  37    15226   7805  11907    836   -616  -1877       C  
ATOM    290  C   LEU A  37      -0.009  34.314 -30.786  1.00 94.13           C  
ANISOU  290  C   LEU A  37    15656   8265  11841    870   -913  -2056       C  
ATOM    291  O   LEU A  37       0.379  33.988 -31.925  1.00 95.59           O  
ANISOU  291  O   LEU A  37    16105   8542  11672   1077   -908  -2276       O  
ATOM    292  CB  LEU A  37       1.653  35.795 -29.652  1.00 92.69           C  
ANISOU  292  CB  LEU A  37    15272   8060  11886    964   -303  -1572       C  
ATOM    293  CG  LEU A  37       1.786  36.395 -28.257  1.00 90.64           C  
ANISOU  293  CG  LEU A  37    14777   7672  11988    828   -194  -1321       C  
ATOM    294  CD1 LEU A  37       2.705  37.614 -28.347  1.00 90.25           C  
ANISOU  294  CD1 LEU A  37    14760   7694  11836    902     80  -1039       C  
ATOM    295  CD2 LEU A  37       0.430  36.756 -27.660  1.00 91.04           C  
ANISOU  295  CD2 LEU A  37    14653   7783  12153    725   -442  -1238       C  
ATOM    296  N   GLU A  38      -1.248  34.689 -30.461  1.00 92.66           N  
ANISOU  296  N   GLU A  38    15268   8211  11726    707  -1152  -1933       N  
ATOM    297  CA  GLU A  38      -2.350  34.778 -31.398  1.00 95.59           C  
ANISOU  297  CA  GLU A  38    15680   8845  11794    712  -1464  -2023       C  
ATOM    298  C   GLU A  38      -1.888  35.780 -32.464  1.00 95.93           C  
ANISOU  298  C   GLU A  38    15915   9119  11413   1027  -1270  -1923       C  
ATOM    299  O   GLU A  38      -1.452  36.908 -32.156  1.00 92.90           O  
ANISOU  299  O   GLU A  38    15480   8773  11044   1138  -1015  -1620       O  
ATOM    300  CB  GLU A  38      -3.676  35.267 -30.719  1.00 95.78           C  
ANISOU  300  CB  GLU A  38    15344   9096  11950    559  -1680  -1815       C  
ATOM    301  CG  GLU A  38      -4.029  34.740 -29.290  1.00 94.75           C  
ANISOU  301  CG  GLU A  38    14892   8850  12257    262  -1736  -1711       C  
ATOM    302  CD  GLU A  38      -3.861  35.757 -28.102  1.00 91.12           C  
ANISOU  302  CD  GLU A  38    14187   8437  11994    374  -1478  -1412       C  
ATOM    303  OE1 GLU A  38      -4.867  36.390 -27.669  1.00 89.99           O  
ANISOU  303  OE1 GLU A  38    13753   8613  11824    422  -1591  -1243       O  
ATOM    304  OE2 GLU A  38      -2.722  35.900 -27.582  1.00 87.95           O  
ANISOU  304  OE2 GLU A  38    13883   7778  11756    436  -1183  -1363       O  
ATOM    305  N   SER A  39      -1.929  35.349 -33.716  1.00 98.82           N  
ANISOU  305  N   SER A  39    16535   9622  11387   1156  -1404  -2170       N  
ATOM    306  CA  SER A  39      -1.725  36.250 -34.847  1.00100.23           C  
ANISOU  306  CA  SER A  39    16883  10111  11090   1430  -1284  -2045       C  
ATOM    307  C   SER A  39      -2.569  37.515 -34.653  1.00 98.59           C  
ANISOU  307  C   SER A  39    16514  10083  10862   1463  -1354  -1702       C  
ATOM    308  O   SER A  39      -3.685  37.444 -34.159  1.00 96.53           O  
ANISOU  308  O   SER A  39    16028   9883  10764   1331  -1630  -1702       O  
ATOM    309  CB  SER A  39      -2.133  35.524 -36.110  1.00105.02           C  
ANISOU  309  CB  SER A  39    17735  10894  11272   1531  -1566  -2398       C  
ATOM    310  OG  SER A  39      -1.832  36.276 -37.244  1.00107.92           O  
ANISOU  310  OG  SER A  39    18278  11599  11128   1813  -1427  -2278       O  
ATOM    311  N   GLU A  40      -2.050  38.677 -35.037  1.00 99.47           N  
ANISOU  311  N   GLU A  40    16740  10296  10759   1648  -1122  -1392       N  
ATOM    312  CA  GLU A  40      -2.805  39.930 -34.844  1.00 99.37           C  
ANISOU  312  CA  GLU A  40    16664  10368  10721   1753  -1218  -1073       C  
ATOM    313  C   GLU A  40      -3.131  40.591 -36.145  1.00101.34           C  
ANISOU  313  C   GLU A  40    17128  10921  10453   1984  -1317   -951       C  
ATOM    314  O   GLU A  40      -2.530  40.318 -37.180  1.00103.30           O  
ANISOU  314  O   GLU A  40    17580  11335  10332   2069  -1212  -1028       O  
ATOM    315  CB  GLU A  40      -2.053  40.898 -33.936  1.00 99.00           C  
ANISOU  315  CB  GLU A  40    16614  10057  10943   1735   -950   -748       C  
ATOM    316  CG  GLU A  40      -0.692  41.356 -34.474  1.00102.70           C  
ANISOU  316  CG  GLU A  40    17292  10500  11229   1745   -616   -532       C  
ATOM    317  CD  GLU A  40      -0.110  42.553 -33.718  1.00103.72           C  
ANISOU  317  CD  GLU A  40    17474  10361  11572   1681   -458   -149       C  
ATOM    318  OE1 GLU A  40       0.054  43.649 -34.318  1.00103.78           O  
ANISOU  318  OE1 GLU A  40    17714  10386  11330   1756   -439    193       O  
ATOM    319  OE2 GLU A  40       0.183  42.385 -32.510  1.00104.04           O  
ANISOU  319  OE2 GLU A  40    17350  10153  12027   1539   -384   -187       O  
ATOM    320  N   GLU A  41      -4.105  41.466 -36.086  1.00101.36           N  
ANISOU  320  N   GLU A  41    17079  11035  10396   2134  -1524   -757       N  
ATOM    321  CA  GLU A  41      -4.555  42.182 -37.258  1.00105.32           C  
ANISOU  321  CA  GLU A  41    17782  11826  10407   2386  -1666   -595       C  
ATOM    322  C   GLU A  41      -3.544  43.278 -37.655  1.00107.11           C  
ANISOU  322  C   GLU A  41    18312  11930  10454   2474  -1385   -186       C  
ATOM    323  O   GLU A  41      -2.710  43.700 -36.865  1.00104.06           O  
ANISOU  323  O   GLU A  41    17945  11220  10370   2344  -1144      3       O  
ATOM    324  CB  GLU A  41      -5.909  42.781 -36.952  1.00105.81           C  
ANISOU  324  CB  GLU A  41    17670  12047  10483   2572  -1986   -503       C  
ATOM    325  CG  GLU A  41      -6.672  43.292 -38.144  1.00110.51           C  
ANISOU  325  CG  GLU A  41    18402  13017  10570   2853  -2240   -403       C  
ATOM    326  CD  GLU A  41      -8.086  43.676 -37.791  1.00111.98           C  
ANISOU  326  CD  GLU A  41    18314  13462  10769   3066  -2581   -369       C  
ATOM    327  OE1 GLU A  41      -8.664  44.540 -38.502  1.00115.96           O  
ANISOU  327  OE1 GLU A  41    18960  14187  10911   3410  -2763   -156       O  
ATOM    328  OE2 GLU A  41      -8.611  43.135 -36.795  1.00109.65           O  
ANISOU  328  OE2 GLU A  41    17646  13191  10823   2914  -2663   -525       O  
ATOM    329  N   GLU A  42      -3.641  43.710 -38.905  1.00113.23           N  
ANISOU  329  N   GLU A  42    19316  12991  10713   2660  -1445    -33       N  
ATOM    330  CA  GLU A  42      -2.807  44.759 -39.538  1.00117.68           C  
ANISOU  330  CA  GLU A  42    20182  13535  10993   2710  -1233    433       C  
ATOM    331  C   GLU A  42      -2.431  45.982 -38.706  1.00117.22           C  
ANISOU  331  C   GLU A  42    20262  13035  11242   2650  -1150    856       C  
ATOM    332  O   GLU A  42      -1.282  46.122 -38.287  1.00115.44           O  
ANISOU  332  O   GLU A  42    20058  12592  11210   2406   -858   1028       O  
ATOM    333  CB  GLU A  42      -3.534  45.236 -40.813  1.00124.24           C  
ANISOU  333  CB  GLU A  42    21212  14740  11251   2990  -1467    578       C  
ATOM    334  CG  GLU A  42      -2.749  46.143 -41.758  1.00129.44           C  
ANISOU  334  CG  GLU A  42    22193  15508  11481   3025  -1278   1078       C  
ATOM    335  CD  GLU A  42      -1.660  45.394 -42.518  1.00131.90           C  
ANISOU  335  CD  GLU A  42    22493  16161  11461   2926   -953    982       C  
ATOM    336  OE1 GLU A  42      -1.661  45.430 -43.779  1.00135.77           O  
ANISOU  336  OE1 GLU A  42    23139  17107  11340   3100   -962   1074       O  
ATOM    337  OE2 GLU A  42      -0.822  44.745 -41.833  1.00129.61           O  
ANISOU  337  OE2 GLU A  42    22027  15719  11497   2720   -695    800       O  
ATOM    338  N   GLY A  43      -3.396  46.869 -38.480  1.00120.03           N  
ANISOU  338  N   GLY A  43    20719  13265  11620   2894  -1435   1013       N  
ATOM    339  CA  GLY A  43      -3.162  48.078 -37.703  1.00121.95           C  
ANISOU  339  CA  GLY A  43    21190  13017  12126   2907  -1449   1363       C  
ATOM    340  C   GLY A  43      -3.045  47.714 -36.244  1.00119.23           C  
ANISOU  340  C   GLY A  43    20595  12379  12326   2764  -1380   1127       C  
ATOM    341  O   GLY A  43      -2.035  47.972 -35.621  1.00118.26           O  
ANISOU  341  O   GLY A  43    20542  11921  12468   2505  -1172   1275       O  
ATOM    342  N   VAL A  44      -4.083  47.061 -35.727  1.00120.21           N  
ANISOU  342  N   VAL A  44    20390  12694  12587   2906  -1563    775       N  
ATOM    343  CA  VAL A  44      -4.219  46.723 -34.295  1.00117.19           C  
ANISOU  343  CA  VAL A  44    19728  12123  12673   2829  -1540    566       C  
ATOM    344  C   VAL A  44      -2.892  46.352 -33.643  1.00113.18           C  
ANISOU  344  C   VAL A  44    19192  11326  12483   2455  -1218    562       C  
ATOM    345  O   VAL A  44      -2.388  45.232 -33.861  1.00115.02           O  
ANISOU  345  O   VAL A  44    19242  11722  12738   2229  -1048    345       O  
ATOM    346  CB  VAL A  44      -5.223  45.565 -34.078  1.00118.64           C  
ANISOU  346  CB  VAL A  44    19464  12698  12915   2826  -1695    188       C  
ATOM    347  CG1 VAL A  44      -5.323  45.158 -32.596  1.00115.88           C  
ANISOU  347  CG1 VAL A  44    18796  12216  13016   2712  -1645     27       C  
ATOM    348  CG2 VAL A  44      -6.599  45.961 -34.583  1.00123.19           C  
ANISOU  348  CG2 VAL A  44    19970  13642  13193   3201  -2037    204       C  
ATOM    349  N   PRO A  45      -2.321  47.279 -32.853  1.00110.16           N  
ANISOU  349  N   PRO A  45    19011  10510  12334   2411  -1165    788       N  
ATOM    350  CA  PRO A  45      -1.074  46.960 -32.184  1.00105.91           C  
ANISOU  350  CA  PRO A  45    18400   9745  12094   2050   -887    800       C  
ATOM    351  C   PRO A  45      -1.400  46.256 -30.876  1.00 99.77           C  
ANISOU  351  C   PRO A  45    17277   8934  11694   2024   -891    494       C  
ATOM    352  O   PRO A  45      -2.444  46.515 -30.271  1.00 96.53           O  
ANISOU  352  O   PRO A  45    16774   8559  11344   2295  -1105    395       O  
ATOM    353  CB  PRO A  45      -0.454  48.324 -31.944  1.00107.90           C  
ANISOU  353  CB  PRO A  45    19047   9544  12402   1989   -918   1186       C  
ATOM    354  CG  PRO A  45      -1.639  49.229 -31.753  1.00110.15           C  
ANISOU  354  CG  PRO A  45    19545   9692  12612   2427  -1260   1210       C  
ATOM    355  CD  PRO A  45      -2.782  48.641 -32.530  1.00111.98           C  
ANISOU  355  CD  PRO A  45    19570  10420  12555   2705  -1396   1020       C  
ATOM    356  N   SER A  46      -0.517  45.335 -30.497  1.00 95.85           N  
ANISOU  356  N   SER A  46    16572   8436  11408   1731   -650    362       N  
ATOM    357  CA  SER A  46      -0.786  44.416 -29.400  1.00 91.44           C  
ANISOU  357  CA  SER A  46    15667   7902  11170   1660   -641     87       C  
ATOM    358  C   SER A  46      -0.534  45.045 -28.058  1.00 89.13           C  
ANISOU  358  C   SER A  46    15379   7300  11183   1650   -637    154       C  
ATOM    359  O   SER A  46       0.611  45.362 -27.704  1.00 87.65           O  
ANISOU  359  O   SER A  46    15298   6858  11144   1432   -473    299       O  
ATOM    360  CB  SER A  46       0.026  43.129 -29.518  1.00 89.61           C  
ANISOU  360  CB  SER A  46    15256   7759  11031   1412   -425    -95       C  
ATOM    361  OG  SER A  46      -0.132  42.348 -28.353  1.00 86.15           O  
ANISOU  361  OG  SER A  46    14534   7268  10931   1310   -426   -283       O  
ATOM    362  N   THR A  47      -1.628  45.231 -27.325  1.00 89.33           N  
ANISOU  362  N   THR A  47    15268   7406  11267   1903   -833     49       N  
ATOM    363  CA  THR A  47      -1.582  45.685 -25.936  1.00 88.15           C  
ANISOU  363  CA  THR A  47    15080   7049  11363   1976   -858     30       C  
ATOM    364  C   THR A  47      -0.956  44.663 -25.020  1.00 83.93           C  
ANISOU  364  C   THR A  47    14240   6517  11131   1687   -671   -100       C  
ATOM    365  O   THR A  47      -0.372  45.042 -24.012  1.00 83.68           O  
ANISOU  365  O   THR A  47    14248   6245  11299   1633   -622    -72       O  
ATOM    366  CB  THR A  47      -2.991  46.009 -25.376  1.00 90.42           C  
ANISOU  366  CB  THR A  47    15206   7581  11566   2395  -1089    -67       C  
ATOM    367  OG1 THR A  47      -3.886  44.902 -25.611  1.00 89.07           O  
ANISOU  367  OG1 THR A  47    14613   7885  11342   2349  -1134   -215       O  
ATOM    368  CG2 THR A  47      -3.550  47.353 -25.992  1.00 94.55           C  
ANISOU  368  CG2 THR A  47    16131   7981  11811   2814  -1321     82       C  
ATOM    369  N   ALA A  48      -1.084  43.386 -25.369  1.00 81.50           N  
ANISOU  369  N   ALA A  48    13669   6451  10844   1513   -605   -247       N  
ATOM    370  CA  ALA A  48      -0.441  42.314 -24.615  1.00 78.10           C  
ANISOU  370  CA  ALA A  48    12999   5983  10690   1248   -446   -354       C  
ATOM    371  C   ALA A  48       1.052  42.556 -24.427  1.00 75.74           C  
ANISOU  371  C   ALA A  48    12844   5409  10522   1056   -228   -242       C  
ATOM    372  O   ALA A  48       1.561  42.497 -23.336  1.00 72.77           O  
ANISOU  372  O   ALA A  48    12359   4906  10381    962   -157   -240       O  
ATOM    373  CB  ALA A  48      -0.709  40.961 -25.282  1.00 78.78           C  
ANISOU  373  CB  ALA A  48    12930   6261  10740   1099   -465   -528       C  
ATOM    374  N   ILE A  49       1.756  42.840 -25.499  1.00 78.07           N  
ANISOU  374  N   ILE A  49    13351   5675  10635    992   -125   -121       N  
ATOM    375  CA  ILE A  49       3.176  43.128 -25.385  1.00 79.57           C  
ANISOU  375  CA  ILE A  49    13609   5709  10911    777     79     46       C  
ATOM    376  C   ILE A  49       3.403  44.440 -24.645  1.00 82.15           C  
ANISOU  376  C   ILE A  49    14141   5733  11336    756    -21    236       C  
ATOM    377  O   ILE A  49       4.289  44.460 -23.793  1.00 80.79           O  
ANISOU  377  O   ILE A  49    13886   5426  11382    566     70    280       O  
ATOM    378  CB  ILE A  49       3.894  43.183 -26.758  1.00 82.40           C  
ANISOU  378  CB  ILE A  49    14104   6216  10985    709    232    191       C  
ATOM    379  CG1 ILE A  49       4.087  41.762 -27.298  1.00 82.86           C  
ANISOU  379  CG1 ILE A  49    13987   6516  10978    731    360    -53       C  
ATOM    380  CG2 ILE A  49       5.257  43.877 -26.660  1.00 83.39           C  
ANISOU  380  CG2 ILE A  49    14289   6240  11154    454    400    490       C  
ATOM    381  CD1 ILE A  49       2.904  41.230 -28.070  1.00 84.38           C  
ANISOU  381  CD1 ILE A  49    14219   6874  10966    906    173   -263       C  
ATOM    382  N   ARG A  50       2.644  45.515 -24.975  1.00 85.84           N  
ANISOU  382  N   ARG A  50    14901   6077  11634    964   -236    339       N  
ATOM    383  CA  ARG A  50       2.746  46.805 -24.250  1.00 89.24           C  
ANISOU  383  CA  ARG A  50    15638   6123  12146   1008   -416    472       C  
ATOM    384  C   ARG A  50       2.828  46.575 -22.743  1.00 85.47           C  
ANISOU  384  C   ARG A  50    14970   5564  11938   1013   -429    298       C  
ATOM    385  O   ARG A  50       3.737  47.063 -22.088  1.00 84.87           O  
ANISOU  385  O   ARG A  50    15004   5223  12020    798   -431    393       O  
ATOM    386  CB  ARG A  50       1.567  47.767 -24.510  1.00 95.62           C  
ANISOU  386  CB  ARG A  50    16748   6828  12754   1411   -703    486       C  
ATOM    387  CG  ARG A  50       1.439  48.374 -25.910  1.00103.68           C  
ANISOU  387  CG  ARG A  50    18081   7836  13475   1455   -771    726       C  
ATOM    388  CD  ARG A  50       2.732  48.988 -26.489  1.00108.41           C  
ANISOU  388  CD  ARG A  50    18944   8200  14048   1049   -674   1092       C  
ATOM    389  NE  ARG A  50       2.621  49.443 -27.908  1.00113.65           N  
ANISOU  389  NE  ARG A  50    19860   8947  14372   1070   -702   1367       N  
ATOM    390  CZ  ARG A  50       2.540  48.657 -28.998  1.00114.19           C  
ANISOU  390  CZ  ARG A  50    19735   9460  14191   1078   -531   1343       C  
ATOM    391  NH1 ARG A  50       2.525  47.316 -28.898  1.00113.32           N  
ANISOU  391  NH1 ARG A  50    19206   9704  14146   1067   -342   1035       N  
ATOM    392  NH2 ARG A  50       2.468  49.214 -30.200  1.00117.44           N  
ANISOU  392  NH2 ARG A  50    20413   9940  14267   1109   -578   1628       N  
ATOM    393  N   GLU A  51       1.892  45.782 -22.228  1.00 82.06           N  
ANISOU  393  N   GLU A  51    14227   5409  11540   1220   -445     68       N  
ATOM    394  CA  GLU A  51       1.865  45.390 -20.822  1.00 78.60           C  
ANISOU  394  CA  GLU A  51    13543   5011  11308   1241   -433    -77       C  
ATOM    395  C   GLU A  51       3.141  44.723 -20.391  1.00 75.55           C  
ANISOU  395  C   GLU A  51    12986   4573  11145    883   -225    -45       C  
ATOM    396  O   GLU A  51       3.704  45.100 -19.388  1.00 76.14           O  
ANISOU  396  O   GLU A  51    13091   4474  11364    811   -253    -41       O  
ATOM    397  CB  GLU A  51       0.697  44.455 -20.560  1.00 78.32           C  
ANISOU  397  CB  GLU A  51    13135   5376  11246   1413   -453   -241       C  
ATOM    398  CG  GLU A  51      -0.673  45.088 -20.726  1.00 82.08           C  
ANISOU  398  CG  GLU A  51    13657   6037  11489   1835   -669   -283       C  
ATOM    399  CD  GLU A  51      -0.939  46.144 -19.691  1.00 85.91           C  
ANISOU  399  CD  GLU A  51    14318   6380  11942   2179   -827   -332       C  
ATOM    400  OE1 GLU A  51      -0.636  45.905 -18.495  1.00 85.03           O  
ANISOU  400  OE1 GLU A  51    14042   6287  11978   2137   -772   -407       O  
ATOM    401  OE2 GLU A  51      -1.448  47.237 -20.087  1.00 91.98           O  
ANISOU  401  OE2 GLU A  51    15432   7004  12512   2530  -1028   -303       O  
ATOM    402  N   ILE A  52       3.593  43.735 -21.148  1.00 73.93           N  
ANISOU  402  N   ILE A  52    12613   4534  10942    701    -37    -42       N  
ATOM    403  CA  ILE A  52       4.762  42.933 -20.761  1.00 72.78           C  
ANISOU  403  CA  ILE A  52    12256   4412  10986    450    166    -33       C  
ATOM    404  C   ILE A  52       6.013  43.783 -20.701  1.00 72.71           C  
ANISOU  404  C   ILE A  52    12394   4212  11018    212    217    177       C  
ATOM    405  O   ILE A  52       6.817  43.666 -19.784  1.00 71.48           O  
ANISOU  405  O   ILE A  52    12099   4009  11049     56    268    194       O  
ATOM    406  CB  ILE A  52       5.026  41.745 -21.733  1.00 74.06           C  
ANISOU  406  CB  ILE A  52    12281   4777  11081    397    333   -103       C  
ATOM    407  CG1 ILE A  52       3.834  40.757 -21.849  1.00 72.29           C  
ANISOU  407  CG1 ILE A  52    11918   4709  10836    525    231   -304       C  
ATOM    408  CG2 ILE A  52       6.247  40.959 -21.295  1.00 74.01           C  
ANISOU  408  CG2 ILE A  52    12067   4803  11247    238    530   -100       C  
ATOM    409  CD1 ILE A  52       3.435  40.046 -20.596  1.00 69.52           C  
ANISOU  409  CD1 ILE A  52    11315   4391  10706    506    183   -390       C  
ATOM    410  N   SER A  53       6.182  44.610 -21.713  1.00 75.13           N  
ANISOU  410  N   SER A  53    12966   4440  11139    150    190    370       N  
ATOM    411  CA  SER A  53       7.206  45.666 -21.718  1.00 77.74           C  
ANISOU  411  CA  SER A  53    13498   4552  11487   -144    156    651       C  
ATOM    412  C   SER A  53       7.297  46.364 -20.367  1.00 76.83           C  
ANISOU  412  C   SER A  53    13502   4126  11564   -180    -49    604       C  
ATOM    413  O   SER A  53       8.342  46.342 -19.726  1.00 78.96           O  
ANISOU  413  O   SER A  53    13633   4375  11992   -461      1    684       O  
ATOM    414  CB  SER A  53       6.881  46.732 -22.772  1.00 81.61           C  
ANISOU  414  CB  SER A  53    14381   4883  11742   -133     21    876       C  
ATOM    415  OG  SER A  53       6.236  46.195 -23.921  1.00 82.25           O  
ANISOU  415  OG  SER A  53    14427   5236  11585     65    109    823       O  
ATOM    416  N   LEU A  54       6.164  46.870 -19.906  1.00 74.64           N  
ANISOU  416  N   LEU A  54    13436   3681  11243    154   -281    441       N  
ATOM    417  CA  LEU A  54       6.097  47.549 -18.649  1.00 74.36           C  
ANISOU  417  CA  LEU A  54    13564   3374  11314    239   -504    331       C  
ATOM    418  C   LEU A  54       6.388  46.719 -17.443  1.00 70.94           C  
ANISOU  418  C   LEU A  54    12766   3125  11059    217   -404    165       C  
ATOM    419  O   LEU A  54       6.973  47.221 -16.502  1.00 72.64           O  
ANISOU  419  O   LEU A  54    13078   3139  11381     94   -535    151       O  
ATOM    420  CB  LEU A  54       4.726  48.203 -18.491  1.00 76.83           C  
ANISOU  420  CB  LEU A  54    14145   3579  11468    733   -750    168       C  
ATOM    421  CG  LEU A  54       4.431  49.570 -19.202  1.00 81.13           C  
ANISOU  421  CG  LEU A  54    15270   3708  11848    848  -1026    319       C  
ATOM    422  CD1 LEU A  54       5.401  49.954 -20.357  1.00 84.24           C  
ANISOU  422  CD1 LEU A  54    15846   3947  12212    388   -961    691       C  
ATOM    423  CD2 LEU A  54       2.971  49.587 -19.677  1.00 80.94           C  
ANISOU  423  CD2 LEU A  54    15269   3884  11598   1374  -1109    192       C  
ATOM    424  N   LEU A  55       5.993  45.457 -17.458  1.00 68.02           N  
ANISOU  424  N   LEU A  55    12011   3116  10717    317   -206     49       N  
ATOM    425  CA  LEU A  55       6.249  44.547 -16.350  1.00 66.47           C  
ANISOU  425  CA  LEU A  55    11465   3104  10684    290   -108    -60       C  
ATOM    426  C   LEU A  55       7.710  44.140 -16.218  1.00 67.64           C  
ANISOU  426  C   LEU A  55    11430   3278  10990    -61     51     67       C  
ATOM    427  O   LEU A  55       8.184  43.750 -15.139  1.00 69.02           O  
ANISOU  427  O   LEU A  55    11402   3518  11302   -116     67     19       O  
ATOM    428  CB  LEU A  55       5.386  43.275 -16.471  1.00 63.96           C  
ANISOU  428  CB  LEU A  55    10832   3107  10361    443     10   -173       C  
ATOM    429  CG  LEU A  55       3.876  43.513 -16.294  1.00 64.28           C  
ANISOU  429  CG  LEU A  55    10887   3288  10247    794   -143   -290       C  
ATOM    430  CD1 LEU A  55       3.041  42.317 -16.735  1.00 63.53           C  
ANISOU  430  CD1 LEU A  55    10505   3498  10134    817    -70   -336       C  
ATOM    431  CD2 LEU A  55       3.470  43.863 -14.867  1.00 63.93           C  
ANISOU  431  CD2 LEU A  55    10784   3313  10192   1016   -262   -394       C  
ATOM    432  N   LYS A  56       8.428  44.195 -17.314  1.00 69.55           N  
ANISOU  432  N   LYS A  56    11701   3543  11180   -273    178    245       N  
ATOM    433  CA  LYS A  56       9.858  43.985 -17.293  1.00 71.38           C  
ANISOU  433  CA  LYS A  56    11728   3885  11506   -589    326    413       C  
ATOM    434  C   LYS A  56      10.566  44.950 -16.352  1.00 74.20           C  
ANISOU  434  C   LYS A  56    12203   4019  11967   -838    129    503       C  
ATOM    435  O   LYS A  56      11.553  44.581 -15.726  1.00 73.20           O  
ANISOU  435  O   LYS A  56    11804   4039  11967  -1028    200    557       O  
ATOM    436  CB  LYS A  56      10.379  44.199 -18.686  1.00 74.87           C  
ANISOU  436  CB  LYS A  56    12222   4436  11788   -752    465    635       C  
ATOM    437  CG  LYS A  56      11.701  43.524 -19.032  1.00 77.43           C  
ANISOU  437  CG  LYS A  56    12189   5110  12119   -940    730    784       C  
ATOM    438  CD  LYS A  56      12.083  43.806 -20.507  1.00 81.83           C  
ANISOU  438  CD  LYS A  56    12795   5869  12426  -1049    882   1023       C  
ATOM    439  CE  LYS A  56      10.871  44.018 -21.463  1.00 81.73           C  
ANISOU  439  CE  LYS A  56    13098   5742  12213   -815    808    943       C  
ATOM    440  NZ  LYS A  56      11.203  44.198 -22.908  1.00 85.31           N  
ANISOU  440  NZ  LYS A  56    13592   6451  12370   -876    966   1169       N  
ATOM    441  N   GLU A  57      10.065  46.184 -16.242  1.00 78.72           N  
ANISOU  441  N   GLU A  57    13207   4222  12477   -817   -154    506       N  
ATOM    442  CA  GLU A  57      10.683  47.191 -15.371  1.00 82.89           C  
ANISOU  442  CA  GLU A  57    13962   4439  13092  -1063   -431    554       C  
ATOM    443  C   GLU A  57      10.779  46.704 -13.953  1.00 77.42           C  
ANISOU  443  C   GLU A  57    13049   3853  12512   -950   -468    344       C  
ATOM    444  O   GLU A  57      11.751  46.987 -13.276  1.00 79.79           O  
ANISOU  444  O   GLU A  57    13292   4108  12914  -1254   -576    415       O  
ATOM    445  CB  GLU A  57       9.903  48.525 -15.312  1.00 91.18           C  
ANISOU  445  CB  GLU A  57    15610   4992  14041   -903   -797    490       C  
ATOM    446  CG  GLU A  57       9.556  49.235 -16.621  1.00101.24           C  
ANISOU  446  CG  GLU A  57    17236   6061  15168   -932   -854    698       C  
ATOM    447  CD  GLU A  57      10.537  48.955 -17.750  1.00109.27           C  
ANISOU  447  CD  GLU A  57    18022   7333  16163  -1360   -600   1056       C  
ATOM    448  OE1 GLU A  57      11.769  49.020 -17.508  1.00117.41           O  
ANISOU  448  OE1 GLU A  57    18860   8444  17303  -1821   -572   1266       O  
ATOM    449  OE2 GLU A  57      10.070  48.692 -18.885  1.00115.44           O  
ANISOU  449  OE2 GLU A  57    18795   8283  16781  -1219   -438   1134       O  
ATOM    450  N   LEU A  58       9.738  46.045 -13.478  1.00 70.90           N  
ANISOU  450  N   LEU A  58    12107   3186  11644   -533   -412    109       N  
ATOM    451  CA  LEU A  58       9.492  45.997 -12.041  1.00 69.37           C  
ANISOU  451  CA  LEU A  58    11863   3025  11467   -336   -545    -97       C  
ATOM    452  C   LEU A  58      10.526  45.135 -11.342  1.00 67.14           C  
ANISOU  452  C   LEU A  58    11168   3003  11336   -551   -402    -38       C  
ATOM    453  O   LEU A  58      10.600  43.926 -11.600  1.00 69.04           O  
ANISOU  453  O   LEU A  58    11049   3540  11640   -515   -136      4       O  
ATOM    454  CB  LEU A  58       8.067  45.494 -11.749  1.00 67.79           C  
ANISOU  454  CB  LEU A  58    11573   3037  11147    137   -503   -291       C  
ATOM    455  CG  LEU A  58       6.872  46.458 -11.893  1.00 69.69           C  
ANISOU  455  CG  LEU A  58    12196   3098  11183    528   -723   -433       C  
ATOM    456  CD1 LEU A  58       6.825  47.162 -13.228  1.00 71.52           C  
ANISOU  456  CD1 LEU A  58    12759   3052  11362    431   -779   -291       C  
ATOM    457  CD2 LEU A  58       5.560  45.708 -11.686  1.00 67.80           C  
ANISOU  457  CD2 LEU A  58    11677   3261  10823    922   -615   -549       C  
ATOM    458  N   ARG A  59      11.255  45.725 -10.417  1.00 67.15           N  
ANISOU  458  N   ARG A  59    11249   2883  11381   -733   -612    -57       N  
ATOM    459  CA  ARG A  59      12.118  45.022  -9.515  1.00 66.76           C  
ANISOU  459  CA  ARG A  59    10829   3097  11437   -860   -542    -32       C  
ATOM    460  C   ARG A  59      11.696  45.273  -8.078  1.00 67.42           C  
ANISOU  460  C   ARG A  59    11006   3178  11432   -610   -760   -264       C  
ATOM    461  O   ARG A  59      11.251  46.335  -7.742  1.00 72.39           O  
ANISOU  461  O   ARG A  59    12055   3508  11941   -483  -1050   -427       O  
ATOM    462  CB  ARG A  59      13.555  45.440  -9.648  1.00 69.43           C  
ANISOU  462  CB  ARG A  59    11085   3414  11879  -1358   -609    183       C  
ATOM    463  CG  ARG A  59      14.151  45.283 -11.030  1.00 71.14           C  
ANISOU  463  CG  ARG A  59    11163   3741  12125  -1621   -386    454       C  
ATOM    464  CD  ARG A  59      14.299  43.839 -11.498  1.00 69.76           C  
ANISOU  464  CD  ARG A  59    10546   3973  11984  -1443     -8    496       C  
ATOM    465  NE  ARG A  59      13.746  43.723 -12.861  1.00 70.57           N  
ANISOU  465  NE  ARG A  59    10763   4056  11993  -1344    160    545       N  
ATOM    466  CZ  ARG A  59      14.367  43.243 -13.949  1.00 71.99           C  
ANISOU  466  CZ  ARG A  59    10727   4497  12129  -1432    413    718       C  
ATOM    467  NH1 ARG A  59      15.614  42.713 -13.904  1.00 73.68           N  
ANISOU  467  NH1 ARG A  59    10531   5076  12389  -1584    575    875       N  
ATOM    468  NH2 ARG A  59      13.694  43.234 -15.112  1.00 72.11           N  
ANISOU  468  NH2 ARG A  59    10916   4467  12013  -1301    514    718       N  
ATOM    469  N   HIS A  60      11.767  44.239  -7.255  1.00 65.87           N  
ANISOU  469  N   HIS A  60    10434   3329  11265   -482   -617   -281       N  
ATOM    470  CA  HIS A  60      11.444  44.301  -5.844  1.00 64.60           C  
ANISOU  470  CA  HIS A  60    10271   3297  10976   -235   -773   -462       C  
ATOM    471  C   HIS A  60      11.859  42.916  -5.348  1.00 62.61           C  
ANISOU  471  C   HIS A  60     9530   3433  10823   -242   -539   -329       C  
ATOM    472  O   HIS A  60      11.828  41.953  -6.109  1.00 59.53           O  
ANISOU  472  O   HIS A  60     8915   3152  10549   -266   -282   -189       O  
ATOM    473  CB  HIS A  60       9.958  44.536  -5.637  1.00 63.79           C  
ANISOU  473  CB  HIS A  60    10346   3233  10659    233   -815   -652       C  
ATOM    474  CG  HIS A  60       9.573  44.658  -4.208  1.00 65.45           C  
ANISOU  474  CG  HIS A  60    10547   3662  10658    551   -959   -840       C  
ATOM    475  ND1 HIS A  60       9.524  43.579  -3.357  1.00 64.18           N  
ANISOU  475  ND1 HIS A  60     9974   3937  10475    642   -795   -756       N  
ATOM    476  CD2 HIS A  60       9.232  45.735  -3.464  1.00 68.83           C  
ANISOU  476  CD2 HIS A  60    11354   3946  10853    830  -1268  -1109       C  
ATOM    477  CE1 HIS A  60       9.155  43.978  -2.154  1.00 66.25           C  
ANISOU  477  CE1 HIS A  60    10310   4385  10475    956   -964   -945       C  
ATOM    478  NE2 HIS A  60       8.982  45.285  -2.190  1.00 69.37           N  
ANISOU  478  NE2 HIS A  60    11191   4434  10730   1102  -1256  -1192       N  
ATOM    479  N   PRO A  61      12.323  42.829  -4.116  1.00 63.68           N  
ANISOU  479  N   PRO A  61     9541   3745  10908   -222   -657   -372       N  
ATOM    480  CA  PRO A  61      12.911  41.551  -3.667  1.00 62.61           C  
ANISOU  480  CA  PRO A  61     8970   3937  10882   -250   -468   -200       C  
ATOM    481  C   PRO A  61      11.883  40.451  -3.498  1.00 60.12           C  
ANISOU  481  C   PRO A  61     8468   3842  10530     25   -272   -144       C  
ATOM    482  O   PRO A  61      12.201  39.277  -3.725  1.00 60.34           O  
ANISOU  482  O   PRO A  61     8233   3983  10707    -14    -82     30       O  
ATOM    483  CB  PRO A  61      13.580  41.912  -2.307  1.00 64.62           C  
ANISOU  483  CB  PRO A  61     9186   4329  11034   -280   -705   -275       C  
ATOM    484  CG  PRO A  61      12.994  43.222  -1.932  1.00 67.03           C  
ANISOU  484  CG  PRO A  61     9932   4400  11133   -150  -1003   -544       C  
ATOM    485  CD  PRO A  61      12.690  43.930  -3.223  1.00 66.73           C  
ANISOU  485  CD  PRO A  61    10202   3985  11168   -264  -1007   -551       C  
ATOM    486  N   ASN A  62      10.719  40.818  -2.990  1.00 59.69           N  
ANISOU  486  N   ASN A  62     8540   3878  10259    308   -347   -279       N  
ATOM    487  CA  ASN A  62       9.549  39.936  -2.918  1.00 58.51           C  
ANISOU  487  CA  ASN A  62     8207   3981  10043    512   -190   -188       C  
ATOM    488  C   ASN A  62       8.671  39.809  -4.180  1.00 56.32           C  
ANISOU  488  C   ASN A  62     8007   3571   9817    523    -79   -177       C  
ATOM    489  O   ASN A  62       7.489  39.508  -4.064  1.00 55.53           O  
ANISOU  489  O   ASN A  62     7807   3702   9586    704    -35   -152       O  
ATOM    490  CB  ASN A  62       8.654  40.335  -1.733  1.00 60.87           C  
ANISOU  490  CB  ASN A  62     8500   4608  10017    851   -298   -302       C  
ATOM    491  CG  ASN A  62       9.407  40.375  -0.433  1.00 63.40           C  
ANISOU  491  CG  ASN A  62     8737   5120  10231    877   -418   -320       C  
ATOM    492  OD1 ASN A  62       9.534  41.434   0.183  1.00 67.73           O  
ANISOU  492  OD1 ASN A  62     9533   5625  10577   1024   -650   -563       O  
ATOM    493  ND2 ASN A  62       9.966  39.242  -0.028  1.00 63.56           N  
ANISOU  493  ND2 ASN A  62     8453   5315  10382    743   -299    -77       N  
ATOM    494  N   ILE A  63       9.223  40.045  -5.373  1.00 55.05           N  
ANISOU  494  N   ILE A  63     7995   3107   9814    325    -39   -177       N  
ATOM    495  CA  ILE A  63       8.565  39.620  -6.631  1.00 53.17           C  
ANISOU  495  CA  ILE A  63     7785   2779   9639    305     85   -138       C  
ATOM    496  C   ILE A  63       9.565  38.997  -7.581  1.00 52.43           C  
ANISOU  496  C   ILE A  63     7636   2536   9749     84    226    -38       C  
ATOM    497  O   ILE A  63      10.759  39.275  -7.505  1.00 51.96           O  
ANISOU  497  O   ILE A  63     7554   2425   9763    -72    217     -1       O  
ATOM    498  CB  ILE A  63       7.842  40.735  -7.384  1.00 53.16           C  
ANISOU  498  CB  ILE A  63     8088   2608   9503    421    -15   -274       C  
ATOM    499  CG1 ILE A  63       8.874  41.585  -8.105  1.00 54.57           C  
ANISOU  499  CG1 ILE A  63     8509   2466   9758    195    -73   -277       C  
ATOM    500  CG2 ILE A  63       6.901  41.492  -6.456  1.00 54.52           C  
ANISOU  500  CG2 ILE A  63     8348   2949   9419    754   -173   -422       C  
ATOM    501  CD1 ILE A  63       8.306  42.703  -8.935  1.00 56.40           C  
ANISOU  501  CD1 ILE A  63     9105   2451   9874    275   -197   -361       C  
ATOM    502  N   VAL A  64       9.058  38.113  -8.427  1.00 53.02           N  
ANISOU  502  N   VAL A  64     7666   2592   9886     88    342      4       N  
ATOM    503  CA  VAL A  64       9.915  37.305  -9.270  1.00 54.62           C  
ANISOU  503  CA  VAL A  64     7812   2705  10233    -10    481     64       C  
ATOM    504  C   VAL A  64      10.214  38.176 -10.425  1.00 56.44           C  
ANISOU  504  C   VAL A  64     8233   2803  10405    -90    506     19       C  
ATOM    505  O   VAL A  64       9.388  38.398 -11.270  1.00 56.00           O  
ANISOU  505  O   VAL A  64     8334   2675  10266    -42    496    -39       O  
ATOM    506  CB  VAL A  64       9.287  35.966  -9.696  1.00 54.66           C  
ANISOU  506  CB  VAL A  64     7769   2683  10317     29    536     96       C  
ATOM    507  CG1 VAL A  64      10.178  35.253 -10.716  1.00 55.44           C  
ANISOU  507  CG1 VAL A  64     7893   2666  10503     33    661     82       C  
ATOM    508  CG2 VAL A  64       9.108  35.056  -8.482  1.00 54.30           C  
ANISOU  508  CG2 VAL A  64     7535   2755  10339     48    497    226       C  
ATOM    509  N   SER A  65      11.443  38.661 -10.453  1.00 59.57           N  
ANISOU  509  N   SER A  65     8588   3210  10835   -238    529     84       N  
ATOM    510  CA  SER A  65      11.807  39.588 -11.474  1.00 61.37           C  
ANISOU  510  CA  SER A  65     8983   3342  10991   -384    538    118       C  
ATOM    511  C   SER A  65      11.826  38.874 -12.807  1.00 61.60           C  
ANISOU  511  C   SER A  65     9004   3408  10992   -324    721    125       C  
ATOM    512  O   SER A  65      12.441  37.765 -13.015  1.00 63.40           O  
ANISOU  512  O   SER A  65     9043   3761  11283   -235    869    140       O  
ATOM    513  CB  SER A  65      13.125  40.310 -11.152  1.00 65.51           C  
ANISOU  513  CB  SER A  65     9422   3920  11548   -643    490    243       C  
ATOM    514  OG  SER A  65      12.896  41.311 -10.111  1.00 67.93           O  
ANISOU  514  OG  SER A  65     9902   4085  11822   -698    234    174       O  
ATOM    515  N   LEU A  66      11.060  39.493 -13.670  1.00 60.86           N  
ANISOU  515  N   LEU A  66     9151   3195  10775   -311    680     87       N  
ATOM    516  CA  LEU A  66      11.001  39.205 -15.071  1.00 62.34           C  
ANISOU  516  CA  LEU A  66     9413   3416  10857   -269    808     84       C  
ATOM    517  C   LEU A  66      12.208  39.835 -15.766  1.00 65.27           C  
ANISOU  517  C   LEU A  66     9740   3906  11151   -468    918    265       C  
ATOM    518  O   LEU A  66      12.177  40.997 -16.162  1.00 66.68           O  
ANISOU  518  O   LEU A  66    10119   3976  11238   -638    829    376       O  
ATOM    519  CB  LEU A  66       9.677  39.772 -15.610  1.00 62.19           C  
ANISOU  519  CB  LEU A  66     9656   3263  10710   -180    684      5       C  
ATOM    520  CG  LEU A  66       9.404  39.858 -17.097  1.00 63.65           C  
ANISOU  520  CG  LEU A  66    10000   3464  10717   -143    750      6       C  
ATOM    521  CD1 LEU A  66       9.737  38.559 -17.776  1.00 65.43           C  
ANISOU  521  CD1 LEU A  66    10105   3821  10932    -36    910    -75       C  
ATOM    522  CD2 LEU A  66       7.949  40.200 -17.318  1.00 63.12           C  
ANISOU  522  CD2 LEU A  66    10117   3316  10549      0    590    -90       C  
ATOM    523  N   GLN A  67      13.260  39.040 -15.920  1.00 67.18           N  
ANISOU  523  N   GLN A  67     9713   4395  11416   -433   1101    317       N  
ATOM    524  CA  GLN A  67      14.537  39.481 -16.488  1.00 71.18           C  
ANISOU  524  CA  GLN A  67    10035   5181  11827   -623   1242    539       C  
ATOM    525  C   GLN A  67      14.589  39.893 -17.936  1.00 73.63           C  
ANISOU  525  C   GLN A  67    10453   5623  11901   -663   1366    648       C  
ATOM    526  O   GLN A  67      15.307  40.831 -18.255  1.00 80.48           O  
ANISOU  526  O   GLN A  67    11270   6621  12686   -975   1379    916       O  
ATOM    527  CB  GLN A  67      15.581  38.391 -16.365  1.00 74.00           C  
ANISOU  527  CB  GLN A  67    10035   5867  12212   -446   1431    543       C  
ATOM    528  CG  GLN A  67      16.485  38.527 -15.165  1.00 75.34           C  
ANISOU  528  CG  GLN A  67     9925   6167  12532   -607   1366    662       C  
ATOM    529  CD  GLN A  67      16.941  37.177 -14.631  1.00 75.38           C  
ANISOU  529  CD  GLN A  67     9690   6320  12629   -280   1456    566       C  
ATOM    530  OE1 GLN A  67      17.607  36.407 -15.342  1.00 76.93           O  
ANISOU  530  OE1 GLN A  67     9710   6804  12714    -20   1658    558       O  
ATOM    531  NE2 GLN A  67      16.589  36.891 -13.381  1.00 73.06           N  
ANISOU  531  NE2 GLN A  67     9407   5843  12508   -254   1299    499       N  
ATOM    532  N   ASP A  68      13.911  39.198 -18.821  1.00 72.68           N  
ANISOU  532  N   ASP A  68    10465   5496  11651   -387   1444    474       N  
ATOM    533  CA  ASP A  68      14.048  39.482 -20.245  1.00 77.21           C  
ANISOU  533  CA  ASP A  68    11113   6282  11939   -375   1586    576       C  
ATOM    534  C   ASP A  68      12.799  39.001 -20.973  1.00 75.80           C  
ANISOU  534  C   ASP A  68    11218   5927  11652   -120   1521    328       C  
ATOM    535  O   ASP A  68      11.988  38.305 -20.431  1.00 72.34           O  
ANISOU  535  O   ASP A  68    10855   5266  11364     24   1397    104       O  
ATOM    536  CB  ASP A  68      15.310  38.797 -20.830  1.00 82.89           C  
ANISOU  536  CB  ASP A  68    11492   7511  12492   -225   1870    652       C  
ATOM    537  CG  ASP A  68      15.983  39.582 -22.019  1.00 88.75           C  
ANISOU  537  CG  ASP A  68    12149   8659  12912   -404   2046    967       C  
ATOM    538  OD1 ASP A  68      15.542  40.687 -22.449  1.00 88.63           O  
ANISOU  538  OD1 ASP A  68    12378   8481  12816   -684   1935   1163       O  
ATOM    539  OD2 ASP A  68      16.972  39.002 -22.564  1.00 95.27           O  
ANISOU  539  OD2 ASP A  68    12652  10016  13531   -211   2307   1025       O  
ATOM    540  N   VAL A  69      12.634  39.452 -22.206  1.00 78.92           N  
ANISOU  540  N   VAL A  69    11763   6453  11768   -115   1583    412       N  
ATOM    541  CA  VAL A  69      11.520  39.065 -23.047  1.00 78.42           C  
ANISOU  541  CA  VAL A  69    11955   6292  11546    105   1505    194       C  
ATOM    542  C   VAL A  69      12.068  38.951 -24.444  1.00 83.39           C  
ANISOU  542  C   VAL A  69    12571   7310  11803    237   1715    257       C  
ATOM    543  O   VAL A  69      12.813  39.855 -24.888  1.00 88.62           O  
ANISOU  543  O   VAL A  69    13150   8220  12300     18   1838    595       O  
ATOM    544  CB  VAL A  69      10.418  40.136 -23.018  1.00 77.35           C  
ANISOU  544  CB  VAL A  69    12099   5876  11415    -20   1276    262       C  
ATOM    545  CG1 VAL A  69       9.293  39.762 -23.962  1.00 77.23           C  
ANISOU  545  CG1 VAL A  69    12294   5846  11201    194   1185     64       C  
ATOM    546  CG2 VAL A  69       9.871  40.312 -21.611  1.00 74.35           C  
ANISOU  546  CG2 VAL A  69    11715   5199  11335    -85   1082    192       C  
ATOM    547  N   LEU A  70      11.666  37.924 -25.178  1.00 83.82           N  
ANISOU  547  N   LEU A  70    12730   7425  11691    565   1730    -42       N  
ATOM    548  CA  LEU A  70      12.256  37.698 -26.487  1.00 88.90           C  
ANISOU  548  CA  LEU A  70    13349   8510  11916    784   1946    -34       C  
ATOM    549  C   LEU A  70      11.213  37.324 -27.488  1.00 91.15           C  
ANISOU  549  C   LEU A  70    13946   8727  11958   1000   1812   -295       C  
ATOM    550  O   LEU A  70      10.155  36.877 -27.115  1.00 87.76           O  
ANISOU  550  O   LEU A  70    13691   7934  11720   1016   1564   -534       O  
ATOM    551  CB  LEU A  70      13.297  36.605 -26.420  1.00 90.92           C  
ANISOU  551  CB  LEU A  70    13372   9044  12129   1097   2144   -187       C  
ATOM    552  CG  LEU A  70      14.148  36.437 -25.151  1.00 89.80           C  
ANISOU  552  CG  LEU A  70    12920   8884  12316    993   2196    -81       C  
ATOM    553  CD1 LEU A  70      14.754  35.026 -25.145  1.00 91.72           C  
ANISOU  553  CD1 LEU A  70    13075   9252  12520   1468   2291   -376       C  
ATOM    554  CD2 LEU A  70      15.225  37.502 -24.996  1.00 91.45           C  
ANISOU  554  CD2 LEU A  70    12798   9468  12481    655   2370    370       C  
ATOM    555  N   MET A  71      11.543  37.494 -28.763  1.00 98.14           N  
ANISOU  555  N   MET A  71    14868  10025  12392   1153   1975   -227       N  
ATOM    556  CA  MET A  71      10.608  37.282 -29.845  1.00104.13           C  
ANISOU  556  CA  MET A  71    15928  10793  12843   1348   1839   -446       C  
ATOM    557  C   MET A  71      11.229  36.412 -30.910  1.00110.56           C  
ANISOU  557  C   MET A  71    16749  12040  13217   1784   2024   -678       C  
ATOM    558  O   MET A  71      12.245  36.774 -31.499  1.00115.24           O  
ANISOU  558  O   MET A  71    17128  13177  13478   1852   2325   -424       O  
ATOM    559  CB  MET A  71      10.215  38.617 -30.455  1.00109.39           C  
ANISOU  559  CB  MET A  71    16713  11546  13304   1117   1810    -88       C  
ATOM    560  CG  MET A  71       9.394  39.500 -29.523  1.00108.91           C  
ANISOU  560  CG  MET A  71    16747  11024  13609    808   1566     62       C  
ATOM    561  SD  MET A  71       7.585  39.391 -29.699  1.00112.68           S  
ANISOU  561  SD  MET A  71    17515  11190  14107    905   1191   -210       S  
ATOM    562  CE  MET A  71       7.239  37.633 -29.874  1.00113.44           C  
ANISOU  562  CE  MET A  71    17645  11249  14206   1183   1093   -746       C  
ATOM    563  N   GLN A  72      10.623  35.252 -31.125  1.00112.80           N  
ANISOU  563  N   GLN A  72    17278  12093  13486   2077   1823  -1157       N  
ATOM    564  CA  GLN A  72      10.981  34.363 -32.213  1.00119.94           C  
ANISOU  564  CA  GLN A  72    18323  13318  13928   2574   1903  -1496       C  
ATOM    565  C   GLN A  72       9.852  34.515 -33.205  1.00121.16           C  
ANISOU  565  C   GLN A  72    18807  13437  13790   2591   1668  -1651       C  
ATOM    566  O   GLN A  72       9.206  35.556 -33.242  1.00118.46           O  
ANISOU  566  O   GLN A  72    18474  13049  13484   2270   1590  -1353       O  
ATOM    567  CB  GLN A  72      11.162  32.909 -31.699  1.00123.11           C  
ANISOU  567  CB  GLN A  72    18845  13392  14539   2892   1775  -1945       C  
ATOM    568  CG  GLN A  72      12.402  32.179 -32.239  1.00129.07           C  
ANISOU  568  CG  GLN A  72    19505  14615  14918   3468   2048  -2128       C  
ATOM    569  CD  GLN A  72      13.718  32.467 -31.490  1.00130.54           C  
ANISOU  569  CD  GLN A  72    19204  15154  15240   3450   2387  -1786       C  
ATOM    570  OE1 GLN A  72      14.671  31.697 -31.613  1.00135.29           O  
ANISOU  570  OE1 GLN A  72    19694  16060  15648   3954   2562  -1967       O  
ATOM    571  NE2 GLN A  72      13.797  33.586 -30.745  1.00128.50           N  
ANISOU  571  NE2 GLN A  72    18659  14885  15279   2903   2462  -1303       N  
ATOM    572  N   ASP A  73       9.623  33.509 -34.032  1.00127.37           N  
ANISOU  572  N   ASP A  73    19885  14249  14261   2992   1530  -2120       N  
ATOM    573  CA  ASP A  73       8.579  33.606 -35.051  1.00130.99           C  
ANISOU  573  CA  ASP A  73    20650  14734  14386   3025   1279  -2292       C  
ATOM    574  C   ASP A  73       7.240  33.577 -34.330  1.00126.23           C  
ANISOU  574  C   ASP A  73    20160  13559  14241   2640    874  -2355       C  
ATOM    575  O   ASP A  73       6.761  32.491 -33.937  1.00130.31           O  
ANISOU  575  O   ASP A  73    20864  13640  15005   2653    575  -2728       O  
ATOM    576  CB  ASP A  73       8.671  32.457 -36.055  1.00137.96           C  
ANISOU  576  CB  ASP A  73    21861  15740  14815   3558   1171  -2843       C  
ATOM    577  CG  ASP A  73      10.069  32.222 -36.554  1.00144.22           C  
ANISOU  577  CG  ASP A  73    22492  17121  15181   4053   1579  -2854       C  
ATOM    578  OD1 ASP A  73      11.015  32.491 -35.790  1.00143.00           O  
ANISOU  578  OD1 ASP A  73    21969  17105  15260   3974   1876  -2547       O  
ATOM    579  OD2 ASP A  73      10.214  31.691 -37.678  1.00152.05           O  
ANISOU  579  OD2 ASP A  73    23721  18456  15593   4553   1580  -3205       O  
ATOM    580  N   SER A  74       6.670  34.762 -34.109  1.00119.82           N  
ANISOU  580  N   SER A  74    19229  12755  13541   2301    856  -1965       N  
ATOM    581  CA  SER A  74       5.371  34.928 -33.422  1.00114.62           C  
ANISOU  581  CA  SER A  74    18591  11704  13255   1976    512  -1956       C  
ATOM    582  C   SER A  74       5.228  34.232 -32.038  1.00107.19           C  
ANISOU  582  C   SER A  74    17536  10306  12883   1777    385  -2048       C  
ATOM    583  O   SER A  74       4.103  34.015 -31.538  1.00101.53           O  
ANISOU  583  O   SER A  74    16828   9324  12423   1548     67  -2118       O  
ATOM    584  CB  SER A  74       4.205  34.527 -34.363  1.00120.40           C  
ANISOU  584  CB  SER A  74    19590  12451  13705   2044    146  -2259       C  
ATOM    585  OG  SER A  74       2.913  34.680 -33.747  1.00119.37           O  
ANISOU  585  OG  SER A  74    19398  12069  13886   1740   -184  -2220       O  
ATOM    586  N   ARG A  75       6.356  33.879 -31.429  1.00104.63           N  
ANISOU  586  N   ARG A  75    17075   9953  12727   1866    629  -2018       N  
ATOM    587  CA  ARG A  75       6.331  33.378 -30.073  1.00100.74           C  
ANISOU  587  CA  ARG A  75    16452   9078  12745   1676    547  -2017       C  
ATOM    588  C   ARG A  75       7.254  34.152 -29.152  1.00 96.46           C  
ANISOU  588  C   ARG A  75    15602   8620  12425   1551    842  -1653       C  
ATOM    589  O   ARG A  75       8.290  34.696 -29.552  1.00 98.20           O  
ANISOU  589  O   ARG A  75    15698   9191  12421   1659   1147  -1458       O  
ATOM    590  CB  ARG A  75       6.592  31.871 -30.013  1.00105.79           C  
ANISOU  590  CB  ARG A  75    17289   9441  13462   1890    406  -2412       C  
ATOM    591  CG  ARG A  75       7.853  31.366 -30.681  1.00112.41           C  
ANISOU  591  CG  ARG A  75    18193  10539  13975   2361    661  -2590       C  
ATOM    592  CD  ARG A  75       7.945  29.861 -30.460  1.00116.46           C  
ANISOU  592  CD  ARG A  75    18989  10628  14631   2587    426  -3002       C  
ATOM    593  NE  ARG A  75       7.007  29.070 -31.264  1.00121.02           N  
ANISOU  593  NE  ARG A  75    19998  10948  15037   2636     15  -3411       N  
ATOM    594  CZ  ARG A  75       7.192  28.729 -32.540  1.00127.90           C  
ANISOU  594  CZ  ARG A  75    21161  12038  15394   3053     -8  -3752       C  
ATOM    595  NH1 ARG A  75       8.260  29.158 -33.226  1.00131.08           N  
ANISOU  595  NH1 ARG A  75    21425  13015  15361   3470    398  -3692       N  
ATOM    596  NH2 ARG A  75       6.282  27.970 -33.159  1.00131.73           N  
ANISOU  596  NH2 ARG A  75    22067  12217  15765   3036   -459  -4145       N  
ATOM    597  N   LEU A  76       6.903  34.076 -27.879  1.00 91.01           N  
ANISOU  597  N   LEU A  76    14780   7628  12170   1311    729  -1571       N  
ATOM    598  CA  LEU A  76       7.328  35.008 -26.860  1.00 84.90           C  
ANISOU  598  CA  LEU A  76    13756   6860  11640   1102    878  -1234       C  
ATOM    599  C   LEU A  76       7.908  34.284 -25.670  1.00 82.36           C  
ANISOU  599  C   LEU A  76    13278   6344  11670   1078    913  -1256       C  
ATOM    600  O   LEU A  76       7.288  33.365 -25.134  1.00 80.92           O  
ANISOU  600  O   LEU A  76    13160   5873  11709   1029    694  -1424       O  
ATOM    601  CB  LEU A  76       6.086  35.702 -26.397  1.00 82.84           C  
ANISOU  601  CB  LEU A  76    13495   6464  11517    881    657  -1124       C  
ATOM    602  CG  LEU A  76       6.219  36.743 -25.285  1.00 79.78           C  
ANISOU  602  CG  LEU A  76    12935   6012  11363    691    712   -836       C  
ATOM    603  CD1 LEU A  76       6.775  38.024 -25.864  1.00 81.58           C  
ANISOU  603  CD1 LEU A  76    13211   6413  11371    658    865   -564       C  
ATOM    604  CD2 LEU A  76       4.870  37.004 -24.674  1.00 77.91           C  
ANISOU  604  CD2 LEU A  76    12676   5660  11264    590    460   -834       C  
ATOM    605  N   TYR A  77       9.111  34.654 -25.279  1.00 80.76           N  
ANISOU  605  N   TYR A  77    12863   6316  11503   1092   1168  -1062       N  
ATOM    606  CA  TYR A  77       9.798  33.918 -24.235  1.00 79.03           C  
ANISOU  606  CA  TYR A  77    12486   5974  11568   1133   1212  -1083       C  
ATOM    607  C   TYR A  77       9.917  34.795 -23.054  1.00 74.43           C  
ANISOU  607  C   TYR A  77    11688   5348  11241    852   1232   -806       C  
ATOM    608  O   TYR A  77      10.527  35.825 -23.132  1.00 74.69           O  
ANISOU  608  O   TYR A  77    11599   5589  11187    729   1380   -563       O  
ATOM    609  CB  TYR A  77      11.182  33.510 -24.714  1.00 83.24           C  
ANISOU  609  CB  TYR A  77    12899   6827  11901   1439   1478  -1110       C  
ATOM    610  CG  TYR A  77      11.121  32.414 -25.767  1.00 87.52           C  
ANISOU  610  CG  TYR A  77    13711   7366  12175   1837   1424  -1480       C  
ATOM    611  CD1 TYR A  77      10.925  32.745 -27.116  1.00 90.31           C  
ANISOU  611  CD1 TYR A  77    14215   7992  12104   1971   1478  -1553       C  
ATOM    612  CD2 TYR A  77      11.261  31.082 -25.421  1.00 89.13           C  
ANISOU  612  CD2 TYR A  77    14063   7277  12525   2091   1292  -1754       C  
ATOM    613  CE1 TYR A  77      10.868  31.787 -28.088  1.00 94.50           C  
ANISOU  613  CE1 TYR A  77    15030   8533  12342   2365   1402  -1931       C  
ATOM    614  CE2 TYR A  77      11.207  30.109 -26.396  1.00 94.69           C  
ANISOU  614  CE2 TYR A  77    15097   7913  12964   2483   1189  -2137       C  
ATOM    615  CZ  TYR A  77      11.007  30.477 -27.726  1.00 97.07           C  
ANISOU  615  CZ  TYR A  77    15537   8520  12825   2625   1245  -2244       C  
ATOM    616  OH  TYR A  77      10.968  29.526 -28.703  1.00102.77           O  
ANISOU  616  OH  TYR A  77    16619   9192  13237   3054   1121  -2667       O  
ATOM    617  N   LEU A  78       9.350  34.391 -21.949  1.00 71.18           N  
ANISOU  617  N   LEU A  78    11240   4674  11129    736   1064   -829       N  
ATOM    618  CA  LEU A  78       9.494  35.159 -20.738  1.00 68.75           C  
ANISOU  618  CA  LEU A  78    10743   4344  11032    527   1068   -611       C  
ATOM    619  C   LEU A  78      10.571  34.605 -19.872  1.00 67.66           C  
ANISOU  619  C   LEU A  78    10398   4238  11071    582   1174   -560       C  
ATOM    620  O   LEU A  78      10.458  33.467 -19.457  1.00 68.00           O  
ANISOU  620  O   LEU A  78    10470   4106  11260    690   1088   -686       O  
ATOM    621  CB  LEU A  78       8.178  35.136 -19.993  1.00 68.53           C  
ANISOU  621  CB  LEU A  78    10748   4127  11163    395    835   -633       C  
ATOM    622  CG  LEU A  78       7.191  36.264 -20.350  1.00 70.24           C  
ANISOU  622  CG  LEU A  78    11065   4381  11239    320    730   -572       C  
ATOM    623  CD1 LEU A  78       7.111  36.591 -21.837  1.00 73.42           C  
ANISOU  623  CD1 LEU A  78    11657   4897  11343    410    769   -619       C  
ATOM    624  CD2 LEU A  78       5.820  35.880 -19.847  1.00 69.81           C  
ANISOU  624  CD2 LEU A  78    10985   4261  11275    265    507   -632       C  
ATOM    625  N   ILE A  79      11.612  35.369 -19.597  1.00 67.20           N  
ANISOU  625  N   ILE A  79    10138   4395  11000    491   1330   -359       N  
ATOM    626  CA  ILE A  79      12.739  34.861 -18.834  1.00 68.80           C  
ANISOU  626  CA  ILE A  79    10089   4717  11333    568   1434   -296       C  
ATOM    627  C   ILE A  79      12.695  35.331 -17.409  1.00 67.05           C  
ANISOU  627  C   ILE A  79     9733   4397  11342    351   1326   -160       C  
ATOM    628  O   ILE A  79      12.710  36.482 -17.189  1.00 66.25           O  
ANISOU  628  O   ILE A  79     9619   4325  11224    125   1294    -17       O  
ATOM    629  CB  ILE A  79      14.069  35.306 -19.413  1.00 71.35           C  
ANISOU  629  CB  ILE A  79    10183   5456  11468    590   1673   -133       C  
ATOM    630  CG1 ILE A  79      14.123  35.085 -20.926  1.00 74.41           C  
ANISOU  630  CG1 ILE A  79    10692   6052  11526    818   1809   -237       C  
ATOM    631  CG2 ILE A  79      15.202  34.525 -18.762  1.00 73.43           C  
ANISOU  631  CG2 ILE A  79    10160   5909  11828    783   1776   -111       C  
ATOM    632  CD1 ILE A  79      13.877  33.664 -21.395  1.00 75.73           C  
ANISOU  632  CD1 ILE A  79    11050   6084  11638   1227   1771   -568       C  
ATOM    633  N   PHE A  80      12.603  34.395 -16.465  1.00 69.91           N  
ANISOU  633  N   PHE A  80    10040   4621  11901    440   1243   -213       N  
ATOM    634  CA  PHE A  80      12.522  34.663 -15.040  1.00 70.96           C  
ANISOU  634  CA  PHE A  80    10042   4706  12214    291   1137   -102       C  
ATOM    635  C   PHE A  80      13.696  34.037 -14.352  1.00 72.30           C  
ANISOU  635  C   PHE A  80     9967   5018  12483    409   1212    -27       C  
ATOM    636  O   PHE A  80      14.288  33.092 -14.884  1.00 75.52           O  
ANISOU  636  O   PHE A  80    10360   5476  12857    678   1308   -106       O  
ATOM    637  CB  PHE A  80      11.280  34.003 -14.441  1.00 73.56           C  
ANISOU  637  CB  PHE A  80    10484   4804  12661    283    959   -165       C  
ATOM    638  CG  PHE A  80       9.987  34.461 -15.022  1.00 79.54           C  
ANISOU  638  CG  PHE A  80    11424   5476  13318    204    855   -237       C  
ATOM    639  CD1 PHE A  80       9.348  35.674 -14.536  1.00 82.32           C  
ANISOU  639  CD1 PHE A  80    11782   5875  13618     84    772   -177       C  
ATOM    640  CD2 PHE A  80       9.342  33.719 -16.012  1.00 81.65           C  
ANISOU  640  CD2 PHE A  80    11876   5621  13523    278    801   -383       C  
ATOM    641  CE1 PHE A  80       8.125  36.149 -15.061  1.00 82.01           C  
ANISOU  641  CE1 PHE A  80    11887   5814  13460     79    667   -235       C  
ATOM    642  CE2 PHE A  80       8.128  34.205 -16.551  1.00 84.90           C  
ANISOU  642  CE2 PHE A  80    12413   6023  13822    203    687   -433       C  
ATOM    643  CZ  PHE A  80       7.515  35.410 -16.076  1.00 85.31           C  
ANISOU  643  CZ  PHE A  80    12424   6170  13817    122    632   -347       C  
ATOM    644  N   GLU A  81      13.974  34.486 -13.135  1.00 78.16           N  
ANISOU  644  N   GLU A  81    10319   5837  13538   -370   2119    472       N  
ATOM    645  CA  GLU A  81      14.927  33.778 -12.265  1.00 80.46           C  
ANISOU  645  CA  GLU A  81    10252   6059  14260   -372   1984    560       C  
ATOM    646  C   GLU A  81      14.399  32.402 -11.910  1.00 79.68           C  
ANISOU  646  C   GLU A  81    10160   6009  14106   -262   1922    506       C  
ATOM    647  O   GLU A  81      13.201  32.262 -11.695  1.00 75.45           O  
ANISOU  647  O   GLU A  81     9885   5591  13190   -226   1780    407       O  
ATOM    648  CB  GLU A  81      15.226  34.548 -10.972  1.00 83.16           C  
ANISOU  648  CB  GLU A  81    10459   6416  14722   -491   1573    631       C  
ATOM    649  CG  GLU A  81      14.094  34.616  -9.949  1.00 83.58           C  
ANISOU  649  CG  GLU A  81    10726   6611  14418   -499   1212    550       C  
ATOM    650  CD  GLU A  81      14.427  35.468  -8.723  1.00 87.14           C  
ANISOU  650  CD  GLU A  81    11079   7083  14946   -651    839    580       C  
ATOM    651  OE1 GLU A  81      15.071  34.900  -7.775  1.00 85.17           O  
ANISOU  651  OE1 GLU A  81    10579   6856  14925   -689    592    679       O  
ATOM    652  OE2 GLU A  81      14.032  36.707  -8.746  1.00 86.20           O  
ANISOU  652  OE2 GLU A  81    11139   6951  14660   -736    799    507       O  
ATOM    653  N   PHE A  82      15.298  31.406 -11.804  1.00 82.27           N  
ANISOU  653  N   PHE A  82    10174   6226  14857   -209   2026    588       N  
ATOM    654  CA  PHE A  82      14.917  30.014 -11.519  1.00 81.81           C  
ANISOU  654  CA  PHE A  82    10081   6163  14839    -97   2013    561       C  
ATOM    655  C   PHE A  82      14.776  29.711 -10.025  1.00 80.15           C  
ANISOU  655  C   PHE A  82     9753   6023  14677   -112   1560    681       C  
ATOM    656  O   PHE A  82      15.770  29.677  -9.318  1.00 81.67           O  
ANISOU  656  O   PHE A  82     9616   6158  15253   -153   1383    859       O  
ATOM    657  CB  PHE A  82      15.925  28.991 -12.082  1.00 85.83           C  
ANISOU  657  CB  PHE A  82    10291   6484  15836    -16   2362    604       C  
ATOM    658  CG  PHE A  82      15.526  27.590 -11.773  1.00 85.65           C  
ANISOU  658  CG  PHE A  82    10224   6418  15899     96   2357    582       C  
ATOM    659  CD1 PHE A  82      14.453  27.026 -12.418  1.00 84.78           C  
ANISOU  659  CD1 PHE A  82    10422   6357  15432    150   2528    374       C  
ATOM    660  CD2 PHE A  82      16.152  26.872 -10.765  1.00 88.08           C  
ANISOU  660  CD2 PHE A  82    10189   6647  16630    136   2135    786       C  
ATOM    661  CE1 PHE A  82      14.030  25.746 -12.111  1.00 84.70           C  
ANISOU  661  CE1 PHE A  82    10376   6288  15518    242   2525    345       C  
ATOM    662  CE2 PHE A  82      15.740  25.587 -10.446  1.00 87.19           C  
ANISOU  662  CE2 PHE A  82    10038   6474  16614    242   2129    794       C  
ATOM    663  CZ  PHE A  82      14.680  25.027 -11.128  1.00 85.85           C  
ANISOU  663  CZ  PHE A  82    10177   6328  16114    294   2341    562       C  
ATOM    664  N   LEU A  83      13.564  29.449  -9.560  1.00 78.10           N  
ANISOU  664  N   LEU A  83     9748   5890  14036    -85   1377    596       N  
ATOM    665  CA  LEU A  83      13.326  29.021  -8.177  1.00 79.47           C  
ANISOU  665  CA  LEU A  83     9851   6145  14197    -98    990    711       C  
ATOM    666  C   LEU A  83      12.736  27.620  -8.222  1.00 81.91           C  
ANISOU  666  C   LEU A  83    10185   6419  14517     26   1090    687       C  
ATOM    667  O   LEU A  83      11.860  27.328  -9.039  1.00 85.54           O  
ANISOU  667  O   LEU A  83    10885   6886  14728     82   1314    504       O  
ATOM    668  CB  LEU A  83      12.373  29.971  -7.511  1.00 75.85           C  
ANISOU  668  CB  LEU A  83     9671   5852  13296   -185    715    628       C  
ATOM    669  CG  LEU A  83      13.026  31.332  -7.315  1.00 77.26           C  
ANISOU  669  CG  LEU A  83     9795   6034  13526   -325    592    651       C  
ATOM    670  CD1 LEU A  83      12.063  32.498  -7.501  1.00 76.28           C  
ANISOU  670  CD1 LEU A  83     9998   5983  12999   -379    575    492       C  
ATOM    671  CD2 LEU A  83      13.676  31.399  -5.951  1.00 78.70           C  
ANISOU  671  CD2 LEU A  83     9765   6274  13860   -433    198    806       C  
ATOM    672  N   SER A  84      13.221  26.753  -7.332  1.00 83.83           N  
ANISOU  672  N   SER A  84    10170   6618  15062     59    909    886       N  
ATOM    673  CA  SER A  84      12.897  25.306  -7.325  1.00 83.53           C  
ANISOU  673  CA  SER A  84    10072   6483  15182    183   1025    915       C  
ATOM    674  C   SER A  84      11.789  24.906  -6.337  1.00 78.73           C  
ANISOU  674  C   SER A  84     9647   6009  14256    182    752    941       C  
ATOM    675  O   SER A  84      11.302  23.763  -6.364  1.00 80.92           O  
ANISOU  675  O   SER A  84     9927   6207  14612    275    858    939       O  
ATOM    676  CB  SER A  84      14.168  24.531  -6.993  1.00 86.88           C  
ANISOU  676  CB  SER A  84    10057   6738  16216    237   1021   1170       C  
ATOM    677  OG  SER A  84      14.947  25.268  -6.046  1.00 89.25           O  
ANISOU  677  OG  SER A  84    10163   7128  16617    126    651   1379       O  
ATOM    678  N   MET A  85      11.376  25.859  -5.516  1.00 72.30           N  
ANISOU  678  N   MET A  85     8994   5383  13094     71    440    947       N  
ATOM    679  CA  MET A  85      10.382  25.622  -4.515  1.00 68.24           C  
ANISOU  679  CA  MET A  85     8656   5009  12261     50    197    973       C  
ATOM    680  C   MET A  85       9.263  26.614  -4.675  1.00 64.70           C  
ANISOU  680  C   MET A  85     8557   4694  11329     -6    188    744       C  
ATOM    681  O   MET A  85       9.478  27.765  -5.054  1.00 64.86           O  
ANISOU  681  O   MET A  85     8648   4741  11253    -76    204    648       O  
ATOM    682  CB  MET A  85      10.997  25.781  -3.140  1.00 68.74           C  
ANISOU  682  CB  MET A  85     8562   5180  12375    -47   -200   1222       C  
ATOM    683  CG  MET A  85      10.072  25.444  -1.975  1.00 67.86           C  
ANISOU  683  CG  MET A  85     8623   5226  11933    -81   -446   1290       C  
ATOM    684  SD  MET A  85       9.398  23.749  -1.812  1.00 67.59           S  
ANISOU  684  SD  MET A  85     8559   5095  12026     60   -333   1413       S  
ATOM    685  CE  MET A  85      10.823  22.800  -2.340  1.00 70.55           C  
ANISOU  685  CE  MET A  85     8491   5216  13096    171   -185   1631       C  
ATOM    686  N   ASP A  86       8.061  26.162  -4.374  1.00 62.25           N  
ANISOU  686  N   ASP A  86     8447   4451  10753     26    170    671       N  
ATOM    687  CA  ASP A  86       6.920  27.047  -4.213  1.00 59.78           C  
ANISOU  687  CA  ASP A  86     8431   4270  10010    -26    106    498       C  
ATOM    688  C   ASP A  86       6.150  26.641  -3.010  1.00 59.37           C  
ANISOU  688  C   ASP A  86     8474   4331   9753    -51    -91    568       C  
ATOM    689  O   ASP A  86       6.423  25.643  -2.371  1.00 61.80           O  
ANISOU  689  O   ASP A  86     8638   4619  10222    -25   -177    760       O  
ATOM    690  CB  ASP A  86       6.017  27.014  -5.415  1.00 58.26           C  
ANISOU  690  CB  ASP A  86     8419   4039   9676     44    368    285       C  
ATOM    691  CG  ASP A  86       5.465  25.691  -5.643  1.00 57.50           C  
ANISOU  691  CG  ASP A  86     8309   3874   9663    134    501    269       C  
ATOM    692  OD1 ASP A  86       6.187  24.883  -6.255  1.00 61.35           O  
ANISOU  692  OD1 ASP A  86     8623   4220  10467    194    685    304       O  
ATOM    693  OD2 ASP A  86       4.336  25.444  -5.220  1.00 55.68           O  
ANISOU  693  OD2 ASP A  86     8227   3712   9216    140    444    214       O  
ATOM    694  N   LEU A  87       5.237  27.485  -2.641  1.00 58.83           N  
ANISOU  694  N   LEU A  87     8638   4375   9337   -111   -164    431       N  
ATOM    695  CA  LEU A  87       4.640  27.347  -1.363  1.00 59.93           C  
ANISOU  695  CA  LEU A  87     8879   4642   9247   -172   -354    493       C  
ATOM    696  C   LEU A  87       3.669  26.179  -1.291  1.00 58.45           C  
ANISOU  696  C   LEU A  87     8740   4434   9034    -84   -251    513       C  
ATOM    697  O   LEU A  87       3.482  25.574  -0.229  1.00 58.50           O  
ANISOU  697  O   LEU A  87     8744   4512   8971   -113   -386    669       O  
ATOM    698  CB  LEU A  87       3.910  28.623  -1.052  1.00 58.73           C  
ANISOU  698  CB  LEU A  87     8958   4584   8770   -256   -401    306       C  
ATOM    699  CG  LEU A  87       3.520  28.624   0.400  1.00 61.83           C  
ANISOU  699  CG  LEU A  87     9460   5127   8904   -358   -599    362       C  
ATOM    700  CD1 LEU A  87       4.730  29.032   1.235  1.00 65.03           C  
ANISOU  700  CD1 LEU A  87     9751   5613   9343   -500   -867    497       C  
ATOM    701  CD2 LEU A  87       2.340  29.582   0.553  1.00 62.77           C  
ANISOU  701  CD2 LEU A  87     9830   5293   8725   -390   -527    129       C  
ATOM    702  N   LYS A  88       2.974  25.920  -2.386  1.00 56.51           N  
ANISOU  702  N   LYS A  88     8557   4102   8813      5    -21    350       N  
ATOM    703  CA  LYS A  88       2.107  24.706  -2.465  1.00 58.05           C  
ANISOU  703  CA  LYS A  88     8762   4239   9053     82     97    350       C  
ATOM    704  C   LYS A  88       2.880  23.407  -2.176  1.00 56.28           C  
ANISOU  704  C   LYS A  88     8311   3906   9165    132     96    579       C  
ATOM    705  O   LYS A  88       2.496  22.623  -1.340  1.00 54.92           O  
ANISOU  705  O   LYS A  88     8126   3747   8993    135     31    727       O  
ATOM    706  CB  LYS A  88       1.538  24.587  -3.862  1.00 59.35           C  
ANISOU  706  CB  LYS A  88     8987   4320   9242    150    328    138       C  
ATOM    707  CG  LYS A  88       0.489  23.529  -4.014  1.00 59.77           C  
ANISOU  707  CG  LYS A  88     9074   4319   9314    201    442     76       C  
ATOM    708  CD  LYS A  88       0.238  23.271  -5.469  1.00 60.12           C  
ANISOU  708  CD  LYS A  88     9145   4279   9417    244    651   -123       C  
ATOM    709  CE  LYS A  88      -0.646  22.075  -5.541  1.00 63.71           C  
ANISOU  709  CE  LYS A  88     9592   4654   9958    275    750   -178       C  
ATOM    710  NZ  LYS A  88      -1.003  21.911  -6.960  1.00 66.55           N  
ANISOU  710  NZ  LYS A  88    10015   4968  10303    284    925   -412       N  
ATOM    711  N   LYS A  89       4.000  23.303  -2.860  1.00 55.86           N  
ANISOU  711  N   LYS A  89     8077   3740   9407    166    174    620       N  
ATOM    712  CA  LYS A  89       4.945  22.278  -2.696  1.00 58.92           C  
ANISOU  712  CA  LYS A  89     8203   3993  10191    221    184    842       C  
ATOM    713  C   LYS A  89       5.395  22.238  -1.249  1.00 59.58           C  
ANISOU  713  C   LYS A  89     8201   4190  10244    153   -126   1136       C  
ATOM    714  O   LYS A  89       5.319  21.228  -0.605  1.00 59.82           O  
ANISOU  714  O   LYS A  89     8140   4178  10410    188   -177   1349       O  
ATOM    715  CB  LYS A  89       6.089  22.525  -3.658  1.00 61.67           C  
ANISOU  715  CB  LYS A  89     8382   4222  10824    248    327    806       C  
ATOM    716  CG  LYS A  89       6.777  21.291  -4.152  1.00 67.33           C  
ANISOU  716  CG  LYS A  89     8849   4709  12022    351    531    898       C  
ATOM    717  CD  LYS A  89       7.716  21.611  -5.298  1.00 72.56           C  
ANISOU  717  CD  LYS A  89     9395   5255  12917    375    763    789       C  
ATOM    718  CE  LYS A  89       8.934  20.697  -5.218  1.00 79.43           C  
ANISOU  718  CE  LYS A  89     9902   5917  14358    452    836   1016       C  
ATOM    719  NZ  LYS A  89       9.818  20.830  -6.405  1.00 84.31           N  
ANISOU  719  NZ  LYS A  89    10394   6386  15252    485   1148    891       N  
ATOM    720  N   TYR A  90       5.806  23.366  -0.715  1.00 59.44           N  
ANISOU  720  N   TYR A  90     8235   4327  10021     41   -342   1146       N  
ATOM    721  CA  TYR A  90       6.301  23.436   0.681  1.00 60.42           C  
ANISOU  721  CA  TYR A  90     8300   4602  10054    -61   -680   1411       C  
ATOM    722  C   TYR A  90       5.266  22.865   1.645  1.00 58.87           C  
ANISOU  722  C   TYR A  90     8267   4509   9591    -81   -747   1498       C  
ATOM    723  O   TYR A  90       5.532  21.998   2.430  1.00 60.07           O  
ANISOU  723  O   TYR A  90     8300   4669   9855    -75   -882   1794       O  
ATOM    724  CB  TYR A  90       6.641  24.922   1.044  1.00 60.57           C  
ANISOU  724  CB  TYR A  90     8426   4780   9806   -213   -873   1299       C  
ATOM    725  CG  TYR A  90       7.241  25.062   2.405  1.00 63.13           C  
ANISOU  725  CG  TYR A  90     8697   5279  10008   -354  -1240   1536       C  
ATOM    726  CD1 TYR A  90       8.587  24.797   2.621  1.00 66.09           C  
ANISOU  726  CD1 TYR A  90     8761   5623  10726   -376  -1436   1802       C  
ATOM    727  CD2 TYR A  90       6.462  25.400   3.493  1.00 63.64           C  
ANISOU  727  CD2 TYR A  90     9014   5545   9618   -473  -1393   1506       C  
ATOM    728  CE1 TYR A  90       9.151  24.877   3.888  1.00 69.45           C  
ANISOU  728  CE1 TYR A  90     9129   6236  11022   -523  -1823   2048       C  
ATOM    729  CE2 TYR A  90       7.019  25.473   4.773  1.00 67.09           C  
ANISOU  729  CE2 TYR A  90     9428   6176   9886   -628  -1747   1730       C  
ATOM    730  CZ  TYR A  90       8.359  25.204   4.963  1.00 69.96           C  
ANISOU  730  CZ  TYR A  90     9481   6525  10573   -656  -1984   2008       C  
ATOM    731  OH  TYR A  90       8.855  25.231   6.250  1.00 73.71           O  
ANISOU  731  OH  TYR A  90     9941   7221  10845   -825  -2376   2251       O  
ATOM    732  N   LEU A  91       4.069  23.394   1.558  1.00 56.69           N  
ANISOU  732  N   LEU A  91     8259   4305   8975   -103   -640   1248       N  
ATOM    733  CA  LEU A  91       3.029  23.042   2.500  1.00 57.15           C  
ANISOU  733  CA  LEU A  91     8491   4473   8747   -140   -674   1299       C  
ATOM    734  C   LEU A  91       2.750  21.572   2.457  1.00 57.96           C  
ANISOU  734  C   LEU A  91     8473   4433   9115    -33   -553   1478       C  
ATOM    735  O   LEU A  91       2.580  20.954   3.498  1.00 60.45           O  
ANISOU  735  O   LEU A  91     8797   4822   9347    -69   -672   1727       O  
ATOM    736  CB  LEU A  91       1.727  23.776   2.205  1.00 54.60           C  
ANISOU  736  CB  LEU A  91     8427   4197   8121   -151   -517    984       C  
ATOM    737  CG  LEU A  91       1.598  25.193   2.716  1.00 54.24           C  
ANISOU  737  CG  LEU A  91     8571   4311   7727   -280   -633    819       C  
ATOM    738  CD1 LEU A  91       0.545  25.884   1.860  1.00 52.52           C  
ANISOU  738  CD1 LEU A  91     8504   4039   7411   -229   -422    512       C  
ATOM    739  CD2 LEU A  91       1.198  25.309   4.170  1.00 55.45           C  
ANISOU  739  CD2 LEU A  91     8889   4656   7523   -409   -784    907       C  
ATOM    740  N   ASP A  92       2.748  21.005   1.256  1.00 56.75           N  
ANISOU  740  N   ASP A  92     8208   4069   9283     86   -311   1358       N  
ATOM    741  CA  ASP A  92       2.591  19.569   1.108  1.00 57.56           C  
ANISOU  741  CA  ASP A  92     8167   3982   9720    186   -166   1502       C  
ATOM    742  C   ASP A  92       3.644  18.738   1.864  1.00 60.79           C  
ANISOU  742  C   ASP A  92     8323   4334  10438    206   -335   1915       C  
ATOM    743  O   ASP A  92       3.338  17.675   2.357  1.00 61.28           O  
ANISOU  743  O   ASP A  92     8323   4312  10648    247   -309   2133       O  
ATOM    744  CB  ASP A  92       2.646  19.144  -0.363  1.00 56.10           C  
ANISOU  744  CB  ASP A  92     7894   3574   9847    288    123   1276       C  
ATOM    745  CG  ASP A  92       2.268  17.655  -0.533  1.00 56.55           C  
ANISOU  745  CG  ASP A  92     7836   3407  10242    375    312   1353       C  
ATOM    746  OD1 ASP A  92       1.213  17.318  -0.001  1.00 56.07           O  
ANISOU  746  OD1 ASP A  92     7899   3390  10012    351    321   1364       O  
ATOM    747  OD2 ASP A  92       2.998  16.870  -1.184  1.00 56.07           O  
ANISOU  747  OD2 ASP A  92     7562   3118  10624    460    470   1389       O  
ATOM    748  N   SER A  93       4.881  19.245   1.887  1.00 62.42           N  
ANISOU  748  N   SER A  93     8368   4572  10777    179   -501   2025       N  
ATOM    749  CA  SER A  93       6.020  18.573   2.482  1.00 66.63           C  
ANISOU  749  CA  SER A  93     8608   5046  11662    202   -691   2428       C  
ATOM    750  C   SER A  93       6.014  18.547   4.006  1.00 70.82           C  
ANISOU  750  C   SER A  93     9196   5806  11905     89  -1034   2763       C  
ATOM    751  O   SER A  93       6.906  17.925   4.607  1.00 74.69           O  
ANISOU  751  O   SER A  93     9436   6268  12674    103  -1241   3162       O  
ATOM    752  CB  SER A  93       7.345  19.177   1.974  1.00 67.00           C  
ANISOU  752  CB  SER A  93     8434   5052  11969    199   -758   2430       C  
ATOM    753  OG  SER A  93       7.648  20.376   2.622  1.00 66.24           O  
ANISOU  753  OG  SER A  93     8446   5207  11514     44  -1046   2414       O  
ATOM    754  N   ILE A  94       5.058  19.220   4.637  1.00 70.88           N  
ANISOU  754  N   ILE A  94     9522   6040  11368    -26  -1098   2617       N  
ATOM    755  CA  ILE A  94       5.014  19.254   6.098  1.00 74.75           C  
ANISOU  755  CA  ILE A  94    10120   6781  11501   -163  -1402   2901       C  
ATOM    756  C   ILE A  94       4.418  17.961   6.629  1.00 76.44           C  
ANISOU  756  C   ILE A  94    10313   6915  11815    -99  -1327   3190       C  
ATOM    757  O   ILE A  94       3.316  17.572   6.208  1.00 73.52           O  
ANISOU  757  O   ILE A  94    10068   6432  11432    -34  -1038   2997       O  
ATOM    758  CB  ILE A  94       4.222  20.480   6.620  1.00 74.10           C  
ANISOU  758  CB  ILE A  94    10393   6957  10801   -322  -1454   2615       C  
ATOM    759  CG1 ILE A  94       5.057  21.736   6.427  1.00 74.82           C  
ANISOU  759  CG1 ILE A  94    10471   7145  10811   -422  -1622   2443       C  
ATOM    760  CG2 ILE A  94       3.885  20.352   8.099  1.00 77.01           C  
ANISOU  760  CG2 ILE A  94    10940   7580  10739   -467  -1671   2862       C  
ATOM    761  CD1 ILE A  94       4.228  22.998   6.459  1.00 73.42           C  
ANISOU  761  CD1 ILE A  94    10611   7102  10181   -527  -1545   2052       C  
ATOM    762  N   PRO A  95       5.117  17.319   7.585  1.00 81.10           N  
ANISOU  762  N   PRO A  95    10744   7569  12501   -130  -1602   3668       N  
ATOM    763  CA  PRO A  95       4.618  16.047   8.031  1.00 83.64           C  
ANISOU  763  CA  PRO A  95    11018   7774  12985    -58  -1513   3983       C  
ATOM    764  C   PRO A  95       3.351  16.224   8.839  1.00 84.17           C  
ANISOU  764  C   PRO A  95    11437   8047  12496   -169  -1458   3912       C  
ATOM    765  O   PRO A  95       3.147  17.277   9.418  1.00 82.57           O  
ANISOU  765  O   PRO A  95    11485   8127  11760   -329  -1602   3752       O  
ATOM    766  CB  PRO A  95       5.762  15.467   8.890  1.00 88.34           C  
ANISOU  766  CB  PRO A  95    11351   8418  13795    -75  -1872   4552       C  
ATOM    767  CG  PRO A  95       6.943  16.325   8.639  1.00 88.53           C  
ANISOU  767  CG  PRO A  95    11215   8517  13904   -125  -2105   4495       C  
ATOM    768  CD  PRO A  95       6.367  17.668   8.276  1.00 85.10           C  
ANISOU  768  CD  PRO A  95    11088   8242  13004   -231  -2011   3967       C  
ATOM    769  N   PRO A  96       2.526  15.156   8.916  1.00 86.26           N  
ANISOU  769  N   PRO A  96    11705   8150  12917    -91  -1234   4044       N  
ATOM    770  CA  PRO A  96       1.214  15.333   9.522  1.00 86.33           C  
ANISOU  770  CA  PRO A  96    12033   8315  12452   -184  -1099   3921       C  
ATOM    771  C   PRO A  96       1.346  15.417  11.028  1.00 91.65           C  
ANISOU  771  C   PRO A  96    12863   9306  12652   -351  -1390   4292       C  
ATOM    772  O   PRO A  96       2.222  14.767  11.613  1.00 96.00           O  
ANISOU  772  O   PRO A  96    13225   9873  13378   -349  -1648   4776       O  
ATOM    773  CB  PRO A  96       0.450  14.086   9.087  1.00 86.71           C  
ANISOU  773  CB  PRO A  96    11979   8059  12905    -52   -782   3980       C  
ATOM    774  CG  PRO A  96       1.475  13.112   8.538  1.00 86.91           C  
ANISOU  774  CG  PRO A  96    11634   7785  13602     97   -795   4241       C  
ATOM    775  CD  PRO A  96       2.820  13.742   8.583  1.00 86.85           C  
ANISOU  775  CD  PRO A  96    11480   7893  13625     70  -1106   4348       C  
ATOM    776  N   GLY A  97       0.530  16.264  11.642  1.00 93.70           N  
ANISOU  776  N   GLY A  97    13461   9824  12313   -502  -1359   4064       N  
ATOM    777  CA  GLY A  97       0.653  16.575  13.066  1.00 98.61           C  
ANISOU  777  CA  GLY A  97    14302  10804  12360   -706  -1630   4322       C  
ATOM    778  C   GLY A  97       1.468  17.837  13.366  1.00100.59           C  
ANISOU  778  C   GLY A  97    14646  11318  12253   -868  -1947   4160       C  
ATOM    779  O   GLY A  97       1.240  18.450  14.412  1.00103.65           O  
ANISOU  779  O   GLY A  97    15323  12023  12033  -1074  -2079   4146       O  
ATOM    780  N   GLN A  98       2.456  18.171  12.515  1.00 99.78           N  
ANISOU  780  N   GLN A  98    14295  11086  12528   -792  -2067   4060       N  
ATOM    781  CA  GLN A  98       3.250  19.418  12.622  1.00101.75           C  
ANISOU  781  CA  GLN A  98    14594  11530  12533   -940  -2338   3858       C  
ATOM    782  C   GLN A  98       2.626  20.567  11.865  1.00 98.20           C  
ANISOU  782  C   GLN A  98    14321  11037  11953   -941  -2090   3276       C  
ATOM    783  O   GLN A  98       1.795  20.359  10.984  1.00 99.42           O  
ANISOU  783  O   GLN A  98    14475  10972  12328   -792  -1740   3038       O  
ATOM    784  CB  GLN A  98       4.655  19.240  12.073  1.00102.85           C  
ANISOU  784  CB  GLN A  98    14352  11538  13186   -861  -2572   4056       C  
ATOM    785  CG  GLN A  98       5.531  18.377  12.953  1.00109.29           C  
ANISOU  785  CG  GLN A  98    14963  12449  14112   -897  -2937   4665       C  
ATOM    786  CD  GLN A  98       6.867  18.100  12.302  1.00111.69           C  
ANISOU  786  CD  GLN A  98    14829  12558  15047   -782  -3106   4864       C  
ATOM    787  OE1 GLN A  98       7.325  18.880  11.442  1.00109.21           O  
ANISOU  787  OE1 GLN A  98    14423  12151  14920   -758  -3050   4530       O  
ATOM    788  NE2 GLN A  98       7.521  16.992  12.714  1.00115.30           N  
ANISOU  788  NE2 GLN A  98    14997  12942  15867   -709  -3305   5431       N  
ATOM    789  N   TYR A  99       3.012  21.779  12.236  1.00 96.05           N  
ANISOU  789  N   TYR A  99    14198  10972  11323  -1121  -2285   3057       N  
ATOM    790  CA  TYR A  99       2.500  22.955  11.591  1.00 91.95           C  
ANISOU  790  CA  TYR A  99    13837  10405  10695  -1132  -2077   2540       C  
ATOM    791  C   TYR A  99       3.644  23.864  11.308  1.00 92.82           C  
ANISOU  791  C   TYR A  99    13822  10543  10899  -1213  -2323   2433       C  
ATOM    792  O   TYR A  99       4.740  23.659  11.819  1.00 96.50           O  
ANISOU  792  O   TYR A  99    14122  11123  11418  -1301  -2681   2743       O  
ATOM    793  CB  TYR A  99       1.482  23.669  12.459  1.00 92.66           C  
ANISOU  793  CB  TYR A  99    14314  10703  10190  -1297  -1965   2293       C  
ATOM    794  CG  TYR A  99       0.231  22.865  12.613  1.00 92.53           C  
ANISOU  794  CG  TYR A  99    14408  10625  10124  -1209  -1654   2346       C  
ATOM    795  CD1 TYR A  99       0.129  21.867  13.575  1.00 96.00           C  
ANISOU  795  CD1 TYR A  99    14884  11189  10403  -1257  -1739   2759       C  
ATOM    796  CD2 TYR A  99      -0.848  23.078  11.782  1.00 89.74           C  
ANISOU  796  CD2 TYR A  99    14104  10082   9910  -1079  -1284   2011       C  
ATOM    797  CE1 TYR A  99      -1.019  21.112  13.705  1.00 96.21           C  
ANISOU  797  CE1 TYR A  99    14994  11138  10424  -1182  -1433   2817       C  
ATOM    798  CE2 TYR A  99      -2.004  22.331  11.905  1.00 89.92           C  
ANISOU  798  CE2 TYR A  99    14196  10035   9932  -1007  -1002   2057       C  
ATOM    799  CZ  TYR A  99      -2.081  21.356  12.870  1.00 93.91           C  
ANISOU  799  CZ  TYR A  99    14737  10652  10291  -1060  -1064   2451       C  
ATOM    800  OH  TYR A  99      -3.230  20.622  12.964  1.00 97.31           O  
ANISOU  800  OH  TYR A  99    15220  10992  10761   -994   -763   2495       O  
ATOM    801  N   MET A 100       3.375  24.845  10.452  1.00 89.05           N  
ANISOU  801  N   MET A 100    13404   9949  10482  -1178  -2128   2015       N  
ATOM    802  CA  MET A 100       4.356  25.819  10.050  1.00 89.25           C  
ANISOU  802  CA  MET A 100    13320   9961  10630  -1251  -2294   1864       C  
ATOM    803  C   MET A 100       4.600  26.723  11.231  1.00 90.97           C  
ANISOU  803  C   MET A 100    13760  10462  10340  -1530  -2566   1778       C  
ATOM    804  O   MET A 100       3.652  27.214  11.850  1.00 88.93           O  
ANISOU  804  O   MET A 100    13825  10327   9637  -1636  -2433   1549       O  
ATOM    805  CB  MET A 100       3.848  26.625   8.849  1.00 86.61           C  
ANISOU  805  CB  MET A 100    13023   9423  10459  -1140  -1982   1460       C  
ATOM    806  CG  MET A 100       4.910  27.483   8.199  1.00 87.61           C  
ANISOU  806  CG  MET A 100    12983   9471  10831  -1175  -2096   1347       C  
ATOM    807  SD  MET A 100       4.241  28.521   6.889  1.00 85.71           S  
ANISOU  807  SD  MET A 100    12832   9022  10708  -1068  -1744    913       S  
ATOM    808  CE  MET A 100       4.178  27.345   5.583  1.00 83.14           C  
ANISOU  808  CE  MET A 100    12269   8455  10863   -802  -1502   1047       C  
ATOM    809  N   ASP A 101       5.872  26.912  11.549  1.00 94.35           N  
ANISOU  809  N   ASP A 101    14007  10991  10850  -1657  -2942   1957       N  
ATOM    810  CA  ASP A 101       6.267  27.671  12.732  1.00100.26           C  
ANISOU  810  CA  ASP A 101    14945  12036  11113  -1960  -3274   1908       C  
ATOM    811  C   ASP A 101       5.661  29.071  12.663  1.00 97.61           C  
ANISOU  811  C   ASP A 101    14895  11692  10498  -2077  -3080   1377       C  
ATOM    812  O   ASP A 101       5.900  29.794  11.701  1.00 98.93           O  
ANISOU  812  O   ASP A 101    14953  11658  10979  -2006  -2952   1138       O  
ATOM    813  CB  ASP A 101       7.782  27.727  12.819  1.00105.21           C  
ANISOU  813  CB  ASP A 101    15258  12717  11998  -2059  -3701   2152       C  
ATOM    814  CG  ASP A 101       8.251  28.443  14.045  1.00113.72           C  
ANISOU  814  CG  ASP A 101    16514  14120  12571  -2398  -4097   2113       C  
ATOM    815  OD1 ASP A 101       8.392  27.816  15.124  1.00118.64           O  
ANISOU  815  OD1 ASP A 101    17202  15008  12867  -2529  -4392   2449       O  
ATOM    816  OD2 ASP A 101       8.480  29.661  13.928  1.00119.33           O  
ANISOU  816  OD2 ASP A 101    17311  14823  13204  -2549  -4116   1741       O  
ATOM    817  N   SER A 102       4.855  29.454  13.653  1.00 96.94           N  
ANISOU  817  N   SER A 102    15176  11807   9847  -2251  -3024   1195       N  
ATOM    818  CA  SER A 102       3.964  30.642  13.524  1.00 92.99           C  
ANISOU  818  CA  SER A 102    14956  11233   9142  -2304  -2713    680       C  
ATOM    819  C   SER A 102       4.662  31.960  13.259  1.00 90.49           C  
ANISOU  819  C   SER A 102    14616  10854   8909  -2448  -2822    367       C  
ATOM    820  O   SER A 102       4.042  32.893  12.756  1.00 85.85           O  
ANISOU  820  O   SER A 102    14152  10096   8371  -2411  -2530    -14       O  
ATOM    821  CB  SER A 102       3.144  30.822  14.771  1.00 95.92           C  
ANISOU  821  CB  SER A 102    15714  11846   8883  -2503  -2651    546       C  
ATOM    822  OG  SER A 102       3.995  31.281  15.790  1.00100.80           O  
ANISOU  822  OG  SER A 102    16435  12739   9125  -2815  -3046    556       O  
ATOM    823  N   SER A 103       5.938  32.003  13.589  1.00 92.62           N  
ANISOU  823  N   SER A 103    14706  11249   9234  -2606  -3242    553       N  
ATOM    824  CA  SER A 103       6.763  33.124  13.262  1.00 95.22           C  
ANISOU  824  CA  SER A 103    14940  11495   9743  -2738  -3374    317       C  
ATOM    825  C   SER A 103       7.244  33.094  11.821  1.00 91.74           C  
ANISOU  825  C   SER A 103    14159  10748   9947  -2497  -3234    375       C  
ATOM    826  O   SER A 103       7.541  34.156  11.255  1.00 93.26           O  
ANISOU  826  O   SER A 103    14317  10781  10335  -2540  -3161    100       O  
ATOM    827  CB  SER A 103       7.984  33.179  14.170  1.00101.41           C  
ANISOU  827  CB  SER A 103    15628  12537  10364  -3020  -3906    503       C  
ATOM    828  OG  SER A 103       8.898  32.192  13.756  1.00101.38           O  
ANISOU  828  OG  SER A 103    15226  12495  10797  -2877  -4129    966       O  
ATOM    829  N   LEU A 104       7.355  31.911  11.235  1.00 88.39           N  
ANISOU  829  N   LEU A 104    13493  10236   9856  -2259  -3187    723       N  
ATOM    830  CA  LEU A 104       7.611  31.797   9.785  1.00 83.78           C  
ANISOU  830  CA  LEU A 104    12639   9355   9838  -2012  -2961    741       C  
ATOM    831  C   LEU A 104       6.399  32.178   8.914  1.00 79.19           C  
ANISOU  831  C   LEU A 104    12230   8574   9284  -1834  -2507    442       C  
ATOM    832  O   LEU A 104       6.536  32.711   7.806  1.00 77.43           O  
ANISOU  832  O   LEU A 104    11897   8134   9386  -1724  -2320    303       O  
ATOM    833  CB  LEU A 104       8.033  30.384   9.440  1.00 83.63           C  
ANISOU  833  CB  LEU A 104    12326   9283  10164  -1819  -3008   1166       C  
ATOM    834  CG  LEU A 104       8.366  30.065   7.991  1.00 80.59           C  
ANISOU  834  CG  LEU A 104    11662   8613  10345  -1575  -2768   1209       C  
ATOM    835  CD1 LEU A 104       9.439  30.993   7.442  1.00 80.81           C  
ANISOU  835  CD1 LEU A 104    11492   8539  10673  -1656  -2857   1108       C  
ATOM    836  CD2 LEU A 104       8.818  28.620   7.937  1.00 81.63           C  
ANISOU  836  CD2 LEU A 104    11519   8708  10785  -1427  -2844   1631       C  
ATOM    837  N   VAL A 105       5.213  31.817   9.385  1.00 77.83           N  
ANISOU  837  N   VAL A 105    12303   8475   8792  -1797  -2331    385       N  
ATOM    838  CA  VAL A 105       3.944  32.270   8.804  1.00 73.69           C  
ANISOU  838  CA  VAL A 105    11964   7800   8233  -1669  -1941     91       C  
ATOM    839  C   VAL A 105       3.962  33.760   8.692  1.00 73.98           C  
ANISOU  839  C   VAL A 105    12123   7758   8227  -1792  -1881   -269       C  
ATOM    840  O   VAL A 105       3.796  34.330   7.601  1.00 70.54           O  
ANISOU  840  O   VAL A 105    11622   7102   8077  -1662  -1670   -414       O  
ATOM    841  CB  VAL A 105       2.761  31.878   9.703  1.00 74.51           C  
ANISOU  841  CB  VAL A 105    12337   8043   7928  -1697  -1811     53       C  
ATOM    842  CG1 VAL A 105       1.466  32.572   9.281  1.00 72.14           C  
ANISOU  842  CG1 VAL A 105    12225   7598   7587  -1608  -1437   -282       C  
ATOM    843  CG2 VAL A 105       2.574  30.357   9.703  1.00 74.49           C  
ANISOU  843  CG2 VAL A 105    12212   8067   8023  -1548  -1806    414       C  
ATOM    844  N   LYS A 106       4.207  34.385   9.854  1.00 78.62           N  
ANISOU  844  N   LYS A 106    12893   8529   8448  -2061  -2081   -405       N  
ATOM    845  CA  LYS A 106       4.229  35.849  10.005  1.00 79.54           C  
ANISOU  845  CA  LYS A 106    13161   8576   8482  -2234  -2036   -787       C  
ATOM    846  C   LYS A 106       5.258  36.457   9.073  1.00 77.83           C  
ANISOU  846  C   LYS A 106    12692   8177   8701  -2218  -2112   -787       C  
ATOM    847  O   LYS A 106       4.945  37.371   8.327  1.00 75.52           O  
ANISOU  847  O   LYS A 106    12423   7664   8605  -2154  -1880  -1016       O  
ATOM    848  CB  LYS A 106       4.503  36.216  11.467  1.00 85.30           C  
ANISOU  848  CB  LYS A 106    14112   9570   8726  -2560  -2292   -903       C  
ATOM    849  CG  LYS A 106       4.461  37.705  11.821  1.00 87.66           C  
ANISOU  849  CG  LYS A 106    14612   9801   8892  -2781  -2231  -1351       C  
ATOM    850  CD  LYS A 106       4.691  37.911  13.303  1.00 93.52           C  
ANISOU  850  CD  LYS A 106    15603  10844   9086  -3123  -2486  -1470       C  
ATOM    851  CE  LYS A 106       3.569  37.353  14.175  1.00 94.72           C  
ANISOU  851  CE  LYS A 106    16054  11176   8757  -3133  -2307  -1490       C  
ATOM    852  NZ  LYS A 106       3.682  37.879  15.578  1.00100.86           N  
ANISOU  852  NZ  LYS A 106    17151  12223   8948  -3504  -2474  -1731       N  
ATOM    853  N   SER A 107       6.472  35.922   9.102  1.00 78.97           N  
ANISOU  853  N   SER A 107    12578   8404   9023  -2268  -2426   -502       N  
ATOM    854  CA  SER A 107       7.482  36.287   8.106  1.00 78.59           C  
ANISOU  854  CA  SER A 107    12237   8170   9452  -2218  -2459   -440       C  
ATOM    855  C   SER A 107       6.923  36.248   6.686  1.00 75.08           C  
ANISOU  855  C   SER A 107    11723   7470   9331  -1937  -2087   -460       C  
ATOM    856  O   SER A 107       6.939  37.251   5.980  1.00 74.17           O  
ANISOU  856  O   SER A 107    11609   7164   9407  -1927  -1924   -653       O  
ATOM    857  CB  SER A 107       8.687  35.354   8.192  1.00 79.45           C  
ANISOU  857  CB  SER A 107    12023   8376   9786  -2224  -2777    -55       C  
ATOM    858  OG  SER A 107       9.489  35.492   7.039  1.00 77.25           O  
ANISOU  858  OG  SER A 107    11449   7885  10016  -2110  -2697     27       O  
ATOM    859  N   TYR A 108       6.415  35.088   6.296  1.00 73.87           N  
ANISOU  859  N   TYR A 108    11519   7321   9226  -1723  -1961   -257       N  
ATOM    860  CA  TYR A 108       5.955  34.885   4.930  1.00 71.60           C  
ANISOU  860  CA  TYR A 108    11154   6827   9220  -1473  -1650   -250       C  
ATOM    861  C   TYR A 108       4.867  35.853   4.524  1.00 69.82           C  
ANISOU  861  C   TYR A 108    11147   6473   8908  -1425  -1373   -545       C  
ATOM    862  O   TYR A 108       4.931  36.430   3.457  1.00 67.85           O  
ANISOU  862  O   TYR A 108    10831   6041   8907  -1334  -1205   -606       O  
ATOM    863  CB  TYR A 108       5.490  33.441   4.700  1.00 70.96           C  
ANISOU  863  CB  TYR A 108    11009   6775   9175  -1282  -1565    -23       C  
ATOM    864  CG  TYR A 108       6.591  32.429   4.388  1.00 72.71           C  
ANISOU  864  CG  TYR A 108    10918   6983   9724  -1216  -1701    295       C  
ATOM    865  CD1 TYR A 108       7.920  32.817   4.227  1.00 75.76           C  
ANISOU  865  CD1 TYR A 108    11070   7332  10382  -1308  -1876    380       C  
ATOM    866  CD2 TYR A 108       6.297  31.073   4.251  1.00 72.73           C  
ANISOU  866  CD2 TYR A 108    10836   6984   9811  -1059  -1634    511       C  
ATOM    867  CE1 TYR A 108       8.913  31.898   3.960  1.00 77.23           C  
ANISOU  867  CE1 TYR A 108    10941   7483  10918  -1237  -1974    674       C  
ATOM    868  CE2 TYR A 108       7.300  30.141   3.980  1.00 74.42           C  
ANISOU  868  CE2 TYR A 108    10747   7149  10378   -988  -1728    799       C  
ATOM    869  CZ  TYR A 108       8.602  30.575   3.822  1.00 76.20           C  
ANISOU  869  CZ  TYR A 108    10736   7337  10879  -1071  -1890    879       C  
ATOM    870  OH  TYR A 108       9.636  29.723   3.568  1.00 77.83           O  
ANISOU  870  OH  TYR A 108    10608   7473  11489  -1000  -1969   1163       O  
ATOM    871  N   LEU A 109       3.880  36.040   5.384  1.00 70.24           N  
ANISOU  871  N   LEU A 109    11451   6617   8620  -1489  -1318   -712       N  
ATOM    872  CA  LEU A 109       2.782  36.932   5.047  1.00 68.83           C  
ANISOU  872  CA  LEU A 109    11451   6294   8407  -1428  -1042   -977       C  
ATOM    873  C   LEU A 109       3.278  38.359   4.780  1.00 72.04           C  
ANISOU  873  C   LEU A 109    11859   6541   8968  -1541  -1028  -1181       C  
ATOM    874  O   LEU A 109       2.839  39.014   3.845  1.00 75.23           O  
ANISOU  874  O   LEU A 109    12261   6747   9574  -1420   -812  -1265       O  
ATOM    875  CB  LEU A 109       1.762  36.933   6.184  1.00 69.53           C  
ANISOU  875  CB  LEU A 109    11796   6507   8112  -1511   -978  -1136       C  
ATOM    876  CG  LEU A 109       0.489  37.751   5.967  1.00 68.51           C  
ANISOU  876  CG  LEU A 109    11834   6223   7973  -1433   -669  -1400       C  
ATOM    877  CD1 LEU A 109      -0.321  37.211   4.809  1.00 65.39           C  
ANISOU  877  CD1 LEU A 109    11342   5708   7794  -1170   -465  -1288       C  
ATOM    878  CD2 LEU A 109      -0.383  37.766   7.209  1.00 70.52           C  
ANISOU  878  CD2 LEU A 109    12336   6604   7851  -1546   -586  -1571       C  
ATOM    879  N   TYR A 110       4.172  38.845   5.626  1.00 73.74           N  
ANISOU  879  N   TYR A 110    12082   6845   9091  -1784  -1267  -1252       N  
ATOM    880  CA  TYR A 110       4.695  40.162   5.498  1.00 75.81           C  
ANISOU  880  CA  TYR A 110    12341   6951   9513  -1924  -1269  -1455       C  
ATOM    881  C   TYR A 110       5.371  40.352   4.161  1.00 72.74           C  
ANISOU  881  C   TYR A 110    11715   6372   9549  -1798  -1196  -1308       C  
ATOM    882  O   TYR A 110       5.215  41.388   3.485  1.00 72.83           O  
ANISOU  882  O   TYR A 110    11743   6162   9768  -1769  -1013  -1439       O  
ATOM    883  CB  TYR A 110       5.712  40.386   6.623  1.00 81.49           C  
ANISOU  883  CB  TYR A 110    13056   7838  10065  -2226  -1610  -1506       C  
ATOM    884  CG  TYR A 110       6.189  41.812   6.839  1.00 84.59           C  
ANISOU  884  CG  TYR A 110    13496   8089  10553  -2449  -1637  -1796       C  
ATOM    885  CD1 TYR A 110       5.378  42.747   7.452  1.00 86.31           C  
ANISOU  885  CD1 TYR A 110    13986   8235  10571  -2562  -1471  -2158       C  
ATOM    886  CD2 TYR A 110       7.490  42.188   6.490  1.00 87.44           C  
ANISOU  886  CD2 TYR A 110    13616   8381  11227  -2561  -1825  -1712       C  
ATOM    887  CE1 TYR A 110       5.842  44.036   7.695  1.00 90.98           C  
ANISOU  887  CE1 TYR A 110    14620   8673  11272  -2785  -1490  -2446       C  
ATOM    888  CE2 TYR A 110       7.968  43.468   6.715  1.00 90.28           C  
ANISOU  888  CE2 TYR A 110    14002   8597  11702  -2787  -1860  -1979       C  
ATOM    889  CZ  TYR A 110       7.143  44.395   7.325  1.00 92.21           C  
ANISOU  889  CZ  TYR A 110    14533   8760  11742  -2903  -1696  -2355       C  
ATOM    890  OH  TYR A 110       7.591  45.686   7.552  1.00 96.79           O  
ANISOU  890  OH  TYR A 110    15145   9162  12467  -3137  -1706  -2651       O  
ATOM    891  N   GLN A 111       6.167  39.361   3.818  1.00 70.77           N  
ANISOU  891  N   GLN A 111    11243   6206   9440  -1732  -1332  -1024       N  
ATOM    892  CA  GLN A 111       6.895  39.383   2.557  1.00 69.09           C  
ANISOU  892  CA  GLN A 111    10798   5836   9616  -1617  -1241   -866       C  
ATOM    893  C   GLN A 111       5.937  39.414   1.377  1.00 65.35           C  
ANISOU  893  C   GLN A 111    10388   5215   9224  -1381   -921   -870       C  
ATOM    894  O   GLN A 111       6.144  40.166   0.444  1.00 64.75           O  
ANISOU  894  O   GLN A 111    10260   4960   9383  -1340   -772   -882       O  
ATOM    895  CB  GLN A 111       7.854  38.184   2.465  1.00 68.90           C  
ANISOU  895  CB  GLN A 111    10516   5919   9744  -1576  -1410   -568       C  
ATOM    896  CG  GLN A 111       8.968  38.229   3.498  1.00 72.05           C  
ANISOU  896  CG  GLN A 111    10788   6454  10133  -1815  -1772   -511       C  
ATOM    897  CD  GLN A 111       9.783  36.969   3.574  1.00 72.17           C  
ANISOU  897  CD  GLN A 111    10541   6577  10302  -1761  -1956   -187       C  
ATOM    898  OE1 GLN A 111       9.699  36.224   4.548  1.00 73.60           O  
ANISOU  898  OE1 GLN A 111    10758   6956  10247  -1819  -2173    -73       O  
ATOM    899  NE2 GLN A 111      10.558  36.715   2.550  1.00 71.30           N  
ANISOU  899  NE2 GLN A 111    10164   6327  10597  -1649  -1849    -25       N  
ATOM    900  N   ILE A 112       4.904  38.578   1.444  1.00 63.29           N  
ANISOU  900  N   ILE A 112    10237   5042   8769  -1242   -833   -841       N  
ATOM    901  CA  ILE A 112       3.834  38.551   0.446  1.00 60.96           C  
ANISOU  901  CA  ILE A 112    10015   4643   8504  -1036   -573   -855       C  
ATOM    902  C   ILE A 112       3.137  39.923   0.359  1.00 61.78           C  
ANISOU  902  C   ILE A 112    10269   4584   8619  -1059   -425  -1070       C  
ATOM    903  O   ILE A 112       2.882  40.423  -0.728  1.00 60.52           O  
ANISOU  903  O   ILE A 112    10089   4272   8632   -944   -257  -1039       O  
ATOM    904  CB  ILE A 112       2.810  37.447   0.786  1.00 59.44           C  
ANISOU  904  CB  ILE A 112     9910   4578   8096   -926   -536   -817       C  
ATOM    905  CG1 ILE A 112       3.454  36.060   0.547  1.00 60.57           C  
ANISOU  905  CG1 ILE A 112     9873   4811   8327   -855   -619   -576       C  
ATOM    906  CG2 ILE A 112       1.553  37.517  -0.056  1.00 56.41           C  
ANISOU  906  CG2 ILE A 112     9610   4103   7716   -748   -307   -866       C  
ATOM    907  CD1 ILE A 112       2.854  34.928   1.377  1.00 60.26           C  
ANISOU  907  CD1 ILE A 112     9892   4924   8079   -832   -680   -505       C  
ATOM    908  N   LEU A 113       2.780  40.494   1.510  1.00 63.66           N  
ANISOU  908  N   LEU A 113    10665   4852   8669  -1207   -474  -1283       N  
ATOM    909  CA  LEU A 113       2.189  41.829   1.549  1.00 64.28           C  
ANISOU  909  CA  LEU A 113    10872   4740   8810  -1244   -318  -1511       C  
ATOM    910  C   LEU A 113       3.091  42.877   0.922  1.00 64.97           C  
ANISOU  910  C   LEU A 113    10854   4633   9197  -1315   -307  -1512       C  
ATOM    911  O   LEU A 113       2.621  43.713   0.158  1.00 64.70           O  
ANISOU  911  O   LEU A 113    10838   4390   9352  -1222   -119  -1536       O  
ATOM    912  CB  LEU A 113       1.839  42.248   2.969  1.00 66.55           C  
ANISOU  912  CB  LEU A 113    11350   5093   8840  -1430   -361  -1776       C  
ATOM    913  CG  LEU A 113       0.523  41.608   3.419  1.00 65.90           C  
ANISOU  913  CG  LEU A 113    11409   5109   8520  -1324   -233  -1821       C  
ATOM    914  CD1 LEU A 113       0.361  41.817   4.909  1.00 68.61           C  
ANISOU  914  CD1 LEU A 113    11951   5576   8540  -1538   -286  -2058       C  
ATOM    915  CD2 LEU A 113      -0.707  42.146   2.696  1.00 64.47           C  
ANISOU  915  CD2 LEU A 113    11266   4728   8501  -1136     41  -1882       C  
ATOM    916  N   GLN A 114       4.375  42.810   1.217  1.00 65.23           N  
ANISOU  916  N   GLN A 114    10758   4729   9298  -1476   -510  -1458       N  
ATOM    917  CA  GLN A 114       5.288  43.753   0.634  1.00 66.27           C  
ANISOU  917  CA  GLN A 114    10764   4672   9743  -1557   -493  -1446       C  
ATOM    918  C   GLN A 114       5.335  43.720  -0.887  1.00 63.83           C  
ANISOU  918  C   GLN A 114    10340   4234   9677  -1361   -306  -1227       C  
ATOM    919  O   GLN A 114       5.293  44.774  -1.540  1.00 63.94           O  
ANISOU  919  O   GLN A 114    10357   4025   9911  -1347   -151  -1248       O  
ATOM    920  CB  GLN A 114       6.674  43.574   1.204  1.00 69.70           C  
ANISOU  920  CB  GLN A 114    11036   5209  10237  -1763   -763  -1400       C  
ATOM    921  CG  GLN A 114       6.801  44.303   2.528  1.00 74.43           C  
ANISOU  921  CG  GLN A 114    11766   5840  10672  -2034   -924  -1685       C  
ATOM    922  CD  GLN A 114       8.198  44.277   3.037  1.00 78.77           C  
ANISOU  922  CD  GLN A 114    12132   6480  11315  -2262  -1225  -1638       C  
ATOM    923  OE1 GLN A 114       8.687  43.241   3.495  1.00 79.67           O  
ANISOU  923  OE1 GLN A 114    12145   6824  11301  -2287  -1459  -1467       O  
ATOM    924  NE2 GLN A 114       8.894  45.416   2.913  1.00 82.52           N  
ANISOU  924  NE2 GLN A 114    12531   6757  12064  -2429  -1227  -1764       N  
ATOM    925  N   GLY A 115       5.349  42.507  -1.452  1.00 60.83           N  
ANISOU  925  N   GLY A 115     9876   3992   9242  -1210   -305  -1021       N  
ATOM    926  CA  GLY A 115       5.369  42.324  -2.891  1.00 57.31           C  
ANISOU  926  CA  GLY A 115     9353   3471   8952  -1039   -124   -829       C  
ATOM    927  C   GLY A 115       4.113  42.852  -3.533  1.00 55.17           C  
ANISOU  927  C   GLY A 115     9229   3091   8643   -892     66   -859       C  
ATOM    928  O   GLY A 115       4.189  43.407  -4.630  1.00 54.12           O  
ANISOU  928  O   GLY A 115     9067   2822   8673   -821    214   -743       O  
ATOM    929  N   ILE A 116       2.969  42.707  -2.860  1.00 54.02           N  
ANISOU  929  N   ILE A 116     9228   3000   8295   -850     66   -995       N  
ATOM    930  CA  ILE A 116       1.698  43.115  -3.453  1.00 53.37           C  
ANISOU  930  CA  ILE A 116     9246   2819   8211   -695    229   -999       C  
ATOM    931  C   ILE A 116       1.488  44.596  -3.357  1.00 55.41           C  
ANISOU  931  C   ILE A 116     9560   2834   8658   -751    328  -1119       C  
ATOM    932  O   ILE A 116       1.059  45.260  -4.333  1.00 55.62           O  
ANISOU  932  O   ILE A 116     9585   2703   8846   -638    464  -1005       O  
ATOM    933  CB  ILE A 116       0.477  42.364  -2.861  1.00 52.84           C  
ANISOU  933  CB  ILE A 116     9280   2881   7915   -611    229  -1082       C  
ATOM    934  CG1 ILE A 116      -0.698  42.432  -3.822  1.00 52.14           C  
ANISOU  934  CG1 ILE A 116     9219   2731   7859   -421    363   -996       C  
ATOM    935  CG2 ILE A 116       0.020  42.897  -1.507  1.00 54.63           C  
ANISOU  935  CG2 ILE A 116     9631   3083   8041   -732    220  -1335       C  
ATOM    936  CD1 ILE A 116      -0.483  41.620  -5.118  1.00 51.19           C  
ANISOU  936  CD1 ILE A 116     9022   2699   7726   -306    375   -777       C  
ATOM    937  N   VAL A 117       1.827  45.143  -2.177  1.00 56.99           N  
ANISOU  937  N   VAL A 117     9810   2996   8845   -939    256  -1345       N  
ATOM    938  CA  VAL A 117       1.852  46.580  -1.988  1.00 58.45           C  
ANISOU  938  CA  VAL A 117    10035   2916   9256  -1035    354  -1500       C  
ATOM    939  C   VAL A 117       2.703  47.191  -3.076  1.00 58.95           C  
ANISOU  939  C   VAL A 117     9972   2819   9607  -1031    411  -1308       C  
ATOM    940  O   VAL A 117       2.299  48.204  -3.628  1.00 60.24           O  
ANISOU  940  O   VAL A 117    10151   2739   9998   -972    568  -1276       O  
ATOM    941  CB  VAL A 117       2.331  47.000  -0.588  1.00 60.72           C  
ANISOU  941  CB  VAL A 117    10395   3214   9462  -1287    242  -1793       C  
ATOM    942  CG1 VAL A 117       2.726  48.467  -0.548  1.00 63.40           C  
ANISOU  942  CG1 VAL A 117    10732   3252  10106  -1424    333  -1944       C  
ATOM    943  CG2 VAL A 117       1.225  46.730   0.404  1.00 60.86           C  
ANISOU  943  CG2 VAL A 117    10582   3322   9219  -1279    285  -2003       C  
ATOM    944  N   PHE A 118       3.866  46.617  -3.370  1.00 58.46           N  
ANISOU  944  N   PHE A 118     9776   2872   9565  -1093    303  -1168       N  
ATOM    945  CA  PHE A 118       4.701  47.134  -4.443  1.00 60.08           C  
ANISOU  945  CA  PHE A 118     9856   2932  10039  -1092    395   -971       C  
ATOM    946  C   PHE A 118       3.982  47.166  -5.772  1.00 60.16           C  
ANISOU  946  C   PHE A 118     9896   2890  10070   -879    568   -742       C  
ATOM    947  O   PHE A 118       4.041  48.148  -6.517  1.00 63.17           O  
ANISOU  947  O   PHE A 118    10263   3054  10682   -858    707   -626       O  
ATOM    948  CB  PHE A 118       6.025  46.365  -4.575  1.00 59.47           C  
ANISOU  948  CB  PHE A 118     9603   2994   9996  -1172    281   -847       C  
ATOM    949  CG  PHE A 118       6.851  46.791  -5.754  1.00 60.25           C  
ANISOU  949  CG  PHE A 118     9572   2957  10360  -1159    427   -630       C  
ATOM    950  CD1 PHE A 118       6.655  46.227  -6.993  1.00 58.68           C  
ANISOU  950  CD1 PHE A 118     9372   2824  10099   -986    571   -401       C  
ATOM    951  CD2 PHE A 118       7.836  47.831  -5.627  1.00 63.03           C  
ANISOU  951  CD2 PHE A 118     9812   3104  11031  -1343    435   -666       C  
ATOM    952  CE1 PHE A 118       7.421  46.659  -8.090  1.00 60.18           C  
ANISOU  952  CE1 PHE A 118     9466   2894  10504   -987    741   -196       C  
ATOM    953  CE2 PHE A 118       8.599  48.253  -6.715  1.00 63.81           C  
ANISOU  953  CE2 PHE A 118     9789   3065  11389  -1338    604   -450       C  
ATOM    954  CZ  PHE A 118       8.376  47.691  -7.960  1.00 62.45           C  
ANISOU  954  CZ  PHE A 118     9635   2970  11121  -1156    770   -207       C  
ATOM    955  N   CYS A 119       3.333  46.073  -6.066  1.00 59.24           N  
ANISOU  955  N   CYS A 119     9819   2977   9711   -734    547   -666       N  
ATOM    956  CA  CYS A 119       2.634  45.908  -7.316  1.00 58.90           C  
ANISOU  956  CA  CYS A 119     9811   2948   9618   -550    662   -456       C  
ATOM    957  C   CYS A 119       1.491  46.848  -7.425  1.00 59.41           C  
ANISOU  957  C   CYS A 119     9961   2836   9775   -461    747   -467       C  
ATOM    958  O   CYS A 119       1.241  47.349  -8.495  1.00 60.60           O  
ANISOU  958  O   CYS A 119    10115   2892  10017   -367    846   -255       O  
ATOM    959  CB  CYS A 119       2.088  44.452  -7.427  1.00 57.86           C  
ANISOU  959  CB  CYS A 119     9705   3075   9203   -439    598   -433       C  
ATOM    960  SG  CYS A 119       3.394  43.223  -7.745  1.00 56.71           S  
ANISOU  960  SG  CYS A 119     9428   3104   9012   -485    561   -336       S  
ATOM    961  N   HIS A 120       0.856  47.132  -6.308  1.00 59.69           N  
ANISOU  961  N   HIS A 120    10059   2816   9802   -500    718   -704       N  
ATOM    962  CA  HIS A 120      -0.391  47.833  -6.307  1.00 60.81           C  
ANISOU  962  CA  HIS A 120    10260   2797  10046   -389    814   -733       C  
ATOM    963  C   HIS A 120      -0.460  49.365  -6.564  1.00 64.75           C  
ANISOU  963  C   HIS A 120    10746   2950  10905   -397    954   -699       C  
ATOM    964  O   HIS A 120      -1.042  49.770  -7.566  1.00 67.54           O  
ANISOU  964  O   HIS A 120    11082   3206  11374   -251   1025   -458       O  
ATOM    965  CB  HIS A 120      -1.133  47.544  -5.004  1.00 59.94           C  
ANISOU  965  CB  HIS A 120    10228   2745   9800   -422    787  -1014       C  
ATOM    966  CG  HIS A 120      -1.957  46.317  -5.022  1.00 58.71           C  
ANISOU  966  CG  HIS A 120    10093   2828   9384   -302    729   -980       C  
ATOM    967  ND1 HIS A 120      -2.853  46.014  -4.015  1.00 59.36           N  
ANISOU  967  ND1 HIS A 120    10244   2961   9348   -297    746  -1182       N  
ATOM    968  CD2 HIS A 120      -2.044  45.292  -5.922  1.00 56.48           C  
ANISOU  968  CD2 HIS A 120     9775   2740   8944   -195    671   -781       C  
ATOM    969  CE1 HIS A 120      -3.429  44.843  -4.283  1.00 55.83           C  
ANISOU  969  CE1 HIS A 120     9784   2724   8702   -190    689  -1092       C  
ATOM    970  NE2 HIS A 120      -2.997  44.423  -5.460  1.00 53.79           N  
ANISOU  970  NE2 HIS A 120     9466   2545   8426   -125    642   -859       N  
ATOM    971  N   SER A 121       0.097  50.288  -5.785  1.00 67.84           N  
ANISOU  971  N   SER A 121    11140   3131  11504   -563    997   -907       N  
ATOM    972  CA  SER A 121       1.456  50.914  -5.860  1.00 70.17           C  
ANISOU  972  CA  SER A 121    11363   3295  12002   -740    999   -898       C  
ATOM    973  C   SER A 121       1.917  51.241  -7.244  1.00 69.92           C  
ANISOU  973  C   SER A 121    11255   3180  12128   -667   1082   -550       C  
ATOM    974  O   SER A 121       2.019  52.404  -7.559  1.00 71.70           O  
ANISOU  974  O   SER A 121    11453   3107  12680   -688   1209   -478       O  
ATOM    975  CB  SER A 121       2.554  50.224  -5.111  1.00 70.74           C  
ANISOU  975  CB  SER A 121    11400   3566  11912   -926    835  -1045       C  
ATOM    976  OG  SER A 121       3.794  50.898  -5.297  1.00 71.98           O  
ANISOU  976  OG  SER A 121    11451   3571  12327  -1088    845  -1009       O  
ATOM    977  N   ARG A 122       2.204  50.223  -8.068  1.00 68.05           N  
ANISOU  977  N   ARG A 122    10993   3198  11663   -591   1032   -336       N  
ATOM    978  CA  ARG A 122       2.538  50.452  -9.485  1.00 67.88           C  
ANISOU  978  CA  ARG A 122    10936   3140  11714   -516   1137      8       C  
ATOM    979  C   ARG A 122       1.386  50.270 -10.507  1.00 67.64           C  
ANISOU  979  C   ARG A 122    10973   3183  11544   -306   1164    258       C  
ATOM    980  O   ARG A 122       1.611  50.186 -11.670  1.00 66.15           O  
ANISOU  980  O   ARG A 122    10788   3055  11289   -252   1222    536       O  
ATOM    981  CB  ARG A 122       3.825  49.740  -9.835  1.00 66.99           C  
ANISOU  981  CB  ARG A 122    10739   3188  11524   -609   1122     82       C  
ATOM    982  CG  ARG A 122       4.955  50.739  -9.918  1.00 70.18           C  
ANISOU  982  CG  ARG A 122    11040   3350  12274   -765   1219    124       C  
ATOM    983  CD  ARG A 122       6.357  50.146  -9.893  1.00 70.83           C  
ANISOU  983  CD  ARG A 122    10983   3545  12380   -900   1191    124       C  
ATOM    984  NE  ARG A 122       7.317  50.980  -9.155  1.00 72.98           N  
ANISOU  984  NE  ARG A 122    11138   3609  12980  -1115   1167    -27       N  
ATOM    985  CZ  ARG A 122       7.291  51.136  -7.822  1.00 73.12           C  
ANISOU  985  CZ  ARG A 122    11163   3604  13012  -1251   1006   -342       C  
ATOM    986  NH1 ARG A 122       6.353  50.547  -7.063  1.00 70.47           N  
ANISOU  986  NH1 ARG A 122    10949   3429  12395  -1185    885   -525       N  
ATOM    987  NH2 ARG A 122       8.218  51.899  -7.241  1.00 75.65           N  
ANISOU  987  NH2 ARG A 122    11373   3743  13626  -1471    971   -481       N  
ATOM    988  N   ARG A 123       0.151  50.358 -10.027  1.00 70.49           N  
ANISOU  988  N   ARG A 123    11379   3508  11895   -204   1129    154       N  
ATOM    989  CA  ARG A 123      -1.086  50.190 -10.805  1.00 72.26           C  
ANISOU  989  CA  ARG A 123    11636   3800  12019    -13   1107    360       C  
ATOM    990  C   ARG A 123      -1.326  48.757 -11.277  1.00 66.87           C  
ANISOU  990  C   ARG A 123    10989   3473  10943     50    997    406       C  
ATOM    991  O   ARG A 123      -2.167  48.532 -12.093  1.00 66.32           O  
ANISOU  991  O   ARG A 123    10944   3500  10755    177    954    598       O  
ATOM    992  CB  ARG A 123      -1.148  51.148 -11.996  1.00 78.99           C  
ANISOU  992  CB  ARG A 123    12474   4477  13059     59   1196    724       C  
ATOM    993  CG  ARG A 123      -1.259  52.655 -11.700  1.00 86.06           C  
ANISOU  993  CG  ARG A 123    13321   4961  14415     46   1323    739       C  
ATOM    994  CD  ARG A 123      -2.421  53.355 -12.479  1.00 92.63           C  
ANISOU  994  CD  ARG A 123    14128   5641  15423    233   1338   1056       C  
ATOM    995  NE  ARG A 123      -3.743  53.255 -11.783  1.00 96.43           N  
ANISOU  995  NE  ARG A 123    14583   6087  15967    351   1294    890       N  
ATOM    996  CZ  ARG A 123      -4.678  52.262 -11.884  1.00 97.60           C  
ANISOU  996  CZ  ARG A 123    14741   6506  15836    460   1157    887       C  
ATOM    997  NH1 ARG A 123      -4.537  51.174 -12.687  1.00 94.29           N  
ANISOU  997  NH1 ARG A 123    14375   6440  15010    472   1029   1025       N  
ATOM    998  NH2 ARG A 123      -5.811  52.366 -11.164  1.00 97.42           N  
ANISOU  998  NH2 ARG A 123    14667   6381  15968    554   1169    729       N  
ATOM    999  N   VAL A 124      -0.648  47.779 -10.691  1.00 64.25           N  
ANISOU  999  N   VAL A 124    10654   3326  10432    -41    940    218       N  
ATOM   1000  CA  VAL A 124      -0.591  46.397 -11.245  1.00 60.45           C  
ANISOU 1000  CA  VAL A 124    10194   3145   9626     -3    877    266       C  
ATOM   1001  C   VAL A 124      -1.214  45.422 -10.280  1.00 58.14           C  
ANISOU 1001  C   VAL A 124     9913   3004   9173     13    774     38       C  
ATOM   1002  O   VAL A 124      -0.910  45.441  -9.089  1.00 57.45           O  
ANISOU 1002  O   VAL A 124     9811   2877   9139    -80    745   -181       O  
ATOM   1003  CB  VAL A 124       0.841  45.928 -11.471  1.00 59.97           C  
ANISOU 1003  CB  VAL A 124    10088   3164   9534   -115    923    282       C  
ATOM   1004  CG1 VAL A 124       0.872  44.496 -12.007  1.00 60.19           C  
ANISOU 1004  CG1 VAL A 124    10135   3461   9272    -73    895    298       C  
ATOM   1005  CG2 VAL A 124       1.558  46.792 -12.456  1.00 61.55           C  
ANISOU 1005  CG2 VAL A 124    10275   3229   9882   -147   1059    517       C  
ATOM   1006  N   LEU A 125      -2.076  44.548 -10.789  1.00 58.10           N  
ANISOU 1006  N   LEU A 125     9936   3179   8957    118    715     93       N  
ATOM   1007  CA  LEU A 125      -2.667  43.437  -9.966  1.00 57.13           C  
ANISOU 1007  CA  LEU A 125     9817   3215   8675    135    632    -96       C  
ATOM   1008  C   LEU A 125      -2.097  42.077 -10.274  1.00 54.80           C  
ANISOU 1008  C   LEU A 125     9515   3135   8171    111    603   -104       C  
ATOM   1009  O   LEU A 125      -1.445  41.867 -11.292  1.00 54.06           O  
ANISOU 1009  O   LEU A 125     9427   3101   8013    101    657     31       O  
ATOM   1010  CB  LEU A 125      -4.171  43.335 -10.177  1.00 57.76           C  
ANISOU 1010  CB  LEU A 125     9902   3323   8719    264    585    -63       C  
ATOM   1011  CG  LEU A 125      -4.963  44.641 -10.098  1.00 61.27           C  
ANISOU 1011  CG  LEU A 125    10325   3534   9418    333    629     -6       C  
ATOM   1012  CD1 LEU A 125      -6.427  44.374 -10.364  1.00 61.27           C  
ANISOU 1012  CD1 LEU A 125    10288   3586   9406    465    564     51       C  
ATOM   1013  CD2 LEU A 125      -4.833  45.283  -8.717  1.00 62.55           C  
ANISOU 1013  CD2 LEU A 125    10490   3520   9756    256    701   -248       C  
ATOM   1014  N   HIS A 126      -2.373  41.154  -9.366  1.00 54.60           N  
ANISOU 1014  N   HIS A 126     9478   3212   8053    100    541   -264       N  
ATOM   1015  CA  HIS A 126      -2.255  39.712  -9.649  1.00 53.21           C  
ANISOU 1015  CA  HIS A 126     9288   3222   7704    113    516   -276       C  
ATOM   1016  C   HIS A 126      -3.501  39.115 -10.224  1.00 53.02           C  
ANISOU 1016  C   HIS A 126     9293   3300   7551    211    477   -255       C  
ATOM   1017  O   HIS A 126      -3.506  38.763 -11.392  1.00 52.50           O  
ANISOU 1017  O   HIS A 126     9254   3321   7370    237    493   -154       O  
ATOM   1018  CB  HIS A 126      -1.859  38.926  -8.457  1.00 51.70           C  
ANISOU 1018  CB  HIS A 126     9059   3090   7493     49    463   -412       C  
ATOM   1019  CG  HIS A 126      -1.130  37.712  -8.853  1.00 53.08           C  
ANISOU 1019  CG  HIS A 126     9182   3378   7606     38    479   -381       C  
ATOM   1020  ND1 HIS A 126      -1.764  36.633  -9.430  1.00 52.30           N  
ANISOU 1020  ND1 HIS A 126     9097   3390   7383    104    488   -384       N  
ATOM   1021  CD2 HIS A 126       0.196  37.440  -8.892  1.00 54.21           C  
ANISOU 1021  CD2 HIS A 126     9244   3516   7834    -28    509   -341       C  
ATOM   1022  CE1 HIS A 126      -0.869  35.712  -9.712  1.00 53.37           C  
ANISOU 1022  CE1 HIS A 126     9173   3573   7530     80    539   -370       C  
ATOM   1023  NE2 HIS A 126       0.333  36.183  -9.411  1.00 54.06           N  
ANISOU 1023  NE2 HIS A 126     9192   3592   7755      7    555   -330       N  
ATOM   1024  N   ARG A 127      -4.549  39.039  -9.415  1.00 54.48           N  
ANISOU 1024  N   ARG A 127     9471   3475   7753    250    432   -355       N  
ATOM   1025  CA  ARG A 127      -5.876  38.481  -9.779  1.00 58.41           C  
ANISOU 1025  CA  ARG A 127     9958   4055   8180    336    379   -351       C  
ATOM   1026  C   ARG A 127      -5.987  37.006  -9.521  1.00 57.05           C  
ANISOU 1026  C   ARG A 127     9765   4020   7888    322    357   -445       C  
ATOM   1027  O   ARG A 127      -6.932  36.541  -8.866  1.00 55.11           O  
ANISOU 1027  O   ARG A 127     9491   3795   7651    351    335   -529       O  
ATOM   1028  CB  ARG A 127      -6.321  38.702 -11.223  1.00 62.20           C  
ANISOU 1028  CB  ARG A 127    10456   4584   8590    392    338   -183       C  
ATOM   1029  CG  ARG A 127      -6.460  40.168 -11.657  1.00 68.26           C  
ANISOU 1029  CG  ARG A 127    11229   5203   9501    432    349    -23       C  
ATOM   1030  CD  ARG A 127      -6.822  40.352 -13.141  1.00 74.23           C  
ANISOU 1030  CD  ARG A 127    12019   6044  10138    473    283    194       C  
ATOM   1031  NE  ARG A 127      -7.700  39.269 -13.635  1.00 83.68           N  
ANISOU 1031  NE  ARG A 127    13208   7427  11159    494    173    161       N  
ATOM   1032  CZ  ARG A 127      -8.053  39.091 -14.908  1.00 88.68           C  
ANISOU 1032  CZ  ARG A 127    13888   8203  11601    495     80    302       C  
ATOM   1033  NH1 ARG A 127      -7.681  39.980 -15.849  1.00 85.12           N  
ANISOU 1033  NH1 ARG A 127    13502   7736  11102    493     86    531       N  
ATOM   1034  NH2 ARG A 127      -8.804  38.007 -15.232  1.00 90.98           N  
ANISOU 1034  NH2 ARG A 127    14167   8658  11740    484    -24    215       N  
ATOM   1035  N   ASP A 128      -5.063  36.275 -10.114  1.00 59.61           N  
ANISOU 1035  N   ASP A 128    10097   4420   8129    281    385   -421       N  
ATOM   1036  CA  ASP A 128      -5.010  34.828  -9.979  1.00 63.85           C  
ANISOU 1036  CA  ASP A 128    10605   5053   8601    267    389   -500       C  
ATOM   1037  C   ASP A 128      -4.022  34.376  -8.865  1.00 60.17           C  
ANISOU 1037  C   ASP A 128    10092   4566   8201    206    406   -545       C  
ATOM   1038  O   ASP A 128      -3.264  33.414  -9.020  1.00 60.94           O  
ANISOU 1038  O   ASP A 128    10146   4698   8310    183    445   -544       O  
ATOM   1039  CB  ASP A 128      -4.726  34.130 -11.335  1.00 67.87           C  
ANISOU 1039  CB  ASP A 128    11144   5651   8993    260    432   -473       C  
ATOM   1040  CG  ASP A 128      -4.888  32.559 -11.249  1.00 74.92           C  
ANISOU 1040  CG  ASP A 128    11998   6608   9860    250    453   -582       C  
ATOM   1041  OD1 ASP A 128      -5.569  32.023 -10.290  1.00 77.92           O  
ANISOU 1041  OD1 ASP A 128    12329   6982  10294    265    410   -646       O  
ATOM   1042  OD2 ASP A 128      -4.352  31.861 -12.156  1.00 77.30           O  
ANISOU 1042  OD2 ASP A 128    12320   6952  10097    223    537   -608       O  
ATOM   1043  N   LEU A 129      -4.073  35.030  -7.728  1.00 55.87           N  
ANISOU 1043  N   LEU A 129     9555   3966   7708    176    373   -584       N  
ATOM   1044  CA  LEU A 129      -3.087  34.751  -6.718  1.00 54.93           C  
ANISOU 1044  CA  LEU A 129     9399   3850   7621     97    344   -599       C  
ATOM   1045  C   LEU A 129      -3.385  33.442  -5.982  1.00 53.68           C  
ANISOU 1045  C   LEU A 129     9207   3767   7421     99    319   -625       C  
ATOM   1046  O   LEU A 129      -4.572  33.145  -5.724  1.00 53.14           O  
ANISOU 1046  O   LEU A 129     9163   3722   7305    141    328   -679       O  
ATOM   1047  CB  LEU A 129      -3.012  35.898  -5.730  1.00 56.34           C  
ANISOU 1047  CB  LEU A 129     9621   3957   7827     33    313   -658       C  
ATOM   1048  CG  LEU A 129      -1.774  35.857  -4.846  1.00 57.62           C  
ANISOU 1048  CG  LEU A 129     9742   4133   8015    -81    240   -654       C  
ATOM   1049  CD1 LEU A 129      -0.492  35.885  -5.644  1.00 59.02           C  
ANISOU 1049  CD1 LEU A 129     9832   4281   8309   -106    257   -553       C  
ATOM   1050  CD2 LEU A 129      -1.791  37.053  -3.900  1.00 60.69           C  
ANISOU 1050  CD2 LEU A 129    10202   4453   8405   -171    213   -763       C  
ATOM   1051  N   LYS A 130      -2.320  32.681  -5.644  1.00 51.13           N  
ANISOU 1051  N   LYS A 130     8807   3467   7150     54    294   -567       N  
ATOM   1052  CA  LYS A 130      -2.443  31.368  -4.960  1.00 49.09           C  
ANISOU 1052  CA  LYS A 130     8498   3260   6892     56    272   -541       C  
ATOM   1053  C   LYS A 130      -1.106  30.722  -4.675  1.00 47.13           C  
ANISOU 1053  C   LYS A 130     8133   3009   6765     15    232   -432       C  
ATOM   1054  O   LYS A 130      -0.105  31.143  -5.278  1.00 48.50           O  
ANISOU 1054  O   LYS A 130     8248   3139   7040     -2    255   -393       O  
ATOM   1055  CB  LYS A 130      -3.241  30.414  -5.801  1.00 50.59           C  
ANISOU 1055  CB  LYS A 130     8676   3456   7089    130    351   -574       C  
ATOM   1056  CG  LYS A 130      -2.609  30.039  -7.125  1.00 52.40           C  
ANISOU 1056  CG  LYS A 130     8865   3658   7384    154    438   -565       C  
ATOM   1057  CD  LYS A 130      -3.701  29.687  -8.122  1.00 54.50           C  
ANISOU 1057  CD  LYS A 130     9181   3951   7575    200    485   -649       C  
ATOM   1058  CE  LYS A 130      -3.114  29.009  -9.332  1.00 58.35           C  
ANISOU 1058  CE  LYS A 130     9650   4427   8091    201    598   -677       C  
ATOM   1059  NZ  LYS A 130      -3.101  29.822 -10.583  1.00 60.61           N  
ANISOU 1059  NZ  LYS A 130    10024   4747   8255    198    636   -682       N  
ATOM   1060  N   PRO A 131      -1.061  29.702  -3.789  1.00 44.05           N  
ANISOU 1060  N   PRO A 131     7688   2655   6393      3    179   -358       N  
ATOM   1061  CA  PRO A 131       0.242  29.237  -3.258  1.00 44.46           C  
ANISOU 1061  CA  PRO A 131     7603   2707   6582    -44     89   -210       C  
ATOM   1062  C   PRO A 131       1.273  28.770  -4.268  1.00 44.78           C  
ANISOU 1062  C   PRO A 131     7497   2661   6856     -2    183   -151       C  
ATOM   1063  O   PRO A 131       2.444  29.017  -4.085  1.00 44.65           O  
ANISOU 1063  O   PRO A 131     7362   2625   6978    -50    116    -56       O  
ATOM   1064  CB  PRO A 131      -0.142  28.121  -2.319  1.00 44.41           C  
ANISOU 1064  CB  PRO A 131     7573   2743   6557    -40     40   -115       C  
ATOM   1065  CG  PRO A 131      -1.469  28.485  -1.825  1.00 43.53           C  
ANISOU 1065  CG  PRO A 131     7617   2686   6233    -48     61   -226       C  
ATOM   1066  CD  PRO A 131      -2.163  29.147  -2.989  1.00 43.06           C  
ANISOU 1066  CD  PRO A 131     7622   2578   6159     12    174   -378       C  
ATOM   1067  N  AGLN A 132       0.848  28.122  -5.342  0.50 44.25           N  
ANISOU 1067  N  AGLN A 132     7434   2541   6838     74    348   -222       N  
ATOM   1068  N  BGLN A 132       0.846  28.120  -5.335  0.50 45.43           N  
ANISOU 1068  N  BGLN A 132     7584   2691   6987     74    347   -222       N  
ATOM   1069  CA AGLN A 132       1.820  27.771  -6.386  0.50 45.58           C  
ANISOU 1069  CA AGLN A 132     7489   2621   7206    104    494   -206       C  
ATOM   1070  CA BGLN A 132       1.808  27.764  -6.372  0.50 47.63           C  
ANISOU 1070  CA BGLN A 132     7749   2882   7465    104    492   -206       C  
ATOM   1071  C  AGLN A 132       2.406  28.977  -7.125  0.50 46.93           C  
ANISOU 1071  C  AGLN A 132     7692   2782   7357     71    540   -232       C  
ATOM   1072  C  BGLN A 132       2.399  28.973  -7.127  0.50 48.18           C  
ANISOU 1072  C  BGLN A 132     7850   2940   7514     71    541   -233       C  
ATOM   1073  O  AGLN A 132       3.389  28.806  -7.851  0.50 48.49           O  
ANISOU 1073  O  AGLN A 132     7781   2907   7733     78    673   -199       O  
ATOM   1074  O  BGLN A 132       3.387  28.803  -7.851  0.50 49.69           O  
ANISOU 1074  O  BGLN A 132     7934   3060   7886     78    673   -199       O  
ATOM   1075  CB AGLN A 132       1.309  26.742  -7.398  0.50 44.87           C  
ANISOU 1075  CB AGLN A 132     7413   2477   7156    167    679   -310       C  
ATOM   1076  CB BGLN A 132       1.273  26.717  -7.347  0.50 48.46           C  
ANISOU 1076  CB BGLN A 132     7869   2934   7609    167    673   -308       C  
ATOM   1077  CG AGLN A 132       0.235  27.221  -8.369  0.50 43.62           C  
ANISOU 1077  CG AGLN A 132     7428   2374   6769    178    739   -466       C  
ATOM   1078  CG BGLN A 132      -0.122  26.931  -7.869  0.50 48.44           C  
ANISOU 1078  CG BGLN A 132     8034   2994   7376    182    689   -454       C  
ATOM   1079  CD AGLN A 132      -0.337  26.042  -9.134  0.50 43.21           C  
ANISOU 1079  CD AGLN A 132     7387   2284   6745    208    876   -585       C  
ATOM   1080  CD BGLN A 132      -1.206  26.445  -6.922  0.50 48.85           C  
ANISOU 1080  CD BGLN A 132     8116   3082   7360    189    597   -455       C  
ATOM   1081  OE1AGLN A 132       0.436  25.393  -9.827  0.50 44.57           O  
ANISOU 1081  OE1AGLN A 132     7486   2374   7075    217   1045   -614       O  
ATOM   1082  OE1BGLN A 132      -1.245  26.722  -5.681  0.50 48.30           O  
ANISOU 1082  OE1BGLN A 132     8046   3057   7247    158    464   -365       O  
ATOM   1083  NE2AGLN A 132      -1.633  25.706  -8.977  0.50 41.97           N  
ANISOU 1083  NE2AGLN A 132     7301   2169   6473    216    823   -665       N  
ATOM   1084  NE2BGLN A 132      -2.196  25.891  -7.558  0.50 48.55           N  
ANISOU 1084  NE2BGLN A 132     8131   3043   7270    212    667   -575       N  
ATOM   1085  N   ASN A 133       1.842  30.182  -6.938  1.00 47.37           N  
ANISOU 1085  N   ASN A 133     7880   2887   7229     35    458   -284       N  
ATOM   1086  CA  ASN A 133       2.465  31.435  -7.466  1.00 47.75           C  
ANISOU 1086  CA  ASN A 133     7946   2900   7296     -7    488   -275       C  
ATOM   1087  C   ASN A 133       3.509  32.050  -6.554  1.00 48.83           C  
ANISOU 1087  C   ASN A 133     7976   3019   7557   -101    351   -195       C  
ATOM   1088  O   ASN A 133       4.167  33.002  -6.933  1.00 51.41           O  
ANISOU 1088  O   ASN A 133     8280   3292   7960   -150    382   -177       O  
ATOM   1089  CB  ASN A 133       1.423  32.495  -7.648  1.00 47.88           C  
ANISOU 1089  CB  ASN A 133     8130   2939   7123     -2    465   -351       C  
ATOM   1090  CG  ASN A 133       0.466  32.184  -8.732  1.00 47.39           C  
ANISOU 1090  CG  ASN A 133     8166   2907   6933     67    567   -412       C  
ATOM   1091  OD1 ASN A 133       0.844  31.757  -9.796  1.00 49.43           O  
ANISOU 1091  OD1 ASN A 133     8413   3157   7210     86    705   -411       O  
ATOM   1092  ND2 ASN A 133      -0.793  32.472  -8.494  1.00 47.15           N  
ANISOU 1092  ND2 ASN A 133     8233   2912   6768     96    503   -471       N  
ATOM   1093  N   LEU A 134       3.542  31.633  -5.296  1.00 49.15           N  
ANISOU 1093  N   LEU A 134     7973   3115   7587   -144    180   -150       N  
ATOM   1094  CA  LEU A 134       4.459  32.165  -4.300  1.00 50.54           C  
ANISOU 1094  CA  LEU A 134     8058   3308   7834   -262     -5    -82       C  
ATOM   1095  C   LEU A 134       5.670  31.273  -4.233  1.00 52.38           C  
ANISOU 1095  C   LEU A 134     8049   3509   8343   -260    -34     81       C  
ATOM   1096  O   LEU A 134       5.667  30.274  -3.536  1.00 53.99           O  
ANISOU 1096  O   LEU A 134     8179   3756   8577   -243   -129    183       O  
ATOM   1097  CB  LEU A 134       3.775  32.262  -2.937  1.00 50.69           C  
ANISOU 1097  CB  LEU A 134     8192   3433   7632   -331   -184   -121       C  
ATOM   1098  CG  LEU A 134       2.427  32.967  -2.938  1.00 50.21           C  
ANISOU 1098  CG  LEU A 134     8346   3383   7346   -309   -119   -285       C  
ATOM   1099  CD1 LEU A 134       1.905  33.044  -1.518  1.00 51.41           C  
ANISOU 1099  CD1 LEU A 134     8607   3636   7290   -395   -257   -333       C  
ATOM   1100  CD2 LEU A 134       2.516  34.381  -3.473  1.00 50.54           C  
ANISOU 1100  CD2 LEU A 134     8450   3338   7413   -344    -63   -375       C  
ATOM   1101  N   LEU A 135       6.723  31.675  -4.918  1.00 54.07           N  
ANISOU 1101  N   LEU A 135     8122   3636   8785   -280     49    127       N  
ATOM   1102  CA  LEU A 135       7.969  30.939  -4.968  1.00 56.29           C  
ANISOU 1102  CA  LEU A 135     8128   3853   9407   -271     56    288       C  
ATOM   1103  C   LEU A 135       8.853  31.235  -3.772  1.00 59.15           C  
ANISOU 1103  C   LEU A 135     8332   4268   9873   -402   -240    415       C  
ATOM   1104  O   LEU A 135       8.674  32.255  -3.135  1.00 59.31           O  
ANISOU 1104  O   LEU A 135     8470   4353   9711   -521   -401    334       O  
ATOM   1105  CB  LEU A 135       8.708  31.288  -6.256  1.00 56.50           C  
ANISOU 1105  CB  LEU A 135     8066   3758   9640   -246    311    277       C  
ATOM   1106  CG  LEU A 135       7.884  31.157  -7.549  1.00 55.07           C  
ANISOU 1106  CG  LEU A 135     8071   3555   9297   -150    590    145       C  
ATOM   1107  CD1 LEU A 135       8.772  31.215  -8.795  1.00 55.75           C  
ANISOU 1107  CD1 LEU A 135     8054   3533   9595   -130    877    162       C  
ATOM   1108  CD2 LEU A 135       7.082  29.877  -7.547  1.00 54.44           C  
ANISOU 1108  CD2 LEU A 135     8042   3498   9142    -55    639    108       C  
ATOM   1109  N   ILE A 136       9.811  30.334  -3.488  1.00 62.51           N  
ANISOU 1109  N   ILE A 136     8483   4658  10609   -384   -311    612       N  
ATOM   1110  CA  ILE A 136      10.788  30.481  -2.404  1.00 67.01           C  
ANISOU 1110  CA  ILE A 136     8849   5290  11320   -513   -633    782       C  
ATOM   1111  C   ILE A 136      12.208  30.123  -2.843  1.00 72.28           C  
ANISOU 1111  C   ILE A 136     9146   5825  12490   -493   -579    961       C  
ATOM   1112  O   ILE A 136      12.405  29.131  -3.560  1.00 73.21           O  
ANISOU 1112  O   ILE A 136     9127   5820  12869   -350   -341   1027       O  
ATOM   1113  CB  ILE A 136      10.447  29.579  -1.209  1.00 67.71           C  
ANISOU 1113  CB  ILE A 136     8943   5506  11278   -521   -879    932       C  
ATOM   1114  CG1 ILE A 136       8.968  29.672  -0.917  1.00 65.50           C  
ANISOU 1114  CG1 ILE A 136     9002   5324  10560   -505   -842    761       C  
ATOM   1115  CG2 ILE A 136      11.275  29.959   0.015  1.00 71.21           C  
ANISOU 1115  CG2 ILE A 136     9252   6075  11727   -701  -1274   1080       C  
ATOM   1116  CD1 ILE A 136       8.510  28.828   0.250  1.00 66.71           C  
ANISOU 1116  CD1 ILE A 136     9200   5607  10537   -521  -1041    905       C  
ATOM   1117  N   ASP A 137      13.200  30.905  -2.387  1.00 78.48           N  
ANISOU 1117  N   ASP A 137     9754   6625  13436   -642   -793   1031       N  
ATOM   1118  CA  ASP A 137      14.616  30.519  -2.501  1.00 84.78           C  
ANISOU 1118  CA  ASP A 137    10136   7315  14758   -643   -824   1251       C  
ATOM   1119  C   ASP A 137      15.169  29.876  -1.204  1.00 91.44           C  
ANISOU 1119  C   ASP A 137    10758   8272  15713   -712  -1238   1520       C  
ATOM   1120  O   ASP A 137      14.546  29.912  -0.132  1.00 90.00           O  
ANISOU 1120  O   ASP A 137    10769   8277  15150   -802  -1525   1522       O  
ATOM   1121  CB  ASP A 137      15.501  31.692  -2.940  1.00 87.73           C  
ANISOU 1121  CB  ASP A 137    10380   7608  15344   -764   -784   1198       C  
ATOM   1122  CG  ASP A 137      15.428  32.905  -2.001  1.00 89.38           C  
ANISOU 1122  CG  ASP A 137    10724   7948  15285   -985  -1115   1094       C  
ATOM   1123  OD1 ASP A 137      15.216  32.738  -0.770  1.00 91.53           O  
ANISOU 1123  OD1 ASP A 137    11053   8395  15327  -1086  -1476   1150       O  
ATOM   1124  OD2 ASP A 137      15.638  34.037  -2.497  1.00 90.20           O  
ANISOU 1124  OD2 ASP A 137    10874   7973  15424  -1072  -1004    958       O  
ATOM   1125  N   ASP A 138      16.327  29.227  -1.354  1.00 99.48           N  
ANISOU 1125  N   ASP A 138    11363   9167  17267   -661  -1241   1764       N  
ATOM   1126  CA  ASP A 138      17.146  28.687  -0.237  1.00105.49           C  
ANISOU 1126  CA  ASP A 138    11811  10011  18257   -732  -1661   2090       C  
ATOM   1127  C   ASP A 138      17.408  29.705   0.887  1.00108.23           C  
ANISOU 1127  C   ASP A 138    12211  10572  18339   -995  -2127   2082       C  
ATOM   1128  O   ASP A 138      17.540  29.310   2.061  1.00111.16           O  
ANISOU 1128  O   ASP A 138    12521  11119  18594  -1087  -2540   2298       O  
ATOM   1129  CB  ASP A 138      18.492  28.179  -0.782  1.00110.20           C  
ANISOU 1129  CB  ASP A 138    11908  10397  19566   -651  -1544   2318       C  
ATOM   1130  CG  ASP A 138      19.224  29.244  -1.654  1.00112.06           C  
ANISOU 1130  CG  ASP A 138    12028  10507  20042   -724  -1331   2168       C  
ATOM   1131  OD1 ASP A 138      18.551  29.918  -2.477  1.00107.46           O  
ANISOU 1131  OD1 ASP A 138    11756   9891  19179   -709  -1022   1883       O  
ATOM   1132  OD2 ASP A 138      20.471  29.386  -1.528  1.00116.38           O  
ANISOU 1132  OD2 ASP A 138    12158  10982  21078   -794  -1472   2360       O  
ATOM   1133  N   LYS A 139      17.493  30.992   0.513  1.00105.93           N  
ANISOU 1133  N   LYS A 139    12033  10259  17956  -1122  -2055   1838       N  
ATOM   1134  CA  LYS A 139      17.645  32.107   1.466  1.00106.75           C  
ANISOU 1134  CA  LYS A 139    12237  10533  17788  -1392  -2435   1735       C  
ATOM   1135  C   LYS A 139      16.383  32.387   2.312  1.00100.47           C  
ANISOU 1135  C   LYS A 139    11898   9946  16330  -1474  -2572   1545       C  
ATOM   1136  O   LYS A 139      16.409  33.262   3.164  1.00101.69           O  
ANISOU 1136  O   LYS A 139    12182  10246  16209  -1707  -2864   1421       O  
ATOM   1137  CB  LYS A 139      18.080  33.400   0.727  1.00111.32           C  
ANISOU 1137  CB  LYS A 139    12796  10973  18525  -1492  -2257   1523       C  
ATOM   1138  CG  LYS A 139      19.595  33.612   0.558  1.00119.01           C  
ANISOU 1138  CG  LYS A 139    13290  11832  20094  -1582  -2363   1704       C  
ATOM   1139  CD  LYS A 139      19.989  33.937  -0.887  1.00121.30           C  
ANISOU 1139  CD  LYS A 139    13460  11864  20762  -1467  -1873   1632       C  
ATOM   1140  CE  LYS A 139      19.988  32.671  -1.751  1.00122.67           C  
ANISOU 1140  CE  LYS A 139    13497  11898  21211  -1196  -1509   1774       C  
ATOM   1141  NZ  LYS A 139      19.089  32.699  -2.957  1.00118.99           N  
ANISOU 1141  NZ  LYS A 139    13344  11329  20536  -1031  -1007   1560       N  
ATOM   1142  N   GLY A 140      15.293  31.659   2.093  1.00 93.74           N  
ANISOU 1142  N   GLY A 140    11282   9097  15236  -1298  -2350   1507       N  
ATOM   1143  CA  GLY A 140      14.063  31.845   2.867  1.00 90.06           C  
ANISOU 1143  CA  GLY A 140    11222   8809  14185  -1359  -2429   1339       C  
ATOM   1144  C   GLY A 140      13.258  33.079   2.495  1.00 85.11           C  
ANISOU 1144  C   GLY A 140    10922   8144  13269  -1414  -2228    974       C  
ATOM   1145  O   GLY A 140      12.511  33.613   3.308  1.00 83.06           O  
ANISOU 1145  O   GLY A 140    10957   8027  12573  -1541  -2349    799       O  
ATOM   1146  N   THR A 141      13.444  33.543   1.265  1.00 81.70           N  
ANISOU 1146  N   THR A 141    10430   7513  13100  -1322  -1911    873       N  
ATOM   1147  CA  THR A 141      12.732  34.704   0.753  1.00 77.64           C  
ANISOU 1147  CA  THR A 141    10184   6922  12392  -1347  -1697    580       C  
ATOM   1148  C   THR A 141      11.621  34.153  -0.102  1.00 73.06           C  
ANISOU 1148  C   THR A 141     9793   6281  11684  -1125  -1358    515       C  
ATOM   1149  O   THR A 141      11.824  33.171  -0.811  1.00 71.83           O  
ANISOU 1149  O   THR A 141     9482   6048  11760   -961  -1184    658       O  
ATOM   1150  CB  THR A 141      13.628  35.630  -0.096  1.00 78.26           C  
ANISOU 1150  CB  THR A 141    10085   6822  12826  -1400  -1562    539       C  
ATOM   1151  OG1 THR A 141      14.761  36.046   0.669  1.00 82.19           O  
ANISOU 1151  OG1 THR A 141    10348   7367  13511  -1616  -1898    616       O  
ATOM   1152  CG2 THR A 141      12.887  36.868  -0.548  1.00 76.62           C  
ANISOU 1152  CG2 THR A 141    10151   6523  12435  -1431  -1365    275       C  
ATOM   1153  N   ILE A 142      10.472  34.825  -0.066  1.00 70.00           N  
ANISOU 1153  N   ILE A 142     9725   5913  10958  -1128  -1256    288       N  
ATOM   1154  CA  ILE A 142       9.268  34.450  -0.810  1.00 65.95           C  
ANISOU 1154  CA  ILE A 142     9410   5361  10286   -944   -975    203       C  
ATOM   1155  C   ILE A 142       8.907  35.528  -1.835  1.00 63.14           C  
ANISOU 1155  C   ILE A 142     9176   4865   9947   -912   -729     41       C  
ATOM   1156  O   ILE A 142       9.086  36.670  -1.569  1.00 63.90           O  
ANISOU 1156  O   ILE A 142     9325   4921  10031  -1045   -792    -74       O  
ATOM   1157  CB  ILE A 142       8.075  34.127   0.139  1.00 65.19           C  
ANISOU 1157  CB  ILE A 142     9559   5410   9798   -949  -1062    123       C  
ATOM   1158  CG1 ILE A 142       6.830  33.673  -0.640  1.00 62.18           C  
ANISOU 1158  CG1 ILE A 142     9339   4985   9299   -764   -793     48       C  
ATOM   1159  CG2 ILE A 142       7.674  35.301   0.979  1.00 66.02           C  
ANISOU 1159  CG2 ILE A 142     9873   5570   9640  -1119  -1176    -86       C  
ATOM   1160  CD1 ILE A 142       5.986  32.693   0.133  1.00 61.43           C  
ANISOU 1160  CD1 ILE A 142     9346   5012   8983   -721   -851     94       C  
ATOM   1161  N   LYS A 143       8.429  35.132  -3.004  1.00 60.38           N  
ANISOU 1161  N   LYS A 143     8866   4441   9633   -743   -456     47       N  
ATOM   1162  CA  LYS A 143       8.296  36.021  -4.115  1.00 60.24           C  
ANISOU 1162  CA  LYS A 143     8919   4298   9669   -707   -230    -24       C  
ATOM   1163  C   LYS A 143       7.055  35.727  -4.952  1.00 58.42           C  
ANISOU 1163  C   LYS A 143     8882   4070   9244   -552    -24    -90       C  
ATOM   1164  O   LYS A 143       6.837  34.604  -5.309  1.00 56.75           O  
ANISOU 1164  O   LYS A 143     8639   3893   9028   -444     56    -37       O  
ATOM   1165  CB  LYS A 143       9.507  35.891  -5.044  1.00 61.50           C  
ANISOU 1165  CB  LYS A 143     8843   4350  10172   -690    -81    105       C  
ATOM   1166  CG  LYS A 143      10.849  35.971  -4.358  1.00 64.48           C  
ANISOU 1166  CG  LYS A 143     8952   4718  10830   -828   -283    213       C  
ATOM   1167  CD  LYS A 143      11.948  36.167  -5.383  1.00 66.24           C  
ANISOU 1167  CD  LYS A 143     8955   4797  11414   -820    -72    312       C  
ATOM   1168  CE  LYS A 143      13.317  36.271  -4.736  1.00 69.67           C  
ANISOU 1168  CE  LYS A 143     9072   5208  12191   -962   -282    433       C  
ATOM   1169  NZ  LYS A 143      13.998  37.511  -5.215  1.00 72.74           N  
ANISOU 1169  NZ  LYS A 143     9387   5457  12793  -1077   -187    406       N  
ATOM   1170  N   LEU A 144       6.320  36.770  -5.343  1.00 58.15           N  
ANISOU 1170  N   LEU A 144     9021   3978   9093   -546     62   -193       N  
ATOM   1171  CA  LEU A 144       5.174  36.609  -6.191  1.00 56.61           C  
ANISOU 1171  CA  LEU A 144     8984   3790   8733   -413    220   -231       C  
ATOM   1172  C   LEU A 144       5.618  36.386  -7.600  1.00 56.40           C  
ANISOU 1172  C   LEU A 144     8905   3712   8810   -342    437   -144       C  
ATOM   1173  O   LEU A 144       6.463  37.102  -8.121  1.00 56.18           O  
ANISOU 1173  O   LEU A 144     8802   3591   8952   -396    525    -84       O  
ATOM   1174  CB  LEU A 144       4.296  37.833  -6.238  1.00 57.87           C  
ANISOU 1174  CB  LEU A 144     9313   3885   8790   -420    245   -327       C  
ATOM   1175  CG  LEU A 144       3.872  38.584  -4.999  1.00 60.64           C  
ANISOU 1175  CG  LEU A 144     9753   4227   9059   -518    106   -464       C  
ATOM   1176  CD1 LEU A 144       2.515  39.248  -5.247  1.00 61.03           C  
ANISOU 1176  CD1 LEU A 144     9970   4222   8996   -437    194   -549       C  
ATOM   1177  CD2 LEU A 144       3.817  37.704  -3.762  1.00 61.76           C  
ANISOU 1177  CD2 LEU A 144     9885   4509   9071   -567    -64   -498       C  
ATOM   1178  N   ALA A 145       4.996  35.407  -8.232  1.00 55.73           N  
ANISOU 1178  N   ALA A 145     8874   3688   8612   -234    540   -151       N  
ATOM   1179  CA  ALA A 145       5.213  35.170  -9.636  1.00 56.41           C  
ANISOU 1179  CA  ALA A 145     8970   3751   8709   -176    767   -109       C  
ATOM   1180  C   ALA A 145       3.930  35.436 -10.363  1.00 55.63           C  
ANISOU 1180  C   ALA A 145     9072   3699   8362   -108    814   -155       C  
ATOM   1181  O   ALA A 145       2.853  35.344  -9.785  1.00 55.01           O  
ANISOU 1181  O   ALA A 145     9082   3674   8145    -75    694   -226       O  
ATOM   1182  CB  ALA A 145       5.696  33.749  -9.864  1.00 56.68           C  
ANISOU 1182  CB  ALA A 145     8882   3803   8849   -128    863    -94       C  
ATOM   1183  N   ASP A 146       4.068  35.766 -11.637  1.00 56.91           N  
ANISOU 1183  N   ASP A 146     9298   3849   8474    -92    990   -100       N  
ATOM   1184  CA  ASP A 146       2.940  35.953 -12.553  1.00 57.08           C  
ANISOU 1184  CA  ASP A 146     9499   3938   8249    -34   1024   -104       C  
ATOM   1185  C   ASP A 146       2.040  37.184 -12.319  1.00 55.41           C  
ANISOU 1185  C   ASP A 146     9386   3688   7978    -22    908    -72       C  
ATOM   1186  O   ASP A 146       0.904  37.267 -12.813  1.00 55.97           O  
ANISOU 1186  O   ASP A 146     9571   3820   7873     36    868    -67       O  
ATOM   1187  CB  ASP A 146       2.110  34.634 -12.665  1.00 57.35           C  
ANISOU 1187  CB  ASP A 146     9576   4079   8132     23   1006   -211       C  
ATOM   1188  CG  ASP A 146       2.908  33.483 -13.250  1.00 58.70           C  
ANISOU 1188  CG  ASP A 146     9676   4258   8369     21   1189   -248       C  
ATOM   1189  OD1 ASP A 146       3.950  33.723 -13.926  1.00 57.28           O  
ANISOU 1189  OD1 ASP A 146     9450   4027   8284    -14   1372   -185       O  
ATOM   1190  OD2 ASP A 146       2.463  32.322 -12.997  1.00 63.69           O  
ANISOU 1190  OD2 ASP A 146    10288   4927   8982     54   1167   -345       O  
ATOM   1191  N   PHE A 147       2.550  38.136 -11.566  1.00 53.89           N  
ANISOU 1191  N   PHE A 147     9134   3381   7961    -84    853    -55       N  
ATOM   1192  CA  PHE A 147       1.884  39.424 -11.382  1.00 51.87           C  
ANISOU 1192  CA  PHE A 147     8951   3029   7727    -80    796    -30       C  
ATOM   1193  C   PHE A 147       1.669  40.057 -12.734  1.00 52.33           C  
ANISOU 1193  C   PHE A 147     9099   3072   7709    -42    909    129       C  
ATOM   1194  O   PHE A 147       2.509  39.965 -13.589  1.00 52.51           O  
ANISOU 1194  O   PHE A 147     9109   3105   7736    -73   1056    222       O  
ATOM   1195  CB  PHE A 147       2.692  40.332 -10.452  1.00 52.22           C  
ANISOU 1195  CB  PHE A 147     8912   2932   7995   -185    751    -62       C  
ATOM   1196  CG  PHE A 147       4.135  40.453 -10.831  1.00 53.29           C  
ANISOU 1196  CG  PHE A 147     8927   3008   8311   -267    856     22       C  
ATOM   1197  CD1 PHE A 147       4.545  41.355 -11.797  1.00 54.17           C  
ANISOU 1197  CD1 PHE A 147     9055   3016   8508   -284   1005    167       C  
ATOM   1198  CD2 PHE A 147       5.092  39.639 -10.214  1.00 53.55           C  
ANISOU 1198  CD2 PHE A 147     8810   3084   8453   -326    809    -18       C  
ATOM   1199  CE1 PHE A 147       5.871  41.445 -12.171  1.00 55.91           C  
ANISOU 1199  CE1 PHE A 147     9147   3174   8919   -362   1135    250       C  
ATOM   1200  CE2 PHE A 147       6.436  39.726 -10.598  1.00 55.16           C  
ANISOU 1200  CE2 PHE A 147     8862   3220   8876   -396    920     71       C  
ATOM   1201  CZ  PHE A 147       6.823  40.615 -11.583  1.00 55.93           C  
ANISOU 1201  CZ  PHE A 147     8979   3214   9057   -415   1098    194       C  
ATOM   1202  N   GLY A 148       0.480  40.639 -12.898  1.00 52.76           N  
ANISOU 1202  N   GLY A 148     9241   3112   7692     25    839    170       N  
ATOM   1203  CA  GLY A 148       0.028  41.286 -14.082  1.00 54.25           C  
ANISOU 1203  CA  GLY A 148     9519   3302   7790     70    885    359       C  
ATOM   1204  C   GLY A 148      -0.053  40.544 -15.357  1.00 55.34           C  
ANISOU 1204  C   GLY A 148     9745   3614   7665     86    951    436       C  
ATOM   1205  O   GLY A 148      -0.341  41.140 -16.410  1.00 58.17           O  
ANISOU 1205  O   GLY A 148    10196   3997   7909    103    981    630       O  
ATOM   1206  N   LEU A 149       0.138  39.243 -15.328  1.00 55.50           N  
ANISOU 1206  N   LEU A 149     9751   3761   7573     75    974    294       N  
ATOM   1207  CA  LEU A 149       0.107  38.494 -16.599  1.00 57.08           C  
ANISOU 1207  CA  LEU A 149    10057   4125   7504     65   1069    321       C  
ATOM   1208  C   LEU A 149      -1.320  38.322 -17.077  1.00 55.94           C  
ANISOU 1208  C   LEU A 149    10007   4110   7135    120    909    339       C  
ATOM   1209  O   LEU A 149      -1.578  38.434 -18.264  1.00 57.13           O  
ANISOU 1209  O   LEU A 149    10281   4378   7045    104    928    461       O  
ATOM   1210  CB  LEU A 149       0.871  37.175 -16.486  1.00 57.26           C  
ANISOU 1210  CB  LEU A 149    10020   4199   7537     31   1188    156       C  
ATOM   1211  CG  LEU A 149       2.387  37.347 -16.327  1.00 58.95           C  
ANISOU 1211  CG  LEU A 149    10118   4297   7981    -27   1366    186       C  
ATOM   1212  CD1 LEU A 149       3.114  36.013 -16.338  1.00 59.32           C  
ANISOU 1212  CD1 LEU A 149    10082   4375   8081    -43   1504     51       C  
ATOM   1213  CD2 LEU A 149       2.990  38.216 -17.436  1.00 61.83           C  
ANISOU 1213  CD2 LEU A 149    10558   4639   8294    -72   1548    372       C  
ATOM   1214  N   ALA A 150      -2.229  38.118 -16.134  1.00 53.54           N  
ANISOU 1214  N   ALA A 150     9639   3785   6915    174    749    233       N  
ATOM   1215  CA  ALA A 150      -3.663  38.042 -16.429  1.00 54.94           C  
ANISOU 1215  CA  ALA A 150     9853   4057   6962    230    576    257       C  
ATOM   1216  C   ALA A 150      -4.150  39.227 -17.258  1.00 59.28           C  
ANISOU 1216  C   ALA A 150    10464   4594   7466    262    512    514       C  
ATOM   1217  O   ALA A 150      -4.811  39.030 -18.306  1.00 61.67           O  
ANISOU 1217  O   ALA A 150    10853   5059   7518    258    420    611       O  
ATOM   1218  CB  ALA A 150      -4.458  37.953 -15.132  1.00 52.59           C  
ANISOU 1218  CB  ALA A 150     9453   3682   6844    286    463    133       C  
ATOM   1219  N   ARG A 151      -3.831  40.436 -16.771  1.00 60.91           N  
ANISOU 1219  N   ARG A 151    10619   4602   7919    285    549    625       N  
ATOM   1220  CA  ARG A 151      -4.177  41.657 -17.459  1.00 65.59           C  
ANISOU 1220  CA  ARG A 151    11245   5124   8550    323    512    902       C  
ATOM   1221  C   ARG A 151      -3.694  41.608 -18.880  1.00 65.80           C  
ANISOU 1221  C   ARG A 151    11410   5301   8290    263    587   1084       C  
ATOM   1222  O   ARG A 151      -4.495  41.835 -19.786  1.00 68.70           O  
ANISOU 1222  O   ARG A 151    11847   5787   8469    288    456   1281       O  
ATOM   1223  CB  ARG A 151      -3.582  42.870 -16.780  1.00 69.38           C  
ANISOU 1223  CB  ARG A 151    11659   5340   9361    324    605    960       C  
ATOM   1224  CG  ARG A 151      -3.693  44.139 -17.595  1.00 75.24           C  
ANISOU 1224  CG  ARG A 151    12434   5974  10179    354    617   1284       C  
ATOM   1225  CD  ARG A 151      -4.786  45.059 -17.097  1.00 81.09           C  
ANISOU 1225  CD  ARG A 151    13084   6531  11194    461    506   1367       C  
ATOM   1226  NE  ARG A 151      -4.188  46.193 -16.358  1.00 84.28           N  
ANISOU 1226  NE  ARG A 151    13424   6632  11967    443    634   1357       N  
ATOM   1227  CZ  ARG A 151      -3.749  47.340 -16.901  1.00 88.09           C  
ANISOU 1227  CZ  ARG A 151    13915   6936  12619    436    727   1616       C  
ATOM   1228  NH1 ARG A 151      -3.873  47.628 -18.204  1.00 90.15           N  
ANISOU 1228  NH1 ARG A 151    14253   7290  12708    455    702   1957       N  
ATOM   1229  NH2 ARG A 151      -3.186  48.236 -16.114  1.00 91.94           N  
ANISOU 1229  NH2 ARG A 151    14336   7141  13453    396    844   1536       N  
ATOM   1230  N   ALA A 152      -2.412  41.313 -19.087  1.00 63.54           N  
ANISOU 1230  N   ALA A 152    11159   5019   7965    180    795   1029       N  
ATOM   1231  CA  ALA A 152      -1.855  41.284 -20.444  1.00 64.75           C  
ANISOU 1231  CA  ALA A 152    11460   5309   7829    108    931   1188       C  
ATOM   1232  C   ALA A 152      -2.515  40.283 -21.425  1.00 65.97           C  
ANISOU 1232  C   ALA A 152    11756   5747   7561     71    849   1135       C  
ATOM   1233  O   ALA A 152      -2.316  40.399 -22.613  1.00 67.94           O  
ANISOU 1233  O   ALA A 152    12163   6140   7509      6    923   1295       O  
ATOM   1234  CB  ALA A 152      -0.376  41.046 -20.384  1.00 64.29           C  
ANISOU 1234  CB  ALA A 152    11376   5185   7864     30   1198   1102       C  
ATOM   1235  N   PHE A 153      -3.336  39.346 -20.929  1.00 64.43           N  
ANISOU 1235  N   PHE A 153    11511   5632   7338     99    696    916       N  
ATOM   1236  CA  PHE A 153      -4.014  38.369 -21.735  1.00 65.85           C  
ANISOU 1236  CA  PHE A 153    11802   6056   7162     47    598    820       C  
ATOM   1237  C   PHE A 153      -5.547  38.307 -21.394  1.00 68.18           C  
ANISOU 1237  C   PHE A 153    12013   6396   7496    119    288    822       C  
ATOM   1238  O   PHE A 153      -6.342  39.018 -21.982  1.00 71.18           O  
ANISOU 1238  O   PHE A 153    12417   6838   7786    147    102   1069       O  
ATOM   1239  CB  PHE A 153      -3.287  37.030 -21.528  1.00 63.96           C  
ANISOU 1239  CB  PHE A 153    11562   5847   6893    -13    785    505       C  
ATOM   1240  CG  PHE A 153      -1.761  37.069 -21.750  1.00 62.61           C  
ANISOU 1240  CG  PHE A 153    11414   5597   6776    -70   1107    499       C  
ATOM   1241  CD1 PHE A 153      -1.240  37.352 -22.968  1.00 64.76           C  
ANISOU 1241  CD1 PHE A 153    11855   5979   6771   -151   1272    636       C  
ATOM   1242  CD2 PHE A 153      -0.852  36.703 -20.745  1.00 59.75           C  
ANISOU 1242  CD2 PHE A 153    10895   5066   6738    -52   1246    349       C  
ATOM   1243  CE1 PHE A 153       0.162  37.371 -23.163  1.00 65.17           C  
ANISOU 1243  CE1 PHE A 153    11901   5943   6917   -203   1601    628       C  
ATOM   1244  CE2 PHE A 153       0.547  36.723 -20.952  1.00 59.83           C  
ANISOU 1244  CE2 PHE A 153    10882   4995   6854   -103   1534    355       C  
ATOM   1245  CZ  PHE A 153       1.053  37.071 -22.149  1.00 62.19           C  
ANISOU 1245  CZ  PHE A 153    11331   5376   6921   -174   1727    489       C  
ATOM   1246  N   GLY A 154      -5.998  37.467 -20.471  1.00 69.18           N  
ANISOU 1246  N   GLY A 154    12024   6487   7771    149    231    576       N  
ATOM   1247  CA  GLY A 154      -7.440  37.187 -20.360  1.00 72.34           C  
ANISOU 1247  CA  GLY A 154    12350   6966   8168    190    -30    556       C  
ATOM   1248  C   GLY A 154      -7.837  35.993 -19.483  1.00 73.71           C  
ANISOU 1248  C   GLY A 154    12423   7127   8456    192    -43    259       C  
ATOM   1249  O   GLY A 154      -8.758  36.107 -18.665  1.00 77.43           O  
ANISOU 1249  O   GLY A 154    12751   7516   9149    270   -171    242       O  
ATOM   1250  N   VAL A 159      -8.659  22.758 -19.324  1.00173.87           N  
ANISOU 1250  N   VAL A 159    24951  19701  21410   -475    714  -2255       N  
ATOM   1251  CA  VAL A 159      -9.421  23.978 -19.578  1.00163.73           C  
ANISOU 1251  CA  VAL A 159    23702  18603  19904   -455    431  -2049       C  
ATOM   1252  C   VAL A 159     -10.101  24.453 -18.289  1.00156.10           C  
ANISOU 1252  C   VAL A 159    22546  17553  19211   -324    279  -1857       C  
ATOM   1253  O   VAL A 159      -9.707  25.454 -17.725  1.00151.58           O  
ANISOU 1253  O   VAL A 159    21949  16951  18692   -214    273  -1639       O  
ATOM   1254  CB  VAL A 159     -10.458  23.784 -20.728  1.00164.33           C  
ANISOU 1254  CB  VAL A 159    23879  18892  19665   -614    211  -2187       C  
ATOM   1255  CG1 VAL A 159     -11.089  25.122 -21.107  1.00156.73           C  
ANISOU 1255  CG1 VAL A 159    22948  18119  18483   -582    -73  -1916       C  
ATOM   1256  CG2 VAL A 159      -9.801  23.151 -21.961  1.00168.37           C  
ANISOU 1256  CG2 VAL A 159    24607  19486  19879   -775    404  -2443       C  
ATOM   1257  N   TYR A 160     -11.079  23.681 -17.813  1.00157.46           N  
ANISOU 1257  N   TYR A 160    22586  17670  19569   -349    191  -1961       N  
ATOM   1258  CA  TYR A 160     -12.042  24.128 -16.796  1.00149.87           C  
ANISOU 1258  CA  TYR A 160    21458  16669  18816   -256     33  -1807       C  
ATOM   1259  C   TYR A 160     -11.776  23.790 -15.320  1.00142.10           C  
ANISOU 1259  C   TYR A 160    20341  15493  18156   -156    173  -1744       C  
ATOM   1260  O   TYR A 160     -12.363  24.437 -14.461  1.00130.33           O  
ANISOU 1260  O   TYR A 160    18754  13981  16783    -71     88  -1595       O  
ATOM   1261  CB  TYR A 160     -13.433  23.552 -17.130  1.00154.53           C  
ANISOU 1261  CB  TYR A 160    21956  17325  19434   -353   -163  -1932       C  
ATOM   1262  CG  TYR A 160     -13.979  23.774 -18.541  1.00156.18           C  
ANISOU 1262  CG  TYR A 160    22272  17758  19310   -484   -383  -1994       C  
ATOM   1263  CD1 TYR A 160     -14.358  25.057 -18.958  1.00150.14           C  
ANISOU 1263  CD1 TYR A 160    21531  17143  18372   -436   -600  -1758       C  
ATOM   1264  CD2 TYR A 160     -14.203  22.691 -19.431  1.00154.77           C  
ANISOU 1264  CD2 TYR A 160    22164  17639  19002   -666   -391  -2283       C  
ATOM   1265  CE1 TYR A 160     -14.899  25.276 -20.218  1.00148.83           C  
ANISOU 1265  CE1 TYR A 160    21457  17205  17884   -561   -841  -1765       C  
ATOM   1266  CE2 TYR A 160     -14.746  22.912 -20.695  1.00154.42           C  
ANISOU 1266  CE2 TYR A 160    22231  17836  18605   -811   -630  -2334       C  
ATOM   1267  CZ  TYR A 160     -15.093  24.197 -21.082  1.00151.28           C  
ANISOU 1267  CZ  TYR A 160    21855  17609  18014   -756   -868  -2056       C  
ATOM   1268  OH  TYR A 160     -15.652  24.385 -22.320  1.00148.43           O  
ANISOU 1268  OH  TYR A 160    21602  17506  17289   -908  -1138  -2069       O  
ATOM   1269  N   THR A 161     -11.034  22.717 -15.028  1.00148.44           N  
ANISOU 1269  N   THR A 161    21130  16156  19112   -174    381  -1859       N  
ATOM   1270  CA  THR A 161     -10.550  22.448 -13.646  1.00153.19           C  
ANISOU 1270  CA  THR A 161    21628  16598  19979    -82    505  -1744       C  
ATOM   1271  C   THR A 161      -9.162  23.051 -13.425  1.00153.03           C  
ANISOU 1271  C   THR A 161    21664  16549  19928    -16    617  -1615       C  
ATOM   1272  O   THR A 161      -8.744  23.266 -12.280  1.00138.07           O  
ANISOU 1272  O   THR A 161    19704  14580  18173     57    647  -1467       O  
ATOM   1273  CB  THR A 161     -10.531  20.952 -13.245  1.00162.77           C  
ANISOU 1273  CB  THR A 161    22747  17642  21457   -120    653  -1869       C  
ATOM   1274  OG1 THR A 161     -10.050  20.154 -14.330  1.00180.90           O  
ANISOU 1274  OG1 THR A 161    25118  19909  23705   -215    779  -2090       O  
ATOM   1275  CG2 THR A 161     -11.923  20.453 -12.832  1.00165.27           C  
ANISOU 1275  CG2 THR A 161    22943  17934  21917   -157    555  -1915       C  
ATOM   1276  N   HIS A 162      -8.464  23.310 -14.534  1.00162.31           N  
ANISOU 1276  N   HIS A 162    22962  17795  20914    -59    678  -1675       N  
ATOM   1277  CA  HIS A 162      -7.405  24.327 -14.602  1.00172.05           C  
ANISOU 1277  CA  HIS A 162    24258  19053  22057     -9    726  -1529       C  
ATOM   1278  C   HIS A 162      -7.861  25.569 -13.793  1.00169.77           C  
ANISOU 1278  C   HIS A 162    23939  18802  21761     67    565  -1333       C  
ATOM   1279  O   HIS A 162      -7.085  26.127 -12.993  1.00177.21           O  
ANISOU 1279  O   HIS A 162    24853  19686  22793    124    603  -1201       O  
ATOM   1280  CB  HIS A 162      -7.116  24.722 -16.079  1.00178.85           C  
ANISOU 1280  CB  HIS A 162    25283  20046  22625    -83    756  -1597       C  
ATOM   1281  CG  HIS A 162      -5.656  24.736 -16.455  1.00185.35           C  
ANISOU 1281  CG  HIS A 162    26153  20812  23460    -83    987  -1592       C  
ATOM   1282  ND1 HIS A 162      -4.723  25.539 -15.830  1.00185.66           N  
ANISOU 1282  ND1 HIS A 162    26143  20792  23605     -9   1027  -1405       N  
ATOM   1283  CD2 HIS A 162      -4.981  24.069 -17.424  1.00187.57           C  
ANISOU 1283  CD2 HIS A 162    26517  21080  23670   -158   1204  -1764       C  
ATOM   1284  CE1 HIS A 162      -3.535  25.348 -16.381  1.00185.07           C  
ANISOU 1284  CE1 HIS A 162    26093  20667  23557    -29   1252  -1440       C  
ATOM   1285  NE2 HIS A 162      -3.664  24.464 -17.354  1.00186.50           N  
ANISOU 1285  NE2 HIS A 162    26360  20871  23630   -114   1382  -1659       N  
ATOM   1286  N   GLU A 163      -9.120  25.976 -14.022  1.00153.86           N  
ANISOU 1286  N   GLU A 163    21922  16878  19659     60    388  -1328       N  
ATOM   1287  CA  GLU A 163      -9.818  26.972 -13.200  1.00141.07           C  
ANISOU 1287  CA  GLU A 163    20243  15256  18100    135    265  -1186       C  
ATOM   1288  C   GLU A 163     -10.172  26.395 -11.796  1.00141.79           C  
ANISOU 1288  C   GLU A 163    20217  15242  18413    170    309  -1185       C  
ATOM   1289  O   GLU A 163      -9.546  26.773 -10.796  1.00141.24           O  
ANISOU 1289  O   GLU A 163    20137  15110  18415    213    365  -1092       O  
ATOM   1290  CB  GLU A 163     -11.044  27.554 -13.959  1.00136.75           C  
ANISOU 1290  CB  GLU A 163    19693  14823  17440    124     69  -1159       C  
ATOM   1291  CG  GLU A 163     -10.656  28.374 -15.213  1.00135.98           C  
ANISOU 1291  CG  GLU A 163    19729  14844  17091     97     11  -1081       C  
ATOM   1292  CD  GLU A 163     -11.829  28.921 -16.059  1.00136.86           C  
ANISOU 1292  CD  GLU A 163    19831  15089  17078     79   -224  -1007       C  
ATOM   1293  OE1 GLU A 163     -12.488  28.122 -16.763  1.00136.65           O  
ANISOU 1293  OE1 GLU A 163    19805  15161  16954    -14   -324  -1138       O  
ATOM   1294  OE2 GLU A 163     -12.071  30.164 -16.081  1.00124.70           O  
ANISOU 1294  OE2 GLU A 163    18281  13553  15544    151   -320   -811       O  
ATOM   1295  N   VAL A 164     -11.122  25.453 -11.727  1.00145.73           N  
ANISOU 1295  N   VAL A 164    20634  15724  19010    134    286  -1286       N  
ATOM   1296  CA  VAL A 164     -11.638  24.860 -10.423  1.00139.87           C  
ANISOU 1296  CA  VAL A 164    19782  14888  18472    156    341  -1266       C  
ATOM   1297  C   VAL A 164     -10.534  24.474  -9.407  1.00118.87           C  
ANISOU 1297  C   VAL A 164    17124  12139  15901    180    471  -1188       C  
ATOM   1298  O   VAL A 164     -10.619  24.779  -8.216  1.00 95.88           O  
ANISOU 1298  O   VAL A 164    14190   9202  13038    214    488  -1089       O  
ATOM   1299  CB  VAL A 164     -12.593  23.619 -10.650  1.00143.28           C  
ANISOU 1299  CB  VAL A 164    20119  15285  19036     89    340  -1404       C  
ATOM   1300  CG1 VAL A 164     -13.012  22.959  -9.330  1.00140.80           C  
ANISOU 1300  CG1 VAL A 164    19700  14864  18932    107    434  -1353       C  
ATOM   1301  CG2 VAL A 164     -13.851  23.985 -11.448  1.00140.67           C  
ANISOU 1301  CG2 VAL A 164    19741  15052  18654     56    163  -1457       C  
ATOM   1302  N   VAL A 165      -8.088  24.560  -8.658  1.00 74.40           N  
ANISOU 1302  N   VAL A 165    11531   6433  10303    208    595  -1028       N  
ATOM   1303  CA  VAL A 165      -7.463  25.245  -7.590  1.00 71.25           C  
ANISOU 1303  CA  VAL A 165    11143   6038   9891    229    569   -893       C  
ATOM   1304  C   VAL A 165      -7.970  26.625  -7.605  1.00 71.31           C  
ANISOU 1304  C   VAL A 165    11216   6110   9768    247    488   -885       C  
ATOM   1305  O   VAL A 165      -8.419  27.096  -6.593  1.00 72.95           O  
ANISOU 1305  O   VAL A 165    11430   6323   9965    255    467   -846       O  
ATOM   1306  CB  VAL A 165      -5.909  25.310  -7.653  1.00 72.93           C  
ANISOU 1306  CB  VAL A 165    11344   6217  10146    227    609   -816       C  
ATOM   1307  CG1 VAL A 165      -5.285  24.241  -6.748  1.00 73.86           C  
ANISOU 1307  CG1 VAL A 165    11363   6256  10443    227    651   -711       C  
ATOM   1308  CG2 VAL A 165      -5.353  25.235  -9.087  1.00 76.46           C  
ANISOU 1308  CG2 VAL A 165    11822   6661  10569    216    687   -905       C  
ATOM   1309  N   THR A 166      -7.923  27.283  -8.750  1.00 74.44           N  
ANISOU 1309  N   THR A 166    11666   6548  10069    251    457   -919       N  
ATOM   1310  CA  THR A 166      -7.908  28.754  -8.720  1.00 80.42           C  
ANISOU 1310  CA  THR A 166    12479   7325  10748    274    399   -859       C  
ATOM   1311  C   THR A 166      -9.093  29.295  -7.932  1.00 73.48           C  
ANISOU 1311  C   THR A 166    11580   6438   9899    305    361   -861       C  
ATOM   1312  O   THR A 166      -8.988  30.360  -7.269  1.00 72.19           O  
ANISOU 1312  O   THR A 166    11451   6246   9730    316    358   -826       O  
ATOM   1313  CB  THR A 166      -7.890  29.445 -10.103  1.00 92.04           C  
ANISOU 1313  CB  THR A 166    14014   8848  12107    277    362   -851       C  
ATOM   1314  OG1 THR A 166      -9.199  29.400 -10.695  1.00100.39           O  
ANISOU 1314  OG1 THR A 166    15053   9958  13130    288    275   -890       O  
ATOM   1315  CG2 THR A 166      -6.804  28.832 -11.070  1.00 97.11           C  
ANISOU 1315  CG2 THR A 166    14690   9503  12702    237    453   -881       C  
ATOM   1316  N   LEU A 167     -10.172  28.508  -7.974  1.00 65.08           N  
ANISOU 1316  N   LEU A 167    10451   5384   8893    307    355   -920       N  
ATOM   1317  CA  LEU A 167     -11.391  28.792  -7.247  1.00 60.55           C  
ANISOU 1317  CA  LEU A 167     9821   4788   8395    335    358   -931       C  
ATOM   1318  C   LEU A 167     -11.315  29.045  -5.758  1.00 56.73           C  
ANISOU 1318  C   LEU A 167     9361   4268   7922    329    440   -909       C  
ATOM   1319  O   LEU A 167     -12.174  29.740  -5.225  1.00 59.00           O  
ANISOU 1319  O   LEU A 167     9632   4527   8258    358    475   -928       O  
ATOM   1320  CB  LEU A 167     -12.373  27.661  -7.493  1.00 61.21           C  
ANISOU 1320  CB  LEU A 167     9808   4876   8571    317    355   -997       C  
ATOM   1321  CG  LEU A 167     -13.655  28.169  -8.062  1.00 65.24           C  
ANISOU 1321  CG  LEU A 167    10238   5406   9143    348    265  -1010       C  
ATOM   1322  CD1 LEU A 167     -13.477  28.749  -9.463  1.00 67.69           C  
ANISOU 1322  CD1 LEU A 167    10593   5788   9336    349    132   -986       C  
ATOM   1323  CD2 LEU A 167     -14.603  27.003  -8.138  1.00 67.13           C  
ANISOU 1323  CD2 LEU A 167    10360   5638   9507    308    263  -1085       C  
ATOM   1324  N   TRP A 168     -10.361  28.458  -5.048  1.00 53.86           N  
ANISOU 1324  N   TRP A 168     9031   3909   7522    287    475   -869       N  
ATOM   1325  CA  TRP A 168     -10.370  28.569  -3.582  1.00 53.13           C  
ANISOU 1325  CA  TRP A 168     8980   3819   7386    254    536   -843       C  
ATOM   1326  C   TRP A 168      -9.889  29.895  -3.049  1.00 54.42           C  
ANISOU 1326  C   TRP A 168     9237   3979   7458    235    526   -857       C  
ATOM   1327  O   TRP A 168     -10.128  30.226  -1.881  1.00 53.87           O  
ANISOU 1327  O   TRP A 168     9228   3918   7319    196    590   -883       O  
ATOM   1328  CB  TRP A 168      -9.521  27.522  -2.957  1.00 52.91           C  
ANISOU 1328  CB  TRP A 168     8948   3808   7347    208    541   -755       C  
ATOM   1329  CG  TRP A 168      -9.887  26.148  -3.347  1.00 53.81           C  
ANISOU 1329  CG  TRP A 168     8969   3886   7589    217    579   -746       C  
ATOM   1330  CD1 TRP A 168     -11.111  25.681  -3.733  1.00 54.01           C  
ANISOU 1330  CD1 TRP A 168     8921   3883   7716    234    619   -818       C  
ATOM   1331  CD2 TRP A 168      -9.025  25.049  -3.338  1.00 54.17           C  
ANISOU 1331  CD2 TRP A 168     8967   3898   7716    200    585   -664       C  
ATOM   1332  NE1 TRP A 168     -11.035  24.399  -4.036  1.00 56.19           N  
ANISOU 1332  NE1 TRP A 168     9125   4109   8116    219    651   -810       N  
ATOM   1333  CE2 TRP A 168      -9.755  23.961  -3.808  1.00 56.06           C  
ANISOU 1333  CE2 TRP A 168     9121   4074   8102    206    645   -713       C  
ATOM   1334  CE3 TRP A 168      -7.666  24.879  -3.012  1.00 55.35           C  
ANISOU 1334  CE3 TRP A 168     9114   4048   7866    181    543   -547       C  
ATOM   1335  CZ2 TRP A 168      -9.204  22.688  -3.921  1.00 55.28           C  
ANISOU 1335  CZ2 TRP A 168     8948   3892   8163    198    694   -660       C  
ATOM   1336  CZ3 TRP A 168      -7.104  23.654  -3.162  1.00 57.35           C  
ANISOU 1336  CZ3 TRP A 168     9276   4227   8287    187    580   -472       C  
ATOM   1337  CH2 TRP A 168      -7.876  22.556  -3.614  1.00 56.82           C  
ANISOU 1337  CH2 TRP A 168     9136   4075   8376    198    669   -534       C  
ATOM   1338  N   TYR A 169      -9.210  30.654  -3.908  1.00 54.35           N  
ANISOU 1338  N   TYR A 169     9248   3955   7447    249    463   -849       N  
ATOM   1339  CA  TYR A 169      -8.539  31.872  -3.480  1.00 56.66           C  
ANISOU 1339  CA  TYR A 169     9618   4220   7687    213    450   -863       C  
ATOM   1340  C   TYR A 169      -9.210  33.140  -4.123  1.00 57.64           C  
ANISOU 1340  C   TYR A 169     9745   4266   7889    275    465   -899       C  
ATOM   1341  O   TYR A 169      -8.637  34.228  -4.175  1.00 56.74           O  
ANISOU 1341  O   TYR A 169     9679   4093   7785    257    456   -903       O  
ATOM   1342  CB  TYR A 169      -7.057  31.777  -3.833  1.00 55.82           C  
ANISOU 1342  CB  TYR A 169     9513   4132   7563    171    381   -792       C  
ATOM   1343  CG  TYR A 169      -6.416  30.515  -3.335  1.00 54.35           C  
ANISOU 1343  CG  TYR A 169     9284   3995   7370    134    360   -719       C  
ATOM   1344  CD1 TYR A 169      -6.080  30.374  -2.024  1.00 55.06           C  
ANISOU 1344  CD1 TYR A 169     9411   4132   7375     60    330   -685       C  
ATOM   1345  CD2 TYR A 169      -6.187  29.443  -4.185  1.00 52.98           C  
ANISOU 1345  CD2 TYR A 169     9033   3816   7279    168    374   -680       C  
ATOM   1346  CE1 TYR A 169      -5.523  29.205  -1.550  1.00 54.64           C  
ANISOU 1346  CE1 TYR A 169     9300   4116   7341     34    295   -567       C  
ATOM   1347  CE2 TYR A 169      -5.633  28.288  -3.722  1.00 52.12           C  
ANISOU 1347  CE2 TYR A 169     8862   3713   7227    148    371   -596       C  
ATOM   1348  CZ  TYR A 169      -5.295  28.179  -2.408  1.00 53.29           C  
ANISOU 1348  CZ  TYR A 169     9029   3904   7312     88    321   -516       C  
ATOM   1349  OH  TYR A 169      -4.703  27.011  -1.970  1.00 56.10           O  
ANISOU 1349  OH  TYR A 169     9304   4258   7753     76    301   -381       O  
ATOM   1350  N   ARG A 170     -10.446  32.947  -4.544  1.00 57.16           N  
ANISOU 1350  N   ARG A 170     9613   4193   7913    342    484   -912       N  
ATOM   1351  CA  ARG A 170     -11.107  33.825  -5.413  1.00 57.62           C  
ANISOU 1351  CA  ARG A 170     9628   4192   8073    415    455   -884       C  
ATOM   1352  C   ARG A 170     -12.122  34.641  -4.602  1.00 58.71           C  
ANISOU 1352  C   ARG A 170     9742   4228   8337    453    564   -953       C  
ATOM   1353  O   ARG A 170     -12.843  34.102  -3.776  1.00 56.40           O  
ANISOU 1353  O   ARG A 170     9421   3944   8064    444    656  -1017       O  
ATOM   1354  CB  ARG A 170     -11.779  33.004  -6.468  1.00 58.69           C  
ANISOU 1354  CB  ARG A 170     9676   4391   8229    451    374   -847       C  
ATOM   1355  CG  ARG A 170     -12.410  33.838  -7.533  1.00 63.66           C  
ANISOU 1355  CG  ARG A 170    10255   4995   8935    518    289   -768       C  
ATOM   1356  CD  ARG A 170     -12.209  33.262  -8.912  1.00 66.63           C  
ANISOU 1356  CD  ARG A 170    10635   5479   9201    502    168   -713       C  
ATOM   1357  NE  ARG A 170     -10.795  33.164  -9.199  1.00 68.01           N  
ANISOU 1357  NE  ARG A 170    10913   5682   9243    449    193   -699       N  
ATOM   1358  CZ  ARG A 170     -10.327  32.783 -10.366  1.00 73.84           C  
ANISOU 1358  CZ  ARG A 170    11694   6504   9856    420    145   -668       C  
ATOM   1359  NH1 ARG A 170     -11.164  32.439 -11.358  1.00 76.24           N  
ANISOU 1359  NH1 ARG A 170    11966   6894  10106    421     37   -657       N  
ATOM   1360  NH2 ARG A 170      -9.017  32.737 -10.529  1.00 77.61           N  
ANISOU 1360  NH2 ARG A 170    12242   6983  10260    377    208   -656       N  
ATOM   1361  N   SER A 171     -12.147  35.966  -4.838  1.00 60.75           N  
ANISOU 1361  N   SER A 171    10008   4370   8703    493    580   -938       N  
ATOM   1362  CA  SER A 171     -12.979  36.913  -4.042  1.00 60.04           C  
ANISOU 1362  CA  SER A 171     9898   4134   8780    529    730  -1028       C  
ATOM   1363  C   SER A 171     -14.439  36.753  -4.374  1.00 57.13           C  
ANISOU 1363  C   SER A 171     9366   3729   8612    628    746   -993       C  
ATOM   1364  O   SER A 171     -14.795  36.460  -5.485  1.00 54.15           O  
ANISOU 1364  O   SER A 171     8893   3404   8275    680    599   -872       O  
ATOM   1365  CB  SER A 171     -12.620  38.323  -4.405  1.00 62.67           C  
ANISOU 1365  CB  SER A 171    10253   4318   9239    557    739   -996       C  
ATOM   1366  OG  SER A 171     -12.871  38.472  -5.798  1.00 66.61           O  
ANISOU 1366  OG  SER A 171    10664   4826   9818    640    599   -816       O  
ATOM   1367  N   PRO A 172     -15.292  37.007  -3.406  1.00 57.25           N  
ANISOU 1367  N   PRO A 172     9344   3650   8758    646    932  -1104       N  
ATOM   1368  CA  PRO A 172     -16.721  36.936  -3.674  1.00 57.38           C  
ANISOU 1368  CA  PRO A 172     9161   3604   9034    745    963  -1064       C  
ATOM   1369  C   PRO A 172     -17.252  38.035  -4.624  1.00 58.03           C  
ANISOU 1369  C   PRO A 172     9107   3549   9392    864    885   -928       C  
ATOM   1370  O   PRO A 172     -18.294  37.778  -5.254  1.00 57.51           O  
ANISOU 1370  O   PRO A 172     8845   3488   9515    941    792   -825       O  
ATOM   1371  CB  PRO A 172     -17.332  37.080  -2.311  1.00 58.62           C  
ANISOU 1371  CB  PRO A 172     9335   3673   9264    725   1237  -1231       C  
ATOM   1372  CG  PRO A 172     -16.348  37.900  -1.562  1.00 60.01           C  
ANISOU 1372  CG  PRO A 172     9710   3793   9296    644   1337  -1355       C  
ATOM   1373  CD  PRO A 172     -14.991  37.622  -2.107  1.00 57.99           C  
ANISOU 1373  CD  PRO A 172     9570   3663   8798    575   1130  -1275       C  
ATOM   1374  N   GLU A 173     -16.571  39.201  -4.737  1.00 57.41           N  
ANISOU 1374  N   GLU A 173     9112   3347   9355    874    906   -911       N  
ATOM   1375  CA  GLU A 173     -16.886  40.162  -5.836  1.00 59.37           C  
ANISOU 1375  CA  GLU A 173     9241   3482   9836    984    786   -708       C  
ATOM   1376  C   GLU A 173     -16.935  39.448  -7.166  1.00 59.18           C  
ANISOU 1376  C   GLU A 173     9159   3646   9681    994    510   -516       C  
ATOM   1377  O   GLU A 173     -17.916  39.529  -7.912  1.00 61.06           O  
ANISOU 1377  O   GLU A 173     9212   3877  10109   1080    378   -360       O  
ATOM   1378  CB  GLU A 173     -15.816  41.228  -6.065  1.00 59.03           C  
ANISOU 1378  CB  GLU A 173     9323   3331   9773    961    790   -668       C  
ATOM   1379  CG  GLU A 173     -15.446  41.984  -4.883  1.00 60.11           C  
ANISOU 1379  CG  GLU A 173     9567   3298   9971    907   1027   -880       C  
ATOM   1380  CD  GLU A 173     -14.091  41.661  -4.342  1.00 58.85           C  
ANISOU 1380  CD  GLU A 173     9616   3254   9489    754   1022  -1008       C  
ATOM   1381  OE1 GLU A 173     -13.106  41.989  -5.016  1.00 58.73           O  
ANISOU 1381  OE1 GLU A 173     9664   3254   9394    720    909   -902       O  
ATOM   1382  OE2 GLU A 173     -14.027  41.138  -3.191  1.00 58.85           O  
ANISOU 1382  OE2 GLU A 173     9708   3318   9332    663   1142  -1205       O  
ATOM   1383  N   VAL A 174     -15.835  38.750  -7.459  1.00 57.30           N  
ANISOU 1383  N   VAL A 174     9078   3576   9116    894    422   -534       N  
ATOM   1384  CA  VAL A 174     -15.652  38.096  -8.747  1.00 57.25           C  
ANISOU 1384  CA  VAL A 174     9073   3751   8927    873    196   -396       C  
ATOM   1385  C   VAL A 174     -16.677  36.949  -8.912  1.00 55.53           C  
ANISOU 1385  C   VAL A 174     8721   3652   8724    870    107   -425       C  
ATOM   1386  O   VAL A 174     -17.353  36.860  -9.931  1.00 56.66           O  
ANISOU 1386  O   VAL A 174     8752   3870   8906    901    -87   -287       O  
ATOM   1387  CB  VAL A 174     -14.245  37.539  -8.880  1.00 56.39           C  
ANISOU 1387  CB  VAL A 174     9145   3762   8516    768    187   -446       C  
ATOM   1388  CG1 VAL A 174     -14.108  36.742 -10.158  1.00 56.60           C  
ANISOU 1388  CG1 VAL A 174     9188   3975   8341    732      6   -357       C  
ATOM   1389  CG2 VAL A 174     -13.233  38.676  -8.874  1.00 57.32           C  
ANISOU 1389  CG2 VAL A 174     9368   3766   8645    758    248   -397       C  
ATOM   1390  N   LEU A 175     -16.839  36.166  -7.862  1.00 52.95           N  
ANISOU 1390  N   LEU A 175     8397   3331   8387    827    250   -593       N  
ATOM   1391  CA  LEU A 175     -17.771  35.068  -7.864  1.00 52.95           C  
ANISOU 1391  CA  LEU A 175     8266   3410   8442    810    208   -636       C  
ATOM   1392  C   LEU A 175     -19.217  35.481  -8.080  1.00 55.31           C  
ANISOU 1392  C   LEU A 175     8320   3626   9068    904    161   -552       C  
ATOM   1393  O   LEU A 175     -19.911  34.926  -8.924  1.00 56.21           O  
ANISOU 1393  O   LEU A 175     8299   3839   9217    896    -36   -481       O  
ATOM   1394  CB  LEU A 175     -17.610  34.241  -6.578  1.00 51.76           C  
ANISOU 1394  CB  LEU A 175     8177   3261   8229    746    405   -800       C  
ATOM   1395  CG  LEU A 175     -16.232  33.573  -6.340  1.00 49.00           C  
ANISOU 1395  CG  LEU A 175     8021   3005   7591    650    420   -856       C  
ATOM   1396  CD1 LEU A 175     -16.131  33.031  -4.928  1.00 48.49           C  
ANISOU 1396  CD1 LEU A 175     8015   2926   7481    596    609   -966       C  
ATOM   1397  CD2 LEU A 175     -15.943  32.519  -7.366  1.00 47.65           C  
ANISOU 1397  CD2 LEU A 175     7852   2968   7282    598    261   -832       C  
ATOM   1398  N   LEU A 176     -19.628  36.565  -7.440  1.00 57.92           N  
ANISOU 1398  N   LEU A 176     8584   3766   9655    992    323   -548       N  
ATOM   1399  CA  LEU A 176     -21.011  37.089  -7.645  1.00 60.01           C  
ANISOU 1399  CA  LEU A 176     8572   3911  10318   1105    295   -439       C  
ATOM   1400  C   LEU A 176     -21.269  37.870  -8.956  1.00 61.18           C  
ANISOU 1400  C   LEU A 176     8608   4059  10575   1183     28   -178       C  
ATOM   1401  O   LEU A 176     -22.360  38.359  -9.176  1.00 63.53           O  
ANISOU 1401  O   LEU A 176     8654   4252  11232   1285    -26    -46       O  
ATOM   1402  CB  LEU A 176     -21.461  37.881  -6.414  1.00 60.98           C  
ANISOU 1402  CB  LEU A 176     8643   3800  10725   1173    621   -555       C  
ATOM   1403  CG  LEU A 176     -21.782  36.905  -5.269  1.00 60.46           C  
ANISOU 1403  CG  LEU A 176     8594   3767  10611   1102    843   -753       C  
ATOM   1404  CD1 LEU A 176     -21.743  37.622  -3.933  1.00 61.19           C  
ANISOU 1404  CD1 LEU A 176     8776   3682  10790   1110   1201   -929       C  
ATOM   1405  CD2 LEU A 176     -23.126  36.227  -5.471  1.00 61.62           C  
ANISOU 1405  CD2 LEU A 176     8455   3924  11032   1135    793   -705       C  
ATOM   1406  N   GLY A 177     -20.269  37.980  -9.821  1.00 60.40           N  
ANISOU 1406  N   GLY A 177     8690   4080  10177   1133   -132    -85       N  
ATOM   1407  CA  GLY A 177     -20.436  38.608 -11.141  1.00 63.01           C  
ANISOU 1407  CA  GLY A 177     8955   4461  10524   1181   -404    191       C  
ATOM   1408  C   GLY A 177     -20.371  40.137 -11.129  1.00 64.01           C  
ANISOU 1408  C   GLY A 177     9044   4355  10920   1301   -327    359       C  
ATOM   1409  O   GLY A 177     -20.935  40.833 -11.974  1.00 65.85           O  
ANISOU 1409  O   GLY A 177     9126   4551  11341   1387   -517    634       O  
ATOM   1410  N   SER A 178     -19.610  40.640 -10.183  1.00 62.42           N  
ANISOU 1410  N   SER A 178     8990   3999  10725   1292    -56    196       N  
ATOM   1411  CA  SER A 178     -19.440  42.088 -10.027  1.00 63.78           C  
ANISOU 1411  CA  SER A 178     9147   3908  11176   1385     71    296       C  
ATOM   1412  C   SER A 178     -18.902  42.805 -11.279  1.00 63.64           C  
ANISOU 1412  C   SER A 178     9185   3920  11074   1405   -133    598       C  
ATOM   1413  O   SER A 178     -17.965  42.355 -11.902  1.00 62.60           O  
ANISOU 1413  O   SER A 178     9243   3983  10557   1304   -242    619       O  
ATOM   1414  CB  SER A 178     -18.510  42.308  -8.838  1.00 62.20           C  
ANISOU 1414  CB  SER A 178     9148   3597  10886   1313    362     22       C  
ATOM   1415  OG  SER A 178     -18.174  43.619  -8.731  1.00 62.90           O  
ANISOU 1415  OG  SER A 178     9257   3439  11203   1367    485     78       O  
ATOM   1416  N   ALA A 179     -19.520  43.911 -11.622  1.00 66.46           N  
ANISOU 1416  N   ALA A 179     9366   4069  11815   1538   -163    840       N  
ATOM   1417  CA  ALA A 179     -19.194  44.711 -12.813  1.00 68.03           C  
ANISOU 1417  CA  ALA A 179     9583   4267  11995   1576   -358   1197       C  
ATOM   1418  C   ALA A 179     -17.715  45.100 -12.940  1.00 66.21           C  
ANISOU 1418  C   ALA A 179     9623   4032  11500   1485   -260   1171       C  
ATOM   1419  O   ALA A 179     -17.141  44.986 -14.025  1.00 65.00           O  
ANISOU 1419  O   ALA A 179     9591   4068  11038   1428   -445   1373       O  
ATOM   1420  CB  ALA A 179     -20.046  45.965 -12.821  1.00 71.51           C  
ANISOU 1420  CB  ALA A 179     9775   4391  13004   1751   -317   1434       C  
ATOM   1421  N   ARG A 180     -17.122  45.562 -11.835  1.00 65.81           N  
ANISOU 1421  N   ARG A 180     9663   3769  11572   1461     33    919       N  
ATOM   1422  CA  ARG A 180     -15.704  45.840 -11.793  1.00 65.66           C  
ANISOU 1422  CA  ARG A 180     9872   3742  11333   1355    132    848       C  
ATOM   1423  C   ARG A 180     -15.020  45.327 -10.563  1.00 62.22           C  
ANISOU 1423  C   ARG A 180     9577   3317  10743   1241    336    465       C  
ATOM   1424  O   ARG A 180     -15.655  45.121  -9.563  1.00 61.39           O  
ANISOU 1424  O   ARG A 180     9406   3136  10782   1260    477    248       O  
ATOM   1425  CB  ARG A 180     -15.461  47.354 -11.905  1.00 70.40           C  
ANISOU 1425  CB  ARG A 180    10439   4016  12293   1427    246   1025       C  
ATOM   1426  CG  ARG A 180     -16.002  47.957 -13.213  1.00 75.87           C  
ANISOU 1426  CG  ARG A 180    11004   4699  13124   1537     22   1486       C  
ATOM   1427  CD  ARG A 180     -15.142  49.123 -13.674  1.00 80.05           C  
ANISOU 1427  CD  ARG A 180    11613   5026  13776   1536     96   1703       C  
ATOM   1428  NE  ARG A 180     -15.775  50.266 -14.351  1.00 87.07           N  
ANISOU 1428  NE  ARG A 180    12325   5679  15077   1685     26   2113       N  
ATOM   1429  CZ  ARG A 180     -16.046  51.460 -13.792  1.00 91.74           C  
ANISOU 1429  CZ  ARG A 180    12786   5846  16225   1788    240   2128       C  
ATOM   1430  NH1 ARG A 180     -15.837  51.687 -12.488  1.00 91.70           N  
ANISOU 1430  NH1 ARG A 180    12814   5613  16413   1750    543   1715       N  
ATOM   1431  NH2 ARG A 180     -16.581  52.443 -14.544  1.00 97.07           N  
ANISOU 1431  NH2 ARG A 180    13288   6314  17279   1931    149   2566       N  
ATOM   1432  N   TYR A 181     -13.709  45.110 -10.650  1.00 60.13           N  
ANISOU 1432  N   TYR A 181     9504   3157  10185   1118    349    401       N  
ATOM   1433  CA  TYR A 181     -12.918  44.652  -9.499  1.00 58.16           C  
ANISOU 1433  CA  TYR A 181     9387   2933   9777    996    501     76       C  
ATOM   1434  C   TYR A 181     -11.623  45.461  -9.473  1.00 56.69           C  
ANISOU 1434  C   TYR A 181     9322   2623   9592    911    586     73       C  
ATOM   1435  O   TYR A 181     -11.213  45.963 -10.483  1.00 56.72           O  
ANISOU 1435  O   TYR A 181     9338   2610   9601    928    512    320       O  
ATOM   1436  CB  TYR A 181     -12.587  43.097  -9.611  1.00 57.18           C  
ANISOU 1436  CB  TYR A 181     9340   3127   9258    908    389    -16       C  
ATOM   1437  CG  TYR A 181     -11.733  42.717 -10.862  1.00 58.31           C  
ANISOU 1437  CG  TYR A 181     9573   3458   9122    856    245    164       C  
ATOM   1438  CD1 TYR A 181     -10.343  42.794 -10.817  1.00 58.17           C  
ANISOU 1438  CD1 TYR A 181     9684   3451   8967    753    310    118       C  
ATOM   1439  CD2 TYR A 181     -12.320  42.353 -12.073  1.00 60.68           C  
ANISOU 1439  CD2 TYR A 181     9827   3916   9311    900     56    375       C  
ATOM   1440  CE1 TYR A 181      -9.563  42.562 -11.917  1.00 59.52           C  
ANISOU 1440  CE1 TYR A 181     9932   3758   8924    708    241    273       C  
ATOM   1441  CE2 TYR A 181     -11.537  42.102 -13.216  1.00 62.06           C  
ANISOU 1441  CE2 TYR A 181    10114   4256   9210    839    -31    522       C  
ATOM   1442  CZ  TYR A 181     -10.142  42.261 -13.134  1.00 62.21           C  
ANISOU 1442  CZ  TYR A 181    10257   4251   9126    750     87    474       C  
ATOM   1443  OH  TYR A 181      -9.241  42.030 -14.194  1.00 66.24           O  
ANISOU 1443  OH  TYR A 181    10882   4904   9382    682     67    597       O  
ATOM   1444  N   SER A 182     -10.918  45.424  -8.356  1.00 54.59           N  
ANISOU 1444  N   SER A 182     9154   2316   9269    797    718   -200       N  
ATOM   1445  CA  SER A 182      -9.648  46.121  -8.220  1.00 54.63           C  
ANISOU 1445  CA  SER A 182     9255   2211   9289    689    785   -238       C  
ATOM   1446  C   SER A 182      -8.762  45.480  -7.166  1.00 52.43           C  
ANISOU 1446  C   SER A 182     9087   2049   8785    533    818   -509       C  
ATOM   1447  O   SER A 182      -8.963  44.299  -6.847  1.00 52.23           O  
ANISOU 1447  O   SER A 182     9076   2239   8527    516    758   -593       O  
ATOM   1448  CB  SER A 182      -9.923  47.603  -7.814  1.00 58.04           C  
ANISOU 1448  CB  SER A 182     9641   2279  10131    726    955   -273       C  
ATOM   1449  OG  SER A 182      -8.811  48.448  -8.166  1.00 58.63           O  
ANISOU 1449  OG  SER A 182     9767   2213  10294    648    987   -191       O  
ATOM   1450  N   THR A 183      -7.851  46.249  -6.562  1.00 52.24           N  
ANISOU 1450  N   THR A 183     9127   1874   8847    415    905   -644       N  
ATOM   1451  CA  THR A 183      -6.877  45.695  -5.644  1.00 50.66           C  
ANISOU 1451  CA  THR A 183     9017   1801   8427    250    884   -853       C  
ATOM   1452  C   THR A 183      -7.464  44.831  -4.526  1.00 50.06           C  
ANISOU 1452  C   THR A 183     8984   1865   8171    221    904  -1068       C  
ATOM   1453  O   THR A 183      -6.789  43.897  -4.019  1.00 48.41           O  
ANISOU 1453  O   THR A 183     8828   1858   7705    118    820  -1141       O  
ATOM   1454  CB  THR A 183      -5.997  46.764  -4.961  1.00 51.99           C  
ANISOU 1454  CB  THR A 183     9241   1767   8746    104    969  -1019       C  
ATOM   1455  OG1 THR A 183      -6.805  47.592  -4.156  1.00 53.32           O  
ANISOU 1455  OG1 THR A 183     9424   1710   9123    116   1135  -1219       O  
ATOM   1456  CG2 THR A 183      -5.172  47.511  -5.951  1.00 52.52           C  
ANISOU 1456  CG2 THR A 183     9270   1708   8976     95    959   -811       C  
ATOM   1457  N   PRO A 184      -8.701  45.108  -4.112  1.00 51.65           N  
ANISOU 1457  N   PRO A 184     9150   1954   8518    309   1026  -1154       N  
ATOM   1458  CA  PRO A 184      -9.198  44.174  -3.069  1.00 51.54           C  
ANISOU 1458  CA  PRO A 184     9185   2097   8297    268   1062  -1336       C  
ATOM   1459  C   PRO A 184      -9.222  42.663  -3.375  1.00 49.03           C  
ANISOU 1459  C   PRO A 184     8845   2061   7721    288    919  -1229       C  
ATOM   1460  O   PRO A 184      -9.138  41.864  -2.450  1.00 47.57           O  
ANISOU 1460  O   PRO A 184     8728   2020   7327    205    923  -1355       O  
ATOM   1461  CB  PRO A 184     -10.612  44.691  -2.790  1.00 53.21           C  
ANISOU 1461  CB  PRO A 184     9322   2129   8763    386   1241  -1405       C  
ATOM   1462  CG  PRO A 184     -10.515  46.138  -3.118  1.00 54.99           C  
ANISOU 1462  CG  PRO A 184     9514   2053   9324    418   1338  -1382       C  
ATOM   1463  CD  PRO A 184      -9.645  46.197  -4.337  1.00 53.72           C  
ANISOU 1463  CD  PRO A 184     9327   1942   9139    431   1161  -1117       C  
ATOM   1464  N   VAL A 185      -9.261  42.284  -4.637  1.00 48.86           N  
ANISOU 1464  N   VAL A 185     8746   2114   7705    380    798  -1001       N  
ATOM   1465  CA  VAL A 185      -9.204  40.859  -4.945  1.00 47.79           C  
ANISOU 1465  CA  VAL A 185     8596   2215   7348    381    684   -936       C  
ATOM   1466  C   VAL A 185      -7.903  40.203  -4.494  1.00 47.42           C  
ANISOU 1466  C   VAL A 185     8622   2301   7093    250    619   -982       C  
ATOM   1467  O   VAL A 185      -7.948  39.107  -3.943  1.00 47.27           O  
ANISOU 1467  O   VAL A 185     8615   2428   6916    216    592  -1028       O  
ATOM   1468  CB  VAL A 185      -9.384  40.538  -6.414  1.00 47.69           C  
ANISOU 1468  CB  VAL A 185     8512   2275   7330    471    568   -718       C  
ATOM   1469  CG1 VAL A 185     -10.696  41.114  -6.921  1.00 49.54           C  
ANISOU 1469  CG1 VAL A 185     8641   2401   7779    603    577   -622       C  
ATOM   1470  CG2 VAL A 185      -8.201  40.935  -7.278  1.00 47.89           C  
ANISOU 1470  CG2 VAL A 185     8576   2296   7323    430    517   -587       C  
ATOM   1471  N   ASP A 186      -6.765  40.880  -4.696  1.00 48.21           N  
ANISOU 1471  N   ASP A 186     8751   2335   7229    175    596   -954       N  
ATOM   1472  CA  ASP A 186      -5.497  40.348  -4.260  1.00 47.73           C  
ANISOU 1472  CA  ASP A 186     8720   2382   7031     50    520   -979       C  
ATOM   1473  C   ASP A 186      -5.402  40.202  -2.740  1.00 49.44           C  
ANISOU 1473  C   ASP A 186     9013   2645   7125    -70    528  -1166       C  
ATOM   1474  O   ASP A 186      -4.767  39.284  -2.239  1.00 49.39           O  
ANISOU 1474  O   ASP A 186     9012   2791   6963   -144    438  -1155       O  
ATOM   1475  CB  ASP A 186      -4.378  41.185  -4.808  1.00 48.22           C  
ANISOU 1475  CB  ASP A 186     8770   2345   7206     -7    506   -907       C  
ATOM   1476  CG  ASP A 186      -4.239  41.040  -6.277  1.00 49.04           C  
ANISOU 1476  CG  ASP A 186     8824   2471   7337     79    494   -701       C  
ATOM   1477  OD1 ASP A 186      -4.767  40.069  -6.892  1.00 51.77           O  
ANISOU 1477  OD1 ASP A 186     9148   2949   7574    159    461   -628       O  
ATOM   1478  OD2 ASP A 186      -3.459  41.758  -6.900  1.00 50.34           O  
ANISOU 1478  OD2 ASP A 186     8975   2544   7606     50    515   -605       O  
ATOM   1479  N   ILE A 187      -6.036  41.094  -1.997  1.00 52.50           N  
ANISOU 1479  N   ILE A 187     9464   2902   7582    -93    644  -1333       N  
ATOM   1480  CA  ILE A 187      -6.030  41.010  -0.536  1.00 54.64           C  
ANISOU 1480  CA  ILE A 187     9845   3233   7681   -228    674  -1534       C  
ATOM   1481  C   ILE A 187      -6.890  39.815  -0.034  1.00 54.35           C  
ANISOU 1481  C   ILE A 187     9818   3355   7478   -183    701  -1529       C  
ATOM   1482  O   ILE A 187      -6.578  39.181   0.941  1.00 53.51           O  
ANISOU 1482  O   ILE A 187     9785   3394   7151   -293    654  -1578       O  
ATOM   1483  CB  ILE A 187      -6.554  42.327   0.058  1.00 57.52           C  
ANISOU 1483  CB  ILE A 187    10284   3386   8184   -265    847  -1750       C  
ATOM   1484  CG1 ILE A 187      -5.720  43.542  -0.447  1.00 59.79           C  
ANISOU 1484  CG1 ILE A 187    10552   3479   8685   -315    837  -1749       C  
ATOM   1485  CG2 ILE A 187      -6.516  42.322   1.573  1.00 59.59           C  
ANISOU 1485  CG2 ILE A 187    10700   3723   8217   -437    898  -1993       C  
ATOM   1486  CD1 ILE A 187      -4.201  43.407  -0.445  1.00 59.67           C  
ANISOU 1486  CD1 ILE A 187    10529   3555   8587   -462    659  -1698       C  
ATOM   1487  N   TRP A 188      -8.016  39.579  -0.699  1.00 54.44           N  
ANISOU 1487  N   TRP A 188     9746   3324   7613    -27    776  -1458       N  
ATOM   1488  CA  TRP A 188      -8.860  38.465  -0.399  1.00 52.65           C  
ANISOU 1488  CA  TRP A 188     9495   3217   7292     20    809  -1435       C  
ATOM   1489  C   TRP A 188      -8.050  37.198  -0.568  1.00 50.97           C  
ANISOU 1489  C   TRP A 188     9257   3183   6925    -14    654  -1298       C  
ATOM   1490  O   TRP A 188      -8.007  36.351   0.341  1.00 51.18           O  
ANISOU 1490  O   TRP A 188     9331   3336   6776    -84    645  -1309       O  
ATOM   1491  CB  TRP A 188     -10.036  38.421  -1.321  1.00 52.69           C  
ANISOU 1491  CB  TRP A 188     9374   3150   7494    182    857  -1352       C  
ATOM   1492  CG  TRP A 188     -10.840  37.323  -0.986  1.00 54.13           C  
ANISOU 1492  CG  TRP A 188     9519   3437   7611    210    895  -1343       C  
ATOM   1493  CD1 TRP A 188     -10.627  36.042  -1.354  1.00 54.40           C  
ANISOU 1493  CD1 TRP A 188     9506   3612   7549    216    788  -1228       C  
ATOM   1494  CD2 TRP A 188     -11.987  37.313  -0.140  1.00 55.90           C  
ANISOU 1494  CD2 TRP A 188     9743   3621   7875    226   1081  -1459       C  
ATOM   1495  NE1 TRP A 188     -11.585  35.232  -0.820  1.00 54.96           N  
ANISOU 1495  NE1 TRP A 188     9543   3729   7608    234    878  -1252       N  
ATOM   1496  CE2 TRP A 188     -12.438  35.989  -0.070  1.00 55.67           C  
ANISOU 1496  CE2 TRP A 188     9659   3718   7775    240   1062  -1386       C  
ATOM   1497  CE3 TRP A 188     -12.684  38.289   0.542  1.00 58.31           C  
ANISOU 1497  CE3 TRP A 188    10080   3776   8299    229   1288  -1623       C  
ATOM   1498  CZ2 TRP A 188     -13.560  35.609   0.659  1.00 56.84           C  
ANISOU 1498  CZ2 TRP A 188     9778   3859   7957    254   1239  -1453       C  
ATOM   1499  CZ3 TRP A 188     -13.802  37.921   1.282  1.00 60.34           C  
ANISOU 1499  CZ3 TRP A 188    10315   4028   8584    247   1483  -1707       C  
ATOM   1500  CH2 TRP A 188     -14.231  36.581   1.324  1.00 59.95           C  
ANISOU 1500  CH2 TRP A 188    10204   4120   8453    259   1453  -1610       C  
ATOM   1501  N   SER A 189      -7.422  37.056  -1.724  1.00 48.04           N  
ANISOU 1501  N   SER A 189     8809   2814   6629     34    552  -1160       N  
ATOM   1502  CA  SER A 189      -6.631  35.890  -1.983  1.00 46.27           C  
ANISOU 1502  CA  SER A 189     8540   2718   6322     14    443  -1042       C  
ATOM   1503  C   SER A 189      -5.607  35.738  -0.904  1.00 48.07           C  
ANISOU 1503  C   SER A 189     8824   3025   6413   -126    363  -1062       C  
ATOM   1504  O   SER A 189      -5.441  34.653  -0.341  1.00 47.87           O  
ANISOU 1504  O   SER A 189     8790   3116   6281   -158    314   -997       O  
ATOM   1505  CB  SER A 189      -5.979  35.991  -3.330  1.00 45.15           C  
ANISOU 1505  CB  SER A 189     8332   2547   6274     63    389   -927       C  
ATOM   1506  OG  SER A 189      -6.980  36.213  -4.307  1.00 45.14           O  
ANISOU 1506  OG  SER A 189     8292   2495   6361    177    429   -894       O  
ATOM   1507  N   ILE A 190      -4.966  36.837  -0.527  1.00 50.86           N  
ANISOU 1507  N   ILE A 190     9235   3312   6774   -222    343  -1148       N  
ATOM   1508  CA  ILE A 190      -3.909  36.769   0.500  1.00 53.19           C  
ANISOU 1508  CA  ILE A 190     9578   3703   6929   -387    218  -1167       C  
ATOM   1509  C   ILE A 190      -4.454  36.385   1.865  1.00 54.86           C  
ANISOU 1509  C   ILE A 190     9906   4025   6910   -472    243  -1254       C  
ATOM   1510  O   ILE A 190      -3.790  35.665   2.630  1.00 58.72           O  
ANISOU 1510  O   ILE A 190    10407   4662   7238   -572    108  -1170       O  
ATOM   1511  CB  ILE A 190      -3.121  38.058   0.660  1.00 55.02           C  
ANISOU 1511  CB  ILE A 190     9846   3835   7223   -503    183  -1272       C  
ATOM   1512  CG1 ILE A 190      -2.280  38.331  -0.584  1.00 55.20           C  
ANISOU 1512  CG1 ILE A 190     9747   3772   7453   -452    146  -1143       C  
ATOM   1513  CG2 ILE A 190      -2.156  37.920   1.818  1.00 57.09           C  
ANISOU 1513  CG2 ILE A 190    10154   4226   7309   -695     17  -1300       C  
ATOM   1514  CD1 ILE A 190      -1.737  39.752  -0.693  1.00 56.68           C  
ANISOU 1514  CD1 ILE A 190     9952   3798   7784   -536    165  -1236       C  
ATOM   1515  N   GLY A 191      -5.682  36.764   2.146  1.00 54.34           N  
ANISOU 1515  N   GLY A 191     9914   3896   6835   -426    422  -1390       N  
ATOM   1516  CA  GLY A 191      -6.313  36.330   3.384  1.00 54.88           C  
ANISOU 1516  CA  GLY A 191    10102   4072   6676   -500    500  -1466       C  
ATOM   1517  C   GLY A 191      -6.497  34.825   3.402  1.00 52.12           C  
ANISOU 1517  C   GLY A 191     9685   3852   6266   -445    455  -1275       C  
ATOM   1518  O   GLY A 191      -6.185  34.145   4.429  1.00 52.81           O  
ANISOU 1518  O   GLY A 191     9846   4096   6124   -555    384  -1210       O  
ATOM   1519  N   THR A 192      -6.943  34.295   2.272  1.00 49.44           N  
ANISOU 1519  N   THR A 192     9207   3449   6127   -289    483  -1174       N  
ATOM   1520  CA  THR A 192      -7.252  32.822   2.165  1.00 47.96           C  
ANISOU 1520  CA  THR A 192     8937   3338   5944   -228    473  -1017       C  
ATOM   1521  C   THR A 192      -5.950  32.062   2.272  1.00 48.47           C  
ANISOU 1521  C   THR A 192     8952   3495   5969   -287    289   -845       C  
ATOM   1522  O   THR A 192      -5.874  31.008   2.944  1.00 49.74           O  
ANISOU 1522  O   THR A 192     9108   3753   6038   -321    252   -712       O  
ATOM   1523  CB  THR A 192      -8.018  32.463   0.900  1.00 45.27           C  
ANISOU 1523  CB  THR A 192     8469   2911   5818    -77    531   -986       C  
ATOM   1524  OG1 THR A 192      -7.418  33.087  -0.242  1.00 45.15           O  
ANISOU 1524  OG1 THR A 192     8400   2824   5931    -30    462   -973       O  
ATOM   1525  CG2 THR A 192      -9.484  32.907   0.979  1.00 45.29           C  
ANISOU 1525  CG2 THR A 192     8476   2838   5893    -12    705  -1105       C  
ATOM   1526  N   ILE A 193      -4.904  32.642   1.708  1.00 48.76           N  
ANISOU 1526  N   ILE A 193     8942   3493   6089   -308    180   -833       N  
ATOM   1527  CA  ILE A 193      -3.594  32.019   1.774  1.00 50.23           C  
ANISOU 1527  CA  ILE A 193     9040   3744   6301   -360      9   -665       C  
ATOM   1528  C   ILE A 193      -3.066  32.048   3.187  1.00 53.28           C  
ANISOU 1528  C   ILE A 193     9518   4268   6457   -524   -123   -635       C  
ATOM   1529  O   ILE A 193      -2.381  31.112   3.620  1.00 55.58           O  
ANISOU 1529  O   ILE A 193     9736   4649   6729   -559   -260   -437       O  
ATOM   1530  CB  ILE A 193      -2.597  32.674   0.802  1.00 49.67           C  
ANISOU 1530  CB  ILE A 193     8880   3588   6403   -349    -47   -658       C  
ATOM   1531  CG1 ILE A 193      -3.088  32.456  -0.628  1.00 48.05           C  
ANISOU 1531  CG1 ILE A 193     8600   3286   6368   -201     69   -655       C  
ATOM   1532  CG2 ILE A 193      -1.230  32.006   0.851  1.00 50.42           C  
ANISOU 1532  CG2 ILE A 193     8839   3729   6589   -393   -204   -477       C  
ATOM   1533  CD1 ILE A 193      -2.530  33.426  -1.602  1.00 48.22           C  
ANISOU 1533  CD1 ILE A 193     8594   3215   6511   -186     82   -683       C  
ATOM   1534  N   PHE A 194      -3.347  33.124   3.892  1.00 55.20           N  
ANISOU 1534  N   PHE A 194     9917   4523   6532   -630    -88   -826       N  
ATOM   1535  CA  PHE A 194      -2.847  33.306   5.250  1.00 57.97           C  
ANISOU 1535  CA  PHE A 194    10396   5029   6600   -826   -224   -843       C  
ATOM   1536  C   PHE A 194      -3.400  32.186   6.097  1.00 58.60           C  
ANISOU 1536  C   PHE A 194    10532   5244   6487   -837   -201   -705       C  
ATOM   1537  O   PHE A 194      -2.674  31.496   6.799  1.00 59.98           O  
ANISOU 1537  O   PHE A 194    10690   5564   6534   -928   -392   -507       O  
ATOM   1538  CB  PHE A 194      -3.257  34.721   5.731  1.00 60.23           C  
ANISOU 1538  CB  PHE A 194    10859   5262   6764   -931   -115  -1141       C  
ATOM   1539  CG  PHE A 194      -2.836  35.090   7.169  1.00 63.34           C  
ANISOU 1539  CG  PHE A 194    11439   5824   6803  -1174   -235  -1240       C  
ATOM   1540  CD1 PHE A 194      -1.697  34.553   7.781  1.00 64.67           C  
ANISOU 1540  CD1 PHE A 194    11569   6172   6831  -1311   -529  -1050       C  
ATOM   1541  CD2 PHE A 194      -3.589  36.023   7.868  1.00 64.38           C  
ANISOU 1541  CD2 PHE A 194    11778   5926   6757  -1270    -49  -1532       C  
ATOM   1542  CE1 PHE A 194      -1.361  34.899   9.074  1.00 67.93           C  
ANISOU 1542  CE1 PHE A 194    12168   6768   6875  -1554   -665  -1141       C  
ATOM   1543  CE2 PHE A 194      -3.256  36.377   9.148  1.00 67.72           C  
ANISOU 1543  CE2 PHE A 194    12402   6513   6814  -1512   -138  -1663       C  
ATOM   1544  CZ  PHE A 194      -2.139  35.815   9.754  1.00 69.69           C  
ANISOU 1544  CZ  PHE A 194    12631   6975   6870  -1664   -465  -1465       C  
ATOM   1545  N   ALA A 195      -4.685  31.949   5.961  1.00 58.30           N  
ANISOU 1545  N   ALA A 195    10532   5147   6470   -734     28   -776       N  
ATOM   1546  CA  ALA A 195      -5.325  30.905   6.736  1.00 60.51           C  
ANISOU 1546  CA  ALA A 195    10864   5532   6595   -743     96   -645       C  
ATOM   1547  C   ALA A 195      -4.693  29.532   6.523  1.00 61.20           C  
ANISOU 1547  C   ALA A 195    10788   5653   6811   -687    -46   -335       C  
ATOM   1548  O   ALA A 195      -4.580  28.716   7.470  1.00 63.08           O  
ANISOU 1548  O   ALA A 195    11071   6027   6869   -762   -117   -138       O  
ATOM   1549  CB  ALA A 195      -6.810  30.869   6.423  1.00 59.21           C  
ANISOU 1549  CB  ALA A 195    10708   5261   6529   -626    376   -768       C  
ATOM   1550  N   GLU A 196      -4.288  29.296   5.276  1.00 60.20           N  
ANISOU 1550  N   GLU A 196    10477   5396   7000   -558    -73   -289       N  
ATOM   1551  CA  GLU A 196      -3.711  28.033   4.855  1.00 61.97           C  
ANISOU 1551  CA  GLU A 196    10520   5590   7436   -480   -153    -39       C  
ATOM   1552  C   GLU A 196      -2.334  27.862   5.408  1.00 65.76           C  
ANISOU 1552  C   GLU A 196    10934   6167   7882   -580   -410    159       C  
ATOM   1553  O   GLU A 196      -1.947  26.739   5.800  1.00 71.85           O  
ANISOU 1553  O   GLU A 196    11609   6976   8714   -572   -500    429       O  
ATOM   1554  CB  GLU A 196      -3.667  27.970   3.337  1.00 59.97           C  
ANISOU 1554  CB  GLU A 196    10118   5172   7493   -337    -76   -101       C  
ATOM   1555  CG  GLU A 196      -3.415  26.599   2.721  1.00 59.15           C  
ANISOU 1555  CG  GLU A 196     9837   4984   7651   -235    -57     76       C  
ATOM   1556  CD  GLU A 196      -3.873  26.501   1.268  1.00 57.74           C  
ANISOU 1556  CD  GLU A 196     9582   4666   7687   -112     84    -56       C  
ATOM   1557  OE1 GLU A 196      -4.738  27.312   0.829  1.00 59.01           O  
ANISOU 1557  OE1 GLU A 196     9825   4806   7789    -86    177   -247       O  
ATOM   1558  OE2 GLU A 196      -3.345  25.649   0.521  1.00 58.68           O  
ANISOU 1558  OE2 GLU A 196     9558   4695   8041    -45    102     26       O  
ATOM   1559  N   LEU A 197      -1.577  28.941   5.430  1.00 66.57           N  
ANISOU 1559  N   LEU A 197    11066   6298   7929   -673   -535     49       N  
ATOM   1560  CA  LEU A 197      -0.258  28.882   6.011  1.00 70.40           C  
ANISOU 1560  CA  LEU A 197    11471   6889   8387   -792   -813    231       C  
ATOM   1561  C   LEU A 197      -0.312  28.397   7.456  1.00 73.88           C  
ANISOU 1561  C   LEU A 197    12035   7536   8500   -932   -952    399       C  
ATOM   1562  O   LEU A 197       0.600  27.708   7.931  1.00 76.33           O  
ANISOU 1562  O   LEU A 197    12222   7934   8844   -981  -1187    690       O  
ATOM   1563  CB  LEU A 197       0.403  30.252   5.973  1.00 71.57           C  
ANISOU 1563  CB  LEU A 197    11662   7040   8488   -911   -915     40       C  
ATOM   1564  CG  LEU A 197       0.951  30.770   4.650  1.00 70.52           C  
ANISOU 1564  CG  LEU A 197    11377   6734   8683   -816   -859    -35       C  
ATOM   1565  CD1 LEU A 197       1.239  32.256   4.736  1.00 71.52           C  
ANISOU 1565  CD1 LEU A 197    11600   6841   8733   -943   -895   -267       C  
ATOM   1566  CD2 LEU A 197       2.246  30.062   4.282  1.00 72.52           C  
ANISOU 1566  CD2 LEU A 197    11370   6959   9223   -787  -1019    217       C  
ATOM   1567  N   ALA A 198      -1.347  28.809   8.166  1.00 75.87           N  
ANISOU 1567  N   ALA A 198    12525   7867   8432  -1004   -807    225       N  
ATOM   1568  CA  ALA A 198      -1.480  28.437   9.565  1.00 81.12           C  
ANISOU 1568  CA  ALA A 198    13357   8751   8711  -1159   -903    362       C  
ATOM   1569  C   ALA A 198      -1.884  26.973   9.680  1.00 80.61           C  
ANISOU 1569  C   ALA A 198    13204   8675   8748  -1053   -840    667       C  
ATOM   1570  O   ALA A 198      -1.199  26.166  10.332  1.00 83.11           O  
ANISOU 1570  O   ALA A 198    13453   9109   9014  -1110  -1059   1004       O  
ATOM   1571  CB  ALA A 198      -2.511  29.326  10.245  1.00 82.44           C  
ANISOU 1571  CB  ALA A 198    13811   8984   8527  -1265   -699     54       C  
ATOM   1572  N   THR A 199      -2.976  26.642   8.989  1.00 77.56           N  
ANISOU 1572  N   THR A 199    12794   8129   8545   -897   -550    560       N  
ATOM   1573  CA  THR A 199      -3.660  25.357   9.145  1.00 76.81           C  
ANISOU 1573  CA  THR A 199    12649   7996   8538   -813   -417    778       C  
ATOM   1574  C   THR A 199      -3.143  24.215   8.284  1.00 74.59           C  
ANISOU 1574  C   THR A 199    12094   7547   8697   -659   -455   1011       C  
ATOM   1575  O   THR A 199      -3.466  23.059   8.557  1.00 75.89           O  
ANISOU 1575  O   THR A 199    12198   7677   8959   -612   -394   1250       O  
ATOM   1576  CB  THR A 199      -5.172  25.487   8.832  1.00 75.43           C  
ANISOU 1576  CB  THR A 199    12556   7718   8385   -733    -81    544       C  
ATOM   1577  OG1 THR A 199      -5.364  25.869   7.467  1.00 70.82           O  
ANISOU 1577  OG1 THR A 199    11844   6945   8118   -592     12    339       O  
ATOM   1578  CG2 THR A 199      -5.822  26.499   9.756  1.00 77.26           C  
ANISOU 1578  CG2 THR A 199    13054   8082   8217   -874     33    312       C  
ATOM   1579  N   LYS A 200      -2.395  24.543   7.233  1.00 72.50           N  
ANISOU 1579  N   LYS A 200    11671   7162   8713   -582   -518    926       N  
ATOM   1580  CA  LYS A 200      -2.046  23.620   6.135  1.00 71.00           C  
ANISOU 1580  CA  LYS A 200    11236   6768   8971   -423   -462   1028       C  
ATOM   1581  C   LYS A 200      -3.213  23.334   5.184  1.00 70.53           C  
ANISOU 1581  C   LYS A 200    11167   6547   9083   -298   -185    828       C  
ATOM   1582  O   LYS A 200      -2.967  22.924   4.056  1.00 72.40           O  
ANISOU 1582  O   LYS A 200    11248   6621   9640   -188   -116    787       O  
ATOM   1583  CB  LYS A 200      -1.416  22.318   6.598  1.00 71.79           C  
ANISOU 1583  CB  LYS A 200    11174   6847   9255   -400   -576   1417       C  
ATOM   1584  CG  LYS A 200      -0.279  22.484   7.566  1.00 74.96           C  
ANISOU 1584  CG  LYS A 200    11553   7424   9501   -529   -896   1671       C  
ATOM   1585  CD  LYS A 200       0.430  21.175   7.915  1.00 78.39           C  
ANISOU 1585  CD  LYS A 200    11772   7806  10205   -481  -1027   2108       C  
ATOM   1586  CE  LYS A 200      -0.421  20.210   8.757  1.00 80.84           C  
ANISOU 1586  CE  LYS A 200    12171   8152  10391   -491   -937   2339       C  
ATOM   1587  NZ  LYS A 200       0.250  18.914   9.159  1.00 84.30           N  
ANISOU 1587  NZ  LYS A 200    12392   8518  11120   -440  -1067   2817       N  
ATOM   1588  N   LYS A 201      -4.457  23.608   5.582  1.00 70.75           N  
ANISOU 1588  N   LYS A 201    11356   6620   8905   -325    -26    683       N  
ATOM   1589  CA  LYS A 201      -5.631  23.367   4.736  1.00 68.26           C  
ANISOU 1589  CA  LYS A 201    11010   6166   8757   -223    202    503       C  
ATOM   1590  C   LYS A 201      -6.111  24.635   4.021  1.00 61.30           C  
ANISOU 1590  C   LYS A 201    10202   5265   7821   -202    269    192       C  
ATOM   1591  O   LYS A 201      -6.120  25.689   4.593  1.00 58.30           O  
ANISOU 1591  O   LYS A 201     9965   4986   7200   -284    237     81       O  
ATOM   1592  CB  LYS A 201      -6.796  22.870   5.586  1.00 73.23           C  
ANISOU 1592  CB  LYS A 201    11731   6833   9260   -256    361    552       C  
ATOM   1593  CG  LYS A 201      -6.628  21.486   6.178  1.00 79.96           C  
ANISOU 1593  CG  LYS A 201    12501   7659  10219   -257    352    876       C  
ATOM   1594  CD  LYS A 201      -6.751  21.495   7.710  1.00 89.08           C  
ANISOU 1594  CD  LYS A 201    13831   9010  11004   -391    320   1060       C  
ATOM   1595  CE  LYS A 201      -7.971  22.252   8.285  1.00 92.12           C  
ANISOU 1595  CE  LYS A 201    14416   9482  11102   -457    523    840       C  
ATOM   1596  NZ  LYS A 201      -9.126  21.358   8.602  1.00 95.86           N  
ANISOU 1596  NZ  LYS A 201    14874   9887  11660   -438    763    926       N  
ATOM   1597  N   PRO A 202      -6.574  24.489   2.784  1.00 57.37           N  
ANISOU 1597  N   PRO A 202     9608   4635   7553    -99    368     59       N  
ATOM   1598  CA  PRO A 202      -7.354  25.534   2.171  1.00 55.66           C  
ANISOU 1598  CA  PRO A 202     9450   4395   7302    -68    448   -184       C  
ATOM   1599  C   PRO A 202      -8.510  25.924   2.989  1.00 56.39           C  
ANISOU 1599  C   PRO A 202     9654   4534   7235   -105    580   -271       C  
ATOM   1600  O   PRO A 202      -9.128  25.089   3.615  1.00 59.30           O  
ANISOU 1600  O   PRO A 202    10020   4911   7600   -120    676   -175       O  
ATOM   1601  CB  PRO A 202      -7.866  24.883   0.901  1.00 53.83           C  
ANISOU 1601  CB  PRO A 202     9092   4039   7321     28    527   -253       C  
ATOM   1602  CG  PRO A 202      -6.772  23.952   0.551  1.00 54.17           C  
ANISOU 1602  CG  PRO A 202     9021   4026   7534     47    461   -105       C  
ATOM   1603  CD  PRO A 202      -6.403  23.352   1.868  1.00 55.89           C  
ANISOU 1603  CD  PRO A 202     9256   4310   7670    -14    408    122       C  
ATOM   1604  N   LEU A 203      -8.832  27.191   3.000  1.00 56.36           N  
ANISOU 1604  N   LEU A 203     9743   4542   7127   -120    613   -451       N  
ATOM   1605  CA  LEU A 203      -9.844  27.661   3.945  1.00 57.61           C  
ANISOU 1605  CA  LEU A 203    10019   4738   7129   -168    775   -551       C  
ATOM   1606  C   LEU A 203     -11.233  27.407   3.417  1.00 55.77           C  
ANISOU 1606  C   LEU A 203     9688   4406   7094    -79    944   -634       C  
ATOM   1607  O   LEU A 203     -12.142  27.056   4.143  1.00 53.88           O  
ANISOU 1607  O   LEU A 203     9471   4176   6822   -102   1110   -629       O  
ATOM   1608  CB  LEU A 203      -9.635  29.162   4.200  1.00 58.94           C  
ANISOU 1608  CB  LEU A 203    10316   4922   7157   -222    770   -731       C  
ATOM   1609  CG  LEU A 203     -10.676  29.862   5.094  1.00 61.13           C  
ANISOU 1609  CG  LEU A 203    10720   5204   7302   -269    986   -897       C  
ATOM   1610  CD1 LEU A 203     -10.740  29.220   6.463  1.00 64.11           C  
ANISOU 1610  CD1 LEU A 203    11229   5721   7408   -389   1050   -798       C  
ATOM   1611  CD2 LEU A 203     -10.365  31.336   5.230  1.00 62.11           C  
ANISOU 1611  CD2 LEU A 203    10955   5297   7345   -322    987  -1095       C  
ATOM   1612  N   PHE A 204     -11.393  27.781   2.167  1.00 56.05           N  
ANISOU 1612  N   PHE A 204     9624   4354   7318     10    900   -721       N  
ATOM   1613  CA  PHE A 204     -12.648  27.685   1.471  1.00 58.39           C  
ANISOU 1613  CA  PHE A 204     9800   4563   7821     91    997   -802       C  
ATOM   1614  C   PHE A 204     -12.444  26.745   0.292  1.00 59.91           C  
ANISOU 1614  C   PHE A 204     9860   4712   8189    140    897   -750       C  
ATOM   1615  O   PHE A 204     -12.004  27.195  -0.782  1.00 57.83           O  
ANISOU 1615  O   PHE A 204     9572   4430   7969    181    789   -792       O  
ATOM   1616  CB  PHE A 204     -13.069  29.058   0.951  1.00 57.74           C  
ANISOU 1616  CB  PHE A 204     9720   4422   7794    143   1010   -945       C  
ATOM   1617  CG  PHE A 204     -13.330  30.048   2.022  1.00 59.74           C  
ANISOU 1617  CG  PHE A 204    10101   4679   7918     94   1148  -1049       C  
ATOM   1618  CD1 PHE A 204     -14.263  29.800   2.998  1.00 62.02           C  
ANISOU 1618  CD1 PHE A 204    10414   4973   8179     63   1355  -1081       C  
ATOM   1619  CD2 PHE A 204     -12.645  31.273   2.057  1.00 60.68           C  
ANISOU 1619  CD2 PHE A 204    10320   4782   7951     67   1098  -1135       C  
ATOM   1620  CE1 PHE A 204     -14.498  30.741   4.007  1.00 62.74           C  
ANISOU 1620  CE1 PHE A 204    10646   5063   8128      2   1524  -1218       C  
ATOM   1621  CE2 PHE A 204     -12.870  32.203   3.064  1.00 60.41           C  
ANISOU 1621  CE2 PHE A 204    10420   4734   7799      2   1247  -1277       C  
ATOM   1622  CZ  PHE A 204     -13.807  31.934   4.034  1.00 61.78           C  
ANISOU 1622  CZ  PHE A 204    10633   4921   7919    -30   1468  -1329       C  
ATOM   1623  N   HIS A 205     -12.778  25.462   0.500  1.00 63.30           N  
ANISOU 1623  N   HIS A 205    10215   5117   8717    127    955   -665       N  
ATOM   1624  CA  HIS A 205     -12.283  24.366  -0.335  1.00 65.20           C  
ANISOU 1624  CA  HIS A 205    10359   5307   9107    143    885   -611       C  
ATOM   1625  C   HIS A 205     -13.358  23.913  -1.305  1.00 64.85           C  
ANISOU 1625  C   HIS A 205    10180   5189   9267    176    911   -717       C  
ATOM   1626  O   HIS A 205     -13.774  22.785  -1.259  1.00 68.58           O  
ANISOU 1626  O   HIS A 205    10564   5597   9895    156    976   -683       O  
ATOM   1627  CB  HIS A 205     -11.873  23.231   0.580  1.00 69.07           C  
ANISOU 1627  CB  HIS A 205    10846   5792   9604     98    929   -431       C  
ATOM   1628  CG  HIS A 205     -11.089  22.167  -0.113  1.00 75.94           C  
ANISOU 1628  CG  HIS A 205    11623   6580  10648    115    877   -364       C  
ATOM   1629  ND1 HIS A 205     -11.637  20.962  -0.485  1.00 83.36           N  
ANISOU 1629  ND1 HIS A 205    12443   7404  11824    118    958   -364       N  
ATOM   1630  CD2 HIS A 205      -9.797  22.124  -0.506  1.00 76.92           C  
ANISOU 1630  CD2 HIS A 205    11744   6700  10780    126    778   -307       C  
ATOM   1631  CE1 HIS A 205     -10.714  20.224  -1.081  1.00 83.75           C  
ANISOU 1631  CE1 HIS A 205    12431   7372  12016    134    924   -325       C  
ATOM   1632  NE2 HIS A 205      -9.582  20.904  -1.084  1.00 79.19           N  
ANISOU 1632  NE2 HIS A 205    11916   6864  11308    144    820   -279       N  
ATOM   1633  N   GLY A 206     -13.863  24.794  -2.164  1.00 60.66           N  
ANISOU 1633  N   GLY A 206     9626   4666   8753    216    850   -834       N  
ATOM   1634  CA  GLY A 206     -15.103  24.506  -2.891  1.00 57.94           C  
ANISOU 1634  CA  GLY A 206     9143   4280   8591    231    850   -923       C  
ATOM   1635  C   GLY A 206     -14.883  23.653  -4.122  1.00 56.56           C  
ANISOU 1635  C   GLY A 206     8905   4080   8502    211    757   -984       C  
ATOM   1636  O   GLY A 206     -13.831  23.727  -4.704  1.00 53.37           O  
ANISOU 1636  O   GLY A 206     8572   3699   8004    213    689   -984       O  
ATOM   1637  N   ASP A 207     -15.930  22.930  -4.543  1.00 57.57           N  
ANISOU 1637  N   ASP A 207     8897   4161   8815    182    763  -1056       N  
ATOM   1638  CA  ASP A 207     -15.912  22.091  -5.738  1.00 58.01           C  
ANISOU 1638  CA  ASP A 207     8897   4193   8949    134    682  -1167       C  
ATOM   1639  C   ASP A 207     -16.380  22.801  -7.018  1.00 56.95           C  
ANISOU 1639  C   ASP A 207     8744   4143   8750    135    506  -1265       C  
ATOM   1640  O   ASP A 207     -16.171  22.309  -8.134  1.00 57.59           O  
ANISOU 1640  O   ASP A 207     8837   4246   8799     79    421  -1376       O  
ATOM   1641  CB  ASP A 207     -16.744  20.831  -5.529  1.00 61.46           C  
ANISOU 1641  CB  ASP A 207     9193   4525   9632     72    768  -1206       C  
ATOM   1642  CG  ASP A 207     -18.267  21.108  -5.249  1.00 65.69           C  
ANISOU 1642  CG  ASP A 207     9575   5053  10328     70    782  -1223       C  
ATOM   1643  OD1 ASP A 207     -19.003  21.596  -6.144  1.00 67.87           O  
ANISOU 1643  OD1 ASP A 207     9769   5384  10634     66    630  -1308       O  
ATOM   1644  OD2 ASP A 207     -18.763  20.686  -4.166  1.00 67.19           O  
ANISOU 1644  OD2 ASP A 207     9707   5174  10647     62    950  -1141       O  
ATOM   1645  N   SER A 208     -17.000  23.957  -6.852  1.00 55.34           N  
ANISOU 1645  N   SER A 208     8516   3983   8527    193    458  -1219       N  
ATOM   1646  CA  SER A 208     -17.546  24.736  -7.946  1.00 54.40           C  
ANISOU 1646  CA  SER A 208     8356   3941   8370    207    273  -1246       C  
ATOM   1647  C   SER A 208     -17.688  26.175  -7.494  1.00 54.52           C  
ANISOU 1647  C   SER A 208     8393   3962   8361    301    281  -1150       C  
ATOM   1648  O   SER A 208     -17.506  26.511  -6.305  1.00 53.90           O  
ANISOU 1648  O   SER A 208     8358   3830   8289    336    439  -1105       O  
ATOM   1649  CB  SER A 208     -18.890  24.211  -8.298  1.00 55.07           C  
ANISOU 1649  CB  SER A 208     8247   4013   8662    160    198  -1310       C  
ATOM   1650  OG  SER A 208     -19.669  24.192  -7.132  1.00 55.59           O  
ANISOU 1650  OG  SER A 208     8199   3993   8928    193    355  -1262       O  
ATOM   1651  N   GLU A 209     -17.951  27.064  -8.444  1.00 56.06           N  
ANISOU 1651  N   GLU A 209     8570   4217   8511    333    113  -1116       N  
ATOM   1652  CA  GLU A 209     -18.138  28.497  -8.113  1.00 56.41           C  
ANISOU 1652  CA  GLU A 209     8614   4226   8592    430    126  -1021       C  
ATOM   1653  C   GLU A 209     -19.181  28.659  -7.054  1.00 53.83           C  
ANISOU 1653  C   GLU A 209     8146   3801   8503    473    274  -1021       C  
ATOM   1654  O   GLU A 209     -18.972  29.299  -6.073  1.00 51.34           O  
ANISOU 1654  O   GLU A 209     7895   3421   8189    515    437  -1011       O  
ATOM   1655  CB  GLU A 209     -18.611  29.280  -9.315  1.00 61.31           C  
ANISOU 1655  CB  GLU A 209     9173   4909   9213    461    -92   -943       C  
ATOM   1656  CG  GLU A 209     -17.546  29.908 -10.185  1.00 63.82           C  
ANISOU 1656  CG  GLU A 209     9661   5299   9289    461   -186   -880       C  
ATOM   1657  CD  GLU A 209     -18.168  30.985 -11.059  1.00 69.63           C  
ANISOU 1657  CD  GLU A 209    10319   6065  10069    520   -374   -734       C  
ATOM   1658  OE1 GLU A 209     -18.662  32.014 -10.503  1.00 72.93           O  
ANISOU 1658  OE1 GLU A 209    10650   6369  10691    620   -316   -647       O  
ATOM   1659  OE2 GLU A 209     -18.174  30.780 -12.288  1.00 72.64           O  
ANISOU 1659  OE2 GLU A 209    10729   6580  10288    461   -572   -705       O  
ATOM   1660  N   ILE A 210     -20.302  28.020  -7.286  1.00 54.03           N  
ANISOU 1660  N   ILE A 210     7978   3819   8729    447    223  -1049       N  
ATOM   1661  CA  ILE A 210     -21.412  28.111  -6.384  1.00 55.23           C  
ANISOU 1661  CA  ILE A 210     7958   3871   9152    485    383  -1048       C  
ATOM   1662  C   ILE A 210     -21.154  27.490  -5.024  1.00 55.33           C  
ANISOU 1662  C   ILE A 210     8053   3829   9140    451    653  -1087       C  
ATOM   1663  O   ILE A 210     -21.525  28.075  -3.996  1.00 56.96           O  
ANISOU 1663  O   ILE A 210     8251   3959   9428    496    863  -1084       O  
ATOM   1664  CB  ILE A 210     -22.706  27.570  -7.013  1.00 56.78           C  
ANISOU 1664  CB  ILE A 210     7890   4070   9612    453    245  -1057       C  
ATOM   1665  CG1 ILE A 210     -23.927  27.939  -6.159  1.00 58.78           C  
ANISOU 1665  CG1 ILE A 210     7924   4199  10210    517    426  -1033       C  
ATOM   1666  CG2 ILE A 210     -22.666  26.097  -7.192  1.00 56.18           C  
ANISOU 1666  CG2 ILE A 210     7800   4019   9524    333    229  -1151       C  
ATOM   1667  CD1 ILE A 210     -24.246  29.426  -6.070  1.00 59.01           C  
ANISOU 1667  CD1 ILE A 210     7895   4153  10371    646    453   -949       C  
ATOM   1668  N   ASP A 211     -20.482  26.341  -4.993  1.00 54.16           N  
ANISOU 1668  N   ASP A 211     7992   3714   8869    369    661  -1117       N  
ATOM   1669  CA  ASP A 211     -20.065  25.721  -3.715  1.00 53.22           C  
ANISOU 1669  CA  ASP A 211     7973   3560   8686    332    885  -1100       C  
ATOM   1670  C   ASP A 211     -19.006  26.552  -3.016  1.00 51.50           C  
ANISOU 1670  C   ASP A 211     7968   3371   8226    357    954  -1067       C  
ATOM   1671  O   ASP A 211     -19.001  26.641  -1.805  1.00 52.04           O  
ANISOU 1671  O   ASP A 211     8110   3422   8239    344   1146  -1050       O  
ATOM   1672  CB  ASP A 211     -19.496  24.334  -3.970  1.00 53.56           C  
ANISOU 1672  CB  ASP A 211     8044   3608   8699    252    855  -1111       C  
ATOM   1673  CG  ASP A 211     -19.154  23.583  -2.688  1.00 53.68           C  
ANISOU 1673  CG  ASP A 211     8131   3583   8679    213   1062  -1037       C  
ATOM   1674  OD1 ASP A 211     -20.045  23.395  -1.845  1.00 54.24           O  
ANISOU 1674  OD1 ASP A 211     8116   3602   8889    203   1240  -1013       O  
ATOM   1675  OD2 ASP A 211     -17.976  23.191  -2.553  1.00 52.08           O  
ANISOU 1675  OD2 ASP A 211     8064   3404   8318    193   1043   -987       O  
ATOM   1676  N   GLN A 212     -18.118  27.172  -3.774  1.00 50.43           N  
ANISOU 1676  N   GLN A 212     7935   3286   7937    379    799  -1062       N  
ATOM   1677  CA  GLN A 212     -17.212  28.153  -3.207  1.00 50.82           C  
ANISOU 1677  CA  GLN A 212     8154   3348   7805    396    842  -1045       C  
ATOM   1678  C   GLN A 212     -17.919  29.321  -2.512  1.00 51.84           C  
ANISOU 1678  C   GLN A 212     8267   3408   8020    449    982  -1078       C  
ATOM   1679  O   GLN A 212     -17.560  29.681  -1.374  1.00 51.99           O  
ANISOU 1679  O   GLN A 212     8418   3422   7914    418   1136  -1105       O  
ATOM   1680  CB  GLN A 212     -16.370  28.822  -4.272  1.00 51.38           C  
ANISOU 1680  CB  GLN A 212     8296   3459   7767    420    668  -1027       C  
ATOM   1681  CG  GLN A 212     -15.206  29.602  -3.679  1.00 50.85           C  
ANISOU 1681  CG  GLN A 212     8399   3400   7521    408    702  -1013       C  
ATOM   1682  CD  GLN A 212     -14.168  28.684  -3.096  1.00 50.52           C  
ANISOU 1682  CD  GLN A 212     8448   3404   7340    338    723   -977       C  
ATOM   1683  OE1 GLN A 212     -14.051  27.513  -3.511  1.00 50.17           O  
ANISOU 1683  OE1 GLN A 212     8351   3374   7334    313    690   -959       O  
ATOM   1684  NE2 GLN A 212     -13.426  29.182  -2.133  1.00 49.95           N  
ANISOU 1684  NE2 GLN A 212     8501   3349   7127    300    774   -967       N  
ATOM   1685  N   LEU A 213     -18.921  29.898  -3.165  1.00 51.54           N  
ANISOU 1685  N   LEU A 213     8066   3315   8203    520    932  -1079       N  
ATOM   1686  CA  LEU A 213     -19.679  30.935  -2.484  1.00 52.63           C  
ANISOU 1686  CA  LEU A 213     8152   3344   8499    581   1109  -1118       C  
ATOM   1687  C   LEU A 213     -20.274  30.390  -1.180  1.00 53.34           C  
ANISOU 1687  C   LEU A 213     8235   3404   8625    537   1381  -1171       C  
ATOM   1688  O   LEU A 213     -20.241  31.068  -0.158  1.00 55.86           O  
ANISOU 1688  O   LEU A 213     8664   3677   8883    528   1594  -1242       O  
ATOM   1689  CB  LEU A 213     -20.803  31.481  -3.377  1.00 53.91           C  
ANISOU 1689  CB  LEU A 213     8076   3436   8968    673   1007  -1071       C  
ATOM   1690  CG  LEU A 213     -20.327  32.342  -4.521  1.00 53.28           C  
ANISOU 1690  CG  LEU A 213     8018   3371   8852    725    781   -989       C  
ATOM   1691  CD1 LEU A 213     -21.426  32.542  -5.555  1.00 54.22           C  
ANISOU 1691  CD1 LEU A 213     7888   3473   9239    793    597   -891       C  
ATOM   1692  CD2 LEU A 213     -19.835  33.663  -3.963  1.00 54.32           C  
ANISOU 1692  CD2 LEU A 213     8274   3399   8966    768    914  -1017       C  
ATOM   1693  N   PHE A 214     -20.882  29.209  -1.238  1.00 52.44           N  
ANISOU 1693  N   PHE A 214     7993   3308   8623    501   1389  -1144       N  
ATOM   1694  CA  PHE A 214     -21.565  28.683  -0.102  1.00 53.35           C  
ANISOU 1694  CA  PHE A 214     8077   3385   8805    460   1660  -1165       C  
ATOM   1695  C   PHE A 214     -20.617  28.397   1.010  1.00 53.28           C  
ANISOU 1695  C   PHE A 214     8319   3451   8471    375   1782  -1157       C  
ATOM   1696  O   PHE A 214     -20.941  28.577   2.170  1.00 54.66           O  
ANISOU 1696  O   PHE A 214     8571   3611   8585    341   2045  -1197       O  
ATOM   1697  CB  PHE A 214     -22.309  27.449  -0.488  1.00 53.62           C  
ANISOU 1697  CB  PHE A 214     7916   3410   9045    427   1621  -1126       C  
ATOM   1698  CG  PHE A 214     -23.586  27.684  -1.249  1.00 54.90           C  
ANISOU 1698  CG  PHE A 214     7783   3496   9580    489   1552  -1133       C  
ATOM   1699  CD1 PHE A 214     -24.002  28.957  -1.632  1.00 55.87           C  
ANISOU 1699  CD1 PHE A 214     7814   3555   9856    590   1512  -1139       C  
ATOM   1700  CD2 PHE A 214     -24.378  26.591  -1.591  1.00 55.54           C  
ANISOU 1700  CD2 PHE A 214     7654   3556   9890    439   1513  -1119       C  
ATOM   1701  CE1 PHE A 214     -25.191  29.134  -2.306  1.00 57.66           C  
ANISOU 1701  CE1 PHE A 214     7737   3715  10455    648   1421  -1105       C  
ATOM   1702  CE2 PHE A 214     -25.548  26.746  -2.283  1.00 57.36           C  
ANISOU 1702  CE2 PHE A 214     7589   3730  10473    477   1411  -1115       C  
ATOM   1703  CZ  PHE A 214     -25.953  28.027  -2.650  1.00 58.92           C  
ANISOU 1703  CZ  PHE A 214     7687   3882  10817    586   1351  -1094       C  
ATOM   1704  N   ARG A 215     -19.408  28.037   0.673  1.00 52.97           N  
ANISOU 1704  N   ARG A 215     8413   3498   8212    337   1595  -1105       N  
ATOM   1705  CA  ARG A 215     -18.433  27.752   1.719  1.00 55.08           C  
ANISOU 1705  CA  ARG A 215     8899   3851   8178    252   1659  -1060       C  
ATOM   1706  C   ARG A 215     -18.077  28.997   2.474  1.00 55.31           C  
ANISOU 1706  C   ARG A 215     9100   3890   8024    235   1759  -1153       C  
ATOM   1707  O   ARG A 215     -18.098  29.012   3.694  1.00 55.71           O  
ANISOU 1707  O   ARG A 215     9290   3983   7895    159   1952  -1174       O  
ATOM   1708  CB  ARG A 215     -17.173  27.073   1.163  1.00 55.67           C  
ANISOU 1708  CB  ARG A 215     9038   3995   8119    223   1437   -970       C  
ATOM   1709  CG  ARG A 215     -17.137  25.580   1.466  1.00 58.90           C  
ANISOU 1709  CG  ARG A 215     9406   4412   8560    169   1470   -854       C  
ATOM   1710  CD  ARG A 215     -16.836  24.758   0.234  1.00 60.86           C  
ANISOU 1710  CD  ARG A 215     9543   4629   8950    188   1293   -838       C  
ATOM   1711  NE  ARG A 215     -17.369  23.410   0.407  1.00 64.90           N  
ANISOU 1711  NE  ARG A 215     9942   5080   9634    149   1381   -774       N  
ATOM   1712  CZ  ARG A 215     -16.745  22.409   0.969  1.00 65.22           C  
ANISOU 1712  CZ  ARG A 215    10028   5116   9634    102   1415   -638       C  
ATOM   1713  NH1 ARG A 215     -15.510  22.518   1.381  1.00 66.73           N  
ANISOU 1713  NH1 ARG A 215    10361   5377   9615     84   1339   -541       N  
ATOM   1714  NH2 ARG A 215     -17.381  21.276   1.112  1.00 69.59           N  
ANISOU 1714  NH2 ARG A 215    10462   5583  10394     69   1520   -583       N  
ATOM   1715  N   ILE A 216     -17.793  30.044   1.704  1.00 54.33           N  
ANISOU 1715  N   ILE A 216     8967   3720   7953    297   1634  -1211       N  
ATOM   1716  CA  ILE A 216     -17.533  31.361   2.221  1.00 54.53           C  
ANISOU 1716  CA  ILE A 216     9124   3705   7888    288   1727  -1328       C  
ATOM   1717  C   ILE A 216     -18.674  31.813   3.096  1.00 58.52           C  
ANISOU 1717  C   ILE A 216     9601   4120   8512    297   2040  -1443       C  
ATOM   1718  O   ILE A 216     -18.449  32.256   4.226  1.00 62.43           O  
ANISOU 1718  O   ILE A 216    10286   4641   8792    210   2224  -1549       O  
ATOM   1719  CB  ILE A 216     -17.363  32.337   1.076  1.00 53.11           C  
ANISOU 1719  CB  ILE A 216     8872   3445   7862    378   1566  -1336       C  
ATOM   1720  CG1 ILE A 216     -15.973  32.132   0.453  1.00 50.78           C  
ANISOU 1720  CG1 ILE A 216     8669   3241   7382    342   1320  -1256       C  
ATOM   1721  CG2 ILE A 216     -17.557  33.772   1.550  1.00 54.71           C  
ANISOU 1721  CG2 ILE A 216     9136   3523   8126    398   1730  -1475       C  
ATOM   1722  CD1 ILE A 216     -15.838  32.632  -0.983  1.00 49.69           C  
ANISOU 1722  CD1 ILE A 216     8435   3061   7382    426   1129  -1201       C  
ATOM   1723  N   PHE A 217     -19.904  31.720   2.599  1.00 59.55           N  
ANISOU 1723  N   PHE A 217     9494   4147   8986    390   2111  -1432       N  
ATOM   1724  CA  PHE A 217     -21.057  32.188   3.389  1.00 62.44           C  
ANISOU 1724  CA  PHE A 217     9790   4395   9538    414   2451  -1544       C  
ATOM   1725  C   PHE A 217     -21.179  31.388   4.684  1.00 65.20           C  
ANISOU 1725  C   PHE A 217    10277   4833   9661    297   2696  -1553       C  
ATOM   1726  O   PHE A 217     -21.432  31.984   5.707  1.00 66.30           O  
ANISOU 1726  O   PHE A 217    10546   4941   9704    248   2989  -1693       O  
ATOM   1727  CB  PHE A 217     -22.394  32.119   2.627  1.00 62.31           C  
ANISOU 1727  CB  PHE A 217     9442   4252   9981    532   2465  -1500       C  
ATOM   1728  CG  PHE A 217     -22.421  32.818   1.274  1.00 60.01           C  
ANISOU 1728  CG  PHE A 217     8993   3892   9916    645   2196  -1437       C  
ATOM   1729  CD1 PHE A 217     -21.489  33.786   0.898  1.00 57.91           C  
ANISOU 1729  CD1 PHE A 217     8867   3614   9522    663   2059  -1454       C  
ATOM   1730  CD2 PHE A 217     -23.461  32.526   0.387  1.00 60.25           C  
ANISOU 1730  CD2 PHE A 217     8717   3867  10306    727   2082  -1347       C  
ATOM   1731  CE1 PHE A 217     -21.576  34.408  -0.334  1.00 56.73           C  
ANISOU 1731  CE1 PHE A 217     8574   3405   9574    764   1829  -1358       C  
ATOM   1732  CE2 PHE A 217     -23.558  33.161  -0.843  1.00 59.20           C  
ANISOU 1732  CE2 PHE A 217     8442   3695  10357    821   1820  -1256       C  
ATOM   1733  CZ  PHE A 217     -22.598  34.086  -1.203  1.00 57.55           C  
ANISOU 1733  CZ  PHE A 217     8395   3480   9988    842   1700  -1251       C  
ATOM   1734  N   ARG A 218     -20.999  30.051   4.650  1.00 66.96           N  
ANISOU 1734  N   ARG A 218    10480   5160   9799    246   2595  -1404       N  
ATOM   1735  CA  ARG A 218     -21.209  29.208   5.887  1.00 70.96           C  
ANISOU 1735  CA  ARG A 218    11102   5746  10113    136   2840  -1357       C  
ATOM   1736  C   ARG A 218     -20.306  29.736   7.007  1.00 68.93           C  
ANISOU 1736  C   ARG A 218    11173   5609   9408     13   2918  -1430       C  
ATOM   1737  O   ARG A 218     -20.687  29.699   8.159  1.00 69.86           O  
ANISOU 1737  O   ARG A 218    11425   5767   9349    -75   3213  -1479       O  
ATOM   1738  CB  ARG A 218     -21.017  27.666   5.643  1.00 74.95           C  
ANISOU 1738  CB  ARG A 218    11534   6317  10623     99   2700  -1158       C  
ATOM   1739  CG  ARG A 218     -21.477  26.687   6.748  1.00 81.77           C  
ANISOU 1739  CG  ARG A 218    12447   7224  11397      6   2962  -1053       C  
ATOM   1740  CD  ARG A 218     -21.839  25.255   6.248  1.00 89.97           C  
ANISOU 1740  CD  ARG A 218    13284   8217  12681      9   2890   -890       C  
ATOM   1741  NE  ARG A 218     -20.777  24.502   5.474  1.00 97.89           N  
ANISOU 1741  NE  ARG A 218    14292   9264  13634      9   2558   -772       N  
ATOM   1742  CZ  ARG A 218     -20.785  24.141   4.157  1.00 99.75           C  
ANISOU 1742  CZ  ARG A 218    14342   9433  14123     71   2323   -786       C  
ATOM   1743  NH1 ARG A 218     -21.833  24.350   3.338  1.00100.26           N  
ANISOU 1743  NH1 ARG A 218    14166   9396  14529    136   2313   -882       N  
ATOM   1744  NH2 ARG A 218     -19.705  23.545   3.620  1.00 99.01           N  
ANISOU 1744  NH2 ARG A 218    14297   9378  13941     60   2086   -703       N  
ATOM   1745  N   ALA A 219     -19.138  30.264   6.640  1.00 65.87           N  
ANISOU 1745  N   ALA A 219    10908   5278   8840      0   2658  -1444       N  
ATOM   1746  CA  ALA A 219     -18.161  30.788   7.605  1.00 67.00           C  
ANISOU 1746  CA  ALA A 219    11348   5547   8562   -137   2658  -1517       C  
ATOM   1747  C   ALA A 219     -18.299  32.277   7.974  1.00 67.97           C  
ANISOU 1747  C   ALA A 219    11581   5574   8668   -152   2837  -1780       C  
ATOM   1748  O   ALA A 219     -17.993  32.646   9.106  1.00 69.71           O  
ANISOU 1748  O   ALA A 219    12054   5887   8545   -296   2986  -1902       O  
ATOM   1749  CB  ALA A 219     -16.747  30.573   7.081  1.00 65.00           C  
ANISOU 1749  CB  ALA A 219    11152   5394   8151   -163   2288  -1396       C  
ATOM   1750  N   LEU A 220     -18.675  33.111   7.001  1.00 66.03           N  
ANISOU 1750  N   LEU A 220    11158   5150   8780    -14   2801  -1856       N  
ATOM   1751  CA  LEU A 220     -18.725  34.603   7.161  1.00 67.02           C  
ANISOU 1751  CA  LEU A 220    11353   5126   8983     -6   2949  -2093       C  
ATOM   1752  C   LEU A 220     -20.121  35.219   7.227  1.00 68.23           C  
ANISOU 1752  C   LEU A 220    11337   5063   9522     99   3296  -2228       C  
ATOM   1753  O   LEU A 220     -20.308  36.383   7.654  1.00 70.71           O  
ANISOU 1753  O   LEU A 220    11727   5229   9908     90   3529  -2455       O  
ATOM   1754  CB  LEU A 220     -17.967  35.287   6.034  1.00 64.85           C  
ANISOU 1754  CB  LEU A 220    11012   4782   8845     69   2652  -2056       C  
ATOM   1755  CG  LEU A 220     -16.543  34.781   5.820  1.00 63.50           C  
ANISOU 1755  CG  LEU A 220    10960   4788   8377    -15   2316  -1923       C  
ATOM   1756  CD1 LEU A 220     -15.867  35.534   4.694  1.00 62.02           C  
ANISOU 1756  CD1 LEU A 220    10702   4514   8350     57   2081  -1893       C  
ATOM   1757  CD2 LEU A 220     -15.686  34.821   7.085  1.00 65.18           C  
ANISOU 1757  CD2 LEU A 220    11460   5161   8141   -215   2340  -2011       C  
ATOM   1758  N   GLY A 221     -21.104  34.386   6.918  1.00 67.24           N  
ANISOU 1758  N   GLY A 221    10982   4912   9651    183   3359  -2099       N  
ATOM   1759  CA  GLY A 221     -22.512  34.744   6.948  1.00 67.90           C  
ANISOU 1759  CA  GLY A 221    10838   4797  10164    291   3675  -2177       C  
ATOM   1760  C   GLY A 221     -22.887  35.039   5.523  1.00 65.16           C  
ANISOU 1760  C   GLY A 221    10185   4316  10257    465   3426  -2054       C  
ATOM   1761  O   GLY A 221     -22.069  35.484   4.741  1.00 62.12           O  
ANISOU 1761  O   GLY A 221     9833   3940   9827    494   3133  -2003       O  
ATOM   1762  N   THR A 222     -24.131  34.777   5.207  1.00 66.15           N  
ANISOU 1762  N   THR A 222    10009   4325  10798    568   3544  -1995       N  
ATOM   1763  CA  THR A 222     -24.653  35.167   3.932  1.00 66.39           C  
ANISOU 1763  CA  THR A 222     9733   4227  11264    727   3323  -1876       C  
ATOM   1764  C   THR A 222     -24.778  36.669   3.831  1.00 69.60           C  
ANISOU 1764  C   THR A 222    10104   4411  11929    822   3444  -1987       C  
ATOM   1765  O   THR A 222     -25.433  37.326   4.698  1.00 73.86           O  
ANISOU 1765  O   THR A 222    10637   4779  12648    835   3861  -2171       O  
ATOM   1766  CB  THR A 222     -26.026  34.576   3.753  1.00 67.65           C  
ANISOU 1766  CB  THR A 222     9554   4306  11842    799   3438  -1796       C  
ATOM   1767  OG1 THR A 222     -25.965  33.250   4.226  1.00 66.92           O  
ANISOU 1767  OG1 THR A 222     9537   4379  11510    684   3463  -1742       O  
ATOM   1768  CG2 THR A 222     -26.451  34.597   2.308  1.00 66.81           C  
ANISOU 1768  CG2 THR A 222     9138   4159  12088    922   3079  -1615       C  
ATOM   1769  N   PRO A 223     -24.178  37.252   2.795  1.00 69.51           N  
ANISOU 1769  N   PRO A 223    10068   4378  11965    889   3122  -1884       N  
ATOM   1770  CA  PRO A 223     -24.243  38.719   2.696  1.00 72.00           C  
ANISOU 1770  CA  PRO A 223    10348   4448  12557    981   3242  -1969       C  
ATOM   1771  C   PRO A 223     -25.572  39.214   2.185  1.00 75.57           C  
ANISOU 1771  C   PRO A 223    10414   4667  13630   1160   3334  -1877       C  
ATOM   1772  O   PRO A 223     -26.331  38.516   1.481  1.00 74.81           O  
ANISOU 1772  O   PRO A 223    10040   4621  13763   1226   3153  -1692       O  
ATOM   1773  CB  PRO A 223     -23.159  39.043   1.699  1.00 69.49           C  
ANISOU 1773  CB  PRO A 223    10121   4202  12080    987   2854  -1837       C  
ATOM   1774  CG  PRO A 223     -23.142  37.847   0.809  1.00 67.01           C  
ANISOU 1774  CG  PRO A 223     9701   4096  11662    985   2511  -1627       C  
ATOM   1775  CD  PRO A 223     -23.341  36.682   1.741  1.00 66.40           C  
ANISOU 1775  CD  PRO A 223     9705   4160  11361    874   2680  -1703       C  
ATOM   1776  N   ASN A 224     -25.856  40.415   2.651  1.00 81.04           N  
ANISOU 1776  N   ASN A 224    11092   5094  14605   1222   3645  -2032       N  
ATOM   1777  CA  ASN A 224     -26.981  41.240   2.269  1.00 85.29           C  
ANISOU 1777  CA  ASN A 224    11269   5333  15804   1409   3784  -1961       C  
ATOM   1778  C   ASN A 224     -26.450  42.668   2.135  1.00 87.20           C  
ANISOU 1778  C   ASN A 224    11593   5336  16199   1465   3839  -2029       C  
ATOM   1779  O   ASN A 224     -25.241  42.918   2.275  1.00 83.55           O  
ANISOU 1779  O   ASN A 224    11452   4968  15324   1348   3738  -2124       O  
ATOM   1780  CB  ASN A 224     -28.031  41.177   3.367  1.00 90.61           C  
ANISOU 1780  CB  ASN A 224    11841   5859  16725   1413   4302  -2159       C  
ATOM   1781  CG  ASN A 224     -27.512  41.702   4.703  1.00 94.03           C  
ANISOU 1781  CG  ASN A 224    12638   6237  16852   1275   4733  -2518       C  
ATOM   1782  OD1 ASN A 224     -26.534  42.458   4.757  1.00 94.90           O  
ANISOU 1782  OD1 ASN A 224    12997   6314  16743   1216   4674  -2629       O  
ATOM   1783  ND2 ASN A 224     -28.173  41.310   5.794  1.00 97.79           N  
ANISOU 1783  ND2 ASN A 224    13149   6703  17303   1207   5175  -2706       N  
ATOM   1784  N   ASN A 225     -27.355  43.615   1.907  1.00 92.08           N  
ANISOU 1784  N   ASN A 225    11908   5626  17453   1641   4016  -1980       N  
ATOM   1785  CA  ASN A 225     -26.946  44.994   1.768  1.00 94.67           C  
ANISOU 1785  CA  ASN A 225    12279   5673  18018   1706   4099  -2030       C  
ATOM   1786  C   ASN A 225     -26.469  45.676   3.061  1.00 97.79           C  
ANISOU 1786  C   ASN A 225    12994   5922  18237   1576   4559  -2449       C  
ATOM   1787  O   ASN A 225     -25.632  46.560   2.979  1.00 97.79           O  
ANISOU 1787  O   ASN A 225    13168   5803  18183   1541   4528  -2526       O  
ATOM   1788  CB  ASN A 225     -28.023  45.795   1.039  1.00 98.26           C  
ANISOU 1788  CB  ASN A 225    12284   5803  19246   1946   4110  -1797       C  
ATOM   1789  CG  ASN A 225     -27.998  45.553  -0.463  1.00 95.91           C  
ANISOU 1789  CG  ASN A 225    11778   5650  19011   2041   3537  -1365       C  
ATOM   1790  OD1 ASN A 225     -26.976  45.087  -1.026  1.00 91.77           O  
ANISOU 1790  OD1 ASN A 225    11489   5407  17972   1935   3168  -1270       O  
ATOM   1791  ND2 ASN A 225     -29.126  45.841  -1.122  1.00 97.82           N  
ANISOU 1791  ND2 ASN A 225    11575   5712  19877   2233   3460  -1099       N  
ATOM   1792  N   GLU A 226     -26.956  45.246   4.229  1.00100.61           N  
ANISOU 1792  N   GLU A 226    13444   6304  18475   1484   4972  -2719       N  
ATOM   1793  CA  GLU A 226     -26.429  45.733   5.520  1.00103.76           C  
ANISOU 1793  CA  GLU A 226    14216   6648  18559   1306   5382  -3144       C  
ATOM   1794  C   GLU A 226     -24.924  45.604   5.603  1.00101.22           C  
ANISOU 1794  C   GLU A 226    14289   6581  17587   1110   5089  -3208       C  
ATOM   1795  O   GLU A 226     -24.240  46.540   5.986  1.00102.26           O  
ANISOU 1795  O   GLU A 226    14636   6566  17649   1022   5215  -3441       O  
ATOM   1796  CB  GLU A 226     -27.004  44.969   6.725  1.00106.67           C  
ANISOU 1796  CB  GLU A 226    14699   7139  18691   1187   5787  -3372       C  
ATOM   1797  CG  GLU A 226     -28.344  45.474   7.222  1.00113.91           C  
ANISOU 1797  CG  GLU A 226    15346   7715  20217   1314   6336  -3519       C  
ATOM   1798  CD  GLU A 226     -29.427  45.409   6.158  1.00115.97           C  
ANISOU 1798  CD  GLU A 226    15071   7816  21176   1569   6167  -3162       C  
ATOM   1799  OE1 GLU A 226     -30.233  46.381   6.080  1.00120.30           O  
ANISOU 1799  OE1 GLU A 226    15326   7963  22418   1743   6467  -3195       O  
ATOM   1800  OE2 GLU A 226     -29.441  44.395   5.399  1.00113.73           O  
ANISOU 1800  OE2 GLU A 226    14659   7801  20749   1586   5724  -2853       O  
ATOM   1801  N   VAL A 227     -24.426  44.416   5.272  1.00 99.05           N  
ANISOU 1801  N   VAL A 227    14094   6673  16865   1035   4712  -3010       N  
ATOM   1802  CA  VAL A 227     -23.022  44.086   5.478  1.00 96.12           C  
ANISOU 1802  CA  VAL A 227    14079   6576  15866    838   4452  -3061       C  
ATOM   1803  C   VAL A 227     -22.183  44.378   4.260  1.00 92.95           C  
ANISOU 1803  C   VAL A 227    13629   6195  15490    898   4002  -2812       C  
ATOM   1804  O   VAL A 227     -20.981  44.558   4.381  1.00 93.00           O  
ANISOU 1804  O   VAL A 227    13893   6310  15133    756   3842  -2885       O  
ATOM   1805  CB  VAL A 227     -22.823  42.610   5.873  1.00 94.90           C  
ANISOU 1805  CB  VAL A 227    14055   6793  15206    713   4320  -2988       C  
ATOM   1806  CG1 VAL A 227     -23.726  42.201   7.031  1.00 97.61           C  
ANISOU 1806  CG1 VAL A 227    14435   7139  15513    654   4772  -3182       C  
ATOM   1807  CG2 VAL A 227     -23.058  41.681   4.700  1.00 93.37           C  
ANISOU 1807  CG2 VAL A 227    13611   6745  15120    831   3928  -2627       C  
ATOM   1808  N   TRP A 228     -22.811  44.391   3.093  1.00 92.96           N  
ANISOU 1808  N   TRP A 228    13302   6111  15906   1093   3792  -2507       N  
ATOM   1809  CA  TRP A 228     -22.116  44.656   1.828  1.00 91.50           C  
ANISOU 1809  CA  TRP A 228    13061   5954  15748   1157   3375  -2233       C  
ATOM   1810  C   TRP A 228     -23.011  45.521   0.965  1.00 94.32           C  
ANISOU 1810  C   TRP A 228    13073   6012  16751   1379   3375  -2025       C  
ATOM   1811  O   TRP A 228     -23.926  45.028   0.280  1.00 97.26           O  
ANISOU 1811  O   TRP A 228    13152   6420  17383   1510   3229  -1784       O  
ATOM   1812  CB  TRP A 228     -21.814  43.357   1.120  1.00 88.33           C  
ANISOU 1812  CB  TRP A 228    12648   5895  15018   1129   2986  -1996       C  
ATOM   1813  CG  TRP A 228     -21.033  43.493  -0.164  1.00 87.10           C  
ANISOU 1813  CG  TRP A 228    12477   5816  14800   1166   2580  -1732       C  
ATOM   1814  CD1 TRP A 228     -20.673  44.650  -0.819  1.00 87.53           C  
ANISOU 1814  CD1 TRP A 228    12494   5663  15097   1239   2511  -1629       C  
ATOM   1815  CD2 TRP A 228     -20.542  42.421  -0.956  1.00 82.60           C  
ANISOU 1815  CD2 TRP A 228    11929   5541  13913   1127   2219  -1535       C  
ATOM   1816  NE1 TRP A 228     -19.991  44.351  -1.959  1.00 83.91           N  
ANISOU 1816  NE1 TRP A 228    12046   5377  14458   1242   2134  -1372       N  
ATOM   1817  CE2 TRP A 228     -19.895  42.990  -2.066  1.00 82.10           C  
ANISOU 1817  CE2 TRP A 228    11855   5454  13882   1173   1957  -1329       C  
ATOM   1818  CE3 TRP A 228     -20.583  41.027  -0.833  1.00 81.73           C  
ANISOU 1818  CE3 TRP A 228    11848   5695  13510   1054   2115  -1517       C  
ATOM   1819  CZ2 TRP A 228     -19.291  42.211  -3.051  1.00 80.81           C  
ANISOU 1819  CZ2 TRP A 228    11724   5537  13442   1143   1613  -1133       C  
ATOM   1820  CZ3 TRP A 228     -19.996  40.244  -1.829  1.00 79.81           C  
ANISOU 1820  CZ3 TRP A 228    11618   5672  13033   1031   1764  -1326       C  
ATOM   1821  CH2 TRP A 228     -19.358  40.843  -2.925  1.00 78.98           C  
ANISOU 1821  CH2 TRP A 228    11515   5550  12941   1073   1526  -1149       C  
ATOM   1822  N   PRO A 229     -22.767  46.823   0.991  1.00 95.43           N  
ANISOU 1822  N   PRO A 229    13231   5845  17182   1419   3529  -2107       N  
ATOM   1823  CA  PRO A 229     -23.694  47.609   0.229  1.00 97.79           C  
ANISOU 1823  CA  PRO A 229    13173   5842  18139   1643   3540  -1874       C  
ATOM   1824  C   PRO A 229     -23.706  47.311  -1.281  1.00 94.78           C  
ANISOU 1824  C   PRO A 229    12594   5606  17810   1756   3045  -1420       C  
ATOM   1825  O   PRO A 229     -22.672  47.064  -1.899  1.00 90.34           O  
ANISOU 1825  O   PRO A 229    12209   5256  16857   1672   2727  -1298       O  
ATOM   1826  CB  PRO A 229     -23.270  49.040   0.567  1.00101.06           C  
ANISOU 1826  CB  PRO A 229    13679   5888  18829   1643   3802  -2056       C  
ATOM   1827  CG  PRO A 229     -22.786  48.901   1.977  1.00101.39           C  
ANISOU 1827  CG  PRO A 229    14062   5996  18466   1426   4129  -2516       C  
ATOM   1828  CD  PRO A 229     -21.980  47.658   1.910  1.00 96.58           C  
ANISOU 1828  CD  PRO A 229    13663   5842  17188   1274   3796  -2453       C  
ATOM   1829  N   GLU A 230     -24.926  47.390  -1.823  1.00 97.16           N  
ANISOU 1829  N   GLU A 230    12515   5775  18625   1942   3011  -1186       N  
ATOM   1830  CA  GLU A 230     -25.284  47.075  -3.214  1.00 95.72           C  
ANISOU 1830  CA  GLU A 230    12086   5731  18549   2053   2553   -751       C  
ATOM   1831  C   GLU A 230     -25.157  45.623  -3.627  1.00 87.35           C  
ANISOU 1831  C   GLU A 230    11086   5095  17009   1951   2228   -672       C  
ATOM   1832  O   GLU A 230     -25.305  45.318  -4.802  1.00 84.56           O  
ANISOU 1832  O   GLU A 230    10590   4897  16641   2000   1829   -351       O  
ATOM   1833  CB  GLU A 230     -24.558  48.012  -4.203  1.00 99.50           C  
ANISOU 1833  CB  GLU A 230    12600   6110  19095   2106   2312   -485       C  
ATOM   1834  CG  GLU A 230     -24.891  49.485  -3.993  1.00106.63           C  
ANISOU 1834  CG  GLU A 230    13353   6535  20626   2246   2607   -484       C  
ATOM   1835  CD  GLU A 230     -25.142  50.236  -5.287  1.00112.51           C  
ANISOU 1835  CD  GLU A 230    13844   7141  21761   2417   2306     -5       C  
ATOM   1836  OE1 GLU A 230     -24.686  51.416  -5.411  1.00114.48           O  
ANISOU 1836  OE1 GLU A 230    14128   7084  22285   2466   2416     52       O  
ATOM   1837  OE2 GLU A 230     -25.810  49.645  -6.174  1.00114.27           O  
ANISOU 1837  OE2 GLU A 230    13834   7562  22022   2492   1955    320       O  
ATOM   1838  N   VAL A 231     -24.916  44.741  -2.666  1.00 83.06           N  
ANISOU 1838  N   VAL A 231    10748   4726  16085   1804   2403   -958       N  
ATOM   1839  CA  VAL A 231     -24.610  43.335  -2.998  1.00 78.77           C  
ANISOU 1839  CA  VAL A 231    10300   4561  15068   1689   2119   -907       C  
ATOM   1840  C   VAL A 231     -25.754  42.640  -3.720  1.00 80.00           C  
ANISOU 1840  C   VAL A 231    10115   4803  15476   1773   1900   -683       C  
ATOM   1841  O   VAL A 231     -25.539  41.930  -4.689  1.00 77.76           O  
ANISOU 1841  O   VAL A 231     9825   4766  14952   1735   1517   -497       O  
ATOM   1842  CB  VAL A 231     -24.158  42.506  -1.787  1.00 75.23           C  
ANISOU 1842  CB  VAL A 231    10121   4268  14193   1520   2350  -1215       C  
ATOM   1843  CG1 VAL A 231     -25.303  42.203  -0.855  1.00 76.91           C  
ANISOU 1843  CG1 VAL A 231    10174   4378  14668   1545   2703  -1370       C  
ATOM   1844  CG2 VAL A 231     -23.489  41.242  -2.267  1.00 71.09           C  
ANISOU 1844  CG2 VAL A 231     9735   4090  13182   1403   2030  -1136       C  
ATOM   1845  N   GLU A 232     -26.970  42.969  -3.325  1.00 83.87           N  
ANISOU 1845  N   GLU A 232    10303   5065  16496   1892   2141   -694       N  
ATOM   1846  CA  GLU A 232     -28.149  42.288  -3.843  1.00 85.81           C  
ANISOU 1846  CA  GLU A 232    10187   5377  17037   1957   1966   -512       C  
ATOM   1847  C   GLU A 232     -28.449  42.645  -5.303  1.00 86.63           C  
ANISOU 1847  C   GLU A 232    10047   5509  17359   2064   1508   -122       C  
ATOM   1848  O   GLU A 232     -29.340  42.051  -5.917  1.00 86.31           O  
ANISOU 1848  O   GLU A 232     9709   5570  17512   2093   1258     57       O  
ATOM   1849  CB  GLU A 232     -29.351  42.552  -2.909  1.00 90.24           C  
ANISOU 1849  CB  GLU A 232    10477   5667  18141   2050   2406   -647       C  
ATOM   1850  CG  GLU A 232     -29.086  42.095  -1.464  1.00 90.87           C  
ANISOU 1850  CG  GLU A 232    10830   5769  17924   1915   2855  -1021       C  
ATOM   1851  CD  GLU A 232     -30.117  42.586  -0.452  1.00 97.55           C  
ANISOU 1851  CD  GLU A 232    11477   6311  19276   1998   3388  -1203       C  
ATOM   1852  OE1 GLU A 232     -31.298  42.855  -0.819  1.00103.74           O  
ANISOU 1852  OE1 GLU A 232    11822   6904  20691   2156   3405  -1031       O  
ATOM   1853  OE2 GLU A 232     -29.741  42.761   0.736  1.00100.60           O  
ANISOU 1853  OE2 GLU A 232    12144   6637  19440   1902   3809  -1525       O  
ATOM   1854  N   SER A 233     -27.707  43.638  -5.820  1.00 87.62           N  
ANISOU 1854  N   SER A 233    10297   5539  17452   2112   1406      8       N  
ATOM   1855  CA  SER A 233     -27.768  44.078  -7.223  1.00 89.07           C  
ANISOU 1855  CA  SER A 233    10329   5772  17741   2195    968    408       C  
ATOM   1856  C   SER A 233     -26.847  43.334  -8.171  1.00 85.52           C  
ANISOU 1856  C   SER A 233    10128   5688  16675   2056    567    508       C  
ATOM   1857  O   SER A 233     -26.908  43.561  -9.378  1.00 85.66           O  
ANISOU 1857  O   SER A 233    10051   5806  16690   2094    186    837       O  
ATOM   1858  CB  SER A 233     -27.406  45.550  -7.299  1.00 90.81           C  
ANISOU 1858  CB  SER A 233    10565   5679  18257   2312   1096    517       C  
ATOM   1859  OG  SER A 233     -28.349  46.260  -6.540  1.00 96.98           O  
ANISOU 1859  OG  SER A 233    11076   6093  19677   2455   1469    438       O  
ATOM   1860  N   LEU A 234     -25.952  42.514  -7.626  1.00 80.82           N  
ANISOU 1860  N   LEU A 234     9860   5283  15565   1895    666    236       N  
ATOM   1861  CA  LEU A 234     -24.999  41.819  -8.452  1.00 78.29           C  
ANISOU 1861  CA  LEU A 234     9781   5272  14690   1765    354    294       C  
ATOM   1862  C   LEU A 234     -25.731  40.781  -9.287  1.00 80.47           C  
ANISOU 1862  C   LEU A 234     9873   5793  14907   1721     11    425       C  
ATOM   1863  O   LEU A 234     -26.804  40.279  -8.874  1.00 83.12           O  
ANISOU 1863  O   LEU A 234     9954   6091  15538   1745     83    368       O  
ATOM   1864  CB  LEU A 234     -23.931  41.180  -7.593  1.00 74.10           C  
ANISOU 1864  CB  LEU A 234     9593   4853  13709   1617    557    -13       C  
ATOM   1865  CG  LEU A 234     -23.123  42.157  -6.767  1.00 73.43           C  
ANISOU 1865  CG  LEU A 234     9712   4560  13627   1618    858   -172       C  
ATOM   1866  CD1 LEU A 234     -22.102  41.460  -5.915  1.00 69.44           C  
ANISOU 1866  CD1 LEU A 234     9518   4195  12670   1460   1003   -445       C  
ATOM   1867  CD2 LEU A 234     -22.441  43.134  -7.703  1.00 75.38           C  
ANISOU 1867  CD2 LEU A 234    10024   4748  13867   1663    681     60       C  
ATOM   1868  N   GLN A 235     -25.176  40.492 -10.468  1.00 80.43           N  
ANISOU 1868  N   GLN A 235     9991   6030  14537   1648   -347    594       N  
ATOM   1869  CA  GLN A 235     -25.879  39.721 -11.505  1.00 83.00           C  
ANISOU 1869  CA  GLN A 235    10141   6589  14804   1597   -740    755       C  
ATOM   1870  C   GLN A 235     -26.242  38.295 -11.051  1.00 79.87           C  
ANISOU 1870  C   GLN A 235     9719   6337  14291   1475   -699    509       C  
ATOM   1871  O   GLN A 235     -27.325  37.751 -11.361  1.00 80.50           O  
ANISOU 1871  O   GLN A 235     9513   6476  14595   1465   -882    571       O  
ATOM   1872  CB  GLN A 235     -25.087  39.724 -12.818  1.00 85.49           C  
ANISOU 1872  CB  GLN A 235    10659   7143  14678   1517  -1081    945       C  
ATOM   1873  CG  GLN A 235     -23.733  39.049 -12.794  1.00 84.96           C  
ANISOU 1873  CG  GLN A 235    10973   7248  14058   1371  -1005    735       C  
ATOM   1874  CD  GLN A 235     -23.151  38.816 -14.192  1.00 89.32           C  
ANISOU 1874  CD  GLN A 235    11693   8071  14172   1270  -1338    899       C  
ATOM   1875  OE1 GLN A 235     -23.822  38.312 -15.102  1.00 90.54           O  
ANISOU 1875  OE1 GLN A 235    11726   8421  14254   1211  -1667   1018       O  
ATOM   1876  NE2 GLN A 235     -21.875  39.190 -14.368  1.00 92.15           N  
ANISOU 1876  NE2 GLN A 235    12340   8446  14226   1235  -1245    896       N  
ATOM   1877  N   ASP A 236     -25.352  37.733 -10.247  1.00 74.97           N  
ANISOU 1877  N   ASP A 236     9375   5746  13363   1385   -446    241       N  
ATOM   1878  CA  ASP A 236     -25.522  36.396  -9.694  1.00 72.54           C  
ANISOU 1878  CA  ASP A 236     9083   5542  12934   1270   -354     15       C  
ATOM   1879  C   ASP A 236     -25.867  36.382  -8.182  1.00 72.05           C  
ANISOU 1879  C   ASP A 236     8981   5286  13106   1306     75   -187       C  
ATOM   1880  O   ASP A 236     -25.743  35.318  -7.536  1.00 73.05           O  
ANISOU 1880  O   ASP A 236     9196   5488  13072   1203    214   -373       O  
ATOM   1881  CB  ASP A 236     -24.243  35.589  -9.969  1.00 68.19           C  
ANISOU 1881  CB  ASP A 236     8869   5195  11843   1127   -411   -108       C  
ATOM   1882  CG  ASP A 236     -23.888  35.522 -11.463  1.00 67.79           C  
ANISOU 1882  CG  ASP A 236     8892   5354  11510   1067   -789     56       C  
ATOM   1883  OD1 ASP A 236     -24.810  35.273 -12.266  1.00 69.00           O  
ANISOU 1883  OD1 ASP A 236     8827   5603  11784   1052  -1074    181       O  
ATOM   1884  OD2 ASP A 236     -22.679  35.667 -11.779  1.00 65.09           O  
ANISOU 1884  OD2 ASP A 236     8826   5087  10817   1022   -786     46       O  
ATOM   1885  N   TYR A 237     -26.274  37.512  -7.597  1.00 71.27           N  
ANISOU 1885  N   TYR A 237     8767   4937  13373   1439    305   -157       N  
ATOM   1886  CA  TYR A 237     -26.784  37.470  -6.252  1.00 70.59           C  
ANISOU 1886  CA  TYR A 237     8622   4682  13517   1461    717   -353       C  
ATOM   1887  C   TYR A 237     -28.132  36.811  -6.407  1.00 74.04           C  
ANISOU 1887  C   TYR A 237     8696   5120  14314   1476    645   -294       C  
ATOM   1888  O   TYR A 237     -28.763  36.918  -7.477  1.00 76.40           O  
ANISOU 1888  O   TYR A 237     8744   5468  14813   1519    300    -71       O  
ATOM   1889  CB  TYR A 237     -26.995  38.843  -5.635  1.00 72.04           C  
ANISOU 1889  CB  TYR A 237     8747   4570  14055   1595   1011   -365       C  
ATOM   1890  CG  TYR A 237     -27.545  38.729  -4.220  1.00 72.12           C  
ANISOU 1890  CG  TYR A 237     8722   4423  14253   1594   1477   -601       C  
ATOM   1891  CD1 TYR A 237     -26.681  38.523  -3.134  1.00 69.98           C  
ANISOU 1891  CD1 TYR A 237     8792   4188  13609   1484   1759   -851       C  
ATOM   1892  CD2 TYR A 237     -28.918  38.713  -3.963  1.00 74.60           C  
ANISOU 1892  CD2 TYR A 237     8668   4584  15090   1682   1628   -571       C  
ATOM   1893  CE1 TYR A 237     -27.151  38.440  -1.844  1.00 70.98           C  
ANISOU 1893  CE1 TYR A 237     8928   4198  13840   1463   2192  -1063       C  
ATOM   1894  CE2 TYR A 237     -29.404  38.604  -2.670  1.00 75.85           C  
ANISOU 1894  CE2 TYR A 237     8816   4606  15396   1670   2097   -792       C  
ATOM   1895  CZ  TYR A 237     -28.509  38.444  -1.619  1.00 74.10           C  
ANISOU 1895  CZ  TYR A 237     8975   4436  14742   1553   2377  -1040       C  
ATOM   1896  OH  TYR A 237     -28.935  38.335  -0.298  1.00 76.20           O  
ANISOU 1896  OH  TYR A 237     9283   4597  15071   1516   2856  -1264       O  
ATOM   1897  N   LYS A 238     -28.578  36.118  -5.353  1.00 74.23           N  
ANISOU 1897  N   LYS A 238     8685   5101  14418   1427    957   -478       N  
ATOM   1898  CA  LYS A 238     -29.976  35.675  -5.261  1.00 76.76           C  
ANISOU 1898  CA  LYS A 238     8613   5348  15204   1457    997   -439       C  
ATOM   1899  C   LYS A 238     -30.461  35.709  -3.826  1.00 77.02           C  
ANISOU 1899  C   LYS A 238     8616   5196  15451   1476   1522   -628       C  
ATOM   1900  O   LYS A 238     -29.739  35.349  -2.877  1.00 75.24           O  
ANISOU 1900  O   LYS A 238     8705   5014  14866   1384   1792   -821       O  
ATOM   1901  CB  LYS A 238     -30.176  34.244  -5.782  1.00 76.55           C  
ANISOU 1901  CB  LYS A 238     8528   5539  15016   1313    739   -447       C  
ATOM   1902  CG  LYS A 238     -29.521  33.874  -7.106  1.00 75.16           C  
ANISOU 1902  CG  LYS A 238     8479   5601  14474   1231    265   -343       C  
ATOM   1903  CD  LYS A 238     -30.364  34.217  -8.336  1.00 78.40           C  
ANISOU 1903  CD  LYS A 238     8565   6055  15168   1280   -151    -99       C  
ATOM   1904  CE  LYS A 238     -29.592  33.798  -9.591  1.00 77.22           C  
ANISOU 1904  CE  LYS A 238     8622   6172  14545   1165   -574    -38       C  
ATOM   1905  NZ  LYS A 238     -30.435  33.379 -10.731  1.00 79.87           N  
ANISOU 1905  NZ  LYS A 238     8685   6657  15003   1099  -1018    105       N  
ATOM   1906  N   ASN A 239     -31.734  35.999  -3.698  1.00 80.30           N  
ANISOU 1906  N   ASN A 239     8635   5428  16447   1578   1651   -562       N  
ATOM   1907  CA  ASN A 239     -32.353  36.056  -2.395  1.00 82.27           C  
ANISOU 1907  CA  ASN A 239     8814   5486  16956   1600   2186   -736       C  
ATOM   1908  C   ASN A 239     -32.675  34.663  -1.893  1.00 79.91           C  
ANISOU 1908  C   ASN A 239     8503   5310  16548   1460   2296   -832       C  
ATOM   1909  O   ASN A 239     -33.220  34.510  -0.803  1.00 80.92           O  
ANISOU 1909  O   ASN A 239     8583   5315  16848   1450   2751   -966       O  
ATOM   1910  CB  ASN A 239     -33.642  36.914  -2.415  1.00 86.89           C  
ANISOU 1910  CB  ASN A 239     8935   5789  18289   1776   2337   -626       C  
ATOM   1911  CG  ASN A 239     -34.624  36.430  -3.453  1.00 89.55           C  
ANISOU 1911  CG  ASN A 239     8830   6188  19006   1796   1929   -391       C  
ATOM   1912  OD1 ASN A 239     -34.745  37.056  -4.486  1.00 91.28           O  
ANISOU 1912  OD1 ASN A 239     8876   6403  19403   1888   1552   -156       O  
ATOM   1913  ND2 ASN A 239     -35.288  35.276  -3.217  1.00 90.19           N  
ANISOU 1913  ND2 ASN A 239     8738   6343  19185   1692   1973   -442       N  
ATOM   1914  N   THR A 240     -32.403  33.667  -2.706  1.00 76.91           N  
ANISOU 1914  N   THR A 240     8149   5153  15920   1350   1902   -761       N  
ATOM   1915  CA  THR A 240     -32.717  32.279  -2.372  1.00 75.78           C  
ANISOU 1915  CA  THR A 240     7965   5105  15721   1210   1964   -829       C  
ATOM   1916  C   THR A 240     -31.549  31.554  -1.692  1.00 72.11           C  
ANISOU 1916  C   THR A 240     7949   4784  14666   1077   2098   -969       C  
ATOM   1917  O   THR A 240     -31.707  30.437  -1.183  1.00 71.86           O  
ANISOU 1917  O   THR A 240     7932   4801  14571    964   2236  -1024       O  
ATOM   1918  CB  THR A 240     -33.155  31.547  -3.654  1.00 75.77           C  
ANISOU 1918  CB  THR A 240     7714   5243  15831   1148   1464   -696       C  
ATOM   1919  OG1 THR A 240     -32.294  31.938  -4.750  1.00 73.71           O  
ANISOU 1919  OG1 THR A 240     7636   5133  15236   1153   1043   -603       O  
ATOM   1920  CG2 THR A 240     -34.598  31.874  -3.986  1.00 79.48           C  
ANISOU 1920  CG2 THR A 240     7657   5566  16975   1239   1408   -562       C  
ATOM   1921  N   PHE A 241     -30.378  32.185  -1.689  1.00 69.84           N  
ANISOU 1921  N   PHE A 241     8004   4554  13977   1090   2050  -1004       N  
ATOM   1922  CA  PHE A 241     -29.193  31.631  -1.029  1.00 67.32           C  
ANISOU 1922  CA  PHE A 241     8093   4365  13117    974   2152  -1110       C  
ATOM   1923  C   PHE A 241     -29.514  31.135   0.368  1.00 68.70           C  
ANISOU 1923  C   PHE A 241     8337   4489  13277    909   2609  -1222       C  
ATOM   1924  O   PHE A 241     -30.361  31.726   1.040  1.00 72.21           O  
ANISOU 1924  O   PHE A 241     8626   4762  14046    977   2954  -1277       O  
ATOM   1925  CB  PHE A 241     -28.113  32.699  -0.857  1.00 66.18           C  
ANISOU 1925  CB  PHE A 241     8254   4217  12675   1012   2175  -1161       C  
ATOM   1926  CG  PHE A 241     -27.377  33.110  -2.115  1.00 65.41           C  
ANISOU 1926  CG  PHE A 241     8218   4210  12423   1043   1756  -1050       C  
ATOM   1927  CD1 PHE A 241     -27.460  32.431  -3.327  1.00 65.19           C  
ANISOU 1927  CD1 PHE A 241     8068   4316  12385   1009   1362   -936       C  
ATOM   1928  CD2 PHE A 241     -26.547  34.220  -2.059  1.00 66.22           C  
ANISOU 1928  CD2 PHE A 241     8527   4264  12367   1091   1777  -1073       C  
ATOM   1929  CE1 PHE A 241     -26.729  32.816  -4.439  1.00 64.31           C  
ANISOU 1929  CE1 PHE A 241     8057   4305  12072   1021   1019   -838       C  
ATOM   1930  CE2 PHE A 241     -25.824  34.634  -3.176  1.00 65.54           C  
ANISOU 1930  CE2 PHE A 241     8515   4256  12128   1114   1431   -956       C  
ATOM   1931  CZ  PHE A 241     -25.906  33.911  -4.365  1.00 64.85           C  
ANISOU 1931  CZ  PHE A 241     8323   4321  11993   1078   1059   -834       C  
ATOM   1932  N   PRO A 242     -28.814  30.089   0.842  1.00 67.43           N  
ANISOU 1932  N   PRO A 242     8416   4464  12737    779   2639  -1247       N  
ATOM   1933  CA  PRO A 242     -28.956  29.760   2.258  1.00 68.79           C  
ANISOU 1933  CA  PRO A 242     8726   4611  12798    708   3082  -1327       C  
ATOM   1934  C   PRO A 242     -28.500  30.921   3.153  1.00 69.22           C  
ANISOU 1934  C   PRO A 242     9034   4613  12653    735   3365  -1460       C  
ATOM   1935  O   PRO A 242     -27.585  31.634   2.816  1.00 66.50           O  
ANISOU 1935  O   PRO A 242     8877   4308  12078    758   3180  -1483       O  
ATOM   1936  CB  PRO A 242     -28.025  28.538   2.457  1.00 66.73           C  
ANISOU 1936  CB  PRO A 242     8709   4518  12125    574   2974  -1282       C  
ATOM   1937  CG  PRO A 242     -27.616  28.124   1.106  1.00 64.65           C  
ANISOU 1937  CG  PRO A 242     8374   4337  11851    576   2518  -1209       C  
ATOM   1938  CD  PRO A 242     -27.667  29.360   0.264  1.00 64.53           C  
ANISOU 1938  CD  PRO A 242     8270   4274  11973    695   2321  -1207       C  
ATOM   1939  N   LYS A 243     -29.144  31.022   4.309  1.00 73.01           N  
ANISOU 1939  N   LYS A 243     9521   5004  13216    711   3830  -1556       N  
ATOM   1940  CA  LYS A 243     -29.029  32.132   5.273  1.00 75.24           C  
ANISOU 1940  CA  LYS A 243    10001   5196  13392    721   4199  -1736       C  
ATOM   1941  C   LYS A 243     -28.279  31.713   6.553  1.00 76.32           C  
ANISOU 1941  C   LYS A 243    10542   5486  12968    558   4439  -1816       C  
ATOM   1942  O   LYS A 243     -28.873  31.208   7.530  1.00 78.32           O  
ANISOU 1942  O   LYS A 243    10816   5736  13205    483   4822  -1845       O  
ATOM   1943  CB  LYS A 243     -30.412  32.618   5.635  1.00 78.73           C  
ANISOU 1943  CB  LYS A 243    10136   5409  14369    811   4598  -1805       C  
ATOM   1944  CG  LYS A 243     -31.368  32.766   4.466  1.00 79.41           C  
ANISOU 1944  CG  LYS A 243     9750   5357  15064    955   4360  -1669       C  
ATOM   1945  CD  LYS A 243     -30.995  33.929   3.576  1.00 78.78           C  
ANISOU 1945  CD  LYS A 243     9632   5198  15101   1080   4080  -1644       C  
ATOM   1946  CE  LYS A 243     -32.067  34.195   2.524  1.00 80.61           C  
ANISOU 1946  CE  LYS A 243     9375   5285  15965   1226   3870  -1484       C  
ATOM   1947  NZ  LYS A 243     -31.431  34.363   1.184  1.00 77.73           N  
ANISOU 1947  NZ  LYS A 243     9010   5031  15492   1265   3309  -1327       N  
ATOM   1948  N   TRP A 244     -26.960  31.873   6.488  1.00 75.29           N  
ANISOU 1948  N   TRP A 244    10718   5502  12384    496   4184  -1823       N  
ATOM   1949  CA  TRP A 244     -26.065  31.640   7.599  1.00 77.13           C  
ANISOU 1949  CA  TRP A 244    11345   5904  12054    338   4309  -1879       C  
ATOM   1950  C   TRP A 244     -25.727  32.996   8.259  1.00 79.72           C  
ANISOU 1950  C   TRP A 244    11902   6166  12221    316   4530  -2119       C  
ATOM   1951  O   TRP A 244     -25.472  33.966   7.580  1.00 76.85           O  
ANISOU 1951  O   TRP A 244    11484   5693  12019    408   4372  -2179       O  
ATOM   1952  CB  TRP A 244     -24.792  30.960   7.114  1.00 74.30           C  
ANISOU 1952  CB  TRP A 244    11148   5737  11344    277   3878  -1733       C  
ATOM   1953  CG  TRP A 244     -25.031  29.554   6.673  1.00 74.72           C  
ANISOU 1953  CG  TRP A 244    11036   5847  11505    264   3724  -1536       C  
ATOM   1954  CD1 TRP A 244     -25.434  28.517   7.442  1.00 76.74           C  
ANISOU 1954  CD1 TRP A 244    11305   6151  11699    176   3941  -1445       C  
ATOM   1955  CD2 TRP A 244     -24.865  29.020   5.344  1.00 73.13           C  
ANISOU 1955  CD2 TRP A 244    10640   5650  11493    327   3329  -1414       C  
ATOM   1956  NE1 TRP A 244     -25.541  27.371   6.692  1.00 75.06           N  
ANISOU 1956  NE1 TRP A 244    10903   5946  11667    183   3713  -1283       N  
ATOM   1957  CE2 TRP A 244     -25.187  27.654   5.398  1.00 72.96           C  
ANISOU 1957  CE2 TRP A 244    10518   5661  11539    269   3335  -1280       C  
ATOM   1958  CE3 TRP A 244     -24.462  29.572   4.112  1.00 71.87           C  
ANISOU 1958  CE3 TRP A 244    10397   5471  11437    416   2983  -1407       C  
ATOM   1959  CZ2 TRP A 244     -25.132  26.831   4.270  1.00 70.61           C  
ANISOU 1959  CZ2 TRP A 244    10043   5369  11416    289   3016  -1182       C  
ATOM   1960  CZ3 TRP A 244     -24.398  28.737   2.993  1.00 70.13           C  
ANISOU 1960  CZ3 TRP A 244    10019   5287  11340    432   2664  -1294       C  
ATOM   1961  CH2 TRP A 244     -24.743  27.385   3.091  1.00 69.24           C  
ANISOU 1961  CH2 TRP A 244     9811   5197  11299    365   2688  -1203       C  
ATOM   1962  N   LYS A 245     -25.735  32.998   9.583  1.00 84.01           N  
ANISOU 1962  N   LYS A 245    12706   6778  12436    180   4901  -2251       N  
ATOM   1963  CA  LYS A 245     -25.233  34.083  10.363  1.00 88.28           C  
ANISOU 1963  CA  LYS A 245    13542   7307  12692     96   5099  -2505       C  
ATOM   1964  C   LYS A 245     -23.715  34.095  10.287  1.00 86.87           C  
ANISOU 1964  C   LYS A 245    13647   7327  12032     -8   4706  -2465       C  
ATOM   1965  O   LYS A 245     -23.108  33.101   9.950  1.00 82.62           O  
ANISOU 1965  O   LYS A 245    13119   6956  11315    -39   4385  -2241       O  
ATOM   1966  CB  LYS A 245     -25.642  33.919  11.843  1.00 94.20           C  
ANISOU 1966  CB  LYS A 245    14530   8127  13134    -59   5599  -2649       C  
ATOM   1967  CG  LYS A 245     -27.136  34.096  12.182  1.00 99.14           C  
ANISOU 1967  CG  LYS A 245    14914   8534  14220     19   6121  -2754       C  
ATOM   1968  CD  LYS A 245     -27.323  34.295  13.684  1.00104.99           C  
ANISOU 1968  CD  LYS A 245    15983   9341  14565   -157   6653  -2980       C  
ATOM   1969  CE  LYS A 245     -28.677  34.871  14.086  1.00111.13           C  
ANISOU 1969  CE  LYS A 245    16560   9851  15813    -79   7253  -3183       C  
ATOM   1970  NZ  LYS A 245     -29.589  33.848  14.663  1.00114.29           N  
ANISOU 1970  NZ  LYS A 245    16859  10293  16271   -123   7598  -3052       N  
ATOM   1971  N   PRO A 246     -23.083  35.229  10.650  1.00 90.75           N  
ANISOU 1971  N   PRO A 246    14364   7784  12332    -73   4752  -2696       N  
ATOM   1972  CA  PRO A 246     -21.642  35.162  10.920  1.00 91.11           C  
ANISOU 1972  CA  PRO A 246    14714   8051  11852   -227   4442  -2675       C  
ATOM   1973  C   PRO A 246     -21.430  34.458  12.269  1.00 96.43           C  
ANISOU 1973  C   PRO A 246    15692   8967  11978   -437   4619  -2672       C  
ATOM   1974  O   PRO A 246     -22.022  34.900  13.249  1.00102.02           O  
ANISOU 1974  O   PRO A 246    16550   9639  12574   -524   5055  -2898       O  
ATOM   1975  CB  PRO A 246     -21.228  36.639  10.984  1.00 91.54           C  
ANISOU 1975  CB  PRO A 246    14893   7960  11927   -248   4505  -2957       C  
ATOM   1976  CG  PRO A 246     -22.343  37.386  10.337  1.00 91.50           C  
ANISOU 1976  CG  PRO A 246    14578   7639  12549    -47   4722  -3033       C  
ATOM   1977  CD  PRO A 246     -23.570  36.620  10.690  1.00 92.77           C  
ANISOU 1977  CD  PRO A 246    14572   7776  12898     -3   5036  -2967       C  
ATOM   1978  N   GLY A 247     -20.590  33.424  12.383  1.00 97.44           N  
ANISOU 1978  N   GLY A 247    15928   9336  11756   -527   4312  -2426       N  
ATOM   1979  CA  GLY A 247     -19.401  33.202  11.564  1.00 95.00           C  
ANISOU 1979  CA  GLY A 247    15594   9114  11387   -505   3811  -2255       C  
ATOM   1980  C   GLY A 247     -18.303  34.071  12.169  1.00 97.29           C  
ANISOU 1980  C   GLY A 247    16186   9509  11268   -673   3705  -2438       C  
ATOM   1981  O   GLY A 247     -18.012  35.106  11.597  1.00 92.82           O  
ANISOU 1981  O   GLY A 247    15577   8795  10894   -617   3624  -2594       O  
ATOM   1982  N   SER A 248     -17.648  33.700  13.282  1.00102.02           N  
ANISOU 1982  N   SER A 248    17085  10362  11316   -886   3677  -2409       N  
ATOM   1983  CA  SER A 248     -17.280  32.339  13.714  1.00103.94           C  
ANISOU 1983  CA  SER A 248    17386  10837  11266   -964   3519  -2087       C  
ATOM   1984  C   SER A 248     -16.160  31.861  12.803  1.00 98.40           C  
ANISOU 1984  C   SER A 248    16556  10186  10643   -903   3029  -1847       C  
ATOM   1985  O   SER A 248     -16.349  30.947  11.972  1.00 97.87           O  
ANISOU 1985  O   SER A 248    16246  10060  10879   -762   2900  -1614       O  
ATOM   1986  CB  SER A 248     -18.442  31.335  13.802  1.00107.63           C  
ANISOU 1986  CB  SER A 248    17697  11260  11936   -884   3789  -1923       C  
ATOM   1987  OG  SER A 248     -17.975  30.083  14.261  1.00112.05           O  
ANISOU 1987  OG  SER A 248    18331  12027  12215   -971   3630  -1599       O  
ATOM   1988  N   LEU A 249     -15.023  32.536  12.964  1.00 94.98           N  
ANISOU 1988  N   LEU A 249    16284   9845   9957  -1020   2784  -1937       N  
ATOM   1989  CA  LEU A 249     -13.869  32.386  12.101  1.00 91.14           C  
ANISOU 1989  CA  LEU A 249    15681   9378   9570   -972   2356  -1774       C  
ATOM   1990  C   LEU A 249     -12.689  31.732  12.769  1.00 91.65           C  
ANISOU 1990  C   LEU A 249    15894   9701   9226  -1135   2053  -1553       C  
ATOM   1991  O   LEU A 249     -12.029  30.896  12.155  1.00 92.25           O  
ANISOU 1991  O   LEU A 249    15810   9804   9434  -1063   1770  -1277       O  
ATOM   1992  CB  LEU A 249     -13.434  33.736  11.581  1.00 90.90           C  
ANISOU 1992  CB  LEU A 249    15651   9206   9679   -959   2288  -2025       C  
ATOM   1993  CG  LEU A 249     -12.340  33.706  10.519  1.00 90.18           C  
ANISOU 1993  CG  LEU A 249    15406   9091   9766   -886   1902  -1876       C  
ATOM   1994  CD1 LEU A 249     -12.865  33.150   9.185  1.00 87.71           C  
ANISOU 1994  CD1 LEU A 249    14797   8624   9905   -656   1866  -1719       C  
ATOM   1995  CD2 LEU A 249     -11.757  35.097  10.331  1.00 90.31           C  
ANISOU 1995  CD2 LEU A 249    15488   9002   9821   -940   1847  -2125       C  
ATOM   1996  N   ALA A 250     -12.408  32.090  14.013  1.00 94.88           N  
ANISOU 1996  N   ALA A 250    16599  10301   9147  -1361   2105  -1667       N  
ATOM   1997  CA  ALA A 250     -11.455  31.323  14.842  1.00 96.65           C  
ANISOU 1997  CA  ALA A 250    16972  10813   8938  -1536   1826  -1397       C  
ATOM   1998  C   ALA A 250     -11.827  29.838  14.844  1.00 94.82           C  
ANISOU 1998  C   ALA A 250    16615  10624   8786  -1449   1840  -1018       C  
ATOM   1999  O   ALA A 250     -10.965  28.952  14.867  1.00 91.90           O  
ANISOU 1999  O   ALA A 250    16186  10378   8354  -1468   1528   -682       O  
ATOM   2000  CB  ALA A 250     -11.441  31.858  16.271  1.00101.40           C  
ANISOU 2000  CB  ALA A 250    17943  11630   8953  -1807   1961  -1591       C  
ATOM   2001  N   SER A 251     -13.134  29.614  14.860  1.00 95.37           N  
ANISOU 2001  N   SER A 251    16635  10572   9025  -1359   2223  -1082       N  
ATOM   2002  CA  SER A 251     -13.734  28.330  14.626  1.00 98.15           C  
ANISOU 2002  CA  SER A 251    16811  10875   9605  -1244   2305   -790       C  
ATOM   2003  C   SER A 251     -13.033  27.584  13.487  1.00 96.89           C  
ANISOU 2003  C   SER A 251    16376  10623   9813  -1092   1970   -544       C  
ATOM   2004  O   SER A 251     -12.594  26.433  13.658  1.00 96.47           O  
ANISOU 2004  O   SER A 251    16270  10651   9733  -1100   1811   -199       O  
ATOM   2005  CB  SER A 251     -15.210  28.550  14.303  1.00 98.17           C  
ANISOU 2005  CB  SER A 251    16689  10666   9945  -1118   2721   -985       C  
ATOM   2006  OG  SER A 251     -15.850  27.366  13.873  1.00 99.09           O  
ANISOU 2006  OG  SER A 251    16581  10685  10380   -996   2791   -741       O  
ATOM   2007  N   HIS A 252     -12.918  28.265  12.349  1.00 96.13           N  
ANISOU 2007  N   HIS A 252    16115  10352  10059   -959   1881   -723       N  
ATOM   2008  CA  HIS A 252     -12.384  27.674  11.119  1.00 94.92           C  
ANISOU 2008  CA  HIS A 252    15703  10084  10277   -808   1630   -560       C  
ATOM   2009  C   HIS A 252     -10.854  27.631  11.004  1.00 92.32           C  
ANISOU 2009  C   HIS A 252    15378   9859   9838   -864   1247   -411       C  
ATOM   2010  O   HIS A 252     -10.348  27.239   9.952  1.00 86.13           O  
ANISOU 2010  O   HIS A 252    14389   8971   9366   -743   1071   -311       O  
ATOM   2011  CB  HIS A 252     -12.987  28.379   9.877  1.00 95.53           C  
ANISOU 2011  CB  HIS A 252    15598   9939  10760   -643   1707   -785       C  
ATOM   2012  CG  HIS A 252     -14.429  28.054   9.622  1.00 99.69           C  
ANISOU 2012  CG  HIS A 252    15988  10326  11562   -540   2000   -835       C  
ATOM   2013  ND1 HIS A 252     -15.468  28.726  10.245  1.00103.74           N  
ANISOU 2013  ND1 HIS A 252    16587  10799  12027   -569   2334  -1044       N  
ATOM   2014  CD2 HIS A 252     -15.009  27.135   8.805  1.00 98.41           C  
ANISOU 2014  CD2 HIS A 252    15593  10045  11752   -417   2013   -717       C  
ATOM   2015  CE1 HIS A 252     -16.624  28.223   9.833  1.00106.38           C  
ANISOU 2015  CE1 HIS A 252    16726  11000  12691   -462   2529  -1025       C  
ATOM   2016  NE2 HIS A 252     -16.375  27.254   8.964  1.00103.63           N  
ANISOU 2016  NE2 HIS A 252    16189  10609  12577   -377   2325   -833       N  
ATOM   2017  N   VAL A 253     -10.112  28.051  12.036  1.00 94.48           N  
ANISOU 2017  N   VAL A 253    15873  10336   9687  -1054   1118   -409       N  
ATOM   2018  CA  VAL A 253      -8.645  28.186  11.889  1.00 93.24           C  
ANISOU 2018  CA  VAL A 253    15685  10265   9474  -1114    740   -296       C  
ATOM   2019  C   VAL A 253      -7.912  28.292  13.189  1.00 96.72           C  
ANISOU 2019  C   VAL A 253    16357  10974   9417  -1348    563   -205       C  
ATOM   2020  O   VAL A 253      -8.267  29.110  14.043  1.00104.12           O  
ANISOU 2020  O   VAL A 253    17547  12016   9997  -1505    709   -447       O  
ATOM   2021  CB  VAL A 253      -8.249  29.388  10.978  1.00 89.83           C  
ANISOU 2021  CB  VAL A 253    15188   9696   9245  -1062    670   -566       C  
ATOM   2022  CG1 VAL A 253      -9.183  30.573  11.157  1.00 89.89           C  
ANISOU 2022  CG1 VAL A 253    15334   9620   9200  -1085    960   -934       C  
ATOM   2023  CG2 VAL A 253      -6.804  29.803  11.192  1.00 90.50           C  
ANISOU 2023  CG2 VAL A 253    15303   9902   9178  -1194    329   -516       C  
ATOM   2024  N   LYS A 254      -6.889  27.459  13.330  1.00 97.30           N  
ANISOU 2024  N   LYS A 254    16338  11156   9475  -1376    249    143       N  
ATOM   2025  CA  LYS A 254      -6.035  27.439  14.516  1.00102.94           C  
ANISOU 2025  CA  LYS A 254    17232  12153   9725  -1604    -14    310       C  
ATOM   2026  C   LYS A 254      -4.611  27.872  14.209  1.00101.12           C  
ANISOU 2026  C   LYS A 254    16890  11962   9566  -1660   -405    350       C  
ATOM   2027  O   LYS A 254      -4.205  27.862  13.065  1.00 98.67           O  
ANISOU 2027  O   LYS A 254    16334  11458   9695  -1498   -469    349       O  
ATOM   2028  CB  LYS A 254      -6.036  26.043  15.153  1.00106.57           C  
ANISOU 2028  CB  LYS A 254    17670  12731  10089  -1613    -76    763       C  
ATOM   2029  CG  LYS A 254      -7.120  25.843  16.215  1.00111.95           C  
ANISOU 2029  CG  LYS A 254    18613  13544  10379  -1722    229    752       C  
ATOM   2030  CD  LYS A 254      -8.491  25.488  15.633  1.00110.02           C  
ANISOU 2030  CD  LYS A 254    18268  13065  10466  -1541    646    643       C  
ATOM   2031  CE  LYS A 254      -9.536  25.311  16.750  1.00113.39           C  
ANISOU 2031  CE  LYS A 254    18949  13624  10511  -1663    982    639       C  
ATOM   2032  NZ  LYS A 254     -10.937  25.174  16.259  1.00110.84           N  
ANISOU 2032  NZ  LYS A 254    18526  13074  10513  -1511   1409    474       N  
ATOM   2033  N   ASN A 255      -3.875  28.214  15.268  1.00104.09           N  
ANISOU 2033  N   ASN A 255    17451  12603   9494  -1906   -662    394       N  
ATOM   2034  CA  ASN A 255      -2.485  28.729  15.236  1.00103.90           C  
ANISOU 2034  CA  ASN A 255    17345  12664   9469  -2024  -1066    422       C  
ATOM   2035  C   ASN A 255      -2.351  30.189  14.862  1.00100.98           C  
ANISOU 2035  C   ASN A 255    17041  12195   9130  -2089  -1017    -27       C  
ATOM   2036  O   ASN A 255      -1.413  30.561  14.150  1.00 99.18           O  
ANISOU 2036  O   ASN A 255    16615  11871   9199  -2056  -1229    -33       O  
ATOM   2037  CB  ASN A 255      -1.558  27.899  14.349  1.00102.95           C  
ANISOU 2037  CB  ASN A 255    16860  12416   9840  -1851  -1303    762       C  
ATOM   2038  CG  ASN A 255      -1.651  26.433  14.640  1.00106.18           C  
ANISOU 2038  CG  ASN A 255    17167  12864  10312  -1769  -1339   1218       C  
ATOM   2039  OD1 ASN A 255      -2.132  25.647  13.812  1.00106.69           O  
ANISOU 2039  OD1 ASN A 255    17044  12707  10783  -1545  -1143   1316       O  
ATOM   2040  ND2 ASN A 255      -1.233  26.049  15.833  1.00110.51           N  
ANISOU 2040  ND2 ASN A 255    17847  13693  10449  -1959  -1585   1501       N  
ATOM   2041  N   LEU A 256      -3.273  31.016  15.346  1.00100.53           N  
ANISOU 2041  N   LEU A 256    17253  12144   8797  -2183   -718   -397       N  
ATOM   2042  CA  LEU A 256      -3.139  32.468  15.240  1.00 99.83           C  
ANISOU 2042  CA  LEU A 256    17273  11972   8685  -2292   -667   -834       C  
ATOM   2043  C   LEU A 256      -3.564  33.133  16.514  1.00101.59           C  
ANISOU 2043  C   LEU A 256    17873  12387   8340  -2561   -538  -1120       C  
ATOM   2044  O   LEU A 256      -4.653  32.894  17.012  1.00102.00           O  
ANISOU 2044  O   LEU A 256    18098  12465   8191  -2551   -205  -1187       O  
ATOM   2045  CB  LEU A 256      -3.992  33.012  14.103  1.00 96.41           C  
ANISOU 2045  CB  LEU A 256    16723  11212   8697  -2060   -326  -1081       C  
ATOM   2046  CG  LEU A 256      -3.599  32.607  12.688  1.00 93.71           C  
ANISOU 2046  CG  LEU A 256    16041  10659   8904  -1812   -413   -896       C  
ATOM   2047  CD1 LEU A 256      -4.615  33.176  11.721  1.00 91.16           C  
ANISOU 2047  CD1 LEU A 256    15656  10062   8919  -1615    -74  -1138       C  
ATOM   2048  CD2 LEU A 256      -2.204  33.081  12.272  1.00 95.11           C  
ANISOU 2048  CD2 LEU A 256    16068  10825   9241  -1878   -749   -861       C  
ATOM   2049  N   ASP A 257      -2.701  33.980  17.054  1.00103.37           N  
ANISOU 2049  N   ASP A 257    18226  12743   8304  -2817   -787  -1309       N  
ATOM   2050  CA  ASP A 257      -3.109  34.865  18.156  1.00106.68           C  
ANISOU 2050  CA  ASP A 257    19028  13300   8203  -3094   -616  -1708       C  
ATOM   2051  C   ASP A 257      -4.267  35.776  17.716  1.00104.46           C  
ANISOU 2051  C   ASP A 257    18813  12716   8160  -2970   -104  -2143       C  
ATOM   2052  O   ASP A 257      -4.592  35.826  16.529  1.00101.89           O  
ANISOU 2052  O   ASP A 257    18229  12098   8385  -2693     32  -2123       O  
ATOM   2053  CB  ASP A 257      -1.919  35.687  18.701  1.00110.11           C  
ANISOU 2053  CB  ASP A 257    19564  13899   8373  -3407   -999  -1876       C  
ATOM   2054  CG  ASP A 257      -1.197  36.500  17.637  1.00107.24           C  
ANISOU 2054  CG  ASP A 257    18942  13267   8534  -3320  -1123  -2015       C  
ATOM   2055  OD1 ASP A 257      -1.653  36.563  16.486  1.00102.58           O  
ANISOU 2055  OD1 ASP A 257    18135  12370   8470  -3031   -893  -2022       O  
ATOM   2056  OD2 ASP A 257      -0.154  37.079  17.966  1.00110.03           O  
ANISOU 2056  OD2 ASP A 257    19312  13730   8763  -3559  -1462  -2108       O  
ATOM   2057  N   GLU A 258      -4.881  36.488  18.655  1.00106.94           N  
ANISOU 2057  N   GLU A 258    19464  13096   8069  -3174    177  -2527       N  
ATOM   2058  CA  GLU A 258      -5.998  37.360  18.321  1.00105.24           C  
ANISOU 2058  CA  GLU A 258    19296  12576   8114  -3056    683  -2931       C  
ATOM   2059  C   GLU A 258      -5.703  38.359  17.199  1.00101.45           C  
ANISOU 2059  C   GLU A 258    18595  11757   8194  -2920    677  -3131       C  
ATOM   2060  O   GLU A 258      -6.615  38.795  16.489  1.00 97.72           O  
ANISOU 2060  O   GLU A 258    18012  10978   8138  -2702   1032  -3286       O  
ATOM   2061  CB  GLU A 258      -6.437  38.200  19.534  1.00110.64           C  
ANISOU 2061  CB  GLU A 258    20388  13363   8288  -3350    967  -3393       C  
ATOM   2062  CG  GLU A 258      -7.552  37.681  20.412  1.00114.11           C  
ANISOU 2062  CG  GLU A 258    21068  13936   8352  -3389   1364  -3414       C  
ATOM   2063  CD  GLU A 258      -7.903  38.629  21.571  1.00120.79           C  
ANISOU 2063  CD  GLU A 258    22335  14867   8692  -3702   1675  -3935       C  
ATOM   2064  OE1 GLU A 258      -7.400  39.778  21.644  1.00122.89           O  
ANISOU 2064  OE1 GLU A 258    22699  15034   8958  -3874   1627  -4334       O  
ATOM   2065  OE2 GLU A 258      -8.716  38.227  22.435  1.00124.81           O  
ANISOU 2065  OE2 GLU A 258    23090  15532   8800  -3787   2005  -3965       O  
ATOM   2066  N   ASN A 259      -4.444  38.776  17.116  1.00101.45           N  
ANISOU 2066  N   ASN A 259    18541  11815   8188  -3072    281  -3130       N  
ATOM   2067  CA  ASN A 259      -3.970  39.653  16.065  1.00 98.44           C  
ANISOU 2067  CA  ASN A 259    17942  11138   8321  -2967    225  -3253       C  
ATOM   2068  C   ASN A 259      -4.102  39.033  14.688  1.00 93.57           C  
ANISOU 2068  C   ASN A 259    16972  10329   8250  -2615    213  -2921       C  
ATOM   2069  O   ASN A 259      -4.626  39.671  13.760  1.00 93.36           O  
ANISOU 2069  O   ASN A 259    16811   9989   8670  -2420    449  -3053       O  
ATOM   2070  CB  ASN A 259      -2.506  39.999  16.297  1.00 99.63           C  
ANISOU 2070  CB  ASN A 259    18072  11430   8350  -3211   -238  -3241       C  
ATOM   2071  CG  ASN A 259      -2.308  40.868  17.497  1.00104.81           C  
ANISOU 2071  CG  ASN A 259    19071  12228   8523  -3585   -238  -3658       C  
ATOM   2072  OD1 ASN A 259      -3.225  41.561  17.924  1.00106.47           O  
ANISOU 2072  OD1 ASN A 259    19510  12316   8626  -3637    176  -4053       O  
ATOM   2073  ND2 ASN A 259      -1.103  40.860  18.037  1.00107.52           N  
ANISOU 2073  ND2 ASN A 259    19442  12820   8589  -3856   -699  -3588       N  
ATOM   2074  N   GLY A 260      -3.584  37.818  14.546  1.00 90.52           N  
ANISOU 2074  N   GLY A 260    16434  10125   7832  -2546    -71  -2489       N  
ATOM   2075  CA  GLY A 260      -3.725  37.077  13.317  1.00 85.00           C  
ANISOU 2075  CA  GLY A 260    15430   9273   7591  -2238    -70  -2186       C  
ATOM   2076  C   GLY A 260      -5.176  36.976  12.883  1.00 82.33           C  
ANISOU 2076  C   GLY A 260    15074   8747   7457  -2015    348  -2263       C  
ATOM   2077  O   GLY A 260      -5.515  37.263  11.751  1.00 79.31           O  
ANISOU 2077  O   GLY A 260    14501   8116   7515  -1799    467  -2274       O  
ATOM   2078  N   LEU A 261      -6.038  36.598  13.807  1.00 84.05           N  
ANISOU 2078  N   LEU A 261    15492   9093   7347  -2080    571  -2314       N  
ATOM   2079  CA  LEU A 261      -7.438  36.387  13.483  1.00 82.89           C  
ANISOU 2079  CA  LEU A 261    15301   8784   7407  -1879    964  -2358       C  
ATOM   2080  C   LEU A 261      -8.111  37.654  13.021  1.00 82.25           C  
ANISOU 2080  C   LEU A 261    15212   8405   7631  -1801   1265  -2714       C  
ATOM   2081  O   LEU A 261      -8.995  37.657  12.155  1.00 78.31           O  
ANISOU 2081  O   LEU A 261    14532   7686   7533  -1564   1475  -2694       O  
ATOM   2082  CB  LEU A 261      -8.172  35.806  14.692  1.00 87.36           C  
ANISOU 2082  CB  LEU A 261    16102   9552   7537  -2000   1173  -2356       C  
ATOM   2083  CG  LEU A 261      -7.688  34.409  15.108  1.00 89.47           C  
ANISOU 2083  CG  LEU A 261    16349  10085   7557  -2037    909  -1928       C  
ATOM   2084  CD1 LEU A 261      -8.208  34.017  16.475  1.00 94.47           C  
ANISOU 2084  CD1 LEU A 261    17277  10961   7653  -2227   1083  -1934       C  
ATOM   2085  CD2 LEU A 261      -8.077  33.339  14.079  1.00 87.49           C  
ANISOU 2085  CD2 LEU A 261    15800   9705   7734  -1758    916  -1610       C  
ATOM   2086  N   ASP A 262      -7.704  38.735  13.663  1.00 87.14           N  
ANISOU 2086  N   ASP A 262    16033   9021   8056  -2019   1283  -3043       N  
ATOM   2087  CA  ASP A 262      -8.234  40.058  13.409  1.00 88.69           C  
ANISOU 2087  CA  ASP A 262    16250   8917   8530  -1987   1579  -3413       C  
ATOM   2088  C   ASP A 262      -7.783  40.536  12.037  1.00 83.93           C  
ANISOU 2088  C   ASP A 262    15376   8071   8441  -1805   1432  -3316       C  
ATOM   2089  O   ASP A 262      -8.607  40.897  11.198  1.00 81.96           O  
ANISOU 2089  O   ASP A 262    14967   7559   8614  -1583   1655  -3337       O  
ATOM   2090  CB  ASP A 262      -7.752  41.000  14.504  1.00 95.39           C  
ANISOU 2090  CB  ASP A 262    17398   9839   9006  -2308   1599  -3794       C  
ATOM   2091  CG  ASP A 262      -8.358  42.358  14.393  1.00 98.57           C  
ANISOU 2091  CG  ASP A 262    17845   9905   9702  -2292   1962  -4208       C  
ATOM   2092  OD1 ASP A 262      -9.551  42.489  14.723  1.00101.53           O  
ANISOU 2092  OD1 ASP A 262    18290  10166  10118  -2222   2389  -4383       O  
ATOM   2093  OD2 ASP A 262      -7.653  43.288  13.953  1.00 99.01           O  
ANISOU 2093  OD2 ASP A 262    17842   9787   9990  -2340   1838  -4345       O  
ATOM   2094  N   LEU A 263      -6.479  40.498  11.805  1.00 82.03           N  
ANISOU 2094  N   LEU A 263    15074   7929   8165  -1901   1052  -3181       N  
ATOM   2095  CA  LEU A 263      -5.927  40.860  10.497  1.00 79.18           C  
ANISOU 2095  CA  LEU A 263    14462   7367   8253  -1744    908  -3050       C  
ATOM   2096  C   LEU A 263      -6.641  40.097   9.386  1.00 77.40           C  
ANISOU 2096  C   LEU A 263    14006   7052   8349  -1442    980  -2775       C  
ATOM   2097  O   LEU A 263      -7.107  40.686   8.407  1.00 77.13           O  
ANISOU 2097  O   LEU A 263    13828   6765   8710  -1263   1115  -2796       O  
ATOM   2098  CB  LEU A 263      -4.432  40.534  10.435  1.00 77.62           C  
ANISOU 2098  CB  LEU A 263    14191   7340   7961  -1873    483  -2855       C  
ATOM   2099  CG  LEU A 263      -3.731  40.786   9.096  1.00 74.05           C  
ANISOU 2099  CG  LEU A 263    13481   6711   7941  -1728    338  -2688       C  
ATOM   2100  CD1 LEU A 263      -4.025  42.151   8.540  1.00 73.54           C  
ANISOU 2100  CD1 LEU A 263    13400   6327   8214  -1682    548  -2930       C  
ATOM   2101  CD2 LEU A 263      -2.220  40.582   9.227  1.00 74.85           C  
ANISOU 2101  CD2 LEU A 263    13510   6971   7957  -1894    -48  -2543       C  
ATOM   2102  N   LEU A 264      -6.704  38.766   9.577  1.00 76.02           N  
ANISOU 2102  N   LEU A 264    13800   7092   7992  -1404    874  -2510       N  
ATOM   2103  CA  LEU A 264      -7.401  37.852   8.700  1.00 71.18           C  
ANISOU 2103  CA  LEU A 264    12993   6432   7616  -1162    933  -2269       C  
ATOM   2104  C   LEU A 264      -8.837  38.284   8.465  1.00 69.81           C  
ANISOU 2104  C   LEU A 264    12795   6059   7668  -1013   1289  -2423       C  
ATOM   2105  O   LEU A 264      -9.272  38.365   7.319  1.00 66.97           O  
ANISOU 2105  O   LEU A 264    12241   5530   7672   -812   1324  -2332       O  
ATOM   2106  CB  LEU A 264      -7.362  36.449   9.285  1.00 71.63           C  
ANISOU 2106  CB  LEU A 264    13073   6733   7407  -1193    830  -2024       C  
ATOM   2107  CG  LEU A 264      -8.074  35.369   8.440  1.00 70.11           C  
ANISOU 2107  CG  LEU A 264    12683   6494   7459   -968    888  -1787       C  
ATOM   2108  CD1 LEU A 264      -7.472  35.208   7.050  1.00 67.05           C  
ANISOU 2108  CD1 LEU A 264    12069   6004   7400   -820    709  -1621       C  
ATOM   2109  CD2 LEU A 264      -8.068  34.024   9.151  1.00 70.79           C  
ANISOU 2109  CD2 LEU A 264    12804   6790   7300  -1016    822  -1553       C  
ATOM   2110  N   SER A 265      -9.557  38.592   9.543  1.00 71.92           N  
ANISOU 2110  N   SER A 265    13255   6346   7723  -1121   1552  -2655       N  
ATOM   2111  CA  SER A 265     -10.954  38.982   9.424  1.00 71.92           C  
ANISOU 2111  CA  SER A 265    13207   6145   7973   -982   1921  -2800       C  
ATOM   2112  C   SER A 265     -11.062  40.200   8.531  1.00 71.55           C  
ANISOU 2112  C   SER A 265    13038   5800   8348   -868   1989  -2924       C  
ATOM   2113  O   SER A 265     -11.986  40.314   7.710  1.00 69.79           O  
ANISOU 2113  O   SER A 265    12623   5391   8503   -658   2127  -2861       O  
ATOM   2114  CB  SER A 265     -11.556  39.260  10.769  1.00 75.74           C  
ANISOU 2114  CB  SER A 265    13938   6684   8157  -1144   2227  -3072       C  
ATOM   2115  OG  SER A 265     -11.160  40.553  11.208  1.00 80.00           O  
ANISOU 2115  OG  SER A 265    14637   7106   8653  -1298   2309  -3406       O  
ATOM   2116  N   LYS A 266     -10.091  41.104   8.656  1.00 73.33           N  
ANISOU 2116  N   LYS A 266    13357   5977   8527  -1010   1870  -3074       N  
ATOM   2117  CA  LYS A 266     -10.098  42.333   7.868  1.00 73.36           C  
ANISOU 2117  CA  LYS A 266    13256   5677   8938   -922   1941  -3180       C  
ATOM   2118  C   LYS A 266      -9.750  42.100   6.404  1.00 69.98           C  
ANISOU 2118  C   LYS A 266    12588   5190   8811   -735   1716  -2873       C  
ATOM   2119  O   LYS A 266     -10.144  42.906   5.539  1.00 70.76           O  
ANISOU 2119  O   LYS A 266    12551   5034   9301   -588   1807  -2863       O  
ATOM   2120  CB  LYS A 266      -9.167  43.340   8.462  1.00 76.04           C  
ANISOU 2120  CB  LYS A 266    13766   5971   9155  -1150   1893  -3442       C  
ATOM   2121  CG  LYS A 266      -9.680  43.873   9.760  1.00 81.19           C  
ANISOU 2121  CG  LYS A 266    14664   6605   9577  -1327   2194  -3820       C  
ATOM   2122  CD  LYS A 266      -8.626  44.749  10.397  1.00 84.85           C  
ANISOU 2122  CD  LYS A 266    15313   7069   9856  -1602   2087  -4092       C  
ATOM   2123  CE  LYS A 266      -9.198  45.635  11.487  1.00 90.14           C  
ANISOU 2123  CE  LYS A 266    16225   7616  10408  -1771   2458  -4554       C  
ATOM   2124  NZ  LYS A 266      -9.359  44.852  12.727  1.00 92.85           N  
ANISOU 2124  NZ  LYS A 266    16818   8288  10173  -1958   2498  -4631       N  
ATOM   2125  N   MET A 267      -8.953  41.062   6.125  1.00 66.57           N  
ANISOU 2125  N   MET A 267    12108   4981   8202   -750   1428  -2624       N  
ATOM   2126  CA  MET A 267      -8.682  40.673   4.745  1.00 62.65           C  
ANISOU 2126  CA  MET A 267    11403   4456   7943   -581   1251  -2346       C  
ATOM   2127  C   MET A 267      -9.863  39.993   4.073  1.00 60.73           C  
ANISOU 2127  C   MET A 267    11010   4186   7877   -374   1350  -2199       C  
ATOM   2128  O   MET A 267      -9.894  39.915   2.890  1.00 58.49           O  
ANISOU 2128  O   MET A 267    10570   3839   7811   -233   1258  -2024       O  
ATOM   2129  CB  MET A 267      -7.511  39.735   4.680  1.00 61.49           C  
ANISOU 2129  CB  MET A 267    11238   4529   7596   -656    960  -2148       C  
ATOM   2130  CG  MET A 267      -6.181  40.431   4.662  1.00 62.27           C  
ANISOU 2130  CG  MET A 267    11360   4608   7690   -799    782  -2187       C  
ATOM   2131  SD  MET A 267      -4.921  39.337   5.310  1.00 63.14           S  
ANISOU 2131  SD  MET A 267    11493   5012   7483   -959    476  -2023       S  
ATOM   2132  CE  MET A 267      -3.388  39.954   4.661  1.00 62.15           C  
ANISOU 2132  CE  MET A 267    11257   4822   7532  -1037    251  -1957       C  
ATOM   2133  N   LEU A 268     -10.831  39.519   4.830  1.00 61.93           N  
ANISOU 2133  N   LEU A 268    11210   4390   7929   -371   1539  -2273       N  
ATOM   2134  CA  LEU A 268     -11.998  38.850   4.275  1.00 60.65           C  
ANISOU 2134  CA  LEU A 268    10885   4200   7957   -196   1631  -2147       C  
ATOM   2135  C   LEU A 268     -13.323  39.597   4.501  1.00 62.59           C  
ANISOU 2135  C   LEU A 268    11085   4239   8458   -109   1948  -2312       C  
ATOM   2136  O   LEU A 268     -14.402  38.977   4.596  1.00 62.14           O  
ANISOU 2136  O   LEU A 268    10933   4190   8486    -25   2091  -2273       O  
ATOM   2137  CB  LEU A 268     -12.099  37.467   4.912  1.00 60.89           C  
ANISOU 2137  CB  LEU A 268    10958   4453   7722   -250   1603  -2043       C  
ATOM   2138  CG  LEU A 268     -10.883  36.554   4.785  1.00 59.08           C  
ANISOU 2138  CG  LEU A 268    10743   4416   7286   -321   1315  -1852       C  
ATOM   2139  CD1 LEU A 268     -11.094  35.282   5.591  1.00 59.19           C  
ANISOU 2139  CD1 LEU A 268    10808   4615   7067   -379   1332  -1747       C  
ATOM   2140  CD2 LEU A 268     -10.601  36.227   3.335  1.00 56.20           C  
ANISOU 2140  CD2 LEU A 268    10194   4009   7148   -183   1138  -1662       C  
ATOM   2141  N   ILE A 269     -13.245  40.919   4.605  1.00 63.37           N  
ANISOU 2141  N   ILE A 269    11231   4131   8717   -131   2073  -2498       N  
ATOM   2142  CA  ILE A 269     -14.437  41.719   4.597  1.00 64.86           C  
ANISOU 2142  CA  ILE A 269    11319   4065   9258    -13   2366  -2621       C  
ATOM   2143  C   ILE A 269     -15.071  41.612   3.208  1.00 62.26           C  
ANISOU 2143  C   ILE A 269    10717   3638   9299    208   2250  -2364       C  
ATOM   2144  O   ILE A 269     -14.342  41.644   2.194  1.00 59.16           O  
ANISOU 2144  O   ILE A 269    10266   3271   8939    247   1990  -2179       O  
ATOM   2145  CB  ILE A 269     -14.091  43.189   4.972  1.00 68.62           C  
ANISOU 2145  CB  ILE A 269    11904   4306   9861    -93   2523  -2879       C  
ATOM   2146  CG1 ILE A 269     -13.671  43.258   6.477  1.00 70.97           C  
ANISOU 2146  CG1 ILE A 269    12494   4724   9748   -342   2667  -3184       C  
ATOM   2147  CG2 ILE A 269     -15.273  44.144   4.695  1.00 71.06           C  
ANISOU 2147  CG2 ILE A 269    12046   4280  10673     74   2813  -2955       C  
ATOM   2148  CD1 ILE A 269     -12.871  44.472   6.874  1.00 72.44           C  
ANISOU 2148  CD1 ILE A 269    12835   4761   9926   -500   2704  -3444       C  
ATOM   2149  N   TYR A 270     -16.397  41.485   3.174  1.00 63.23           N  
ANISOU 2149  N   TYR A 270    10675   3661   9686    337   2441  -2352       N  
ATOM   2150  CA  TYR A 270     -17.133  41.315   1.930  1.00 63.76           C  
ANISOU 2150  CA  TYR A 270    10472   3665  10087    529   2309  -2106       C  
ATOM   2151  C   TYR A 270     -16.993  42.547   1.048  1.00 65.81           C  
ANISOU 2151  C   TYR A 270    10635   3692  10678    630   2251  -2028       C  
ATOM   2152  O   TYR A 270     -16.386  42.483  -0.027  1.00 65.55           O  
ANISOU 2152  O   TYR A 270    10558   3723  10626    668   1974  -1815       O  
ATOM   2153  CB  TYR A 270     -18.611  41.020   2.184  1.00 65.81           C  
ANISOU 2153  CB  TYR A 270    10548   3844  10613    633   2537  -2121       C  
ATOM   2154  CG  TYR A 270     -18.967  39.593   2.535  1.00 66.93           C  
ANISOU 2154  CG  TYR A 270    10680   4208  10539    589   2521  -2065       C  
ATOM   2155  CD1 TYR A 270     -18.512  38.492   1.735  1.00 66.17           C  
ANISOU 2155  CD1 TYR A 270    10544   4322  10275    587   2200  -1853       C  
ATOM   2156  CD2 TYR A 270     -19.816  39.298   3.591  1.00 69.86           C  
ANISOU 2156  CD2 TYR A 270    11065   4563  10913    554   2845  -2214       C  
ATOM   2157  CE1 TYR A 270     -18.868  37.182   2.033  1.00 65.19           C  
ANISOU 2157  CE1 TYR A 270    10394   4361  10014    549   2201  -1797       C  
ATOM   2158  CE2 TYR A 270     -20.185  37.989   3.894  1.00 69.66           C  
ANISOU 2158  CE2 TYR A 270    11016   4719  10733    515   2846  -2135       C  
ATOM   2159  CZ  TYR A 270     -19.705  36.937   3.124  1.00 68.05           C  
ANISOU 2159  CZ  TYR A 270    10768   4698  10388    513   2518  -1925       C  
ATOM   2160  OH  TYR A 270     -20.039  35.614   3.434  1.00 69.87           O  
ANISOU 2160  OH  TYR A 270    10971   5077  10499    468   2530  -1846       O  
ATOM   2161  N   ASP A 271     -17.502  43.678   1.540  1.00 70.34           N  
ANISOU 2161  N   ASP A 271    11189   3987  11548    663   2537  -2207       N  
ATOM   2162  CA  ASP A 271     -17.442  44.976   0.879  1.00 72.23           C  
ANISOU 2162  CA  ASP A 271    11333   3941  12167    759   2548  -2147       C  
ATOM   2163  C   ASP A 271     -15.990  45.350   0.544  1.00 71.70           C  
ANISOU 2163  C   ASP A 271    11430   3925  11887    646   2340  -2118       C  
ATOM   2164  O   ASP A 271     -15.165  45.498   1.441  1.00 71.64           O  
ANISOU 2164  O   ASP A 271    11645   3965  11608    464   2407  -2354       O  
ATOM   2165  CB  ASP A 271     -18.020  46.000   1.812  1.00 76.45           C  
ANISOU 2165  CB  ASP A 271    11889   4176  12981    756   2951  -2436       C  
ATOM   2166  CG  ASP A 271     -18.164  47.409   1.182  1.00 79.54           C  
ANISOU 2166  CG  ASP A 271    12137   4195  13889    883   3023  -2367       C  
ATOM   2167  OD1 ASP A 271     -17.850  47.623  -0.035  1.00 78.58           O  
ANISOU 2167  OD1 ASP A 271    11896   4060  13898    979   2743  -2054       O  
ATOM   2168  OD2 ASP A 271     -18.635  48.268   1.960  1.00 81.07           O  
ANISOU 2168  OD2 ASP A 271    12343   4105  14355    880   3390  -2633       O  
ATOM   2169  N   PRO A 272     -15.652  45.419  -0.762  1.00 71.16           N  
ANISOU 2169  N   PRO A 272    11250   3874  11911    738   2072  -1818       N  
ATOM   2170  CA  PRO A 272     -14.242  45.649  -1.203  1.00 68.89           C  
ANISOU 2170  CA  PRO A 272    11092   3653  11429    634   1875  -1752       C  
ATOM   2171  C   PRO A 272     -13.712  47.054  -0.872  1.00 68.74           C  
ANISOU 2171  C   PRO A 272    11149   3342  11626    570   2032  -1912       C  
ATOM   2172  O   PRO A 272     -12.537  47.234  -0.562  1.00 66.89           O  
ANISOU 2172  O   PRO A 272    11074   3157  11182    406   1968  -2020       O  
ATOM   2173  CB  PRO A 272     -14.292  45.429  -2.737  1.00 68.29           C  
ANISOU 2173  CB  PRO A 272    10861   3644  11439    767   1612  -1384       C  
ATOM   2174  CG  PRO A 272     -15.642  44.896  -3.057  1.00 68.49           C  
ANISOU 2174  CG  PRO A 272    10691   3699  11632    913   1608  -1266       C  
ATOM   2175  CD  PRO A 272     -16.548  45.074  -1.889  1.00 71.10           C  
ANISOU 2175  CD  PRO A 272    10999   3888  12125    919   1916  -1517       C  
ATOM   2176  N   ALA A 273     -14.608  48.024  -0.913  1.00 70.66           N  
ANISOU 2176  N   ALA A 273    11257   3265  12322    697   2245  -1930       N  
ATOM   2177  CA  ALA A 273     -14.307  49.419  -0.476  1.00 72.12           C  
ANISOU 2177  CA  ALA A 273    11500   3101  12800    642   2470  -2133       C  
ATOM   2178  C   ALA A 273     -13.885  49.458   0.993  1.00 72.69           C  
ANISOU 2178  C   ALA A 273    11814   3205  12599    420   2671  -2569       C  
ATOM   2179  O   ALA A 273     -13.044  50.249   1.348  1.00 72.82           O  
ANISOU 2179  O   ALA A 273    11959   3083  12623    274   2721  -2754       O  
ATOM   2180  CB  ALA A 273     -15.505  50.298  -0.669  1.00 74.70           C  
ANISOU 2180  CB  ALA A 273    11612   3069  13698    835   2701  -2084       C  
ATOM   2181  N   LYS A 274     -14.424  48.542   1.802  1.00 72.38           N  
ANISOU 2181  N   LYS A 274    11839   3373  12286    378   2758  -2712       N  
ATOM   2182  CA  LYS A 274     -14.172  48.479   3.242  1.00 74.28           C  
ANISOU 2182  CA  LYS A 274    12327   3690  12205    161   2953  -3107       C  
ATOM   2183  C   LYS A 274     -13.049  47.473   3.615  1.00 70.89           C  
ANISOU 2183  C   LYS A 274    12087   3650  11197    -32   2676  -3100       C  
ATOM   2184  O   LYS A 274     -12.622  47.357   4.751  1.00 70.89           O  
ANISOU 2184  O   LYS A 274    12309   3774  10849   -244   2747  -3375       O  
ATOM   2185  CB  LYS A 274     -15.491  48.104   3.926  1.00 77.40           C  
ANISOU 2185  CB  LYS A 274    12674   4065  12667    235   3252  -3238       C  
ATOM   2186  CG  LYS A 274     -15.895  48.910   5.174  1.00 82.95           C  
ANISOU 2186  CG  LYS A 274    13527   4546  13442    120   3689  -3682       C  
ATOM   2187  CD  LYS A 274     -17.284  49.556   5.055  1.00 87.04           C  
ANISOU 2187  CD  LYS A 274    13812   4706  14552    332   4045  -3708       C  
ATOM   2188  CE  LYS A 274     -17.386  50.816   5.899  1.00 93.17           C  
ANISOU 2188  CE  LYS A 274    14706   5120  15571    238   4464  -4131       C  
ATOM   2189  NZ  LYS A 274     -18.749  51.429   5.862  1.00 97.45           N  
ANISOU 2189  NZ  LYS A 274    14999   5286  16739    451   4857  -4168       N  
ATOM   2190  N   ARG A 275     -12.609  46.662   2.663  1.00 68.08           N  
ANISOU 2190  N   ARG A 275    11636   3502  10729     37   2358  -2772       N  
ATOM   2191  CA  ARG A 275     -11.657  45.571   2.988  1.00 65.18           C  
ANISOU 2191  CA  ARG A 275    11398   3487   9879   -112   2112  -2726       C  
ATOM   2192  C   ARG A 275     -10.326  46.268   3.147  1.00 66.52           C  
ANISOU 2192  C   ARG A 275    11685   3618   9968   -292   1996  -2832       C  
ATOM   2193  O   ARG A 275     -10.078  47.298   2.507  1.00 67.65           O  
ANISOU 2193  O   ARG A 275    11756   3508  10437   -248   2016  -2797       O  
ATOM   2194  CB  ARG A 275     -11.594  44.527   1.908  1.00 60.55           C  
ANISOU 2194  CB  ARG A 275    10669   3094   9243     14   1853  -2380       C  
ATOM   2195  CG  ARG A 275     -10.754  43.287   2.238  1.00 58.03           C  
ANISOU 2195  CG  ARG A 275    10442   3104   8500   -107   1635  -2311       C  
ATOM   2196  CD  ARG A 275     -10.747  42.242   1.076  1.00 53.71           C  
ANISOU 2196  CD  ARG A 275     9746   2710   7948     24   1419  -1998       C  
ATOM   2197  NE  ARG A 275     -12.110  41.870   0.709  1.00 52.66           N  
ANISOU 2197  NE  ARG A 275     9472   2540   7996    189   1519  -1917       N  
ATOM   2198  CZ  ARG A 275     -12.534  41.647  -0.536  1.00 51.20           C  
ANISOU 2198  CZ  ARG A 275     9119   2344   7989    342   1401  -1688       C  
ATOM   2199  NH1 ARG A 275     -11.710  41.651  -1.599  1.00 49.39           N  
ANISOU 2199  NH1 ARG A 275     8860   2157   7748    359   1199  -1502       N  
ATOM   2200  NH2 ARG A 275     -13.827  41.413  -0.741  1.00 51.82           N  
ANISOU 2200  NH2 ARG A 275     9052   2375   8259    471   1488  -1640       N  
ATOM   2201  N   ILE A 276      -9.505  45.729   4.037  1.00 66.35           N  
ANISOU 2201  N   ILE A 276    11836   3838   9535   -502   1877  -2952       N  
ATOM   2202  CA  ILE A 276      -8.161  46.260   4.304  1.00 66.77           C  
ANISOU 2202  CA  ILE A 276    11990   3900   9478   -709   1721  -3058       C  
ATOM   2203  C   ILE A 276      -7.323  46.352   3.031  1.00 64.70           C  
ANISOU 2203  C   ILE A 276    11573   3601   9408   -631   1500  -2770       C  
ATOM   2204  O   ILE A 276      -7.581  45.662   2.051  1.00 61.37           O  
ANISOU 2204  O   ILE A 276    11011   3259   9047   -456   1400  -2480       O  
ATOM   2205  CB  ILE A 276      -7.432  45.426   5.362  1.00 66.41           C  
ANISOU 2205  CB  ILE A 276    12111   4179   8939   -930   1553  -3140       C  
ATOM   2206  CG1 ILE A 276      -6.332  46.232   6.019  1.00 68.07           C  
ANISOU 2206  CG1 ILE A 276    12456   4359   9047  -1192   1466  -3377       C  
ATOM   2207  CG2 ILE A 276      -6.855  44.139   4.745  1.00 63.39           C  
ANISOU 2207  CG2 ILE A 276    11620   4060   8404   -864   1263  -2797       C  
ATOM   2208  CD1 ILE A 276      -5.905  45.683   7.342  1.00 69.53           C  
ANISOU 2208  CD1 ILE A 276    12849   4833   8734  -1440   1363  -3539       C  
ATOM   2209  N   SER A 277      -6.402  47.300   3.041  1.00 66.53           N  
ANISOU 2209  N   SER A 277    11834   3682   9761   -768   1461  -2875       N  
ATOM   2210  CA  SER A 277      -5.499  47.509   1.933  1.00 65.65           C  
ANISOU 2210  CA  SER A 277    11593   3519   9832   -729   1291  -2627       C  
ATOM   2211  C   SER A 277      -4.220  46.789   2.281  1.00 65.66           C  
ANISOU 2211  C   SER A 277    11627   3787   9534   -906   1023  -2586       C  
ATOM   2212  O   SER A 277      -4.000  46.425   3.440  1.00 66.43           O  
ANISOU 2212  O   SER A 277    11862   4061   9315  -1085    967  -2777       O  
ATOM   2213  CB  SER A 277      -5.230  48.983   1.784  1.00 67.85           C  
ANISOU 2213  CB  SER A 277    11862   3448  10468   -785   1423  -2759       C  
ATOM   2214  OG  SER A 277      -4.219  49.363   2.693  1.00 70.39           O  
ANISOU 2214  OG  SER A 277    12304   3797  10643  -1061   1344  -3016       O  
ATOM   2215  N   GLY A 278      -3.369  46.599   1.283  1.00 65.23           N  
ANISOU 2215  N   GLY A 278    11440   3759   9582   -863    864  -2326       N  
ATOM   2216  CA  GLY A 278      -2.047  46.043   1.508  1.00 66.06           C  
ANISOU 2216  CA  GLY A 278    11522   4065   9511  -1022    620  -2264       C  
ATOM   2217  C   GLY A 278      -1.240  46.834   2.528  1.00 71.85           C  
ANISOU 2217  C   GLY A 278    12352   4747  10199  -1297    562  -2543       C  
ATOM   2218  O   GLY A 278      -0.641  46.222   3.418  1.00 72.78           O  
ANISOU 2218  O   GLY A 278    12531   5104  10019  -1469    373  -2606       O  
ATOM   2219  N   LYS A 279      -1.233  48.184   2.405  1.00 75.65           N  
ANISOU 2219  N   LYS A 279    12843   4915  10983  -1348    713  -2704       N  
ATOM   2220  CA  LYS A 279      -0.438  49.064   3.262  1.00 80.47           C  
ANISOU 2220  CA  LYS A 279    13536   5432  11606  -1629    667  -2999       C  
ATOM   2221  C   LYS A 279      -0.859  48.986   4.699  1.00 83.45           C  
ANISOU 2221  C   LYS A 279    14131   5937  11638  -1807    701  -3341       C  
ATOM   2222  O   LYS A 279      -0.015  48.902   5.586  1.00 87.49           O  
ANISOU 2222  O   LYS A 279    14721   6618  11903  -2069    498  -3494       O  
ATOM   2223  CB  LYS A 279      -0.584  50.524   2.868  1.00 85.68           C  
ANISOU 2223  CB  LYS A 279    14174   5681  12697  -1627    886  -3126       C  
ATOM   2224  CG  LYS A 279       0.037  50.911   1.548  1.00 86.70           C  
ANISOU 2224  CG  LYS A 279    14114   5642  13184  -1523    866  -2821       C  
ATOM   2225  CD  LYS A 279      -0.832  51.948   0.829  1.00 90.25           C  
ANISOU 2225  CD  LYS A 279    14526   5718  14047  -1345   1143  -2777       C  
ATOM   2226  CE  LYS A 279      -0.261  52.355  -0.546  1.00 91.67           C  
ANISOU 2226  CE  LYS A 279    14537   5738  14555  -1239   1139  -2429       C  
ATOM   2227  NZ  LYS A 279       0.945  53.238  -0.494  1.00 94.16           N  
ANISOU 2227  NZ  LYS A 279    14797   5863  15114  -1458   1102  -2514       N  
ATOM   2228  N   MET A 280      -2.156  49.097   4.945  1.00 83.59           N  
ANISOU 2228  N   MET A 280    14245   5863  11651  -1683    966  -3470       N  
ATOM   2229  CA  MET A 280      -2.689  49.021   6.314  1.00 86.59           C  
ANISOU 2229  CA  MET A 280    14855   6361  11681  -1845   1068  -3808       C  
ATOM   2230  C   MET A 280      -2.309  47.705   6.964  1.00 85.60           C  
ANISOU 2230  C   MET A 280    14792   6658  11072  -1936    809  -3687       C  
ATOM   2231  O   MET A 280      -1.873  47.673   8.131  1.00 89.19           O  
ANISOU 2231  O   MET A 280    15425   7297  11165  -2206    695  -3916       O  
ATOM   2232  CB  MET A 280      -4.201  49.028   6.338  1.00 87.95           C  
ANISOU 2232  CB  MET A 280    15068   6411  11935  -1644   1397  -3873       C  
ATOM   2233  CG  MET A 280      -4.982  49.950   5.456  1.00 89.87           C  
ANISOU 2233  CG  MET A 280    15184   6265  12695  -1426   1663  -3834       C  
ATOM   2234  SD  MET A 280      -5.261  51.588   6.150  1.00103.38           S  
ANISOU 2234  SD  MET A 280    17023   7556  14698  -1578   2003  -4316       S  
ATOM   2235  CE  MET A 280      -4.051  51.871   7.465  1.00104.15           C  
ANISOU 2235  CE  MET A 280    17354   7815  14400  -2018   1828  -4714       C  
ATOM   2236  N   ALA A 281      -2.506  46.622   6.216  1.00 80.54           N  
ANISOU 2236  N   ALA A 281    14009   6166  10424  -1717    719  -3327       N  
ATOM   2237  CA  ALA A 281      -2.199  45.313   6.696  1.00 79.44           C  
ANISOU 2237  CA  ALA A 281    13891   6382   9910  -1761    494  -3156       C  
ATOM   2238  C   ALA A 281      -0.755  45.236   7.187  1.00 80.93           C  
ANISOU 2238  C   ALA A 281    14069   6745   9936  -2014    158  -3145       C  
ATOM   2239  O   ALA A 281      -0.487  44.648   8.219  1.00 82.13           O  
ANISOU 2239  O   ALA A 281    14345   7168   9692  -2190     -8  -3184       O  
ATOM   2240  CB  ALA A 281      -2.465  44.277   5.614  1.00 76.79           C  
ANISOU 2240  CB  ALA A 281    13369   6113   9692  -1493    452  -2781       C  
ATOM   2241  N   LEU A 282       0.175  45.868   6.488  1.00 81.09           N  
ANISOU 2241  N   LEU A 282    13937   6607  10264  -2047     55  -3086       N  
ATOM   2242  CA  LEU A 282       1.564  45.920   6.991  1.00 84.25           C  
ANISOU 2242  CA  LEU A 282    14296   7145  10568  -2311   -267  -3099       C  
ATOM   2243  C   LEU A 282       1.770  46.655   8.354  1.00 89.17           C  
ANISOU 2243  C   LEU A 282    15149   7819  10910  -2651   -320  -3503       C  
ATOM   2244  O   LEU A 282       2.815  46.479   8.971  1.00 92.38           O  
ANISOU 2244  O   LEU A 282    15541   8425  11133  -2892   -644  -3499       O  
ATOM   2245  CB  LEU A 282       2.487  46.543   5.953  1.00 83.42           C  
ANISOU 2245  CB  LEU A 282    13971   6827  10897  -2287   -321  -2971       C  
ATOM   2246  CG  LEU A 282       2.784  45.687   4.735  1.00 80.12           C  
ANISOU 2246  CG  LEU A 282    13323   6446  10672  -2048   -371  -2566       C  
ATOM   2247  CD1 LEU A 282       3.142  46.518   3.529  1.00 79.74           C  
ANISOU 2247  CD1 LEU A 282    13119   6109  11067  -1954   -249  -2471       C  
ATOM   2248  CD2 LEU A 282       3.931  44.753   5.040  1.00 81.39           C  
ANISOU 2248  CD2 LEU A 282    13349   6869  10705  -2158   -707  -2361       C  
ATOM   2249  N   ASN A 283       0.791  47.431   8.822  1.00 90.15           N  
ANISOU 2249  N   ASN A 283    15477   7773  11001  -2677     -9  -3846       N  
ATOM   2250  CA  ASN A 283       0.847  48.051  10.157  1.00 94.71           C  
ANISOU 2250  CA  ASN A 283    16320   8414  11250  -3007     -6  -4275       C  
ATOM   2251  C   ASN A 283       0.076  47.290  11.256  1.00 95.45           C  
ANISOU 2251  C   ASN A 283    16663   8800  10804  -3069     52  -4366       C  
ATOM   2252  O   ASN A 283       0.006  47.788  12.397  1.00 99.98           O  
ANISOU 2252  O   ASN A 283    17502   9445  11041  -3350    100  -4749       O  
ATOM   2253  CB  ASN A 283       0.311  49.502  10.120  1.00 97.74           C  
ANISOU 2253  CB  ASN A 283    16797   8391  11948  -3043    348  -4669       C  
ATOM   2254  CG  ASN A 283       1.041  50.374   9.128  1.00 97.46           C  
ANISOU 2254  CG  ASN A 283    16541   8040  12445  -3012    322  -4597       C  
ATOM   2255  OD1 ASN A 283       2.258  50.262   8.981  1.00 98.57           O  
ANISOU 2255  OD1 ASN A 283    16541   8284  12625  -3151      0  -4458       O  
ATOM   2256  ND2 ASN A 283       0.287  51.136   8.347  1.00 95.94           N  
ANISOU 2256  ND2 ASN A 283    16285   7473  12694  -2798    657  -4618       N  
ATOM   2257  N   HIS A 284      -0.525  46.133  10.947  1.00 90.47           N  
ANISOU 2257  N   HIS A 284    15966   8325  10081  -2828     76  -4045       N  
ATOM   2258  CA  HIS A 284      -1.304  45.410  11.957  1.00 91.17           C  
ANISOU 2258  CA  HIS A 284    16281   8668   9688  -2878    171  -4103       C  
ATOM   2259  C   HIS A 284      -0.432  44.882  13.115  1.00 94.49           C  
ANISOU 2259  C   HIS A 284    16849   9480   9570  -3194   -197  -4093       C  
ATOM   2260  O   HIS A 284       0.683  44.424  12.896  1.00 93.46           O  
ANISOU 2260  O   HIS A 284    16543   9497   9470  -3249   -584  -3823       O  
ATOM   2261  CB  HIS A 284      -2.051  44.241  11.345  1.00 86.82           C  
ANISOU 2261  CB  HIS A 284    15599   8190   9197  -2568    249  -3740       C  
ATOM   2262  CG  HIS A 284      -3.249  43.826  12.121  1.00 87.07           C  
ANISOU 2262  CG  HIS A 284    15836   8322   8921  -2546    529  -3855       C  
ATOM   2263  ND1 HIS A 284      -3.179  42.961  13.184  1.00 88.67           N  
ANISOU 2263  ND1 HIS A 284    16216   8878   8597  -2708    393  -3786       N  
ATOM   2264  CD2 HIS A 284      -4.550  44.180  12.007  1.00 86.61           C  
ANISOU 2264  CD2 HIS A 284    15826   8052   9028  -2386    950  -4023       C  
ATOM   2265  CE1 HIS A 284      -4.389  42.782  13.686  1.00 89.67           C  
ANISOU 2265  CE1 HIS A 284    16503   9007   8560  -2653    741  -3914       C  
ATOM   2266  NE2 HIS A 284      -5.241  43.506  12.983  1.00 88.31           N  
ANISOU 2266  NE2 HIS A 284    16241   8489   8820  -2453   1085  -4065       N  
ATOM   2267  N   PRO A 285      -0.930  44.959  14.348  1.00 98.89           N  
ANISOU 2267  N   PRO A 285    17725  10207   9639  -3410    -76  -4378       N  
ATOM   2268  CA  PRO A 285      -0.166  44.513  15.522  1.00103.55           C  
ANISOU 2268  CA  PRO A 285    18493  11197   9651  -3739   -438  -4370       C  
ATOM   2269  C   PRO A 285       0.546  43.164  15.371  1.00102.75           C  
ANISOU 2269  C   PRO A 285    18196  11392   9453  -3664   -848  -3835       C  
ATOM   2270  O   PRO A 285       1.633  42.934  15.952  1.00103.86           O  
ANISOU 2270  O   PRO A 285    18330  11798   9335  -3913  -1287  -3727       O  
ATOM   2271  CB  PRO A 285      -1.251  44.416  16.613  1.00106.63           C  
ANISOU 2271  CB  PRO A 285    19240  11726   9548  -3844   -117  -4630       C  
ATOM   2272  CG  PRO A 285      -2.549  44.864  15.993  1.00104.13           C  
ANISOU 2272  CG  PRO A 285    18894  11049   9621  -3563    416  -4790       C  
ATOM   2273  CD  PRO A 285      -2.198  45.597  14.748  1.00100.95           C  
ANISOU 2273  CD  PRO A 285    18208  10281   9864  -3386    418  -4758       C  
ATOM   2274  N   TYR A 286      -0.141  42.255  14.658  1.00101.19           N  
ANISOU 2274  N   TYR A 286    17845  11146   9456  -3331   -692  -3514       N  
ATOM   2275  CA  TYR A 286       0.376  40.936  14.218  1.00 99.07           C  
ANISOU 2275  CA  TYR A 286    17333  11047   9260  -3171   -981  -2993       C  
ATOM   2276  C   TYR A 286       1.853  40.970  13.841  1.00 99.88           C  
ANISOU 2276  C   TYR A 286    17186  11184   9578  -3261  -1409  -2801       C  
ATOM   2277  O   TYR A 286       2.643  40.198  14.379  1.00101.98           O  
ANISOU 2277  O   TYR A 286    17399  11734   9614  -3386  -1786  -2526       O  
ATOM   2278  CB  TYR A 286      -0.440  40.401  13.048  1.00 95.32           C  
ANISOU 2278  CB  TYR A 286    16660  10360   9197  -2787   -715  -2783       C  
ATOM   2279  CG  TYR A 286      -0.051  38.985  12.617  1.00 93.02           C  
ANISOU 2279  CG  TYR A 286    16141  10212   8988  -2618   -939  -2292       C  
ATOM   2280  CD1 TYR A 286      -0.398  37.893  13.388  1.00 94.67           C  
ANISOU 2280  CD1 TYR A 286    16453  10678   8837  -2638   -986  -2078       C  
ATOM   2281  CD2 TYR A 286       0.686  38.764  11.451  1.00 90.16           C  
ANISOU 2281  CD2 TYR A 286    15464   9713   9078  -2448  -1078  -2050       C  
ATOM   2282  CE1 TYR A 286      -0.013  36.609  13.023  1.00 94.33           C  
ANISOU 2282  CE1 TYR A 286    16193  10730   8916  -2490  -1179  -1634       C  
ATOM   2283  CE2 TYR A 286       1.069  37.492  11.062  1.00 88.31           C  
ANISOU 2283  CE2 TYR A 286    15020   9578   8955  -2301  -1249  -1637       C  
ATOM   2284  CZ  TYR A 286       0.727  36.403  11.846  1.00 90.96           C  
ANISOU 2284  CZ  TYR A 286    15446  10146   8967  -2317  -1305  -1426       C  
ATOM   2285  OH  TYR A 286       1.091  35.112  11.507  1.00 87.13           O  
ANISOU 2285  OH  TYR A 286    14747   9728   8628  -2171  -1456  -1015       O  
ATOM   2286  N   PHE A 287       2.238  41.936  13.018  1.00 99.41           N  
ANISOU 2286  N   PHE A 287    16981  10837   9950  -3226  -1350  -2954       N  
ATOM   2287  CA  PHE A 287       3.640  42.120  12.698  1.00100.89           C  
ANISOU 2287  CA  PHE A 287    16930  11030  10372  -3339  -1716  -2819       C  
ATOM   2288  C   PHE A 287       4.308  43.004  13.746  1.00108.64           C  
ANISOU 2288  C   PHE A 287    18088  12128  11059  -3744  -1941  -3149       C  
ATOM   2289  O   PHE A 287       4.440  44.222  13.580  1.00111.23           O  
ANISOU 2289  O   PHE A 287    18451  12215  11595  -3859  -1822  -3494       O  
ATOM   2290  CB  PHE A 287       3.799  42.732  11.330  1.00 97.15           C  
ANISOU 2290  CB  PHE A 287    16219  10202  10490  -3134  -1548  -2806       C  
ATOM   2291  CG  PHE A 287       3.051  42.010  10.274  1.00 93.25           C  
ANISOU 2291  CG  PHE A 287    15590   9587  10252  -2766  -1308  -2552       C  
ATOM   2292  CD1 PHE A 287       3.519  40.813   9.780  1.00 90.55           C  
ANISOU 2292  CD1 PHE A 287    15020   9361  10022  -2609  -1484  -2138       C  
ATOM   2293  CD2 PHE A 287       1.856  42.515   9.791  1.00 92.30           C  
ANISOU 2293  CD2 PHE A 287    15565   9231  10272  -2585   -906  -2733       C  
ATOM   2294  CE1 PHE A 287       2.813  40.131   8.826  1.00 86.32           C  
ANISOU 2294  CE1 PHE A 287    14381   8721   9695  -2299  -1265  -1943       C  
ATOM   2295  CE2 PHE A 287       1.145  41.834   8.828  1.00 87.81           C  
ANISOU 2295  CE2 PHE A 287    14872   8575   9915  -2271   -721  -2504       C  
ATOM   2296  CZ  PHE A 287       1.618  40.638   8.357  1.00 85.39           C  
ANISOU 2296  CZ  PHE A 287    14368   8400   9676  -2139   -900  -2128       C  
ATOM   2297  N   ASN A 288       4.734  42.395  14.838  1.00113.45           N  
ANISOU 2297  N   ASN A 288    18814  13108  11184  -3976  -2276  -3042       N  
ATOM   2298  CA  ASN A 288       5.678  43.055  15.725  1.00119.59           C  
ANISOU 2298  CA  ASN A 288    19682  14050  11707  -4383  -2630  -3262       C  
ATOM   2299  C   ASN A 288       6.911  42.195  16.021  1.00122.95           C  
ANISOU 2299  C   ASN A 288    19874  14775  12064  -4498  -3193  -2837       C  
ATOM   2300  O   ASN A 288       7.609  42.469  16.979  1.00129.14           O  
ANISOU 2300  O   ASN A 288    20762  15806  12499  -4859  -3560  -2950       O  
ATOM   2301  CB  ASN A 288       4.956  43.481  17.008  1.00123.21           C  
ANISOU 2301  CB  ASN A 288    20592  14684  11537  -4659  -2492  -3673       C  
ATOM   2302  CG  ASN A 288       3.998  44.642  16.784  1.00121.64           C  
ANISOU 2302  CG  ASN A 288    20583  14132  11501  -4617  -1971  -4174       C  
ATOM   2303  OD1 ASN A 288       4.178  45.430  15.870  1.00118.22           O  
ANISOU 2303  OD1 ASN A 288    19965  13346  11605  -4507  -1832  -4281       O  
ATOM   2304  ND2 ASN A 288       2.979  44.751  17.624  1.00122.58           N  
ANISOU 2304  ND2 ASN A 288    21065  14336  11175  -4704  -1667  -4465       N  
ATOM   2305  N   ASP A 289       7.184  41.168  15.205  1.00120.76           N  
ANISOU 2305  N   ASP A 289    19276  14472  12133  -4203  -3263  -2357       N  
ATOM   2306  CA  ASP A 289       8.264  40.209  15.495  1.00121.98           C  
ANISOU 2306  CA  ASP A 289    19180  14892  12271  -4268  -3763  -1899       C  
ATOM   2307  C   ASP A 289       8.671  39.392  14.261  1.00115.00           C  
ANISOU 2307  C   ASP A 289    17883  13829  11982  -3919  -3736  -1470       C  
ATOM   2308  O   ASP A 289       9.694  39.690  13.659  1.00112.06           O  
ANISOU 2308  O   ASP A 289    17199  13327  12051  -3933  -3908  -1384       O  
ATOM   2309  CB  ASP A 289       7.930  39.308  16.735  1.00125.71           C  
ANISOU 2309  CB  ASP A 289    19897  15770  12094  -4404  -3959  -1714       C  
ATOM   2310  CG  ASP A 289       6.400  39.131  17.005  1.00125.22           C  
ANISOU 2310  CG  ASP A 289    20189  15699  11690  -4276  -3487  -1891       C  
ATOM   2311  OD1 ASP A 289       5.731  40.097  17.423  1.00125.60           O  
ANISOU 2311  OD1 ASP A 289    20554  15682  11486  -4427  -3217  -2376       O  
ATOM   2312  OD2 ASP A 289       5.858  38.012  16.858  1.00123.66           O  
ANISOU 2312  OD2 ASP A 289    19948  15555  11480  -4037  -3378  -1552       O  
TER    2313      ASP A 289                                                      
ATOM   2314  N   GLN B   5     -20.835  10.306 -15.197  1.00103.21           N  
ANISOU 2314  N   GLN B   5    13320  10406  15487   2347    566  -3656       N  
ATOM   2315  CA  GLN B   5     -21.895  10.124 -14.146  1.00 99.25           C  
ANISOU 2315  CA  GLN B   5    12903   9591  15214   2187    258  -3398       C  
ATOM   2316  C   GLN B   5     -22.046  11.270 -13.147  1.00 88.72           C  
ANISOU 2316  C   GLN B   5    11419   8417  13870   2056    139  -2924       C  
ATOM   2317  O   GLN B   5     -21.142  12.034 -12.896  1.00 84.16           O  
ANISOU 2317  O   GLN B   5    10640   8077  13259   2125    247  -2744       O  
ATOM   2318  CB  GLN B   5     -21.653   8.836 -13.367  1.00106.12           C  
ANISOU 2318  CB  GLN B   5    13807   9937  16574   2391    212  -3445       C  
ATOM   2319  CG  GLN B   5     -21.724   7.609 -14.266  1.00118.29           C  
ANISOU 2319  CG  GLN B   5    15568  11181  18196   2486    321  -3959       C  
ATOM   2320  CD  GLN B   5     -22.471   6.424 -13.654  1.00124.45           C  
ANISOU 2320  CD  GLN B   5    16558  11359  19366   2430    146  -3992       C  
ATOM   2321  OE1 GLN B   5     -22.891   6.457 -12.485  1.00121.91           O  
ANISOU 2321  OE1 GLN B   5    16211  10853  19257   2339    -41  -3593       O  
ATOM   2322  NE2 GLN B   5     -22.632   5.349 -14.451  1.00130.34           N  
ANISOU 2322  NE2 GLN B   5    17545  11781  20195   2456    235  -4489       N  
ATOM   2323  N   ILE B   6     -23.200  11.296 -12.513  1.00 83.17           N  
ANISOU 2323  N   ILE B   6    10813   7545  13239   1854    -66  -2752       N  
ATOM   2324  CA  ILE B   6     -23.668  12.430 -11.723  1.00 77.37           C  
ANISOU 2324  CA  ILE B   6    10000   6951  12445   1685   -145  -2387       C  
ATOM   2325  C   ILE B   6     -23.046  12.509 -10.329  1.00 77.18           C  
ANISOU 2325  C   ILE B   6     9873   6808  12641   1748   -169  -2106       C  
ATOM   2326  O   ILE B   6     -23.080  11.506  -9.612  1.00 82.35           O  
ANISOU 2326  O   ILE B   6    10596   7131  13561   1814   -254  -2074       O  
ATOM   2327  CB  ILE B   6     -25.200  12.309 -11.561  1.00 74.73           C  
ANISOU 2327  CB  ILE B   6     9769   6475  12148   1454   -316  -2347       C  
ATOM   2328  CG1 ILE B   6     -25.870  12.440 -12.936  1.00 74.86           C  
ANISOU 2328  CG1 ILE B   6     9855   6704  11881   1347   -377  -2568       C  
ATOM   2329  CG2 ILE B   6     -25.736  13.333 -10.579  1.00 71.70           C  
ANISOU 2329  CG2 ILE B   6     9307   6150  11785   1316   -342  -2008       C  
ATOM   2330  CD1 ILE B   6     -27.380  12.397 -12.920  1.00 73.61           C  
ANISOU 2330  CD1 ILE B   6     9703   6486  11775   1115   -581  -2529       C  
ATOM   2331  N   TYR B   7     -22.538  13.684  -9.919  1.00 72.66           N  
ANISOU 2331  N   TYR B   7     9171   6488  11949   1692   -116  -1888       N  
ATOM   2332  CA  TYR B   7     -21.948  13.877  -8.562  1.00 71.34           C  
ANISOU 2332  CA  TYR B   7     8920   6277  11907   1687   -182  -1630       C  
ATOM   2333  C   TYR B   7     -22.972  14.531  -7.625  1.00 64.55           C  
ANISOU 2333  C   TYR B   7     8171   5358  10995   1445   -236  -1424       C  
ATOM   2334  O   TYR B   7     -23.769  15.342  -8.049  1.00 67.40           O  
ANISOU 2334  O   TYR B   7     8563   5816  11228   1315   -182  -1425       O  
ATOM   2335  CB  TYR B   7     -20.602  14.628  -8.643  1.00 75.83           C  
ANISOU 2335  CB  TYR B   7     9256   7144  12410   1749    -87  -1579       C  
ATOM   2336  CG  TYR B   7     -20.096  15.312  -7.359  1.00 81.75           C  
ANISOU 2336  CG  TYR B   7     9922   7976  13163   1620   -180  -1321       C  
ATOM   2337  CD1 TYR B   7     -20.582  16.608  -6.985  1.00 83.79           C  
ANISOU 2337  CD1 TYR B   7    10256   8337  13241   1357   -134  -1204       C  
ATOM   2338  CD2 TYR B   7     -19.117  14.709  -6.531  1.00 85.59           C  
ANISOU 2338  CD2 TYR B   7    10256   8437  13826   1756   -327  -1201       C  
ATOM   2339  CE1 TYR B   7     -20.139  17.261  -5.829  1.00 83.57           C  
ANISOU 2339  CE1 TYR B   7    10202   8383  13166   1187   -208  -1039       C  
ATOM   2340  CE2 TYR B   7     -18.662  15.357  -5.370  1.00 89.40           C  
ANISOU 2340  CE2 TYR B   7    10681   9049  14235   1582   -461   -982       C  
ATOM   2341  CZ  TYR B   7     -19.174  16.641  -5.023  1.00 88.80           C  
ANISOU 2341  CZ  TYR B   7    10727   9078  13933   1272   -388   -933       C  
ATOM   2342  OH  TYR B   7     -18.725  17.318  -3.894  1.00 91.06           O  
ANISOU 2342  OH  TYR B   7    11002   9490  14103   1052   -505   -788       O  
ATOM   2343  N   TYR B   8     -23.026  14.084  -6.383  1.00 59.37           N  
ANISOU 2343  N   TYR B   8     7585   4524  10448   1399   -335  -1249       N  
ATOM   2344  CA  TYR B   8     -24.006  14.515  -5.418  1.00 54.85           C  
ANISOU 2344  CA  TYR B   8     7138   3878   9824   1171   -326  -1093       C  
ATOM   2345  C   TYR B   8     -23.193  15.079  -4.281  1.00 55.28           C  
ANISOU 2345  C   TYR B   8     7178   4056   9770   1093   -368   -906       C  
ATOM   2346  O   TYR B   8     -22.328  14.395  -3.778  1.00 57.34           O  
ANISOU 2346  O   TYR B   8     7403   4281  10102   1207   -511   -803       O  
ATOM   2347  CB  TYR B   8     -24.885  13.346  -4.906  1.00 54.64           C  
ANISOU 2347  CB  TYR B   8     7266   3530   9964   1114   -388  -1046       C  
ATOM   2348  CG  TYR B   8     -25.865  12.800  -5.908  1.00 54.03           C  
ANISOU 2348  CG  TYR B   8     7205   3327   9994   1096   -381  -1249       C  
ATOM   2349  CD1 TYR B   8     -25.437  11.928  -6.894  1.00 55.73           C  
ANISOU 2349  CD1 TYR B   8     7421   3446  10307   1273   -427  -1474       C  
ATOM   2350  CD2 TYR B   8     -27.228  13.133  -5.878  1.00 52.69           C  
ANISOU 2350  CD2 TYR B   8     7036   3145   9840    895   -327  -1243       C  
ATOM   2351  CE1 TYR B   8     -26.313  11.421  -7.857  1.00 57.21           C  
ANISOU 2351  CE1 TYR B   8     7650   3545  10540   1205   -454  -1710       C  
ATOM   2352  CE2 TYR B   8     -28.133  12.622  -6.832  1.00 54.23           C  
ANISOU 2352  CE2 TYR B   8     7203   3271  10130    840   -385  -1433       C  
ATOM   2353  CZ  TYR B   8     -27.673  11.756  -7.831  1.00 56.76           C  
ANISOU 2353  CZ  TYR B   8     7569   3509  10485    971   -468  -1678       C  
ATOM   2354  OH  TYR B   8     -28.484  11.203  -8.827  1.00 58.27           O  
ANISOU 2354  OH  TYR B   8     7771   3652  10715    877   -559  -1922       O  
ATOM   2355  N   SER B   9     -23.499  16.307  -3.826  1.00 54.90           N  
ANISOU 2355  N   SER B   9     7166   4133   9559    894   -259   -862       N  
ATOM   2356  CA  SER B   9     -22.733  16.943  -2.741  1.00 54.01           C  
ANISOU 2356  CA  SER B   9     7073   4160   9288    748   -308   -742       C  
ATOM   2357  C   SER B   9     -23.178  16.302  -1.438  1.00 55.59           C  
ANISOU 2357  C   SER B   9     7477   4221   9421    623   -383   -576       C  
ATOM   2358  O   SER B   9     -24.273  15.736  -1.354  1.00 55.15           O  
ANISOU 2358  O   SER B   9     7540   3965   9446    587   -306   -565       O  
ATOM   2359  CB  SER B   9     -22.970  18.457  -2.686  1.00 51.91           C  
ANISOU 2359  CB  SER B   9     6838   3998   8888    556   -129   -800       C  
ATOM   2360  OG  SER B   9     -24.295  18.805  -2.276  1.00 50.95           O  
ANISOU 2360  OG  SER B   9     6870   3728   8759    432     40   -813       O  
ATOM   2361  N   ASP B  10     -22.349  16.436  -0.419  1.00 57.81           N  
ANISOU 2361  N   ASP B  10     7796   4638   9532    517   -534   -436       N  
ATOM   2362  CA  ASP B  10     -22.836  16.323   0.931  1.00 60.57           C  
ANISOU 2362  CA  ASP B  10     8407   4946   9660    287   -540   -285       C  
ATOM   2363  C   ASP B  10     -23.982  17.301   1.149  1.00 59.29           C  
ANISOU 2363  C   ASP B  10     8388   4748   9392     72   -221   -428       C  
ATOM   2364  O   ASP B  10     -24.238  18.208   0.318  1.00 56.34           O  
ANISOU 2364  O   ASP B  10     7899   4391   9115    108    -51   -605       O  
ATOM   2365  CB  ASP B  10     -21.736  16.604   1.918  1.00 65.23           C  
ANISOU 2365  CB  ASP B  10     9016   5771   9997    150   -775   -149       C  
ATOM   2366  CG  ASP B  10     -20.757  15.485   2.010  1.00 72.69           C  
ANISOU 2366  CG  ASP B  10     9823   6718  11076    380  -1115     78       C  
ATOM   2367  OD1 ASP B  10     -21.117  14.297   1.724  1.00 79.71           O  
ANISOU 2367  OD1 ASP B  10    10747   7334  12201    591  -1151    180       O  
ATOM   2368  OD2 ASP B  10     -19.597  15.761   2.388  1.00 78.21           O  
ANISOU 2368  OD2 ASP B  10    10361   7673  11680    355  -1364    163       O  
ATOM   2369  N   LYS B  11     -24.672  17.123   2.261  1.00 60.89           N  
ANISOU 2369  N   LYS B  11     8836   4894   9403   -137   -120   -336       N  
ATOM   2370  CA  LYS B  11     -25.791  17.991   2.597  1.00 62.01           C  
ANISOU 2370  CA  LYS B  11     9092   4990   9478   -318    239   -486       C  
ATOM   2371  C   LYS B  11     -25.316  19.098   3.507  1.00 65.69           C  
ANISOU 2371  C   LYS B  11     9730   5622   9606   -569    312   -586       C  
ATOM   2372  O   LYS B  11     -24.267  18.983   4.161  1.00 71.75           O  
ANISOU 2372  O   LYS B  11    10574   6570  10116   -677     43   -479       O  
ATOM   2373  CB  LYS B  11     -26.900  17.227   3.257  1.00 62.93           C  
ANISOU 2373  CB  LYS B  11     9365   4962   9581   -438    405   -377       C  
ATOM   2374  CG  LYS B  11     -27.518  16.221   2.335  1.00 62.33           C  
ANISOU 2374  CG  LYS B  11     9126   4687   9867   -258    359   -338       C  
ATOM   2375  CD  LYS B  11     -28.671  15.530   3.033  1.00 64.40           C  
ANISOU 2375  CD  LYS B  11     9520   4804  10143   -447    565   -227       C  
ATOM   2376  CE  LYS B  11     -29.178  14.329   2.241  1.00 63.86           C  
ANISOU 2376  CE  LYS B  11     9332   4503  10429   -339    461   -176       C  
ATOM   2377  NZ  LYS B  11     -29.911  13.345   3.110  1.00 67.08           N  
ANISOU 2377  NZ  LYS B  11     9927   4738  10820   -569    574     38       N  
ATOM   2378  N   TYR B  12     -26.072  20.183   3.531  1.00 64.86           N  
ANISOU 2378  N   TYR B  12     9672   5447   9525   -659    660   -801       N  
ATOM   2379  CA  TYR B  12     -25.780  21.316   4.399  1.00 66.02           C  
ANISOU 2379  CA  TYR B  12    10036   5677   9370   -930    808   -980       C  
ATOM   2380  C   TYR B  12     -27.117  21.962   4.774  1.00 67.85           C  
ANISOU 2380  C   TYR B  12    10383   5740   9657  -1004   1296  -1169       C  
ATOM   2381  O   TYR B  12     -28.160  21.689   4.146  1.00 65.33           O  
ANISOU 2381  O   TYR B  12     9878   5270   9675   -815   1467  -1148       O  
ATOM   2382  CB  TYR B  12     -24.787  22.288   3.719  1.00 64.54           C  
ANISOU 2382  CB  TYR B  12     9709   5547   9265   -909    694  -1099       C  
ATOM   2383  CG  TYR B  12     -25.046  22.582   2.254  1.00 61.19           C  
ANISOU 2383  CG  TYR B  12     9013   4991   9244   -627    755  -1118       C  
ATOM   2384  CD1 TYR B  12     -25.874  23.610   1.850  1.00 60.74           C  
ANISOU 2384  CD1 TYR B  12     8952   4733   9392   -578   1076  -1263       C  
ATOM   2385  CD2 TYR B  12     -24.475  21.817   1.265  1.00 60.20           C  
ANISOU 2385  CD2 TYR B  12     8645   4940   9286   -398    493   -981       C  
ATOM   2386  CE1 TYR B  12     -26.101  23.865   0.490  1.00 59.26           C  
ANISOU 2386  CE1 TYR B  12     8537   4460   9518   -328   1074  -1216       C  
ATOM   2387  CE2 TYR B  12     -24.698  22.073  -0.105  1.00 57.15           C  
ANISOU 2387  CE2 TYR B  12     8055   4485   9174   -175    540   -996       C  
ATOM   2388  CZ  TYR B  12     -25.531  23.066  -0.495  1.00 56.26           C  
ANISOU 2388  CZ  TYR B  12     7953   4208   9215   -147    801  -1083       C  
ATOM   2389  OH  TYR B  12     -25.797  23.285  -1.842  1.00 53.13           O  
ANISOU 2389  OH  TYR B  12     7378   3771   9034     63    798  -1039       O  
ATOM   2390  N   ASP B  13     -27.099  22.801   5.806  1.00 73.15           N  
ANISOU 2390  N   ASP B  13    11342   6446  10006  -1284   1524  -1375       N  
ATOM   2391  CA  ASP B  13     -28.345  23.441   6.270  1.00 76.82           C  
ANISOU 2391  CA  ASP B  13    11914   6740  10532  -1339   2062  -1599       C  
ATOM   2392  C   ASP B  13     -28.263  24.810   7.025  1.00 79.68           C  
ANISOU 2392  C   ASP B  13    12566   7030  10678  -1581   2394  -1966       C  
ATOM   2393  O   ASP B  13     -27.295  25.131   7.716  1.00 79.49           O  
ANISOU 2393  O   ASP B  13    12798   7168  10235  -1873   2216  -2062       O  
ATOM   2394  CB  ASP B  13     -29.145  22.417   7.107  1.00 80.30           C  
ANISOU 2394  CB  ASP B  13    12481   7248  10780  -1462   2218  -1456       C  
ATOM   2395  CG  ASP B  13     -28.251  21.528   7.945  1.00 82.62           C  
ANISOU 2395  CG  ASP B  13    13024   7784  10581  -1685   1848  -1218       C  
ATOM   2396  OD1 ASP B  13     -27.930  21.885   9.087  1.00 86.11           O  
ANISOU 2396  OD1 ASP B  13    13825   8389  10502  -2011   1916  -1324       O  
ATOM   2397  OD2 ASP B  13     -27.868  20.470   7.434  1.00 86.41           O  
ANISOU 2397  OD2 ASP B  13    13344   8283  11204  -1522   1475   -923       O  
ATOM   2398  N   ASP B  14     -29.369  25.551   6.869  1.00 81.77           N  
ANISOU 2398  N   ASP B  14    12761   7034  11272  -1444   2879  -2172       N  
ATOM   2399  CA  ASP B  14     -29.807  26.687   7.695  1.00 85.65           C  
ANISOU 2399  CA  ASP B  14    13533   7357  11652  -1616   3394  -2570       C  
ATOM   2400  C   ASP B  14     -30.414  26.229   8.990  1.00 90.56           C  
ANISOU 2400  C   ASP B  14    14437   8129  11840  -1880   3729  -2665       C  
ATOM   2401  O   ASP B  14     -30.394  25.061   9.327  1.00 91.91           O  
ANISOU 2401  O   ASP B  14    14631   8534  11757  -1972   3522  -2385       O  
ATOM   2402  CB  ASP B  14     -31.003  27.350   7.041  1.00 85.17           C  
ANISOU 2402  CB  ASP B  14    13197   6962  12201  -1275   3818  -2674       C  
ATOM   2403  CG  ASP B  14     -30.701  28.003   5.776  1.00 82.91           C  
ANISOU 2403  CG  ASP B  14    12666   6468  12367   -998   3619  -2585       C  
ATOM   2404  OD1 ASP B  14     -29.655  28.662   5.681  1.00 84.20           O  
ANISOU 2404  OD1 ASP B  14    12999   6597  12396  -1147   3433  -2671       O  
ATOM   2405  OD2 ASP B  14     -31.556  27.930   4.888  1.00 80.94           O  
ANISOU 2405  OD2 ASP B  14    12055   6088  12609   -654   3670  -2432       O  
ATOM   2406  N   GLU B  15     -30.999  27.175   9.707  1.00 96.40           N  
ANISOU 2406  N   GLU B  15    15409   8702  12513  -1998   4298  -3068       N  
ATOM   2407  CA  GLU B  15     -32.080  26.860  10.618  1.00100.83           C  
ANISOU 2407  CA  GLU B  15    16085   9321  12904  -2110   4838  -3182       C  
ATOM   2408  C   GLU B  15     -33.383  26.534   9.868  1.00 97.19           C  
ANISOU 2408  C   GLU B  15    15115   8698  13115  -1725   5105  -3035       C  
ATOM   2409  O   GLU B  15     -34.170  25.768  10.395  1.00 98.26           O  
ANISOU 2409  O   GLU B  15    15211   8972  13149  -1819   5369  -2938       O  
ATOM   2410  CB  GLU B  15     -32.280  27.977  11.656  1.00108.92           C  
ANISOU 2410  CB  GLU B  15    17534  10223  13625  -2363   5424  -3726       C  
ATOM   2411  CG  GLU B  15     -31.157  28.015  12.679  1.00114.54           C  
ANISOU 2411  CG  GLU B  15    18793  11227  13500  -2870   5160  -3857       C  
ATOM   2412  CD  GLU B  15     -31.216  29.234  13.597  1.00126.28           C  
ANISOU 2412  CD  GLU B  15    20748  12559  14672  -3159   5694  -4478       C  
ATOM   2413  OE1 GLU B  15     -32.182  29.366  14.369  1.00134.32           O  
ANISOU 2413  OE1 GLU B  15    21934  13549  15550  -3234   6367  -4760       O  
ATOM   2414  OE2 GLU B  15     -30.285  30.075  13.571  1.00128.95           O  
ANISOU 2414  OE2 GLU B  15    21299  12796  14898  -3341   5473  -4720       O  
ATOM   2415  N   GLU B  16     -33.627  27.122   8.693  1.00 93.51           N  
ANISOU 2415  N   GLU B  16    14266   7958  13303  -1333   5040  -3006       N  
ATOM   2416  CA  GLU B  16     -34.880  26.914   7.920  1.00 93.22           C  
ANISOU 2416  CA  GLU B  16    13695   7792  13931   -963   5229  -2865       C  
ATOM   2417  C   GLU B  16     -34.947  25.713   6.969  1.00 86.92           C  
ANISOU 2417  C   GLU B  16    12528   7150  13345   -819   4725  -2437       C  
ATOM   2418  O   GLU B  16     -35.883  24.913   7.056  1.00 89.26           O  
ANISOU 2418  O   GLU B  16    12574   7536  13803   -816   4883  -2309       O  
ATOM   2419  CB  GLU B  16     -35.269  28.159   7.104  1.00 95.82           C  
ANISOU 2419  CB  GLU B  16    13776   7742  14889   -582   5406  -3003       C  
ATOM   2420  CG  GLU B  16     -35.299  29.498   7.841  1.00102.88           C  
ANISOU 2420  CG  GLU B  16    14999   8334  15758   -642   5949  -3471       C  
ATOM   2421  CD  GLU B  16     -36.494  29.676   8.779  1.00112.00           C  
ANISOU 2421  CD  GLU B  16    16127   9430  16996   -648   6715  -3777       C  
ATOM   2422  OE1 GLU B  16     -37.282  28.709   8.954  1.00114.41           O  
ANISOU 2422  OE1 GLU B  16    16164   9975  17330   -668   6828  -3600       O  
ATOM   2423  OE2 GLU B  16     -36.642  30.796   9.373  1.00120.25           O  
ANISOU 2423  OE2 GLU B  16    17433  10172  18083   -656   7250  -4225       O  
ATOM   2424  N   PHE B  17     -34.034  25.593   6.018  1.00 80.48           N  
ANISOU 2424  N   PHE B  17    11653   6352  12573   -704   4165  -2241       N  
ATOM   2425  CA  PHE B  17     -34.020  24.399   5.100  1.00 74.56           C  
ANISOU 2425  CA  PHE B  17    10610   5738  11981   -585   3692  -1894       C  
ATOM   2426  C   PHE B  17     -32.814  23.486   5.275  1.00 71.00           C  
ANISOU 2426  C   PHE B  17    10406   5492  11077   -782   3218  -1710       C  
ATOM   2427  O   PHE B  17     -31.852  23.814   5.967  1.00 71.69           O  
ANISOU 2427  O   PHE B  17    10844   5663  10732   -999   3143  -1804       O  
ATOM   2428  CB  PHE B  17     -33.950  24.841   3.648  1.00 71.13           C  
ANISOU 2428  CB  PHE B  17     9856   5183  11984   -246   3400  -1784       C  
ATOM   2429  CG  PHE B  17     -35.103  25.647   3.195  1.00 73.59           C  
ANISOU 2429  CG  PHE B  17     9829   5289  12841     40   3713  -1850       C  
ATOM   2430  CD1 PHE B  17     -36.242  25.030   2.709  1.00 74.33           C  
ANISOU 2430  CD1 PHE B  17     9483   5434  13324    188   3721  -1711       C  
ATOM   2431  CD2 PHE B  17     -35.054  27.037   3.217  1.00 73.94           C  
ANISOU 2431  CD2 PHE B  17     9968   5065  13061    171   3979  -2040       C  
ATOM   2432  CE1 PHE B  17     -37.330  25.787   2.263  1.00 76.90           C  
ANISOU 2432  CE1 PHE B  17     9413   5594  14212    493   3964  -1732       C  
ATOM   2433  CE2 PHE B  17     -36.112  27.763   2.762  1.00 75.92           C  
ANISOU 2433  CE2 PHE B  17     9873   5092  13881    499   4237  -2050       C  
ATOM   2434  CZ  PHE B  17     -37.248  27.155   2.277  1.00 76.99           C  
ANISOU 2434  CZ  PHE B  17     9517   5324  14410    680   4214  -1883       C  
ATOM   2435  N   GLU B  18     -32.868  22.345   4.607  1.00 68.68           N  
ANISOU 2435  N   GLU B  18     9904   5267  10921   -695   2881  -1455       N  
ATOM   2436  CA  GLU B  18     -31.663  21.597   4.295  1.00 65.94           C  
ANISOU 2436  CA  GLU B  18     9660   5038  10354   -716   2372  -1270       C  
ATOM   2437  C   GLU B  18     -31.486  21.646   2.812  1.00 61.74           C  
ANISOU 2437  C   GLU B  18     8824   4457  10175   -424   2077  -1204       C  
ATOM   2438  O   GLU B  18     -32.435  21.883   2.059  1.00 59.88           O  
ANISOU 2438  O   GLU B  18     8292   4129  10328   -237   2182  -1218       O  
ATOM   2439  CB  GLU B  18     -31.682  20.168   4.815  1.00 66.68           C  
ANISOU 2439  CB  GLU B  18     9860   5210  10265   -872   2223  -1040       C  
ATOM   2440  CG  GLU B  18     -32.707  19.239   4.161  1.00 66.40           C  
ANISOU 2440  CG  GLU B  18     9522   5082  10623   -778   2221   -919       C  
ATOM   2441  CD  GLU B  18     -32.567  17.768   4.578  1.00 66.02           C  
ANISOU 2441  CD  GLU B  18     9622   5025  10437   -935   2028   -663       C  
ATOM   2442  OE1 GLU B  18     -31.423  17.298   4.860  1.00 63.77           O  
ANISOU 2442  OE1 GLU B  18     9570   4795   9864   -964   1699   -515       O  
ATOM   2443  OE2 GLU B  18     -33.630  17.110   4.573  1.00 66.44           O  
ANISOU 2443  OE2 GLU B  18     9521   4997  10726  -1018   2203   -600       O  
ATOM   2444  N   TYR B  19     -30.252  21.401   2.428  1.00 60.00           N  
ANISOU 2444  N   TYR B  19     8671   4331   9794   -398   1702  -1123       N  
ATOM   2445  CA  TYR B  19     -29.813  21.647   1.080  1.00 59.63           C  
ANISOU 2445  CA  TYR B  19     8413   4281   9959   -166   1462  -1094       C  
ATOM   2446  C   TYR B  19     -28.827  20.590   0.591  1.00 56.93           C  
ANISOU 2446  C   TYR B  19     8048   4051   9532   -105   1067   -959       C  
ATOM   2447  O   TYR B  19     -28.086  19.969   1.397  1.00 58.15           O  
ANISOU 2447  O   TYR B  19     8376   4287   9428   -237    920   -874       O  
ATOM   2448  CB  TYR B  19     -29.010  22.983   1.004  1.00 61.08           C  
ANISOU 2448  CB  TYR B  19     8694   4450  10060   -191   1511  -1211       C  
ATOM   2449  CG  TYR B  19     -29.733  24.228   1.338  1.00 64.00           C  
ANISOU 2449  CG  TYR B  19     9116   4635  10567   -202   1899  -1379       C  
ATOM   2450  CD1 TYR B  19     -30.440  24.926   0.357  1.00 65.52           C  
ANISOU 2450  CD1 TYR B  19     9084   4669  11139     45   1990  -1355       C  
ATOM   2451  CD2 TYR B  19     -29.721  24.725   2.628  1.00 68.17           C  
ANISOU 2451  CD2 TYR B  19     9928   5131  10842   -448   2177  -1565       C  
ATOM   2452  CE1 TYR B  19     -31.156  26.066   0.668  1.00 69.72           C  
ANISOU 2452  CE1 TYR B  19     9640   4964  11885     97   2368  -1496       C  
ATOM   2453  CE2 TYR B  19     -30.404  25.879   2.963  1.00 72.11           C  
ANISOU 2453  CE2 TYR B  19    10493   5402  11503   -435   2599  -1778       C  
ATOM   2454  CZ  TYR B  19     -31.136  26.568   1.990  1.00 74.05           C  
ANISOU 2454  CZ  TYR B  19    10481   5433  12219   -136   2710  -1740       C  
ATOM   2455  OH  TYR B  19     -31.836  27.763   2.296  1.00 76.90           O  
ANISOU 2455  OH  TYR B  19    10884   5494  12839    -55   3151  -1941       O  
ATOM   2456  N   ARG B  20     -28.822  20.412  -0.728  1.00 54.01           N  
ANISOU 2456  N   ARG B  20     7464   3684   9372    104    898   -937       N  
ATOM   2457  CA  ARG B  20     -27.690  19.850  -1.417  1.00 53.73           C  
ANISOU 2457  CA  ARG B  20     7384   3753   9279    210    604   -890       C  
ATOM   2458  C   ARG B  20     -27.677  20.265  -2.867  1.00 51.08           C  
ANISOU 2458  C   ARG B  20     6868   3457   9081    395    538   -921       C  
ATOM   2459  O   ARG B  20     -28.674  20.728  -3.390  1.00 49.99           O  
ANISOU 2459  O   ARG B  20     6622   3258   9113    462    637   -929       O  
ATOM   2460  CB  ARG B  20     -27.692  18.300  -1.352  1.00 56.68           C  
ANISOU 2460  CB  ARG B  20     7768   4075   9692    243    418   -804       C  
ATOM   2461  CG  ARG B  20     -28.478  17.647  -2.479  1.00 57.03           C  
ANISOU 2461  CG  ARG B  20     7647   4045   9974    372    347   -850       C  
ATOM   2462  CD  ARG B  20     -27.949  16.260  -2.862  1.00 57.60           C  
ANISOU 2462  CD  ARG B  20     7736   4042  10105    468    119   -836       C  
ATOM   2463  NE  ARG B  20     -29.005  15.362  -2.412  1.00 58.30           N  
ANISOU 2463  NE  ARG B  20     7869   3947  10336    338    167   -788       N  
ATOM   2464  CZ  ARG B  20     -28.863  14.348  -1.584  1.00 58.80           C  
ANISOU 2464  CZ  ARG B  20     8095   3852  10392    253    115   -651       C  
ATOM   2465  NH1 ARG B  20     -27.659  13.951  -1.132  1.00 59.28           N  
ANISOU 2465  NH1 ARG B  20     8273   3916  10333    335    -47   -534       N  
ATOM   2466  NH2 ARG B  20     -29.952  13.720  -1.245  1.00 60.00           N  
ANISOU 2466  NH2 ARG B  20     8266   3844  10685     84    217   -605       N  
ATOM   2467  N   HIS B  21     -26.533  20.065  -3.509  1.00 50.26           N  
ANISOU 2467  N   HIS B  21     6718   3479   8897    479    368   -919       N  
ATOM   2468  CA  HIS B  21     -26.444  20.265  -4.939  1.00 50.89           C  
ANISOU 2468  CA  HIS B  21     6670   3642   9024    631    307   -939       C  
ATOM   2469  C   HIS B  21     -25.899  19.000  -5.676  1.00 53.03           C  
ANISOU 2469  C   HIS B  21     6878   3977   9293    766    121   -996       C  
ATOM   2470  O   HIS B  21     -25.172  18.175  -5.098  1.00 51.87           O  
ANISOU 2470  O   HIS B  21     6760   3815   9134    780     26   -988       O  
ATOM   2471  CB  HIS B  21     -25.622  21.519  -5.295  1.00 50.65           C  
ANISOU 2471  CB  HIS B  21     6635   3702   8906    595    389   -917       C  
ATOM   2472  CG  HIS B  21     -24.226  21.524  -4.774  1.00 50.09           C  
ANISOU 2472  CG  HIS B  21     6566   3757   8709    502    333   -927       C  
ATOM   2473  ND1 HIS B  21     -23.914  21.963  -3.512  1.00 51.27           N  
ANISOU 2473  ND1 HIS B  21     6831   3881   8768    303    375   -935       N  
ATOM   2474  CD2 HIS B  21     -23.048  21.213  -5.357  1.00 52.17           C  
ANISOU 2474  CD2 HIS B  21     6698   4200   8922    568    242   -937       C  
ATOM   2475  CE1 HIS B  21     -22.604  21.889  -3.319  1.00 52.49           C  
ANISOU 2475  CE1 HIS B  21     6902   4209   8831    240    250   -926       C  
ATOM   2476  NE2 HIS B  21     -22.045  21.456  -4.433  1.00 53.00           N  
ANISOU 2476  NE2 HIS B  21     6789   4397   8952    414    190   -923       N  
ATOM   2477  N   VAL B  22     -26.246  18.921  -6.964  1.00 52.95           N  
ANISOU 2477  N   VAL B  22     6795   4033   9288    872     71  -1053       N  
ATOM   2478  CA  VAL B  22     -25.935  17.829  -7.787  1.00 54.13           C  
ANISOU 2478  CA  VAL B  22     6920   4216   9428    988    -47  -1181       C  
ATOM   2479  C   VAL B  22     -25.304  18.362  -9.056  1.00 56.87           C  
ANISOU 2479  C   VAL B  22     7220   4784   9602   1065    -18  -1224       C  
ATOM   2480  O   VAL B  22     -25.899  19.167  -9.771  1.00 55.62           O  
ANISOU 2480  O   VAL B  22     7056   4708   9367   1046     -6  -1153       O  
ATOM   2481  CB  VAL B  22     -27.229  17.091  -8.159  1.00 56.17           C  
ANISOU 2481  CB  VAL B  22     7176   4363   9803    964   -144  -1253       C  
ATOM   2482  CG1 VAL B  22     -26.925  15.858  -8.975  1.00 57.34           C  
ANISOU 2482  CG1 VAL B  22     7356   4483   9946   1053   -256  -1455       C  
ATOM   2483  CG2 VAL B  22     -27.988  16.652  -6.913  1.00 56.22           C  
ANISOU 2483  CG2 VAL B  22     7221   4160   9977    839   -110  -1179       C  
ATOM   2484  N   MET B  23     -24.146  17.805  -9.403  1.00 61.16           N  
ANISOU 2484  N   MET B  23     7720   5424  10092   1167     -4  -1331       N  
ATOM   2485  CA  MET B  23     -23.435  18.171 -10.613  1.00 63.44           C  
ANISOU 2485  CA  MET B  23     7964   5955  10185   1223     86  -1395       C  
ATOM   2486  C   MET B  23     -23.703  17.176 -11.725  1.00 64.03           C  
ANISOU 2486  C   MET B  23     8095   6064  10167   1321     34  -1629       C  
ATOM   2487  O   MET B  23     -23.355  15.999 -11.626  1.00 66.12           O  
ANISOU 2487  O   MET B  23     8361   6201  10559   1437     10  -1814       O  
ATOM   2488  CB  MET B  23     -21.953  18.299 -10.312  1.00 67.77           C  
ANISOU 2488  CB  MET B  23     8370   6628  10749   1260    191  -1390       C  
ATOM   2489  CG  MET B  23     -21.656  19.408  -9.289  1.00 70.74           C  
ANISOU 2489  CG  MET B  23     8717   6998  11160   1089    226  -1199       C  
ATOM   2490  SD  MET B  23     -19.942  19.709  -8.712  1.00 80.82           S  
ANISOU 2490  SD  MET B  23     9760   8461  12484   1038    274  -1162       S  
ATOM   2491  CE  MET B  23     -18.939  18.965 -10.008  1.00 81.97           C  
ANISOU 2491  CE  MET B  23     9708   8833  12602   1254    409  -1342       C  
ATOM   2492  N   LEU B  24     -24.363  17.651 -12.782  1.00 65.32           N  
ANISOU 2492  N   LEU B  24     8327   6384  10107   1267      0  -1619       N  
ATOM   2493  CA  LEU B  24     -24.613  16.869 -14.004  1.00 67.65           C  
ANISOU 2493  CA  LEU B  24     8719   6790  10193   1297    -60  -1872       C  
ATOM   2494  C   LEU B  24     -23.449  16.900 -14.983  1.00 75.34           C  
ANISOU 2494  C   LEU B  24     9700   8028  10894   1367    151  -2016       C  
ATOM   2495  O   LEU B  24     -22.697  17.872 -15.006  1.00 72.36           O  
ANISOU 2495  O   LEU B  24     9247   7816  10427   1337    316  -1831       O  
ATOM   2496  CB  LEU B  24     -25.793  17.400 -14.783  1.00 66.70           C  
ANISOU 2496  CB  LEU B  24     8663   6801   9880   1190   -239  -1767       C  
ATOM   2497  CG  LEU B  24     -27.094  17.668 -14.052  1.00 64.42           C  
ANISOU 2497  CG  LEU B  24     8297   6333   9844   1117   -412  -1588       C  
ATOM   2498  CD1 LEU B  24     -28.135  18.113 -15.049  1.00 64.99           C  
ANISOU 2498  CD1 LEU B  24     8372   6598   9722   1054   -632  -1485       C  
ATOM   2499  CD2 LEU B  24     -27.589  16.461 -13.286  1.00 63.52           C  
ANISOU 2499  CD2 LEU B  24     8169   5943  10021   1089   -494  -1760       C  
ATOM   2500  N   PRO B  25     -23.283  15.820 -15.792  1.00 86.96           N  
ANISOU 2500  N   PRO B  25    11267   9528  12246   1441    185  -2374       N  
ATOM   2501  CA  PRO B  25     -22.346  15.839 -16.923  1.00 96.04           C  
ANISOU 2501  CA  PRO B  25    12452  10979  13057   1488    439  -2563       C  
ATOM   2502  C   PRO B  25     -22.760  16.859 -17.957  1.00105.61           C  
ANISOU 2502  C   PRO B  25    13796  12526  13803   1323    414  -2377       C  
ATOM   2503  O   PRO B  25     -23.956  17.043 -18.172  1.00110.58           O  
ANISOU 2503  O   PRO B  25    14527  13151  14337   1212    131  -2267       O  
ATOM   2504  CB  PRO B  25     -22.475  14.444 -17.509  1.00 98.93           C  
ANISOU 2504  CB  PRO B  25    12963  11226  13397   1567    437  -3026       C  
ATOM   2505  CG  PRO B  25     -23.739  13.907 -16.938  1.00 95.67           C  
ANISOU 2505  CG  PRO B  25    12621  10511  13217   1476    114  -3016       C  
ATOM   2506  CD  PRO B  25     -23.782  14.454 -15.572  1.00 89.29           C  
ANISOU 2506  CD  PRO B  25    11641   9523  12760   1488     55  -2654       C  
ATOM   2507  N   LYS B  26     -21.773  17.466 -18.618  1.00116.37           N  
ANISOU 2507  N   LYS B  26    15140  14187  14888   1305    705  -2328       N  
ATOM   2508  CA  LYS B  26     -21.919  18.814 -19.198  1.00121.66           C  
ANISOU 2508  CA  LYS B  26    15891  15106  15226   1141    721  -1949       C  
ATOM   2509  C   LYS B  26     -23.003  18.922 -20.261  1.00131.12           C  
ANISOU 2509  C   LYS B  26    17340  16499  15979   1023    464  -1900       C  
ATOM   2510  O   LYS B  26     -24.075  19.463 -19.963  1.00135.09           O  
ANISOU 2510  O   LYS B  26    17845  16886  16597    978    157  -1611       O  
ATOM   2511  CB  LYS B  26     -20.570  19.357 -19.647  1.00122.01           C  
ANISOU 2511  CB  LYS B  26    15850  15419  15089   1104   1128  -1906       C  
ATOM   2512  CG  LYS B  26     -19.638  19.601 -18.465  1.00117.48           C  
ANISOU 2512  CG  LYS B  26    14970  14679  14986   1160   1270  -1818       C  
ATOM   2513  CD  LYS B  26     -19.778  20.988 -17.858  1.00110.92           C  
ANISOU 2513  CD  LYS B  26    14109  13753  14281    997   1215  -1378       C  
ATOM   2514  CE  LYS B  26     -18.777  21.173 -16.731  1.00107.77           C  
ANISOU 2514  CE  LYS B  26    13417  13247  14281    995   1331  -1351       C  
ATOM   2515  NZ  LYS B  26     -17.372  21.335 -17.216  1.00112.86           N  
ANISOU 2515  NZ  LYS B  26    13847  14189  14843    943   1703  -1412       N  
ATOM   2516  N  AASP B  27     -22.713  18.258 -21.402  0.50136.63           N  
ANISOU 2516  N  AASP B  27    18220  17473  16218    992    590  -2239       N  
ATOM   2517  N  BASP B  27     -22.747  18.666 -21.531  0.50141.58           N  
ANISOU 2517  N  BASP B  27    18867  18166  16758    951    584  -2095       N  
ATOM   2518  CA AASP B  27     -23.622  17.493 -22.332  0.50145.25           C  
ANISOU 2518  CA AASP B  27    19559  18705  16922    898    324  -2525       C  
ATOM   2519  CA BASP B  27     -23.883  18.991 -22.493  0.50153.40           C  
ANISOU 2519  CA BASP B  27    20601  19896  17786    799    232  -1926       C  
ATOM   2520  C  AASP B  27     -25.119  17.563 -22.209  0.50144.05           C  
ANISOU 2520  C  AASP B  27    19425  18462  16844    809   -183  -2350       C  
ATOM   2521  C  BASP B  27     -25.195  17.959 -22.246  0.50148.81           C  
ANISOU 2521  C  BASP B  27    20022  19109  17408    792   -210  -2191       C  
ATOM   2522  O  AASP B  27     -25.851  17.512 -23.194  0.50150.09           O  
ANISOU 2522  O  AASP B  27    20383  19501  17143    658   -453  -2376       O  
ATOM   2523  O  BASP B  27     -25.846  17.516 -23.199  0.50154.64           O  
ANISOU 2523  O  BASP B  27    20960  20079  17716    658   -452  -2375       O  
ATOM   2524  CB AASP B  27     -23.196  16.003 -22.466  1.00149.52           C  
ANISOU 2524  CB AASP B  27    20157  19120  17533    998    493  -3158       C  
ATOM   2525  CB BASP B  27     -23.380  19.457 -23.990  1.00170.58           C  
ANISOU 2525  CB BASP B  27    23057  22583  19170    638    433  -1863       C  
ATOM   2526  CG AASP B  27     -22.615  15.667 -23.856  1.00155.47           C  
ANISOU 2526  CG AASP B  27    21174  20268  17629    921    779  -3526       C  
ATOM   2527  CG BASP B  27     -23.485  21.007 -24.254  1.00175.86           C  
ANISOU 2527  CG BASP B  27    23785  23379  19652    532    391  -1197       C  
ATOM   2528  OD1AASP B  27     -22.941  16.326 -24.865  1.00153.80           O  
ANISOU 2528  OD1AASP B  27    21187  20460  16790    724    688  -3338       O  
ATOM   2529  OD1BASP B  27     -24.338  21.705 -23.654  1.00170.07           O  
ANISOU 2529  OD1BASP B  27    22952  22408  19258    573     78   -804       O  
ATOM   2530  OD2AASP B  27     -21.804  14.734 -23.913  1.00160.28           O  
ANISOU 2530  OD2AASP B  27    21767  20774  18358   1072   1116  -3999       O  
ATOM   2531  OD2BASP B  27     -22.706  21.521 -25.110  1.00184.06           O  
ANISOU 2531  OD2BASP B  27    24987  24747  20199    405    705  -1069       O  
ATOM   2532  N   ILE B  28     -25.525  17.541 -20.974  1.00137.97           N  
ANISOU 2532  N   ILE B  28    18436  17320  16665    896   -297  -2225       N  
ATOM   2533  CA  ILE B  28     -26.930  17.334 -20.562  1.00130.38           C  
ANISOU 2533  CA  ILE B  28    17388  16187  15964    838   -713  -2148       C  
ATOM   2534  C   ILE B  28     -27.538  18.676 -20.193  1.00126.69           C  
ANISOU 2534  C   ILE B  28    16785  15704  15644    852   -858  -1595       C  
ATOM   2535  O   ILE B  28     -28.704  18.928 -20.476  1.00125.17           O  
ANISOU 2535  O   ILE B  28    16540  15588  15428    792  -1220  -1408       O  
ATOM   2536  CB  ILE B  28     -27.054  16.364 -19.354  1.00123.86           C  
ANISOU 2536  CB  ILE B  28    16419  14927  15713    912   -697  -2373       C  
ATOM   2537  CG1 ILE B  28     -27.042  14.911 -19.829  1.00122.46           C  
ANISOU 2537  CG1 ILE B  28    16399  14674  15456    865   -715  -2918       C  
ATOM   2538  CG2 ILE B  28     -28.335  16.618 -18.569  1.00122.90           C  
ANISOU 2538  CG2 ILE B  28    16110  14613  15972    863   -987  -2123       C  
ATOM   2539  CD1 ILE B  28     -27.190  13.883 -18.725  1.00118.24           C  
ANISOU 2539  CD1 ILE B  28    15775  13672  15475    920   -714  -3098       C  
ATOM   2540  N   ALA B  29     -26.737  19.524 -19.553  1.00126.88           N  
ANISOU 2540  N   ALA B  29    16735  15615  15856    933   -576  -1351       N  
ATOM   2541  CA  ALA B  29     -27.077  20.939 -19.285  1.00129.60           C  
ANISOU 2541  CA  ALA B  29    17015  15899  16328    953   -614   -844       C  
ATOM   2542  C   ALA B  29     -27.534  21.794 -20.490  1.00138.24           C  
ANISOU 2542  C   ALA B  29    18256  17293  16975    893   -813   -487       C  
ATOM   2543  O   ALA B  29     -28.193  22.811 -20.273  1.00138.00           O  
ANISOU 2543  O   ALA B  29    18148  17136  17148    952   -951    -65       O  
ATOM   2544  CB  ALA B  29     -25.923  21.648 -18.595  1.00125.89           C  
ANISOU 2544  CB  ALA B  29    16502  15295  16036    977   -248   -722       C  
ATOM   2545  N   LYS B  30     -27.225  21.382 -21.734  1.00142.88           N  
ANISOU 2545  N   LYS B  30    19067  18261  16960    785   -829   -645       N  
ATOM   2546  CA  LYS B  30     -27.929  21.918 -22.938  1.00144.90           C  
ANISOU 2546  CA  LYS B  30    19488  18860  16708    697  -1161   -326       C  
ATOM   2547  C   LYS B  30     -29.449  21.916 -22.728  1.00147.50           C  
ANISOU 2547  C   LYS B  30    19613  19104  17323    743  -1664   -160       C  
ATOM   2548  O   LYS B  30     -30.159  22.807 -23.199  1.00151.99           O  
ANISOU 2548  O   LYS B  30    20170  19781  17797    777  -1960    321       O  
ATOM   2549  CB  LYS B  30     -27.621  21.108 -24.229  1.00146.11           C  
ANISOU 2549  CB  LYS B  30    19927  19456  16130    531  -1174   -679       C  
ATOM   2550  CG  LYS B  30     -26.763  21.808 -25.290  1.00145.88           C  
ANISOU 2550  CG  LYS B  30    20187  19794  15445    417   -920   -450       C  
ATOM   2551  CD  LYS B  30     -27.545  22.436 -26.441  1.00147.42           C  
ANISOU 2551  CD  LYS B  30    20599  20367  15047    298  -1336    -14       C  
ATOM   2552  CE  LYS B  30     -26.621  23.288 -27.294  1.00148.88           C  
ANISOU 2552  CE  LYS B  30    21074  20840  14652    175  -1006    322       C  
ATOM   2553  NZ  LYS B  30     -27.292  23.886 -28.476  1.00153.99           N  
ANISOU 2553  NZ  LYS B  30    21995  21889  14625     45  -1415    802       N  
ATOM   2554  N   LEU B  31     -29.915  20.911 -21.987  1.00145.51           N  
ANISOU 2554  N   LEU B  31    19178  18643  17463    750  -1741   -537       N  
ATOM   2555  CA  LEU B  31     -31.302  20.531 -21.918  1.00146.89           C  
ANISOU 2555  CA  LEU B  31    19135  18816  17861    718  -2193   -538       C  
ATOM   2556  C   LEU B  31     -31.898  20.762 -20.528  1.00137.93           C  
ANISOU 2556  C   LEU B  31    17667  17262  17477    856  -2136   -419       C  
ATOM   2557  O   LEU B  31     -32.980  20.272 -20.241  1.00140.56           O  
ANISOU 2557  O   LEU B  31    17754  17543  18108    815  -2412   -495       O  
ATOM   2558  CB  LEU B  31     -31.394  19.061 -22.319  1.00152.29           C  
ANISOU 2558  CB  LEU B  31    19922  19612  18329    535  -2306  -1121       C  
ATOM   2559  CG  LEU B  31     -30.457  18.707 -23.501  1.00161.84           C  
ANISOU 2559  CG  LEU B  31    21516  21170  18802    413  -2151  -1394       C  
ATOM   2560  CD1 LEU B  31     -30.379  17.212 -23.706  1.00166.30           C  
ANISOU 2560  CD1 LEU B  31    22212  21704  19271    269  -2139  -2061       C  
ATOM   2561  CD2 LEU B  31     -30.845  19.399 -24.809  1.00168.01           C  
ANISOU 2561  CD2 LEU B  31    22480  22436  18917    300  -2484  -1059       C  
ATOM   2562  N   VAL B  32     -31.202  21.523 -19.681  1.00126.34           N  
ANISOU 2562  N   VAL B  32    16190  15518  16292    986  -1766   -245       N  
ATOM   2563  CA  VAL B  32     -31.764  21.998 -18.430  1.00114.90           C  
ANISOU 2563  CA  VAL B  32    14483  13706  15467   1111  -1675    -89       C  
ATOM   2564  C   VAL B  32     -32.434  23.300 -18.746  1.00110.11           C  
ANISOU 2564  C   VAL B  32    13778  13098  14958   1251  -1842    428       C  
ATOM   2565  O   VAL B  32     -31.778  24.210 -19.245  1.00114.99           O  
ANISOU 2565  O   VAL B  32    14599  13762  15329   1283  -1724    716       O  
ATOM   2566  CB  VAL B  32     -30.694  22.277 -17.372  1.00113.23           C  
ANISOU 2566  CB  VAL B  32    14340  13207  15474   1152  -1228   -159       C  
ATOM   2567  CG1 VAL B  32     -31.262  23.027 -16.177  1.00112.34           C  
ANISOU 2567  CG1 VAL B  32    14032  12746  15903   1264  -1103     28       C  
ATOM   2568  CG2 VAL B  32     -30.097  20.966 -16.903  1.00113.08           C  
ANISOU 2568  CG2 VAL B  32    14367  13129  15469   1072  -1092   -613       C  
ATOM   2569  N   PRO B  33     -33.719  23.419 -18.416  1.00103.65           N  
ANISOU 2569  N   PRO B  33    12633  12196  14552   1344  -2085    569       N  
ATOM   2570  CA  PRO B  33     -34.428  24.635 -18.749  1.00104.40           C  
ANISOU 2570  CA  PRO B  33    12590  12260  14816   1541  -2273   1090       C  
ATOM   2571  C   PRO B  33     -33.751  25.822 -18.107  1.00 99.85           C  
ANISOU 2571  C   PRO B  33    12147  11317  14474   1677  -1868   1322       C  
ATOM   2572  O   PRO B  33     -33.411  25.763 -16.920  1.00 93.83           O  
ANISOU 2572  O   PRO B  33    11357  10247  14044   1674  -1506   1093       O  
ATOM   2573  CB  PRO B  33     -35.810  24.406 -18.144  1.00106.56           C  
ANISOU 2573  CB  PRO B  33    12402  12436  15649   1630  -2463   1085       C  
ATOM   2574  CG  PRO B  33     -35.586  23.416 -17.057  1.00101.99           C  
ANISOU 2574  CG  PRO B  33    11790  11670  15289   1493  -2170    618       C  
ATOM   2575  CD  PRO B  33     -34.520  22.525 -17.563  1.00100.81           C  
ANISOU 2575  CD  PRO B  33    11988  11702  14611   1291  -2119    285       C  
ATOM   2576  N   LYS B  34     -33.561  26.879 -18.896  1.00102.58           N  
ANISOU 2576  N   LYS B  34    12659  11694  14620   1764  -1944   1778       N  
ATOM   2577  CA  LYS B  34     -32.830  28.075 -18.445  1.00102.03           C  
ANISOU 2577  CA  LYS B  34    12777  11251  14735   1837  -1563   2013       C  
ATOM   2578  C   LYS B  34     -33.716  29.119 -17.804  1.00100.25           C  
ANISOU 2578  C   LYS B  34    12329  10599  15161   2116  -1522   2320       C  
ATOM   2579  O   LYS B  34     -33.314  29.755 -16.842  1.00 97.17           O  
ANISOU 2579  O   LYS B  34    12006   9792  15120   2148  -1122   2252       O  
ATOM   2580  CB  LYS B  34     -32.018  28.678 -19.591  1.00108.95           C  
ANISOU 2580  CB  LYS B  34    14006  12325  15065   1740  -1577   2350       C  
ATOM   2581  CG  LYS B  34     -30.659  28.003 -19.719  1.00111.87           C  
ANISOU 2581  CG  LYS B  34    14621  12907  14977   1480  -1286   1976       C  
ATOM   2582  CD  LYS B  34     -30.079  27.995 -21.130  1.00119.80           C  
ANISOU 2582  CD  LYS B  34    15921  14345  15252   1323  -1381   2153       C  
ATOM   2583  CE  LYS B  34     -28.857  27.073 -21.200  1.00118.46           C  
ANISOU 2583  CE  LYS B  34    15888  14409  14710   1111  -1074   1667       C  
ATOM   2584  NZ  LYS B  34     -28.167  27.121 -22.518  1.00122.94           N  
ANISOU 2584  NZ  LYS B  34    16760  15401  14551    937  -1034   1795       N  
ATOM   2585  N   THR B  35     -34.936  29.246 -18.293  1.00102.32           N  
ANISOU 2585  N   THR B  35    12301  10969  15606   2314  -1932   2614       N  
ATOM   2586  CA  THR B  35     -35.863  30.234 -17.783  1.00104.45           C  
ANISOU 2586  CA  THR B  35    12296  10834  16554   2648  -1899   2924       C  
ATOM   2587  C   THR B  35     -36.916  29.707 -16.792  1.00102.48           C  
ANISOU 2587  C   THR B  35    11577  10485  16875   2758  -1850   2632       C  
ATOM   2588  O   THR B  35     -37.902  30.389 -16.532  1.00106.24           O  
ANISOU 2588  O   THR B  35    11714  10718  17931   3071  -1886   2886       O  
ATOM   2589  CB  THR B  35     -36.608  30.871 -18.954  1.00113.29           C  
ANISOU 2589  CB  THR B  35    13317  12116  17611   2864  -2404   3544       C  
ATOM   2590  OG1 THR B  35     -37.356  29.860 -19.625  1.00115.20           O  
ANISOU 2590  OG1 THR B  35    13296  12887  17588   2772  -2922   3459       O  
ATOM   2591  CG2 THR B  35     -35.625  31.530 -19.945  1.00117.02           C  
ANISOU 2591  CG2 THR B  35    14284  12662  17515   2749  -2415   3926       C  
ATOM   2592  N   HIS B  36     -36.757  28.488 -16.273  1.00 97.60           N  
ANISOU 2592  N   HIS B  36    10914  10048  16120   2512  -1764   2128       N  
ATOM   2593  CA  HIS B  36     -37.599  28.005 -15.160  1.00 94.87           C  
ANISOU 2593  CA  HIS B  36    10188   9561  16295   2550  -1588   1835       C  
ATOM   2594  C   HIS B  36     -36.977  26.849 -14.392  1.00 88.36           C  
ANISOU 2594  C   HIS B  36     9510   8791  15272   2248  -1344   1314       C  
ATOM   2595  O   HIS B  36     -36.149  26.101 -14.904  1.00 87.96           O  
ANISOU 2595  O   HIS B  36     9730   8984  14705   2024  -1445   1136       O  
ATOM   2596  CB  HIS B  36     -39.011  27.600 -15.618  1.00 99.28           C  
ANISOU 2596  CB  HIS B  36    10215  10390  17116   2653  -2040   1972       C  
ATOM   2597  CG  HIS B  36     -39.066  26.320 -16.403  1.00 99.31           C  
ANISOU 2597  CG  HIS B  36    10213  10879  16640   2356  -2462   1764       C  
ATOM   2598  ND1 HIS B  36     -39.109  26.297 -17.782  1.00102.69           N  
ANISOU 2598  ND1 HIS B  36    10727  11699  16591   2313  -2984   2024       N  
ATOM   2599  CD2 HIS B  36     -39.131  25.024 -16.003  1.00 95.74           C  
ANISOU 2599  CD2 HIS B  36     9700  10559  16117   2074  -2437   1315       C  
ATOM   2600  CE1 HIS B  36     -39.184  25.045 -18.196  1.00102.28           C  
ANISOU 2600  CE1 HIS B  36    10674  11997  16188   2009  -3247   1685       C  
ATOM   2601  NE2 HIS B  36     -39.208  24.254 -17.135  1.00 98.18           N  
ANISOU 2601  NE2 HIS B  36    10059  11296  15947   1869  -2923   1263       N  
ATOM   2602  N   LEU B  37     -37.438  26.694 -13.161  1.00 85.66           N  
ANISOU 2602  N   LEU B  37     8970   8215  15360   2261  -1017   1086       N  
ATOM   2603  CA  LEU B  37     -37.032  25.587 -12.307  1.00 80.58           C  
ANISOU 2603  CA  LEU B  37     8428   7589  14598   1996   -806    662       C  
ATOM   2604  C   LEU B  37     -37.905  24.348 -12.562  1.00 82.39           C  
ANISOU 2604  C   LEU B  37     8346   8095  14863   1842  -1111    509       C  
ATOM   2605  O   LEU B  37     -39.043  24.470 -13.025  1.00 84.59           O  
ANISOU 2605  O   LEU B  37     8211   8509  15421   1958  -1396    697       O  
ATOM   2606  CB  LEU B  37     -37.128  25.987 -10.841  1.00 77.76           C  
ANISOU 2606  CB  LEU B  37     8056   6878  14610   2028   -298    500       C  
ATOM   2607  CG  LEU B  37     -36.367  27.243 -10.462  1.00 75.43           C  
ANISOU 2607  CG  LEU B  37     8060   6253  14346   2134     26    589       C  
ATOM   2608  CD1 LEU B  37     -36.761  27.712  -9.073  1.00 75.03           C  
ANISOU 2608  CD1 LEU B  37     7951   5865  14690   2182    512    408       C  
ATOM   2609  CD2 LEU B  37     -34.885  26.968 -10.539  1.00 72.06           C  
ANISOU 2609  CD2 LEU B  37     8060   5899  13420   1909     68    453       C  
ATOM   2610  N   MET B  38     -37.398  23.179 -12.142  1.00 80.09           N  
ANISOU 2610  N   MET B  38     8227   7844  14357   1579  -1030    172       N  
ATOM   2611  CA  MET B  38     -37.881  21.888 -12.604  1.00 80.89           C  
ANISOU 2611  CA  MET B  38     8190   8181  14362   1358  -1345    -17       C  
ATOM   2612  C   MET B  38     -38.753  21.261 -11.549  1.00 79.91           C  
ANISOU 2612  C   MET B  38     7770   7933  14657   1232  -1148   -172       C  
ATOM   2613  O   MET B  38     -38.433  21.331 -10.354  1.00 75.02           O  
ANISOU 2613  O   MET B  38     7277   7068  14157   1209   -720   -274       O  
ATOM   2614  CB  MET B  38     -36.719  20.950 -12.840  1.00 79.68           C  
ANISOU 2614  CB  MET B  38     8444   8081  13748   1166  -1351   -286       C  
ATOM   2615  CG  MET B  38     -35.761  21.435 -13.890  1.00 81.50           C  
ANISOU 2615  CG  MET B  38     8977   8475  13513   1238  -1476   -180       C  
ATOM   2616  SD  MET B  38     -34.340  20.330 -14.035  1.00 81.55           S  
ANISOU 2616  SD  MET B  38     9393   8514  13079   1068  -1375   -539       S  
ATOM   2617  CE  MET B  38     -34.915  19.482 -15.505  1.00 86.08           C  
ANISOU 2617  CE  MET B  38     9934   9445  13327    917  -1866   -674       C  
ATOM   2618  N   SER B  39     -39.832  20.629 -12.004  1.00 83.06           N  
ANISOU 2618  N   SER B  39     7787   8529  15242   1110  -1467   -190       N  
ATOM   2619  CA  SER B  39     -40.621  19.734 -11.156  1.00 84.42           C  
ANISOU 2619  CA  SER B  39     7692   8626  15757    879  -1312   -370       C  
ATOM   2620  C   SER B  39     -39.824  18.506 -10.793  1.00 82.38           C  
ANISOU 2620  C   SER B  39     7826   8248  15225    601  -1216   -663       C  
ATOM   2621  O   SER B  39     -38.748  18.240 -11.348  1.00 77.31           O  
ANISOU 2621  O   SER B  39     7591   7630  14152    595  -1325   -764       O  
ATOM   2622  CB  SER B  39     -41.920  19.325 -11.846  1.00 89.69           C  
ANISOU 2622  CB  SER B  39     7827   9561  16688    760  -1733   -326       C  
ATOM   2623  OG  SER B  39     -41.681  19.037 -13.208  1.00 91.61           O  
ANISOU 2623  OG  SER B  39     8208  10085  16514    689  -2257   -338       O  
ATOM   2624  N   GLU B  40     -40.373  17.759  -9.845  1.00 86.75           N  
ANISOU 2624  N   GLU B  40     8239   8659  16060    381   -986   -779       N  
ATOM   2625  CA  GLU B  40     -39.777  16.495  -9.417  1.00 87.77           C  
ANISOU 2625  CA  GLU B  40     8709   8613  16024    114   -905  -1005       C  
ATOM   2626  C   GLU B  40     -39.653  15.535 -10.595  1.00 89.30           C  
ANISOU 2626  C   GLU B  40     9012   8931  15987    -63  -1348  -1203       C  
ATOM   2627  O   GLU B  40     -38.558  15.078 -10.909  1.00 88.15           O  
ANISOU 2627  O   GLU B  40     9290   8710  15493    -50  -1382  -1353       O  
ATOM   2628  CB  GLU B  40     -40.587  15.876  -8.304  1.00 91.35           C  
ANISOU 2628  CB  GLU B  40     8957   8912  16838   -132   -611  -1033       C  
ATOM   2629  CG  GLU B  40     -39.913  14.667  -7.687  1.00 93.30           C  
ANISOU 2629  CG  GLU B  40     9610   8901  16939   -371   -485  -1178       C  
ATOM   2630  CD  GLU B  40     -40.307  14.459  -6.231  1.00 97.70           C  
ANISOU 2630  CD  GLU B  40    10142   9273  17706   -538    -26  -1103       C  
ATOM   2631  OE1 GLU B  40     -40.365  15.460  -5.463  1.00 97.88           O  
ANISOU 2631  OE1 GLU B  40    10108   9308  17773   -370    320   -988       O  
ATOM   2632  OE2 GLU B  40     -40.554  13.286  -5.854  1.00100.05           O  
ANISOU 2632  OE2 GLU B  40    10511   9396  18108   -858      6  -1165       O  
ATOM   2633  N   SER B  41     -40.753  15.323 -11.303  1.00 94.57           N  
ANISOU 2633  N   SER B  41     9277   9815  16838   -211  -1693  -1213       N  
ATOM   2634  CA  SER B  41     -40.716  14.587 -12.569  1.00 98.87           C  
ANISOU 2634  CA  SER B  41     9926  10541  17097   -393  -2163  -1428       C  
ATOM   2635  C   SER B  41     -39.585  15.084 -13.492  1.00 97.98           C  
ANISOU 2635  C   SER B  41    10212  10569  16447   -165  -2291  -1431       C  
ATOM   2636  O   SER B  41     -38.755  14.290 -13.958  1.00101.59           O  
ANISOU 2636  O   SER B  41    11065  10960  16571   -260  -2341  -1706       O  
ATOM   2637  CB  SER B  41     -42.067  14.627 -13.292  1.00104.51           C  
ANISOU 2637  CB  SER B  41    10094  11575  18038   -546  -2596  -1370       C  
ATOM   2638  OG  SER B  41     -42.737  15.865 -13.091  1.00108.69           O  
ANISOU 2638  OG  SER B  41    10181  12250  18865   -259  -2550  -1021       O  
ATOM   2639  N   GLU B  42     -39.514  16.393 -13.701  1.00 96.62           N  
ANISOU 2639  N   GLU B  42     9944  10548  16218    138  -2285  -1127       N  
ATOM   2640  CA  GLU B  42     -38.548  16.966 -14.639  1.00 95.21           C  
ANISOU 2640  CA  GLU B  42    10100  10539  15534    317  -2399  -1069       C  
ATOM   2641  C   GLU B  42     -37.114  16.576 -14.329  1.00 89.04           C  
ANISOU 2641  C   GLU B  42     9803   9553  14475    351  -2091  -1263       C  
ATOM   2642  O   GLU B  42     -36.396  16.153 -15.230  1.00 89.21           O  
ANISOU 2642  O   GLU B  42    10121   9702  14071    308  -2221  -1458       O  
ATOM   2643  CB  GLU B  42     -38.729  18.487 -14.761  1.00 97.64           C  
ANISOU 2643  CB  GLU B  42    10237  10945  15916    633  -2390   -655       C  
ATOM   2644  CG  GLU B  42     -39.834  18.864 -15.748  1.00105.05           C  
ANISOU 2644  CG  GLU B  42    10792  12226  16894    649  -2896   -433       C  
ATOM   2645  CD  GLU B  42     -40.140  20.343 -15.770  1.00107.60           C  
ANISOU 2645  CD  GLU B  42    10906  12554  17424   1003  -2879     23       C  
ATOM   2646  OE1 GLU B  42     -39.217  21.110 -16.064  1.00106.40           O  
ANISOU 2646  OE1 GLU B  42    11099  12363  16964   1177  -2757    183       O  
ATOM   2647  OE2 GLU B  42     -41.293  20.735 -15.509  1.00112.90           O  
ANISOU 2647  OE2 GLU B  42    11055  13248  18594   1110  -2973    224       O  
ATOM   2648  N   TRP B  43     -36.695  16.708 -13.073  1.00 83.89           N  
ANISOU 2648  N   TRP B  43     9216   8610  14047    425  -1688  -1219       N  
ATOM   2649  CA  TRP B  43     -35.308  16.373 -12.720  1.00 79.15           C  
ANISOU 2649  CA  TRP B  43     9007   7841  13222    478  -1438  -1358       C  
ATOM   2650  C   TRP B  43     -35.066  14.861 -12.610  1.00 78.46           C  
ANISOU 2650  C   TRP B  43     9100   7564  13147    282  -1457  -1681       C  
ATOM   2651  O   TRP B  43     -33.984  14.377 -12.962  1.00 77.52           O  
ANISOU 2651  O   TRP B  43     9277   7402  12773    336  -1408  -1868       O  
ATOM   2652  CB  TRP B  43     -34.753  17.160 -11.502  1.00 75.06           C  
ANISOU 2652  CB  TRP B  43     8550   7131  12837    622  -1056  -1183       C  
ATOM   2653  CG  TRP B  43     -35.526  17.195 -10.200  1.00 76.17           C  
ANISOU 2653  CG  TRP B  43     8500   7075  13364    552   -819  -1102       C  
ATOM   2654  CD1 TRP B  43     -36.254  18.243  -9.736  1.00 78.84           C  
ANISOU 2654  CD1 TRP B  43     8590   7409  13954    659   -670   -903       C  
ATOM   2655  CD2 TRP B  43     -35.562  16.199  -9.152  1.00 76.47           C  
ANISOU 2655  CD2 TRP B  43     8618   6879  13557    372   -644  -1206       C  
ATOM   2656  NE1 TRP B  43     -36.775  17.955  -8.501  1.00 79.68           N  
ANISOU 2656  NE1 TRP B  43     8605   7339  14331    539   -388   -918       N  
ATOM   2657  CE2 TRP B  43     -36.349  16.716  -8.112  1.00 77.25           C  
ANISOU 2657  CE2 TRP B  43     8512   6897  13941    346   -378  -1073       C  
ATOM   2658  CE3 TRP B  43     -35.020  14.921  -9.002  1.00 77.41           C  
ANISOU 2658  CE3 TRP B  43     8973   6826  13614    240   -673  -1384       C  
ATOM   2659  CZ2 TRP B  43     -36.622  16.000  -6.945  1.00 77.79           C  
ANISOU 2659  CZ2 TRP B  43     8621   6770  14165    149   -142  -1092       C  
ATOM   2660  CZ3 TRP B  43     -35.279  14.213  -7.822  1.00 77.16           C  
ANISOU 2660  CZ3 TRP B  43     8986   6550  13781     68   -475  -1358       C  
ATOM   2661  CH2 TRP B  43     -36.073  14.754  -6.816  1.00 77.41           C  
ANISOU 2661  CH2 TRP B  43     8828   6557  14025      3   -213  -1205       C  
ATOM   2662  N   ARG B  44     -36.039  14.107 -12.126  1.00 77.76           N  
ANISOU 2662  N   ARG B  44     8828   7331  13383     58  -1498  -1747       N  
ATOM   2663  CA  ARG B  44     -35.878  12.648 -12.127  1.00 77.83           C  
ANISOU 2663  CA  ARG B  44     9037   7094  13439   -150  -1539  -2046       C  
ATOM   2664  C   ARG B  44     -35.546  12.150 -13.520  1.00 82.82           C  
ANISOU 2664  C   ARG B  44     9857   7887  13723   -197  -1811  -2350       C  
ATOM   2665  O   ARG B  44     -34.639  11.368 -13.681  1.00 81.89           O  
ANISOU 2665  O   ARG B  44    10052   7581  13479   -163  -1725  -2597       O  
ATOM   2666  CB  ARG B  44     -37.107  11.930 -11.613  1.00 78.12           C  
ANISOU 2666  CB  ARG B  44     8825   6984  13873   -460  -1582  -2070       C  
ATOM   2667  CG  ARG B  44     -37.204  11.985 -10.111  1.00 75.09           C  
ANISOU 2667  CG  ARG B  44     8405   6354  13771   -473  -1220  -1859       C  
ATOM   2668  CD  ARG B  44     -38.307  11.102  -9.546  1.00 78.13           C  
ANISOU 2668  CD  ARG B  44     8590   6553  14542   -832  -1188  -1885       C  
ATOM   2669  NE  ARG B  44     -38.464  11.338  -8.114  1.00 76.89           N  
ANISOU 2669  NE  ARG B  44     8396   6241  14574   -849   -798  -1647       N  
ATOM   2670  CZ  ARG B  44     -37.599  10.956  -7.168  1.00 74.22           C  
ANISOU 2670  CZ  ARG B  44     8414   5633  14153   -806   -558  -1567       C  
ATOM   2671  NH1 ARG B  44     -36.488  10.297  -7.467  1.00 72.25           N  
ANISOU 2671  NH1 ARG B  44     8537   5197  13717   -700   -652  -1695       N  
ATOM   2672  NH2 ARG B  44     -37.845  11.254  -5.886  1.00 74.54           N  
ANISOU 2672  NH2 ARG B  44     8428   5604  14289   -862   -213  -1351       N  
ATOM   2673  N   ASN B  45     -36.248  12.662 -14.527  1.00 89.25           N  
ANISOU 2673  N   ASN B  45    10481   9065  14363   -252  -2132  -2320       N  
ATOM   2674  CA  ASN B  45     -35.964  12.334 -15.935  1.00 93.64           C  
ANISOU 2674  CA  ASN B  45    11249   9866  14461   -323  -2402  -2602       C  
ATOM   2675  C   ASN B  45     -34.548  12.541 -16.391  1.00 92.59           C  
ANISOU 2675  C   ASN B  45    11471   9785  13922    -93  -2201  -2694       C  
ATOM   2676  O   ASN B  45     -34.118  11.913 -17.332  1.00 93.38           O  
ANISOU 2676  O   ASN B  45    11832   9966  13681   -168  -2282  -3044       O  
ATOM   2677  CB  ASN B  45     -36.871  13.128 -16.863  1.00 99.67           C  
ANISOU 2677  CB  ASN B  45    11746  11082  15041   -371  -2800  -2417       C  
ATOM   2678  CG  ASN B  45     -38.245  12.519 -16.951  1.00106.03           C  
ANISOU 2678  CG  ASN B  45    12215  11935  16134   -706  -3136  -2513       C  
ATOM   2679  OD1 ASN B  45     -38.764  12.018 -15.950  1.00107.04           O  
ANISOU 2679  OD1 ASN B  45    12155  11766  16746   -839  -2976  -2509       O  
ATOM   2680  ND2 ASN B  45     -38.869  12.605 -18.123  1.00111.16           N  
ANISOU 2680  ND2 ASN B  45    12761  12990  16483   -867  -3612  -2566       N  
ATOM   2681  N   LEU B  46     -33.850  13.494 -15.784  1.00 91.83           N  
ANISOU 2681  N   LEU B  46    11368   9677  13847    167  -1932  -2394       N  
ATOM   2682  CA  LEU B  46     -32.432  13.682 -16.090  1.00 92.88           C  
ANISOU 2682  CA  LEU B  46    11771   9852  13665    366  -1695  -2466       C  
ATOM   2683  C   LEU B  46     -31.561  12.620 -15.447  1.00 91.43           C  
ANISOU 2683  C   LEU B  46    11775   9297  13667    420  -1451  -2715       C  
ATOM   2684  O   LEU B  46     -30.350  12.558 -15.725  1.00 92.71           O  
ANISOU 2684  O   LEU B  46    12114   9480  13631    590  -1248  -2839       O  
ATOM   2685  CB  LEU B  46     -31.943  15.071 -15.655  1.00 89.10           C  
ANISOU 2685  CB  LEU B  46    11214   9469  13169    577  -1504  -2073       C  
ATOM   2686  CG  LEU B  46     -32.537  16.253 -16.398  1.00 90.94           C  
ANISOU 2686  CG  LEU B  46    11320  10028  13202    607  -1709  -1767       C  
ATOM   2687  CD1 LEU B  46     -31.999  17.506 -15.738  1.00 89.67           C  
ANISOU 2687  CD1 LEU B  46    11122   9806  13140    794  -1451  -1424       C  
ATOM   2688  CD2 LEU B  46     -32.234  16.283 -17.895  1.00 94.76           C  
ANISOU 2688  CD2 LEU B  46    12006  10881  13116    559  -1885  -1879       C  
ATOM   2689  N   GLY B  47     -32.168  11.838 -14.560  1.00 89.74           N  
ANISOU 2689  N   GLY B  47    11493   8746  13856    286  -1457  -2743       N  
ATOM   2690  CA  GLY B  47     -31.500  10.747 -13.891  1.00 88.39           C  
ANISOU 2690  CA  GLY B  47    11502   8160  13920    331  -1280  -2911       C  
ATOM   2691  C   GLY B  47     -31.052  11.118 -12.505  1.00 81.89           C  
ANISOU 2691  C   GLY B  47    10622   7159  13333    466  -1060  -2589       C  
ATOM   2692  O   GLY B  47     -30.038  10.622 -12.042  1.00 84.27           O  
ANISOU 2692  O   GLY B  47    11064   7242  13711    628   -905  -2623       O  
ATOM   2693  N   VAL B  48     -31.758  12.017 -11.847  1.00 75.60           N  
ANISOU 2693  N   VAL B  48     9616   6466  12639    415  -1044  -2282       N  
ATOM   2694  CA  VAL B  48     -31.334  12.418 -10.526  1.00 70.25           C  
ANISOU 2694  CA  VAL B  48     8932   5655  12104    500   -828  -2017       C  
ATOM   2695  C   VAL B  48     -32.071  11.522  -9.579  1.00 68.00           C  
ANISOU 2695  C   VAL B  48     8647   5050  12140    299   -800  -1977       C  
ATOM   2696  O   VAL B  48     -33.265  11.389  -9.711  1.00 67.78           O  
ANISOU 2696  O   VAL B  48     8448   5039  12264     88   -898  -1994       O  
ATOM   2697  CB  VAL B  48     -31.624  13.926 -10.260  1.00 68.53           C  
ANISOU 2697  CB  VAL B  48     8538   5677  11823    559   -749  -1745       C  
ATOM   2698  CG1 VAL B  48     -31.450  14.275  -8.783  1.00 65.89           C  
ANISOU 2698  CG1 VAL B  48     8216   5191  11624    557   -525  -1530       C  
ATOM   2699  CG2 VAL B  48     -30.700  14.810 -11.108  1.00 66.88           C  
ANISOU 2699  CG2 VAL B  48     8381   5731  11297    738   -736  -1731       C  
ATOM   2700  N   GLN B  49     -31.345  10.995  -8.599  1.00 65.91           N  
ANISOU 2700  N   GLN B  49     8548   4523  11970    360   -669  -1878       N  
ATOM   2701  CA  GLN B  49     -31.871  10.053  -7.651  1.00 68.68           C  
ANISOU 2701  CA  GLN B  49     8976   4531  12588    165   -618  -1786       C  
ATOM   2702  C   GLN B  49     -31.682  10.559  -6.252  1.00 66.97           C  
ANISOU 2702  C   GLN B  49     8788   4301  12355    163   -430  -1470       C  
ATOM   2703  O   GLN B  49     -30.573  10.730  -5.779  1.00 66.89           O  
ANISOU 2703  O   GLN B  49     8901   4295  12218    344   -391  -1361       O  
ATOM   2704  CB  GLN B  49     -31.178   8.699  -7.788  1.00 73.89           C  
ANISOU 2704  CB  GLN B  49     9884   4810  13379    229   -673  -1943       C  
ATOM   2705  CG  GLN B  49     -30.887   8.301  -9.229  1.00 76.73           C  
ANISOU 2705  CG  GLN B  49    10298   5214  13641    314   -802  -2336       C  
ATOM   2706  CD  GLN B  49     -30.964   6.827  -9.470  1.00 81.57           C  
ANISOU 2706  CD  GLN B  49    11122   5362  14506    217   -857  -2586       C  
ATOM   2707  OE1 GLN B  49     -29.942   6.189  -9.714  1.00 87.65           O  
ANISOU 2707  OE1 GLN B  49    12070   5910  15321    459   -815  -2742       O  
ATOM   2708  NE2 GLN B  49     -32.169   6.267  -9.417  1.00 84.14           N  
ANISOU 2708  NE2 GLN B  49    11412   5515  15039   -137   -936  -2640       N  
ATOM   2709  N   GLN B  50     -32.802  10.693  -5.554  1.00 68.81           N  
ANISOU 2709  N   GLN B  50     8901   4517  12725    -73   -309  -1336       N  
ATOM   2710  CA  GLN B  50     -32.935  11.402  -4.291  1.00 66.73           C  
ANISOU 2710  CA  GLN B  50     8640   4323  12390   -133    -74  -1089       C  
ATOM   2711  C   GLN B  50     -34.319  11.075  -3.686  1.00 68.12           C  
ANISOU 2711  C   GLN B  50     8676   4406  12798   -448     88  -1009       C  
ATOM   2712  O   GLN B  50     -35.254  10.734  -4.413  1.00 67.58           O  
ANISOU 2712  O   GLN B  50     8390   4340  12947   -590    -13  -1148       O  
ATOM   2713  CB  GLN B  50     -32.995  12.832  -4.678  1.00 69.64           C  
ANISOU 2713  CB  GLN B  50     8820   5010  12629      5    -23  -1110       C  
ATOM   2714  CG  GLN B  50     -32.206  13.799  -3.862  1.00 71.17           C  
ANISOU 2714  CG  GLN B  50     9124   5315  12599    107    131   -980       C  
ATOM   2715  CD  GLN B  50     -32.290  15.165  -4.473  1.00 71.84           C  
ANISOU 2715  CD  GLN B  50     9040   5634  12622    246    165  -1019       C  
ATOM   2716  OE1 GLN B  50     -32.896  15.404  -5.541  1.00 70.06           O  
ANISOU 2716  OE1 GLN B  50     8611   5516  12489    299     40  -1100       O  
ATOM   2717  NE2 GLN B  50     -31.691  16.079  -3.796  1.00 76.93           N  
ANISOU 2717  NE2 GLN B  50     9782   6346  13101    289    315   -947       N  
ATOM   2718  N   SER B  51     -34.501  11.251  -2.389  1.00 69.54           N  
ANISOU 2718  N   SER B  51     8947   4556  12915   -583    350   -799       N  
ATOM   2719  CA  SER B  51     -35.850  11.124  -1.780  1.00 74.02           C  
ANISOU 2719  CA  SER B  51     9326   5103  13693   -887    603   -725       C  
ATOM   2720  C   SER B  51     -36.849  12.223  -2.220  1.00 77.25           C  
ANISOU 2720  C   SER B  51     9306   5788  14254   -846    711   -824       C  
ATOM   2721  O   SER B  51     -36.498  13.175  -2.904  1.00 76.20           O  
ANISOU 2721  O   SER B  51     9076   5847  14030   -587    601   -906       O  
ATOM   2722  CB  SER B  51     -35.757  11.083  -0.249  1.00 73.90           C  
ANISOU 2722  CB  SER B  51     9561   5027  13490  -1055    909   -479       C  
ATOM   2723  OG  SER B  51     -34.723  11.906   0.207  1.00 72.14           O  
ANISOU 2723  OG  SER B  51     9537   4950  12924   -856    924   -431       O  
ATOM   2724  N   GLN B  52     -38.098  12.063  -1.806  1.00 83.39           N  
ANISOU 2724  N   GLN B  52     9813   6572  15298  -1102    937   -786       N  
ATOM   2725  CA  GLN B  52     -39.144  13.017  -2.114  1.00 85.48           C  
ANISOU 2725  CA  GLN B  52     9602   7072  15802  -1043   1058   -843       C  
ATOM   2726  C   GLN B  52     -38.939  14.391  -1.531  1.00 82.25           C  
ANISOU 2726  C   GLN B  52     9201   6805  15245   -822   1351   -813       C  
ATOM   2727  O   GLN B  52     -38.196  14.577  -0.574  1.00 78.72           O  
ANISOU 2727  O   GLN B  52     9117   6303  14488   -828   1552   -746       O  
ATOM   2728  CB  GLN B  52     -40.493  12.497  -1.636  1.00 93.72           C  
ANISOU 2728  CB  GLN B  52    10312   8096  17200  -1386   1306   -800       C  
ATOM   2729  CG  GLN B  52     -41.439  12.112  -2.771  1.00101.08           C  
ANISOU 2729  CG  GLN B  52    10782   9119  18504  -1498    991   -920       C  
ATOM   2730  CD  GLN B  52     -42.450  13.215  -3.093  1.00107.29           C  
ANISOU 2730  CD  GLN B  52    10979  10195  19591  -1336   1071   -929       C  
ATOM   2731  OE1 GLN B  52     -42.151  14.433  -3.007  1.00105.64           O  
ANISOU 2731  OE1 GLN B  52    10764  10097  19277   -998   1199   -900       O  
ATOM   2732  NE2 GLN B  52     -43.678  12.791  -3.451  1.00114.77           N  
ANISOU 2732  NE2 GLN B  52    11400  11244  20963  -1584    993   -959       N  
ATOM   2733  N   GLY B  53     -39.626  15.363  -2.140  1.00 82.49           N  
ANISOU 2733  N   GLY B  53     8822   7007  15512   -630   1348   -864       N  
ATOM   2734  CA  GLY B  53     -39.750  16.723  -1.599  1.00 81.00           C  
ANISOU 2734  CA  GLY B  53     8559   6886  15330   -427   1697   -864       C  
ATOM   2735  C   GLY B  53     -38.522  17.606  -1.617  1.00 77.55           C  
ANISOU 2735  C   GLY B  53     8479   6435  14552   -190   1649   -883       C  
ATOM   2736  O   GLY B  53     -38.548  18.668  -1.017  1.00 79.46           O  
ANISOU 2736  O   GLY B  53     8749   6664  14776    -78   1977   -918       O  
ATOM   2737  N   TRP B  54     -37.433  17.172  -2.259  1.00 74.06           N  
ANISOU 2737  N   TRP B  54     8308   5979  13852   -133   1282   -884       N  
ATOM   2738  CA  TRP B  54     -36.331  18.062  -2.580  1.00 71.51           C  
ANISOU 2738  CA  TRP B  54     8204   5686  13278     88   1184   -897       C  
ATOM   2739  C   TRP B  54     -36.851  18.970  -3.682  1.00 72.98           C  
ANISOU 2739  C   TRP B  54     8069   5971  13689    328   1042   -878       C  
ATOM   2740  O   TRP B  54     -37.522  18.464  -4.596  1.00 75.39           O  
ANISOU 2740  O   TRP B  54     8096   6367  14180    320    769   -869       O  
ATOM   2741  CB  TRP B  54     -35.067  17.341  -3.062  1.00 67.89           C  
ANISOU 2741  CB  TRP B  54     8036   5219  12540    105    861   -906       C  
ATOM   2742  CG  TRP B  54     -34.330  16.639  -1.971  1.00 66.49           C  
ANISOU 2742  CG  TRP B  54     8197   4939  12125    -54    945   -856       C  
ATOM   2743  CD1 TRP B  54     -34.370  15.326  -1.707  1.00 67.71           C  
ANISOU 2743  CD1 TRP B  54     8459   4962  12302   -222    858   -806       C  
ATOM   2744  CD2 TRP B  54     -33.427  17.217  -1.005  1.00 64.46           C  
ANISOU 2744  CD2 TRP B  54     8226   4697  11568    -73   1094   -826       C  
ATOM   2745  NE1 TRP B  54     -33.589  15.027  -0.629  1.00 67.24           N  
ANISOU 2745  NE1 TRP B  54     8727   4841  11980   -315    931   -694       N  
ATOM   2746  CE2 TRP B  54     -32.986  16.163  -0.177  1.00 64.62           C  
ANISOU 2746  CE2 TRP B  54     8501   4629  11419   -240   1056   -716       C  
ATOM   2747  CE3 TRP B  54     -32.949  18.514  -0.763  1.00 61.50           C  
ANISOU 2747  CE3 TRP B  54     7928   4385  11054     11   1236   -879       C  
ATOM   2748  CZ2 TRP B  54     -32.092  16.350   0.868  1.00 64.23           C  
ANISOU 2748  CZ2 TRP B  54     8754   4618  11029   -322   1105   -641       C  
ATOM   2749  CZ3 TRP B  54     -32.080  18.706   0.320  1.00 61.82           C  
ANISOU 2749  CZ3 TRP B  54     8279   4447  10761   -115   1322   -863       C  
ATOM   2750  CH2 TRP B  54     -31.657  17.630   1.114  1.00 62.95           C  
ANISOU 2750  CH2 TRP B  54     8646   4567  10701   -278   1232   -736       C  
ATOM   2751  N   VAL B  55     -36.600  20.288  -3.547  1.00 70.23           N  
ANISOU 2751  N   VAL B  55     7765   5588  13330    514   1221   -862       N  
ATOM   2752  CA  VAL B  55     -37.080  21.260  -4.506  1.00 70.09           C  
ANISOU 2752  CA  VAL B  55     7476   5612  13543    772   1101   -771       C  
ATOM   2753  C   VAL B  55     -35.951  21.959  -5.235  1.00 66.67           C  
ANISOU 2753  C   VAL B  55     7288   5190  12852    918    919   -716       C  
ATOM   2754  O   VAL B  55     -35.046  22.503  -4.590  1.00 64.76           O  
ANISOU 2754  O   VAL B  55     7350   4847  12406    888   1112   -769       O  
ATOM   2755  CB  VAL B  55     -37.921  22.342  -3.854  1.00 73.42           C  
ANISOU 2755  CB  VAL B  55     7691   5905  14298    910   1503   -770       C  
ATOM   2756  CG1 VAL B  55     -38.723  23.063  -4.937  1.00 75.95           C  
ANISOU 2756  CG1 VAL B  55     7608   6272  14976   1196   1293   -601       C  
ATOM   2757  CG2 VAL B  55     -38.866  21.759  -2.811  1.00 75.49           C  
ANISOU 2757  CG2 VAL B  55     7772   6155  14754    719   1852   -856       C  
ATOM   2758  N   HIS B  56     -36.009  21.938  -6.578  1.00 65.06           N  
ANISOU 2758  N   HIS B  56     6953   5133  12631   1036    547   -611       N  
ATOM   2759  CA  HIS B  56     -35.087  22.716  -7.411  1.00 62.97           C  
ANISOU 2759  CA  HIS B  56     6878   4903  12141   1171    407   -508       C  
ATOM   2760  C   HIS B  56     -35.451  24.181  -7.146  1.00 65.52           C  
ANISOU 2760  C   HIS B  56     7135   5028  12728   1367    655   -384       C  
ATOM   2761  O   HIS B  56     -36.562  24.592  -7.431  1.00 66.47           O  
ANISOU 2761  O   HIS B  56     6919   5130  13203   1537    627   -255       O  
ATOM   2762  CB  HIS B  56     -35.245  22.371  -8.890  1.00 63.85           C  
ANISOU 2762  CB  HIS B  56     6875   5249  12137   1229    -20   -412       C  
ATOM   2763  CG  HIS B  56     -34.213  22.994  -9.775  1.00 64.02           C  
ANISOU 2763  CG  HIS B  56     7130   5348  11845   1310   -132   -303       C  
ATOM   2764  ND1 HIS B  56     -32.983  23.412  -9.307  1.00 62.92           N  
ANISOU 2764  ND1 HIS B  56     7284   5111  11510   1263     78   -351       N  
ATOM   2765  CD2 HIS B  56     -34.217  23.270 -11.103  1.00 66.54           C  
ANISOU 2765  CD2 HIS B  56     7431   5862  11989   1399   -428   -134       C  
ATOM   2766  CE1 HIS B  56     -32.280  23.931 -10.300  1.00 63.13           C  
ANISOU 2766  CE1 HIS B  56     7440   5250  11297   1317    -38   -219       C  
ATOM   2767  NE2 HIS B  56     -33.008  23.862 -11.401  1.00 66.29           N  
ANISOU 2767  NE2 HIS B  56     7683   5827  11675   1404   -336    -76       N  
ATOM   2768  N   TYR B  57     -34.547  24.913  -6.506  1.00 64.01           N  
ANISOU 2768  N   TYR B  57     7247   4668  12404   1330    909   -443       N  
ATOM   2769  CA  TYR B  57     -34.877  26.207  -5.907  1.00 66.12           C  
ANISOU 2769  CA  TYR B  57     7526   4647  12949   1461   1257   -430       C  
ATOM   2770  C   TYR B  57     -34.119  27.436  -6.470  1.00 68.23           C  
ANISOU 2770  C   TYR B  57     8003   4750  13171   1563   1258   -281       C  
ATOM   2771  O   TYR B  57     -34.552  28.547  -6.241  1.00 69.42           O  
ANISOU 2771  O   TYR B  57     8132   4604  13640   1729   1497   -227       O  
ATOM   2772  CB  TYR B  57     -34.711  26.166  -4.376  1.00 65.60           C  
ANISOU 2772  CB  TYR B  57     7655   4446  12824   1269   1661   -688       C  
ATOM   2773  CG  TYR B  57     -33.289  26.263  -3.848  1.00 63.72           C  
ANISOU 2773  CG  TYR B  57     7820   4201  12189   1049   1704   -811       C  
ATOM   2774  CD1 TYR B  57     -32.480  25.104  -3.742  1.00 60.43           C  
ANISOU 2774  CD1 TYR B  57     7527   4007  11427    859   1489   -859       C  
ATOM   2775  CD2 TYR B  57     -32.737  27.497  -3.488  1.00 64.37           C  
ANISOU 2775  CD2 TYR B  57     8138   4042  12277   1030   1936   -875       C  
ATOM   2776  CE1 TYR B  57     -31.183  25.174  -3.257  1.00 59.27           C  
ANISOU 2776  CE1 TYR B  57     7665   3895  10960    676   1483   -944       C  
ATOM   2777  CE2 TYR B  57     -31.439  27.576  -3.006  1.00 63.25           C  
ANISOU 2777  CE2 TYR B  57     8307   3939  11785    784   1931   -992       C  
ATOM   2778  CZ  TYR B  57     -30.678  26.403  -2.876  1.00 61.46           C  
ANISOU 2778  CZ  TYR B  57     8135   3990  11226    617   1691  -1013       C  
ATOM   2779  OH  TYR B  57     -29.387  26.453  -2.405  1.00 62.29           O  
ANISOU 2779  OH  TYR B  57     8469   4175  11023    394   1639  -1099       O  
ATOM   2780  N   MET B  58     -33.017  27.228  -7.190  1.00 67.14           N  
ANISOU 2780  N   MET B  58     8058   4780  12672   1462   1029   -219       N  
ATOM   2781  CA  MET B  58     -32.341  28.301  -7.874  1.00 67.59           C  
ANISOU 2781  CA  MET B  58     8287   4717  12675   1517   1016    -27       C  
ATOM   2782  C   MET B  58     -31.394  27.780  -8.936  1.00 64.53           C  
ANISOU 2782  C   MET B  58     7996   4635  11887   1426    731     61       C  
ATOM   2783  O   MET B  58     -31.031  26.605  -8.939  1.00 64.08           O  
ANISOU 2783  O   MET B  58     7927   4829  11592   1308    593    -96       O  
ATOM   2784  CB  MET B  58     -31.551  29.129  -6.866  1.00 69.67           C  
ANISOU 2784  CB  MET B  58     8837   4705  12927   1353   1358   -199       C  
ATOM   2785  CG  MET B  58     -30.349  28.420  -6.242  1.00 67.32           C  
ANISOU 2785  CG  MET B  58     8728   4597  12252   1058   1352   -422       C  
ATOM   2786  SD  MET B  58     -29.234  29.539  -5.335  1.00 69.06           S  
ANISOU 2786  SD  MET B  58     9280   4562  12397    796   1639   -589       S  
ATOM   2787  CE  MET B  58     -27.976  29.862  -6.575  1.00 67.04           C  
ANISOU 2787  CE  MET B  58     9090   4459  11923    713   1449   -370       C  
ATOM   2788  N   ILE B  59     -30.923  28.704  -9.753  1.00 64.34           N  
ANISOU 2788  N   ILE B  59     8098   4548  11800   1468    703    304       N  
ATOM   2789  CA  ILE B  59     -29.926  28.458 -10.777  1.00 62.73           C  
ANISOU 2789  CA  ILE B  59     8014   4620  11199   1365    537    399       C  
ATOM   2790  C   ILE B  59     -28.744  29.419 -10.596  1.00 63.97           C  
ANISOU 2790  C   ILE B  59     8413   4609  11283   1191    768    434       C  
ATOM   2791  O   ILE B  59     -28.951  30.643 -10.434  1.00 65.81           O  
ANISOU 2791  O   ILE B  59     8747   4477  11778   1241    940    593       O  
ATOM   2792  CB  ILE B  59     -30.528  28.708 -12.161  1.00 65.23           C  
ANISOU 2792  CB  ILE B  59     8259   5079  11444   1536    257    746       C  
ATOM   2793  CG1 ILE B  59     -31.651  27.705 -12.382  1.00 66.15           C  
ANISOU 2793  CG1 ILE B  59     8106   5406  11621   1642    -17    680       C  
ATOM   2794  CG2 ILE B  59     -29.466  28.646 -13.258  1.00 64.82           C  
ANISOU 2794  CG2 ILE B  59     8387   5309  10933   1407    173    860       C  
ATOM   2795  CD1 ILE B  59     -32.362  27.831 -13.715  1.00 70.78           C  
ANISOU 2795  CD1 ILE B  59     8586   6207  12099   1786   -385   1006       C  
ATOM   2796  N   HIS B  60     -27.520  28.872 -10.609  1.00 61.37           N  
ANISOU 2796  N   HIS B  60     8152   4518  10647    985    780    279       N  
ATOM   2797  CA  HIS B  60     -26.342  29.690 -10.764  1.00 63.11           C  
ANISOU 2797  CA  HIS B  60     8531   4685  10759    783    943    354       C  
ATOM   2798  C   HIS B  60     -26.061  29.789 -12.252  1.00 67.23           C  
ANISOU 2798  C   HIS B  60     9089   5448  11006    812    827    636       C  
ATOM   2799  O   HIS B  60     -25.580  28.842 -12.852  1.00 68.32           O  
ANISOU 2799  O   HIS B  60     9163   5957  10836    788    719    537       O  
ATOM   2800  CB  HIS B  60     -25.193  29.115  -9.975  1.00 60.65           C  
ANISOU 2800  CB  HIS B  60     8205   4530  10310    557   1014     67       C  
ATOM   2801  CG  HIS B  60     -24.052  30.053  -9.802  1.00 63.40           C  
ANISOU 2801  CG  HIS B  60     8665   4780  10643    286   1202     89       C  
ATOM   2802  ND1 HIS B  60     -24.197  31.315  -9.257  1.00 66.53           N  
ANISOU 2802  ND1 HIS B  60     9235   4756  11285    177   1400    131       N  
ATOM   2803  CD2 HIS B  60     -22.733  29.917 -10.085  1.00 65.22           C  
ANISOU 2803  CD2 HIS B  60     8835   5267  10677     78   1241     55       C  
ATOM   2804  CE1 HIS B  60     -23.020  31.924  -9.229  1.00 68.61           C  
ANISOU 2804  CE1 HIS B  60     9562   5016  11488   -127   1527    127       C  
ATOM   2805  NE2 HIS B  60     -22.113  31.103  -9.732  1.00 69.20           N  
ANISOU 2805  NE2 HIS B  60     9467   5524  11301   -192   1434     96       N  
ATOM   2806  N   GLU B  61     -26.374  30.924 -12.880  1.00 72.96           N  
ANISOU 2806  N   GLU B  61     9941   5953  11827    869    860    997       N  
ATOM   2807  CA  GLU B  61     -26.332  30.986 -14.362  1.00 78.07           C  
ANISOU 2807  CA  GLU B  61    10654   6867  12141    909    706   1330       C  
ATOM   2808  C   GLU B  61     -25.007  30.552 -14.999  1.00 74.61           C  
ANISOU 2808  C   GLU B  61    10259   6812  11276    681    805   1251       C  
ATOM   2809  O   GLU B  61     -25.043  29.897 -16.059  1.00 78.17           O  
ANISOU 2809  O   GLU B  61    10711   7646  11343    725    650   1300       O  
ATOM   2810  CB  GLU B  61     -26.733  32.347 -14.948  1.00 88.00           C  
ANISOU 2810  CB  GLU B  61    12082   7801  13551    988    727   1817       C  
ATOM   2811  CG  GLU B  61     -28.087  32.876 -14.493  1.00 95.05           C  
ANISOU 2811  CG  GLU B  61    12887   8300  14927   1287    645   1950       C  
ATOM   2812  CD  GLU B  61     -27.923  33.871 -13.339  1.00100.32           C  
ANISOU 2812  CD  GLU B  61    13668   8406  16044   1219    983   1828       C  
ATOM   2813  OE1 GLU B  61     -27.878  35.101 -13.650  1.00105.56           O  
ANISOU 2813  OE1 GLU B  61    14530   8668  16909   1231   1103   2176       O  
ATOM   2814  OE2 GLU B  61     -27.765  33.388 -12.157  1.00 98.47           O  
ANISOU 2814  OE2 GLU B  61    13360   8142  15911   1118   1125   1385       O  
ATOM   2815  N   PRO B  62     -23.854  30.903 -14.391  1.00 69.26           N  
ANISOU 2815  N   PRO B  62     9600   6057  10656    427   1064   1111       N  
ATOM   2816  CA  PRO B  62     -22.617  30.463 -15.010  1.00 68.82           C  
ANISOU 2816  CA  PRO B  62     9498   6395  10254    239   1187   1033       C  
ATOM   2817  C   PRO B  62     -22.274  28.965 -14.795  1.00 64.95           C  
ANISOU 2817  C   PRO B  62     8801   6250   9625    312   1100    633       C  
ATOM   2818  O   PRO B  62     -21.334  28.506 -15.399  1.00 66.61           O  
ANISOU 2818  O   PRO B  62     8939   6796   9572    224   1217    544       O  
ATOM   2819  CB  PRO B  62     -21.560  31.344 -14.358  1.00 69.69           C  
ANISOU 2819  CB  PRO B  62     9627   6305  10546    -70   1455   1017       C  
ATOM   2820  CG  PRO B  62     -22.128  31.778 -13.067  1.00 68.11           C  
ANISOU 2820  CG  PRO B  62     9462   5675  10742    -47   1448    880       C  
ATOM   2821  CD  PRO B  62     -23.610  31.575 -13.109  1.00 67.59           C  
ANISOU 2821  CD  PRO B  62     9417   5461  10802    285   1245    960       C  
ATOM   2822  N   GLU B  63     -23.036  28.230 -13.993  1.00 60.66           N  
ANISOU 2822  N   GLU B  63     8170   5606   9271    475    928    413       N  
ATOM   2823  CA  GLU B  63     -22.857  26.806 -13.810  1.00 58.72           C  
ANISOU 2823  CA  GLU B  63     7774   5593   8942    567    825     87       C  
ATOM   2824  C   GLU B  63     -24.199  26.109 -13.895  1.00 58.18           C  
ANISOU 2824  C   GLU B  63     7700   5489   8917    769    572     41       C  
ATOM   2825  O   GLU B  63     -24.762  25.656 -12.889  1.00 55.72           O  
ANISOU 2825  O   GLU B  63     7317   5002   8850    827    500   -111       O  
ATOM   2826  CB  GLU B  63     -22.235  26.560 -12.453  1.00 56.89           C  
ANISOU 2826  CB  GLU B  63     7425   5252   8936    474    885   -137       C  
ATOM   2827  CG  GLU B  63     -20.765  26.917 -12.421  1.00 58.66           C  
ANISOU 2827  CG  GLU B  63     7548   5626   9110    258   1080   -160       C  
ATOM   2828  CD  GLU B  63     -20.155  26.697 -11.057  1.00 57.49           C  
ANISOU 2828  CD  GLU B  63     7272   5415   9155    147   1058   -353       C  
ATOM   2829  OE1 GLU B  63     -20.903  26.727 -10.065  1.00 56.24           O  
ANISOU 2829  OE1 GLU B  63     7200   5013   9154    170    969   -410       O  
ATOM   2830  OE2 GLU B  63     -18.923  26.568 -10.951  1.00 59.37           O  
ANISOU 2830  OE2 GLU B  63     7315   5862   9380     16   1135   -431       O  
ATOM   2831  N   PRO B  64     -24.737  26.026 -15.104  1.00 61.51           N  
ANISOU 2831  N   PRO B  64     8193   6099   9078    844    429    183       N  
ATOM   2832  CA  PRO B  64     -26.121  25.617 -15.290  1.00 62.69           C  
ANISOU 2832  CA  PRO B  64     8302   6220   9294    995    147    208       C  
ATOM   2833  C   PRO B  64     -26.310  24.121 -15.145  1.00 61.95           C  
ANISOU 2833  C   PRO B  64     8117   6248   9171   1038     14   -151       C  
ATOM   2834  O   PRO B  64     -27.445  23.657 -14.971  1.00 65.26           O  
ANISOU 2834  O   PRO B  64     8449   6598   9747   1111   -197   -192       O  
ATOM   2835  CB  PRO B  64     -26.429  26.064 -16.733  1.00 66.74           C  
ANISOU 2835  CB  PRO B  64     8946   6965   9446   1008      3    504       C  
ATOM   2836  CG  PRO B  64     -25.116  26.035 -17.427  1.00 68.24           C  
ANISOU 2836  CG  PRO B  64     9245   7421   9259    863    233    456       C  
ATOM   2837  CD  PRO B  64     -24.124  26.463 -16.373  1.00 65.95           C  
ANISOU 2837  CD  PRO B  64     8885   6924   9249    756    521    377       C  
ATOM   2838  N   HIS B  65     -25.219  23.375 -15.242  1.00 60.71           N  
ANISOU 2838  N   HIS B  65     7961   6251   8853    994    148   -401       N  
ATOM   2839  CA  HIS B  65     -25.217  21.960 -14.941  1.00 58.37           C  
ANISOU 2839  CA  HIS B  65     7601   5962   8615   1048     73   -746       C  
ATOM   2840  C   HIS B  65     -25.292  21.613 -13.455  1.00 55.67           C  
ANISOU 2840  C   HIS B  65     7162   5345   8645   1058     93   -837       C  
ATOM   2841  O   HIS B  65     -25.224  20.433 -13.110  1.00 54.99           O  
ANISOU 2841  O   HIS B  65     7042   5208   8642   1102     38  -1072       O  
ATOM   2842  CB  HIS B  65     -23.953  21.345 -15.484  1.00 58.84           C  
ANISOU 2842  CB  HIS B  65     7664   6240   8450   1051    251   -968       C  
ATOM   2843  CG  HIS B  65     -22.721  21.863 -14.844  1.00 58.38           C  
ANISOU 2843  CG  HIS B  65     7501   6166   8512    994    491   -920       C  
ATOM   2844  ND1 HIS B  65     -22.053  22.971 -15.311  1.00 60.51           N  
ANISOU 2844  ND1 HIS B  65     7798   6563   8629    869    682   -702       N  
ATOM   2845  CD2 HIS B  65     -22.017  21.429 -13.772  1.00 57.50           C  
ANISOU 2845  CD2 HIS B  65     7247   5943   8657   1016    544  -1043       C  
ATOM   2846  CE1 HIS B  65     -20.980  23.193 -14.565  1.00 59.79           C  
ANISOU 2846  CE1 HIS B  65     7554   6450   8711    793    848   -731       C  
ATOM   2847  NE2 HIS B  65     -20.930  22.272 -13.623  1.00 57.78           N  
ANISOU 2847  NE2 HIS B  65     7189   6072   8693    892    745   -930       N  
ATOM   2848  N   ILE B  66     -25.348  22.592 -12.552  1.00 53.86           N  
ANISOU 2848  N   ILE B  66     6920   4924   8619   1002    191   -665       N  
ATOM   2849  CA  ILE B  66     -25.352  22.290 -11.128  1.00 52.12           C  
ANISOU 2849  CA  ILE B  66     6657   4496   8649    970    226   -755       C  
ATOM   2850  C   ILE B  66     -26.736  22.525 -10.610  1.00 53.61           C  
ANISOU 2850  C   ILE B  66     6827   4486   9056    991    166   -677       C  
ATOM   2851  O   ILE B  66     -27.161  23.649 -10.467  1.00 59.19           O  
ANISOU 2851  O   ILE B  66     7553   5063   9872    987    251   -506       O  
ATOM   2852  CB  ILE B  66     -24.344  23.129 -10.364  1.00 50.66           C  
ANISOU 2852  CB  ILE B  66     6482   4262   8505    844    400   -701       C  
ATOM   2853  CG1 ILE B  66     -22.935  22.837 -10.871  1.00 51.87           C  
ANISOU 2853  CG1 ILE B  66     6557   4653   8498    823    473   -779       C  
ATOM   2854  CG2 ILE B  66     -24.437  22.860  -8.879  1.00 49.01           C  
ANISOU 2854  CG2 ILE B  66     6278   3879   8464    777    405   -780       C  
ATOM   2855  CD1 ILE B  66     -21.794  23.307  -9.970  1.00 52.14           C  
ANISOU 2855  CD1 ILE B  66     6514   4694   8602    669    574   -782       C  
ATOM   2856  N   LEU B  67     -27.428  21.467 -10.259  1.00 54.63           N  
ANISOU 2856  N   LEU B  67     6905   4557   9294   1012     53   -807       N  
ATOM   2857  CA  LEU B  67     -28.782  21.596  -9.791  1.00 55.81           C  
ANISOU 2857  CA  LEU B  67     6967   4556   9679   1019     28   -748       C  
ATOM   2858  C   LEU B  67     -28.778  21.820  -8.292  1.00 55.69           C  
ANISOU 2858  C   LEU B  67     6992   4342   9823    933    220   -770       C  
ATOM   2859  O   LEU B  67     -28.042  21.101  -7.561  1.00 54.93           O  
ANISOU 2859  O   LEU B  67     6970   4236   9665    862    235   -872       O  
ATOM   2860  CB  LEU B  67     -29.558  20.337 -10.120  1.00 58.19           C  
ANISOU 2860  CB  LEU B  67     7188   4891  10027   1013   -165   -881       C  
ATOM   2861  CG  LEU B  67     -29.573  19.998 -11.618  1.00 60.88           C  
ANISOU 2861  CG  LEU B  67     7537   5463  10132   1051   -377   -930       C  
ATOM   2862  CD1 LEU B  67     -30.405  18.742 -11.821  1.00 60.67           C  
ANISOU 2862  CD1 LEU B  67     7444   5420  10187    983   -573  -1114       C  
ATOM   2863  CD2 LEU B  67     -30.085  21.168 -12.496  1.00 63.46           C  
ANISOU 2863  CD2 LEU B  67     7816   5913  10383   1120   -462   -677       C  
ATOM   2864  N   LEU B  68     -29.551  22.821  -7.828  1.00 55.74           N  
ANISOU 2864  N   LEU B  68     6963   4192  10022    948    370   -672       N  
ATOM   2865  CA  LEU B  68     -29.526  23.213  -6.411  1.00 54.95           C  
ANISOU 2865  CA  LEU B  68     6957   3916  10003    837    611   -735       C  
ATOM   2866  C   LEU B  68     -30.823  22.905  -5.784  1.00 54.78           C  
ANISOU 2866  C   LEU B  68     6813   3787  10212    838    706   -762       C  
ATOM   2867  O   LEU B  68     -31.917  23.242  -6.300  1.00 55.46           O  
ANISOU 2867  O   LEU B  68     6695   3842  10532    965    686   -674       O  
ATOM   2868  CB  LEU B  68     -29.130  24.665  -6.221  1.00 56.66           C  
ANISOU 2868  CB  LEU B  68     7284   3994  10248    816    806   -678       C  
ATOM   2869  CG  LEU B  68     -27.659  24.856  -6.625  1.00 57.48           C  
ANISOU 2869  CG  LEU B  68     7492   4233  10115    729    747   -670       C  
ATOM   2870  CD1 LEU B  68     -27.512  25.847  -7.770  1.00 61.47           C  
ANISOU 2870  CD1 LEU B  68     8002   4733  10621    805    745   -485       C  
ATOM   2871  CD2 LEU B  68     -26.794  25.287  -5.468  1.00 58.28           C  
ANISOU 2871  CD2 LEU B  68     7745   4269  10128    519    890   -782       C  
ATOM   2872  N   PHE B  69     -30.701  22.192  -4.670  1.00 54.35           N  
ANISOU 2872  N   PHE B  69     6859   3700  10091    688    794   -859       N  
ATOM   2873  CA  PHE B  69     -31.847  21.550  -4.063  1.00 56.51           C  
ANISOU 2873  CA  PHE B  69     7017   3910  10540    628    893   -886       C  
ATOM   2874  C   PHE B  69     -31.931  21.854  -2.613  1.00 56.90           C  
ANISOU 2874  C   PHE B  69     7227   3856  10535    472   1206   -957       C  
ATOM   2875  O   PHE B  69     -30.919  22.046  -1.931  1.00 56.11           O  
ANISOU 2875  O   PHE B  69     7369   3771  10177    352   1238  -1000       O  
ATOM   2876  CB  PHE B  69     -31.775  20.034  -4.202  1.00 58.66           C  
ANISOU 2876  CB  PHE B  69     7290   4238  10758    553    680   -907       C  
ATOM   2877  CG  PHE B  69     -32.037  19.530  -5.582  1.00 59.10           C  
ANISOU 2877  CG  PHE B  69     7187   4395  10874    656    399   -910       C  
ATOM   2878  CD1 PHE B  69     -33.323  19.491  -6.060  1.00 61.29           C  
ANISOU 2878  CD1 PHE B  69     7198   4692  11398    677    344   -884       C  
ATOM   2879  CD2 PHE B  69     -30.991  19.076  -6.375  1.00 58.77           C  
ANISOU 2879  CD2 PHE B  69     7248   4450  10629    715    196   -957       C  
ATOM   2880  CE1 PHE B  69     -33.578  19.013  -7.326  1.00 65.01           C  
ANISOU 2880  CE1 PHE B  69     7548   5294  11858    722     41   -908       C  
ATOM   2881  CE2 PHE B  69     -31.226  18.606  -7.643  1.00 61.50           C  
ANISOU 2881  CE2 PHE B  69     7503   4909  10955    776    -36  -1009       C  
ATOM   2882  CZ  PHE B  69     -32.526  18.557  -8.120  1.00 65.01           C  
ANISOU 2882  CZ  PHE B  69     7724   5387  11589    759   -140   -988       C  
ATOM   2883  N   ARG B  70     -33.167  21.869  -2.146  1.00 59.30           N  
ANISOU 2883  N   ARG B  70     7372   4085  11071    455   1437   -977       N  
ATOM   2884  CA  ARG B  70     -33.497  22.441  -0.870  1.00 60.95           C  
ANISOU 2884  CA  ARG B  70     7711   4192  11253    334   1841  -1083       C  
ATOM   2885  C   ARG B  70     -34.771  21.810  -0.449  1.00 61.08           C  
ANISOU 2885  C   ARG B  70     7511   4204  11492    264   2035  -1081       C  
ATOM   2886  O   ARG B  70     -35.667  21.608  -1.254  1.00 57.96           O  
ANISOU 2886  O   ARG B  70     6763   3833  11424    389   1927  -1016       O  
ATOM   2887  CB  ARG B  70     -33.683  23.951  -1.070  1.00 65.49           C  
ANISOU 2887  CB  ARG B  70     8248   4613  12022    502   2053  -1136       C  
ATOM   2888  CG  ARG B  70     -34.660  24.647  -0.141  1.00 71.19           C  
ANISOU 2888  CG  ARG B  70     8922   5173  12951    503   2545  -1280       C  
ATOM   2889  CD  ARG B  70     -35.688  25.488  -0.899  1.00 74.69           C  
ANISOU 2889  CD  ARG B  70     9000   5474  13904    820   2635  -1209       C  
ATOM   2890  NE  ARG B  70     -35.378  26.902  -0.755  1.00 78.72           N  
ANISOU 2890  NE  ARG B  70     9686   5718  14504    931   2874  -1302       N  
ATOM   2891  CZ  ARG B  70     -36.209  27.913  -0.989  1.00 81.72           C  
ANISOU 2891  CZ  ARG B  70     9849   5852  15348   1213   3106  -1286       C  
ATOM   2892  NH1 ARG B  70     -37.454  27.678  -1.406  1.00 83.88           N  
ANISOU 2892  NH1 ARG B  70     9645   6173  16052   1430   3104  -1163       N  
ATOM   2893  NH2 ARG B  70     -35.766  29.162  -0.840  1.00 82.43           N  
ANISOU 2893  NH2 ARG B  70    10183   5632  15504   1279   3317  -1382       N  
ATOM   2894  N   ARG B  71     -34.843  21.537   0.841  1.00 63.66           N  
ANISOU 2894  N   ARG B  71     8048   4523  11616     33   2326  -1147       N  
ATOM   2895  CA  ARG B  71     -36.043  20.947   1.426  1.00 68.76           C  
ANISOU 2895  CA  ARG B  71     8509   5172  12443    -99   2611  -1143       C  
ATOM   2896  C   ARG B  71     -36.233  21.463   2.880  1.00 72.31           C  
ANISOU 2896  C   ARG B  71     9208   5594  12672   -289   3135  -1293       C  
ATOM   2897  O   ARG B  71     -35.264  21.449   3.635  1.00 71.86           O  
ANISOU 2897  O   ARG B  71     9568   5580  12155   -468   3108  -1320       O  
ATOM   2898  CB  ARG B  71     -35.929  19.431   1.398  1.00 68.83           C  
ANISOU 2898  CB  ARG B  71     8569   5229  12352   -282   2349   -999       C  
ATOM   2899  CG  ARG B  71     -37.034  18.672   2.119  1.00 72.97           C  
ANISOU 2899  CG  ARG B  71     8965   5750  13009   -520   2651   -957       C  
ATOM   2900  CD  ARG B  71     -36.479  17.451   2.844  1.00 74.83           C  
ANISOU 2900  CD  ARG B  71     9554   5964  12911   -793   2547   -803       C  
ATOM   2901  NE  ARG B  71     -36.450  16.254   1.969  1.00 75.19           N  
ANISOU 2901  NE  ARG B  71     9491   5933  13142   -798   2145   -692       N  
ATOM   2902  CZ  ARG B  71     -35.613  15.217   2.078  1.00 74.44           C  
ANISOU 2902  CZ  ARG B  71     9689   5745  12848   -879   1863   -552       C  
ATOM   2903  NH1 ARG B  71     -34.662  15.142   3.009  1.00 74.55           N  
ANISOU 2903  NH1 ARG B  71    10104   5773  12446   -960   1854   -441       N  
ATOM   2904  NH2 ARG B  71     -35.727  14.242   1.211  1.00 75.96           N  
ANISOU 2904  NH2 ARG B  71     9764   5820  13276   -868   1565   -528       N  
ATOM   2905  N   PRO B  72     -37.474  21.871   3.270  1.00 76.74           N  
ANISOU 2905  N   PRO B  72     9500   6111  13545   -263   3607  -1397       N  
ATOM   2906  CA  PRO B  72     -37.731  22.370   4.598  1.00 81.78           C  
ANISOU 2906  CA  PRO B  72    10377   6732  13962   -443   4178  -1595       C  
ATOM   2907  C   PRO B  72     -37.467  21.391   5.694  1.00 87.79           C  
ANISOU 2907  C   PRO B  72    11501   7626  14227   -829   4265  -1515       C  
ATOM   2908  O   PRO B  72     -37.474  20.172   5.460  1.00 93.01           O  
ANISOU 2908  O   PRO B  72    12113   8344  14882   -950   3975  -1283       O  
ATOM   2909  CB  PRO B  72     -39.217  22.647   4.583  1.00 84.42           C  
ANISOU 2909  CB  PRO B  72    10215   7027  14832   -314   4619  -1669       C  
ATOM   2910  CG  PRO B  72     -39.639  22.689   3.169  1.00 82.01           C  
ANISOU 2910  CG  PRO B  72     9416   6696  15047     -2   4228  -1521       C  
ATOM   2911  CD  PRO B  72     -38.717  21.805   2.466  1.00 78.67           C  
ANISOU 2911  CD  PRO B  72     9165   6352  14372    -74   3619  -1337       C  
ATOM   2912  N   LEU B  73     -37.237  21.901   6.887  1.00 95.29           N  
ANISOU 2912  N   LEU B  73    12845   8609  14749  -1037   4656  -1701       N  
ATOM   2913  CA  LEU B  73     -37.050  21.067   8.070  1.00105.73           C  
ANISOU 2913  CA  LEU B  73    14566  10088  15516  -1435   4786  -1597       C  
ATOM   2914  C   LEU B  73     -38.360  21.010   8.837  1.00122.17           C  
ANISOU 2914  C   LEU B  73    16494  12212  17712  -1595   5471  -1700       C  
ATOM   2915  O   LEU B  73     -39.326  21.634   8.414  1.00123.03           O  
ANISOU 2915  O   LEU B  73    16148  12224  18373  -1356   5799  -1862       O  
ATOM   2916  CB  LEU B  73     -35.955  21.663   8.957  1.00105.52           C  
ANISOU 2916  CB  LEU B  73    15105  10143  14845  -1629   4771  -1748       C  
ATOM   2917  CG  LEU B  73     -34.617  22.005   8.290  1.00100.61           C  
ANISOU 2917  CG  LEU B  73    14596   9498  14132  -1488   4192  -1716       C  
ATOM   2918  CD1 LEU B  73     -33.706  22.768   9.230  1.00100.77           C  
ANISOU 2918  CD1 LEU B  73    15110   9608  13570  -1729   4245  -1936       C  
ATOM   2919  CD2 LEU B  73     -33.917  20.751   7.790  1.00 98.04           C  
ANISOU 2919  CD2 LEU B  73    14254   9243  13753  -1481   3589  -1350       C  
ATOM   2920  N   PRO B  74     -38.403  20.244   9.944  1.00 78.16           N  
ATOM   2921  CA  PRO B  74     -39.370  20.400  11.033  1.00 86.74           C  
ATOM   2922  C   PRO B  74     -39.828  21.836  11.342  1.00 89.40           C  
ATOM   2923  O   PRO B  74     -40.484  22.084  12.359  1.00 85.19           O  
ATOM   2924  CB  PRO B  74     -38.588  19.844  12.238  1.00 94.33           C  
ATOM   2925  CG  PRO B  74     -37.511  18.949  11.652  1.00 88.40           C  
ATOM   2926  CD  PRO B  74     -37.638  18.999  10.152  1.00 81.27           C  
TER    2927      PRO B  74                                                      
ATOM   2928  N   MET C   1     -46.038  -8.819 -23.439  1.00129.83           N  
ANISOU 2928  N   MET C   1    14964  17822  16540   -565   -608   -963       N  
ATOM   2929  CA  MET C   1     -46.805  -7.524 -23.347  1.00136.11           C  
ANISOU 2929  CA  MET C   1    15706  18776  17231    -46   -813   -696       C  
ATOM   2930  C   MET C   1     -48.287  -7.600 -23.714  1.00136.06           C  
ANISOU 2930  C   MET C   1    15219  19653  16823    151   -906  -1088       C  
ATOM   2931  O   MET C   1     -48.975  -6.576 -23.689  1.00139.39           O  
ANISOU 2931  O   MET C   1    15573  20278  17108    655  -1083   -893       O  
ATOM   2932  CB  MET C   1     -46.137  -6.394 -24.181  1.00143.71           C  
ANISOU 2932  CB  MET C   1    16857  19644  18100    368   -922    -58       C  
ATOM   2933  CG  MET C   1     -45.789  -5.135 -23.390  1.00148.73           C  
ANISOU 2933  CG  MET C   1    17881  19559  19067    631   -985    390       C  
ATOM   2934  SD  MET C   1     -44.153  -5.231 -22.606  1.00156.62           S  
ANISOU 2934  SD  MET C   1    19323  19617  20566    217   -832    588       S  
ATOM   2935  CE  MET C   1     -44.280  -6.643 -21.500  1.00150.01           C  
ANISOU 2935  CE  MET C   1    18412  18654  19930   -280   -699      2       C  
ATOM   2936  N   GLU C   2     -48.771  -8.775 -24.105  1.00131.81           N  
ANISOU 2936  N   GLU C   2    14336  19670  16073   -219   -778  -1655       N  
ATOM   2937  CA  GLU C   2     -50.207  -9.007 -24.262  1.00131.89           C  
ANISOU 2937  CA  GLU C   2    13833  20558  15721   -165   -819  -2182       C  
ATOM   2938  C   GLU C   2     -50.925  -8.714 -22.974  1.00125.82           C  
ANISOU 2938  C   GLU C   2    13102  19546  15156   -161   -839  -2340       C  
ATOM   2939  O   GLU C   2     -51.826  -7.896 -22.926  1.00127.39           O  
ANISOU 2939  O   GLU C   2    13079  20183  15140    302  -1026  -2325       O  
ATOM   2940  CB  GLU C   2     -50.468 -10.458 -24.665  1.00135.14           C  
ANISOU 2940  CB  GLU C   2    13943  21410  15992   -747   -588  -2851       C  
ATOM   2941  CG  GLU C   2     -50.458 -10.720 -26.162  1.00141.36           C  
ANISOU 2941  CG  GLU C   2    14367  23011  16330   -650   -622  -2961       C  
ATOM   2942  CD  GLU C   2     -49.340 -10.001 -26.902  1.00143.19           C  
ANISOU 2942  CD  GLU C   2    14877  22974  16551   -291   -743  -2268       C  
ATOM   2943  OE1 GLU C   2     -48.191 -10.013 -26.418  1.00141.28           O  
ANISOU 2943  OE1 GLU C   2    15114  21844  16720   -464   -662  -1923       O  
ATOM   2944  OE2 GLU C   2     -49.618  -9.395 -27.958  1.00149.40           O  
ANISOU 2944  OE2 GLU C   2    15397  24479  16889    179   -912  -2062       O  
ATOM   2945  N   ASP C   3     -50.456  -9.348 -21.910  1.00118.83           N  
ANISOU 2945  N   ASP C   3    12524  17945  14680   -631   -647  -2451       N  
ATOM   2946  CA  ASP C   3     -51.072  -9.226 -20.578  1.00115.14           C  
ANISOU 2946  CA  ASP C   3    12101  17230  14416   -719   -621  -2637       C  
ATOM   2947  C   ASP C   3     -50.802  -7.907 -19.823  1.00109.89           C  
ANISOU 2947  C   ASP C   3    11733  16016  14001   -257   -814  -2145       C  
ATOM   2948  O   ASP C   3     -51.437  -7.679 -18.791  1.00108.67           O  
ANISOU 2948  O   ASP C   3    11543  15793  13954   -247   -831  -2322       O  
ATOM   2949  CB  ASP C   3     -50.632 -10.402 -19.683  1.00112.99           C  
ANISOU 2949  CB  ASP C   3    12089  16381  14459  -1356   -321  -2889       C  
ATOM   2950  CG  ASP C   3     -51.148 -11.763 -20.170  1.00116.45           C  
ANISOU 2950  CG  ASP C   3    12252  17290  14700  -1895    -57  -3507       C  
ATOM   2951  OD1 ASP C   3     -52.043 -11.856 -21.043  1.00121.62           O  
ANISOU 2951  OD1 ASP C   3    12413  18840  14954  -1847   -104  -3880       O  
ATOM   2952  OD2 ASP C   3     -50.644 -12.768 -19.655  1.00114.80           O  
ANISOU 2952  OD2 ASP C   3    12334  16547  14736  -2371    219  -3641       O  
ATOM   2953  N   TYR C   4     -49.914  -7.043 -20.346  1.00106.27           N  
ANISOU 2953  N   TYR C   4    11550  15206  13623     96   -935  -1571       N  
ATOM   2954  CA  TYR C   4     -49.428  -5.841 -19.654  1.00102.14           C  
ANISOU 2954  CA  TYR C   4    11387  14010  13410    432  -1050  -1112       C  
ATOM   2955  C   TYR C   4     -49.432  -4.572 -20.503  1.00105.38           C  
ANISOU 2955  C   TYR C   4    11861  14524  13652   1063  -1236   -624       C  
ATOM   2956  O   TYR C   4     -48.910  -4.548 -21.606  1.00105.91           O  
ANISOU 2956  O   TYR C   4    11954  14751  13534   1150  -1235   -351       O  
ATOM   2957  CB  TYR C   4     -48.004  -6.074 -19.185  1.00 96.19           C  
ANISOU 2957  CB  TYR C   4    11056  12442  13046    106   -915   -858       C  
ATOM   2958  CG  TYR C   4     -47.882  -7.207 -18.243  1.00 91.93           C  
ANISOU 2958  CG  TYR C   4    10565  11671  12691   -409   -722  -1220       C  
ATOM   2959  CD1 TYR C   4     -48.121  -7.018 -16.903  1.00 90.68           C  
ANISOU 2959  CD1 TYR C   4    10506  11180  12769   -461   -708  -1328       C  
ATOM   2960  CD2 TYR C   4     -47.534  -8.468 -18.670  1.00 90.07           C  
ANISOU 2960  CD2 TYR C   4    10300  11536  12386   -826   -533  -1450       C  
ATOM   2961  CE1 TYR C   4     -48.021  -8.064 -15.997  1.00 88.29           C  
ANISOU 2961  CE1 TYR C   4    10285  10658  12600   -904   -505  -1608       C  
ATOM   2962  CE2 TYR C   4     -47.416  -9.517 -17.778  1.00 88.16           C  
ANISOU 2962  CE2 TYR C   4    10181  11000  12312  -1261   -316  -1732       C  
ATOM   2963  CZ  TYR C   4     -47.671  -9.314 -16.435  1.00 87.18           C  
ANISOU 2963  CZ  TYR C   4    10170  10559  12394  -1294   -298  -1788       C  
ATOM   2964  OH  TYR C   4     -47.585 -10.338 -15.502  1.00 85.51           O  
ANISOU 2964  OH  TYR C   4    10116  10059  12313  -1688    -61  -2015       O  
ATOM   2965  N   THR C   5     -49.956  -3.492 -19.932  1.00108.03           N  
ANISOU 2965  N   THR C   5    12273  14699  14072   1509  -1373   -488       N  
ATOM   2966  CA  THR C   5     -49.762  -2.145 -20.486  1.00111.49           C  
ANISOU 2966  CA  THR C   5    12962  14915  14482   2115  -1494     75       C  
ATOM   2967  C   THR C   5     -48.568  -1.455 -19.824  1.00109.17           C  
ANISOU 2967  C   THR C   5    13194  13593  14693   1993  -1407    462       C  
ATOM   2968  O   THR C   5     -48.464  -1.452 -18.585  1.00106.03           O  
ANISOU 2968  O   THR C   5    12900  12744  14640   1774  -1370    263       O  
ATOM   2969  CB  THR C   5     -50.958  -1.229 -20.215  1.00115.31           C  
ANISOU 2969  CB  THR C   5    13299  15705  14808   2745  -1677     22       C  
ATOM   2970  OG1 THR C   5     -51.153  -1.115 -18.795  1.00112.80           O  
ANISOU 2970  OG1 THR C   5    13050  14962  14844   2582  -1665   -242       O  
ATOM   2971  CG2 THR C   5     -52.198  -1.757 -20.869  1.00118.30           C  
ANISOU 2971  CG2 THR C   5    13100  17213  14635   2936  -1780   -389       C  
ATOM   2972  N   LYS C   6     -47.679  -0.876 -20.640  1.00110.68           N  
ANISOU 2972  N   LYS C   6    13684  13469  14899   2115  -1359    982       N  
ATOM   2973  CA  LYS C   6     -46.622   0.021 -20.138  1.00109.55           C  
ANISOU 2973  CA  LYS C   6    14026  12398  15197   2054  -1262   1357       C  
ATOM   2974  C   LYS C   6     -47.362   1.255 -19.694  1.00111.95           C  
ANISOU 2974  C   LYS C   6    14478  12462  15592   2616  -1364   1487       C  
ATOM   2975  O   LYS C   6     -48.187   1.756 -20.431  1.00115.27           O  
ANISOU 2975  O   LYS C   6    14807  13320  15669   3191  -1481   1659       O  
ATOM   2976  CB  LYS C   6     -45.542   0.373 -21.213  1.00111.76           C  
ANISOU 2976  CB  LYS C   6    14582  12454  15428   2022  -1149   1882       C  
ATOM   2977  CG  LYS C   6     -44.427  -0.685 -21.411  1.00108.07           C  
ANISOU 2977  CG  LYS C   6    14075  11970  15013   1416  -1015   1775       C  
ATOM   2978  CD  LYS C   6     -43.323  -0.346 -22.440  1.00109.57           C  
ANISOU 2978  CD  LYS C   6    14496  11995  15138   1342   -893   2254       C  
ATOM   2979  CE  LYS C   6     -42.580  -1.624 -22.877  1.00106.46           C  
ANISOU 2979  CE  LYS C   6    13906  11916  14628    868   -816   2037       C  
ATOM   2980  NZ  LYS C   6     -41.153  -1.517 -23.314  1.00106.03           N  
ANISOU 2980  NZ  LYS C   6    14068  11543  14673    565   -659   2327       N  
ATOM   2981  N   ILE C   7     -47.102   1.677 -18.462  1.00110.27           N  
ANISOU 2981  N   ILE C   7    14459  11621  15814   2471  -1325   1356       N  
ATOM   2982  CA  ILE C   7     -47.579   2.956 -17.944  1.00114.59           C  
ANISOU 2982  CA  ILE C   7    15237  11747  16554   2964  -1381   1481       C  
ATOM   2983  C   ILE C   7     -46.447   3.978 -18.095  1.00117.47           C  
ANISOU 2983  C   ILE C   7    16138  11233  17259   2923  -1205   1960       C  
ATOM   2984  O   ILE C   7     -46.651   4.998 -18.719  1.00123.31           O  
ANISOU 2984  O   ILE C   7    17164  11753  17933   3434  -1192   2385       O  
ATOM   2985  CB  ILE C   7     -48.028   2.879 -16.455  1.00111.69           C  
ANISOU 2985  CB  ILE C   7    14734  11248  16455   2831  -1432    991       C  
ATOM   2986  CG1 ILE C   7     -49.031   1.723 -16.222  1.00109.28           C  
ANISOU 2986  CG1 ILE C   7    13906  11780  15834   2697  -1535    475       C  
ATOM   2987  CG2 ILE C   7     -48.635   4.206 -15.998  1.00115.66           C  
ANISOU 2987  CG2 ILE C   7    15440  11383  17123   3413  -1504   1071       C  
ATOM   2988  CD1 ILE C   7     -49.053   1.233 -14.784  1.00105.10           C  
ANISOU 2988  CD1 ILE C   7    13263  11106  15563   2298  -1500     25       C  
ATOM   2989  N   GLU C   8     -45.286   3.725 -17.481  1.00115.57           N  
ANISOU 2989  N   GLU C   8    16035  10504  17372   2330  -1053   1872       N  
ATOM   2990  CA  GLU C   8     -44.135   4.646 -17.571  1.00119.17           C  
ANISOU 2990  CA  GLU C   8    16954  10162  18161   2164   -843   2235       C  
ATOM   2991  C   GLU C   8     -42.748   4.078 -17.241  1.00117.95           C  
ANISOU 2991  C   GLU C   8    16822   9765  18228   1474   -683   2125       C  
ATOM   2992  O   GLU C   8     -42.621   3.145 -16.431  1.00113.83           O  
ANISOU 2992  O   GLU C   8    16033   9458  17755   1134   -728   1705       O  
ATOM   2993  CB  GLU C   8     -44.351   5.845 -16.655  1.00122.51           C  
ANISOU 2993  CB  GLU C   8    17659   9913  18974   2400   -806   2185       C  
ATOM   2994  CG  GLU C   8     -44.300   5.530 -15.161  1.00118.91           C  
ANISOU 2994  CG  GLU C   8    17013   9348  18817   2075   -840   1635       C  
ATOM   2995  CD  GLU C   8     -44.921   6.617 -14.298  1.00122.46           C  
ANISOU 2995  CD  GLU C   8    17621   9358  19550   2446   -871   1487       C  
ATOM   2996  OE1 GLU C   8     -45.423   7.623 -14.827  1.00126.21           O  
ANISOU 2996  OE1 GLU C   8    18383   9560  20007   2993   -863   1811       O  
ATOM   2997  OE2 GLU C   8     -44.864   6.460 -13.064  1.00122.04           O  
ANISOU 2997  OE2 GLU C   8    17412   9226  19731   2201   -892   1042       O  
ATOM   2998  N   LYS C   9     -41.718   4.648 -17.890  1.00123.01           N  
ANISOU 2998  N   LYS C   9    17785   9985  18968   1295   -483   2513       N  
ATOM   2999  CA  LYS C   9     -40.272   4.450 -17.548  1.00123.15           C  
ANISOU 2999  CA  LYS C   9    17869   9687  19233    673   -296   2423       C  
ATOM   3000  C   LYS C   9     -39.955   4.828 -16.106  1.00124.04           C  
ANISOU 3000  C   LYS C   9    18012   9346  19770    442   -248   2034       C  
ATOM   3001  O   LYS C   9     -40.473   5.827 -15.606  1.00130.57           O  
ANISOU 3001  O   LYS C   9    19041   9737  20832    717   -237   2024       O  
ATOM   3002  CB  LYS C   9     -39.324   5.250 -18.500  1.00128.16           C  
ANISOU 3002  CB  LYS C   9    18875   9912  19907    536    -48   2917       C  
ATOM   3003  CG  LYS C   9     -37.927   4.641 -18.712  1.00126.39           C  
ANISOU 3003  CG  LYS C   9    18561   9778  19682    -60     99   2862       C  
ATOM   3004  CD  LYS C   9     -36.819   5.639 -19.071  1.00131.24           C  
ANISOU 3004  CD  LYS C   9    19547   9807  20509   -380    413   3163       C  
ATOM   3005  CE  LYS C   9     -36.031   6.071 -17.836  1.00132.43           C  
ANISOU 3005  CE  LYS C   9    19738   9476  21104   -810    555   2767       C  
ATOM   3006  NZ  LYS C   9     -34.880   6.985 -18.108  1.00137.92           N  
ANISOU 3006  NZ  LYS C   9    20746   9634  22022  -1249    906   2947       N  
ATOM   3007  N   ILE C  10     -39.091   4.059 -15.451  1.00122.42           N  
ANISOU 3007  N   ILE C  10    17607   9261  19645    -23   -214   1710       N  
ATOM   3008  CA  ILE C  10     -38.667   4.353 -14.065  1.00124.83           C  
ANISOU 3008  CA  ILE C  10    17881   9250  20298   -263   -165   1307       C  
ATOM   3009  C   ILE C  10     -37.218   3.958 -13.766  1.00125.74           C  
ANISOU 3009  C   ILE C  10    17908   9368  20496   -794    -21   1136       C  
ATOM   3010  O   ILE C  10     -36.928   3.476 -12.667  1.00127.84           O  
ANISOU 3010  O   ILE C  10    17958   9774  20840   -969    -62    736       O  
ATOM   3011  CB  ILE C  10     -39.624   3.704 -13.000  1.00123.29           C  
ANISOU 3011  CB  ILE C  10    17393   9394  20056    -96   -368    898       C  
ATOM   3012  CG1 ILE C  10     -39.975   2.250 -13.349  1.00118.51           C  
ANISOU 3012  CG1 ILE C  10    16503   9438  19086   -117   -489    832       C  
ATOM   3013  CG2 ILE C  10     -40.893   4.533 -12.824  1.00127.83           C  
ANISOU 3013  CG2 ILE C  10    18056   9818  20692    395   -474    914       C  
ATOM   3014  CD1 ILE C  10     -40.674   1.512 -12.228  1.00116.19           C  
ANISOU 3014  CD1 ILE C  10    15951   9442  18754    -96   -608    426       C  
ATOM   3015  N   GLY C  11     -36.317   4.100 -14.733  1.00129.20           N  
ANISOU 3015  N   GLY C  11    18481   9740  20868  -1026    141   1428       N  
ATOM   3016  CA  GLY C  11     -34.884   3.956 -14.451  1.00130.79           C  
ANISOU 3016  CA  GLY C  11    18596   9938  21159  -1526    304   1238       C  
ATOM   3017  C   GLY C  11     -34.150   2.933 -15.278  1.00129.86           C  
ANISOU 3017  C   GLY C  11    18311  10302  20728  -1709    308   1341       C  
ATOM   3018  O   GLY C  11     -34.706   2.433 -16.257  1.00128.53           O  
ANISOU 3018  O   GLY C  11    18135  10421  20280  -1485    217   1613       O  
ATOM   3019  N   GLU C  12     -32.906   2.643 -14.863  1.00132.81           N  
ANISOU 3019  N   GLU C  12    18521  10807  21132  -2096    412   1080       N  
ATOM   3020  CA  GLU C  12     -32.037   1.605 -15.479  1.00137.58           C  
ANISOU 3020  CA  GLU C  12    18923  11906  21443  -2270    416   1082       C  
ATOM   3021  C   GLU C  12     -31.206   0.750 -14.455  1.00142.02           C  
ANISOU 3021  C   GLU C  12    19183  12817  21959  -2422    375    631       C  
ATOM   3022  O   GLU C  12     -29.970   0.862 -14.355  1.00145.10           O  
ANISOU 3022  O   GLU C  12    19450  13329  22351  -2747    512    461       O  
ATOM   3023  CB  GLU C  12     -31.126   2.244 -16.529  1.00140.23           C  
ANISOU 3023  CB  GLU C  12    19401  12128  21749  -2574    645   1365       C  
ATOM   3024  CG  GLU C  12     -31.880   2.960 -17.649  1.00143.05           C  
ANISOU 3024  CG  GLU C  12    20074  12221  22057  -2354    695   1886       C  
ATOM   3025  CD  GLU C  12     -31.224   2.812 -19.003  1.00144.05           C  
ANISOU 3025  CD  GLU C  12    20223  12600  21908  -2515    820   2223       C  
ATOM   3026  OE1 GLU C  12     -30.937   3.857 -19.633  1.00144.47           O  
ANISOU 3026  OE1 GLU C  12    20576  12273  22042  -2664   1056   2568       O  
ATOM   3027  OE2 GLU C  12     -31.010   1.640 -19.418  1.00138.10           O  
ANISOU 3027  OE2 GLU C  12    19203  12412  20856  -2489    699   2136       O  
ATOM   3028  N   GLY C  13     -31.900  -0.124 -13.715  1.00143.09           N  
ANISOU 3028  N   GLY C  13    19194  13155  22017  -2166    199    444       N  
ATOM   3029  CA  GLY C  13     -31.315  -0.901 -12.617  1.00142.86           C  
ANISOU 3029  CA  GLY C  13    18934  13422  21923  -2188    154     70       C  
ATOM   3030  C   GLY C  13     -30.339  -1.960 -13.104  1.00146.56           C  
ANISOU 3030  C   GLY C  13    19249  14328  22109  -2252    173     41       C  
ATOM   3031  O   GLY C  13     -30.716  -3.145 -13.211  1.00147.30           O  
ANISOU 3031  O   GLY C  13    19312  14660  21996  -2044     81     51       O  
ATOM   3032  N   THR C  14     -29.097  -1.516 -13.393  1.00147.15           N  
ANISOU 3032  N   THR C  14    19230  14499  22178  -2554    315    -23       N  
ATOM   3033  CA  THR C  14     -27.884  -2.342 -13.800  1.00142.76           C  
ANISOU 3033  CA  THR C  14    18467  14427  21346  -2643    354   -127       C  
ATOM   3034  C   THR C  14     -28.075  -3.369 -14.938  1.00130.93           C  
ANISOU 3034  C   THR C  14    17002  13163  19583  -2491    299     98       C  
ATOM   3035  O   THR C  14     -27.189  -3.529 -15.777  1.00129.07           O  
ANISOU 3035  O   THR C  14    16668  13198  19175  -2648    378    141       O  
ATOM   3036  CB  THR C  14     -27.131  -3.062 -12.612  1.00142.78           C  
ANISOU 3036  CB  THR C  14    18213  14819  21215  -2527    303   -522       C  
ATOM   3037  OG1 THR C  14     -28.012  -3.967 -11.939  1.00138.37           O  
ANISOU 3037  OG1 THR C  14    17721  14258  20596  -2171    167   -535       O  
ATOM   3038  CG2 THR C  14     -26.504  -2.069 -11.580  1.00144.07           C  
ANISOU 3038  CG2 THR C  14    18212  14964  21563  -2765    390   -867       C  
ATOM   3039  N   TYR C  15     -29.202  -4.072 -14.916  1.00118.86           N  
ANISOU 3039  N   TYR C  15    15578  11570  18013  -2212    180    184       N  
ATOM   3040  CA  TYR C  15     -29.591  -4.992 -15.959  1.00113.31           C  
ANISOU 3040  CA  TYR C  15    14905  11056  17091  -2089    141    340       C  
ATOM   3041  C   TYR C  15     -30.336  -4.291 -17.072  1.00112.26           C  
ANISOU 3041  C   TYR C  15    14901  10776  16973  -2120    150    673       C  
ATOM   3042  O   TYR C  15     -29.719  -3.922 -18.078  1.00116.57           O  
ANISOU 3042  O   TYR C  15    15435  11436  17418  -2288    239    856       O  
ATOM   3043  CB  TYR C  15     -30.393  -6.148 -15.349  1.00110.07           C  
ANISOU 3043  CB  TYR C  15    14530  10676  16614  -1829     56    206       C  
ATOM   3044  CG  TYR C  15     -29.556  -6.855 -14.291  1.00107.80           C  
ANISOU 3044  CG  TYR C  15    14149  10556  16253  -1725     66    -57       C  
ATOM   3045  CD1 TYR C  15     -28.298  -7.415 -14.622  1.00106.50           C  
ANISOU 3045  CD1 TYR C  15    13848  10732  15885  -1729    113   -159       C  
ATOM   3046  CD2 TYR C  15     -29.963  -6.899 -12.958  1.00105.89           C  
ANISOU 3046  CD2 TYR C  15    13930  10195  16108  -1592     29   -207       C  
ATOM   3047  CE1 TYR C  15     -27.501  -8.017 -13.663  1.00104.48           C  
ANISOU 3047  CE1 TYR C  15    13492  10695  15510  -1549    114   -389       C  
ATOM   3048  CE2 TYR C  15     -29.166  -7.504 -11.984  1.00104.18           C  
ANISOU 3048  CE2 TYR C  15    13622  10194  15767  -1434     39   -416       C  
ATOM   3049  CZ  TYR C  15     -27.940  -8.059 -12.345  1.00103.88           C  
ANISOU 3049  CZ  TYR C  15    13459  10497  15513  -1389     77   -500       C  
ATOM   3050  OH  TYR C  15     -27.143  -8.655 -11.391  1.00104.73           O  
ANISOU 3050  OH  TYR C  15    13463  10883  15444  -1146     77   -697       O  
ATOM   3051  N   GLY C  16     -31.625  -4.043 -16.898  1.00107.61           N  
ANISOU 3051  N   GLY C  16    14426   9977  16481  -1945     68    760       N  
ATOM   3052  CA  GLY C  16     -32.421  -3.522 -17.990  1.00106.86           C  
ANISOU 3052  CA  GLY C  16    14430   9852  16318  -1860     52   1078       C  
ATOM   3053  C   GLY C  16     -32.732  -2.042 -17.925  1.00107.85           C  
ANISOU 3053  C   GLY C  16    14747   9563  16668  -1863    102   1302       C  
ATOM   3054  O   GLY C  16     -32.035  -1.242 -17.279  1.00112.31           O  
ANISOU 3054  O   GLY C  16    15370   9842  17461  -2060    205   1226       O  
ATOM   3055  N   VAL C  17     -33.737  -1.691 -18.723  1.00106.37           N  
ANISOU 3055  N   VAL C  17    14654   9381  16382  -1636     48   1578       N  
ATOM   3056  CA  VAL C  17     -34.542  -0.478 -18.593  1.00105.39           C  
ANISOU 3056  CA  VAL C  17    14741   8865  16436  -1443     44   1786       C  
ATOM   3057  C   VAL C  17     -35.749  -0.891 -17.756  1.00101.45           C  
ANISOU 3057  C   VAL C  17    14150   8420  15976  -1189   -122   1540       C  
ATOM   3058  O   VAL C  17     -36.406  -1.858 -18.091  1.00101.53           O  
ANISOU 3058  O   VAL C  17    13999   8823  15753  -1069   -220   1444       O  
ATOM   3059  CB  VAL C  17     -35.094  -0.031 -19.957  1.00107.88           C  
ANISOU 3059  CB  VAL C  17    15167   9303  16518  -1216     48   2222       C  
ATOM   3060  CG1 VAL C  17     -35.750   1.330 -19.832  1.00112.18           C  
ANISOU 3060  CG1 VAL C  17    16001   9365  17255   -970     82   2485       C  
ATOM   3061  CG2 VAL C  17     -34.007  -0.010 -21.030  1.00109.46           C  
ANISOU 3061  CG2 VAL C  17    15385   9662  16542  -1464    202   2467       C  
ATOM   3062  N   VAL C  18     -36.068  -0.192 -16.682  1.00 98.59           N  
ANISOU 3062  N   VAL C  18    13871   7695  15893  -1132   -136   1401       N  
ATOM   3063  CA  VAL C  18     -37.178  -0.622 -15.815  1.00 93.49           C  
ANISOU 3063  CA  VAL C  18    13104   7155  15260   -927   -282   1134       C  
ATOM   3064  C   VAL C  18     -38.418   0.193 -16.114  1.00 94.96           C  
ANISOU 3064  C   VAL C  18    13383   7258  15438   -551   -370   1308       C  
ATOM   3065  O   VAL C  18     -38.344   1.402 -16.135  1.00 99.61           O  
ANISOU 3065  O   VAL C  18    14202   7419  16224   -459   -302   1506       O  
ATOM   3066  CB  VAL C  18     -36.808  -0.474 -14.332  1.00 91.79           C  
ANISOU 3066  CB  VAL C  18    12858   6709  15308  -1061   -264    807       C  
ATOM   3067  CG1 VAL C  18     -37.895  -1.018 -13.425  1.00 89.55           C  
ANISOU 3067  CG1 VAL C  18    12437   6588  14997   -889   -389    536       C  
ATOM   3068  CG2 VAL C  18     -35.506  -1.202 -14.036  1.00 90.30           C  
ANISOU 3068  CG2 VAL C  18    12566   6659  15083  -1356   -181    645       C  
ATOM   3069  N   TYR C  19     -39.555  -0.470 -16.273  1.00 92.81           N  
ANISOU 3069  N   TYR C  19    12930   7393  14940   -333   -503   1196       N  
ATOM   3070  CA  TYR C  19     -40.826   0.172 -16.585  1.00 95.45           C  
ANISOU 3070  CA  TYR C  19    13269   7817  15177     93   -617   1308       C  
ATOM   3071  C   TYR C  19     -41.888  -0.128 -15.533  1.00 92.48           C  
ANISOU 3071  C   TYR C  19    12708   7596  14832    215   -734    932       C  
ATOM   3072  O   TYR C  19     -41.807  -1.108 -14.810  1.00 87.18           O  
ANISOU 3072  O   TYR C  19    11884   7079  14158    -29   -722    621       O  
ATOM   3073  CB  TYR C  19     -41.342  -0.312 -17.935  1.00 98.21           C  
ANISOU 3073  CB  TYR C  19    13482   8705  15126    268   -673   1483       C  
ATOM   3074  CG  TYR C  19     -40.742   0.425 -19.095  1.00103.63           C  
ANISOU 3074  CG  TYR C  19    14385   9262  15726    352   -583   1963       C  
ATOM   3075  CD1 TYR C  19     -41.201   1.711 -19.436  1.00108.87           C  
ANISOU 3075  CD1 TYR C  19    15299   9645  16421    760   -583   2322       C  
ATOM   3076  CD2 TYR C  19     -39.722  -0.147 -19.875  1.00104.12           C  
ANISOU 3076  CD2 TYR C  19    14424   9481  15654     52   -481   2080       C  
ATOM   3077  CE1 TYR C  19     -40.654   2.439 -20.497  1.00113.57           C  
ANISOU 3077  CE1 TYR C  19    16158  10070  16924    843   -456   2827       C  
ATOM   3078  CE2 TYR C  19     -39.162   0.568 -20.946  1.00108.57           C  
ANISOU 3078  CE2 TYR C  19    15191   9946  16112    104   -372   2546       C  
ATOM   3079  CZ  TYR C  19     -39.632   1.868 -21.255  1.00113.67           C  
ANISOU 3079  CZ  TYR C  19    16124  10271  16793    489   -346   2942       C  
ATOM   3080  OH  TYR C  19     -39.091   2.616 -22.300  1.00118.52           O  
ANISOU 3080  OH  TYR C  19    17004  10734  17293    545   -193   3462       O  
ATOM   3081  N   LYS C  20     -42.869   0.769 -15.424  1.00 94.29           N  
ANISOU 3081  N   LYS C  20    12974   7765  15085    618   -830    977       N  
ATOM   3082  CA  LYS C  20     -44.067   0.514 -14.633  1.00 92.28           C  
ANISOU 3082  CA  LYS C  20    12486   7804  14772    787   -955    621       C  
ATOM   3083  C   LYS C  20     -45.134  -0.008 -15.575  1.00 91.84           C  
ANISOU 3083  C   LYS C  20    12174   8418  14300   1027  -1059    602       C  
ATOM   3084  O   LYS C  20     -45.222   0.442 -16.708  1.00 93.63           O  
ANISOU 3084  O   LYS C  20    12471   8770  14334   1306  -1084    935       O  
ATOM   3085  CB  LYS C  20     -44.554   1.789 -13.945  1.00 95.79           C  
ANISOU 3085  CB  LYS C  20    13072   7864  15459   1129  -1010    612       C  
ATOM   3086  CG  LYS C  20     -45.399   1.529 -12.697  1.00 94.88           C  
ANISOU 3086  CG  LYS C  20    12722   7940  15388   1151  -1098    162       C  
ATOM   3087  CD  LYS C  20     -45.918   2.820 -12.060  1.00 98.64           C  
ANISOU 3087  CD  LYS C  20    13321   8059  16096   1537  -1161    115       C  
ATOM   3088  CE  LYS C  20     -46.916   2.500 -10.951  1.00 97.71           C  
ANISOU 3088  CE  LYS C  20    12898   8294  15931   1594  -1267   -347       C  
ATOM   3089  NZ  LYS C  20     -47.547   3.714 -10.366  1.00101.30           N  
ANISOU 3089  NZ  LYS C  20    13428   8485  16576   2031  -1349   -447       N  
ATOM   3090  N   GLY C  21     -45.913  -0.977 -15.108  1.00 88.77           N  
ANISOU 3090  N   GLY C  21    11483   8491  13754    894  -1096    200       N  
ATOM   3091  CA  GLY C  21     -46.970  -1.550 -15.921  1.00 89.61           C  
ANISOU 3091  CA  GLY C  21    11271   9324  13453   1045  -1173     56       C  
ATOM   3092  C   GLY C  21     -48.131  -2.106 -15.136  1.00 88.72           C  
ANISOU 3092  C   GLY C  21    10838   9647  13224    999  -1216   -425       C  
ATOM   3093  O   GLY C  21     -48.087  -2.179 -13.909  1.00 86.27           O  
ANISOU 3093  O   GLY C  21    10563   9074  13141    821  -1178   -636       O  
ATOM   3094  N   ARG C  22     -49.179  -2.484 -15.860  1.00 90.81           N  
ANISOU 3094  N   ARG C  22    10763  10641  13100   1154  -1286   -618       N  
ATOM   3095  CA  ARG C  22     -50.354  -3.100 -15.263  1.00 91.18           C  
ANISOU 3095  CA  ARG C  22    10443  11231  12970   1044  -1294  -1131       C  
ATOM   3096  C   ARG C  22     -50.803  -4.387 -16.004  1.00 90.98           C  
ANISOU 3096  C   ARG C  22    10094  11872  12602    702  -1191  -1459       C  
ATOM   3097  O   ARG C  22     -50.876  -4.410 -17.224  1.00 92.52           O  
ANISOU 3097  O   ARG C  22    10160  12477  12514    873  -1239  -1344       O  
ATOM   3098  CB  ARG C  22     -51.493  -2.068 -15.215  1.00 95.95           C  
ANISOU 3098  CB  ARG C  22    10857  12185  13415   1651  -1495  -1189       C  
ATOM   3099  CG  ARG C  22     -52.647  -2.413 -14.274  1.00 97.02           C  
ANISOU 3099  CG  ARG C  22    10635  12785  13441   1565  -1513  -1727       C  
ATOM   3100  CD  ARG C  22     -53.184  -1.194 -13.539  1.00 99.95           C  
ANISOU 3100  CD  ARG C  22    11035  13004  13937   2086  -1677  -1723       C  
ATOM   3101  NE  ARG C  22     -53.398  -0.041 -14.421  1.00105.13           N  
ANISOU 3101  NE  ARG C  22    11784  13696  14464   2805  -1849  -1362       N  
ATOM   3102  CZ  ARG C  22     -53.698   1.203 -14.007  1.00109.20           C  
ANISOU 3102  CZ  ARG C  22    12450  13917  15123   3377  -1980  -1238       C  
ATOM   3103  NH1 ARG C  22     -53.820   1.488 -12.706  1.00108.03           N  
ANISOU 3103  NH1 ARG C  22    12325  13463  15256   3297  -1980  -1489       N  
ATOM   3104  NH2 ARG C  22     -53.894   2.183 -14.910  1.00114.33           N  
ANISOU 3104  NH2 ARG C  22    13240  14581  15617   4068  -2101   -855       N  
ATOM   3105  N   HIS C  23     -51.148  -5.405 -15.222  1.00 89.42           N  
ANISOU 3105  N   HIS C  23     9768  11784  12424    227  -1032  -1882       N  
ATOM   3106  CA  HIS C  23     -51.751  -6.665 -15.685  1.00 90.79           C  
ANISOU 3106  CA  HIS C  23     9630  12552  12313   -186   -872  -2324       C  
ATOM   3107  C   HIS C  23     -53.208  -6.445 -16.086  1.00 95.62           C  
ANISOU 3107  C   HIS C  23     9728  14086  12517     81   -998  -2699       C  
ATOM   3108  O   HIS C  23     -54.031  -6.026 -15.279  1.00 96.26           O  
ANISOU 3108  O   HIS C  23     9638  14357  12577    234  -1073  -2919       O  
ATOM   3109  CB  HIS C  23     -51.692  -7.704 -14.557  1.00 88.73           C  
ANISOU 3109  CB  HIS C  23     9472  12012  12229   -759   -619  -2620       C  
ATOM   3110  CG  HIS C  23     -51.772  -9.134 -15.004  1.00 89.94           C  
ANISOU 3110  CG  HIS C  23     9537  12393  12243  -1310   -351  -2959       C  
ATOM   3111  ND1 HIS C  23     -52.413  -9.543 -16.156  1.00 93.70           N  
ANISOU 3111  ND1 HIS C  23     9643  13587  12368  -1359   -340  -3251       N  
ATOM   3112  CD2 HIS C  23     -51.334 -10.269 -14.405  1.00 88.31           C  
ANISOU 3112  CD2 HIS C  23     9572  11786  12195  -1832    -56  -3085       C  
ATOM   3113  CE1 HIS C  23     -52.347 -10.857 -16.259  1.00 93.63           C  
ANISOU 3113  CE1 HIS C  23     9658  13569  12348  -1934    -39  -3574       C  
ATOM   3114  NE2 HIS C  23     -51.705 -11.321 -15.203  1.00 90.45           N  
ANISOU 3114  NE2 HIS C  23     9654  12455  12255  -2212    145  -3455       N  
ATOM   3115  N   LYS C  24     -53.527  -6.722 -17.344  1.00 99.68           N  
ANISOU 3115  N   LYS C  24     9954  15248  12669    160  -1028  -2800       N  
ATOM   3116  CA  LYS C  24     -54.872  -6.419 -17.913  1.00106.24           C  
ANISOU 3116  CA  LYS C  24    10233  17110  13021    530  -1185  -3143       C  
ATOM   3117  C   LYS C  24     -56.014  -7.299 -17.400  1.00108.13           C  
ANISOU 3117  C   LYS C  24    10023  18002  13057     73  -1027  -3873       C  
ATOM   3118  O   LYS C  24     -57.172  -6.920 -17.493  1.00111.49           O  
ANISOU 3118  O   LYS C  24     9980  19252  13129    393  -1169  -4205       O  
ATOM   3119  CB  LYS C  24     -54.852  -6.510 -19.456  1.00110.28           C  
ANISOU 3119  CB  LYS C  24    10517  18239  13143    745  -1255  -3069       C  
ATOM   3120  CG  LYS C  24     -53.866  -5.565 -20.121  1.00110.44           C  
ANISOU 3120  CG  LYS C  24    10931  17762  13267   1233  -1398  -2342       C  
ATOM   3121  CD  LYS C  24     -54.015  -5.575 -21.624  1.00115.18           C  
ANISOU 3121  CD  LYS C  24    11247  19123  13393   1528  -1484  -2273       C  
ATOM   3122  CE  LYS C  24     -52.974  -4.672 -22.270  1.00116.16           C  
ANISOU 3122  CE  LYS C  24    11810  18701  13622   1944  -1572  -1514       C  
ATOM   3123  NZ  LYS C  24     -52.617  -5.101 -23.657  1.00118.44           N  
ANISOU 3123  NZ  LYS C  24    11938  19497  13564   1930  -1548  -1427       N  
ATOM   3124  N   THR C  25     -55.659  -8.491 -16.921  1.00106.21           N  
ANISOU 3124  N   THR C  25     9933  17405  13014   -668   -714  -4117       N  
ATOM   3125  CA  THR C  25     -56.581  -9.399 -16.237  1.00108.18           C  
ANISOU 3125  CA  THR C  25     9895  18044  13164  -1242   -468  -4761       C  
ATOM   3126  C   THR C  25     -56.771  -8.938 -14.785  1.00106.45           C  
ANISOU 3126  C   THR C  25     9831  17426  13186  -1201   -487  -4716       C  
ATOM   3127  O   THR C  25     -57.845  -8.467 -14.426  1.00110.17           O  
ANISOU 3127  O   THR C  25     9910  18515  13433   -976   -608  -5034       O  
ATOM   3128  CB  THR C  25     -56.080 -10.886 -16.278  1.00107.16           C  
ANISOU 3128  CB  THR C  25     9969  17570  13176  -2045    -67  -4992       C  
ATOM   3129  OG1 THR C  25     -55.933 -11.337 -17.632  1.00109.28           O  
ANISOU 3129  OG1 THR C  25    10047  18262  13210  -2101    -43  -5109       O  
ATOM   3130  CG2 THR C  25     -57.048 -11.829 -15.563  1.00109.62           C  
ANISOU 3130  CG2 THR C  25    10039  18219  13392  -2699    256  -5646       C  
ATOM   3131  N   THR C  26     -55.712  -9.029 -13.979  1.00102.03           N  
ANISOU 3131  N   THR C  26     9813  15903  13051  -1366   -387  -4332       N  
ATOM   3132  CA  THR C  26     -55.799  -8.815 -12.518  1.00100.56           C  
ANISOU 3132  CA  THR C  26     9783  15336  13088  -1442   -344  -4335       C  
ATOM   3133  C   THR C  26     -55.682  -7.352 -12.054  1.00100.51           C  
ANISOU 3133  C   THR C  26     9864  15094  13231   -767   -668  -3994       C  
ATOM   3134  O   THR C  26     -55.741  -7.106 -10.859  1.00 99.88           O  
ANISOU 3134  O   THR C  26     9877  14746  13324   -796   -652  -4021       O  
ATOM   3135  CB  THR C  26     -54.706  -9.606 -11.748  1.00 96.52           C  
ANISOU 3135  CB  THR C  26     9796  13949  12926  -1894    -77  -4100       C  
ATOM   3136  OG1 THR C  26     -53.419  -8.974 -11.887  1.00 92.89           O  
ANISOU 3136  OG1 THR C  26     9741  12801  12749  -1560   -231  -3529       O  
ATOM   3137  CG2 THR C  26     -54.606 -11.041 -12.239  1.00 97.51           C  
ANISOU 3137  CG2 THR C  26     9978  14089  12981  -2519    274  -4354       C  
ATOM   3138  N   GLY C  27     -55.429  -6.399 -12.962  1.00101.79           N  
ANISOU 3138  N   GLY C  27    10049  15278  13346   -179   -928  -3649       N  
ATOM   3139  CA  GLY C  27     -55.200  -4.990 -12.584  1.00102.22           C  
ANISOU 3139  CA  GLY C  27    10290  14949  13599    446  -1183  -3290       C  
ATOM   3140  C   GLY C  27     -53.972  -4.681 -11.730  1.00 98.87           C  
ANISOU 3140  C   GLY C  27    10371  13553  13640    361  -1137  -2909       C  
ATOM   3141  O   GLY C  27     -53.706  -3.520 -11.420  1.00 98.71           O  
ANISOU 3141  O   GLY C  27    10531  13150  13824    812  -1307  -2647       O  
ATOM   3142  N   GLN C  28     -53.234  -5.730 -11.361  1.00 97.00           N  
ANISOU 3142  N   GLN C  28    10357  12943  13554   -205   -892  -2905       N  
ATOM   3143  CA  GLN C  28     -51.985  -5.650 -10.600  1.00 94.72           C  
ANISOU 3143  CA  GLN C  28    10499  11850  13638   -329   -824  -2588       C  
ATOM   3144  C   GLN C  28     -50.996  -4.668 -11.235  1.00 93.31           C  
ANISOU 3144  C   GLN C  28    10603  11195  13656     42   -975  -2105       C  
ATOM   3145  O   GLN C  28     -50.793  -4.661 -12.459  1.00 94.89           O  
ANISOU 3145  O   GLN C  28    10802  11531  13719    157  -1014  -1916       O  
ATOM   3146  CB  GLN C  28     -51.368  -7.060 -10.520  1.00 95.33           C  
ANISOU 3146  CB  GLN C  28    10757  11721  13740   -906   -535  -2631       C  
ATOM   3147  CG  GLN C  28     -49.857  -7.172 -10.261  1.00 94.71           C  
ANISOU 3147  CG  GLN C  28    11104  10929  13949   -993   -465  -2257       C  
ATOM   3148  CD  GLN C  28     -49.491  -7.539  -8.851  1.00 95.08           C  
ANISOU 3148  CD  GLN C  28    11328  10644  14152  -1204   -326  -2295       C  
ATOM   3149  OE1 GLN C  28     -48.692  -8.438  -8.635  1.00 94.81           O  
ANISOU 3149  OE1 GLN C  28    11545  10301  14176  -1476   -131  -2197       O  
ATOM   3150  NE2 GLN C  28     -50.123  -6.888  -7.876  1.00 98.31           N  
ANISOU 3150  NE2 GLN C  28    11591  11169  14591  -1050   -419  -2455       N  
ATOM   3151  N   VAL C  29     -50.377  -3.867 -10.387  1.00 91.25           N  
ANISOU 3151  N   VAL C  29    10570  10396  13701    188  -1031  -1932       N  
ATOM   3152  CA  VAL C  29     -49.381  -2.902 -10.800  1.00 91.18           C  
ANISOU 3152  CA  VAL C  29    10862   9854  13927    445  -1113  -1515       C  
ATOM   3153  C   VAL C  29     -48.042  -3.625 -10.720  1.00 88.67           C  
ANISOU 3153  C   VAL C  29    10805   9118  13767     52   -949  -1341       C  
ATOM   3154  O   VAL C  29     -47.789  -4.348  -9.739  1.00 88.91           O  
ANISOU 3154  O   VAL C  29    10870   9048  13863   -255   -820  -1504       O  
ATOM   3155  CB  VAL C  29     -49.354  -1.682  -9.854  1.00 91.83           C  
ANISOU 3155  CB  VAL C  29    11047   9561  14284    743  -1220  -1504       C  
ATOM   3156  CG1 VAL C  29     -48.413  -0.618 -10.385  1.00 92.09           C  
ANISOU 3156  CG1 VAL C  29    11406   9025  14559    975  -1257  -1096       C  
ATOM   3157  CG2 VAL C  29     -50.758  -1.119  -9.669  1.00 95.47           C  
ANISOU 3157  CG2 VAL C  29    11214  10486  14572   1135  -1373  -1770       C  
ATOM   3158  N   VAL C  30     -47.180  -3.438 -11.728  1.00 87.74           N  
ANISOU 3158  N   VAL C  30    10867   8791  13679     91   -946  -1006       N  
ATOM   3159  CA  VAL C  30     -45.889  -4.151 -11.800  1.00 83.45           C  
ANISOU 3159  CA  VAL C  30    10529   7941  13234   -239   -802   -861       C  
ATOM   3160  C   VAL C  30     -44.686  -3.306 -12.202  1.00 84.06           C  
ANISOU 3160  C   VAL C  30    10858   7563  13518   -155   -817   -503       C  
ATOM   3161  O   VAL C  30     -44.797  -2.272 -12.868  1.00 85.18           O  
ANISOU 3161  O   VAL C  30    11069   7613  13683    142   -906   -267       O  
ATOM   3162  CB  VAL C  30     -45.936  -5.349 -12.774  1.00 82.00           C  
ANISOU 3162  CB  VAL C  30    10259   8098  12798   -473   -696   -916       C  
ATOM   3163  CG1 VAL C  30     -46.862  -6.411 -12.237  1.00 82.16           C  
ANISOU 3163  CG1 VAL C  30    10096   8458  12662   -729   -580  -1307       C  
ATOM   3164  CG2 VAL C  30     -46.346  -4.946 -14.180  1.00 84.29           C  
ANISOU 3164  CG2 VAL C  30    10428   8732  12865   -223   -800   -763       C  
ATOM   3165  N   ALA C  31     -43.522  -3.838 -11.829  1.00 83.12           N  
ANISOU 3165  N   ALA C  31    10879   7188  13514   -428   -701   -466       N  
ATOM   3166  CA  ALA C  31     -42.218  -3.381 -12.298  1.00 83.36           C  
ANISOU 3166  CA  ALA C  31    11098   6892  13679   -484   -660   -190       C  
ATOM   3167  C   ALA C  31     -41.726  -4.348 -13.376  1.00 83.12           C  
ANISOU 3167  C   ALA C  31    11064   7072  13445   -650   -583    -90       C  
ATOM   3168  O   ALA C  31     -41.731  -5.554 -13.158  1.00 82.13           O  
ANISOU 3168  O   ALA C  31    10893   7104  13208   -844   -491   -275       O  
ATOM   3169  CB  ALA C  31     -41.251  -3.378 -11.142  1.00 81.68           C  
ANISOU 3169  CB  ALA C  31    10967   6393  13672   -646   -594   -290       C  
ATOM   3170  N   MET C  32     -41.356  -3.828 -14.540  1.00 85.81           N  
ANISOU 3170  N   MET C  32    11465   7412  13724   -563   -601    195       N  
ATOM   3171  CA  MET C  32     -40.973  -4.652 -15.686  1.00 86.93           C  
ANISOU 3171  CA  MET C  32    11560   7827  13640   -686   -544    274       C  
ATOM   3172  C   MET C  32     -39.564  -4.325 -16.144  1.00 87.18           C  
ANISOU 3172  C   MET C  32    11740   7629  13753   -807   -473    522       C  
ATOM   3173  O   MET C  32     -39.339  -3.239 -16.585  1.00 88.99           O  
ANISOU 3173  O   MET C  32    12083   7672  14054   -692   -487    796       O  
ATOM   3174  CB  MET C  32     -41.912  -4.378 -16.840  1.00 90.87           C  
ANISOU 3174  CB  MET C  32    11927   8714  13884   -449   -631    385       C  
ATOM   3175  CG  MET C  32     -43.357  -4.722 -16.548  1.00 93.09           C  
ANISOU 3175  CG  MET C  32    11982   9371  14016   -340   -698     83       C  
ATOM   3176  SD  MET C  32     -44.594  -4.036 -17.693  1.00100.19           S  
ANISOU 3176  SD  MET C  32    12674  10803  14587    100   -851    198       S  
ATOM   3177  CE  MET C  32     -43.695  -3.855 -19.225  1.00102.42           C  
ANISOU 3177  CE  MET C  32    13045  11177  14690    144   -821    609       C  
ATOM   3178  N   LYS C  33     -38.624  -5.255 -16.011  1.00 86.42           N  
ANISOU 3178  N   LYS C  33    11653   7545  13637  -1031   -378    420       N  
ATOM   3179  CA  LYS C  33     -37.266  -5.072 -16.532  1.00 87.35           C  
ANISOU 3179  CA  LYS C  33    11843   7574  13770  -1165   -307    598       C  
ATOM   3180  C   LYS C  33     -37.225  -5.572 -17.943  1.00 87.85           C  
ANISOU 3180  C   LYS C  33    11826   7987  13565  -1178   -291    715       C  
ATOM   3181  O   LYS C  33     -37.544  -6.682 -18.172  1.00 88.57           O  
ANISOU 3181  O   LYS C  33    11819   8335  13499  -1227   -266    516       O  
ATOM   3182  CB  LYS C  33     -36.253  -5.835 -15.680  1.00 87.61           C  
ANISOU 3182  CB  LYS C  33    11890   7533  13864  -1321   -229    405       C  
ATOM   3183  CG  LYS C  33     -35.425  -4.962 -14.755  1.00 89.69           C  
ANISOU 3183  CG  LYS C  33    12207   7510  14358  -1383   -209    392       C  
ATOM   3184  CD  LYS C  33     -34.935  -5.693 -13.499  1.00 90.80           C  
ANISOU 3184  CD  LYS C  33    12320   7652  14526  -1404   -176    138       C  
ATOM   3185  CE  LYS C  33     -33.940  -4.857 -12.668  1.00 91.80           C  
ANISOU 3185  CE  LYS C  33    12420   7630  14829  -1492   -150     57       C  
ATOM   3186  NZ  LYS C  33     -34.273  -4.835 -11.212  1.00 90.88           N  
ANISOU 3186  NZ  LYS C  33    12268   7447  14812  -1409   -181   -166       N  
ATOM   3187  N   LYS C  34     -36.850  -4.760 -18.901  1.00 91.19           N  
ANISOU 3187  N   LYS C  34    12297   8425  13927  -1143   -282   1027       N  
ATOM   3188  CA  LYS C  34     -36.796  -5.189 -20.293  1.00 93.96           C  
ANISOU 3188  CA  LYS C  34    12537   9185  13975  -1137   -270   1146       C  
ATOM   3189  C   LYS C  34     -35.332  -5.457 -20.556  1.00 93.31           C  
ANISOU 3189  C   LYS C  34    12473   9094  13886  -1366   -166   1180       C  
ATOM   3190  O   LYS C  34     -34.502  -4.620 -20.278  1.00 92.16           O  
ANISOU 3190  O   LYS C  34    12444   8665  13905  -1473   -103   1330       O  
ATOM   3191  CB  LYS C  34     -37.363  -4.095 -21.203  1.00100.00           C  
ANISOU 3191  CB  LYS C  34    13353  10026  14616   -898   -317   1517       C  
ATOM   3192  CG  LYS C  34     -37.332  -4.355 -22.713  1.00104.54           C  
ANISOU 3192  CG  LYS C  34    13796  11101  14822   -842   -311   1696       C  
ATOM   3193  CD  LYS C  34     -37.697  -3.088 -23.523  1.00110.73           C  
ANISOU 3193  CD  LYS C  34    14711  11878  15480   -553   -326   2174       C  
ATOM   3194  CE  LYS C  34     -36.469  -2.226 -23.916  1.00112.88           C  
ANISOU 3194  CE  LYS C  34    15219  11832  15838   -725   -168   2560       C  
ATOM   3195  NZ  LYS C  34     -35.819  -2.603 -25.213  1.00113.75           N  
ANISOU 3195  NZ  LYS C  34    15208  12399  15610   -827   -100   2726       N  
ATOM   3196  N   ILE C  35     -35.008  -6.670 -21.006  1.00 93.92           N  
ANISOU 3196  N   ILE C  35    12422   9483  13780  -1454   -132    979       N  
ATOM   3197  CA  ILE C  35     -33.607  -7.088 -21.222  1.00 94.41           C  
ANISOU 3197  CA  ILE C  35    12458   9618  13796  -1625    -44    942       C  
ATOM   3198  C   ILE C  35     -33.413  -7.675 -22.618  1.00 96.59           C  
ANISOU 3198  C   ILE C  35    12580  10359  13759  -1649    -21    967       C  
ATOM   3199  O   ILE C  35     -34.092  -8.602 -22.992  1.00 96.33           O  
ANISOU 3199  O   ILE C  35    12439  10583  13578  -1602    -36    752       O  
ATOM   3200  CB  ILE C  35     -33.138  -8.083 -20.142  1.00 92.89           C  
ANISOU 3200  CB  ILE C  35    12288   9298  13708  -1659     -8    619       C  
ATOM   3201  CG1 ILE C  35     -33.011  -7.379 -18.786  1.00 94.35           C  
ANISOU 3201  CG1 ILE C  35    12577   9108  14162  -1656    -22    601       C  
ATOM   3202  CG2 ILE C  35     -31.767  -8.672 -20.462  1.00 92.16           C  
ANISOU 3202  CG2 ILE C  35    12125   9393  13497  -1748     64    534       C  
ATOM   3203  CD1 ILE C  35     -33.180  -8.328 -17.613  1.00 93.76           C  
ANISOU 3203  CD1 ILE C  35    12549   8920  14153  -1586     -9    326       C  
ATOM   3204  N   ARG C  36     -32.454  -7.124 -23.358  1.00101.50           N  
ANISOU 3204  N   ARG C  36    13182  11103  14280  -1758     38   1197       N  
ATOM   3205  CA  ARG C  36     -32.139  -7.505 -24.742  1.00104.71           C  
ANISOU 3205  CA  ARG C  36    13422  12003  14359  -1789     66   1261       C  
ATOM   3206  C   ARG C  36     -31.074  -8.553 -24.660  1.00104.64           C  
ANISOU 3206  C   ARG C  36    13314  12144  14299  -1897    124    961       C  
ATOM   3207  O   ARG C  36     -30.002  -8.293 -24.083  1.00104.84           O  
ANISOU 3207  O   ARG C  36    13374  12015  14443  -2013    178    945       O  
ATOM   3208  CB  ARG C  36     -31.582  -6.306 -25.518  1.00109.11           C  
ANISOU 3208  CB  ARG C  36    14036  12595  14824  -1872    138   1694       C  
ATOM   3209  CG  ARG C  36     -31.280  -6.579 -26.980  1.00113.40           C  
ANISOU 3209  CG  ARG C  36    14395  13706  14984  -1892    172   1811       C  
ATOM   3210  CD  ARG C  36     -30.525  -5.418 -27.640  1.00118.73           C  
ANISOU 3210  CD  ARG C  36    15171  14367  15573  -2039    303   2259       C  
ATOM   3211  NE  ARG C  36     -30.989  -5.201 -29.019  1.00123.21           N  
ANISOU 3211  NE  ARG C  36    15651  15408  15754  -1891    300   2569       N  
ATOM   3212  CZ  ARG C  36     -32.099  -4.541 -29.360  1.00125.68           C  
ANISOU 3212  CZ  ARG C  36    16064  15717  15969  -1602    239   2879       C  
ATOM   3213  NH1 ARG C  36     -32.879  -3.984 -28.427  1.00124.63           N  
ANISOU 3213  NH1 ARG C  36    16135  15091  16126  -1444    179   2917       N  
ATOM   3214  NH2 ARG C  36     -32.418  -4.435 -30.643  1.00128.77           N  
ANISOU 3214  NH2 ARG C  36    16332  16655  15937  -1433    235   3142       N  
ATOM   3215  N   LEU C  37     -31.361  -9.740 -25.182  1.00106.55           N  
ANISOU 3215  N   LEU C  37    13426  12692  14366  -1846    122    683       N  
ATOM   3216  CA  LEU C  37     -30.415 -10.830 -25.056  1.00107.30           C  
ANISOU 3216  CA  LEU C  37    13470  12879  14420  -1869    183    376       C  
ATOM   3217  C   LEU C  37     -29.478 -10.960 -26.215  1.00109.33           C  
ANISOU 3217  C   LEU C  37    13531  13609  14401  -1947    225    398       C  
ATOM   3218  O   LEU C  37     -29.867 -10.841 -27.377  1.00109.00           O  
ANISOU 3218  O   LEU C  37    13340  13962  14111  -1958    213    507       O  
ATOM   3219  CB  LEU C  37     -31.098 -12.158 -24.779  1.00107.72           C  
ANISOU 3219  CB  LEU C  37    13561  12871  14496  -1789    214      1       C  
ATOM   3220  CG  LEU C  37     -31.184 -12.456 -23.277  1.00107.44           C  
ANISOU 3220  CG  LEU C  37    13746  12346  14729  -1718    236   -117       C  
ATOM   3221  CD1 LEU C  37     -32.099 -13.655 -23.083  1.00106.70           C  
ANISOU 3221  CD1 LEU C  37    13737  12143  14659  -1696    318   -436       C  
ATOM   3222  CD2 LEU C  37     -29.806 -12.684 -22.622  1.00107.76           C  
ANISOU 3222  CD2 LEU C  37    13831  12303  14807  -1652    272   -180       C  
ATOM   3223  N   GLU C  38     -28.227 -11.216 -25.829  1.00111.18           N  
ANISOU 3223  N   GLU C  38    13740  13852  14650  -1978    272    273       N  
ATOM   3224  CA  GLU C  38     -27.113 -11.411 -26.743  1.00113.85           C  
ANISOU 3224  CA  GLU C  38    13864  14664  14727  -2056    321    224       C  
ATOM   3225  C   GLU C  38     -27.539 -12.629 -27.590  1.00113.12           C  
ANISOU 3225  C   GLU C  38    13653  14887  14438  -1952    326    -70       C  
ATOM   3226  O   GLU C  38     -27.945 -13.666 -27.056  1.00112.63           O  
ANISOU 3226  O   GLU C  38    13706  14596  14489  -1819    345   -376       O  
ATOM   3227  CB  GLU C  38     -25.757 -11.678 -25.994  1.00113.45           C  
ANISOU 3227  CB  GLU C  38    13774  14617  14713  -2033    357     25       C  
ATOM   3228  CG  GLU C  38     -25.433 -10.851 -24.717  1.00112.33           C  
ANISOU 3228  CG  GLU C  38    13751  14103  14823  -2091    356    114       C  
ATOM   3229  CD  GLU C  38     -25.562 -11.627 -23.369  1.00111.82           C  
ANISOU 3229  CD  GLU C  38    13845  13701  14939  -1840    325   -129       C  
ATOM   3230  OE1 GLU C  38     -24.531 -12.125 -22.818  1.00115.55           O  
ANISOU 3230  OE1 GLU C  38    14241  14318  15342  -1697    339   -353       O  
ATOM   3231  OE2 GLU C  38     -26.686 -11.762 -22.809  1.00109.64           O  
ANISOU 3231  OE2 GLU C  38    13766  13049  14844  -1757    294   -100       O  
ATOM   3232  N   SER C  39     -27.506 -12.466 -28.905  1.00111.74           N  
ANISOU 3232  N   SER C  39    13263  15226  13967  -2029    332     24       N  
ATOM   3233  CA  SER C  39     -27.642 -13.571 -29.833  1.00109.80           C  
ANISOU 3233  CA  SER C  39    12829  15399  13491  -1971    353   -315       C  
ATOM   3234  C   SER C  39     -26.748 -14.723 -29.388  1.00108.50           C  
ANISOU 3234  C   SER C  39    12689  15159  13374  -1846    408   -719       C  
ATOM   3235  O   SER C  39     -25.652 -14.515 -28.901  1.00108.32           O  
ANISOU 3235  O   SER C  39    12666  15112  13376  -1826    417   -691       O  
ATOM   3236  CB  SER C  39     -27.221 -13.096 -31.213  1.00112.66           C  
ANISOU 3236  CB  SER C  39    12915  16408  13481  -2076    362   -128       C  
ATOM   3237  OG  SER C  39     -27.434 -14.081 -32.179  1.00114.60           O  
ANISOU 3237  OG  SER C  39    12933  17129  13479  -2027    376   -479       O  
ATOM   3238  N   GLU C  40     -27.209 -15.948 -29.535  1.00109.32           N  
ANISOU 3238  N   GLU C  40    12822  15230  13483  -1745    462  -1117       N  
ATOM   3239  CA  GLU C  40     -26.429 -17.100 -29.063  1.00110.18           C  
ANISOU 3239  CA  GLU C  40    13039  15171  13651  -1545    539  -1481       C  
ATOM   3240  C   GLU C  40     -26.055 -18.023 -30.216  1.00109.60           C  
ANISOU 3240  C   GLU C  40    12739  15582  13322  -1506    597  -1853       C  
ATOM   3241  O   GLU C  40     -26.664 -17.993 -31.261  1.00109.00           O  
ANISOU 3241  O   GLU C  40    12445  15911  13057  -1643    592  -1910       O  
ATOM   3242  CB  GLU C  40     -27.172 -17.871 -27.951  1.00111.35           C  
ANISOU 3242  CB  GLU C  40    13545  14663  14097  -1428    619  -1651       C  
ATOM   3243  CG  GLU C  40     -28.523 -18.456 -28.362  1.00114.59           C  
ANISOU 3243  CG  GLU C  40    13983  15009  14545  -1560    697  -1885       C  
ATOM   3244  CD  GLU C  40     -29.088 -19.448 -27.345  1.00116.70           C  
ANISOU 3244  CD  GLU C  40    14626  14633  15080  -1483    852  -2121       C  
ATOM   3245  OE1 GLU C  40     -29.254 -20.653 -27.743  1.00120.58           O  
ANISOU 3245  OE1 GLU C  40    15189  15060  15565  -1477   1021  -2547       O  
ATOM   3246  OE2 GLU C  40     -29.378 -19.010 -26.186  1.00112.82           O  
ANISOU 3246  OE2 GLU C  40    14361  13707  14798  -1449    827  -1890       O  
ATOM   3247  N   GLU C  41     -25.072 -18.870 -29.966  1.00107.93           N  
ANISOU 3247  N   GLU C  41    12578  15336  13093  -1274    653  -2129       N  
ATOM   3248  CA  GLU C  41     -24.578 -19.794 -30.950  1.00108.65           C  
ANISOU 3248  CA  GLU C  41    12471  15849  12961  -1184    714  -2531       C  
ATOM   3249  C   GLU C  41     -25.571 -20.954 -31.120  1.00111.77           C  
ANISOU 3249  C   GLU C  41    13036  15946  13484  -1184    857  -2944       C  
ATOM   3250  O   GLU C  41     -26.433 -21.205 -30.248  1.00112.46           O  
ANISOU 3250  O   GLU C  41    13455  15422  13852  -1201    933  -2935       O  
ATOM   3251  CB  GLU C  41     -23.222 -20.294 -30.492  1.00107.22           C  
ANISOU 3251  CB  GLU C  41    12320  15691  12728   -864    726  -2692       C  
ATOM   3252  CG  GLU C  41     -22.436 -21.034 -31.527  1.00108.99           C  
ANISOU 3252  CG  GLU C  41    12271  16469  12671   -739    759  -3078       C  
ATOM   3253  CD  GLU C  41     -21.041 -21.343 -31.062  1.00109.67           C  
ANISOU 3253  CD  GLU C  41    12322  16697  12649   -385    739  -3205       C  
ATOM   3254  OE1 GLU C  41     -20.434 -22.307 -31.567  1.00111.83           O  
ANISOU 3254  OE1 GLU C  41    12511  17207  12771   -122    795  -3615       O  
ATOM   3255  OE2 GLU C  41     -20.530 -20.607 -30.201  1.00108.46           O  
ANISOU 3255  OE2 GLU C  41    12196  16472  12541   -356    668  -2928       O  
ATOM   3256  N   GLU C  42     -25.439 -21.640 -32.254  1.00115.92           N  
ANISOU 3256  N   GLU C  42    13315  16935  13792  -1201    914  -3334       N  
ATOM   3257  CA  GLU C  42     -26.244 -22.805 -32.685  1.00118.00           C  
ANISOU 3257  CA  GLU C  42    13651  17054  14127  -1264   1090  -3858       C  
ATOM   3258  C   GLU C  42     -26.655 -23.827 -31.614  1.00117.25           C  
ANISOU 3258  C   GLU C  42    14080  16074  14395  -1135   1294  -4080       C  
ATOM   3259  O   GLU C  42     -27.817 -23.870 -31.194  1.00114.17           O  
ANISOU 3259  O   GLU C  42    13869  15306  14202  -1346   1380  -4087       O  
ATOM   3260  CB  GLU C  42     -25.476 -23.520 -33.813  1.00122.39           C  
ANISOU 3260  CB  GLU C  42    13909  18180  14411  -1166   1130  -4296       C  
ATOM   3261  CG  GLU C  42     -26.241 -24.599 -34.550  1.00127.35           C  
ANISOU 3261  CG  GLU C  42    14486  18851  15048  -1303   1313  -4907       C  
ATOM   3262  CD  GLU C  42     -27.307 -24.018 -35.470  1.00129.11           C  
ANISOU 3262  CD  GLU C  42    14320  19679  15057  -1647   1246  -4898       C  
ATOM   3263  OE1 GLU C  42     -27.287 -24.339 -36.689  1.00132.84           O  
ANISOU 3263  OE1 GLU C  42    14389  20853  15232  -1732   1258  -5272       O  
ATOM   3264  OE2 GLU C  42     -28.160 -23.234 -34.969  1.00126.68           O  
ANISOU 3264  OE2 GLU C  42    14092  19189  14850  -1795   1173  -4526       O  
ATOM   3265  N   GLY C  43     -25.700 -24.637 -31.174  1.00119.61           N  
ANISOU 3265  N   GLY C  43    14624  16070  14753   -771   1384  -4249       N  
ATOM   3266  CA  GLY C  43     -25.954 -25.639 -30.150  1.00122.36           C  
ANISOU 3266  CA  GLY C  43    15536  15545  15410   -577   1612  -4398       C  
ATOM   3267  C   GLY C  43     -26.091 -24.977 -28.797  1.00120.81           C  
ANISOU 3267  C   GLY C  43    15619  14888  15396   -500   1540  -3913       C  
ATOM   3268  O   GLY C  43     -27.124 -25.085 -28.157  1.00120.85           O  
ANISOU 3268  O   GLY C  43    15903  14381  15631   -684   1659  -3865       O  
ATOM   3269  N   VAL C  44     -25.060 -24.230 -28.412  1.00121.27           N  
ANISOU 3269  N   VAL C  44    15541  15213  15323   -271   1345  -3587       N  
ATOM   3270  CA  VAL C  44     -24.962 -23.582 -27.101  1.00121.43           C  
ANISOU 3270  CA  VAL C  44    15770  14889  15475   -147   1262  -3174       C  
ATOM   3271  C   VAL C  44     -26.306 -23.076 -26.549  1.00121.57           C  
ANISOU 3271  C   VAL C  44    15939  14532  15719   -479   1282  -2963       C  
ATOM   3272  O   VAL C  44     -26.809 -22.048 -26.971  1.00115.73           O  
ANISOU 3272  O   VAL C  44    14912  14134  14927   -787   1137  -2757       O  
ATOM   3273  CB  VAL C  44     -23.964 -22.400 -27.108  1.00120.75           C  
ANISOU 3273  CB  VAL C  44    15319  15371  15188   -122   1026  -2871       C  
ATOM   3274  CG1 VAL C  44     -23.891 -21.683 -25.736  1.00117.75           C  
ANISOU 3274  CG1 VAL C  44    15114  14677  14949    -30    947  -2509       C  
ATOM   3275  CG2 VAL C  44     -22.571 -22.898 -27.487  1.00124.23           C  
ANISOU 3275  CG2 VAL C  44    15588  16235  15378    239   1004  -3101       C  
ATOM   3276  N   PRO C  45     -26.883 -23.826 -25.594  1.00125.90           N  
ANISOU 3276  N   PRO C  45    16958  14374  16502   -387   1479  -3011       N  
ATOM   3277  CA  PRO C  45     -28.125 -23.381 -24.992  1.00124.16           C  
ANISOU 3277  CA  PRO C  45    16861  13836  16475   -687   1504  -2843       C  
ATOM   3278  C   PRO C  45     -27.813 -22.430 -23.864  1.00121.47           C  
ANISOU 3278  C   PRO C  45    16563  13405  16183   -549   1339  -2415       C  
ATOM   3279  O   PRO C  45     -26.786 -22.581 -23.190  1.00121.42           O  
ANISOU 3279  O   PRO C  45    16678  13333  16122   -161   1312  -2318       O  
ATOM   3280  CB  PRO C  45     -28.737 -24.679 -24.478  1.00127.46           C  
ANISOU 3280  CB  PRO C  45    17778  13552  17097   -661   1835  -3105       C  
ATOM   3281  CG  PRO C  45     -27.550 -25.537 -24.129  1.00130.33           C  
ANISOU 3281  CG  PRO C  45    18427  13683  17409   -136   1930  -3166       C  
ATOM   3282  CD  PRO C  45     -26.409 -25.103 -25.010  1.00129.01           C  
ANISOU 3282  CD  PRO C  45    17813  14229  16974     22   1706  -3199       C  
ATOM   3283  N   SER C  46     -28.705 -21.472 -23.659  1.00120.33           N  
ANISOU 3283  N   SER C  46    16301  13294  16125   -842   1233  -2198       N  
ATOM   3284  CA  SER C  46     -28.458 -20.395 -22.717  1.00117.91           C  
ANISOU 3284  CA  SER C  46    15966  12965  15869   -776   1065  -1830       C  
ATOM   3285  C   SER C  46     -28.737 -20.806 -21.260  1.00118.30           C  
ANISOU 3285  C   SER C  46    16424  12433  16091   -592   1182  -1739       C  
ATOM   3286  O   SER C  46     -29.880 -21.035 -20.857  1.00115.56           O  
ANISOU 3286  O   SER C  46    16270  11736  15898   -787   1305  -1773       O  
ATOM   3287  CB  SER C  46     -29.274 -19.162 -23.075  1.00116.60           C  
ANISOU 3287  CB  SER C  46    15536  13043  15722  -1102    909  -1624       C  
ATOM   3288  OG  SER C  46     -29.157 -18.197 -22.053  1.00114.36           O  
ANISOU 3288  OG  SER C  46    15283  12625  15543  -1056    790  -1325       O  
ATOM   3289  N   THR C  47     -27.656 -20.864 -20.486  1.00120.14           N  
ANISOU 3289  N   THR C  47    16746  12647  16254   -211   1142  -1632       N  
ATOM   3290  CA  THR C  47     -27.716 -21.041 -19.034  1.00119.11           C  
ANISOU 3290  CA  THR C  47    16939  12106  16210     35   1207  -1474       C  
ATOM   3291  C   THR C  47     -28.358 -19.850 -18.340  1.00115.18           C  
ANISOU 3291  C   THR C  47    16318  11608  15834   -192   1065  -1240       C  
ATOM   3292  O   THR C  47     -28.936 -20.019 -17.268  1.00115.54           O  
ANISOU 3292  O   THR C  47    16629  11281  15987   -139   1153  -1147       O  
ATOM   3293  CB  THR C  47     -26.311 -21.254 -18.409  1.00120.19           C  
ANISOU 3293  CB  THR C  47    17098  12406  16163    555   1155  -1429       C  
ATOM   3294  OG1 THR C  47     -25.422 -20.198 -18.828  1.00118.36           O  
ANISOU 3294  OG1 THR C  47    16404  12773  15793    487    926  -1385       O  
ATOM   3295  CG2 THR C  47     -25.750 -22.659 -18.774  1.00122.23           C  
ANISOU 3295  CG2 THR C  47    17626  12497  16317    933   1346  -1650       C  
ATOM   3296  N   ALA C  48     -28.225 -18.652 -18.930  1.00112.39           N  
ANISOU 3296  N   ALA C  48    15586  11659  15455   -427    864  -1139       N  
ATOM   3297  CA  ALA C  48     -28.863 -17.431 -18.409  1.00107.27           C  
ANISOU 3297  CA  ALA C  48    14825  10991  14942   -644    734   -935       C  
ATOM   3298  C   ALA C  48     -30.377 -17.632 -18.186  1.00104.58           C  
ANISOU 3298  C   ALA C  48    14654  10323  14759   -861    830   -963       C  
ATOM   3299  O   ALA C  48     -30.872 -17.391 -17.091  1.00103.14           O  
ANISOU 3299  O   ALA C  48    14607   9891  14690   -838    837   -867       O  
ATOM   3300  CB  ALA C  48     -28.588 -16.236 -19.323  1.00105.36           C  
ANISOU 3300  CB  ALA C  48    14228  11155  14649   -877    571   -818       C  
ATOM   3301  N   ILE C  49     -31.084 -18.138 -19.179  1.00104.84           N  
ANISOU 3301  N   ILE C  49    14656  10407  14772  -1067    917  -1140       N  
ATOM   3302  CA  ILE C  49     -32.497 -18.406 -18.999  1.00108.29           C  
ANISOU 3302  CA  ILE C  49    15202  10623  15320  -1300   1031  -1247       C  
ATOM   3303  C   ILE C  49     -32.723 -19.549 -18.022  1.00114.47           C  
ANISOU 3303  C   ILE C  49    16405  10903  16185  -1196   1286  -1345       C  
ATOM   3304  O   ILE C  49     -33.595 -19.427 -17.161  1.00115.92           O  
ANISOU 3304  O   ILE C  49    16713  10856  16475  -1301   1343  -1299       O  
ATOM   3305  CB  ILE C  49     -33.200 -18.742 -20.315  1.00111.22           C  
ANISOU 3305  CB  ILE C  49    15389  11258  15608  -1560   1085  -1493       C  
ATOM   3306  CG1 ILE C  49     -33.397 -17.471 -21.128  1.00110.10           C  
ANISOU 3306  CG1 ILE C  49    14875  11581  15376  -1668    851  -1319       C  
ATOM   3307  CG2 ILE C  49     -34.564 -19.396 -20.074  1.00112.60           C  
ANISOU 3307  CG2 ILE C  49    15702  11206  15874  -1816   1287  -1737       C  
ATOM   3308  CD1 ILE C  49     -32.213 -17.108 -21.992  1.00111.39           C  
ANISOU 3308  CD1 ILE C  49    14837  12104  15380  -1570    738  -1214       C  
ATOM   3309  N   ARG C  50     -31.959 -20.646 -18.140  1.00121.49           N  
ANISOU 3309  N   ARG C  50    17530  11615  17014   -972   1453  -1467       N  
ATOM   3310  CA  ARG C  50     -32.081 -21.775 -17.179  1.00127.43           C  
ANISOU 3310  CA  ARG C  50    18777  11809  17830   -805   1741  -1495       C  
ATOM   3311  C   ARG C  50     -32.171 -21.252 -15.743  1.00118.42           C  
ANISOU 3311  C   ARG C  50    17755  10509  16729   -652   1683  -1222       C  
ATOM   3312  O   ARG C  50     -33.048 -21.640 -14.974  1.00118.65           O  
ANISOU 3312  O   ARG C  50    18053  10181  16847   -777   1877  -1215       O  
ATOM   3313  CB  ARG C  50     -30.893 -22.775 -17.257  1.00139.25           C  
ANISOU 3313  CB  ARG C  50    20529  13159  19221   -377   1865  -1548       C  
ATOM   3314  CG  ARG C  50     -30.750 -23.634 -18.517  1.00150.52           C  
ANISOU 3314  CG  ARG C  50    21950  14622  20615   -461   2005  -1881       C  
ATOM   3315  CD  ARG C  50     -32.034 -24.342 -18.960  1.00158.77           C  
ANISOU 3315  CD  ARG C  50    23138  15385  21800   -917   2285  -2195       C  
ATOM   3316  NE  ARG C  50     -31.887 -25.053 -20.245  1.00167.80           N  
ANISOU 3316  NE  ARG C  50    24188  16665  22900  -1031   2396  -2578       N  
ATOM   3317  CZ  ARG C  50     -31.763 -24.485 -21.459  1.00170.74           C  
ANISOU 3317  CZ  ARG C  50    24068  17659  23145  -1190   2182  -2710       C  
ATOM   3318  NH1 ARG C  50     -31.746 -23.157 -21.630  1.00167.01           N  
ANISOU 3318  NH1 ARG C  50    23177  17693  22585  -1257   1854  -2459       N  
ATOM   3319  NH2 ARG C  50     -31.647 -25.271 -22.538  1.00175.74           N  
ANISOU 3319  NH2 ARG C  50    24642  18400  23728  -1277   2320  -3102       N  
ATOM   3320  N   GLU C  51     -31.220 -20.397 -15.392  1.00110.20           N  
ANISOU 3320  N   GLU C  51    16497   9770  15603   -398   1437  -1031       N  
ATOM   3321  CA  GLU C  51     -31.181 -19.764 -14.079  1.00105.91           C  
ANISOU 3321  CA  GLU C  51    15972   9196  15071   -245   1345   -820       C  
ATOM   3322  C   GLU C  51     -32.454 -19.017 -13.758  1.00100.54           C  
ANISOU 3322  C   GLU C  51    15183   8478  14538   -598   1296   -795       C  
ATOM   3323  O   GLU C  51     -33.014 -19.185 -12.688  1.00 97.41           O  
ANISOU 3323  O   GLU C  51    14993   7837  14180   -575   1403   -723       O  
ATOM   3324  CB  GLU C  51     -30.005 -18.785 -13.997  1.00105.77           C  
ANISOU 3324  CB  GLU C  51    15620   9615  14951    -47   1082   -722       C  
ATOM   3325  CG  GLU C  51     -28.630 -19.442 -14.030  1.00108.72           C  
ANISOU 3325  CG  GLU C  51    16049  10141  15120    398   1101   -754       C  
ATOM   3326  CD  GLU C  51     -28.367 -20.287 -12.805  1.00111.42           C  
ANISOU 3326  CD  GLU C  51    16768  10213  15352    852   1258   -651       C  
ATOM   3327  OE1 GLU C  51     -28.688 -19.821 -11.681  1.00108.67           O  
ANISOU 3327  OE1 GLU C  51    16439   9829  15022    891   1222   -516       O  
ATOM   3328  OE2 GLU C  51     -27.841 -21.413 -12.977  1.00115.54           O  
ANISOU 3328  OE2 GLU C  51    17575  10566  15756   1197   1426   -699       O  
ATOM   3329  N   ILE C  52     -32.888 -18.167 -14.682  1.00 99.30           N  
ANISOU 3329  N   ILE C  52    14694   8601  14433   -886   1131   -843       N  
ATOM   3330  CA  ILE C  52     -34.065 -17.315 -14.463  1.00 98.07           C  
ANISOU 3330  CA  ILE C  52    14384   8488  14389  -1150   1042   -825       C  
ATOM   3331  C   ILE C  52     -35.335 -18.145 -14.242  1.00 97.11           C  
ANISOU 3331  C   ILE C  52    14469   8108  14319  -1388   1285   -995       C  
ATOM   3332  O   ILE C  52     -36.125 -17.860 -13.348  1.00 95.62           O  
ANISOU 3332  O   ILE C  52    14316   7822  14193  -1469   1304   -965       O  
ATOM   3333  CB  ILE C  52     -34.323 -16.376 -15.646  1.00 99.13           C  
ANISOU 3333  CB  ILE C  52    14169   8975  14520  -1345    853   -826       C  
ATOM   3334  CG1 ILE C  52     -33.132 -15.450 -15.963  1.00 97.66           C  
ANISOU 3334  CG1 ILE C  52    13773   9039  14291  -1215    656   -660       C  
ATOM   3335  CG2 ILE C  52     -35.559 -15.518 -15.366  1.00100.79           C  
ANISOU 3335  CG2 ILE C  52    14239   9233  14822  -1520    759   -807       C  
ATOM   3336  CD1 ILE C  52     -32.736 -14.509 -14.862  1.00 96.71           C  
ANISOU 3336  CD1 ILE C  52    13609   8883  14253  -1099    533   -514       C  
ATOM   3337  N   SER C  53     -35.513 -19.156 -15.075  1.00 98.83           N  
ANISOU 3337  N   SER C  53    14800   8245  14506  -1528   1485  -1213       N  
ATOM   3338  CA  SER C  53     -36.524 -20.191 -14.860  1.00101.73           C  
ANISOU 3338  CA  SER C  53    15430   8301  14921  -1791   1810  -1435       C  
ATOM   3339  C   SER C  53     -36.605 -20.570 -13.377  1.00101.72           C  
ANISOU 3339  C   SER C  53    15794   7904  14951  -1652   1982  -1272       C  
ATOM   3340  O   SER C  53     -37.647 -20.466 -12.740  1.00100.41           O  
ANISOU 3340  O   SER C  53    15646   7673  14829  -1882   2073  -1318       O  
ATOM   3341  CB  SER C  53     -36.193 -21.466 -15.693  1.00104.65           C  
ANISOU 3341  CB  SER C  53    16017   8477  15266  -1835   2070  -1677       C  
ATOM   3342  OG  SER C  53     -35.541 -21.158 -16.926  1.00103.90           O  
ANISOU 3342  OG  SER C  53    15620   8772  15085  -1779   1880  -1740       O  
ATOM   3343  N   LEU C  54     -35.469 -20.983 -12.836  1.00101.99           N  
ANISOU 3343  N   LEU C  54    16088   7742  14919  -1239   2017  -1079       N  
ATOM   3344  CA  LEU C  54     -35.397 -21.446 -11.462  1.00103.30           C  
ANISOU 3344  CA  LEU C  54    16631   7569  15048  -1009   2196   -883       C  
ATOM   3345  C   LEU C  54     -35.706 -20.382 -10.412  1.00 96.77           C  
ANISOU 3345  C   LEU C  54    15600   6946  14221   -973   1991   -719       C  
ATOM   3346  O   LEU C  54     -36.275 -20.685  -9.377  1.00 97.40           O  
ANISOU 3346  O   LEU C  54    15913   6808  14284   -998   2172   -640       O  
ATOM   3347  CB  LEU C  54     -34.022 -22.056 -11.199  1.00108.36           C  
ANISOU 3347  CB  LEU C  54    17534   8082  15554   -471   2235   -717       C  
ATOM   3348  CG  LEU C  54     -33.766 -23.510 -11.646  1.00116.46           C  
ANISOU 3348  CG  LEU C  54    19024   8654  16572   -371   2587   -823       C  
ATOM   3349  CD1 LEU C  54     -34.741 -24.100 -12.683  1.00119.40           C  
ANISOU 3349  CD1 LEU C  54    19424   8855  17087   -907   2818  -1177       C  
ATOM   3350  CD2 LEU C  54     -32.312 -23.632 -12.125  1.00118.94           C  
ANISOU 3350  CD2 LEU C  54    19272   9171  16746    109   2434   -785       C  
ATOM   3351  N   LEU C  55     -35.328 -19.141 -10.679  1.00 90.26           N  
ANISOU 3351  N   LEU C  55    14353   6525  13414   -926   1641   -677       N  
ATOM   3352  CA  LEU C  55     -35.583 -18.021  -9.739  1.00 85.51           C  
ANISOU 3352  CA  LEU C  55    13530   6116  12842   -895   1437   -575       C  
ATOM   3353  C   LEU C  55     -37.040 -17.621  -9.687  1.00 83.39           C  
ANISOU 3353  C   LEU C  55    13126   5884  12672  -1269   1450   -707       C  
ATOM   3354  O   LEU C  55     -37.505 -17.008  -8.736  1.00 80.19           O  
ANISOU 3354  O   LEU C  55    12634   5548  12287  -1264   1376   -664       O  
ATOM   3355  CB  LEU C  55     -34.700 -16.819 -10.111  1.00 82.77           C  
ANISOU 3355  CB  LEU C  55    12815   6120  12511   -771   1111   -519       C  
ATOM   3356  CG  LEU C  55     -33.185 -17.024  -9.897  1.00 82.85           C  
ANISOU 3356  CG  LEU C  55    12860   6240  12379   -374   1063   -424       C  
ATOM   3357  CD1 LEU C  55     -32.364 -15.943 -10.586  1.00 82.42           C  
ANISOU 3357  CD1 LEU C  55    12435   6531  12347   -395    809   -434       C  
ATOM   3358  CD2 LEU C  55     -32.798 -17.082  -8.437  1.00 83.13           C  
ANISOU 3358  CD2 LEU C  55    13006   6286  12294    -47   1085   -308       C  
ATOM   3359  N   LYS C  56     -37.750 -17.938 -10.757  1.00 84.88           N  
ANISOU 3359  N   LYS C  56    13247   6103  12899  -1580   1529   -909       N  
ATOM   3360  CA  LYS C  56     -39.187 -17.709 -10.811  1.00 87.08           C  
ANISOU 3360  CA  LYS C  56    13364   6504  13219  -1932   1568  -1103       C  
ATOM   3361  C   LYS C  56     -39.896 -18.438  -9.688  1.00 88.56           C  
ANISOU 3361  C   LYS C  56    13838   6426  13382  -2061   1861  -1132       C  
ATOM   3362  O   LYS C  56     -40.871 -17.956  -9.167  1.00 86.50           O  
ANISOU 3362  O   LYS C  56    13414   6319  13130  -2229   1830  -1218       O  
ATOM   3363  CB  LYS C  56     -39.692 -18.182 -12.149  1.00 90.20           C  
ANISOU 3363  CB  LYS C  56    13650   7023  13597  -2218   1656  -1364       C  
ATOM   3364  CG  LYS C  56     -40.995 -17.587 -12.626  1.00 93.39           C  
ANISOU 3364  CG  LYS C  56    13695   7802  13986  -2497   1562  -1589       C  
ATOM   3365  CD  LYS C  56     -41.388 -18.162 -14.002  1.00 97.93           C  
ANISOU 3365  CD  LYS C  56    14128   8591  14490  -2757   1663  -1891       C  
ATOM   3366  CE  LYS C  56     -40.189 -18.542 -14.902  1.00 98.19           C  
ANISOU 3366  CE  LYS C  56    14243   8563  14502  -2590   1641  -1818       C  
ATOM   3367  NZ  LYS C  56     -40.538 -19.015 -16.276  1.00100.25           N  
ANISOU 3367  NZ  LYS C  56    14306   9115  14668  -2823   1712  -2136       N  
ATOM   3368  N   GLU C  57     -39.361 -19.590  -9.295  1.00 93.47           N  
ANISOU 3368  N   GLU C  57    14906   6650  13957  -1947   2155  -1039       N  
ATOM   3369  CA  GLU C  57     -39.974 -20.409  -8.230  1.00 97.88           C  
ANISOU 3369  CA  GLU C  57    15835   6884  14470  -2071   2510  -1009       C  
ATOM   3370  C   GLU C  57     -40.062 -19.693  -6.927  1.00 94.74           C  
ANISOU 3370  C   GLU C  57    15356   6627  14014  -1885   2376   -825       C  
ATOM   3371  O   GLU C  57     -41.058 -19.801  -6.245  1.00 96.35           O  
ANISOU 3371  O   GLU C  57    15592   6823  14191  -2140   2543   -901       O  
ATOM   3372  CB  GLU C  57     -39.206 -21.715  -7.935  1.00103.48           C  
ANISOU 3372  CB  GLU C  57    17121   7078  15116  -1840   2852   -842       C  
ATOM   3373  CG  GLU C  57     -38.874 -22.655  -9.097  1.00109.02           C  
ANISOU 3373  CG  GLU C  57    18020   7528  15873  -1931   3047  -1017       C  
ATOM   3374  CD  GLU C  57     -39.865 -22.607 -10.255  1.00110.32           C  
ANISOU 3374  CD  GLU C  57    17875   7911  16128  -2466   3070  -1429       C  
ATOM   3375  OE1 GLU C  57     -41.094 -22.621  -9.994  1.00111.26           O  
ANISOU 3375  OE1 GLU C  57    17913   8096  16265  -2897   3227  -1634       O  
ATOM   3376  OE2 GLU C  57     -39.392 -22.589 -11.420  1.00112.37           O  
ANISOU 3376  OE2 GLU C  57    17955   8331  16407  -2439   2939  -1565       O  
ATOM   3377  N   LEU C  58     -39.020 -18.949  -6.604  1.00 92.14           N  
ANISOU 3377  N   LEU C  58    14881   6474  13651  -1469   2082   -627       N  
ATOM   3378  CA  LEU C  58     -38.769 -18.569  -5.218  1.00 92.74           C  
ANISOU 3378  CA  LEU C  58    14976   6638  13620  -1188   2022   -437       C  
ATOM   3379  C   LEU C  58     -39.778 -17.561  -4.687  1.00 91.53           C  
ANISOU 3379  C   LEU C  58    14477   6779  13521  -1393   1859   -568       C  
ATOM   3380  O   LEU C  58     -39.906 -16.445  -5.224  1.00 88.64           O  
ANISOU 3380  O   LEU C  58    13715   6686  13275  -1444   1552   -685       O  
ATOM   3381  CB  LEU C  58     -37.370 -17.981  -5.057  1.00 91.54           C  
ANISOU 3381  CB  LEU C  58    14681   6690  13407   -730   1750   -286       C  
ATOM   3382  CG  LEU C  58     -36.197 -18.956  -4.991  1.00 94.40           C  
ANISOU 3382  CG  LEU C  58    15395   6860  13610   -318   1898    -99       C  
ATOM   3383  CD1 LEU C  58     -36.159 -19.944  -6.164  1.00 97.60           C  
ANISOU 3383  CD1 LEU C  58    16055   6946  14079   -461   2106   -183       C  
ATOM   3384  CD2 LEU C  58     -34.888 -18.195  -4.921  1.00 92.18           C  
ANISOU 3384  CD2 LEU C  58    14828   6941  13254     62   1592    -49       C  
ATOM   3385  N   ARG C  59     -40.520 -17.983  -3.667  1.00 91.96           N  
ANISOU 3385  N   ARG C  59    14703   6759  13476  -1506   2091   -545       N  
ATOM   3386  CA  ARG C  59     -41.419 -17.093  -2.964  1.00 91.06           C  
ANISOU 3386  CA  ARG C  59    14270   6957  13372  -1636   1952   -674       C  
ATOM   3387  C   ARG C  59     -40.968 -17.032  -1.534  1.00 88.44           C  
ANISOU 3387  C   ARG C  59    14032   6703  12866  -1311   1967   -472       C  
ATOM   3388  O   ARG C  59     -40.589 -18.054  -0.968  1.00 89.48           O  
ANISOU 3388  O   ARG C  59    14588   6582  12828  -1150   2257   -246       O  
ATOM   3389  CB  ARG C  59     -42.883 -17.561  -3.027  1.00 95.59           C  
ANISOU 3389  CB  ARG C  59    14857   7524  13939  -2131   2212   -906       C  
ATOM   3390  CG  ARG C  59     -43.486 -17.680  -4.425  1.00 99.25           C  
ANISOU 3390  CG  ARG C  59    15167   8027  14516  -2479   2220  -1178       C  
ATOM   3391  CD  ARG C  59     -43.617 -16.356  -5.179  1.00100.49           C  
ANISOU 3391  CD  ARG C  59    14834   8560  14787  -2402   1797  -1309       C  
ATOM   3392  NE  ARG C  59     -43.050 -16.494  -6.529  1.00104.54           N  
ANISOU 3392  NE  ARG C  59    15335   9014  15370  -2387   1722  -1319       N  
ATOM   3393  CZ  ARG C  59     -43.649 -16.205  -7.691  1.00108.29           C  
ANISOU 3393  CZ  ARG C  59    15533   9737  15874  -2576   1619  -1537       C  
ATOM   3394  NH1 ARG C  59     -44.875 -15.666  -7.752  1.00109.73           N  
ANISOU 3394  NH1 ARG C  59    15383  10282  16024  -2764   1540  -1786       N  
ATOM   3395  NH2 ARG C  59     -42.977 -16.442  -8.828  1.00110.60           N  
ANISOU 3395  NH2 ARG C  59    15853   9975  16195  -2533   1580  -1511       N  
ATOM   3396  N   HIS C  60     -41.043 -15.833  -0.956  1.00 82.71           N  
ANISOU 3396  N   HIS C  60    12918   6334  12173  -1199   1670   -564       N  
ATOM   3397  CA  HIS C  60     -40.789 -15.644   0.456  1.00 81.61           C  
ANISOU 3397  CA  HIS C  60    12762   6398  11848   -929   1662   -455       C  
ATOM   3398  C   HIS C  60     -41.242 -14.234   0.683  1.00 79.44           C  
ANISOU 3398  C   HIS C  60    12000   6471  11710   -974   1340   -701       C  
ATOM   3399  O   HIS C  60     -41.188 -13.446  -0.235  1.00 78.14           O  
ANISOU 3399  O   HIS C  60    11603   6328  11759  -1039   1108   -831       O  
ATOM   3400  CB  HIS C  60     -39.324 -15.853   0.769  1.00 80.49           C  
ANISOU 3400  CB  HIS C  60    12747   6273  11562   -452   1608   -233       C  
ATOM   3401  CG  HIS C  60     -38.985 -15.706   2.217  1.00 81.24           C  
ANISOU 3401  CG  HIS C  60    12793   6672  11400   -119   1598   -132       C  
ATOM   3402  ND1 HIS C  60     -38.913 -14.488   2.834  1.00 80.01           N  
ANISOU 3402  ND1 HIS C  60    12189   6929  11281    -35   1310   -331       N  
ATOM   3403  CD2 HIS C  60     -38.663 -16.617   3.162  1.00 84.28           C  
ANISOU 3403  CD2 HIS C  60    13521   7034  11465    183   1848    145       C  
ATOM   3404  CE1 HIS C  60     -38.575 -14.645   4.100  1.00 81.96           C  
ANISOU 3404  CE1 HIS C  60    12447   7461  11230    282   1364   -221       C  
ATOM   3405  NE2 HIS C  60     -38.423 -15.933   4.328  1.00 84.47           N  
ANISOU 3405  NE2 HIS C  60    13250   7536  11308    444   1687     98       N  
ATOM   3406  N   PRO C  61     -41.751 -13.923   1.874  1.00 80.31           N  
ANISOU 3406  N   PRO C  61    11976   6843  11694   -941   1347   -765       N  
ATOM   3407  CA  PRO C  61     -42.292 -12.576   2.082  1.00 79.24           C  
ANISOU 3407  CA  PRO C  61    11390   7006  11710   -981   1057  -1046       C  
ATOM   3408  C   PRO C  61     -41.260 -11.447   2.059  1.00 77.76           C  
ANISOU 3408  C   PRO C  61    10938   6942  11666   -716    742  -1116       C  
ATOM   3409  O   PRO C  61     -41.571 -10.346   1.570  1.00 76.41           O  
ANISOU 3409  O   PRO C  61    10492   6806  11733   -786    512  -1316       O  
ATOM   3410  CB  PRO C  61     -42.936 -12.654   3.477  1.00 81.48           C  
ANISOU 3410  CB  PRO C  61    11612   7572  11773   -974   1173  -1095       C  
ATOM   3411  CG  PRO C  61     -42.350 -13.865   4.120  1.00 83.92           C  
ANISOU 3411  CG  PRO C  61    12334   7759  11792   -803   1472   -767       C  
ATOM   3412  CD  PRO C  61     -42.071 -14.817   2.996  1.00 83.49           C  
ANISOU 3412  CD  PRO C  61    12648   7260  11811   -919   1658   -601       C  
ATOM   3413  N   ASN C  62     -40.099 -11.709   2.639  1.00 78.01           N  
ANISOU 3413  N   ASN C  62    11048   7061  11530   -410    754   -970       N  
ATOM   3414  CA  ASN C  62     -38.943 -10.846   2.509  1.00 77.77           C  
ANISOU 3414  CA  ASN C  62    10792   7153  11604   -213    519  -1055       C  
ATOM   3415  C   ASN C  62     -38.063 -10.990   1.262  1.00 76.15           C  
ANISOU 3415  C   ASN C  62    10693   6721  11520   -213    477   -947       C  
ATOM   3416  O   ASN C  62     -36.878 -10.641   1.313  1.00 75.94           O  
ANISOU 3416  O   ASN C  62    10539   6847  11465    -18    367   -974       O  
ATOM   3417  CB  ASN C  62     -38.064 -10.990   3.744  1.00 80.16           C  
ANISOU 3417  CB  ASN C  62    11029   7814  11615    138    530  -1023       C  
ATOM   3418  CG  ASN C  62     -38.837 -10.756   5.019  1.00 82.88           C  
ANISOU 3418  CG  ASN C  62    11214   8466  11809    158    554  -1148       C  
ATOM   3419  OD1 ASN C  62     -38.947 -11.652   5.859  1.00 86.59           O  
ANISOU 3419  OD1 ASN C  62    11891   9055  11952    313    762   -948       O  
ATOM   3420  ND2 ASN C  62     -39.393  -9.544   5.178  1.00 82.19           N  
ANISOU 3420  ND2 ASN C  62    10776   8502  11948     17    358  -1474       N  
ATOM   3421  N   ILE C  63     -38.606 -11.449   0.141  1.00 75.03           N  
ANISOU 3421  N   ILE C  63    10729   6286  11492   -441    560   -872       N  
ATOM   3422  CA  ILE C  63     -37.942 -11.260  -1.152  1.00 74.41           C  
ANISOU 3422  CA  ILE C  63    10651   6052  11568   -490    468   -832       C  
ATOM   3423  C   ILE C  63     -38.937 -10.775  -2.199  1.00 74.70           C  
ANISOU 3423  C   ILE C  63    10604   5956  11820   -769    397   -920       C  
ATOM   3424  O   ILE C  63     -40.118 -11.116  -2.136  1.00 75.19           O  
ANISOU 3424  O   ILE C  63    10706   6004  11857   -945    500   -982       O  
ATOM   3425  CB  ILE C  63     -37.203 -12.513  -1.686  1.00 74.78           C  
ANISOU 3425  CB  ILE C  63    11018   5933  11461   -377    647   -624       C  
ATOM   3426  CG1 ILE C  63     -38.208 -13.507  -2.262  1.00 75.97           C  
ANISOU 3426  CG1 ILE C  63    11441   5814  11607   -627    878   -575       C  
ATOM   3427  CG2 ILE C  63     -36.262 -13.076  -0.621  1.00 76.34           C  
ANISOU 3427  CG2 ILE C  63    11321   6308  11377      2    726   -505       C  
ATOM   3428  CD1 ILE C  63     -37.608 -14.765  -2.846  1.00 77.28           C  
ANISOU 3428  CD1 ILE C  63    11962   5737  11664   -542   1089   -413       C  
ATOM   3429  N   VAL C  64     -38.431 -10.048  -3.198  1.00 75.27           N  
ANISOU 3429  N   VAL C  64    10565   5971  12063   -801    244   -919       N  
ATOM   3430  CA  VAL C  64     -39.263  -9.506  -4.233  1.00 76.73           C  
ANISOU 3430  CA  VAL C  64    10663   6085  12405   -973    158   -961       C  
ATOM   3431  C   VAL C  64     -39.576 -10.581  -5.229  1.00 79.86           C  
ANISOU 3431  C   VAL C  64    11240   6390  12712  -1118    310   -886       C  
ATOM   3432  O   VAL C  64     -38.725 -11.011  -6.017  1.00 82.08           O  
ANISOU 3432  O   VAL C  64    11625   6595  12966  -1095    342   -775       O  
ATOM   3433  CB  VAL C  64     -38.625  -8.326  -4.924  1.00 76.85           C  
ANISOU 3433  CB  VAL C  64    10538   6049  12612   -950    -20   -944       C  
ATOM   3434  CG1 VAL C  64     -39.503  -7.847  -6.088  1.00 78.30           C  
ANISOU 3434  CG1 VAL C  64    10670   6185  12895  -1049    -96   -922       C  
ATOM   3435  CG2 VAL C  64     -38.470  -7.190  -3.920  1.00 77.15           C  
ANISOU 3435  CG2 VAL C  64    10391   6142  12780   -863   -140  -1102       C  
ATOM   3436  N   SER C  65     -40.815 -11.036  -5.192  1.00 83.54           N  
ANISOU 3436  N   SER C  65    11718   6900  13122  -1289    419   -994       N  
ATOM   3437  CA  SER C  65     -41.177 -12.178  -5.997  1.00 85.51           C  
ANISOU 3437  CA  SER C  65    12138   7073  13279  -1485    622  -1003       C  
ATOM   3438  C   SER C  65     -41.171 -11.769  -7.476  1.00 85.71           C  
ANISOU 3438  C   SER C  65    12033   7161  13372  -1540    493  -1001       C  
ATOM   3439  O   SER C  65     -41.747 -10.735  -7.892  1.00 87.31           O  
ANISOU 3439  O   SER C  65    12004   7515  13654  -1513    302  -1052       O  
ATOM   3440  CB  SER C  65     -42.477 -12.846  -5.517  1.00 87.67           C  
ANISOU 3440  CB  SER C  65    12446   7413  13451  -1727    828  -1174       C  
ATOM   3441  OG  SER C  65     -42.240 -13.599  -4.310  1.00 88.83           O  
ANISOU 3441  OG  SER C  65    12838   7434  13477  -1676   1039  -1085       O  
ATOM   3442  N   LEU C  66     -40.383 -12.555  -8.208  1.00 84.52           N  
ANISOU 3442  N   LEU C  66    12049   6892  13171  -1552    596   -913       N  
ATOM   3443  CA  LEU C  66     -40.295 -12.530  -9.650  1.00 83.16           C  
ANISOU 3443  CA  LEU C  66    11794   6807  12995  -1625    541   -911       C  
ATOM   3444  C   LEU C  66     -41.496 -13.280 -10.237  1.00 86.72           C  
ANISOU 3444  C   LEU C  66    12210   7387  13353  -1896    699  -1136       C  
ATOM   3445  O   LEU C  66     -41.480 -14.524 -10.329  1.00 89.14           O  
ANISOU 3445  O   LEU C  66    12735   7542  13590  -2056    961  -1222       O  
ATOM   3446  CB  LEU C  66     -38.980 -13.199 -10.040  1.00 81.90           C  
ANISOU 3446  CB  LEU C  66    11816   6509  12792  -1527    616   -787       C  
ATOM   3447  CG  LEU C  66     -38.720 -13.586 -11.499  1.00 81.63           C  
ANISOU 3447  CG  LEU C  66    11750   6561  12703  -1614    633   -807       C  
ATOM   3448  CD1 LEU C  66     -39.056 -12.458 -12.442  1.00 80.92           C  
ANISOU 3448  CD1 LEU C  66    11389   6712  12644  -1624    417   -764       C  
ATOM   3449  CD2 LEU C  66     -37.271 -13.998 -11.637  1.00 81.15           C  
ANISOU 3449  CD2 LEU C  66    11824   6407  12601  -1440    659   -686       C  
ATOM   3450  N   GLN C  67     -42.544 -12.529 -10.578  1.00 86.59           N  
ANISOU 3450  N   GLN C  67    11919   7654  13327  -1938    561  -1257       N  
ATOM   3451  CA  GLN C  67     -43.841 -13.101 -10.989  1.00 87.79           C  
ANISOU 3451  CA  GLN C  67    11931   8070  13352  -2207    695  -1558       C  
ATOM   3452  C   GLN C  67     -43.891 -13.807 -12.283  1.00 88.15           C  
ANISOU 3452  C   GLN C  67    11933   8267  13293  -2377    794  -1694       C  
ATOM   3453  O   GLN C  67     -44.594 -14.803 -12.403  1.00 91.48           O  
ANISOU 3453  O   GLN C  67    12377   8754  13628  -2694   1046  -1982       O  
ATOM   3454  CB  GLN C  67     -44.886 -12.007 -11.086  1.00 89.00           C  
ANISOU 3454  CB  GLN C  67    11750   8591  13475  -2103    477  -1658       C  
ATOM   3455  CG  GLN C  67     -45.780 -11.903  -9.870  1.00 89.93           C  
ANISOU 3455  CG  GLN C  67    11803   8780  13587  -2169    526  -1825       C  
ATOM   3456  CD  GLN C  67     -46.232 -10.493  -9.603  1.00 89.65           C  
ANISOU 3456  CD  GLN C  67    11531   8922  13608  -1877    242  -1794       C  
ATOM   3457  OE1 GLN C  67     -46.904  -9.879 -10.437  1.00 91.07           O  
ANISOU 3457  OE1 GLN C  67    11457   9442  13700  -1748     83  -1865       O  
ATOM   3458  NE2 GLN C  67     -45.871  -9.968  -8.436  1.00 89.23           N  
ANISOU 3458  NE2 GLN C  67    11559   8658  13684  -1736    183  -1700       N  
ATOM   3459  N   ASP C  68     -43.232 -13.270 -13.291  1.00 87.46           N  
ANISOU 3459  N   ASP C  68    11755   8277  13198  -2205    615  -1525       N  
ATOM   3460  CA  ASP C  68     -43.347 -13.860 -14.643  1.00 91.09           C  
ANISOU 3460  CA  ASP C  68    12097   9000  13514  -2349    681  -1687       C  
ATOM   3461  C   ASP C  68     -42.089 -13.579 -15.452  1.00 89.14           C  
ANISOU 3461  C   ASP C  68    11902   8685  13280  -2165    564  -1421       C  
ATOM   3462  O   ASP C  68     -41.291 -12.762 -15.068  1.00 84.06           O  
ANISOU 3462  O   ASP C  68    11329   7859  12749  -1948    414  -1137       O  
ATOM   3463  CB  ASP C  68     -44.613 -13.323 -15.369  1.00 94.17           C  
ANISOU 3463  CB  ASP C  68    12090   9961  13726  -2361    554  -1895       C  
ATOM   3464  CG  ASP C  68     -45.272 -14.350 -16.375  1.00 97.82           C  
ANISOU 3464  CG  ASP C  68    12372  10804  13990  -2678    745  -2306       C  
ATOM   3465  OD1 ASP C  68     -44.830 -15.531 -16.543  1.00 96.21           O  
ANISOU 3465  OD1 ASP C  68    12379  10358  13815  -2930   1008  -2459       O  
ATOM   3466  OD2 ASP C  68     -46.284 -13.913 -16.990  1.00100.57           O  
ANISOU 3466  OD2 ASP C  68    12342  11734  14136  -2646    627  -2503       O  
ATOM   3467  N   VAL C  69     -41.915 -14.314 -16.552  1.00 91.10           N  
ANISOU 3467  N   VAL C  69    12101   9106  13405  -2292    661  -1565       N  
ATOM   3468  CA  VAL C  69     -40.809 -14.114 -17.485  1.00 90.74           C  
ANISOU 3468  CA  VAL C  69    12047   9110  13317  -2153    564  -1362       C  
ATOM   3469  C   VAL C  69     -41.343 -14.311 -18.906  1.00 96.21           C  
ANISOU 3469  C   VAL C  69    12452  10321  13783  -2247    551  -1561       C  
ATOM   3470  O   VAL C  69     -42.131 -15.221 -19.138  1.00101.10           O  
ANISOU 3470  O   VAL C  69    12992  11107  14314  -2507    736  -1948       O  
ATOM   3471  CB  VAL C  69     -39.714 -15.123 -17.233  1.00 88.06           C  
ANISOU 3471  CB  VAL C  69    12004   8409  13045  -2174    745  -1363       C  
ATOM   3472  CG1 VAL C  69     -38.613 -14.942 -18.249  1.00 88.08           C  
ANISOU 3472  CG1 VAL C  69    11939   8557  12967  -2053    649  -1209       C  
ATOM   3473  CG2 VAL C  69     -39.176 -14.975 -15.833  1.00 85.86           C  
ANISOU 3473  CG2 VAL C  69    11973   7727  12923  -2033    756  -1181       C  
ATOM   3474  N   LEU C  70     -40.962 -13.444 -19.838  1.00 98.47           N  
ANISOU 3474  N   LEU C  70    12568  10891  13954  -2054    355  -1314       N  
ATOM   3475  CA  LEU C  70     -41.591 -13.457 -21.156  1.00103.74           C  
ANISOU 3475  CA  LEU C  70    12906  12168  14340  -2071    306  -1471       C  
ATOM   3476  C   LEU C  70     -40.569 -13.266 -22.211  1.00106.26           C  
ANISOU 3476  C   LEU C  70    13186  12646  14541  -1965    239  -1251       C  
ATOM   3477  O   LEU C  70     -39.518 -12.732 -21.943  1.00104.91           O  
ANISOU 3477  O   LEU C  70    13193  12165  14500  -1844    177   -919       O  
ATOM   3478  CB  LEU C  70     -42.639 -12.354 -21.290  1.00106.44           C  
ANISOU 3478  CB  LEU C  70    13002  12885  14552  -1857    107  -1372       C  
ATOM   3479  CG  LEU C  70     -43.488 -11.929 -20.072  1.00108.15           C  
ANISOU 3479  CG  LEU C  70    13258  12918  14915  -1822     75  -1421       C  
ATOM   3480  CD1 LEU C  70     -44.105 -10.548 -20.334  1.00110.64           C  
ANISOU 3480  CD1 LEU C  70    13399  13518  15120  -1453   -169  -1170       C  
ATOM   3481  CD2 LEU C  70     -44.565 -12.946 -19.689  1.00109.59           C  
ANISOU 3481  CD2 LEU C  70    13323  13272  15041  -2143    271  -1934       C  
ATOM   3482  N   MET C  71     -40.913 -13.653 -23.430  1.00114.08           N  
ANISOU 3482  N   MET C  71    13898  14192  15255  -2024    253  -1464       N  
ATOM   3483  CA  MET C  71     -39.996 -13.633 -24.563  1.00119.87           C  
ANISOU 3483  CA  MET C  71    14545  15184  15815  -1959    216  -1319       C  
ATOM   3484  C   MET C  71     -40.646 -12.988 -25.770  1.00124.22           C  
ANISOU 3484  C   MET C  71    14735  16457  16003  -1786     69  -1242       C  
ATOM   3485  O   MET C  71     -41.645 -13.485 -26.274  1.00127.16           O  
ANISOU 3485  O   MET C  71    14811  17350  16155  -1879    107  -1638       O  
ATOM   3486  CB  MET C  71     -39.581 -15.056 -24.913  1.00126.06           C  
ANISOU 3486  CB  MET C  71    15358  15951  16588  -2204    432  -1731       C  
ATOM   3487  CG  MET C  71     -38.734 -15.732 -23.834  1.00129.31           C  
ANISOU 3487  CG  MET C  71    16165  15665  17299  -2268    584  -1735       C  
ATOM   3488  SD  MET C  71     -36.920 -15.626 -24.059  1.00131.62           S  
ANISOU 3488  SD  MET C  71    16608  15778  17623  -2107    542  -1433       S  
ATOM   3489  CE  MET C  71     -36.632 -13.944 -24.562  1.00132.00           C  
ANISOU 3489  CE  MET C  71    16498  16098  17558  -1908    290   -905       C  
ATOM   3490  N   GLN C  72     -40.073 -11.875 -26.206  1.00127.47           N  
ANISOU 3490  N   GLN C  72    15181  16912  16340  -1536    -76   -738       N  
ATOM   3491  CA  GLN C  72     -40.443 -11.225 -27.458  1.00135.06           C  
ANISOU 3491  CA  GLN C  72    15862  18547  16909  -1300   -201   -542       C  
ATOM   3492  C   GLN C  72     -39.321 -11.555 -28.445  1.00138.34           C  
ANISOU 3492  C   GLN C  72    16228  19169  17163  -1374   -149   -463       C  
ATOM   3493  O   GLN C  72     -38.652 -12.584 -28.267  1.00135.61           O  
ANISOU 3493  O   GLN C  72    15961  18608  16956  -1618    -10   -763       O  
ATOM   3494  CB  GLN C  72     -40.625  -9.714 -27.229  1.00136.26           C  
ANISOU 3494  CB  GLN C  72    16154  18527  17091   -958   -354      4       C  
ATOM   3495  CG  GLN C  72     -41.878  -9.127 -27.886  1.00140.21           C  
ANISOU 3495  CG  GLN C  72    16364  19683  17225   -618   -493     45       C  
ATOM   3496  CD  GLN C  72     -43.191  -9.306 -27.099  1.00140.52           C  
ANISOU 3496  CD  GLN C  72    16265  19810  17314   -602   -528   -329       C  
ATOM   3497  OE1 GLN C  72     -44.156  -8.577 -27.347  1.00142.50           O  
ANISOU 3497  OE1 GLN C  72    16338  20480  17324   -238   -669   -228       O  
ATOM   3498  NE2 GLN C  72     -43.245 -10.259 -26.156  1.00139.54           N  
ANISOU 3498  NE2 GLN C  72    16223  19321  17471   -968   -390   -752       N  
ATOM   3499  N   ASP C  73     -39.090 -10.705 -29.448  1.00143.70           N  
ANISOU 3499  N   ASP C  73    16803  20250  17547  -1147   -242    -53       N  
ATOM   3500  CA  ASP C  73     -38.033 -10.948 -30.447  1.00149.25           C  
ANISOU 3500  CA  ASP C  73    17420  21240  18046  -1220   -191     35       C  
ATOM   3501  C   ASP C  73     -36.678 -10.774 -29.788  1.00146.05           C  
ANISOU 3501  C   ASP C  73    17341  20188  17964  -1358   -122    264       C  
ATOM   3502  O   ASP C  73     -36.230  -9.664 -29.564  1.00139.67           O  
ANISOU 3502  O   ASP C  73    16742  19071  17255  -1260   -154    750       O  
ATOM   3503  CB  ASP C  73     -38.137 -10.002 -31.643  1.00155.11           C  
ANISOU 3503  CB  ASP C  73    18002  22571  18362   -932   -284    486       C  
ATOM   3504  CG  ASP C  73     -39.545  -9.860 -32.156  1.00161.35           C  
ANISOU 3504  CG  ASP C  73    18472  24031  18799   -668   -394    356       C  
ATOM   3505  OD1 ASP C  73     -40.492 -10.012 -31.342  1.00162.93           O  
ANISOU 3505  OD1 ASP C  73    18664  24073  19166   -666   -424     81       O  
ATOM   3506  OD2 ASP C  73     -39.701  -9.569 -33.360  1.00164.88           O  
ANISOU 3506  OD2 ASP C  73    18659  25214  18771   -444   -449    530       O  
ATOM   3507  N   SER C  74     -36.102 -11.900 -29.371  1.00147.87           N  
ANISOU 3507  N   SER C  74    17625  20186  18373  -1580    -10   -131       N  
ATOM   3508  CA  SER C  74     -34.811 -11.947 -28.655  1.00146.12           C  
ANISOU 3508  CA  SER C  74    17657  19440  18421  -1680     53    -30       C  
ATOM   3509  C   SER C  74     -34.684 -11.009 -27.412  1.00141.17           C  
ANISOU 3509  C   SER C  74    17325  18180  18132  -1634     15    277       C  
ATOM   3510  O   SER C  74     -33.562 -10.758 -26.930  1.00141.00           O  
ANISOU 3510  O   SER C  74    17455  17845  18271  -1701     54    416       O  
ATOM   3511  CB  SER C  74     -33.658 -11.728 -29.649  1.00146.69           C  
ANISOU 3511  CB  SER C  74    17618  19855  18260  -1709     74    173       C  
ATOM   3512  OG  SER C  74     -32.393 -11.808 -29.008  1.00144.10           O  
ANISOU 3512  OG  SER C  74    17461  19150  18139  -1802    135    201       O  
ATOM   3513  N   ARG C  75     -35.817 -10.543 -26.866  1.00134.41           N  
ANISOU 3513  N   ARG C  75    16514  17184  17369  -1526    -53    318       N  
ATOM   3514  CA  ARG C  75     -35.803  -9.797 -25.613  1.00125.97           C  
ANISOU 3514  CA  ARG C  75    15698  15531  16632  -1489    -82    500       C  
ATOM   3515  C   ARG C  75     -36.730 -10.347 -24.535  1.00115.54           C  
ANISOU 3515  C   ARG C  75    14438  13955  15504  -1511    -72    185       C  
ATOM   3516  O   ARG C  75     -37.718 -11.030 -24.797  1.00114.28           O  
ANISOU 3516  O   ARG C  75    14115  14092  15213  -1539    -55   -127       O  
ATOM   3517  CB  ARG C  75     -36.057  -8.330 -25.849  1.00129.18           C  
ANISOU 3517  CB  ARG C  75    16177  15893  17012  -1309   -163    972       C  
ATOM   3518  CG  ARG C  75     -37.321  -8.000 -26.581  1.00135.53           C  
ANISOU 3518  CG  ARG C  75    16804  17150  17541  -1069   -259   1037       C  
ATOM   3519  CD  ARG C  75     -37.409  -6.490 -26.652  1.00143.81           C  
ANISOU 3519  CD  ARG C  75    18040  17985  18617   -835   -307   1567       C  
ATOM   3520  NE  ARG C  75     -36.473  -5.885 -27.615  1.00152.76           N  
ANISOU 3520  NE  ARG C  75    19233  19230  19575   -855   -236   1980       N  
ATOM   3521  CZ  ARG C  75     -36.671  -5.797 -28.938  1.00161.04           C  
ANISOU 3521  CZ  ARG C  75    20104  20882  20199   -695   -254   2176       C  
ATOM   3522  NH1 ARG C  75     -37.761  -6.324 -29.500  1.00166.43           N  
ANISOU 3522  NH1 ARG C  75    20487  22177  20571   -502   -353   1937       N  
ATOM   3523  NH2 ARG C  75     -35.769  -5.192 -29.719  1.00162.86           N  
ANISOU 3523  NH2 ARG C  75    20430  21166  20283   -746   -156   2588       N  
ATOM   3524  N   LEU C  76     -36.356 -10.022 -23.307  1.00104.51           N  
ANISOU 3524  N   LEU C  76    13262  12038  14407  -1524    -64    253       N  
ATOM   3525  CA  LEU C  76     -36.734 -10.749 -22.138  1.00 97.15           C  
ANISOU 3525  CA  LEU C  76    12445  10796  13670  -1590     -2    -31       C  
ATOM   3526  C   LEU C  76     -37.321  -9.798 -21.143  1.00 91.37           C  
ANISOU 3526  C   LEU C  76    11810   9765  13138  -1487    -85    106       C  
ATOM   3527  O   LEU C  76     -36.666  -8.866 -20.725  1.00 88.57           O  
ANISOU 3527  O   LEU C  76    11573   9140  12938  -1441   -124    358       O  
ATOM   3528  CB  LEU C  76     -35.473 -11.367 -21.538  1.00 96.00           C  
ANISOU 3528  CB  LEU C  76    12457  10367  13650  -1657     91   -100       C  
ATOM   3529  CG  LEU C  76     -35.581 -12.179 -20.237  1.00 96.08           C  
ANISOU 3529  CG  LEU C  76    12657  10009  13839  -1677    189   -324       C  
ATOM   3530  CD1 LEU C  76     -36.134 -13.571 -20.515  1.00 98.16           C  
ANISOU 3530  CD1 LEU C  76    12931  10351  14013  -1789    345   -680       C  
ATOM   3531  CD2 LEU C  76     -34.229 -12.317 -19.566  1.00 96.68           C  
ANISOU 3531  CD2 LEU C  76    12866   9862  14004  -1617    225   -272       C  
ATOM   3532  N   TYR C  77     -38.516 -10.106 -20.674  1.00 87.79           N  
ANISOU 3532  N   TYR C  77    11305   9355  12695  -1485    -86   -119       N  
ATOM   3533  CA  TYR C  77     -39.184  -9.243 -19.743  1.00 85.42           C  
ANISOU 3533  CA  TYR C  77    11060   8835  12560  -1365   -173    -40       C  
ATOM   3534  C   TYR C  77     -39.261  -9.882 -18.386  1.00 80.16           C  
ANISOU 3534  C   TYR C  77    10529   7845  12081  -1471    -83   -263       C  
ATOM   3535  O   TYR C  77     -39.865 -10.901 -18.237  1.00 80.06           O  
ANISOU 3535  O   TYR C  77    10490   7922  12008  -1611     30   -558       O  
ATOM   3536  CB  TYR C  77     -40.572  -8.966 -20.260  1.00 88.87           C  
ANISOU 3536  CB  TYR C  77    11280   9680  12806  -1234   -260   -121       C  
ATOM   3537  CG  TYR C  77     -40.536  -8.129 -21.499  1.00 93.44           C  
ANISOU 3537  CG  TYR C  77    11758  10574  13171  -1026   -361    190       C  
ATOM   3538  CD1 TYR C  77     -40.329  -8.711 -22.750  1.00 95.22           C  
ANISOU 3538  CD1 TYR C  77    11812  11251  13113  -1083   -327    142       C  
ATOM   3539  CD2 TYR C  77     -40.674  -6.738 -21.428  1.00 96.44           C  
ANISOU 3539  CD2 TYR C  77    12238  10781  13622   -755   -471    550       C  
ATOM   3540  CE1 TYR C  77     -40.295  -7.948 -23.896  1.00 98.83           C  
ANISOU 3540  CE1 TYR C  77    12180  12046  13322   -866   -407    468       C  
ATOM   3541  CE2 TYR C  77     -40.649  -5.967 -22.579  1.00100.57           C  
ANISOU 3541  CE2 TYR C  77    12728  11561  13919   -527   -530    902       C  
ATOM   3542  CZ  TYR C  77     -40.457  -6.586 -23.807  1.00101.74           C  
ANISOU 3542  CZ  TYR C  77    12688  12218  13748   -581   -501    874       C  
ATOM   3543  OH  TYR C  77     -40.422  -5.826 -24.949  1.00107.52           O  
ANISOU 3543  OH  TYR C  77    13391  13250  14211   -333   -548   1260       O  
ATOM   3544  N   LEU C  78     -38.680  -9.264 -17.387  1.00 76.36           N  
ANISOU 3544  N   LEU C  78    10193   7003  11814  -1417   -113   -132       N  
ATOM   3545  CA  LEU C  78     -38.811  -9.761 -16.050  1.00 74.46           C  
ANISOU 3545  CA  LEU C  78    10066   6515  11707  -1466    -39   -306       C  
ATOM   3546  C   LEU C  78     -39.904  -9.013 -15.323  1.00 75.14           C  
ANISOU 3546  C   LEU C  78    10090   6578  11880  -1373   -130   -349       C  
ATOM   3547  O   LEU C  78     -39.783  -7.827 -15.120  1.00 76.48           O  
ANISOU 3547  O   LEU C  78    10268   6612  12176  -1234   -245   -172       O  
ATOM   3548  CB  LEU C  78     -37.508  -9.590 -15.319  1.00 73.53           C  
ANISOU 3548  CB  LEU C  78    10083   6127  11725  -1439    -22   -203       C  
ATOM   3549  CG  LEU C  78     -36.522 -10.747 -15.427  1.00 73.77           C  
ANISOU 3549  CG  LEU C  78    10213   6146  11670  -1486    108   -279       C  
ATOM   3550  CD1 LEU C  78     -36.452 -11.381 -16.817  1.00 75.71           C  
ANISOU 3550  CD1 LEU C  78    10383   6649  11734  -1561    155   -318       C  
ATOM   3551  CD2 LEU C  78     -35.141 -10.262 -15.018  1.00 73.55           C  
ANISOU 3551  CD2 LEU C  78    10211   6022  11711  -1422     78   -163       C  
ATOM   3552  N   ILE C  79     -40.953  -9.691 -14.886  1.00 74.49           N  
ANISOU 3552  N   ILE C  79     9953   6610  11737  -1465    -57   -609       N  
ATOM   3553  CA  ILE C  79     -42.055  -9.026 -14.229  1.00 74.83           C  
ANISOU 3553  CA  ILE C  79     9888   6722  11823  -1369   -147   -699       C  
ATOM   3554  C   ILE C  79     -41.940  -9.202 -12.738  1.00 74.99           C  
ANISOU 3554  C   ILE C  79    10031   6473  11986  -1409    -81   -785       C  
ATOM   3555  O   ILE C  79     -42.015 -10.326 -12.256  1.00 76.09           O  
ANISOU 3555  O   ILE C  79    10271   6563  12075  -1585     99   -945       O  
ATOM   3556  CB  ILE C  79     -43.394  -9.584 -14.679  1.00 76.12           C  
ANISOU 3556  CB  ILE C  79     9838   7301  11781  -1468   -104   -983       C  
ATOM   3557  CG1 ILE C  79     -43.450  -9.686 -16.198  1.00 78.09           C  
ANISOU 3557  CG1 ILE C  79     9932   7920  11818  -1445   -139   -952       C  
ATOM   3558  CG2 ILE C  79     -44.531  -8.717 -14.191  1.00 77.26           C  
ANISOU 3558  CG2 ILE C  79     9808   7625  11922  -1291   -240  -1069       C  
ATOM   3559  CD1 ILE C  79     -43.204  -8.402 -16.947  1.00 79.15           C  
ANISOU 3559  CD1 ILE C  79    10027   8114  11932  -1138   -332   -610       C  
ATOM   3560  N   PHE C  80     -41.831  -8.093 -12.007  1.00 75.67           N  
ANISOU 3560  N   PHE C  80    10117   6394  12238  -1243   -208   -692       N  
ATOM   3561  CA  PHE C  80     -41.795  -8.092 -10.547  1.00 76.27           C  
ANISOU 3561  CA  PHE C  80    10251   6306  12423  -1244   -174   -795       C  
ATOM   3562  C   PHE C  80     -42.969  -7.330  -9.977  1.00 79.64           C  
ANISOU 3562  C   PHE C  80    10518   6855  12884  -1129   -281   -937       C  
ATOM   3563  O   PHE C  80     -43.572  -6.525 -10.681  1.00 81.60           O  
ANISOU 3563  O   PHE C  80    10647   7238  13118   -966   -414   -891       O  
ATOM   3564  CB  PHE C  80     -40.561  -7.371 -10.079  1.00 75.53           C  
ANISOU 3564  CB  PHE C  80    10243   5955  12499  -1156   -228   -648       C  
ATOM   3565  CG  PHE C  80     -39.293  -7.974 -10.568  1.00 74.64           C  
ANISOU 3565  CG  PHE C  80    10243   5777  12339  -1222   -147   -527       C  
ATOM   3566  CD1 PHE C  80     -38.656  -8.993  -9.831  1.00 74.17           C  
ANISOU 3566  CD1 PHE C  80    10305   5667  12207  -1249    -14   -583       C  
ATOM   3567  CD2 PHE C  80     -38.688  -7.498 -11.710  1.00 75.68           C  
ANISOU 3567  CD2 PHE C  80    10365   5912  12475  -1220   -197   -347       C  
ATOM   3568  CE1 PHE C  80     -37.446  -9.534 -10.252  1.00 74.07           C  
ANISOU 3568  CE1 PHE C  80    10379   5636  12128  -1243     46   -495       C  
ATOM   3569  CE2 PHE C  80     -37.469  -8.038 -12.134  1.00 75.39           C  
ANISOU 3569  CE2 PHE C  80    10394   5874  12375  -1277   -126   -272       C  
ATOM   3570  CZ  PHE C  80     -36.855  -9.053 -11.413  1.00 74.42           C  
ANISOU 3570  CZ  PHE C  80    10367   5727  12182  -1273    -15   -364       C  
ATOM   3571  N   GLU C  81     -43.256  -7.536  -8.687  1.00 91.04           N  
ANISOU 3571  N   GLU C  81    10029  11164  13397  -1192  -1292  -1119       N  
ATOM   3572  CA  GLU C  81     -44.221  -6.669  -7.965  1.00 93.41           C  
ANISOU 3572  CA  GLU C  81    10074  11280  14137  -1108  -1182   -912       C  
ATOM   3573  C   GLU C  81     -43.689  -5.255  -7.884  1.00 91.37           C  
ANISOU 3573  C   GLU C  81     9885  11025  13803   -895  -1158   -558       C  
ATOM   3574  O   GLU C  81     -42.491  -5.088  -7.710  1.00 88.04           O  
ANISOU 3574  O   GLU C  81     9792  10563  13097   -829  -1041   -504       O  
ATOM   3575  CB  GLU C  81     -44.538  -7.188  -6.539  1.00 93.92           C  
ANISOU 3575  CB  GLU C  81    10193  10935  14556  -1182   -779  -1034       C  
ATOM   3576  CG  GLU C  81     -43.417  -7.077  -5.507  1.00 91.21           C  
ANISOU 3576  CG  GLU C  81    10242  10344  14067  -1117   -446   -979       C  
ATOM   3577  CD  GLU C  81     -43.771  -7.667  -4.140  1.00 91.16           C  
ANISOU 3577  CD  GLU C  81    10291   9994  14350  -1209    -66  -1080       C  
ATOM   3578  OE1 GLU C  81     -44.418  -6.932  -3.336  1.00 91.58           O  
ANISOU 3578  OE1 GLU C  81    10209   9888  14697  -1144    136   -963       O  
ATOM   3579  OE2 GLU C  81     -43.380  -8.848  -3.897  1.00 89.98           O  
ANISOU 3579  OE2 GLU C  81    10316   9738  14133  -1343     36  -1267       O  
ATOM   3580  N   PHE C  82     -44.581  -4.263  -7.977  1.00 94.49           N  
ANISOU 3580  N   PHE C  82     9954  11438  14508   -790  -1259   -324       N  
ATOM   3581  CA  PHE C  82     -44.201  -2.841  -7.993  1.00 93.89           C  
ANISOU 3581  CA  PHE C  82     9876  11344  14453   -583  -1260     32       C  
ATOM   3582  C   PHE C  82     -44.108  -2.244  -6.595  1.00 91.21           C  
ANISOU 3582  C   PHE C  82     9631  10600  14424   -501   -856     67       C  
ATOM   3583  O   PHE C  82     -45.107  -2.085  -5.906  1.00 93.57           O  
ANISOU 3583  O   PHE C  82     9690  10696  15165   -505   -694     32       O  
ATOM   3584  CB  PHE C  82     -45.185  -1.962  -8.747  1.00 98.26           C  
ANISOU 3584  CB  PHE C  82    10006  12077  15250   -487  -1559    307       C  
ATOM   3585  CG  PHE C  82     -44.776  -0.543  -8.715  1.00 98.73           C  
ANISOU 3585  CG  PHE C  82    10054  12057  15401   -278  -1532    677       C  
ATOM   3586  CD1 PHE C  82     -43.695  -0.122  -9.458  1.00 98.68           C  
ANISOU 3586  CD1 PHE C  82    10258  12262  14971   -201  -1673    880       C  
ATOM   3587  CD2 PHE C  82     -45.405   0.365  -7.879  1.00100.59           C  
ANISOU 3587  CD2 PHE C  82    10078  11972  16168   -162  -1320    803       C  
ATOM   3588  CE1 PHE C  82     -43.278   1.202  -9.426  1.00 99.31           C  
ANISOU 3588  CE1 PHE C  82    10317  12235  15181    -14  -1635   1236       C  
ATOM   3589  CE2 PHE C  82     -44.995   1.686  -7.835  1.00101.31           C  
ANISOU 3589  CE2 PHE C  82    10149  11944  16399     27  -1280   1123       C  
ATOM   3590  CZ  PHE C  82     -43.922   2.109  -8.606  1.00 99.97           C  
ANISOU 3590  CZ  PHE C  82    10178  11976  15827    100  -1443   1351       C  
ATOM   3591  N   LEU C  83     -42.907  -1.897  -6.179  1.00 88.99           N  
ANISOU 3591  N   LEU C  83     9687  10212  13910   -429   -690    122       N  
ATOM   3592  CA  LEU C  83     -42.677  -1.204  -4.906  1.00 87.30           C  
ANISOU 3592  CA  LEU C  83     9590   9657  13923   -347   -336    147       C  
ATOM   3593  C   LEU C  83     -42.088   0.144  -5.223  1.00 86.64           C  
ANISOU 3593  C   LEU C  83     9504   9573  13841   -165   -408    446       C  
ATOM   3594  O   LEU C  83     -41.224   0.251  -6.077  1.00 86.76           O  
ANISOU 3594  O   LEU C  83     9655   9800  13509   -129   -605    580       O  
ATOM   3595  CB  LEU C  83     -41.729  -2.022  -4.053  1.00 83.48           C  
ANISOU 3595  CB  LEU C  83     9504   9031  13183   -439    -86    -60       C  
ATOM   3596  CG  LEU C  83     -42.384  -3.329  -3.590  1.00 84.16           C  
ANISOU 3596  CG  LEU C  83     9568   9048  13359   -620     35   -323       C  
ATOM   3597  CD1 LEU C  83     -41.422  -4.497  -3.515  1.00 82.99           C  
ANISOU 3597  CD1 LEU C  83     9752   8910  12867   -735     76   -496       C  
ATOM   3598  CD2 LEU C  83     -43.049  -3.124  -2.242  1.00 85.19           C  
ANISOU 3598  CD2 LEU C  83     9643   8891  13834   -631    399   -388       C  
ATOM   3599  N   SER C  84     -42.586   1.166  -4.545  1.00 88.44           N  
ANISOU 3599  N   SER C  84     9558   9554  14491    -53   -230    543       N  
ATOM   3600  CA  SER C  84     -42.267   2.554  -4.852  1.00 90.41           C  
ANISOU 3600  CA  SER C  84     9708   9746  14897    127   -297    848       C  
ATOM   3601  C   SER C  84     -41.159   3.120  -3.968  1.00 88.57           C  
ANISOU 3601  C   SER C  84     9781   9269  14599    182    -35    808       C  
ATOM   3602  O   SER C  84     -40.670   4.257  -4.200  1.00 95.89           O  
ANISOU 3602  O   SER C  84    10669  10116  15646    322    -73   1048       O  
ATOM   3603  CB  SER C  84     -43.529   3.389  -4.682  1.00 93.28           C  
ANISOU 3603  CB  SER C  84     9642   9949  15850    225   -264    965       C  
ATOM   3604  OG  SER C  84     -44.317   2.880  -3.604  1.00 92.91           O  
ANISOU 3604  OG  SER C  84     9542   9698  16060    135     37    678       O  
ATOM   3605  N   MET C  85     -40.761   2.365  -2.958  1.00 82.56           N  
ANISOU 3605  N   MET C  85     9309   8386  13672     71    219    524       N  
ATOM   3606  CA  MET C  85     -39.785   2.831  -2.008  1.00 79.10           C  
ANISOU 3606  CA  MET C  85     9152   7733  13166    102    457    448       C  
ATOM   3607  C   MET C  85     -38.665   1.841  -1.933  1.00 78.13           C  
ANISOU 3607  C   MET C  85     9405   7713  12565     -1    448    327       C  
ATOM   3608  O   MET C  85     -38.871   0.635  -2.056  1.00 80.41           O  
ANISOU 3608  O   MET C  85     9758   8124  12668   -128    411    185       O  
ATOM   3609  CB  MET C  85     -40.403   2.950  -0.634  1.00 78.17           C  
ANISOU 3609  CB  MET C  85     9020   7354  13325     71    815    222       C  
ATOM   3610  CG  MET C  85     -39.489   3.538   0.444  1.00 77.55           C  
ANISOU 3610  CG  MET C  85     9211   7063  13188     96   1060    106       C  
ATOM   3611  SD  MET C  85     -38.813   5.244   0.243  1.00 77.07           S  
ANISOU 3611  SD  MET C  85     9073   6822  13389    279   1023    303       S  
ATOM   3612  CE  MET C  85     -40.240   6.060  -0.482  1.00 80.03           C  
ANISOU 3612  CE  MET C  85     8920   7151  14335    407    919    520       C  
ATOM   3613  N   ASP C  86     -37.466   2.345  -1.726  1.00 76.21           N  
ANISOU 3613  N   ASP C  86     9391   7399  12166     50    482    379       N  
ATOM   3614  CA  ASP C  86     -36.341   1.496  -1.368  1.00 72.40           C  
ANISOU 3614  CA  ASP C  86     9265   6943  11299    -37    528    250       C  
ATOM   3615  C   ASP C  86     -35.606   2.132  -0.239  1.00 71.90           C  
ANISOU 3615  C   ASP C  86     9397   6652  11266    -10    738    171       C  
ATOM   3616  O   ASP C  86     -35.841   3.291   0.128  1.00 73.78           O  
ANISOU 3616  O   ASP C  86     9505   6717  11810     82    836    210       O  
ATOM   3617  CB  ASP C  86     -35.416   1.278  -2.551  1.00 71.89           C  
ANISOU 3617  CB  ASP C  86     9286   7104  10925    -17    282    402       C  
ATOM   3618  CG  ASP C  86     -34.854   2.547  -3.069  1.00 72.85           C  
ANISOU 3618  CG  ASP C  86     9333   7205  11141    120    193    660       C  
ATOM   3619  OD1 ASP C  86     -35.576   3.219  -3.832  1.00 77.29           O  
ANISOU 3619  OD1 ASP C  86     9611   7847  11907    203     51    870       O  
ATOM   3620  OD2 ASP C  86     -33.726   2.894  -2.690  1.00 70.16           O  
ANISOU 3620  OD2 ASP C  86     9194   6756  10707    145    261    670       O  
ATOM   3621  N   LEU C  87     -34.673   1.398   0.306  1.00 69.65           N  
ANISOU 3621  N   LEU C  87     9416   6363  10682    -91    798     56       N  
ATOM   3622  CA  LEU C  87     -34.053   1.847   1.517  1.00 69.32           C  
ANISOU 3622  CA  LEU C  87     9572   6138  10628    -96    989    -61       C  
ATOM   3623  C   LEU C  87     -33.072   3.008   1.330  1.00 66.70           C  
ANISOU 3623  C   LEU C  87     9265   5718  10360      8    922     60       C  
ATOM   3624  O   LEU C  87     -32.900   3.811   2.219  1.00 67.35           O  
ANISOU 3624  O   LEU C  87     9387   5617  10585     31   1073    -42       O  
ATOM   3625  CB  LEU C  87     -33.325   0.689   2.086  1.00 70.31           C  
ANISOU 3625  CB  LEU C  87     9991   6299  10422   -209   1030   -171       C  
ATOM   3626  CG  LEU C  87     -32.949   0.980   3.516  1.00 73.02           C  
ANISOU 3626  CG  LEU C  87    10532   6495  10714   -247   1239   -320       C  
ATOM   3627  CD1 LEU C  87     -34.155   0.728   4.391  1.00 75.60           C  
ANISOU 3627  CD1 LEU C  87    10790   6769  11165   -317   1483   -469       C  
ATOM   3628  CD2 LEU C  87     -31.778   0.067   3.843  1.00 74.50           C  
ANISOU 3628  CD2 LEU C  87    11012   6727  10565   -320   1184   -329       C  
ATOM   3629  N   LYS C  88     -32.383   3.060   0.198  1.00 64.35           N  
ANISOU 3629  N   LYS C  88     8951   5552   9946     60    709    261       N  
ATOM   3630  CA  LYS C  88     -31.511   4.190  -0.130  1.00 63.28           C  
ANISOU 3630  CA  LYS C  88     8791   5330   9922    161    644    427       C  
ATOM   3631  C   LYS C  88     -32.292   5.511  -0.113  1.00 65.03           C  
ANISOU 3631  C   LYS C  88     8735   5378  10594    268    702    516       C  
ATOM   3632  O   LYS C  88     -31.916   6.485   0.526  1.00 63.61           O  
ANISOU 3632  O   LYS C  88     8558   4971  10638    311    812    463       O  
ATOM   3633  CB  LYS C  88     -30.930   3.989  -1.494  1.00 63.31           C  
ANISOU 3633  CB  LYS C  88     8766   5551   9737    197    428    662       C  
ATOM   3634  CG  LYS C  88     -29.864   4.967  -1.840  1.00 65.34           C  
ANISOU 3634  CG  LYS C  88     9025   5729  10069    280    377    853       C  
ATOM   3635  CD  LYS C  88     -29.600   4.977  -3.335  1.00 67.20           C  
ANISOU 3635  CD  LYS C  88     9159   6214  10160    334    185   1143       C  
ATOM   3636  CE  LYS C  88     -28.730   6.169  -3.665  1.00 68.97           C  
ANISOU 3636  CE  LYS C  88     9319   6319  10565    427    167   1391       C  
ATOM   3637  NZ  LYS C  88     -28.380   6.058  -5.088  1.00 71.75           N  
ANISOU 3637  NZ  LYS C  88     9610   6960  10691    463      6   1676       N  
ATOM   3638  N   LYS C  89     -33.398   5.483  -0.820  1.00 66.65           N  
ANISOU 3638  N   LYS C  89     8686   5686  10949    304    621    636       N  
ATOM   3639  CA  LYS C  89     -34.360   6.556  -0.878  1.00 69.70           C  
ANISOU 3639  CA  LYS C  89     8757   5918  11808    408    664    738       C  
ATOM   3640  C   LYS C  89     -34.838   6.876   0.528  1.00 68.83           C  
ANISOU 3640  C   LYS C  89     8667   5552  11933    381    957    437       C  
ATOM   3641  O   LYS C  89     -34.770   7.960   0.942  1.00 70.41           O  
ANISOU 3641  O   LYS C  89     8774   5513  12464    454   1068    416       O  
ATOM   3642  CB  LYS C  89     -35.498   6.112  -1.786  1.00 73.47           C  
ANISOU 3642  CB  LYS C  89     8983   6602  12327    416    504    875       C  
ATOM   3643  CG  LYS C  89     -36.192   7.195  -2.542  1.00 78.37           C  
ANISOU 3643  CG  LYS C  89     9239   7178  13358    556    386   1177       C  
ATOM   3644  CD  LYS C  89     -37.139   6.606  -3.591  1.00 82.95           C  
ANISOU 3644  CD  LYS C  89     9599   8050  13866    544    148   1330       C  
ATOM   3645  CE  LYS C  89     -38.362   7.494  -3.701  1.00 89.70           C  
ANISOU 3645  CE  LYS C  89    10044   8766  15272    656    140   1487       C  
ATOM   3646  NZ  LYS C  89     -39.231   7.114  -4.839  1.00 94.61           N  
ANISOU 3646  NZ  LYS C  89    10408   9691  15849    659   -153   1699       N  
ATOM   3647  N   TYR C  90     -35.243   5.886   1.282  1.00 70.28           N  
ANISOU 3647  N   TYR C  90     8991   5791  11920    263   1095    193       N  
ATOM   3648  CA  TYR C  90     -35.731   6.092   2.639  1.00 71.52           C  
ANISOU 3648  CA  TYR C  90     9187   5760  12225    220   1401   -100       C  
ATOM   3649  C   TYR C  90     -34.705   6.827   3.465  1.00 70.33           C  
ANISOU 3649  C   TYR C  90     9232   5435  12053    224   1509   -241       C  
ATOM   3650  O   TYR C  90     -34.978   7.859   4.063  1.00 74.94           O  
ANISOU 3650  O   TYR C  90     9697   5789  12984    279   1686   -374       O  
ATOM   3651  CB  TYR C  90     -36.064   4.758   3.313  1.00 72.22           C  
ANISOU 3651  CB  TYR C  90     9461   5972  12006     71   1524   -291       C  
ATOM   3652  CG  TYR C  90     -36.607   4.951   4.702  1.00 75.58           C  
ANISOU 3652  CG  TYR C  90     9930   6251  12533     18   1864   -576       C  
ATOM   3653  CD1 TYR C  90     -35.754   5.133   5.798  1.00 76.17           C  
ANISOU 3653  CD1 TYR C  90    10292   6259  12390    -36   2008   -775       C  
ATOM   3654  CD2 TYR C  90     -37.981   4.953   4.925  1.00 79.65           C  
ANISOU 3654  CD2 TYR C  90    10192   6715  13354     18   2046   -654       C  
ATOM   3655  CE1 TYR C  90     -36.264   5.338   7.074  1.00 79.45           C  
ANISOU 3655  CE1 TYR C  90    10757   6583  12847    -93   2335  -1055       C  
ATOM   3656  CE2 TYR C  90     -38.501   5.139   6.187  1.00 82.82           C  
ANISOU 3656  CE2 TYR C  90    10628   7001  13836    -32   2398   -926       C  
ATOM   3657  CZ  TYR C  90     -37.643   5.338   7.258  1.00 83.16           C  
ANISOU 3657  CZ  TYR C  90    10977   7004  13615    -89   2547  -1132       C  
ATOM   3658  OH  TYR C  90     -38.200   5.529   8.513  1.00 86.65           O  
ANISOU 3658  OH  TYR C  90    11458   7373  14089   -148   2914  -1422       O  
ATOM   3659  N   LEU C  91     -33.506   6.300   3.516  1.00 67.19           N  
ANISOU 3659  N   LEU C  91     9120   5136  11272    162   1404   -237       N  
ATOM   3660  CA  LEU C  91     -32.458   6.881   4.362  1.00 66.49           C  
ANISOU 3660  CA  LEU C  91     9230   4907  11123    142   1475   -394       C  
ATOM   3661  C   LEU C  91     -32.221   8.328   4.002  1.00 66.46           C  
ANISOU 3661  C   LEU C  91     9021   4680  11548    265   1448   -294       C  
ATOM   3662  O   LEU C  91     -32.040   9.132   4.886  1.00 67.57           O  
ANISOU 3662  O   LEU C  91     9185   4616  11871    262   1608   -521       O  
ATOM   3663  CB  LEU C  91     -31.141   6.119   4.228  1.00 64.96           C  
ANISOU 3663  CB  LEU C  91     9316   4854  10511     78   1310   -331       C  
ATOM   3664  CG  LEU C  91     -31.006   4.811   5.008  1.00 65.77           C  
ANISOU 3664  CG  LEU C  91     9689   5097  10201    -56   1371   -477       C  
ATOM   3665  CD1 LEU C  91     -29.958   3.934   4.327  1.00 65.72           C  
ANISOU 3665  CD1 LEU C  91     9838   5241   9890    -80   1157   -315       C  
ATOM   3666  CD2 LEU C  91     -30.608   5.009   6.462  1.00 67.00           C  
ANISOU 3666  CD2 LEU C  91    10060   5176  10218   -137   1539   -745       C  
ATOM   3667  N   ASP C  92     -32.222   8.638   2.709  1.00 65.18           N  
ANISOU 3667  N   ASP C  92     8658   4564  11540    365   1249     43       N  
ATOM   3668  CA  ASP C  92     -32.093  10.007   2.247  1.00 66.58           C  
ANISOU 3668  CA  ASP C  92     8597   4517  12182    491   1219    220       C  
ATOM   3669  C   ASP C  92     -33.154  10.941   2.774  1.00 70.36           C  
ANISOU 3669  C   ASP C  92     8815   4733  13186    560   1426     82       C  
ATOM   3670  O   ASP C  92     -32.874  12.097   3.074  1.00 72.67           O  
ANISOU 3670  O   ASP C  92     8998   4735  13875    621   1514     26       O  
ATOM   3671  CB  ASP C  92     -32.161  10.119   0.729  1.00 66.06           C  
ANISOU 3671  CB  ASP C  92     8329   4596  12174    587    978    659       C  
ATOM   3672  CG  ASP C  92     -31.780  11.518   0.243  1.00 67.63           C  
ANISOU 3672  CG  ASP C  92     8308   4553  12832    711    938    909       C  
ATOM   3673  OD1 ASP C  92     -30.736  11.991   0.685  1.00 66.90           O  
ANISOU 3673  OD1 ASP C  92     8346   4301  12770    689    979    816       O  
ATOM   3674  OD2 ASP C  92     -32.474  12.141  -0.574  1.00 69.09           O  
ANISOU 3674  OD2 ASP C  92     8184   4702  13363    826    857   1214       O  
ATOM   3675  N   SER C  93     -34.363  10.433   2.886  1.00 71.75           N  
ANISOU 3675  N   SER C  93     8873   4988  13400    547   1515     14       N  
ATOM   3676  CA  SER C  93     -35.496  11.211   3.373  1.00 75.71           C  
ANISOU 3676  CA  SER C  93     9093   5248  14423    615   1739   -126       C  
ATOM   3677  C   SER C  93     -35.469  11.563   4.880  1.00 78.07           C  
ANISOU 3677  C   SER C  93     9534   5352  14776    546   2067   -597       C  
ATOM   3678  O   SER C  93     -36.362  12.275   5.339  1.00 81.41           O  
ANISOU 3678  O   SER C  93     9720   5549  15663    604   2297   -763       O  
ATOM   3679  CB  SER C  93     -36.827  10.487   3.034  1.00 75.52           C  
ANISOU 3679  CB  SER C  93     8877   5383  14432    612   1738    -61       C  
ATOM   3680  OG  SER C  93     -37.106   9.449   3.931  1.00 72.42           O  
ANISOU 3680  OG  SER C  93     8706   5123  13686    471   1913   -353       O  
ATOM   3681  N   ILE C  94     -34.511  11.047   5.648  1.00 77.35           N  
ANISOU 3681  N   ILE C  94     9811   5362  14216    420   2094   -816       N  
ATOM   3682  CA  ILE C  94     -34.462  11.307   7.087  1.00 79.80           C  
ANISOU 3682  CA  ILE C  94    10285   5560  14475    334   2382  -1269       C  
ATOM   3683  C   ILE C  94     -33.861  12.667   7.364  1.00 81.80           C  
ANISOU 3683  C   ILE C  94    10455   5498  15125    392   2436  -1411       C  
ATOM   3684  O   ILE C  94     -32.764  12.980   6.844  1.00 79.62           O  
ANISOU 3684  O   ILE C  94    10239   5187  14827    412   2219  -1229       O  
ATOM   3685  CB  ILE C  94     -33.662  10.238   7.841  1.00 79.21           C  
ANISOU 3685  CB  ILE C  94    10626   5731  13737    174   2362  -1423       C  
ATOM   3686  CG1 ILE C  94     -34.481   8.960   7.931  1.00 79.63           C  
ANISOU 3686  CG1 ILE C  94    10743   6022  13490     97   2426  -1393       C  
ATOM   3687  CG2 ILE C  94     -33.327  10.676   9.260  1.00 82.30           C  
ANISOU 3687  CG2 ILE C  94    11210   6037  14021     82   2596  -1865       C  
ATOM   3688  CD1 ILE C  94     -33.650   7.716   8.222  1.00 77.92           C  
ANISOU 3688  CD1 ILE C  94    10886   6058  12661    -32   2308  -1367       C  
ATOM   3689  N   PRO C  95     -34.569  13.493   8.183  1.00 85.14           N  
ANISOU 3689  N   PRO C  95    10725   5675  15949    415   2744  -1752       N  
ATOM   3690  CA  PRO C  95     -34.084  14.876   8.333  1.00 87.03           C  
ANISOU 3690  CA  PRO C  95    10819   5553  16693    481   2797  -1889       C  
ATOM   3691  C   PRO C  95     -32.841  14.885   9.172  1.00 87.23           C  
ANISOU 3691  C   PRO C  95    11181   5620  16341    350   2770  -2183       C  
ATOM   3692  O   PRO C  95     -32.618  13.952   9.950  1.00 85.88           O  
ANISOU 3692  O   PRO C  95    11333   5726  15570    210   2809  -2377       O  
ATOM   3693  CB  PRO C  95     -35.225  15.593   9.040  1.00 90.87           C  
ANISOU 3693  CB  PRO C  95    11065   5789  17673    527   3161  -2230       C  
ATOM   3694  CG  PRO C  95     -36.397  14.667   8.967  1.00 91.21           C  
ANISOU 3694  CG  PRO C  95    11043   6048  17562    519   3257  -2149       C  
ATOM   3695  CD  PRO C  95     -35.837  13.288   8.903  1.00 86.57           C  
ANISOU 3695  CD  PRO C  95    10810   5858  16223    392   3065  -2013       C  
ATOM   3696  N   PRO C  96     -32.006  15.909   8.990  1.00 90.39           N  
ANISOU 3696  N   PRO C  96    11494   5751  17099    391   2683  -2184       N  
ATOM   3697  CA  PRO C  96     -30.722  15.883   9.670  1.00 90.88           C  
ANISOU 3697  CA  PRO C  96    11854   5869  16805    261   2592  -2423       C  
ATOM   3698  C   PRO C  96     -30.900  16.075  11.174  1.00 94.28           C  
ANISOU 3698  C   PRO C  96    12452   6290  17079    137   2874  -3036       C  
ATOM   3699  O   PRO C  96     -31.739  16.865  11.603  1.00 98.05           O  
ANISOU 3699  O   PRO C  96    12720   6519  18014    185   3159  -3327       O  
ATOM   3700  CB  PRO C  96     -29.936  17.045   9.007  1.00 91.69           C  
ANISOU 3700  CB  PRO C  96    11742   5630  17464    346   2453  -2250       C  
ATOM   3701  CG  PRO C  96     -30.936  17.856   8.264  1.00 93.77           C  
ANISOU 3701  CG  PRO C  96    11591   5607  18431    519   2548  -2021       C  
ATOM   3702  CD  PRO C  96     -32.287  17.234   8.403  1.00 93.82           C  
ANISOU 3702  CD  PRO C  96    11534   5769  18341    544   2721  -2054       C  
ATOM   3703  N   GLY C  97     -30.101  15.353  11.954  1.00 94.21           N  
ANISOU 3703  N   GLY C  97    12812   6559  16424    -19   2793  -3223       N  
ATOM   3704  CA  GLY C  97     -30.216  15.370  13.412  1.00 97.01           C  
ANISOU 3704  CA  GLY C  97    13382   7011  16465   -161   3035  -3780       C  
ATOM   3705  C   GLY C  97     -31.018  14.220  13.971  1.00 95.19           C  
ANISOU 3705  C   GLY C  97    13342   7122  15703   -236   3201  -3813       C  
ATOM   3706  O   GLY C  97     -30.766  13.823  15.102  1.00 96.39           O  
ANISOU 3706  O   GLY C  97    13788   7506  15330   -387   3293  -4134       O  
ATOM   3707  N   GLN C  98     -31.986  13.726  13.197  1.00 92.79           N  
ANISOU 3707  N   GLN C  98    12858   6849  15550   -139   3239  -3483       N  
ATOM   3708  CA  GLN C  98     -32.743  12.514  13.536  1.00 92.49           C  
ANISOU 3708  CA  GLN C  98    12965   7118  15056   -209   3367  -3425       C  
ATOM   3709  C   GLN C  98     -32.088  11.235  13.033  1.00 88.94           C  
ANISOU 3709  C   GLN C  98    12740   6959  14094   -258   3064  -3039       C  
ATOM   3710  O   GLN C  98     -31.260  11.255  12.112  1.00 87.93           O  
ANISOU 3710  O   GLN C  98    12582   6790  14035   -200   2757  -2734       O  
ATOM   3711  CB  GLN C  98     -34.140  12.558  12.949  1.00 93.31           C  
ANISOU 3711  CB  GLN C  98    12736   7108  15606    -92   3544  -3277       C  
ATOM   3712  CG  GLN C  98     -35.040  13.566  13.618  1.00 98.14           C  
ANISOU 3712  CG  GLN C  98    13127   7467  16691    -53   3932  -3689       C  
ATOM   3713  CD  GLN C  98     -36.384  13.670  12.919  1.00 99.75           C  
ANISOU 3713  CD  GLN C  98    12943   7528  17430     82   4063  -3489       C  
ATOM   3714  OE1 GLN C  98     -36.811  12.740  12.214  1.00 96.85           O  
ANISOU 3714  OE1 GLN C  98    12537   7341  16918     99   3922  -3122       O  
ATOM   3715  NE2 GLN C  98     -37.056  14.820  13.087  1.00103.88           N  
ANISOU 3715  NE2 GLN C  98    13149   7706  18613    182   4323  -3735       N  
ATOM   3716  N   TYR C  99     -32.477  10.118  13.629  1.00 87.57           N  
ANISOU 3716  N   TYR C  99    12775   7065  13430   -365   3174  -3049       N  
ATOM   3717  CA  TYR C  99     -31.978   8.830  13.221  1.00 83.50           C  
ANISOU 3717  CA  TYR C  99    12453   6796  12477   -414   2931  -2709       C  
ATOM   3718  C   TYR C  99     -33.109   7.909  13.124  1.00 83.26           C  
ANISOU 3718  C   TYR C  99    12362   6891  12379   -429   3090  -2580       C  
ATOM   3719  O   TYR C  99     -34.191   8.180  13.582  1.00 82.96           O  
ANISOU 3719  O   TYR C  99    12188   6799  12534   -427   3405  -2778       O  
ATOM   3720  CB  TYR C  99     -30.956   8.302  14.218  1.00 83.93           C  
ANISOU 3720  CB  TYR C  99    12881   7072  11935   -562   2845  -2837       C  
ATOM   3721  CG  TYR C  99     -29.702   9.131  14.220  1.00 84.47           C  
ANISOU 3721  CG  TYR C  99    12994   7020  12077   -557   2626  -2937       C  
ATOM   3722  CD1 TYR C  99     -29.617  10.306  14.948  1.00 88.12           C  
ANISOU 3722  CD1 TYR C  99    13419   7322  12737   -579   2774  -3356       C  
ATOM   3723  CD2 TYR C  99     -28.610   8.760  13.474  1.00 82.05           C  
ANISOU 3723  CD2 TYR C  99    12745   6742  11688   -532   2284  -2633       C  
ATOM   3724  CE1 TYR C  99     -28.468  11.063  14.927  1.00 89.27           C  
ANISOU 3724  CE1 TYR C  99    13580   7336  13002   -585   2564  -3453       C  
ATOM   3725  CE2 TYR C  99     -27.450   9.520  13.447  1.00 81.54           C  
ANISOU 3725  CE2 TYR C  99    12691   6552  11736   -532   2086  -2709       C  
ATOM   3726  CZ  TYR C  99     -27.389  10.648  14.175  1.00 85.53           C  
ANISOU 3726  CZ  TYR C  99    13156   6897  12441   -563   2218  -3111       C  
ATOM   3727  OH  TYR C  99     -26.237  11.386  14.150  1.00 89.40           O  
ANISOU 3727  OH  TYR C  99    13638   7247  13081   -576   2016  -3195       O  
ATOM   3728  N   MET C 100     -32.812   6.783  12.509  1.00 85.47           N  
ANISOU 3728  N   MET C 100    12737   7332  12405   -449   2871  -2253       N  
ATOM   3729  CA  MET C 100     -33.787   5.714  12.332  1.00 88.08           C  
ANISOU 3729  CA  MET C 100    13018   7787  12661   -484   2976  -2099       C  
ATOM   3730  C   MET C 100     -34.022   5.073  13.684  1.00 89.01           C  
ANISOU 3730  C   MET C 100    13387   8089  12343   -634   3236  -2286       C  
ATOM   3731  O   MET C 100     -33.074   4.715  14.378  1.00 87.29           O  
ANISOU 3731  O   MET C 100    13470   8017  11679   -729   3144  -2318       O  
ATOM   3732  CB  MET C 100     -33.267   4.677  11.327  1.00 86.54           C  
ANISOU 3732  CB  MET C 100    12870   7700  12311   -476   2664  -1742       C  
ATOM   3733  CG  MET C 100     -34.320   3.695  10.870  1.00 88.36           C  
ANISOU 3733  CG  MET C 100    12969   8005  12598   -496   2729  -1584       C  
ATOM   3734  SD  MET C 100     -33.666   2.403   9.802  1.00 86.97           S  
ANISOU 3734  SD  MET C 100    12873   7956  12214   -511   2394  -1252       S  
ATOM   3735  CE  MET C 100     -33.611   3.301   8.269  1.00 84.96           C  
ANISOU 3735  CE  MET C 100    12321   7591  12368   -346   2149  -1082       C  
ATOM   3736  N   ASP C 101     -35.290   4.956  14.045  1.00 92.15           N  
ANISOU 3736  N   ASP C 101    13644   8484  12883   -656   3559  -2390       N  
ATOM   3737  CA  ASP C 101     -35.673   4.452  15.358  1.00 96.36           C  
ANISOU 3737  CA  ASP C 101    14386   9198  13028   -799   3877  -2569       C  
ATOM   3738  C   ASP C 101     -35.048   3.060  15.563  1.00 95.86           C  
ANISOU 3738  C   ASP C 101    14611   9357  12455   -912   3717  -2306       C  
ATOM   3739  O   ASP C 101     -35.305   2.148  14.773  1.00 95.26           O  
ANISOU 3739  O   ASP C 101    14447   9284  12464   -902   3588  -2023       O  
ATOM   3740  CB  ASP C 101     -37.194   4.402  15.460  1.00 99.18           C  
ANISOU 3740  CB  ASP C 101    14487   9500  13697   -793   4237  -2644       C  
ATOM   3741  CG  ASP C 101     -37.659   3.949  16.811  1.00104.42           C  
ANISOU 3741  CG  ASP C 101    15346  10356  13972   -941   4620  -2825       C  
ATOM   3742  OD1 ASP C 101     -37.793   4.786  17.729  1.00108.77           O  
ANISOU 3742  OD1 ASP C 101    15943  10908  14474   -967   4900  -3194       O  
ATOM   3743  OD2 ASP C 101     -37.881   2.735  16.942  1.00106.84           O  
ANISOU 3743  OD2 ASP C 101    15757  10814  14022  -1037   4648  -2595       O  
ATOM   3744  N   SER C 102     -34.232   2.898  16.606  1.00 94.97           N  
ANISOU 3744  N   SER C 102    14824   9423  11836  -1021   3713  -2401       N  
ATOM   3745  CA  SER C 102     -33.342   1.726  16.718  1.00 91.07           C  
ANISOU 3745  CA  SER C 102    14592   9099  10910  -1102   3474  -2115       C  
ATOM   3746  C   SER C 102     -34.054   0.373  16.712  1.00 91.33           C  
ANISOU 3746  C   SER C 102    14628   9216  10855  -1177   3596  -1854       C  
ATOM   3747  O   SER C 102     -33.435  -0.657  16.442  1.00 90.04           O  
ANISOU 3747  O   SER C 102    14588   9107  10514  -1209   3373  -1568       O  
ATOM   3748  CB  SER C 102     -32.520   1.813  17.989  1.00 91.24           C  
ANISOU 3748  CB  SER C 102    14942   9330  10392  -1217   3480  -2263       C  
ATOM   3749  OG  SER C 102     -33.357   1.577  19.077  1.00 94.47           O  
ANISOU 3749  OG  SER C 102    15446   9907  10538  -1330   3864  -2397       O  
ATOM   3750  N   SER C 103     -35.331   0.374  17.075  1.00 92.69           N  
ANISOU 3750  N   SER C 103    14659   9386  11173  -1211   3967  -1964       N  
ATOM   3751  CA  SER C 103     -36.157  -0.815  17.016  1.00 91.96           C  
ANISOU 3751  CA  SER C 103    14505   9328  11106  -1284   4117  -1738       C  
ATOM   3752  C   SER C 103     -36.619  -1.069  15.587  1.00 88.61           C  
ANISOU 3752  C   SER C 103    13773   8722  11171  -1186   3933  -1578       C  
ATOM   3753  O   SER C 103     -36.947  -2.204  15.246  1.00 88.24           O  
ANISOU 3753  O   SER C 103    13685   8677  11161  -1242   3908  -1351       O  
ATOM   3754  CB  SER C 103     -37.360  -0.671  17.933  1.00 95.16           C  
ANISOU 3754  CB  SER C 103    14845   9796  11513  -1360   4605  -1925       C  
ATOM   3755  OG  SER C 103     -38.279   0.215  17.331  1.00 94.95           O  
ANISOU 3755  OG  SER C 103    14468   9576  12032  -1250   4733  -2113       O  
ATOM   3756  N   LEU C 104     -36.708  -0.021  14.767  1.00 86.14           N  
ANISOU 3756  N   LEU C 104    13229   8255  11244  -1049   3817  -1697       N  
ATOM   3757  CA  LEU C 104     -36.981  -0.198  13.321  1.00 84.12           C  
ANISOU 3757  CA  LEU C 104    12702   7877  11382   -952   3570  -1524       C  
ATOM   3758  C   LEU C 104     -35.777  -0.732  12.520  1.00 79.98           C  
ANISOU 3758  C   LEU C 104    12310   7375  10702   -925   3167  -1308       C  
ATOM   3759  O   LEU C 104     -35.944  -1.505  11.559  1.00 78.75           O  
ANISOU 3759  O   LEU C 104    12034   7202  10685   -916   2996  -1129       O  
ATOM   3760  CB  LEU C 104     -37.425   1.117  12.693  1.00 84.99           C  
ANISOU 3760  CB  LEU C 104    12516   7825  11949   -809   3562  -1663       C  
ATOM   3761  CG  LEU C 104     -37.764   1.128  11.199  1.00 83.79           C  
ANISOU 3761  CG  LEU C 104    12063   7586  12186   -702   3300  -1481       C  
ATOM   3762  CD1 LEU C 104     -38.841   0.117  10.837  1.00 83.81           C  
ANISOU 3762  CD1 LEU C 104    11879   7616  12349   -765   3374  -1370       C  
ATOM   3763  CD2 LEU C 104     -38.221   2.537  10.848  1.00 87.10           C  
ANISOU 3763  CD2 LEU C 104    12200   7838  13053   -562   3343  -1602       C  
ATOM   3764  N   VAL C 105     -34.595  -0.275  12.908  1.00 77.87           N  
ANISOU 3764  N   VAL C 105    12268   7144  10173   -913   3026  -1355       N  
ATOM   3765  CA  VAL C 105     -33.346  -0.838  12.458  1.00 74.67           C  
ANISOU 3765  CA  VAL C 105    12030   6777   9564   -907   2701  -1167       C  
ATOM   3766  C   VAL C 105     -33.352  -2.342  12.669  1.00 74.89           C  
ANISOU 3766  C   VAL C 105    12187   6883   9383  -1014   2707   -965       C  
ATOM   3767  O   VAL C 105     -33.214  -3.137  11.701  1.00 75.19           O  
ANISOU 3767  O   VAL C 105    12146   6883   9537   -996   2518   -794       O  
ATOM   3768  CB  VAL C 105     -32.173  -0.259  13.266  1.00 75.41           C  
ANISOU 3768  CB  VAL C 105    12373   6927   9351   -924   2616  -1271       C  
ATOM   3769  CG1 VAL C 105     -30.884  -1.030  13.000  1.00 73.76           C  
ANISOU 3769  CG1 VAL C 105    12345   6766   8913   -935   2311  -1056       C  
ATOM   3770  CG2 VAL C 105     -31.997   1.205  12.940  1.00 75.22           C  
ANISOU 3770  CG2 VAL C 105    12207   6775   9595   -816   2572  -1456       C  
ATOM   3771  N   LYS C 106     -33.577  -2.727  13.932  1.00 76.18           N  
ANISOU 3771  N   LYS C 106    12534   7155   9253  -1132   2948   -990       N  
ATOM   3772  CA  LYS C 106     -33.635  -4.133  14.365  1.00 74.94           C  
ANISOU 3772  CA  LYS C 106    12510   7062   8900  -1248   3008   -767       C  
ATOM   3773  C   LYS C 106     -34.675  -4.925  13.586  1.00 73.18           C  
ANISOU 3773  C   LYS C 106    12042   6740   9022  -1266   3080   -675       C  
ATOM   3774  O   LYS C 106     -34.371  -5.966  13.044  1.00 72.66           O  
ANISOU 3774  O   LYS C 106    11981   6627   9000  -1289   2921   -490       O  
ATOM   3775  CB  LYS C 106     -33.927  -4.183  15.876  1.00 79.79           C  
ANISOU 3775  CB  LYS C 106    13326   7835   9153  -1370   3315   -820       C  
ATOM   3776  CG  LYS C 106     -33.900  -5.554  16.554  1.00 80.80           C  
ANISOU 3776  CG  LYS C 106    13624   8047   9027  -1500   3400   -541       C  
ATOM   3777  CD  LYS C 106     -34.120  -5.440  18.040  1.00 84.28           C  
ANISOU 3777  CD  LYS C 106    14280   8699   9042  -1616   3697   -590       C  
ATOM   3778  CE  LYS C 106     -32.984  -4.721  18.758  1.00 85.18           C  
ANISOU 3778  CE  LYS C 106    14651   8975   8736  -1614   3532   -704       C  
ATOM   3779  NZ  LYS C 106     -33.084  -4.925  20.244  1.00 91.10           N  
ANISOU 3779  NZ  LYS C 106    15658   9994   8960  -1756   3781   -680       N  
ATOM   3780  N   SER C 107     -35.900  -4.422  13.518  1.00 73.78           N  
ANISOU 3780  N   SER C 107    11883   6773   9375  -1254   3314   -824       N  
ATOM   3781  CA  SER C 107     -36.904  -4.979  12.616  1.00 73.96           C  
ANISOU 3781  CA  SER C 107    11614   6699   9786  -1258   3326   -774       C  
ATOM   3782  C   SER C 107     -36.357  -5.226  11.205  1.00 72.95           C  
ANISOU 3782  C   SER C 107    11384   6513   9821  -1177   2952   -689       C  
ATOM   3783  O   SER C 107     -36.377  -6.341  10.705  1.00 72.48           O  
ANISOU 3783  O   SER C 107    11292   6416   9831  -1233   2856   -564       O  
ATOM   3784  CB  SER C 107     -38.086  -4.033  12.490  1.00 75.22           C  
ANISOU 3784  CB  SER C 107    11485   6805  10289  -1203   3529   -963       C  
ATOM   3785  OG  SER C 107     -38.897  -4.397  11.375  1.00 74.38           O  
ANISOU 3785  OG  SER C 107    11064   6618  10577  -1181   3425   -918       O  
ATOM   3786  N   TYR C 108     -35.834  -4.174  10.589  1.00 73.33           N  
ANISOU 3786  N   TYR C 108    11384   6552   9926  -1049   2757   -764       N  
ATOM   3787  CA  TYR C 108     -35.383  -4.237   9.218  1.00 73.18           C  
ANISOU 3787  CA  TYR C 108    11251   6512  10040   -966   2435   -692       C  
ATOM   3788  C   TYR C 108     -34.305  -5.264   9.033  1.00 70.00           C  
ANISOU 3788  C   TYR C 108    11049   6125   9422  -1004   2245   -551       C  
ATOM   3789  O   TYR C 108     -34.363  -6.054   8.076  1.00 68.13           O  
ANISOU 3789  O   TYR C 108    10706   5871   9309  -1015   2094   -495       O  
ATOM   3790  CB  TYR C 108     -34.915  -2.839   8.693  1.00 74.43           C  
ANISOU 3790  CB  TYR C 108    11337   6654  10285   -823   2285   -754       C  
ATOM   3791  CG  TYR C 108     -36.020  -1.914   8.209  1.00 77.72           C  
ANISOU 3791  CG  TYR C 108    11434   7018  11074   -744   2356   -834       C  
ATOM   3792  CD1 TYR C 108     -37.351  -2.351   8.111  1.00 82.00           C  
ANISOU 3792  CD1 TYR C 108    11744   7545  11867   -795   2509   -857       C  
ATOM   3793  CD2 TYR C 108     -35.723  -0.620   7.790  1.00 79.81           C  
ANISOU 3793  CD2 TYR C 108    11601   7232  11491   -615   2255   -861       C  
ATOM   3794  CE1 TYR C 108     -38.338  -1.528   7.641  1.00 87.15           C  
ANISOU 3794  CE1 TYR C 108    12074   8144  12894   -714   2546   -905       C  
ATOM   3795  CE2 TYR C 108     -36.709   0.227   7.311  1.00 83.17           C  
ANISOU 3795  CE2 TYR C 108    11709   7588  12304   -528   2300   -891       C  
ATOM   3796  CZ  TYR C 108     -38.014  -0.231   7.245  1.00 87.97           C  
ANISOU 3796  CZ  TYR C 108    12087   8193  13143   -574   2439   -912       C  
ATOM   3797  OH  TYR C 108     -39.064   0.548   6.787  1.00 92.49           O  
ANISOU 3797  OH  TYR C 108    12307   8692  14141   -488   2477   -923       O  
ATOM   3798  N   LEU C 109     -33.325  -5.258   9.924  1.00 68.85           N  
ANISOU 3798  N   LEU C 109    11176   6012   8972  -1027   2243   -508       N  
ATOM   3799  CA  LEU C 109     -32.222  -6.208   9.776  1.00 69.15           C  
ANISOU 3799  CA  LEU C 109    11384   6042   8847  -1049   2054   -355       C  
ATOM   3800  C   LEU C 109     -32.695  -7.698   9.781  1.00 70.79           C  
ANISOU 3800  C   LEU C 109    11569   6189   9136  -1159   2132   -238       C  
ATOM   3801  O   LEU C 109     -32.265  -8.508   8.991  1.00 67.81           O  
ANISOU 3801  O   LEU C 109    11160   5753   8848  -1155   1966   -176       O  
ATOM   3802  CB  LEU C 109     -31.203  -5.969  10.886  1.00 69.36           C  
ANISOU 3802  CB  LEU C 109    11687   6127   8537  -1068   2042   -312       C  
ATOM   3803  CG  LEU C 109     -29.931  -6.826  10.834  1.00 68.44           C  
ANISOU 3803  CG  LEU C 109    11736   5991   8275  -1074   1829   -134       C  
ATOM   3804  CD1 LEU C 109     -29.112  -6.532   9.583  1.00 65.64           C  
ANISOU 3804  CD1 LEU C 109    11292   5596   8050   -962   1567   -145       C  
ATOM   3805  CD2 LEU C 109     -29.056  -6.585  12.055  1.00 69.19           C  
ANISOU 3805  CD2 LEU C 109    12085   6174   8026  -1109   1809    -82       C  
ATOM   3806  N   TYR C 110     -33.606  -7.998  10.689  1.00 74.00           N  
ANISOU 3806  N   TYR C 110    11978   6602   9537  -1259   2410   -227       N  
ATOM   3807  CA  TYR C 110     -34.140  -9.320  10.843  1.00 76.94           C  
ANISOU 3807  CA  TYR C 110    12314   6892  10026  -1375   2531   -103       C  
ATOM   3808  C   TYR C 110     -34.829  -9.760   9.577  1.00 76.85           C  
ANISOU 3808  C   TYR C 110    12027   6799  10374  -1373   2437   -185       C  
ATOM   3809  O   TYR C 110     -34.647 -10.912   9.111  1.00 78.47           O  
ANISOU 3809  O   TYR C 110    12205   6902  10708  -1427   2352   -114       O  
ATOM   3810  CB  TYR C 110     -35.135  -9.300  11.978  1.00 81.58           C  
ANISOU 3810  CB  TYR C 110    12909   7520  10564  -1475   2885    -96       C  
ATOM   3811  CG  TYR C 110     -35.609 -10.641  12.473  1.00 83.88           C  
ANISOU 3811  CG  TYR C 110    13208   7730  10933  -1615   3067     91       C  
ATOM   3812  CD1 TYR C 110     -34.809 -11.412  13.302  1.00 86.28           C  
ANISOU 3812  CD1 TYR C 110    13760   8040  10980  -1677   3067    336       C  
ATOM   3813  CD2 TYR C 110     -36.899 -11.084  12.198  1.00 86.09           C  
ANISOU 3813  CD2 TYR C 110    13229   7921  11557  -1692   3253     44       C  
ATOM   3814  CE1 TYR C 110     -35.260 -12.626  13.802  1.00 90.21           C  
ANISOU 3814  CE1 TYR C 110    14254   8442  11579  -1807   3254    555       C  
ATOM   3815  CE2 TYR C 110     -37.374 -12.282  12.704  1.00 90.24           C  
ANISOU 3815  CE2 TYR C 110    13742   8347  12197  -1832   3452    229       C  
ATOM   3816  CZ  TYR C 110     -36.547 -13.057  13.504  1.00 92.29           C  
ANISOU 3816  CZ  TYR C 110    14258   8599  12209  -1888   3459    497       C  
ATOM   3817  OH  TYR C 110     -37.007 -14.265  13.994  1.00 98.31           O  
ANISOU 3817  OH  TYR C 110    14994   9235  13123  -2026   3661    726       O  
ATOM   3818  N   GLN C 111     -35.613  -8.843   9.019  1.00 74.80           N  
ANISOU 3818  N   GLN C 111    11549   6581  10288  -1311   2443   -341       N  
ATOM   3819  CA  GLN C 111     -36.339  -9.124   7.783  1.00 74.39           C  
ANISOU 3819  CA  GLN C 111    11213   6502  10549  -1309   2319   -430       C  
ATOM   3820  C   GLN C 111     -35.382  -9.364   6.632  1.00 72.10           C  
ANISOU 3820  C   GLN C 111    10945   6231  10218  -1242   2003   -436       C  
ATOM   3821  O   GLN C 111     -35.560 -10.339   5.871  1.00 73.22           O  
ANISOU 3821  O   GLN C 111    10975   6322  10523  -1301   1908   -473       O  
ATOM   3822  CB  GLN C 111     -37.266  -7.984   7.433  1.00 75.04           C  
ANISOU 3822  CB  GLN C 111    11054   6639  10819  -1236   2353   -551       C  
ATOM   3823  CG  GLN C 111     -38.369  -7.807   8.436  1.00 77.84           C  
ANISOU 3823  CG  GLN C 111    11323   6963  11286  -1305   2698   -585       C  
ATOM   3824  CD  GLN C 111     -39.163  -6.546   8.230  1.00 78.45           C  
ANISOU 3824  CD  GLN C 111    11167   7065  11573  -1211   2754   -702       C  
ATOM   3825  OE1 GLN C 111     -39.128  -5.625   9.063  1.00 82.55           O  
ANISOU 3825  OE1 GLN C 111    11772   7598  11995  -1167   2936   -763       O  
ATOM   3826  NE2 GLN C 111     -39.937  -6.517   7.172  1.00 77.94           N  
ANISOU 3826  NE2 GLN C 111    10793   7003  11818  -1187   2609   -744       N  
ATOM   3827  N   ILE C 112     -34.346  -8.529   6.547  1.00 67.73           N  
ANISOU 3827  N   ILE C 112    10534   5742   9456  -1131   1862   -414       N  
ATOM   3828  CA  ILE C 112     -33.261  -8.727   5.572  1.00 66.26           C  
ANISOU 3828  CA  ILE C 112    10399   5581   9192  -1065   1600   -401       C  
ATOM   3829  C   ILE C 112     -32.526 -10.093   5.765  1.00 66.69           C  
ANISOU 3829  C   ILE C 112    10601   5528   9210  -1138   1581   -319       C  
ATOM   3830  O   ILE C 112     -32.287 -10.833   4.796  1.00 64.09           O  
ANISOU 3830  O   ILE C 112    10197   5173   8981  -1146   1444   -379       O  
ATOM   3831  CB  ILE C 112     -32.250  -7.577   5.666  1.00 64.70           C  
ANISOU 3831  CB  ILE C 112    10332   5444   8804   -946   1496   -367       C  
ATOM   3832  CG1 ILE C 112     -32.896  -6.289   5.147  1.00 67.09           C  
ANISOU 3832  CG1 ILE C 112    10442   5819   9231   -857   1470   -433       C  
ATOM   3833  CG2 ILE C 112     -30.983  -7.829   4.868  1.00 62.31           C  
ANISOU 3833  CG2 ILE C 112    10110   5158   8404   -885   1275   -327       C  
ATOM   3834  CD1 ILE C 112     -32.291  -5.020   5.738  1.00 67.13           C  
ANISOU 3834  CD1 ILE C 112    10553   5824   9127   -773   1488   -426       C  
ATOM   3835  N   LEU C 113     -32.173 -10.408   7.011  1.00 67.28           N  
ANISOU 3835  N   LEU C 113    10876   5544   9144  -1189   1718   -184       N  
ATOM   3836  CA  LEU C 113     -31.603 -11.710   7.313  1.00 69.07           C  
ANISOU 3836  CA  LEU C 113    11212   5637   9392  -1258   1720    -55       C  
ATOM   3837  C   LEU C 113     -32.508 -12.878   6.910  1.00 71.64           C  
ANISOU 3837  C   LEU C 113    11361   5835  10024  -1370   1804   -103       C  
ATOM   3838  O   LEU C 113     -32.031 -13.876   6.344  1.00 71.66           O  
ANISOU 3838  O   LEU C 113    11343   5715  10170  -1391   1710   -113       O  
ATOM   3839  CB  LEU C 113     -31.242 -11.836   8.783  1.00 69.30           C  
ANISOU 3839  CB  LEU C 113    11467   5658   9203  -1307   1856    141       C  
ATOM   3840  CG  LEU C 113     -29.928 -11.117   9.097  1.00 66.22           C  
ANISOU 3840  CG  LEU C 113    11271   5348   8541  -1214   1694    201       C  
ATOM   3841  CD1 LEU C 113     -29.783 -11.018  10.599  1.00 68.43           C  
ANISOU 3841  CD1 LEU C 113    11762   5692   8544  -1273   1826    354       C  
ATOM   3842  CD2 LEU C 113     -28.700 -11.803   8.513  1.00 64.20           C  
ANISOU 3842  CD2 LEU C 113    11060   4998   8335  -1164   1486    277       C  
ATOM   3843  N   GLN C 114     -33.797 -12.743   7.166  1.00 72.07           N  
ANISOU 3843  N   GLN C 114    11266   5902  10214  -1440   1983   -157       N  
ATOM   3844  CA  GLN C 114     -34.697 -13.802   6.788  1.00 75.25           C  
ANISOU 3844  CA  GLN C 114    11471   6174  10946  -1559   2058   -220       C  
ATOM   3845  C   GLN C 114     -34.721 -14.096   5.300  1.00 74.17           C  
ANISOU 3845  C   GLN C 114    11149   6048  10984  -1541   1836   -432       C  
ATOM   3846  O   GLN C 114     -34.694 -15.272   4.879  1.00 77.76           O  
ANISOU 3846  O   GLN C 114    11533   6348  11662  -1622   1811   -489       O  
ATOM   3847  CB  GLN C 114     -36.088 -13.529   7.299  1.00 79.07           C  
ANISOU 3847  CB  GLN C 114    11795   6675  11571  -1635   2293   -245       C  
ATOM   3848  CG  GLN C 114     -36.222 -13.971   8.745  1.00 83.76           C  
ANISOU 3848  CG  GLN C 114    12545   7200  12079  -1727   2576    -24       C  
ATOM   3849  CD  GLN C 114     -37.642 -13.853   9.203  1.00 88.08           C  
ANISOU 3849  CD  GLN C 114    12904   7745  12816  -1818   2852    -58       C  
ATOM   3850  OE1 GLN C 114     -38.117 -12.740   9.472  1.00 90.24           O  
ANISOU 3850  OE1 GLN C 114    13137   8150  12997  -1761   2946   -141       O  
ATOM   3851  NE2 GLN C 114     -38.342 -14.995   9.303  1.00 90.86           N  
ANISOU 3851  NE2 GLN C 114    13115   7924  13480  -1960   3002      0       N  
ATOM   3852  N   GLY C 115     -34.732 -13.034   4.507  1.00 71.73           N  
ANISOU 3852  N   GLY C 115    10762   5922  10569  -1436   1675   -548       N  
ATOM   3853  CA  GLY C 115     -34.768 -13.167   3.057  1.00 69.09           C  
ANISOU 3853  CA  GLY C 115    10260   5674  10314  -1416   1451   -742       C  
ATOM   3854  C   GLY C 115     -33.517 -13.811   2.542  1.00 66.79           C  
ANISOU 3854  C   GLY C 115    10101   5333   9942  -1384   1318   -765       C  
ATOM   3855  O   GLY C 115     -33.582 -14.564   1.578  1.00 66.91           O  
ANISOU 3855  O   GLY C 115     9996   5334  10093  -1433   1214   -951       O  
ATOM   3856  N   ILE C 116     -32.379 -13.522   3.187  1.00 65.03           N  
ANISOU 3856  N   ILE C 116    10112   5083   9511  -1305   1324   -598       N  
ATOM   3857  CA  ILE C 116     -31.109 -14.030   2.706  1.00 64.30           C  
ANISOU 3857  CA  ILE C 116    10126   4939   9365  -1254   1203   -607       C  
ATOM   3858  C   ILE C 116     -30.911 -15.480   3.101  1.00 65.01           C  
ANISOU 3858  C   ILE C 116    10243   4771   9686  -1350   1297   -567       C  
ATOM   3859  O   ILE C 116     -30.462 -16.320   2.263  1.00 65.01           O  
ANISOU 3859  O   ILE C 116    10184   4683   9832  -1363   1221   -721       O  
ATOM   3860  CB  ILE C 116     -29.896 -13.166   3.128  1.00 64.59           C  
ANISOU 3860  CB  ILE C 116    10363   5041   9138  -1131   1137   -451       C  
ATOM   3861  CG1 ILE C 116     -28.712 -13.408   2.168  1.00 64.69           C  
ANISOU 3861  CG1 ILE C 116    10400   5068   9111  -1055    985   -523       C  
ATOM   3862  CG2 ILE C 116     -29.428 -13.415   4.565  1.00 64.83           C  
ANISOU 3862  CG2 ILE C 116    10589   4944   9098  -1155   1252   -218       C  
ATOM   3863  CD1 ILE C 116     -28.914 -12.898   0.738  1.00 64.01           C  
ANISOU 3863  CD1 ILE C 116    10166   5193   8961  -1009    848   -713       C  
ATOM   3864  N   VAL C 117     -31.277 -15.776   4.351  1.00 63.84           N  
ANISOU 3864  N   VAL C 117    10172   4500   9583  -1420   1476   -365       N  
ATOM   3865  CA  VAL C 117     -31.291 -17.149   4.834  1.00 64.23           C  
ANISOU 3865  CA  VAL C 117    10219   4281   9904  -1524   1594   -265       C  
ATOM   3866  C   VAL C 117     -32.160 -18.019   3.916  1.00 65.10           C  
ANISOU 3866  C   VAL C 117    10084   4284  10365  -1633   1600   -524       C  
ATOM   3867  O   VAL C 117     -31.717 -19.072   3.549  1.00 64.60           O  
ANISOU 3867  O   VAL C 117     9984   4017  10543  -1668   1582   -593       O  
ATOM   3868  CB  VAL C 117     -31.748 -17.254   6.296  1.00 65.49           C  
ANISOU 3868  CB  VAL C 117    10482   4377  10025  -1598   1809     13       C  
ATOM   3869  CG1 VAL C 117     -32.142 -18.681   6.634  1.00 67.98           C  
ANISOU 3869  CG1 VAL C 117    10716   4405  10708  -1731   1958    114       C  
ATOM   3870  CG2 VAL C 117     -30.634 -16.776   7.211  1.00 64.49           C  
ANISOU 3870  CG2 VAL C 117    10611   4313   9578  -1513   1768    262       C  
ATOM   3871  N   PHE C 118     -33.333 -17.534   3.512  1.00 65.02           N  
ANISOU 3871  N   PHE C 118     9895   4412  10394  -1679   1607   -683       N  
ATOM   3872  CA  PHE C 118     -34.143 -18.242   2.542  1.00 67.37           C  
ANISOU 3872  CA  PHE C 118     9943   4659  10994  -1785   1559   -969       C  
ATOM   3873  C   PHE C 118     -33.425 -18.498   1.221  1.00 69.18           C  
ANISOU 3873  C   PHE C 118    10136   4954  11193  -1739   1354  -1238       C  
ATOM   3874  O   PHE C 118     -33.446 -19.601   0.671  1.00 71.86           O  
ANISOU 3874  O   PHE C 118    10364   5119  11820  -1829   1346  -1445       O  
ATOM   3875  CB  PHE C 118     -35.436 -17.507   2.243  1.00 66.90           C  
ANISOU 3875  CB  PHE C 118     9681   4786  10951  -1819   1547  -1084       C  
ATOM   3876  CG  PHE C 118     -36.237 -18.147   1.143  1.00 68.76           C  
ANISOU 3876  CG  PHE C 118     9644   5021  11460  -1930   1436  -1405       C  
ATOM   3877  CD1 PHE C 118     -36.002 -17.827  -0.187  1.00 67.85           C  
ANISOU 3877  CD1 PHE C 118     9455   5134  11188  -1878   1187  -1656       C  
ATOM   3878  CD2 PHE C 118     -37.217 -19.130   1.446  1.00 71.41           C  
ANISOU 3878  CD2 PHE C 118     9788   5127  12214  -2101   1585  -1458       C  
ATOM   3879  CE1 PHE C 118     -36.761 -18.444  -1.184  1.00 70.93           C  
ANISOU 3879  CE1 PHE C 118     9594   5557  11797  -1998   1065  -1980       C  
ATOM   3880  CE2 PHE C 118     -37.973 -19.723   0.469  1.00 73.24           C  
ANISOU 3880  CE2 PHE C 118     9753   5355  12718  -2220   1468  -1783       C  
ATOM   3881  CZ  PHE C 118     -37.743 -19.395  -0.856  1.00 73.31           C  
ANISOU 3881  CZ  PHE C 118     9699   5621  12534  -2172   1195  -2061       C  
ATOM   3882  N   CYS C 119     -32.785 -17.460   0.714  1.00 70.07           N  
ANISOU 3882  N   CYS C 119    10339   5319  10965  -1602   1205  -1244       N  
ATOM   3883  CA  CYS C 119     -32.060 -17.548  -0.538  1.00 71.13           C  
ANISOU 3883  CA  CYS C 119    10456   5575  10994  -1548   1034  -1476       C  
ATOM   3884  C   CYS C 119     -30.927 -18.521  -0.452  1.00 70.00           C  
ANISOU 3884  C   CYS C 119    10418   5191  10986  -1534   1078  -1473       C  
ATOM   3885  O   CYS C 119     -30.629 -19.202  -1.418  1.00 69.75           O  
ANISOU 3885  O   CYS C 119    10306   5135  11059  -1562   1017  -1754       O  
ATOM   3886  CB  CYS C 119     -31.492 -16.170  -0.920  1.00 71.36           C  
ANISOU 3886  CB  CYS C 119    10577   5898  10638  -1396    902  -1392       C  
ATOM   3887  SG  CYS C 119     -32.764 -15.017  -1.518  1.00 77.31           S  
ANISOU 3887  SG  CYS C 119    11136   6963  11273  -1389    785  -1452       S  
ATOM   3888  N   HIS C 120     -30.292 -18.579   0.715  1.00 68.41           N  
ANISOU 3888  N   HIS C 120    10390   4819  10782  -1492   1182  -1161       N  
ATOM   3889  CA  HIS C 120     -29.006 -19.252   0.868  1.00 67.18           C  
ANISOU 3889  CA  HIS C 120    10345   4460  10719  -1435   1191  -1079       C  
ATOM   3890  C   HIS C 120     -28.911 -20.816   0.926  1.00 70.16           C  
ANISOU 3890  C   HIS C 120    10636   4460  11558  -1530   1294  -1149       C  
ATOM   3891  O   HIS C 120     -28.347 -21.400   0.007  1.00 71.22           O  
ANISOU 3891  O   HIS C 120    10704   4528  11829  -1516   1250  -1411       O  
ATOM   3892  CB  HIS C 120     -28.275 -18.687   2.082  1.00 64.12           C  
ANISOU 3892  CB  HIS C 120    10167   4058  10135  -1350   1217   -701       C  
ATOM   3893  CG  HIS C 120     -27.466 -17.464   1.815  1.00 60.85           C  
ANISOU 3893  CG  HIS C 120     9861   3891   9365  -1211   1089   -661       C  
ATOM   3894  ND1 HIS C 120     -26.578 -16.946   2.741  1.00 59.05           N  
ANISOU 3894  ND1 HIS C 120     9812   3663   8961  -1130   1068   -381       N  
ATOM   3895  CD2 HIS C 120     -27.359 -16.675   0.723  1.00 59.35           C  
ANISOU 3895  CD2 HIS C 120     9618   3953   8978  -1143    970   -849       C  
ATOM   3896  CE1 HIS C 120     -25.952 -15.902   2.224  1.00 56.23           C  
ANISOU 3896  CE1 HIS C 120     9495   3513   8357  -1021    951   -418       C  
ATOM   3897  NE2 HIS C 120     -26.405 -15.715   1.003  1.00 56.11           N  
ANISOU 3897  NE2 HIS C 120     9344   3652   8322  -1023    900   -677       N  
ATOM   3898  N   SER C 121     -29.481 -21.552   1.867  1.00 72.51           N  
ANISOU 3898  N   SER C 121    10909   4504  12135  -1633   1442   -957       N  
ATOM   3899  CA  SER C 121     -30.854 -22.168   1.894  1.00 75.23           C  
ANISOU 3899  CA  SER C 121    11063   4729  12789  -1800   1552  -1076       C  
ATOM   3900  C   SER C 121     -31.311 -22.770   0.579  1.00 77.49           C  
ANISOU 3900  C   SER C 121    11131   5001  13308  -1887   1481  -1547       C  
ATOM   3901  O   SER C 121     -31.406 -23.971   0.513  1.00 79.97           O  
ANISOU 3901  O   SER C 121    11326   4989  14068  -1986   1568  -1659       O  
ATOM   3902  CB  SER C 121     -31.946 -21.354   2.485  1.00 74.25           C  
ANISOU 3902  CB  SER C 121    10927   4792  12492  -1843   1615   -949       C  
ATOM   3903  OG  SER C 121     -33.187 -22.045   2.397  1.00 74.41           O  
ANISOU 3903  OG  SER C 121    10726   4671  12875  -2008   1717  -1089       O  
ATOM   3904  N   ARG C 122     -31.569 -21.960  -0.440  1.00 76.77           N  
ANISOU 3904  N   ARG C 122    10985   5257  12925  -1853   1321  -1813       N  
ATOM   3905  CA  ARG C 122     -31.887 -22.476  -1.752  1.00 79.24           C  
ANISOU 3905  CA  ARG C 122    11113   5629  13365  -1933   1221  -2282       C  
ATOM   3906  C   ARG C 122     -30.742 -22.524  -2.747  1.00 77.97           C  
ANISOU 3906  C   ARG C 122    11012   5569  13041  -1837   1125  -2517       C  
ATOM   3907  O   ARG C 122     -30.965 -22.627  -3.950  1.00 77.27           O  
ANISOU 3907  O   ARG C 122    10804   5673  12882  -1884   1013  -2919       O  
ATOM   3908  CB  ARG C 122     -33.170 -21.836  -2.284  1.00 83.10           C  
ANISOU 3908  CB  ARG C 122    11434   6411  13727  -2006   1109  -2449       C  
ATOM   3909  CG  ARG C 122     -34.304 -22.847  -2.188  1.00 92.47           C  
ANISOU 3909  CG  ARG C 122    12387   7350  15398  -2202   1195  -2617       C  
ATOM   3910  CD  ARG C 122     -35.701 -22.296  -2.308  1.00100.09           C  
ANISOU 3910  CD  ARG C 122    13158   8517  16353  -2287   1131  -2672       C  
ATOM   3911  NE  ARG C 122     -36.640 -23.029  -1.431  1.00107.30           N  
ANISOU 3911  NE  ARG C 122    13929   9112  17727  -2437   1329  -2554       N  
ATOM   3912  CZ  ARG C 122     -36.653 -22.900  -0.089  1.00111.13           C  
ANISOU 3912  CZ  ARG C 122    14539   9436  18247  -2413   1544  -2129       C  
ATOM   3913  NH1 ARG C 122     -35.746 -22.109   0.555  1.00114.21           N  
ANISOU 3913  NH1 ARG C 122    15201   9936  18256  -2250   1568  -1810       N  
ATOM   3914  NH2 ARG C 122     -37.554 -23.545   0.638  1.00110.30           N  
ANISOU 3914  NH2 ARG C 122    14289   9073  18545  -2558   1740  -2016       N  
ATOM   3915  N   ARG C 123     -29.516 -22.499  -2.236  1.00 78.46           N  
ANISOU 3915  N   ARG C 123    11249   5506  13056  -1712   1176  -2273       N  
ATOM   3916  CA  ARG C 123     -28.290 -22.466  -3.037  1.00 81.52           C  
ANISOU 3916  CA  ARG C 123    11700   5973  13299  -1601   1124  -2435       C  
ATOM   3917  C   ARG C 123     -28.062 -21.142  -3.821  1.00 77.19           C  
ANISOU 3917  C   ARG C 123    11218   5895  12215  -1495    972  -2474       C  
ATOM   3918  O   ARG C 123     -27.191 -21.081  -4.695  1.00 76.51           O  
ANISOU 3918  O   ARG C 123    11156   5939  11976  -1423    937  -2660       O  
ATOM   3919  CB  ARG C 123     -28.225 -23.638  -4.029  1.00 91.23           C  
ANISOU 3919  CB  ARG C 123    12771   7041  14849  -1691   1157  -2912       C  
ATOM   3920  CG  ARG C 123     -28.087 -25.057  -3.439  1.00100.53           C  
ANISOU 3920  CG  ARG C 123    13869   7684  16644  -1767   1321  -2899       C  
ATOM   3921  CD  ARG C 123     -26.933 -25.886  -4.097  1.00109.17           C  
ANISOU 3921  CD  ARG C 123    14930   8564  17984  -1712   1390  -3174       C  
ATOM   3922  NE  ARG C 123     -25.581 -25.669  -3.505  1.00115.00           N  
ANISOU 3922  NE  ARG C 123    15818   9190  18685  -1540   1423  -2820       N  
ATOM   3923  CZ  ARG C 123     -24.647 -24.737  -3.858  1.00119.55           C  
ANISOU 3923  CZ  ARG C 123    16520  10060  18843  -1391   1349  -2753       C  
ATOM   3924  NH1 ARG C 123     -24.828 -23.831  -4.841  1.00118.02           N  
ANISOU 3924  NH1 ARG C 123    16345  10325  18170  -1373   1241  -2977       N  
ATOM   3925  NH2 ARG C 123     -23.480 -24.698  -3.196  1.00119.85           N  
ANISOU 3925  NH2 ARG C 123    16655   9926  18955  -1256   1376  -2422       N  
ATOM   3926  N   VAL C 124     -28.761 -20.070  -3.464  1.00 73.63           N  
ANISOU 3926  N   VAL C 124    10795   5678  11502  -1478    904  -2269       N  
ATOM   3927  CA  VAL C 124     -28.767 -18.839  -4.258  1.00 72.39           C  
ANISOU 3927  CA  VAL C 124    10652   5943  10906  -1396    755  -2294       C  
ATOM   3928  C   VAL C 124     -28.113 -17.700  -3.511  1.00 69.50           C  
ANISOU 3928  C   VAL C 124    10458   5654  10294  -1255    749  -1914       C  
ATOM   3929  O   VAL C 124     -28.462 -17.447  -2.363  1.00 68.80           O  
ANISOU 3929  O   VAL C 124    10431   5443  10266  -1262    815  -1647       O  
ATOM   3930  CB  VAL C 124     -30.208 -18.389  -4.609  1.00 71.81           C  
ANISOU 3930  CB  VAL C 124    10420   6097  10765  -1484    654  -2392       C  
ATOM   3931  CG1 VAL C 124     -30.223 -17.091  -5.426  1.00 70.00           C  
ANISOU 3931  CG1 VAL C 124    10189   6296  10111  -1390    489  -2356       C  
ATOM   3932  CG2 VAL C 124     -30.908 -19.446  -5.410  1.00 74.11           C  
ANISOU 3932  CG2 VAL C 124    10520   6349  11287  -1640    624  -2805       C  
ATOM   3933  N   LEU C 125     -27.268 -16.950  -4.197  1.00 70.21           N  
ANISOU 3933  N   LEU C 125    10609   5974  10091  -1141    671  -1908       N  
ATOM   3934  CA  LEU C 125     -26.693 -15.673  -3.620  1.00 70.96           C  
ANISOU 3934  CA  LEU C 125    10839   6175   9948  -1012    640  -1576       C  
ATOM   3935  C   LEU C 125     -27.236 -14.368  -4.228  1.00 67.72           C  
ANISOU 3935  C   LEU C 125    10374   6113   9242   -963    517  -1527       C  
ATOM   3936  O   LEU C 125     -27.905 -14.378  -5.291  1.00 68.72           O  
ANISOU 3936  O   LEU C 125    10366   6475   9269  -1012    423  -1740       O  
ATOM   3937  CB  LEU C 125     -25.191 -15.618  -3.829  1.00 71.86           C  
ANISOU 3937  CB  LEU C 125    11052   6259   9993   -901    652  -1521       C  
ATOM   3938  CG  LEU C 125     -24.404 -16.890  -3.496  1.00 74.37           C  
ANISOU 3938  CG  LEU C 125    11392   6241  10622   -917    756  -1577       C  
ATOM   3939  CD1 LEU C 125     -22.950 -16.671  -3.801  1.00 74.61           C  
ANISOU 3939  CD1 LEU C 125    11484   6280  10585   -795    760  -1523       C  
ATOM   3940  CD2 LEU C 125     -24.548 -17.212  -2.035  1.00 75.72           C  
ANISOU 3940  CD2 LEU C 125    11642   6133  10992   -946    818  -1303       C  
ATOM   3941  N   HIS C 126     -26.975 -13.280  -3.515  1.00 65.07           N  
ANISOU 3941  N   HIS C 126    10131   5799   8791   -874    512  -1247       N  
ATOM   3942  CA  HIS C 126     -27.117 -11.939  -4.088  1.00 64.36           C  
ANISOU 3942  CA  HIS C 126     9999   5991   8461   -791    407  -1142       C  
ATOM   3943  C   HIS C 126     -25.873 -11.469  -4.781  1.00 62.67           C  
ANISOU 3943  C   HIS C 126     9845   5905   8061   -687    372  -1092       C  
ATOM   3944  O   HIS C 126     -25.880 -11.352  -6.004  1.00 60.31           O  
ANISOU 3944  O   HIS C 126     9466   5865   7583   -678    299  -1213       O  
ATOM   3945  CB  HIS C 126     -27.548 -10.920  -3.083  1.00 62.29           C  
ANISOU 3945  CB  HIS C 126     9772   5686   8208   -753    430   -910       C  
ATOM   3946  CG  HIS C 126     -28.258  -9.800  -3.729  1.00 63.21           C  
ANISOU 3946  CG  HIS C 126     9759   6049   8206   -707    326   -852       C  
ATOM   3947  ND1 HIS C 126     -27.614  -8.850  -4.495  1.00 62.70           N  
ANISOU 3947  ND1 HIS C 126     9690   6179   7953   -603    239   -738       N  
ATOM   3948  CD2 HIS C 126     -29.574  -9.529  -3.815  1.00 65.63           C  
ANISOU 3948  CD2 HIS C 126     9909   6441   8586   -752    288   -878       C  
ATOM   3949  CE1 HIS C 126     -28.503  -8.013  -4.994  1.00 64.34           C  
ANISOU 3949  CE1 HIS C 126     9748   6576   8120   -580    144   -670       C  
ATOM   3950  NE2 HIS C 126     -29.701  -8.390  -4.578  1.00 66.53           N  
ANISOU 3950  NE2 HIS C 126     9926   6789   8562   -665    166   -758       N  
ATOM   3951  N   ARG C 127     -24.819 -11.270  -3.998  1.00 63.43           N  
ANISOU 3951  N   ARG C 127    10073   5828   8199   -619    426   -919       N  
ATOM   3952  CA  ARG C 127     -23.506 -10.794  -4.455  1.00 69.44           C  
ANISOU 3952  CA  ARG C 127    10883   6654   8845   -517    416   -834       C  
ATOM   3953  C   ARG C 127     -23.421  -9.255  -4.511  1.00 69.33           C  
ANISOU 3953  C   ARG C 127    10861   6795   8687   -428    351   -609       C  
ATOM   3954  O   ARG C 127     -22.470  -8.680  -3.987  1.00 66.38           O  
ANISOU 3954  O   ARG C 127    10563   6323   8333   -359    361   -441       O  
ATOM   3955  CB  ARG C 127     -23.078 -11.297  -5.831  1.00 75.66           C  
ANISOU 3955  CB  ARG C 127    11606   7624   9516   -516    419  -1047       C  
ATOM   3956  CG  ARG C 127     -22.932 -12.794  -5.959  1.00 84.48           C  
ANISOU 3956  CG  ARG C 127    12712   8568  10819   -590    500  -1314       C  
ATOM   3957  CD  ARG C 127     -22.575 -13.237  -7.393  1.00 95.81           C  
ANISOU 3957  CD  ARG C 127    14077  10223  12101   -599    522  -1591       C  
ATOM   3958  NE  ARG C 127     -21.711 -12.265  -8.105  1.00107.30           N  
ANISOU 3958  NE  ARG C 127    15545  11917  13304   -495    517  -1452       N  
ATOM   3959  CZ  ARG C 127     -21.330 -12.351  -9.382  1.00115.65           C  
ANISOU 3959  CZ  ARG C 127    16557  13247  14134   -488    549  -1628       C  
ATOM   3960  NH1 ARG C 127     -21.700 -13.391 -10.133  1.00118.36           N  
ANISOU 3960  NH1 ARG C 127    16842  13667  14460   -580    580  -2007       N  
ATOM   3961  NH2 ARG C 127     -20.565 -11.381  -9.902  1.00118.32           N  
ANISOU 3961  NH2 ARG C 127    16905  13786  14263   -394    562  -1430       N  
ATOM   3962  N   ASP C 128     -24.359  -8.647  -5.241  1.00 69.32           N  
ANISOU 3962  N   ASP C 128    10744   7028   8563   -433    276   -611       N  
ATOM   3963  CA  ASP C 128     -24.405  -7.237  -5.405  1.00 72.30           C  
ANISOU 3963  CA  ASP C 128    11077   7533   8861   -349    217   -391       C  
ATOM   3964  C   ASP C 128     -25.400  -6.610  -4.419  1.00 70.71           C  
ANISOU 3964  C   ASP C 128    10850   7220   8795   -362    220   -300       C  
ATOM   3965  O   ASP C 128     -26.126  -5.661  -4.756  1.00 72.33           O  
ANISOU 3965  O   ASP C 128    10936   7556   8990   -324    156   -190       O  
ATOM   3966  CB  ASP C 128     -24.684  -6.833  -6.874  1.00 75.77           C  
ANISOU 3966  CB  ASP C 128    11390   8317   9080   -326    124   -384       C  
ATOM   3967  CG  ASP C 128     -24.486  -5.292  -7.122  1.00 79.53           C  
ANISOU 3967  CG  ASP C 128    11808   8898   9510   -220     73    -81       C  
ATOM   3968  OD1 ASP C 128     -23.825  -4.567  -6.297  1.00 71.05           O  
ANISOU 3968  OD1 ASP C 128    10800   7625   8571   -161    122     79       O  
ATOM   3969  OD2 ASP C 128     -25.040  -4.796  -8.157  1.00 89.21           O  
ANISOU 3969  OD2 ASP C 128    12908  10410  10578   -201    -27      0       O  
ATOM   3970  N   LEU C 129     -25.358  -7.048  -3.171  1.00 64.92           N  
ANISOU 3970  N   LEU C 129    10226   6246   8194   -404    304   -318       N  
ATOM   3971  CA  LEU C 129     -26.319  -6.532  -2.235  1.00 63.24           C  
ANISOU 3971  CA  LEU C 129     9993   5947   8089   -427    348   -271       C  
ATOM   3972  C   LEU C 129     -26.017  -5.090  -1.807  1.00 61.69           C  
ANISOU 3972  C   LEU C 129     9803   5721   7915   -338    342    -98       C  
ATOM   3973  O   LEU C 129     -24.839  -4.722  -1.581  1.00 60.92           O  
ANISOU 3973  O   LEU C 129     9800   5555   7790   -286    333    -11       O  
ATOM   3974  CB  LEU C 129     -26.388  -7.430  -1.022  1.00 64.24           C  
ANISOU 3974  CB  LEU C 129    10240   5859   8307   -508    454   -324       C  
ATOM   3975  CG  LEU C 129     -27.626  -7.208  -0.152  1.00 66.20           C  
ANISOU 3975  CG  LEU C 129    10447   6048   8657   -563    545   -331       C  
ATOM   3976  CD1 LEU C 129     -28.911  -7.406  -0.938  1.00 68.42           C  
ANISOU 3976  CD1 LEU C 129    10529   6455   9011   -609    511   -435       C  
ATOM   3977  CD2 LEU C 129     -27.617  -8.180   1.016  1.00 67.64           C  
ANISOU 3977  CD2 LEU C 129    10762   6045   8892   -652    664   -342       C  
ATOM   3978  N   LYS C 130     -27.073  -4.281  -1.644  1.00 60.49           N  
ANISOU 3978  N   LYS C 130     9533   5591   7860   -324    353    -60       N  
ATOM   3979  CA  LYS C 130     -26.956  -2.847  -1.219  1.00 56.67           C  
ANISOU 3979  CA  LYS C 130     9019   5040   7473   -243    366     71       C  
ATOM   3980  C   LYS C 130     -28.307  -2.170  -1.025  1.00 54.83           C  
ANISOU 3980  C   LYS C 130     8621   4801   7409   -235    406     74       C  
ATOM   3981  O   LYS C 130     -29.288  -2.683  -1.550  1.00 56.32           O  
ANISOU 3981  O   LYS C 130     8682   5098   7618   -277    374     16       O  
ATOM   3982  CB  LYS C 130     -26.147  -2.075  -2.242  1.00 57.56           C  
ANISOU 3982  CB  LYS C 130     9070   5263   7536   -150    268    231       C  
ATOM   3983  CG  LYS C 130     -26.777  -2.000  -3.619  1.00 60.13           C  
ANISOU 3983  CG  LYS C 130     9218   5834   7791   -124    161    296       C  
ATOM   3984  CD  LYS C 130     -25.689  -1.857  -4.664  1.00 60.46           C  
ANISOU 3984  CD  LYS C 130     9271   6026   7672    -70     98    414       C  
ATOM   3985  CE  LYS C 130     -26.300  -1.431  -5.962  1.00 64.54           C  
ANISOU 3985  CE  LYS C 130     9609   6819   8094    -31    -18    548       C  
ATOM   3986  NZ  LYS C 130     -26.311  -2.482  -7.016  1.00 67.62           N  
ANISOU 3986  NZ  LYS C 130     9999   7469   8225    -89    -81    411       N  
ATOM   3987  N   PRO C 131     -28.374  -0.983  -0.318  1.00 53.82           N  
ANISOU 3987  N   PRO C 131     8469   4541   7437   -180    473    126       N  
ATOM   3988  CA  PRO C 131     -29.672  -0.363   0.064  1.00 53.29           C  
ANISOU 3988  CA  PRO C 131     8238   4418   7590   -170    559     96       C  
ATOM   3989  C   PRO C 131     -30.666  -0.135  -1.033  1.00 55.30           C  
ANISOU 3989  C   PRO C 131     8237   4822   7952   -130    452    188       C  
ATOM   3990  O   PRO C 131     -31.843  -0.362  -0.818  1.00 57.16           O  
ANISOU 3990  O   PRO C 131     8344   5052   8322   -170    511    109       O  
ATOM   3991  CB  PRO C 131     -29.275   0.915   0.693  1.00 52.67           C  
ANISOU 3991  CB  PRO C 131     8165   4180   7665   -102    622    133       C  
ATOM   3992  CG  PRO C 131     -27.936   0.673   1.253  1.00 51.61           C  
ANISOU 3992  CG  PRO C 131     8262   3983   7363   -129    617    103       C  
ATOM   3993  CD  PRO C 131     -27.257  -0.196   0.261  1.00 51.95           C  
ANISOU 3993  CD  PRO C 131     8347   4174   7217   -135    489    175       C  
ATOM   3994  N  AGLN C 132     -30.233   0.251  -2.230  0.50 55.57           N  
ANISOU 3994  N  AGLN C 132     8186   5011   7916    -59    292    363       N  
ATOM   3995  N  BGLN C 132     -30.230   0.253  -2.223  0.50 56.16           N  
ANISOU 3995  N  BGLN C 132     8261   5084   7990    -59    293    363       N  
ATOM   3996  CA AGLN C 132     -31.202   0.368  -3.332  0.50 57.98           C  
ANISOU 3996  CA AGLN C 132     8247   5515   8265    -32    148    469       C  
ATOM   3997  CA BGLN C 132     -31.188   0.377  -3.320  0.50 58.96           C  
ANISOU 3997  CA BGLN C 132     8373   5636   8390    -32    150    469       C  
ATOM   3998  C  AGLN C 132     -31.808  -0.960  -3.788  0.50 58.04           C  
ANISOU 3998  C  AGLN C 132     8236   5690   8123   -141     84    305       C  
ATOM   3999  C  BGLN C 132     -31.801  -0.959  -3.790  0.50 58.59           C  
ANISOU 3999  C  BGLN C 132     8307   5761   8192   -140     84    306       C  
ATOM   4000  O  AGLN C 132     -32.766  -0.952  -4.554  0.50 60.47           O  
ANISOU 4000  O  AGLN C 132     8329   6166   8480   -142    -44    348       O  
ATOM   4001  O  BGLN C 132     -32.765  -0.959  -4.553  0.50 60.99           O  
ANISOU 4001  O  BGLN C 132     8395   6231   8544   -143    -44    347       O  
ATOM   4002  CB AGLN C 132     -30.682   1.189  -4.541  0.50 58.73           C  
ANISOU 4002  CB AGLN C 132     8239   5778   8297     68     -9    744       C  
ATOM   4003  CB BGLN C 132     -30.628   1.211  -4.493  0.50 60.44           C  
ANISOU 4003  CB BGLN C 132     8465   5982   8516     69     -2    743       C  
ATOM   4004  CG AGLN C 132     -29.612   0.536  -5.389  0.50 57.84           C  
ANISOU 4004  CG AGLN C 132     8265   5861   7847     46    -89    757       C  
ATOM   4005  CG BGLN C 132     -29.243   0.855  -4.955  0.50 59.56           C  
ANISOU 4005  CG BGLN C 132     8536   5958   8133     67    -30    772       C  
ATOM   4006  CD AGLN C 132     -29.044   1.550  -6.366  0.50 58.01           C  
ANISOU 4006  CD AGLN C 132     8193   6011   7835    151   -187   1070       C  
ATOM   4007  CD BGLN C 132     -28.146   1.465  -4.110  0.50 58.09           C  
ANISOU 4007  CD BGLN C 132     8497   5534   8042    103     81    795       C  
ATOM   4008  OE1AGLN C 132     -29.797   2.037  -7.159  0.50 60.96           O  
ANISOU 4008  OE1AGLN C 132     8360   6553   8246    197   -316   1256       O  
ATOM   4009  OE1BGLN C 132     -28.138   1.498  -2.852  0.50 55.46           O  
ANISOU 4009  OE1BGLN C 132     8267   4972   7833     70    211    645       O  
ATOM   4010  NE2AGLN C 132     -27.773   1.906  -6.290  0.50 56.48           N  
ANISOU 4010  NE2AGLN C 132     8124   5734   7599    188   -129   1155       N  
ATOM   4011  NE2BGLN C 132     -27.168   1.893  -4.833  0.50 58.57           N  
ANISOU 4011  NE2BGLN C 132     8568   5673   8012    159     28    977       N  
ATOM   4012  N   ASN C 133     -31.258  -2.068  -3.332  1.00 56.99           N  
ANISOU 4012  N   ASN C 133     8308   5503   7841   -231    160    127       N  
ATOM   4013  CA  ASN C 133     -31.851  -3.433  -3.585  1.00 58.85           C  
ANISOU 4013  CA  ASN C 133     8525   5821   8011   -353    136    -72       C  
ATOM   4014  C   ASN C 133     -32.857  -3.896  -2.539  1.00 59.05           C  
ANISOU 4014  C   ASN C 133     8516   5678   8242   -439    291   -205       C  
ATOM   4015  O   ASN C 133     -33.551  -4.874  -2.778  1.00 59.05           O  
ANISOU 4015  O   ASN C 133     8436   5725   8272   -541    270   -350       O  
ATOM   4016  CB  ASN C 133     -30.797  -4.526  -3.570  1.00 56.80           C  
ANISOU 4016  CB  ASN C 133     8481   5538   7561   -413    165   -195       C  
ATOM   4017  CG  ASN C 133     -29.851  -4.437  -4.714  1.00 57.93           C  
ANISOU 4017  CG  ASN C 133     8654   5878   7478   -360     42   -129       C  
ATOM   4018  OD1 ASN C 133     -30.248  -4.188  -5.867  1.00 61.34           O  
ANISOU 4018  OD1 ASN C 133     8933   6566   7806   -339   -109    -74       O  
ATOM   4019  ND2 ASN C 133     -28.583  -4.669  -4.430  1.00 56.79           N  
ANISOU 4019  ND2 ASN C 133     8698   5637   7243   -342    105   -127       N  
ATOM   4020  N   LEU C 134     -32.907  -3.196  -1.406  1.00 57.94           N  
ANISOU 4020  N   LEU C 134     8429   5346   8239   -405    457   -169       N  
ATOM   4021  CA  LEU C 134     -33.845  -3.500  -0.352  1.00 58.28           C  
ANISOU 4021  CA  LEU C 134     8440   5244   8457   -481    648   -277       C  
ATOM   4022  C   LEU C 134     -35.091  -2.637  -0.450  1.00 60.05           C  
ANISOU 4022  C   LEU C 134     8382   5470   8962   -432    663   -233       C  
ATOM   4023  O   LEU C 134     -35.072  -1.487  -0.027  1.00 62.85           O  
ANISOU 4023  O   LEU C 134     8700   5727   9453   -340    736   -158       O  
ATOM   4024  CB  LEU C 134     -33.161  -3.288   0.976  1.00 57.31           C  
ANISOU 4024  CB  LEU C 134     8551   4946   8278   -485    833   -293       C  
ATOM   4025  CG  LEU C 134     -31.805  -3.995   1.131  1.00 56.81           C  
ANISOU 4025  CG  LEU C 134     8749   4862   7974   -512    798   -291       C  
ATOM   4026  CD1 LEU C 134     -31.284  -3.778   2.538  1.00 56.63           C  
ANISOU 4026  CD1 LEU C 134     8934   4695   7886   -530    958   -304       C  
ATOM   4027  CD2 LEU C 134     -31.912  -5.491   0.898  1.00 57.80           C  
ANISOU 4027  CD2 LEU C 134     8908   5001   8049   -622    787   -384       C  
ATOM   4028  N   LEU C 135     -36.148  -3.177  -1.053  1.00 60.58           N  
ANISOU 4028  N   LEU C 135     8228   5639   9148   -491    580   -286       N  
ATOM   4029  CA  LEU C 135     -37.379  -2.468  -1.294  1.00 62.36           C  
ANISOU 4029  CA  LEU C 135     8135   5883   9673   -445    553   -229       C  
ATOM   4030  C   LEU C 135     -38.284  -2.510  -0.091  1.00 64.47           C  
ANISOU 4030  C   LEU C 135     8341   5958  10195   -499    833   -339       C  
ATOM   4031  O   LEU C 135     -38.085  -3.349   0.748  1.00 64.32           O  
ANISOU 4031  O   LEU C 135     8512   5845  10079   -601   1010   -454       O  
ATOM   4032  CB  LEU C 135     -38.084  -3.062  -2.508  1.00 63.36           C  
ANISOU 4032  CB  LEU C 135     8038   6233   9802   -497    307   -248       C  
ATOM   4033  CG  LEU C 135     -37.251  -3.187  -3.787  1.00 62.53           C  
ANISOU 4033  CG  LEU C 135     7997   6379   9380   -468     41   -175       C  
ATOM   4034  CD1 LEU C 135     -38.116  -3.477  -4.995  1.00 64.99           C  
ANISOU 4034  CD1 LEU C 135     8039   6956   9696   -508   -225   -183       C  
ATOM   4035  CD2 LEU C 135     -36.455  -1.934  -4.050  1.00 62.30           C  
ANISOU 4035  CD2 LEU C 135     8013   6368   9287   -316    -11     60       C  
ATOM   4036  N   ILE C 136     -39.235  -1.559  -0.004  1.00 67.96           N  
ANISOU 4036  N   ILE C 136     8511   6340  10970   -421    886   -283       N  
ATOM   4037  CA  ILE C 136     -40.213  -1.466   1.085  1.00 71.56           C  
ANISOU 4037  CA  ILE C 136     8856   6622  11711   -461   1186   -396       C  
ATOM   4038  C   ILE C 136     -41.636  -1.181   0.573  1.00 76.63           C  
ANISOU 4038  C   ILE C 136     9072   7288  12754   -437   1122   -361       C  
ATOM   4039  O   ILE C 136     -41.815  -0.379  -0.352  1.00 75.91           O  
ANISOU 4039  O   ILE C 136     8760   7285  12795   -322    890   -192       O  
ATOM   4040  CB  ILE C 136     -39.879  -0.332   2.065  1.00 72.67           C  
ANISOU 4040  CB  ILE C 136     9090   6584  11934   -370   1414   -409       C  
ATOM   4041  CG1 ILE C 136     -38.400  -0.353   2.395  1.00 71.56           C  
ANISOU 4041  CG1 ILE C 136     9320   6439  11428   -366   1398   -405       C  
ATOM   4042  CG2 ILE C 136     -40.711  -0.446   3.334  1.00 74.84           C  
ANISOU 4042  CG2 ILE C 136     9335   6710  12388   -440   1783   -575       C  
ATOM   4043  CD1 ILE C 136     -37.952   0.731   3.364  1.00 72.62           C  
ANISOU 4043  CD1 ILE C 136     9568   6411  11613   -297   1595   -463       C  
ATOM   4044  N   ASP C 137     -42.629  -1.862   1.163  1.00 80.79           N  
ANISOU 4044  N   ASP C 137     9472   7741  13484   -550   1321   -494       N  
ATOM   4045  CA  ASP C 137     -44.036  -1.521   0.940  1.00 87.31           C  
ANISOU 4045  CA  ASP C 137     9868   8539  14766   -528   1327   -480       C  
ATOM   4046  C   ASP C 137     -44.596  -0.624   2.039  1.00 91.66           C  
ANISOU 4046  C   ASP C 137    10317   8870  15640   -462   1688   -538       C  
ATOM   4047  O   ASP C 137     -43.980  -0.441   3.121  1.00 88.76           O  
ANISOU 4047  O   ASP C 137    10237   8386  15098   -470   1969   -635       O  
ATOM   4048  CB  ASP C 137     -44.925  -2.761   0.743  1.00 91.06           C  
ANISOU 4048  CB  ASP C 137    10173   9066  15358   -692   1304   -591       C  
ATOM   4049  CG  ASP C 137     -44.870  -3.758   1.912  1.00 92.70           C  
ANISOU 4049  CG  ASP C 137    10609   9142  15470   -845   1648   -742       C  
ATOM   4050  OD1 ASP C 137     -44.645  -3.344   3.077  1.00 94.44           O  
ANISOU 4050  OD1 ASP C 137    11006   9221  15653   -824   1979   -780       O  
ATOM   4051  OD2 ASP C 137     -45.048  -4.978   1.656  1.00 93.37           O  
ANISOU 4051  OD2 ASP C 137    10693   9267  15515   -993   1583   -822       O  
ATOM   4052  N   ASP C 138     -45.751  -0.025   1.722  1.00 98.60           N  
ANISOU 4052  N   ASP C 138    10769   9704  16991   -391   1666   -483       N  
ATOM   4053  CA  ASP C 138     -46.589   0.731   2.687  1.00104.00           C  
ANISOU 4053  CA  ASP C 138    11250  10166  18099   -337   2039   -577       C  
ATOM   4054  C   ASP C 138     -46.860  -0.039   4.010  1.00106.48           C  
ANISOU 4054  C   ASP C 138    11734  10383  18339   -488   2476   -792       C  
ATOM   4055  O   ASP C 138     -47.022   0.594   5.078  1.00113.87           O  
ANISOU 4055  O   ASP C 138    12704  11161  19399   -454   2854   -920       O  
ATOM   4056  CB  ASP C 138     -47.933   1.114   2.038  1.00107.23           C  
ANISOU 4056  CB  ASP C 138    11120  10559  19063   -274   1917   -482       C  
ATOM   4057  CG  ASP C 138     -48.657  -0.101   1.410  1.00108.66           C  
ANISOU 4057  CG  ASP C 138    11116  10896  19272   -425   1721   -501       C  
ATOM   4058  OD1 ASP C 138     -47.963  -0.940   0.763  1.00106.28           O  
ANISOU 4058  OD1 ASP C 138    11037  10783  18558   -512   1455   -487       O  
ATOM   4059  OD2 ASP C 138     -49.901  -0.223   1.576  1.00108.11           O  
ANISOU 4059  OD2 ASP C 138    10669  10747  19659   -462   1845   -551       O  
ATOM   4060  N   LYS C 139     -46.914  -1.377   3.927  1.00102.19           N  
ANISOU 4060  N   LYS C 139    11286   9935  17604   -654   2433   -829       N  
ATOM   4061  CA  LYS C 139     -47.087  -2.259   5.094  1.00 99.82           C  
ANISOU 4061  CA  LYS C 139    11166   9565  17195   -812   2817   -963       C  
ATOM   4062  C   LYS C 139     -45.850  -2.349   5.996  1.00 95.23           C  
ANISOU 4062  C   LYS C 139    11080   8982  16120   -838   2977  -1004       C  
ATOM   4063  O   LYS C 139     -45.877  -3.041   7.015  1.00 95.39           O  
ANISOU 4063  O   LYS C 139    11288   8969  15984   -964   3288  -1072       O  
ATOM   4064  CB  LYS C 139     -47.523  -3.676   4.636  1.00101.61           C  
ANISOU 4064  CB  LYS C 139    11306   9859  17441   -983   2694   -968       C  
ATOM   4065  CG  LYS C 139     -49.037  -3.927   4.494  1.00105.53           C  
ANISOU 4065  CG  LYS C 139    11328  10296  18469  -1047   2779  -1008       C  
ATOM   4066  CD  LYS C 139     -49.416  -4.539   3.140  1.00106.01           C  
ANISOU 4066  CD  LYS C 139    11129  10493  18653  -1098   2335   -971       C  
ATOM   4067  CE  LYS C 139     -49.413  -3.481   2.037  1.00106.70           C  
ANISOU 4067  CE  LYS C 139    10999  10700  18840   -922   1951   -841       C  
ATOM   4068  NZ  LYS C 139     -48.504  -3.753   0.884  1.00104.82           N  
ANISOU 4068  NZ  LYS C 139    10933  10679  18215   -910   1504   -770       N  
ATOM   4069  N   GLY C 140     -44.769  -1.662   5.649  1.00 92.37           N  
ANISOU 4069  N   GLY C 140    10919   8661  15515   -725   2767   -944       N  
ATOM   4070  CA  GLY C 140     -43.538  -1.696   6.449  1.00 91.98           C  
ANISOU 4070  CA  GLY C 140    11314   8619  15013   -746   2867   -979       C  
ATOM   4071  C   GLY C 140     -42.731  -2.999   6.337  1.00 90.66           C  
ANISOU 4071  C   GLY C 140    11437   8543  14465   -868   2730   -922       C  
ATOM   4072  O   GLY C 140     -41.964  -3.352   7.259  1.00 93.14           O  
ANISOU 4072  O   GLY C 140    12092   8856  14439   -931   2884   -942       O  
ATOM   4073  N   THR C 141     -42.907  -3.716   5.231  1.00 87.23           N  
ANISOU 4073  N   THR C 141    10858   8188  14097   -903   2442   -859       N  
ATOM   4074  CA  THR C 141     -42.175  -4.941   4.983  1.00 84.61           C  
ANISOU 4074  CA  THR C 141    10751   7910  13484  -1008   2303   -830       C  
ATOM   4075  C   THR C 141     -41.039  -4.562   4.063  1.00 81.93           C  
ANISOU 4075  C   THR C 141    10548   7676  12906   -904   1968   -754       C  
ATOM   4076  O   THR C 141     -41.243  -3.761   3.171  1.00 81.94           O  
ANISOU 4076  O   THR C 141    10341   7745  13046   -794   1760   -700       O  
ATOM   4077  CB  THR C 141     -43.068  -6.039   4.342  1.00 84.24           C  
ANISOU 4077  CB  THR C 141    10457   7878  13672  -1133   2214   -865       C  
ATOM   4078  OG1 THR C 141     -44.199  -6.281   5.186  1.00 85.12           O  
ANISOU 4078  OG1 THR C 141    10394   7880  14066  -1224   2551   -918       O  
ATOM   4079  CG2 THR C 141     -42.317  -7.325   4.174  1.00 81.82           C  
ANISOU 4079  CG2 THR C 141    10374   7576  13135  -1244   2115   -865       C  
ATOM   4080  N   ILE C 142     -39.883  -5.197   4.248  1.00 80.19           N  
ANISOU 4080  N   ILE C 142    10650   7468  12349   -943   1917   -729       N  
ATOM   4081  CA  ILE C 142     -38.672  -4.965   3.455  1.00 78.19           C  
ANISOU 4081  CA  ILE C 142    10551   7307  11850   -859   1640   -661       C  
ATOM   4082  C   ILE C 142     -38.302  -6.245   2.672  1.00 78.12           C  
ANISOU 4082  C   ILE C 142    10590   7360  11730   -947   1454   -684       C  
ATOM   4083  O   ILE C 142     -38.487  -7.342   3.174  1.00 77.45           O  
ANISOU 4083  O   ILE C 142    10570   7191  11667  -1074   1586   -728       O  
ATOM   4084  CB  ILE C 142     -37.500  -4.463   4.331  1.00 77.94           C  
ANISOU 4084  CB  ILE C 142    10838   7225  11550   -811   1731   -628       C  
ATOM   4085  CG1 ILE C 142     -36.251  -4.221   3.495  1.00 77.78           C  
ANISOU 4085  CG1 ILE C 142    10945   7285  11322   -726   1463   -549       C  
ATOM   4086  CG2 ILE C 142     -37.099  -5.440   5.405  1.00 78.63           C  
ANISOU 4086  CG2 ILE C 142    11186   7247  11442   -928   1915   -635       C  
ATOM   4087  CD1 ILE C 142     -35.403  -3.093   4.066  1.00 79.50           C  
ANISOU 4087  CD1 ILE C 142    11317   7453  11433   -630   1502   -519       C  
ATOM   4088  N   LYS C 143     -37.805  -6.112   1.444  1.00 75.37           N  
ANISOU 4088  N   LYS C 143    10201   7155  11281   -884   1165   -658       N  
ATOM   4089  CA  LYS C 143     -37.676  -7.256   0.539  1.00 74.26           C  
ANISOU 4089  CA  LYS C 143    10036   7094  11083   -970    990   -745       C  
ATOM   4090  C   LYS C 143     -36.461  -7.146  -0.331  1.00 71.22           C  
ANISOU 4090  C   LYS C 143     9796   6837  10427   -895    776   -707       C  
ATOM   4091  O   LYS C 143     -36.227  -6.091  -0.885  1.00 72.70           O  
ANISOU 4091  O   LYS C 143     9929   7140  10553   -775    647   -600       O  
ATOM   4092  CB  LYS C 143     -38.871  -7.313  -0.403  1.00 77.99           C  
ANISOU 4092  CB  LYS C 143    10164   7691  11776  -1004    831   -813       C  
ATOM   4093  CG  LYS C 143     -40.228  -7.258   0.274  1.00 82.17           C  
ANISOU 4093  CG  LYS C 143    10461   8110  12649  -1063   1026   -843       C  
ATOM   4094  CD  LYS C 143     -41.326  -7.671  -0.705  1.00 85.11           C  
ANISOU 4094  CD  LYS C 143    10489   8601  13247  -1136    829   -940       C  
ATOM   4095  CE  LYS C 143     -42.704  -7.640  -0.072  1.00 88.70           C  
ANISOU 4095  CE  LYS C 143    10667   8934  14098  -1198   1028   -969       C  
ATOM   4096  NZ  LYS C 143     -43.384  -8.944  -0.298  1.00 91.30           N  
ANISOU 4096  NZ  LYS C 143    10845   9223  14621  -1379   1012  -1133       N  
ATOM   4097  N   LEU C 144     -35.724  -8.244  -0.505  1.00 67.20           N  
ANISOU 4097  N   LEU C 144     9443   6298   9790   -965    747   -788       N  
ATOM   4098  CA  LEU C 144     -34.554  -8.250  -1.366  1.00 62.96           C  
ANISOU 4098  CA  LEU C 144     9030   5883   9009   -902    576   -778       C  
ATOM   4099  C   LEU C 144     -34.964  -8.314  -2.779  1.00 63.29           C  
ANISOU 4099  C   LEU C 144     8874   6162   9009   -909    344   -864       C  
ATOM   4100  O   LEU C 144     -35.830  -9.099  -3.139  1.00 63.64           O  
ANISOU 4100  O   LEU C 144     8753   6233   9193  -1020    300  -1024       O  
ATOM   4101  CB  LEU C 144     -33.683  -9.442  -1.155  1.00 62.82           C  
ANISOU 4101  CB  LEU C 144     9203   5742   8922   -971    628   -858       C  
ATOM   4102  CG  LEU C 144     -33.271  -9.909   0.247  1.00 63.14           C  
ANISOU 4102  CG  LEU C 144     9449   5547   8995  -1013    841   -782       C  
ATOM   4103  CD1 LEU C 144     -31.914 -10.613   0.120  1.00 62.64           C  
ANISOU 4103  CD1 LEU C 144     9578   5416   8804  -1000    801   -783       C  
ATOM   4104  CD2 LEU C 144     -33.219  -8.812   1.282  1.00 61.94           C  
ANISOU 4104  CD2 LEU C 144     9388   5353   8793   -942    963   -637       C  
ATOM   4105  N   ALA C 145     -34.341  -7.470  -3.593  1.00 63.10           N  
ANISOU 4105  N   ALA C 145     8862   6327   8787   -795    189   -750       N  
ATOM   4106  CA  ALA C 145     -34.561  -7.485  -5.034  1.00 65.77           C  
ANISOU 4106  CA  ALA C 145     9044   6961   8983   -796    -51   -803       C  
ATOM   4107  C   ALA C 145     -33.292  -7.856  -5.721  1.00 66.07           C  
ANISOU 4107  C   ALA C 145     9256   7105   8741   -774   -107   -851       C  
ATOM   4108  O   ALA C 145     -32.219  -7.714  -5.141  1.00 62.33           O  
ANISOU 4108  O   ALA C 145     8989   6486   8206   -717      8   -766       O  
ATOM   4109  CB  ALA C 145     -35.047  -6.151  -5.535  1.00 66.66           C  
ANISOU 4109  CB  ALA C 145     8974   7243   9109   -683   -187   -584       C  
ATOM   4110  N   ASP C 146     -33.433  -8.398  -6.934  1.00 70.13           N  
ANISOU 4110  N   ASP C 146     9677   7875   9094   -832   -278  -1015       N  
ATOM   4111  CA  ASP C 146     -32.294  -8.817  -7.779  1.00 72.54           C  
ANISOU 4111  CA  ASP C 146    10118   8329   9114   -821   -318  -1112       C  
ATOM   4112  C   ASP C 146     -31.376  -9.994  -7.259  1.00 70.86           C  
ANISOU 4112  C   ASP C 146    10100   7862   8962   -878   -148  -1300       C  
ATOM   4113  O   ASP C 146     -30.267 -10.196  -7.741  1.00 68.86           O  
ANISOU 4113  O   ASP C 146     9969   7666   8525   -840   -129  -1342       O  
ATOM   4114  CB  ASP C 146     -31.471  -7.574  -8.147  1.00 72.63           C  
ANISOU 4114  CB  ASP C 146    10191   8484   8920   -671   -360   -823       C  
ATOM   4115  CG  ASP C 146     -32.266  -6.582  -8.935  1.00 76.86           C  
ANISOU 4115  CG  ASP C 146    10519   9303   9381   -616   -556   -634       C  
ATOM   4116  OD1 ASP C 146     -33.304  -6.948  -9.578  1.00 81.84           O  
ANISOU 4116  OD1 ASP C 146    10958  10132  10005   -700   -720   -765       O  
ATOM   4117  OD2 ASP C 146     -31.865  -5.401  -8.941  1.00 82.29           O  
ANISOU 4117  OD2 ASP C 146    11212  10014  10039   -490   -563   -336       O  
ATOM   4118  N   PHE C 147     -31.871 -10.771  -6.306  1.00 71.28           N  
ANISOU 4118  N   PHE C 147    10156   7633   9292   -969    -20  -1394       N  
ATOM   4119  CA  PHE C 147     -31.213 -12.001  -5.865  1.00 72.28           C  
ANISOU 4119  CA  PHE C 147    10413   7506   9543  -1037    118  -1554       C  
ATOM   4120  C   PHE C 147     -31.008 -12.942  -7.068  1.00 74.34           C  
ANISOU 4120  C   PHE C 147    10620   7918   9706  -1114     34  -1882       C  
ATOM   4121  O   PHE C 147     -31.847 -13.011  -7.963  1.00 74.85           O  
ANISOU 4121  O   PHE C 147    10513   8227   9699  -1184   -120  -2052       O  
ATOM   4122  CB  PHE C 147     -32.028 -12.695  -4.791  1.00 73.24           C  
ANISOU 4122  CB  PHE C 147    10496   7341   9988  -1142    254  -1581       C  
ATOM   4123  CG  PHE C 147     -33.459 -12.872  -5.171  1.00 78.66           C  
ANISOU 4123  CG  PHE C 147    10939   8126  10820  -1248    166  -1723       C  
ATOM   4124  CD1 PHE C 147     -33.869 -13.959  -5.984  1.00 82.07           C  
ANISOU 4124  CD1 PHE C 147    11240   8602  11340  -1382     86  -2055       C  
ATOM   4125  CD2 PHE C 147     -34.424 -11.959  -4.743  1.00 80.02           C  
ANISOU 4125  CD2 PHE C 147    10985   8341  11075  -1219    160  -1554       C  
ATOM   4126  CE1 PHE C 147     -35.211 -14.134  -6.344  1.00 84.86           C  
ANISOU 4126  CE1 PHE C 147    11339   9050  11852  -1493    -21  -2200       C  
ATOM   4127  CE2 PHE C 147     -35.768 -12.128  -5.109  1.00 84.53           C  
ANISOU 4127  CE2 PHE C 147    11293   8999  11823  -1316     66  -1678       C  
ATOM   4128  CZ  PHE C 147     -36.162 -13.213  -5.916  1.00 86.58           C  
ANISOU 4128  CZ  PHE C 147    11421   9317  12159  -1456    -38  -1996       C  
ATOM   4129  N   GLY C 148     -29.828 -13.555  -7.102  1.00 74.63           N  
ANISOU 4129  N   GLY C 148    10801   7829   9723  -1090    130  -1961       N  
ATOM   4130  CA  GLY C 148     -29.368 -14.425  -8.161  1.00 79.16           C  
ANISOU 4130  CA  GLY C 148    11356   8512  10209  -1144    108  -2292       C  
ATOM   4131  C   GLY C 148     -29.296 -13.929  -9.597  1.00 83.61           C  
ANISOU 4131  C   GLY C 148    11858   9525  10382  -1122    -48  -2400       C  
ATOM   4132  O   GLY C 148     -29.000 -14.717 -10.506  1.00 88.06           O  
ANISOU 4132  O   GLY C 148    12401  10208  10848  -1187    -53  -2739       O  
ATOM   4133  N   LEU C 149     -29.501 -12.644  -9.836  1.00 84.63           N  
ANISOU 4133  N   LEU C 149    11960   9911  10282  -1029   -164  -2118       N  
ATOM   4134  CA  LEU C 149     -29.470 -12.164 -11.209  1.00 88.44           C  
ANISOU 4134  CA  LEU C 149    12381  10852  10367  -1012   -321  -2163       C  
ATOM   4135  C   LEU C 149     -28.047 -12.070 -11.694  1.00 87.94           C  
ANISOU 4135  C   LEU C 149    12463  10870  10080   -925   -215  -2144       C  
ATOM   4136  O   LEU C 149     -27.777 -12.423 -12.859  1.00 93.46           O  
ANISOU 4136  O   LEU C 149    13146  11877  10488   -964   -253  -2386       O  
ATOM   4137  CB  LEU C 149     -30.236 -10.854 -11.376  1.00 89.50           C  
ANISOU 4137  CB  LEU C 149    12401  11226  10378   -943   -492  -1839       C  
ATOM   4138  CG  LEU C 149     -31.771 -11.002 -11.213  1.00 91.13           C  
ANISOU 4138  CG  LEU C 149    12400  11439  10785  -1043   -628  -1915       C  
ATOM   4139  CD1 LEU C 149     -32.483  -9.692 -11.488  1.00 91.57           C  
ANISOU 4139  CD1 LEU C 149    12309  11734  10747   -960   -806  -1584       C  
ATOM   4140  CD2 LEU C 149     -32.354 -12.068 -12.124  1.00 93.98           C  
ANISOU 4140  CD2 LEU C 149    12639  11994  11072  -1204   -753  -2343       C  
ATOM   4141  N   ALA C 150     -27.141 -11.670 -10.800  1.00 82.15           N  
ANISOU 4141  N   ALA C 150    11862   9865   9485   -819    -74  -1891       N  
ATOM   4142  CA  ALA C 150     -25.707 -11.648 -11.097  1.00 81.92           C  
ANISOU 4142  CA  ALA C 150    11952   9837   9335   -736     52  -1864       C  
ATOM   4143  C   ALA C 150     -25.191 -12.965 -11.697  1.00 85.07           C  
ANISOU 4143  C   ALA C 150    12365  10209   9748   -812    158  -2286       C  
ATOM   4144  O   ALA C 150     -24.544 -12.990 -12.756  1.00 87.62           O  
ANISOU 4144  O   ALA C 150    12699  10809   9783   -795    193  -2420       O  
ATOM   4145  CB  ALA C 150     -24.932 -11.319  -9.844  1.00 77.92           C  
ANISOU 4145  CB  ALA C 150    11561   8967   9075   -647    169  -1601       C  
ATOM   4146  N   ARG C 151     -25.491 -14.052 -11.004  1.00 87.44           N  
ANISOU 4146  N   ARG C 151    12654  10164  10402   -897    226  -2492       N  
ATOM   4147  CA  ARG C 151     -25.153 -15.404 -11.465  1.00 91.68           C  
ANISOU 4147  CA  ARG C 151    13171  10589  11071   -982    335  -2927       C  
ATOM   4148  C   ARG C 151     -25.626 -15.649 -12.876  1.00 91.90           C  
ANISOU 4148  C   ARG C 151    13107  11041  10767  -1075    236  -3288       C  
ATOM   4149  O   ARG C 151     -24.836 -16.037 -13.701  1.00 94.15           O  
ANISOU 4149  O   ARG C 151    13419  11466  10888  -1069    337  -3536       O  
ATOM   4150  CB  ARG C 151     -25.777 -16.467 -10.556  1.00 94.85           C  
ANISOU 4150  CB  ARG C 151    13528  10577  11931  -1085    384  -3064       C  
ATOM   4151  CG  ARG C 151     -25.662 -17.878 -11.103  1.00100.97           C  
ANISOU 4151  CG  ARG C 151    14237  11219  12908  -1195    479  -3554       C  
ATOM   4152  CD  ARG C 151     -24.570 -18.675 -10.431  1.00103.47           C  
ANISOU 4152  CD  ARG C 151    14619  11094  13601  -1141    679  -3546       C  
ATOM   4153  NE  ARG C 151     -25.186 -19.595  -9.471  1.00106.04           N  
ANISOU 4153  NE  ARG C 151    14892  10993  14404  -1233    725  -3563       N  
ATOM   4154  CZ  ARG C 151     -25.619 -20.832  -9.744  1.00111.41           C  
ANISOU 4154  CZ  ARG C 151    15454  11474  15402  -1367    780  -3965       C  
ATOM   4155  NH1 ARG C 151     -25.495 -21.399 -10.954  1.00115.84           N  
ANISOU 4155  NH1 ARG C 151    15939  12215  15859  -1434    800  -4456       N  
ATOM   4156  NH2 ARG C 151     -26.172 -21.544  -8.766  1.00115.52           N  
ANISOU 4156  NH2 ARG C 151    15926  11595  16370  -1443    833  -3881       N  
ATOM   4157  N   ALA C 152     -26.903 -15.407 -13.136  1.00 90.34           N  
ANISOU 4157  N   ALA C 152    12794  11061  10468  -1160     39  -3317       N  
ATOM   4158  CA  ALA C 152     -27.453 -15.635 -14.454  1.00 93.36           C  
ANISOU 4158  CA  ALA C 152    13077  11887  10506  -1266   -104  -3660       C  
ATOM   4159  C   ALA C 152     -26.790 -14.842 -15.599  1.00 95.55           C  
ANISOU 4159  C   ALA C 152    13409  12664  10232  -1189   -135  -3570       C  
ATOM   4160  O   ALA C 152     -27.029 -15.152 -16.766  1.00101.63           O  
ANISOU 4160  O   ALA C 152    14125  13838  10651  -1281   -224  -3900       O  
ATOM   4161  CB  ALA C 152     -28.950 -15.402 -14.442  1.00 93.76           C  
ANISOU 4161  CB  ALA C 152    12968  12076  10580  -1359   -341  -3637       C  
ATOM   4162  N   PHE C 153     -25.964 -13.848 -15.279  1.00 93.64           N  
ANISOU 4162  N   PHE C 153    13265  12402   9909  -1034    -59  -3136       N  
ATOM   4163  CA  PHE C 153     -25.292 -13.019 -16.270  1.00 95.41           C  
ANISOU 4163  CA  PHE C 153    13534  13061   9655   -954    -57  -2968       C  
ATOM   4164  C   PHE C 153     -23.762 -12.838 -15.968  1.00 92.14           C  
ANISOU 4164  C   PHE C 153    13243  12437   9326   -825    193  -2805       C  
ATOM   4165  O   PHE C 153     -22.952 -13.638 -16.367  1.00 90.24           O  
ANISOU 4165  O   PHE C 153    13041  12158   9088   -842    377  -3124       O  
ATOM   4166  CB  PHE C 153     -26.047 -11.662 -16.332  1.00 96.93           C  
ANISOU 4166  CB  PHE C 153    13657  13513   9656   -893   -279  -2504       C  
ATOM   4167  CG  PHE C 153     -27.562 -11.760 -16.587  1.00 99.94           C  
ANISOU 4167  CG  PHE C 153    13878  14090  10002  -1007   -545  -2616       C  
ATOM   4168  CD1 PHE C 153     -28.078 -12.314 -17.771  1.00106.35           C  
ANISOU 4168  CD1 PHE C 153    14612  15338  10457  -1137   -692  -2990       C  
ATOM   4169  CD2 PHE C 153     -28.487 -11.228 -15.672  1.00 98.53           C  
ANISOU 4169  CD2 PHE C 153    13612  13691  10134   -985   -658  -2345       C  
ATOM   4170  CE1 PHE C 153     -29.468 -12.379 -18.007  1.00108.84           C  
ANISOU 4170  CE1 PHE C 153    14750  15839  10762  -1246   -968  -3083       C  
ATOM   4171  CE2 PHE C 153     -29.879 -11.291 -15.897  1.00100.46           C  
ANISOU 4171  CE2 PHE C 153    13675  14101  10395  -1084   -899  -2430       C  
ATOM   4172  CZ  PHE C 153     -30.369 -11.865 -17.065  1.00106.05           C  
ANISOU 4172  CZ  PHE C 153    14291  15227  10775  -1215  -1070  -2789       C  
ATOM   4173  N   GLY C 154     -23.365 -11.821 -15.219  1.00 89.71           N  
ANISOU 4173  N   GLY C 154    12981  11964   9140   -700    207  -2335       N  
ATOM   4174  CA  GLY C 154     -21.954 -11.518 -15.080  1.00 91.84           C  
ANISOU 4174  CA  GLY C 154    13334  12106   9454   -586    406  -2163       C  
ATOM   4175  C   GLY C 154     -21.764 -10.260 -14.229  1.00 90.96           C  
ANISOU 4175  C   GLY C 154    13246  11832   9482   -470    362  -1647       C  
ATOM   4176  O   GLY C 154     -20.719 -10.086 -13.569  1.00 92.29           O  
ANISOU 4176  O   GLY C 154    13474  11715   9874   -385    496  -1487       O  
ATOM   4177  N   VAL C 159     -20.805   2.705 -17.073  1.00181.55           N  
ANISOU 4177  N   VAL C 159    23966  24398  20617    370    -34   2916       N  
ATOM   4178  CA  VAL C 159     -20.029   1.467 -17.099  1.00177.51           C  
ANISOU 4178  CA  VAL C 159    23615  23924  19906    299    123   2469       C  
ATOM   4179  C   VAL C 159     -19.316   1.244 -15.745  1.00171.50           C  
ANISOU 4179  C   VAL C 159    22934  22618  19608    309    245   2254       C  
ATOM   4180  O   VAL C 159     -19.699   0.348 -14.988  1.00166.25           O  
ANISOU 4180  O   VAL C 159    22353  21766  19047    254    207   1871       O  
ATOM   4181  CB  VAL C 159     -19.011   1.444 -18.283  1.00179.16           C  
ANISOU 4181  CB  VAL C 159    23847  24509  19716    299    306   2603       C  
ATOM   4182  CG1 VAL C 159     -18.351   0.066 -18.401  1.00176.56           C  
ANISOU 4182  CG1 VAL C 159    23659  24238  19187    226    470   2085       C  
ATOM   4183  CG2 VAL C 159     -19.683   1.811 -19.605  1.00177.97           C  
ANISOU 4183  CG2 VAL C 159    23617  24935  19067    290    170   2891       C  
ATOM   4184  N   TYR C 160     -18.314   2.084 -15.441  1.00166.81           N  
ANISOU 4184  N   TYR C 160    22301  21780  19298    372    375   2524       N  
ATOM   4185  CA  TYR C 160     -17.324   1.819 -14.360  1.00156.56           C  
ANISOU 4185  CA  TYR C 160    21078  20050  18357    373    500   2331       C  
ATOM   4186  C   TYR C 160     -17.550   2.476 -12.974  1.00152.63           C  
ANISOU 4186  C   TYR C 160    20558  19080  18352    399    424   2362       C  
ATOM   4187  O   TYR C 160     -17.017   1.977 -11.984  1.00152.09           O  
ANISOU 4187  O   TYR C 160    20579  18708  18497    375    466   2114       O  
ATOM   4188  CB  TYR C 160     -15.881   2.061 -14.870  1.00152.66           C  
ANISOU 4188  CB  TYR C 160    20558  19585  17859    402    715   2495       C  
ATOM   4189  CG  TYR C 160     -15.423   0.989 -15.857  1.00150.65           C  
ANISOU 4189  CG  TYR C 160    20375  19691  17171    358    856   2252       C  
ATOM   4190  CD1 TYR C 160     -15.045  -0.291 -15.413  1.00145.75           C  
ANISOU 4190  CD1 TYR C 160    19864  18935  16578    312    926   1794       C  
ATOM   4191  CD2 TYR C 160     -15.399   1.237 -17.233  1.00150.39           C  
ANISOU 4191  CD2 TYR C 160    20298  20140  16702    359    923   2472       C  
ATOM   4192  CE1 TYR C 160     -14.655  -1.275 -16.314  1.00145.38           C  
ANISOU 4192  CE1 TYR C 160    19867  19189  16181    272   1074   1525       C  
ATOM   4193  CE2 TYR C 160     -15.011   0.257 -18.138  1.00149.84           C  
ANISOU 4193  CE2 TYR C 160    20298  20422  16212    310   1071   2195       C  
ATOM   4194  CZ  TYR C 160     -14.641  -0.991 -17.674  1.00148.84           C  
ANISOU 4194  CZ  TYR C 160    20267  20118  16166    268   1153   1701       C  
ATOM   4195  OH  TYR C 160     -14.245  -1.953 -18.572  1.00149.64           O  
ANISOU 4195  OH  TYR C 160    20421  20537  15899    220   1324   1388       O  
ATOM   4196  N   THR C 161     -18.314   3.570 -12.892  1.00153.24           N  
ANISOU 4196  N   THR C 161    20513  19098  18611    446    317   2654       N  
ATOM   4197  CA  THR C 161     -18.812   4.092 -11.582  1.00150.40           C  
ANISOU 4197  CA  THR C 161    20137  18331  18676    458    245   2594       C  
ATOM   4198  C   THR C 161     -20.194   3.524 -11.229  1.00148.84           C  
ANISOU 4198  C   THR C 161    19965  18181  18405    419    112   2362       C  
ATOM   4199  O   THR C 161     -20.633   3.575 -10.061  1.00126.83           O  
ANISOU 4199  O   THR C 161    17209  15092  15888    404     87   2193       O  
ATOM   4200  CB  THR C 161     -18.841   5.644 -11.487  1.00154.53           C  
ANISOU 4200  CB  THR C 161    20487  18653  19574    534    235   2992       C  
ATOM   4201  OG1 THR C 161     -19.332   6.210 -12.707  1.00160.46           O  
ANISOU 4201  OG1 THR C 161    21099  19729  20136    580    180   3374       O  
ATOM   4202  CG2 THR C 161     -17.454   6.213 -11.188  1.00152.97           C  
ANISOU 4202  CG2 THR C 161    20268  18201  19653    550    367   3109       C  
ATOM   4203  N   HIS C 162     -20.899   3.053 -12.264  1.00164.91           N  
ANISOU 4203  N   HIS C 162    21972  20613  20074    397     29   2369       N  
ATOM   4204  CA  HIS C 162     -21.980   2.058 -12.129  1.00176.82           C  
ANISOU 4204  CA  HIS C 162    23524  22231  21426    326    -74   2050       C  
ATOM   4205  C   HIS C 162     -21.540   1.009 -11.082  1.00173.48           C  
ANISOU 4205  C   HIS C 162    23270  21541  21100    262     13   1652       C  
ATOM   4206  O   HIS C 162     -22.317   0.637 -10.182  1.00177.54           O  
ANISOU 4206  O   HIS C 162    23815  21873  21767    222    -28   1447       O  
ATOM   4207  CB  HIS C 162     -22.270   1.388 -13.504  1.00183.89           C  
ANISOU 4207  CB  HIS C 162    24410  23629  21830    282   -140   2008       C  
ATOM   4208  CG  HIS C 162     -23.725   1.308 -13.874  1.00194.54           C  
ANISOU 4208  CG  HIS C 162    25646  25199  23069    255   -341   2001       C  
ATOM   4209  ND1 HIS C 162     -24.660   0.642 -13.106  1.00199.90           N  
ANISOU 4209  ND1 HIS C 162    26337  25721  23892    194   -406   1696       N  
ATOM   4210  CD2 HIS C 162     -24.398   1.781 -14.951  1.00197.26           C  
ANISOU 4210  CD2 HIS C 162    25850  25927  23173    276   -500   2275       C  
ATOM   4211  CE1 HIS C 162     -25.847   0.730 -13.683  1.00198.82           C  
ANISOU 4211  CE1 HIS C 162    26057  25840  23646    180   -595   1765       C  
ATOM   4212  NE2 HIS C 162     -25.713   1.411 -14.808  1.00199.60           N  
ANISOU 4212  NE2 HIS C 162    26061  26278  23499    230   -672   2117       N  
ATOM   4213  N   GLU C 163     -20.280   0.570 -11.215  1.00165.21           N  
ANISOU 4213  N   GLU C 163    22315  20474  19982    257    142   1578       N  
ATOM   4214  CA  GLU C 163     -19.582  -0.241 -10.202  1.00152.74           C  
ANISOU 4214  CA  GLU C 163    20872  18604  18558    219    225   1302       C  
ATOM   4215  C   GLU C 163     -19.221   0.605  -8.941  1.00144.70           C  
ANISOU 4215  C   GLU C 163    19859  17198  17923    252    233   1401       C  
ATOM   4216  O   GLU C 163     -19.861   0.454  -7.899  1.00123.33           O  
ANISOU 4216  O   GLU C 163    17201  14291  15366    220    191   1254       O  
ATOM   4217  CB  GLU C 163     -18.360  -0.971 -10.841  1.00151.34           C  
ANISOU 4217  CB  GLU C 163    20750  18537  18215    212    360   1201       C  
ATOM   4218  CG  GLU C 163     -18.753  -2.028 -11.909  1.00150.69           C  
ANISOU 4218  CG  GLU C 163    20688  18809  17757    155    366    968       C  
ATOM   4219  CD  GLU C 163     -17.588  -2.734 -12.638  1.00144.46           C  
ANISOU 4219  CD  GLU C 163    19936  18147  16803    151    538    832       C  
ATOM   4220  OE1 GLU C 163     -16.932  -2.086 -13.487  1.00140.95           O  
ANISOU 4220  OE1 GLU C 163    19432  17906  16216    197    627   1071       O  
ATOM   4221  OE2 GLU C 163     -17.360  -3.952 -12.404  1.00132.35           O  
ANISOU 4221  OE2 GLU C 163    18477  16514  15293    103    599    490       O  
ATOM   4222  N   VAL C 164     -18.264   1.532  -9.073  1.00152.04           N  
ANISOU 4222  N   VAL C 164    20724  18040  19002    308    291   1647       N  
ATOM   4223  CA  VAL C 164     -17.745   2.373  -7.931  1.00154.52           C  
ANISOU 4223  CA  VAL C 164    21032  17989  19689    327    295   1707       C  
ATOM   4224  C   VAL C 164     -18.841   2.963  -7.030  1.00145.17           C  
ANISOU 4224  C   VAL C 164    19824  16626  18707    324    221   1673       C  
ATOM   4225  O   VAL C 164     -18.787   2.939  -5.784  1.00122.83           O  
ANISOU 4225  O   VAL C 164    17076  13539  16053    291    214   1502       O  
ATOM   4226  CB  VAL C 164     -16.804   3.545  -8.410  1.00157.18           C  
ANISOU 4226  CB  VAL C 164    21237  18272  20209    387    358   2036       C  
ATOM   4227  CG1 VAL C 164     -16.396   4.466  -7.256  1.00151.46           C  
ANISOU 4227  CG1 VAL C 164    20483  17169  19893    392    341   2054       C  
ATOM   4228  CG2 VAL C 164     -15.544   3.021  -9.108  1.00155.22           C  
ANISOU 4228  CG2 VAL C 164    21002  18144  19828    389    475   2055       C  
ATOM   4229  N   VAL C 165     -21.405   3.105  -6.396  1.00102.89           N  
ANISOU 4229  N   VAL C 165    14401  11266  13424    304    114   1541       N  
ATOM   4230  CA  VAL C 165     -21.948   2.628  -5.125  1.00 99.30           C  
ANISOU 4230  CA  VAL C 165    14052  10624  13050    244    131   1271       C  
ATOM   4231  C   VAL C 165     -21.420   1.264  -4.828  1.00 93.64           C  
ANISOU 4231  C   VAL C 165    13508   9930  12141    173    155   1042       C  
ATOM   4232  O   VAL C 165     -20.995   1.010  -3.706  1.00 96.65           O  
ANISOU 4232  O   VAL C 165    14010  10109  12602    133    183    902       O  
ATOM   4233  CB  VAL C 165     -23.512   2.524  -5.125  1.00102.74           C  
ANISOU 4233  CB  VAL C 165    14402  11138  13494    230     92   1211       C  
ATOM   4234  CG1 VAL C 165     -24.130   3.770  -4.438  1.00107.31           C  
ANISOU 4234  CG1 VAL C 165    14860  11491  14419    279    120   1285       C  
ATOM   4235  CG2 VAL C 165     -24.077   2.299  -6.542  1.00101.44           C  
ANISOU 4235  CG2 VAL C 165    14118  11312  13111    248      0   1347       C  
ATOM   4236  N   THR C 166     -21.457   0.380  -5.809  1.00 91.08           N  
ANISOU 4236  N   THR C 166    13187   9850  11568    153    140    999       N  
ATOM   4237  CA  THR C 166     -21.495  -1.054  -5.468  1.00 91.54           C  
ANISOU 4237  CA  THR C 166    13374   9903  11503     75    162    734       C  
ATOM   4238  C   THR C 166     -20.325  -1.402  -4.580  1.00 80.61           C  
ANISOU 4238  C   THR C 166    12118   8300  10209     61    207    668       C  
ATOM   4239  O   THR C 166     -20.435  -2.324  -3.690  1.00 78.08           O  
ANISOU 4239  O   THR C 166    11914   7851   9901     -1    222    494       O  
ATOM   4240  CB  THR C 166     -21.516  -2.014  -6.677  1.00101.53           C  
ANISOU 4240  CB  THR C 166    14624  11440  12509     48    155    637       C  
ATOM   4241  OG1 THR C 166     -20.213  -2.079  -7.260  1.00105.27           O  
ANISOU 4241  OG1 THR C 166    15119  11965  12913     84    215    698       O  
ATOM   4242  CG2 THR C 166     -22.598  -1.615  -7.732  1.00104.98           C  
ANISOU 4242  CG2 THR C 166    14915  12166  12804     60     65    736       C  
ATOM   4243  N   LEU C 167     -19.260  -0.616  -4.775  1.00 67.35           N  
ANISOU 4243  N   LEU C 167    10401   6571   8618    118    219    834       N  
ATOM   4244  CA  LEU C 167     -18.048  -0.759  -4.003  1.00 64.54           C  
ANISOU 4244  CA  LEU C 167    10124   6015   8380    113    231    808       C  
ATOM   4245  C   LEU C 167     -18.104  -0.688  -2.465  1.00 62.46           C  
ANISOU 4245  C   LEU C 167     9967   5521   8244     68    196    711       C  
ATOM   4246  O   LEU C 167     -17.253  -1.292  -1.807  1.00 64.39           O  
ANISOU 4246  O   LEU C 167    10300   5646   8516     42    176    650       O  
ATOM   4247  CB  LEU C 167     -17.056   0.252  -4.475  1.00 66.20           C  
ANISOU 4247  CB  LEU C 167    10235   6202   8713    174    248   1017       C  
ATOM   4248  CG  LEU C 167     -15.767  -0.376  -4.930  1.00 68.48           C  
ANISOU 4248  CG  LEU C 167    10528   6510   8979    187    301   1016       C  
ATOM   4249  CD1 LEU C 167     -15.954  -1.231  -6.184  1.00 71.34           C  
ANISOU 4249  CD1 LEU C 167    10874   7142   9090    190    370    955       C  
ATOM   4250  CD2 LEU C 167     -14.803   0.742  -5.240  1.00 69.24           C  
ANISOU 4250  CD2 LEU C 167    10506   6544   9255    238    329   1240       C  
ATOM   4251  N   TRP C 168     -19.068   0.016  -1.876  1.00 58.34           N  
ANISOU 4251  N   TRP C 168     9430   4941   7792     57    190    695       N  
ATOM   4252  CA  TRP C 168     -19.062   0.213  -0.426  1.00 56.80           C  
ANISOU 4252  CA  TRP C 168     9340   4563   7677      8    176    589       C  
ATOM   4253  C   TRP C 168     -19.535  -1.003   0.362  1.00 59.13           C  
ANISOU 4253  C   TRP C 168     9778   4849   7838    -67    193    436       C  
ATOM   4254  O   TRP C 168     -19.297  -1.092   1.570  1.00 56.32           O  
ANISOU 4254  O   TRP C 168     9541   4382   7476   -117    174    367       O  
ATOM   4255  CB  TRP C 168     -19.924   1.386  -0.022  1.00 56.44           C  
ANISOU 4255  CB  TRP C 168     9222   4445   7777     22    204    587       C  
ATOM   4256  CG  TRP C 168     -19.580   2.647  -0.668  1.00 57.60           C  
ANISOU 4256  CG  TRP C 168     9212   4550   8121     94    196    761       C  
ATOM   4257  CD1 TRP C 168     -18.355   3.026  -1.173  1.00 58.82           C  
ANISOU 4257  CD1 TRP C 168     9310   4674   8363    131    169    903       C  
ATOM   4258  CD2 TRP C 168     -20.457   3.695  -0.953  1.00 57.76           C  
ANISOU 4258  CD2 TRP C 168     9083   4544   8319    144    226    847       C  
ATOM   4259  NE1 TRP C 168     -18.436   4.253  -1.751  1.00 57.81           N  
ANISOU 4259  NE1 TRP C 168     9014   4501   8447    194    186   1088       N  
ATOM   4260  CE2 TRP C 168     -19.723   4.690  -1.622  1.00 58.23           C  
ANISOU 4260  CE2 TRP C 168     9005   4549   8569    208    212   1062       C  
ATOM   4261  CE3 TRP C 168     -21.803   3.912  -0.687  1.00 60.08           C  
ANISOU 4261  CE3 TRP C 168     9322   4835   8669    143    271    777       C  
ATOM   4262  CZ2 TRP C 168     -20.283   5.871  -2.007  1.00 59.96           C  
ANISOU 4262  CZ2 TRP C 168     9043   4697   9040    272    233   1224       C  
ATOM   4263  CZ3 TRP C 168     -22.365   5.128  -1.040  1.00 61.55           C  
ANISOU 4263  CZ3 TRP C 168     9318   4944   9124    213    290    915       C  
ATOM   4264  CH2 TRP C 168     -21.611   6.074  -1.715  1.00 61.28           C  
ANISOU 4264  CH2 TRP C 168     9155   4849   9279    279    264   1148       C  
ATOM   4265  N   TYR C 169     -20.226  -1.928  -0.321  1.00 60.20           N  
ANISOU 4265  N   TYR C 169     9897   5111   7865    -84    225    388       N  
ATOM   4266  CA  TYR C 169     -20.892  -3.039   0.353  1.00 59.03           C  
ANISOU 4266  CA  TYR C 169     9849   4936   7643   -163    263    263       C  
ATOM   4267  C   TYR C 169     -20.221  -4.385   0.003  1.00 59.63           C  
ANISOU 4267  C   TYR C 169     9973   5009   7674   -182    258    225       C  
ATOM   4268  O   TYR C 169     -20.795  -5.470   0.164  1.00 58.78           O  
ANISOU 4268  O   TYR C 169     9904   4886   7541   -244    298    132       O  
ATOM   4269  CB  TYR C 169     -22.349  -3.023  -0.033  1.00 59.26           C  
ANISOU 4269  CB  TYR C 169     9787   5066   7661   -183    309    208       C  
ATOM   4270  CG  TYR C 169     -22.980  -1.678   0.200  1.00 59.95           C  
ANISOU 4270  CG  TYR C 169     9787   5131   7860   -145    327    254       C  
ATOM   4271  CD1 TYR C 169     -23.309  -1.260   1.460  1.00 61.22           C  
ANISOU 4271  CD1 TYR C 169    10021   5168   8070   -181    387    183       C  
ATOM   4272  CD2 TYR C 169     -23.242  -0.817  -0.848  1.00 59.82           C  
ANISOU 4272  CD2 TYR C 169     9606   5217   7905    -72    290    373       C  
ATOM   4273  CE1 TYR C 169     -23.898  -0.006   1.694  1.00 62.65           C  
ANISOU 4273  CE1 TYR C 169    10102   5293   8408   -143    430    186       C  
ATOM   4274  CE2 TYR C 169     -23.828   0.416  -0.637  1.00 61.65           C  
ANISOU 4274  CE2 TYR C 169     9727   5383   8311    -27    312    430       C  
ATOM   4275  CZ  TYR C 169     -24.153   0.836   0.639  1.00 61.85           C  
ANISOU 4275  CZ  TYR C 169     9815   5249   8434    -61    391    317       C  
ATOM   4276  OH  TYR C 169     -24.721   2.076   0.827  1.00 59.53           O  
ANISOU 4276  OH  TYR C 169     9392   4860   8365    -11    435    341       O  
ATOM   4277  N   ARG C 170     -18.974  -4.293  -0.429  1.00 56.99           N  
ANISOU 4277  N   ARG C 170     9619   4658   7376   -130    222    296       N  
ATOM   4278  CA  ARG C 170     -18.331  -5.349  -1.114  1.00 55.44           C  
ANISOU 4278  CA  ARG C 170     9409   4476   7176   -122    243    249       C  
ATOM   4279  C   ARG C 170     -17.330  -5.975  -0.157  1.00 55.31           C  
ANISOU 4279  C   ARG C 170     9483   4277   7256   -135    201    283       C  
ATOM   4280  O   ARG C 170     -16.607  -5.258   0.526  1.00 55.81           O  
ANISOU 4280  O   ARG C 170     9572   4261   7372   -117    130    376       O  
ATOM   4281  CB  ARG C 170     -17.663  -4.761  -2.319  1.00 56.25           C  
ANISOU 4281  CB  ARG C 170     9401   4707   7262    -50    257    321       C  
ATOM   4282  CG  ARG C 170     -17.030  -5.795  -3.200  1.00 59.97           C  
ANISOU 4282  CG  ARG C 170     9841   5227   7716    -38    318    229       C  
ATOM   4283  CD  ARG C 170     -17.214  -5.525  -4.682  1.00 60.95           C  
ANISOU 4283  CD  ARG C 170     9862   5610   7684     -6    369    218       C  
ATOM   4284  NE  ARG C 170     -18.615  -5.511  -4.995  1.00 61.40           N  
ANISOU 4284  NE  ARG C 170     9896   5817   7614    -49    342    148       N  
ATOM   4285  CZ  ARG C 170     -19.076  -5.325  -6.207  1.00 64.62           C  
ANISOU 4285  CZ  ARG C 170    10220   6492   7841    -41    345    137       C  
ATOM   4286  NH1 ARG C 170     -18.233  -5.182  -7.247  1.00 66.50           N  
ANISOU 4286  NH1 ARG C 170    10405   6893   7969      5    405    184       N  
ATOM   4287  NH2 ARG C 170     -20.394  -5.255  -6.379  1.00 67.63           N  
ANISOU 4287  NH2 ARG C 170    10558   6996   8142    -81    288     90       N  
ATOM   4288  N   SER C 171     -17.298  -7.319  -0.108  1.00 53.86           N  
ANISOU 4288  N   SER C 171     9331   4016   7117   -168    234    209       N  
ATOM   4289  CA  SER C 171     -16.462  -8.057   0.856  1.00 51.29           C  
ANISOU 4289  CA  SER C 171     9078   3505   6904   -180    180    283       C  
ATOM   4290  C   SER C 171     -15.003  -7.967   0.498  1.00 49.08           C  
ANISOU 4290  C   SER C 171     8726   3166   6756   -107    142    353       C  
ATOM   4291  O   SER C 171     -14.643  -7.905  -0.657  1.00 48.51           O  
ANISOU 4291  O   SER C 171     8551   3177   6701    -57    213    299       O  
ATOM   4292  CB  SER C 171     -16.812  -9.493   0.781  1.00 52.40           C  
ANISOU 4292  CB  SER C 171     9226   3553   7129   -223    246    198       C  
ATOM   4293  OG  SER C 171     -16.569  -9.928  -0.555  1.00 53.48           O  
ANISOU 4293  OG  SER C 171     9254   3754   7313   -185    325     60       O  
ATOM   4294  N   PRO C 172     -14.159  -8.046   1.472  1.00 47.83           N  
ANISOU 4294  N   PRO C 172     8609   2873   6688   -106     34    473       N  
ATOM   4295  CA  PRO C 172     -12.743  -8.002   1.189  1.00 48.51           C  
ANISOU 4295  CA  PRO C 172     8596   2883   6953    -38     -9    547       C  
ATOM   4296  C   PRO C 172     -12.193  -9.259   0.507  1.00 51.06           C  
ANISOU 4296  C   PRO C 172     8832   3104   7464      1     81    486       C  
ATOM   4297  O   PRO C 172     -11.146  -9.146  -0.162  1.00 51.69           O  
ANISOU 4297  O   PRO C 172     8788   3164   7688     69    117    497       O  
ATOM   4298  CB  PRO C 172     -12.113  -7.878   2.553  1.00 48.97           C  
ANISOU 4298  CB  PRO C 172     8723   2832   7051    -62   -186    691       C  
ATOM   4299  CG  PRO C 172     -13.096  -8.522   3.468  1.00 49.74           C  
ANISOU 4299  CG  PRO C 172     8964   2914   7019   -140   -191    698       C  
ATOM   4300  CD  PRO C 172     -14.461  -8.376   2.865  1.00 48.47           C  
ANISOU 4300  CD  PRO C 172     8823   2876   6716   -172    -49    554       C  
ATOM   4301  N   GLU C 173     -12.852 -10.426   0.655  1.00 51.13           N  
ANISOU 4301  N   GLU C 173     8886   3031   7508    -41    136    414       N  
ATOM   4302  CA  GLU C 173     -12.532 -11.547  -0.240  1.00 52.14           C  
ANISOU 4302  CA  GLU C 173     8912   3071   7828     -8    267    273       C  
ATOM   4303  C   GLU C 173     -12.469 -11.105  -1.682  1.00 51.29           C  
ANISOU 4303  C   GLU C 173     8710   3155   7621     30    398    113       C  
ATOM   4304  O   GLU C 173     -11.531 -11.395  -2.402  1.00 51.25           O  
ANISOU 4304  O   GLU C 173     8591   3116   7766     92    488     55       O  
ATOM   4305  CB  GLU C 173     -13.624 -12.611  -0.245  1.00 53.35           C  
ANISOU 4305  CB  GLU C 173     9107   3167   7996    -80    347    140       C  
ATOM   4306  CG  GLU C 173     -13.995 -13.121   1.082  1.00 54.97           C  
ANISOU 4306  CG  GLU C 173     9414   3221   8247   -138    262    304       C  
ATOM   4307  CD  GLU C 173     -15.346 -12.713   1.549  1.00 54.54           C  
ANISOU 4307  CD  GLU C 173     9472   3293   7957   -224    264    291       C  
ATOM   4308  OE1 GLU C 173     -16.324 -13.201   0.940  1.00 57.72           O  
ANISOU 4308  OE1 GLU C 173     9847   3734   8349   -275    372    110       O  
ATOM   4309  OE2 GLU C 173     -15.404 -12.000   2.558  1.00 52.75           O  
ANISOU 4309  OE2 GLU C 173     9347   3112   7584   -247    162    447       O  
ATOM   4310  N   VAL C 174     -13.570 -10.489  -2.108  1.00 50.53           N  
ANISOU 4310  N   VAL C 174     8658   3270   7269    -11    420     38       N  
ATOM   4311  CA  VAL C 174     -13.778 -10.169  -3.509  1.00 51.75           C  
ANISOU 4311  CA  VAL C 174     8739   3661   7262      6    531   -102       C  
ATOM   4312  C   VAL C 174     -12.774  -9.097  -3.919  1.00 51.86           C  
ANISOU 4312  C   VAL C 174     8678   3758   7266     80    536     40       C  
ATOM   4313  O   VAL C 174     -12.102  -9.211  -4.928  1.00 53.67           O  
ANISOU 4313  O   VAL C 174     8812   4074   7504    125    661    -29       O  
ATOM   4314  CB  VAL C 174     -15.184  -9.649  -3.755  1.00 51.05           C  
ANISOU 4314  CB  VAL C 174     8693   3775   6927    -49    509   -152       C  
ATOM   4315  CG1 VAL C 174     -15.341  -9.136  -5.177  1.00 51.59           C  
ANISOU 4315  CG1 VAL C 174     8683   4136   6783    -26    582   -228       C  
ATOM   4316  CG2 VAL C 174     -16.196 -10.761  -3.520  1.00 52.16           C  
ANISOU 4316  CG2 VAL C 174     8872   3840   7107   -132    530   -319       C  
ATOM   4317  N   LEU C 175     -12.631  -8.114  -3.063  1.00 50.31           N  
ANISOU 4317  N   LEU C 175     8521   3515   7079     83    412    230       N  
ATOM   4318  CA  LEU C 175     -11.709  -7.050  -3.309  1.00 49.74           C  
ANISOU 4318  CA  LEU C 175     8365   3476   7058    138    404    379       C  
ATOM   4319  C   LEU C 175     -10.299  -7.606  -3.461  1.00 50.85           C  
ANISOU 4319  C   LEU C 175     8398   3473   7447    195    455    395       C  
ATOM   4320  O   LEU C 175      -9.561  -7.148  -4.347  1.00 53.41           O  
ANISOU 4320  O   LEU C 175     8606   3888   7798    246    565    432       O  
ATOM   4321  CB  LEU C 175     -11.819  -5.953  -2.197  1.00 48.11           C  
ANISOU 4321  CB  LEU C 175     8215   3199   6864    116    248    531       C  
ATOM   4322  CG  LEU C 175     -13.203  -5.265  -2.080  1.00 46.79           C  
ANISOU 4322  CG  LEU C 175     8118   3155   6501     73    226    514       C  
ATOM   4323  CD1 LEU C 175     -13.316  -4.424  -0.831  1.00 46.07           C  
ANISOU 4323  CD1 LEU C 175     8096   2961   6446     40     98    590       C  
ATOM   4324  CD2 LEU C 175     -13.507  -4.447  -3.294  1.00 47.24           C  
ANISOU 4324  CD2 LEU C 175     8084   3420   6443    108    308    559       C  
ATOM   4325  N   LEU C 176      -9.886  -8.534  -2.592  1.00 50.24           N  
ANISOU 4325  N   LEU C 176     8341   3173   7573    191    381    398       N  
ATOM   4326  CA  LEU C 176      -8.494  -9.006  -2.642  1.00 51.48           C  
ANISOU 4326  CA  LEU C 176     8362   3161   8034    256    409    443       C  
ATOM   4327  C   LEU C 176      -8.209 -10.049  -3.737  1.00 53.16           C  
ANISOU 4327  C   LEU C 176     8478   3375   8345    296    628    241       C  
ATOM   4328  O   LEU C 176      -7.091 -10.503  -3.888  1.00 53.06           O  
ANISOU 4328  O   LEU C 176     8326   3214   8617    358    693    249       O  
ATOM   4329  CB  LEU C 176      -8.017  -9.454  -1.283  1.00 51.55           C  
ANISOU 4329  CB  LEU C 176     8399   2938   8249    247    215    581       C  
ATOM   4330  CG  LEU C 176      -7.698  -8.288  -0.350  1.00 51.24           C  
ANISOU 4330  CG  LEU C 176     8390   2899   8180    224     14    757       C  
ATOM   4331  CD1 LEU C 176      -7.722  -8.695   1.107  1.00 51.91           C  
ANISOU 4331  CD1 LEU C 176     8576   2852   8293    178   -202    874       C  
ATOM   4332  CD2 LEU C 176      -6.353  -7.665  -0.681  1.00 52.40           C  
ANISOU 4332  CD2 LEU C 176     8353   2995   8559    283     12    853       C  
ATOM   4333  N   GLY C 177      -9.199 -10.313  -4.568  1.00 54.93           N  
ANISOU 4333  N   GLY C 177     8756   3785   8328    258    746     46       N  
ATOM   4334  CA  GLY C 177      -9.030 -11.146  -5.762  1.00 58.58           C  
ANISOU 4334  CA  GLY C 177     9134   4318   8804    278    970   -208       C  
ATOM   4335  C   GLY C 177      -9.163 -12.637  -5.464  1.00 60.06           C  
ANISOU 4335  C   GLY C 177     9316   4263   9241    262   1007   -386       C  
ATOM   4336  O   GLY C 177      -8.525 -13.465  -6.128  1.00 62.77           O  
ANISOU 4336  O   GLY C 177     9542   4520   9787    304   1187   -578       O  
ATOM   4337  N   SER C 178      -9.916 -12.950  -4.418  1.00 58.77           N  
ANISOU 4337  N   SER C 178     9262   3966   9099    206    852   -305       N  
ATOM   4338  CA  SER C 178     -10.038 -14.309  -3.930  1.00 59.28           C  
ANISOU 4338  CA  SER C 178     9316   3751   9455    187    864   -387       C  
ATOM   4339  C   SER C 178     -10.624 -15.215  -4.992  1.00 61.16           C  
ANISOU 4339  C   SER C 178     9516   4043   9676    148   1054   -754       C  
ATOM   4340  O   SER C 178     -11.539 -14.828  -5.732  1.00 60.43           O  
ANISOU 4340  O   SER C 178     9479   4236   9245     90   1090   -914       O  
ATOM   4341  CB  SER C 178     -10.929 -14.296  -2.741  1.00 58.01           C  
ANISOU 4341  CB  SER C 178     9297   3524   9220    115    691   -222       C  
ATOM   4342  OG  SER C 178     -11.275 -15.566  -2.394  1.00 58.02           O  
ANISOU 4342  OG  SER C 178     9291   3287   9466     80    725   -294       O  
ATOM   4343  N   ALA C 179     -10.019 -16.392  -5.133  1.00 63.70           N  
ANISOU 4343  N   ALA C 179     9720   4097  10385    184   1176   -901       N  
ATOM   4344  CA  ALA C 179     -10.355 -17.322  -6.212  1.00 65.79           C  
ANISOU 4344  CA  ALA C 179     9918   4382  10697    149   1386  -1319       C  
ATOM   4345  C   ALA C 179     -11.823 -17.688  -6.285  1.00 64.91           C  
ANISOU 4345  C   ALA C 179     9900   4357  10405     27   1352  -1501       C  
ATOM   4346  O   ALA C 179     -12.414 -17.707  -7.382  1.00 64.66           O  
ANISOU 4346  O   ALA C 179     9865   4591  10110    -27   1453  -1821       O  
ATOM   4347  CB  ALA C 179      -9.523 -18.569  -6.059  1.00 69.12           C  
ANISOU 4347  CB  ALA C 179    10188   4404  11670    208   1501  -1409       C  
ATOM   4348  N   ARG C 180     -12.394 -18.008  -5.128  1.00 64.29           N  
ANISOU 4348  N   ARG C 180     9892   4066  10468    -18   1212  -1298       N  
ATOM   4349  CA  ARG C 180     -13.814 -18.359  -5.056  1.00 65.66           C  
ANISOU 4349  CA  ARG C 180    10134   4286  10527   -140   1181  -1433       C  
ATOM   4350  C   ARG C 180     -14.471 -17.577  -3.937  1.00 60.90           C  
ANISOU 4350  C   ARG C 180     9669   3741   9727   -175    996  -1095       C  
ATOM   4351  O   ARG C 180     -13.810 -17.169  -2.993  1.00 59.39           O  
ANISOU 4351  O   ARG C 180     9518   3445   9599   -119    886   -773       O  
ATOM   4352  CB  ARG C 180     -14.031 -19.898  -4.845  1.00 71.83           C  
ANISOU 4352  CB  ARG C 180    10831   4686  11775   -189   1274  -1606       C  
ATOM   4353  CG  ARG C 180     -13.534 -20.895  -5.929  1.00 78.85           C  
ANISOU 4353  CG  ARG C 180    11565   5453  12941   -173   1492  -2037       C  
ATOM   4354  CD  ARG C 180     -13.241 -22.360  -5.547  1.00 87.46           C  
ANISOU 4354  CD  ARG C 180    12525   6041  14661   -170   1593  -2116       C  
ATOM   4355  NE  ARG C 180     -11.785 -22.384  -5.352  1.00 91.72           N  
ANISOU 4355  NE  ARG C 180    12967   6391  15491    -27   1632  -1936       N  
ATOM   4356  CZ  ARG C 180     -11.140 -22.289  -4.177  1.00 93.12           C  
ANISOU 4356  CZ  ARG C 180    13150   6347  15883     45   1484  -1475       C  
ATOM   4357  NH1 ARG C 180     -11.810 -22.321  -3.018  1.00 91.23           N  
ANISOU 4357  NH1 ARG C 180    13020   6011  15631    -13   1317  -1147       N  
ATOM   4358  NH2 ARG C 180      -9.792 -22.199  -4.162  1.00 94.46           N  
ANISOU 4358  NH2 ARG C 180    13202   6396  16291    175   1509  -1345       N  
ATOM   4359  N   TYR C 181     -15.771 -17.394  -4.016  1.00 58.97           N  
ANISOU 4359  N   TYR C 181     9484   3661   9259   -273    962  -1185       N  
ATOM   4360  CA  TYR C 181     -16.522 -16.729  -2.949  1.00 57.75           C  
ANISOU 4360  CA  TYR C 181     9448   3550   8941   -316    829   -913       C  
ATOM   4361  C   TYR C 181     -17.797 -17.521  -2.711  1.00 57.79           C  
ANISOU 4361  C   TYR C 181     9452   3459   9044   -437    858  -1032       C  
ATOM   4362  O   TYR C 181     -18.221 -18.246  -3.580  1.00 59.48           O  
ANISOU 4362  O   TYR C 181     9577   3674   9347   -493    948  -1358       O  
ATOM   4363  CB  TYR C 181     -16.897 -15.248  -3.348  1.00 57.47           C  
ANISOU 4363  CB  TYR C 181     9465   3883   8488   -300    755   -858       C  
ATOM   4364  CG  TYR C 181     -17.835 -15.178  -4.565  1.00 59.36           C  
ANISOU 4364  CG  TYR C 181     9649   4397   8505   -359    797  -1151       C  
ATOM   4365  CD1 TYR C 181     -17.319 -15.289  -5.846  1.00 61.87           C  
ANISOU 4365  CD1 TYR C 181     9889   4881   8736   -327    888  -1388       C  
ATOM   4366  CD2 TYR C 181     -19.230 -15.088  -4.435  1.00 60.02           C  
ANISOU 4366  CD2 TYR C 181     9746   4580   8477   -454    750  -1202       C  
ATOM   4367  CE1 TYR C 181     -18.130 -15.293  -6.992  1.00 64.49           C  
ANISOU 4367  CE1 TYR C 181    10172   5505   8826   -391    905  -1665       C  
ATOM   4368  CE2 TYR C 181     -20.059 -15.069  -5.581  1.00 62.64           C  
ANISOU 4368  CE2 TYR C 181    10006   5180   8614   -512    751  -1469       C  
ATOM   4369  CZ  TYR C 181     -19.509 -15.173  -6.881  1.00 64.65           C  
ANISOU 4369  CZ  TYR C 181    10196   5633   8733   -484    816  -1704       C  
ATOM   4370  OH  TYR C 181     -20.250 -15.173  -8.081  1.00 66.26           O  
ANISOU 4370  OH  TYR C 181    10332   6158   8684   -548    797  -1977       O  
ATOM   4371  N   SER C 182     -18.471 -17.282  -1.594  1.00 56.15           N  
ANISOU 4371  N   SER C 182     9337   3207   8787   -487    790   -794       N  
ATOM   4372  CA  SER C 182     -19.731 -17.940  -1.319  1.00 56.42           C  
ANISOU 4372  CA  SER C 182     9357   3157   8921   -608    834   -876       C  
ATOM   4373  C   SER C 182     -20.630 -17.054  -0.463  1.00 55.11           C  
ANISOU 4373  C   SER C 182     9292   3136   8508   -652    772   -672       C  
ATOM   4374  O   SER C 182     -20.439 -15.846  -0.368  1.00 52.76           O  
ANISOU 4374  O   SER C 182     9060   3048   7936   -594    694   -555       O  
ATOM   4375  CB  SER C 182     -19.463 -19.273  -0.618  1.00 58.89           C  
ANISOU 4375  CB  SER C 182     9637   3075   9663   -637    898   -779       C  
ATOM   4376  OG  SER C 182     -20.571 -20.183  -0.783  1.00 60.30           O  
ANISOU 4376  OG  SER C 182     9734   3126  10048   -762    987   -975       O  
ATOM   4377  N   THR C 183     -21.561 -17.672   0.255  1.00 56.21           N  
ANISOU 4377  N   THR C 183     9437   3131   8786   -754    825   -612       N  
ATOM   4378  CA  THR C 183     -22.517 -16.910   1.068  1.00 54.75           C  
ANISOU 4378  CA  THR C 183     9332   3079   8391   -805    812   -457       C  
ATOM   4379  C   THR C 183     -21.934 -15.810   1.968  1.00 53.19           C  
ANISOU 4379  C   THR C 183     9278   2987   7945   -734    728   -186       C  
ATOM   4380  O   THR C 183     -22.629 -14.866   2.304  1.00 52.42           O  
ANISOU 4380  O   THR C 183     9224   3063   7629   -751    719   -147       O  
ATOM   4381  CB  THR C 183     -23.399 -17.844   1.960  1.00 55.94           C  
ANISOU 4381  CB  THR C 183     9480   3013   8761   -923    915   -353       C  
ATOM   4382  OG1 THR C 183     -22.599 -18.514   2.921  1.00 56.01           O  
ANISOU 4382  OG1 THR C 183     9562   2779   8941   -904    920    -74       O  
ATOM   4383  CG2 THR C 183     -24.235 -18.832   1.131  1.00 57.24           C  
ANISOU 4383  CG2 THR C 183     9480   3072   9194  -1024    997   -654       C  
ATOM   4384  N   PRO C 184     -20.692 -15.956   2.419  1.00 53.84           N  
ANISOU 4384  N   PRO C 184     9416   2949   8091   -662    665     -8       N  
ATOM   4385  CA  PRO C 184     -20.248 -14.898   3.314  1.00 52.98           C  
ANISOU 4385  CA  PRO C 184     9433   2954   7739   -620    570    209       C  
ATOM   4386  C   PRO C 184     -20.243 -13.506   2.708  1.00 50.79           C  
ANISOU 4386  C   PRO C 184     9148   2928   7221   -562    515    111       C  
ATOM   4387  O   PRO C 184     -20.292 -12.563   3.432  1.00 49.74           O  
ANISOU 4387  O   PRO C 184     9103   2894   6901   -557    468    223       O  
ATOM   4388  CB  PRO C 184     -18.821 -15.344   3.669  1.00 54.42           C  
ANISOU 4388  CB  PRO C 184     9629   2969   8076   -547    482    386       C  
ATOM   4389  CG  PRO C 184     -18.880 -16.849   3.651  1.00 56.50           C  
ANISOU 4389  CG  PRO C 184     9819   2955   8690   -586    566    391       C  
ATOM   4390  CD  PRO C 184     -19.775 -17.121   2.465  1.00 56.32           C  
ANISOU 4390  CD  PRO C 184     9682   2985   8729   -633    677     52       C  
ATOM   4391  N   VAL C 185     -20.174 -13.388   1.394  1.00 50.30           N  
ANISOU 4391  N   VAL C 185     8975   2966   7168   -523    528    -91       N  
ATOM   4392  CA  VAL C 185     -20.207 -12.101   0.799  1.00 48.30           C  
ANISOU 4392  CA  VAL C 185     8698   2940   6710   -469    482   -130       C  
ATOM   4393  C   VAL C 185     -21.507 -11.380   1.099  1.00 49.49           C  
ANISOU 4393  C   VAL C 185     8858   3221   6723   -521    504   -142       C  
ATOM   4394  O   VAL C 185     -21.479 -10.179   1.389  1.00 49.75           O  
ANISOU 4394  O   VAL C 185     8924   3358   6621   -482    460    -61       O  
ATOM   4395  CB  VAL C 185     -20.023 -12.099  -0.705  1.00 48.00           C  
ANISOU 4395  CB  VAL C 185     8543   3041   6651   -428    499   -323       C  
ATOM   4396  CG1 VAL C 185     -18.723 -12.746  -1.096  1.00 49.01           C  
ANISOU 4396  CG1 VAL C 185     8638   3047   6935   -367    516   -345       C  
ATOM   4397  CG2 VAL C 185     -21.202 -12.661  -1.478  1.00 48.90           C  
ANISOU 4397  CG2 VAL C 185     8568   3242   6770   -506    552   -550       C  
ATOM   4398  N   ASP C 186     -22.633 -12.087   1.048  1.00 50.90           N  
ANISOU 4398  N   ASP C 186     8988   3373   6979   -610    580   -251       N  
ATOM   4399  CA  ASP C 186     -23.905 -11.457   1.319  1.00 51.72           C  
ANISOU 4399  CA  ASP C 186     9064   3583   7001   -658    617   -268       C  
ATOM   4400  C   ASP C 186     -24.011 -11.016   2.797  1.00 54.69           C  
ANISOU 4400  C   ASP C 186     9575   3901   7302   -682    655    -92       C  
ATOM   4401  O   ASP C 186     -24.657  -9.991   3.098  1.00 53.83           O  
ANISOU 4401  O   ASP C 186     9461   3898   7092   -676    676    -87       O  
ATOM   4402  CB  ASP C 186     -25.044 -12.363   0.955  1.00 52.92           C  
ANISOU 4402  CB  ASP C 186     9110   3705   7291   -757    688   -425       C  
ATOM   4403  CG  ASP C 186     -25.224 -12.488  -0.517  1.00 54.25           C  
ANISOU 4403  CG  ASP C 186     9138   4022   7449   -748    634   -642       C  
ATOM   4404  OD1 ASP C 186     -24.641 -11.712  -1.298  1.00 55.04           O  
ANISOU 4404  OD1 ASP C 186     9221   4292   7399   -662    556   -643       O  
ATOM   4405  OD2 ASP C 186     -25.953 -13.387  -0.967  1.00 55.43           O  
ANISOU 4405  OD2 ASP C 186     9186   4137   7735   -836    667   -823       O  
ATOM   4406  N   ILE C 187     -23.384 -11.766   3.718  1.00 55.51           N  
ANISOU 4406  N   ILE C 187     9791   3845   7452   -708    664     50       N  
ATOM   4407  CA  ILE C 187     -23.377 -11.381   5.134  1.00 55.49           C  
ANISOU 4407  CA  ILE C 187     9937   3837   7309   -739    685    217       C  
ATOM   4408  C   ILE C 187     -22.509 -10.132   5.396  1.00 54.32           C  
ANISOU 4408  C   ILE C 187     9857   3783   6997   -662    573    265       C  
ATOM   4409  O   ILE C 187     -22.861  -9.267   6.196  1.00 53.99           O  
ANISOU 4409  O   ILE C 187     9887   3819   6804   -681    602    277       O  
ATOM   4410  CB  ILE C 187     -22.881 -12.553   5.994  1.00 57.35           C  
ANISOU 4410  CB  ILE C 187    10263   3898   7626   -787    694    404       C  
ATOM   4411  CG1 ILE C 187     -23.716 -13.841   5.740  1.00 59.29           C  
ANISOU 4411  CG1 ILE C 187    10419   3996   8109   -872    819    359       C  
ATOM   4412  CG2 ILE C 187     -22.910 -12.221   7.480  1.00 58.03           C  
ANISOU 4412  CG2 ILE C 187    10517   4032   7497   -836    713    587       C  
ATOM   4413  CD1 ILE C 187     -25.228 -13.694   5.710  1.00 59.60           C  
ANISOU 4413  CD1 ILE C 187    10384   4106   8155   -956    960    241       C  
ATOM   4414  N   TRP C 188     -21.382 -10.056   4.717  1.00 54.04           N  
ANISOU 4414  N   TRP C 188     9783   3729   7019   -581    461    272       N  
ATOM   4415  CA  TRP C 188     -20.574  -8.888   4.753  1.00 54.09           C  
ANISOU 4415  CA  TRP C 188     9808   3804   6938   -512    358    300       C  
ATOM   4416  C   TRP C 188     -21.376  -7.638   4.319  1.00 53.15           C  
ANISOU 4416  C   TRP C 188     9616   3818   6760   -489    398    194       C  
ATOM   4417  O   TRP C 188     -21.428  -6.622   5.034  1.00 52.11           O  
ANISOU 4417  O   TRP C 188     9537   3720   6539   -489    389    200       O  
ATOM   4418  CB  TRP C 188     -19.400  -9.018   3.832  1.00 53.90           C  
ANISOU 4418  CB  TRP C 188     9705   3747   7027   -429    275    306       C  
ATOM   4419  CG  TRP C 188     -18.603  -7.851   3.927  1.00 54.13           C  
ANISOU 4419  CG  TRP C 188     9736   3823   7008   -372    181    350       C  
ATOM   4420  CD1 TRP C 188     -18.815  -6.685   3.284  1.00 53.92           C  
ANISOU 4420  CD1 TRP C 188     9630   3900   6957   -327    187    295       C  
ATOM   4421  CD2 TRP C 188     -17.457  -7.662   4.760  1.00 54.19           C  
ANISOU 4421  CD2 TRP C 188     9811   3764   7012   -360     52    471       C  
ATOM   4422  NE1 TRP C 188     -17.846  -5.778   3.637  1.00 54.44           N  
ANISOU 4422  NE1 TRP C 188     9704   3943   7034   -289     88    360       N  
ATOM   4423  CE2 TRP C 188     -17.017  -6.345   4.563  1.00 53.50           C  
ANISOU 4423  CE2 TRP C 188     9676   3732   6916   -314     -5    452       C  
ATOM   4424  CE3 TRP C 188     -16.743  -8.486   5.622  1.00 55.10           C  
ANISOU 4424  CE3 TRP C 188    10003   3777   7155   -383    -34    611       C  
ATOM   4425  CZ2 TRP C 188     -15.897  -5.817   5.202  1.00 53.59           C  
ANISOU 4425  CZ2 TRP C 188     9713   3701   6947   -302   -148    527       C  
ATOM   4426  CZ3 TRP C 188     -15.639  -7.976   6.271  1.00 56.25           C  
ANISOU 4426  CZ3 TRP C 188    10177   3906   7287   -365   -197    708       C  
ATOM   4427  CH2 TRP C 188     -15.210  -6.635   6.035  1.00 55.80           C  
ANISOU 4427  CH2 TRP C 188    10067   3907   7226   -329   -254    645       C  
ATOM   4428  N   SER C 189     -21.977  -7.719   3.150  1.00 51.25           N  
ANISOU 4428  N   SER C 189     9242   3646   6581   -469    434     96       N  
ATOM   4429  CA  SER C 189     -22.773  -6.622   2.653  1.00 49.93           C  
ANISOU 4429  CA  SER C 189     8975   3598   6398   -439    454     41       C  
ATOM   4430  C   SER C 189     -23.817  -6.242   3.698  1.00 50.91           C  
ANISOU 4430  C   SER C 189     9142   3712   6488   -499    555     15       C  
ATOM   4431  O   SER C 189     -23.987  -5.092   4.002  1.00 50.29           O  
ANISOU 4431  O   SER C 189     9048   3658   6400   -468    565      6       O  
ATOM   4432  CB  SER C 189     -23.438  -7.017   1.351  1.00 49.24           C  
ANISOU 4432  CB  SER C 189     8742   3615   6350   -436    463    -52       C  
ATOM   4433  OG  SER C 189     -22.441  -7.430   0.445  1.00 49.81           O  
ANISOU 4433  OG  SER C 189     8789   3709   6426   -389    406    -58       O  
ATOM   4434  N   ILE C 190     -24.469  -7.227   4.293  1.00 53.61           N  
ANISOU 4434  N   ILE C 190     9533   4001   6833   -587    649      3       N  
ATOM   4435  CA  ILE C 190     -25.523  -6.929   5.247  1.00 54.72           C  
ANISOU 4435  CA  ILE C 190     9702   4149   6938   -651    787    -27       C  
ATOM   4436  C   ILE C 190     -24.951  -6.223   6.455  1.00 54.47           C  
ANISOU 4436  C   ILE C 190     9825   4111   6757   -656    786     13       C  
ATOM   4437  O   ILE C 190     -25.641  -5.453   7.111  1.00 55.15           O  
ANISOU 4437  O   ILE C 190     9919   4230   6804   -676    896    -59       O  
ATOM   4438  CB  ILE C 190     -26.311  -8.186   5.684  1.00 57.72           C  
ANISOU 4438  CB  ILE C 190    10098   4465   7365   -757    912    -17       C  
ATOM   4439  CG1 ILE C 190     -27.146  -8.722   4.513  1.00 60.49           C  
ANISOU 4439  CG1 ILE C 190    10261   4837   7883   -772    919   -124       C  
ATOM   4440  CG2 ILE C 190     -27.292  -7.855   6.792  1.00 58.02           C  
ANISOU 4440  CG2 ILE C 190    10179   4523   7341   -826   1091    -32       C  
ATOM   4441  CD1 ILE C 190     -27.693 -10.163   4.681  1.00 62.87           C  
ANISOU 4441  CD1 ILE C 190    10546   5027   8315   -879   1013   -128       C  
ATOM   4442  N   GLY C 191     -23.729  -6.545   6.815  1.00 54.34           N  
ANISOU 4442  N   GLY C 191     9927   4054   6665   -646    668    113       N  
ATOM   4443  CA  GLY C 191     -23.133  -5.920   8.007  1.00 55.56           C  
ANISOU 4443  CA  GLY C 191    10231   4230   6646   -668    629    136       C  
ATOM   4444  C   GLY C 191     -22.962  -4.449   7.737  1.00 54.48           C  
ANISOU 4444  C   GLY C 191    10023   4117   6559   -602    590     30       C  
ATOM   4445  O   GLY C 191     -23.251  -3.599   8.579  1.00 53.49           O  
ANISOU 4445  O   GLY C 191     9952   4021   6349   -630    655    -70       O  
ATOM   4446  N   THR C 192     -22.496  -4.160   6.510  1.00 52.90           N  
ANISOU 4446  N   THR C 192     9688   3900   6510   -514    498     50       N  
ATOM   4447  CA  THR C 192     -22.172  -2.785   6.082  1.00 49.36           C  
ANISOU 4447  CA  THR C 192     9142   3444   6167   -440    448      9       C  
ATOM   4448  C   THR C 192     -23.470  -2.003   5.996  1.00 50.32           C  
ANISOU 4448  C   THR C 192     9154   3583   6379   -432    585    -91       C  
ATOM   4449  O   THR C 192     -23.546  -0.833   6.460  1.00 50.69           O  
ANISOU 4449  O   THR C 192     9179   3588   6490   -417    618   -180       O  
ATOM   4450  CB  THR C 192     -21.399  -2.732   4.757  1.00 46.47           C  
ANISOU 4450  CB  THR C 192     8655   3081   5921   -354    345     98       C  
ATOM   4451  OG1 THR C 192     -22.008  -3.559   3.777  1.00 44.60           O  
ANISOU 4451  OG1 THR C 192     8334   2903   5706   -348    384    106       O  
ATOM   4452  CG2 THR C 192     -19.944  -3.129   4.931  1.00 45.55           C  
ANISOU 4452  CG2 THR C 192     8608   2912   5784   -345    213    183       C  
ATOM   4453  N   ILE C 193     -24.525  -2.689   5.542  1.00 49.70           N  
ANISOU 4453  N   ILE C 193     9001   3549   6331   -453    673    -99       N  
ATOM   4454  CA  ILE C 193     -25.859  -2.075   5.488  1.00 50.94           C  
ANISOU 4454  CA  ILE C 193     9025   3719   6611   -448    805   -183       C  
ATOM   4455  C   ILE C 193     -26.414  -1.811   6.895  1.00 54.15           C  
ANISOU 4455  C   ILE C 193     9537   4102   6936   -520    970   -303       C  
ATOM   4456  O   ILE C 193     -27.047  -0.789   7.128  1.00 56.48           O  
ANISOU 4456  O   ILE C 193     9740   4361   7356   -494   1073   -408       O  
ATOM   4457  CB  ILE C 193     -26.832  -2.903   4.674  1.00 49.56           C  
ANISOU 4457  CB  ILE C 193     8724   3603   6501   -466    837   -173       C  
ATOM   4458  CG1 ILE C 193     -26.323  -2.999   3.264  1.00 49.15           C  
ANISOU 4458  CG1 ILE C 193     8567   3619   6486   -397    687    -92       C  
ATOM   4459  CG2 ILE C 193     -28.195  -2.222   4.604  1.00 50.87           C  
ANISOU 4459  CG2 ILE C 193     8713   3776   6838   -452    954   -242       C  
ATOM   4460  CD1 ILE C 193     -26.895  -4.151   2.520  1.00 51.11           C  
ANISOU 4460  CD1 ILE C 193     8747   3936   6734   -442    677   -119       C  
ATOM   4461  N   PHE C 194     -26.146  -2.724   7.816  1.00 55.34           N  
ANISOU 4461  N   PHE C 194     9873   4272   6879   -609   1001   -280       N  
ATOM   4462  CA  PHE C 194     -26.617  -2.612   9.165  1.00 57.70           C  
ANISOU 4462  CA  PHE C 194    10301   4600   7022   -693   1168   -375       C  
ATOM   4463  C   PHE C 194     -26.054  -1.309   9.745  1.00 59.05           C  
ANISOU 4463  C   PHE C 194    10516   4751   7167   -668   1140   -510       C  
ATOM   4464  O   PHE C 194     -26.761  -0.513  10.332  1.00 60.04           O  
ANISOU 4464  O   PHE C 194    10613   4868   7330   -683   1307   -682       O  
ATOM   4465  CB  PHE C 194     -26.172  -3.888   9.946  1.00 59.10           C  
ANISOU 4465  CB  PHE C 194    10677   4818   6961   -786   1153   -246       C  
ATOM   4466  CG  PHE C 194     -26.565  -3.934  11.406  1.00 61.37           C  
ANISOU 4466  CG  PHE C 194    11133   5188   6996   -890   1323   -297       C  
ATOM   4467  CD1 PHE C 194     -27.704  -3.297  11.891  1.00 63.05           C  
ANISOU 4467  CD1 PHE C 194    11291   5428   7234   -919   1567   -468       C  
ATOM   4468  CD2 PHE C 194     -25.793  -4.668  12.296  1.00 62.71           C  
ANISOU 4468  CD2 PHE C 194    11510   5420   6896   -961   1245   -155       C  
ATOM   4469  CE1 PHE C 194     -28.047  -3.386  13.238  1.00 66.29           C  
ANISOU 4469  CE1 PHE C 194    11869   5949   7366  -1025   1753   -523       C  
ATOM   4470  CE2 PHE C 194     -26.117  -4.738  13.641  1.00 65.75           C  
ANISOU 4470  CE2 PHE C 194    12067   5930   6982  -1066   1396   -175       C  
ATOM   4471  CZ  PHE C 194     -27.253  -4.107  14.112  1.00 67.27           C  
ANISOU 4471  CZ  PHE C 194    12222   6173   7164  -1102   1666   -370       C  
ATOM   4472  N   ALA C 195     -24.762  -1.087   9.567  1.00 58.34           N  
ANISOU 4472  N   ALA C 195    10479   4637   7050   -633    934   -450       N  
ATOM   4473  CA  ALA C 195     -24.118   0.072  10.156  1.00 59.18           C  
ANISOU 4473  CA  ALA C 195    10624   4709   7151   -629    883   -592       C  
ATOM   4474  C   ALA C 195     -24.728   1.392   9.657  1.00 60.02           C  
ANISOU 4474  C   ALA C 195    10528   4709   7566   -552    974   -721       C  
ATOM   4475  O   ALA C 195     -24.853   2.355  10.407  1.00 63.97           O  
ANISOU 4475  O   ALA C 195    11041   5165   8098   -574   1063   -931       O  
ATOM   4476  CB  ALA C 195     -22.638   0.008   9.863  1.00 58.12           C  
ANISOU 4476  CB  ALA C 195    10527   4548   7006   -601    638   -476       C  
ATOM   4477  N   GLU C 196     -25.130   1.383   8.397  1.00 58.19           N  
ANISOU 4477  N   GLU C 196    10106   4441   7559   -466    952   -593       N  
ATOM   4478  CA  GLU C 196     -25.703   2.514   7.729  1.00 57.73           C  
ANISOU 4478  CA  GLU C 196     9824   4283   7827   -376   1004   -623       C  
ATOM   4479  C   GLU C 196     -27.084   2.778   8.219  1.00 59.37           C  
ANISOU 4479  C   GLU C 196     9953   4475   8131   -395   1235   -773       C  
ATOM   4480  O   GLU C 196     -27.480   3.950   8.360  1.00 65.13           O  
ANISOU 4480  O   GLU C 196    10548   5080   9118   -348   1333   -904       O  
ATOM   4481  CB  GLU C 196     -25.741   2.238   6.221  1.00 57.34           C  
ANISOU 4481  CB  GLU C 196     9610   4266   7910   -292    889   -404       C  
ATOM   4482  CG  GLU C 196     -25.982   3.448   5.313  1.00 57.64           C  
ANISOU 4482  CG  GLU C 196     9405   4211   8283   -181    868   -325       C  
ATOM   4483  CD  GLU C 196     -25.517   3.246   3.871  1.00 56.21           C  
ANISOU 4483  CD  GLU C 196     9117   4108   8130   -108    710    -83       C  
ATOM   4484  OE1 GLU C 196     -24.667   2.349   3.629  1.00 56.13           O  
ANISOU 4484  OE1 GLU C 196     9230   4183   7912   -136    609    -16       O  
ATOM   4485  OE2 GLU C 196     -26.065   3.924   2.975  1.00 55.47           O  
ANISOU 4485  OE2 GLU C 196     8809   4006   8259    -23    696     43       O  
ATOM   4486  N   LEU C 197     -27.852   1.728   8.454  1.00 57.76           N  
ANISOU 4486  N   LEU C 197     9800   4368   7776   -460   1340   -757       N  
ATOM   4487  CA  LEU C 197     -29.182   1.889   9.004  1.00 59.52           C  
ANISOU 4487  CA  LEU C 197     9942   4581   8091   -490   1592   -902       C  
ATOM   4488  C   LEU C 197     -29.125   2.662  10.326  1.00 63.41           C  
ANISOU 4488  C   LEU C 197    10553   5042   8495   -544   1756  -1161       C  
ATOM   4489  O   LEU C 197     -30.029   3.431  10.647  1.00 66.43           O  
ANISOU 4489  O   LEU C 197    10802   5345   9091   -524   1967  -1338       O  
ATOM   4490  CB  LEU C 197     -29.840   0.541   9.241  1.00 59.28           C  
ANISOU 4490  CB  LEU C 197     9981   4656   7884   -580   1688   -840       C  
ATOM   4491  CG  LEU C 197     -30.392  -0.241   8.040  1.00 57.95           C  
ANISOU 4491  CG  LEU C 197     9646   4518   7853   -552   1602   -680       C  
ATOM   4492  CD1 LEU C 197     -30.668  -1.682   8.459  1.00 58.63           C  
ANISOU 4492  CD1 LEU C 197     9854   4673   7747   -665   1674   -624       C  
ATOM   4493  CD2 LEU C 197     -31.676   0.365   7.539  1.00 58.74           C  
ANISOU 4493  CD2 LEU C 197     9464   4570   8282   -495   1710   -723       C  
ATOM   4494  N   ALA C 198     -28.079   2.424  11.110  1.00 64.34           N  
ANISOU 4494  N   ALA C 198    10914   5233   8298   -617   1662  -1196       N  
ATOM   4495  CA  ALA C 198     -27.952   3.056  12.393  1.00 68.52           C  
ANISOU 4495  CA  ALA C 198    11584   5786   8661   -691   1791  -1465       C  
ATOM   4496  C   ALA C 198     -27.541   4.530  12.196  1.00 71.49           C  
ANISOU 4496  C   ALA C 198    11825   5983   9353   -617   1745  -1634       C  
ATOM   4497  O   ALA C 198     -28.236   5.450  12.677  1.00 74.43           O  
ANISOU 4497  O   ALA C 198    12102   6260   9916   -610   1962  -1897       O  
ATOM   4498  CB  ALA C 198     -26.922   2.328  13.245  1.00 68.61           C  
ANISOU 4498  CB  ALA C 198    11882   5955   8230   -794   1653  -1419       C  
ATOM   4499  N   THR C 199     -26.432   4.709  11.475  1.00 68.33           N  
ANISOU 4499  N   THR C 199    11399   5520   9040   -562   1482  -1479       N  
ATOM   4500  CA  THR C 199     -25.767   5.978  11.370  1.00 69.20           C  
ANISOU 4500  CA  THR C 199    11411   5456   9425   -515   1404  -1603       C  
ATOM   4501  C   THR C 199     -26.291   6.930  10.276  1.00 69.62           C  
ANISOU 4501  C   THR C 199    11154   5301   9997   -380   1437  -1516       C  
ATOM   4502  O   THR C 199     -25.970   8.126  10.308  1.00 70.06           O  
ANISOU 4502  O   THR C 199    11091   5159  10366   -342   1439  -1650       O  
ATOM   4503  CB  THR C 199     -24.257   5.781  11.097  1.00 67.29           C  
ANISOU 4503  CB  THR C 199    11259   5230   9078   -522   1113  -1453       C  
ATOM   4504  OG1 THR C 199     -24.067   5.145   9.832  1.00 63.84           O  
ANISOU 4504  OG1 THR C 199    10728   4810   8718   -442    982  -1127       O  
ATOM   4505  CG2 THR C 199     -23.620   4.984  12.188  1.00 67.81           C  
ANISOU 4505  CG2 THR C 199    11601   5483   8678   -647   1033  -1512       C  
ATOM   4506  N   LYS C 200     -27.034   6.388   9.305  1.00 68.74           N  
ANISOU 4506  N   LYS C 200    10906   5232   9979   -312   1442  -1279       N  
ATOM   4507  CA  LYS C 200     -27.370   7.065   8.041  1.00 67.86           C  
ANISOU 4507  CA  LYS C 200    10508   4990  10283   -179   1390  -1075       C  
ATOM   4508  C   LYS C 200     -26.211   7.154   7.078  1.00 67.12           C  
ANISOU 4508  C   LYS C 200    10387   4884  10229   -125   1150   -824       C  
ATOM   4509  O   LYS C 200     -26.448   7.310   5.892  1.00 68.79           O  
ANISOU 4509  O   LYS C 200    10408   5089  10637    -30   1077   -573       O  
ATOM   4510  CB  LYS C 200     -28.006   8.444   8.239  1.00 69.21           C  
ANISOU 4510  CB  LYS C 200    10460   4922  10912   -114   1556  -1248       C  
ATOM   4511  CG  LYS C 200     -29.152   8.482   9.215  1.00 70.95           C  
ANISOU 4511  CG  LYS C 200    10680   5136  11139   -161   1841  -1534       C  
ATOM   4512  CD  LYS C 200     -29.868   9.829   9.268  1.00 74.50           C  
ANISOU 4512  CD  LYS C 200    10858   5314  12133    -75   2022  -1695       C  
ATOM   4513  CE  LYS C 200     -29.042  10.958   9.911  1.00 77.64           C  
ANISOU 4513  CE  LYS C 200    11281   5504  12713    -95   2039  -1965       C  
ATOM   4514  NZ  LYS C 200     -29.712  12.313  10.054  1.00 80.69           N  
ANISOU 4514  NZ  LYS C 200    11391   5569  13698    -14   2246  -2172       N  
ATOM   4515  N   LYS C 201     -24.976   6.991   7.533  1.00 69.52           N  
ANISOU 4515  N   LYS C 201    10871   5211  10330   -187   1023   -869       N  
ATOM   4516  CA  LYS C 201     -23.776   7.042   6.656  1.00 71.78           C  
ANISOU 4516  CA  LYS C 201    11125   5483  10665   -142    817   -636       C  
ATOM   4517  C   LYS C 201     -23.251   5.666   6.230  1.00 65.91           C  
ANISOU 4517  C   LYS C 201    10521   4937   9581   -169    689   -458       C  
ATOM   4518  O   LYS C 201     -23.284   4.720   6.985  1.00 63.57           O  
ANISOU 4518  O   LYS C 201    10418   4760   8976   -254    704   -546       O  
ATOM   4519  CB  LYS C 201     -22.617   7.693   7.377  1.00 79.28           C  
ANISOU 4519  CB  LYS C 201    12150   6315  11654   -195    734   -792       C  
ATOM   4520  CG  LYS C 201     -22.800   9.171   7.674  1.00 89.71           C  
ANISOU 4520  CG  LYS C 201    13308   7382  13396   -167    831   -977       C  
ATOM   4521  CD  LYS C 201     -22.698   9.484   9.172  1.00101.32           C  
ANISOU 4521  CD  LYS C 201    14936   8826  14733   -284    906  -1387       C  
ATOM   4522  CE  LYS C 201     -21.481   8.863   9.899  1.00108.65           C  
ANISOU 4522  CE  LYS C 201    16099   9894  15286   -394    719  -1454       C  
ATOM   4523  NZ  LYS C 201     -20.329   9.800  10.027  1.00116.79           N  
ANISOU 4523  NZ  LYS C 201    17061  10746  16567   -418    580  -1550       N  
ATOM   4524  N   PRO C 202     -22.739   5.561   5.005  1.00 63.76           N  
ANISOU 4524  N   PRO C 202    10146   4699   9381    -97    573   -201       N  
ATOM   4525  CA  PRO C 202     -22.045   4.359   4.588  1.00 60.50           C  
ANISOU 4525  CA  PRO C 202     9848   4434   8703   -118    462    -71       C  
ATOM   4526  C   PRO C 202     -20.867   4.141   5.465  1.00 59.25           C  
ANISOU 4526  C   PRO C 202     9856   4249   8407   -188    365   -158       C  
ATOM   4527  O   PRO C 202     -20.254   5.089   5.896  1.00 60.27           O  
ANISOU 4527  O   PRO C 202     9955   4246   8698   -196    328   -244       O  
ATOM   4528  CB  PRO C 202     -21.552   4.722   3.206  1.00 60.72           C  
ANISOU 4528  CB  PRO C 202     9711   4472   8888    -26    384    178       C  
ATOM   4529  CG  PRO C 202     -22.644   5.569   2.662  1.00 62.45           C  
ANISOU 4529  CG  PRO C 202     9727   4646   9354     44    463    244       C  
ATOM   4530  CD  PRO C 202     -22.979   6.449   3.856  1.00 64.75           C  
ANISOU 4530  CD  PRO C 202    10026   4750   9823     11    566      2       C  
ATOM   4531  N   LEU C 203     -20.568   2.888   5.759  1.00 58.41           N  
ANISOU 4531  N   LEU C 203     9908   4257   8025   -242    314   -137       N  
ATOM   4532  CA  LEU C 203     -19.542   2.559   6.773  1.00 56.62           C  
ANISOU 4532  CA  LEU C 203     9848   4029   7634   -317    200   -205       C  
ATOM   4533  C   LEU C 203     -18.133   2.619   6.210  1.00 53.60           C  
ANISOU 4533  C   LEU C 203     9407   3598   7360   -280     43    -65       C  
ATOM   4534  O   LEU C 203     -17.250   3.200   6.820  1.00 52.79           O  
ANISOU 4534  O   LEU C 203     9320   3417   7320   -315    -62   -137       O  
ATOM   4535  CB  LEU C 203     -19.786   1.181   7.308  1.00 56.56           C  
ANISOU 4535  CB  LEU C 203    10010   4141   7340   -382    210   -185       C  
ATOM   4536  CG  LEU C 203     -18.749   0.714   8.326  1.00 59.15           C  
ANISOU 4536  CG  LEU C 203    10501   4493   7478   -455     63   -191       C  
ATOM   4537  CD1 LEU C 203     -18.686   1.644   9.538  1.00 62.97           C  
ANISOU 4537  CD1 LEU C 203    11066   4967   7892   -529     55   -409       C  
ATOM   4538  CD2 LEU C 203     -19.065  -0.703   8.793  1.00 58.89           C  
ANISOU 4538  CD2 LEU C 203    10615   4557   7202   -511     87   -109       C  
ATOM   4539  N   PHE C 204     -17.994   2.057   5.011  1.00 51.26           N  
ANISOU 4539  N   PHE C 204     9025   3353   7095   -214     42    114       N  
ATOM   4540  CA  PHE C 204     -16.786   2.063   4.288  1.00 50.80           C  
ANISOU 4540  CA  PHE C 204     8884   3264   7153   -167    -51    258       C  
ATOM   4541  C   PHE C 204     -17.011   2.746   2.980  1.00 54.24           C  
ANISOU 4541  C   PHE C 204     9135   3705   7769    -80     14    399       C  
ATOM   4542  O   PHE C 204     -17.443   2.109   2.015  1.00 57.35           O  
ANISOU 4542  O   PHE C 204     9491   4225   8073    -41     64    492       O  
ATOM   4543  CB  PHE C 204     -16.383   0.646   4.076  1.00 49.25           C  
ANISOU 4543  CB  PHE C 204     8767   3148   6797   -173    -88    332       C  
ATOM   4544  CG  PHE C 204     -16.129  -0.107   5.349  1.00 48.97           C  
ANISOU 4544  CG  PHE C 204     8906   3113   6584   -255   -169    265       C  
ATOM   4545  CD1 PHE C 204     -15.167   0.337   6.248  1.00 49.40           C  
ANISOU 4545  CD1 PHE C 204     9001   3105   6663   -298   -314    225       C  
ATOM   4546  CD2 PHE C 204     -16.837  -1.289   5.635  1.00 48.76           C  
ANISOU 4546  CD2 PHE C 204     8993   3158   6373   -294   -111    260       C  
ATOM   4547  CE1 PHE C 204     -14.938  -0.345   7.422  1.00 51.08           C  
ANISOU 4547  CE1 PHE C 204     9375   3359   6671   -375   -412    200       C  
ATOM   4548  CE2 PHE C 204     -16.598  -2.002   6.810  1.00 49.77           C  
ANISOU 4548  CE2 PHE C 204     9280   3298   6331   -368   -185    260       C  
ATOM   4549  CZ  PHE C 204     -15.646  -1.531   7.713  1.00 51.00           C  
ANISOU 4549  CZ  PHE C 204     9488   3426   6463   -407   -343    241       C  
ATOM   4550  N   HIS C 205     -16.673   4.049   2.912  1.00 57.41           N  
ANISOU 4550  N   HIS C 205     9407   3971   8433    -54      8    426       N  
ATOM   4551  CA  HIS C 205     -17.121   4.937   1.861  1.00 57.76           C  
ANISOU 4551  CA  HIS C 205     9265   4000   8681     25     81    585       C  
ATOM   4552  C   HIS C 205     -16.020   5.196   0.835  1.00 56.04           C  
ANISOU 4552  C   HIS C 205     8916   3777   8597     79     56    811       C  
ATOM   4553  O   HIS C 205     -15.634   6.310   0.619  1.00 61.19           O  
ANISOU 4553  O   HIS C 205     9423   4287   9538    107     65    909       O  
ATOM   4554  CB  HIS C 205     -17.532   6.264   2.527  1.00 63.04           C  
ANISOU 4554  CB  HIS C 205     9855   4473   9621     17    118    468       C  
ATOM   4555  CG  HIS C 205     -18.316   7.170   1.637  1.00 66.52           C  
ANISOU 4555  CG  HIS C 205    10097   4874  10301    102    200    636       C  
ATOM   4556  ND1 HIS C 205     -17.745   8.223   0.967  1.00 69.53           N  
ANISOU 4556  ND1 HIS C 205    10289   5121  11005    158    201    838       N  
ATOM   4557  CD2 HIS C 205     -19.611   7.128   1.239  1.00 68.11           C  
ANISOU 4557  CD2 HIS C 205    10241   5162  10476    143    273    675       C  
ATOM   4558  CE1 HIS C 205     -18.673   8.827   0.236  1.00 73.89           C  
ANISOU 4558  CE1 HIS C 205    10682   5675  11717    235    266   1008       C  
ATOM   4559  NE2 HIS C 205     -19.812   8.176   0.382  1.00 70.72           N  
ANISOU 4559  NE2 HIS C 205    10351   5412  11106    228    299    905       N  
ATOM   4560  N   GLY C 206     -15.547   4.194   0.152  1.00 52.57           N  
ANISOU 4560  N   GLY C 206     8511   3485   7976     94     51    897       N  
ATOM   4561  CA  GLY C 206     -14.313   4.308  -0.633  1.00 51.41           C  
ANISOU 4561  CA  GLY C 206     8258   3334   7941    131     50   1074       C  
ATOM   4562  C   GLY C 206     -14.517   4.827  -2.015  1.00 51.57           C  
ANISOU 4562  C   GLY C 206     8122   3468   8003    205    139   1322       C  
ATOM   4563  O   GLY C 206     -15.594   4.679  -2.560  1.00 49.73           O  
ANISOU 4563  O   GLY C 206     7884   3387   7622    231    176   1357       O  
ATOM   4564  N   ASP C 207     -13.468   5.427  -2.574  1.00 53.70           N  
ANISOU 4564  N   ASP C 207     8255   3674   8472    235    167   1509       N  
ATOM   4565  CA  ASP C 207     -13.513   6.035  -3.924  1.00 56.64           C  
ANISOU 4565  CA  ASP C 207     8468   4169   8884    304    263   1812       C  
ATOM   4566  C   ASP C 207     -13.091   5.053  -5.022  1.00 55.58           C  
ANISOU 4566  C   ASP C 207     8352   4301   8464    328    341   1890       C  
ATOM   4567  O   ASP C 207     -13.235   5.350  -6.230  1.00 58.90           O  
ANISOU 4567  O   ASP C 207     8672   4917   8789    376    424   2132       O  
ATOM   4568  CB  ASP C 207     -12.680   7.353  -4.023  1.00 59.59           C  
ANISOU 4568  CB  ASP C 207     8652   4321   9668    320    292   2017       C  
ATOM   4569  CG  ASP C 207     -11.164   7.181  -3.740  1.00 62.87           C  
ANISOU 4569  CG  ASP C 207     9033   4612  10242    286    277   1990       C  
ATOM   4570  OD1 ASP C 207     -10.424   6.489  -4.452  1.00 66.31           O  
ANISOU 4570  OD1 ASP C 207     9457   5194  10544    304    348   2071       O  
ATOM   4571  OD2 ASP C 207     -10.661   7.756  -2.751  1.00 68.59           O  
ANISOU 4571  OD2 ASP C 207     9729   5080  11252    235    190   1864       O  
ATOM   4572  N   SER C 208     -12.473   3.955  -4.608  1.00 50.96           N  
ANISOU 4572  N   SER C 208     7877   3716   7769    293    319   1700       N  
ATOM   4573  CA  SER C 208     -11.900   2.988  -5.509  1.00 49.72           C  
ANISOU 4573  CA  SER C 208     7726   3752   7411    312    413   1708       C  
ATOM   4574  C   SER C 208     -11.793   1.655  -4.772  1.00 48.79           C  
ANISOU 4574  C   SER C 208     7757   3596   7182    271    357   1444       C  
ATOM   4575  O   SER C 208     -11.924   1.604  -3.557  1.00 46.79           O  
ANISOU 4575  O   SER C 208     7592   3170   7014    228    242   1310       O  
ATOM   4576  CB  SER C 208     -10.526   3.441  -5.976  1.00 49.91           C  
ANISOU 4576  CB  SER C 208     7603   3710   7649    337    501   1887       C  
ATOM   4577  OG  SER C 208      -9.745   3.707  -4.851  1.00 48.00           O  
ANISOU 4577  OG  SER C 208     7347   3188   7700    301    396   1806       O  
ATOM   4578  N   GLU C 209     -11.518   0.595  -5.521  1.00 50.10           N  
ANISOU 4578  N   GLU C 209     7944   3923   7168    284    448   1375       N  
ATOM   4579  CA  GLU C 209     -11.307  -0.714  -4.928  1.00 50.21           C  
ANISOU 4579  CA  GLU C 209     8065   3866   7145    255    414   1161       C  
ATOM   4580  C   GLU C 209     -10.247  -0.651  -3.889  1.00 47.86           C  
ANISOU 4580  C   GLU C 209     7752   3317   7112    242    317   1160       C  
ATOM   4581  O   GLU C 209     -10.456  -1.066  -2.765  1.00 46.00           O  
ANISOU 4581  O   GLU C 209     7627   2958   6893    198    192   1047       O  
ATOM   4582  CB  GLU C 209     -10.841  -1.725  -5.943  1.00 54.19           C  
ANISOU 4582  CB  GLU C 209     8541   4522   7525    280    557   1085       C  
ATOM   4583  CG  GLU C 209     -11.914  -2.540  -6.641  1.00 56.62           C  
ANISOU 4583  CG  GLU C 209     8921   5058   7534    259    606    927       C  
ATOM   4584  CD  GLU C 209     -11.316  -3.796  -7.266  1.00 59.32           C  
ANISOU 4584  CD  GLU C 209     9253   5456   7828    267    737    747       C  
ATOM   4585  OE1 GLU C 209     -10.811  -4.658  -6.531  1.00 58.36           O  
ANISOU 4585  OE1 GLU C 209     9164   5123   7885    260    707    631       O  
ATOM   4586  OE2 GLU C 209     -11.294  -3.854  -8.501  1.00 64.41           O  
ANISOU 4586  OE2 GLU C 209     9846   6357   8270    284    874    737       O  
ATOM   4587  N   ILE C 210      -9.128  -0.053  -4.252  1.00 47.84           N  
ANISOU 4587  N   ILE C 210     7603   3254   7319    273    367   1305       N  
ATOM   4588  CA  ILE C 210      -7.998   0.048  -3.317  1.00 48.42           C  
ANISOU 4588  CA  ILE C 210     7622   3093   7680    256    250   1310       C  
ATOM   4589  C   ILE C 210      -8.268   0.950  -2.095  1.00 47.71           C  
ANISOU 4589  C   ILE C 210     7577   2842   7706    201     70   1287       C  
ATOM   4590  O   ILE C 210      -7.915   0.585  -0.975  1.00 48.63           O  
ANISOU 4590  O   ILE C 210     7759   2832   7883    158    -90   1192       O  
ATOM   4591  CB  ILE C 210      -6.695   0.416  -4.040  1.00 49.90           C  
ANISOU 4591  CB  ILE C 210     7608   3244   8105    297    365   1463       C  
ATOM   4592  CG1 ILE C 210      -5.504   0.252  -3.130  1.00 50.36           C  
ANISOU 4592  CG1 ILE C 210     7590   3077   8467    280    226   1446       C  
ATOM   4593  CG2 ILE C 210      -6.746   1.843  -4.527  1.00 51.87           C  
ANISOU 4593  CG2 ILE C 210     7738   3500   8470    304    423   1665       C  
ATOM   4594  CD1 ILE C 210      -5.202  -1.180  -2.721  1.00 50.58           C  
ANISOU 4594  CD1 ILE C 210     7682   3062   8473    290    177   1316       C  
ATOM   4595  N   ASP C 211      -8.951   2.062  -2.309  1.00 47.23           N  
ANISOU 4595  N   ASP C 211     7485   2800   7659    200     98   1362       N  
ATOM   4596  CA  ASP C 211      -9.377   2.911  -1.219  1.00 47.45           C  
ANISOU 4596  CA  ASP C 211     7557   2683   7787    147    -33   1283       C  
ATOM   4597  C   ASP C 211     -10.403   2.241  -0.343  1.00 46.78           C  
ANISOU 4597  C   ASP C 211     7672   2642   7458    103   -105   1096       C  
ATOM   4598  O   ASP C 211     -10.431   2.434   0.870  1.00 46.89           O  
ANISOU 4598  O   ASP C 211     7769   2549   7496     42   -237    967       O  
ATOM   4599  CB  ASP C 211      -9.952   4.224  -1.770  1.00 48.28           C  
ANISOU 4599  CB  ASP C 211     7553   2774   8015    172     45   1421       C  
ATOM   4600  CG  ASP C 211     -10.290   5.226  -0.682  1.00 48.72           C  
ANISOU 4600  CG  ASP C 211     7618   2637   8254    119    -59   1304       C  
ATOM   4601  OD1 ASP C 211      -9.405   5.602   0.114  1.00 50.46           O  
ANISOU 4601  OD1 ASP C 211     7796   2682   8693     68   -175   1229       O  
ATOM   4602  OD2 ASP C 211     -11.456   5.650  -0.599  1.00 48.27           O  
ANISOU 4602  OD2 ASP C 211     7600   2603   8136    124    -26   1265       O  
ATOM   4603  N   GLN C 212     -11.301   1.485  -0.953  1.00 46.64           N  
ANISOU 4603  N   GLN C 212     7727   2796   7196    126    -14   1073       N  
ATOM   4604  CA  GLN C 212     -12.230   0.673  -0.165  1.00 46.36           C  
ANISOU 4604  CA  GLN C 212     7866   2795   6951     78    -59    911       C  
ATOM   4605  C   GLN C 212     -11.481  -0.239   0.775  1.00 47.73           C  
ANISOU 4605  C   GLN C 212     8128   2881   7126     40   -173    843       C  
ATOM   4606  O   GLN C 212     -11.888  -0.424   1.938  1.00 48.54           O  
ANISOU 4606  O   GLN C 212     8364   2945   7133    -22   -266    742       O  
ATOM   4607  CB  GLN C 212     -13.072  -0.213  -1.064  1.00 45.54           C  
ANISOU 4607  CB  GLN C 212     7796   2875   6632    100     47    886       C  
ATOM   4608  CG  GLN C 212     -14.224  -0.832  -0.330  1.00 44.63           C  
ANISOU 4608  CG  GLN C 212     7823   2782   6349     46     29    743       C  
ATOM   4609  CD  GLN C 212     -15.228   0.199   0.083  1.00 45.37           C  
ANISOU 4609  CD  GLN C 212     7916   2861   6460     30     31    720       C  
ATOM   4610  OE1 GLN C 212     -15.392   1.235  -0.594  1.00 46.00           O  
ANISOU 4610  OE1 GLN C 212     7869   2961   6645     76     69    831       O  
ATOM   4611  NE2 GLN C 212     -15.975  -0.097   1.104  1.00 45.25           N  
ANISOU 4611  NE2 GLN C 212     8025   2815   6353    -28     12    593       N  
ATOM   4612  N   LEU C 213     -10.450  -0.927   0.256  1.00 47.99           N  
ANISOU 4612  N   LEU C 213     8084   2898   7249     78   -155    905       N  
ATOM   4613  CA  LEU C 213      -9.733  -1.854   1.118  1.00 48.80           C  
ANISOU 4613  CA  LEU C 213     8244   2903   7395     53   -278    881       C  
ATOM   4614  C   LEU C 213      -9.111  -1.118   2.265  1.00 49.39           C  
ANISOU 4614  C   LEU C 213     8320   2861   7585      2   -467    881       C  
ATOM   4615  O   LEU C 213      -9.211  -1.542   3.417  1.00 49.91           O  
ANISOU 4615  O   LEU C 213     8514   2904   7545    -55   -607    830       O  
ATOM   4616  CB  LEU C 213      -8.645  -2.593   0.345  1.00 50.56           C  
ANISOU 4616  CB  LEU C 213     8339   3095   7776    115   -213    945       C  
ATOM   4617  CG  LEU C 213      -9.134  -3.732  -0.587  1.00 50.08           C  
ANISOU 4617  CG  LEU C 213     8299   3136   7590    148    -48    874       C  
ATOM   4618  CD1 LEU C 213      -8.054  -4.132  -1.562  1.00 50.59           C  
ANISOU 4618  CD1 LEU C 213     8204   3189   7825    216     77    909       C  
ATOM   4619  CD2 LEU C 213      -9.613  -4.894   0.236  1.00 49.64           C  
ANISOU 4619  CD2 LEU C 213     8382   3023   7456    109   -115    803       C  
ATOM   4620  N   PHE C 214      -8.501   0.005   1.951  1.00 49.85           N  
ANISOU 4620  N   PHE C 214     8232   2855   7853     14   -470    937       N  
ATOM   4621  CA  PHE C 214      -7.867   0.788   2.977  1.00 50.99           C  
ANISOU 4621  CA  PHE C 214     8351   2882   8142    -46   -657    896       C  
ATOM   4622  C   PHE C 214      -8.855   1.285   4.007  1.00 50.50           C  
ANISOU 4622  C   PHE C 214     8448   2843   7897   -121   -720    740       C  
ATOM   4623  O   PHE C 214      -8.532   1.382   5.172  1.00 49.98           O  
ANISOU 4623  O   PHE C 214     8453   2745   7792   -195   -904    651       O  
ATOM   4624  CB  PHE C 214      -7.130   1.928   2.340  1.00 52.46           C  
ANISOU 4624  CB  PHE C 214     8326   2969   8635    -23   -615    984       C  
ATOM   4625  CG  PHE C 214      -5.851   1.539   1.651  1.00 53.60           C  
ANISOU 4625  CG  PHE C 214     8291   3062   9011     28   -583   1122       C  
ATOM   4626  CD1 PHE C 214      -5.452   0.226   1.515  1.00 53.49           C  
ANISOU 4626  CD1 PHE C 214     8297   3081   8945     67   -577   1147       C  
ATOM   4627  CD2 PHE C 214      -5.072   2.532   1.066  1.00 55.05           C  
ANISOU 4627  CD2 PHE C 214     8260   3147   9509     43   -526   1233       C  
ATOM   4628  CE1 PHE C 214      -4.273  -0.080   0.870  1.00 54.60           C  
ANISOU 4628  CE1 PHE C 214     8245   3158   9340    121   -517   1254       C  
ATOM   4629  CE2 PHE C 214      -3.881   2.228   0.426  1.00 55.80           C  
ANISOU 4629  CE2 PHE C 214     8166   3193   9842     89   -464   1360       C  
ATOM   4630  CZ  PHE C 214      -3.485   0.920   0.332  1.00 55.87           C  
ANISOU 4630  CZ  PHE C 214     8196   3240   9790    131   -456   1358       C  
ATOM   4631  N   ARG C 215     -10.069   1.558   3.593  1.00 51.50           N  
ANISOU 4631  N   ARG C 215     8625   3042   7898   -105   -569    701       N  
ATOM   4632  CA  ARG C 215     -11.036   2.072   4.555  1.00 55.35           C  
ANISOU 4632  CA  ARG C 215     9242   3541   8246   -171   -588    533       C  
ATOM   4633  C   ARG C 215     -11.394   1.026   5.552  1.00 55.14           C  
ANISOU 4633  C   ARG C 215     9412   3598   7937   -229   -660    464       C  
ATOM   4634  O   ARG C 215     -11.363   1.252   6.748  1.00 58.94           O  
ANISOU 4634  O   ARG C 215    10000   4083   8310   -311   -782    343       O  
ATOM   4635  CB  ARG C 215     -12.282   2.619   3.864  1.00 56.58           C  
ANISOU 4635  CB  ARG C 215     9371   3741   8385   -132   -408    526       C  
ATOM   4636  CG  ARG C 215     -12.274   4.142   3.846  1.00 61.46           C  
ANISOU 4636  CG  ARG C 215     9856   4221   9272   -132   -390    493       C  
ATOM   4637  CD  ARG C 215     -12.562   4.694   2.481  1.00 65.10           C  
ANISOU 4637  CD  ARG C 215    10152   4690   9890    -44   -248    680       C  
ATOM   4638  NE  ARG C 215     -12.033   6.029   2.378  1.00 71.57           N  
ANISOU 4638  NE  ARG C 215    10801   5327  11065    -40   -255    725       N  
ATOM   4639  CZ  ARG C 215     -12.679   7.134   2.690  1.00 74.71           C  
ANISOU 4639  CZ  ARG C 215    11140   5595  11651    -50   -212    638       C  
ATOM   4640  NH1 ARG C 215     -13.922   7.112   3.130  1.00 77.83           N  
ANISOU 4640  NH1 ARG C 215    11632   6037  11901    -59   -150    497       N  
ATOM   4641  NH2 ARG C 215     -12.063   8.293   2.557  1.00 78.05           N  
ANISOU 4641  NH2 ARG C 215    11382   5813  12457    -50   -218    691       N  
ATOM   4642  N   ILE C 216     -11.678  -0.143   5.024  1.00 54.50           N  
ANISOU 4642  N   ILE C 216     9372   3588   7745   -191   -583    548       N  
ATOM   4643  CA  ILE C 216     -11.903  -1.341   5.807  1.00 53.48           C  
ANISOU 4643  CA  ILE C 216     9401   3511   7408   -236   -637    552       C  
ATOM   4644  C   ILE C 216     -10.767  -1.630   6.765  1.00 54.61           C  
ANISOU 4644  C   ILE C 216     9570   3611   7569   -277   -862    605       C  
ATOM   4645  O   ILE C 216     -11.005  -1.793   7.965  1.00 56.73           O  
ANISOU 4645  O   ILE C 216     9991   3939   7623   -358   -965    558       O  
ATOM   4646  CB  ILE C 216     -12.080  -2.536   4.876  1.00 52.49           C  
ANISOU 4646  CB  ILE C 216     9251   3409   7283   -179   -523    635       C  
ATOM   4647  CG1 ILE C 216     -13.471  -2.489   4.232  1.00 51.01           C  
ANISOU 4647  CG1 ILE C 216     9082   3311   6986   -170   -341    564       C  
ATOM   4648  CG2 ILE C 216     -11.906  -3.846   5.649  1.00 54.87           C  
ANISOU 4648  CG2 ILE C 216     9663   3694   7491   -213   -605    701       C  
ATOM   4649  CD1 ILE C 216     -13.619  -3.264   2.942  1.00 49.84           C  
ANISOU 4649  CD1 ILE C 216     8854   3211   6871   -111   -219    594       C  
ATOM   4650  N   PHE C 217      -9.538  -1.659   6.257  1.00 54.21           N  
ANISOU 4650  N   PHE C 217     9360   3471   7765   -226   -941    708       N  
ATOM   4651  CA  PHE C 217      -8.387  -1.892   7.121  1.00 56.46           C  
ANISOU 4651  CA  PHE C 217     9626   3710   8116   -261  -1189    777       C  
ATOM   4652  C   PHE C 217      -8.281  -0.841   8.217  1.00 61.33           C  
ANISOU 4652  C   PHE C 217    10298   4353   8650   -358  -1358    635       C  
ATOM   4653  O   PHE C 217      -8.035  -1.207   9.354  1.00 63.77           O  
ANISOU 4653  O   PHE C 217    10719   4729   8778   -429  -1555    645       O  
ATOM   4654  CB  PHE C 217      -7.054  -1.953   6.367  1.00 55.55           C  
ANISOU 4654  CB  PHE C 217     9285   3476   8342   -189  -1231    897       C  
ATOM   4655  CG  PHE C 217      -7.020  -2.908   5.190  1.00 53.91           C  
ANISOU 4655  CG  PHE C 217     8998   3243   8241    -94  -1041    986       C  
ATOM   4656  CD1 PHE C 217      -7.951  -3.965   5.035  1.00 52.55           C  
ANISOU 4656  CD1 PHE C 217     8952   3125   7888    -84   -914    978       C  
ATOM   4657  CD2 PHE C 217      -5.975  -2.823   4.272  1.00 53.89           C  
ANISOU 4657  CD2 PHE C 217     8779   3154   8541    -21   -986   1063       C  
ATOM   4658  CE1 PHE C 217      -7.876  -4.804   3.955  1.00 50.93           C  
ANISOU 4658  CE1 PHE C 217     8662   2893   7794     -8   -744   1002       C  
ATOM   4659  CE2 PHE C 217      -5.879  -3.695   3.195  1.00 51.92           C  
ANISOU 4659  CE2 PHE C 217     8453   2896   8377     59   -794   1100       C  
ATOM   4660  CZ  PHE C 217      -6.845  -4.651   3.025  1.00 51.37           C  
ANISOU 4660  CZ  PHE C 217     8516   2886   8115     63   -678   1050       C  
ATOM   4661  N   ARG C 218      -8.480   0.448   7.906  1.00 63.13           N  
ANISOU 4661  N   ARG C 218    10447   4531   9007   -366  -1284    504       N  
ATOM   4662  CA  ARG C 218      -8.294   1.490   8.942  1.00 70.24           C  
ANISOU 4662  CA  ARG C 218    11376   5426   9882   -467  -1442    313       C  
ATOM   4663  C   ARG C 218      -9.165   1.168  10.159  1.00 66.37           C  
ANISOU 4663  C   ARG C 218    11135   5097   8983   -558  -1474    187       C  
ATOM   4664  O   ARG C 218      -8.791   1.520  11.278  1.00 69.40           O  
ANISOU 4664  O   ARG C 218    11592   5546   9229   -658  -1675     58       O  
ATOM   4665  CB  ARG C 218      -8.509   2.964   8.396  1.00 78.58           C  
ANISOU 4665  CB  ARG C 218    12293   6357  11204   -458  -1319    183       C  
ATOM   4666  CG  ARG C 218      -8.057   4.141   9.263  1.00 88.64           C  
ANISOU 4666  CG  ARG C 218    13523   7556  12597   -559  -1479    -42       C  
ATOM   4667  CD  ARG C 218      -7.725   5.437   8.460  1.00106.11           C  
ANISOU 4667  CD  ARG C 218    15497   9558  15261   -529  -1390    -58       C  
ATOM   4668  NE  ARG C 218      -8.786   5.983   7.537  1.00117.39           N  
ANISOU 4668  NE  ARG C 218    16881  10933  16787   -451  -1113    -22       N  
ATOM   4669  CZ  ARG C 218      -8.737   6.109   6.183  1.00123.52           C  
ANISOU 4669  CZ  ARG C 218    17497  11650  17786   -348   -948    207       C  
ATOM   4670  NH1 ARG C 218      -7.677   5.748   5.435  1.00121.92           N  
ANISOU 4670  NH1 ARG C 218    17147  11414  17761   -298   -974    417       N  
ATOM   4671  NH2 ARG C 218      -9.793   6.610   5.535  1.00126.96           N  
ANISOU 4671  NH2 ARG C 218    17907  12071  18258   -291   -745    237       N  
ATOM   4672  N   ALA C 219     -10.329   0.572   9.920  1.00 60.48           N  
ANISOU 4672  N   ALA C 219    10507   4425   8047   -530  -1269    211       N  
ATOM   4673  CA  ALA C 219     -11.312   0.291  10.984  1.00 59.80           C  
ANISOU 4673  CA  ALA C 219    10646   4492   7583   -615  -1227    103       C  
ATOM   4674  C   ALA C 219     -11.177  -1.065  11.655  1.00 59.79           C  
ANISOU 4674  C   ALA C 219    10787   4601   7330   -645  -1333    289       C  
ATOM   4675  O   ALA C 219     -11.476  -1.174  12.835  1.00 62.08           O  
ANISOU 4675  O   ALA C 219    11254   5042   7290   -743  -1402    228       O  
ATOM   4676  CB  ALA C 219     -12.720   0.416  10.429  1.00 57.74           C  
ANISOU 4676  CB  ALA C 219    10411   4239   7288   -580   -941     32       C  
ATOM   4677  N   LEU C 220     -10.759  -2.074  10.886  1.00 56.41           N  
ANISOU 4677  N   LEU C 220    10273   4095   7065   -561  -1326    512       N  
ATOM   4678  CA  LEU C 220     -10.715  -3.463  11.343  1.00 55.56           C  
ANISOU 4678  CA  LEU C 220    10264   4032   6815   -568  -1387    727       C  
ATOM   4679  C   LEU C 220      -9.321  -4.007  11.537  1.00 56.28           C  
ANISOU 4679  C   LEU C 220    10256   4061   7065   -544  -1650    926       C  
ATOM   4680  O   LEU C 220      -9.120  -5.096  12.182  1.00 58.25           O  
ANISOU 4680  O   LEU C 220    10582   4346   7204   -560  -1767   1142       O  
ATOM   4681  CB  LEU C 220     -11.471  -4.394  10.371  1.00 52.87           C  
ANISOU 4681  CB  LEU C 220     9897   3624   6565   -497  -1151    809       C  
ATOM   4682  CG  LEU C 220     -12.894  -3.962  10.040  1.00 51.02           C  
ANISOU 4682  CG  LEU C 220     9718   3442   6224   -511   -897    641       C  
ATOM   4683  CD1 LEU C 220     -13.565  -4.930   9.104  1.00 49.01           C  
ANISOU 4683  CD1 LEU C 220     9423   3135   6061   -457   -710    706       C  
ATOM   4684  CD2 LEU C 220     -13.751  -3.731  11.286  1.00 52.43           C  
ANISOU 4684  CD2 LEU C 220    10092   3768   6059   -619   -864    541       C  
ATOM   4685  N   GLY C 221      -8.359  -3.241  11.066  1.00 54.71           N  
ANISOU 4685  N   GLY C 221     9877   3768   7142   -509  -1750    875       N  
ATOM   4686  CA  GLY C 221      -6.959  -3.612  11.153  1.00 55.51           C  
ANISOU 4686  CA  GLY C 221     9827   3789   7475   -478  -1998   1047       C  
ATOM   4687  C   GLY C 221      -6.561  -4.212   9.831  1.00 53.11           C  
ANISOU 4687  C   GLY C 221     9337   3317   7524   -352  -1842   1160       C  
ATOM   4688  O   GLY C 221      -7.376  -4.815   9.141  1.00 50.14           O  
ANISOU 4688  O   GLY C 221     9002   2923   7123   -305  -1603   1163       O  
ATOM   4689  N   THR C 222      -5.304  -4.023   9.480  1.00 53.78           N  
ANISOU 4689  N   THR C 222     9206   3287   7939   -305  -1971   1229       N  
ATOM   4690  CA  THR C 222      -4.780  -4.657   8.309  1.00 53.58           C  
ANISOU 4690  CA  THR C 222     8994   3115   8246   -189  -1821   1330       C  
ATOM   4691  C   THR C 222      -4.662  -6.154   8.548  1.00 55.39           C  
ANISOU 4691  C   THR C 222     9246   3286   8513   -147  -1859   1528       C  
ATOM   4692  O   THR C 222      -4.002  -6.605   9.498  1.00 57.33           O  
ANISOU 4692  O   THR C 222     9485   3529   8768   -173  -2131   1697       O  
ATOM   4693  CB  THR C 222      -3.410  -4.111   7.994  1.00 54.39           C  
ANISOU 4693  CB  THR C 222     8842   3104   8719   -156  -1946   1370       C  
ATOM   4694  OG1 THR C 222      -3.494  -2.726   8.167  1.00 55.15           O  
ANISOU 4694  OG1 THR C 222     8936   3242   8776   -226  -1984   1204       O  
ATOM   4695  CG2 THR C 222      -2.989  -4.425   6.580  1.00 53.20           C  
ANISOU 4695  CG2 THR C 222     8494   2832   8887    -41  -1700   1406       C  
ATOM   4696  N   PRO C 223      -5.300  -6.942   7.676  1.00 55.48           N  
ANISOU 4696  N   PRO C 223     9269   3244   8565    -85  -1595   1512       N  
ATOM   4697  CA  PRO C 223      -5.213  -8.378   7.852  1.00 57.12           C  
ANISOU 4697  CA  PRO C 223     9474   3344   8882    -45  -1604   1687       C  
ATOM   4698  C   PRO C 223      -3.854  -8.969   7.467  1.00 59.80           C  
ANISOU 4698  C   PRO C 223     9558   3491   9670     52  -1680   1828       C  
ATOM   4699  O   PRO C 223      -3.104  -8.435   6.604  1.00 60.22           O  
ANISOU 4699  O   PRO C 223     9416   3484   9980    111  -1601   1755       O  
ATOM   4700  CB  PRO C 223      -6.282  -8.888   6.921  1.00 55.14           C  
ANISOU 4700  CB  PRO C 223     9283   3087   8580    -19  -1291   1557       C  
ATOM   4701  CG  PRO C 223      -6.304  -7.903   5.812  1.00 53.03           C  
ANISOU 4701  CG  PRO C 223     8924   2869   8353     12  -1120   1376       C  
ATOM   4702  CD  PRO C 223      -6.102  -6.594   6.484  1.00 53.22           C  
ANISOU 4702  CD  PRO C 223     8982   2989   8248    -52  -1292   1341       C  
ATOM   4703  N   ASN C 224      -3.547 -10.033   8.181  1.00 62.68           N  
ANISOU 4703  N   ASN C 224     9918   3763  10133     66  -1835   2055       N  
ATOM   4704  CA  ASN C 224      -2.428 -10.908   7.945  1.00 65.67           C  
ANISOU 4704  CA  ASN C 224    10055   3919  10976    168  -1896   2228       C  
ATOM   4705  C   ASN C 224      -2.967 -12.365   8.082  1.00 66.32           C  
ANISOU 4705  C   ASN C 224    10193   3860  11142    196  -1802   2366       C  
ATOM   4706  O   ASN C 224      -4.173 -12.590   8.268  1.00 63.60           O  
ANISOU 4706  O   ASN C 224    10064   3605  10496    130  -1679   2310       O  
ATOM   4707  CB  ASN C 224      -1.380 -10.626   9.012  1.00 69.44           C  
ANISOU 4707  CB  ASN C 224    10446   4419  11520    142  -2294   2441       C  
ATOM   4708  CG  ASN C 224      -1.907 -10.872  10.419  1.00 72.62           C  
ANISOU 4708  CG  ASN C 224    11079   4978  11535     41  -2540   2625       C  
ATOM   4709  OD1 ASN C 224      -2.884 -11.631  10.613  1.00 74.50           O  
ANISOU 4709  OD1 ASN C 224    11490   5223  11593     19  -2406   2682       O  
ATOM   4710  ND2 ASN C 224      -1.252 -10.283  11.408  1.00 75.33           N  
ANISOU 4710  ND2 ASN C 224    11416   5453  11752    -25  -2899   2726       N  
ATOM   4711  N   ASN C 225      -2.060 -13.329   8.062  1.00 69.12           N  
ANISOU 4711  N   ASN C 225    10338   3978  11944    289  -1871   2563       N  
ATOM   4712  CA  ASN C 225      -2.458 -14.718   8.206  1.00 70.91           C  
ANISOU 4712  CA  ASN C 225    10577   4014  12350    321  -1789   2717       C  
ATOM   4713  C   ASN C 225      -2.908 -15.157   9.593  1.00 73.78           C  
ANISOU 4713  C   ASN C 225    11125   4457  12449    240  -2027   3028       C  
ATOM   4714  O   ASN C 225      -3.759 -16.016   9.681  1.00 73.50           O  
ANISOU 4714  O   ASN C 225    11194   4341  12390    218  -1882   3084       O  
ATOM   4715  CB  ASN C 225      -1.388 -15.595   7.633  1.00 72.23           C  
ANISOU 4715  CB  ASN C 225    10436   3869  13139    457  -1739   2799       C  
ATOM   4716  CG  ASN C 225      -1.383 -15.537   6.091  1.00 69.71           C  
ANISOU 4716  CG  ASN C 225     9991   3475  13019    525  -1361   2441       C  
ATOM   4717  OD1 ASN C 225      -2.426 -15.350   5.460  1.00 66.04           O  
ANISOU 4717  OD1 ASN C 225     9685   3132  12274    475  -1118   2182       O  
ATOM   4718  ND2 ASN C 225      -0.262 -15.947   5.505  1.00 71.24           N  
ANISOU 4718  ND2 ASN C 225     9887   3442  13736    644  -1298   2448       N  
ATOM   4719  N   GLU C 226      -2.434 -14.499  10.648  1.00 77.17           N  
ANISOU 4719  N   GLU C 226    11610   5074  12635    178  -2372   3201       N  
ATOM   4720  CA  GLU C 226      -2.971 -14.721  12.003  1.00 80.79           C  
ANISOU 4720  CA  GLU C 226    12295   5709  12693     75  -2585   3468       C  
ATOM   4721  C   GLU C 226      -4.473 -14.572  12.045  1.00 79.02           C  
ANISOU 4721  C   GLU C 226    12347   5641  12033    -23  -2340   3292       C  
ATOM   4722  O   GLU C 226      -5.157 -15.411  12.622  1.00 82.80           O  
ANISOU 4722  O   GLU C 226    12951   6100  12408    -65  -2302   3503       O  
ATOM   4723  CB  GLU C 226      -2.414 -13.732  13.043  1.00 84.64           C  
ANISOU 4723  CB  GLU C 226    12848   6470  12841    -10  -2963   3542       C  
ATOM   4724  CG  GLU C 226      -1.069 -14.118  13.651  1.00 90.03           C  
ANISOU 4724  CG  GLU C 226    13309   7068  13829     44  -3350   3890       C  
ATOM   4725  CD  GLU C 226       0.026 -14.224  12.599  1.00 91.68           C  
ANISOU 4725  CD  GLU C 226    13168   6992  14671    185  -3281   3815       C  
ATOM   4726  OE1 GLU C 226       0.846 -15.155  12.710  1.00 96.95           O  
ANISOU 4726  OE1 GLU C 226    13606   7428  15800    285  -3419   4120       O  
ATOM   4727  OE2 GLU C 226       0.027 -13.398  11.634  1.00 90.87           O  
ANISOU 4727  OE2 GLU C 226    13013   6893  14618    199  -3063   3462       O  
ATOM   4728  N   VAL C 227      -4.983 -13.480  11.482  1.00 74.46           N  
ANISOU 4728  N   VAL C 227    11852   5218  11220    -64  -2181   2933       N  
ATOM   4729  CA  VAL C 227      -6.386 -13.130  11.642  1.00 71.93           C  
ANISOU 4729  CA  VAL C 227    11780   5080  10467   -164  -1989   2762       C  
ATOM   4730  C   VAL C 227      -7.218 -13.696  10.532  1.00 69.41           C  
ANISOU 4730  C   VAL C 227    11433   4610  10326   -125  -1634   2572       C  
ATOM   4731  O   VAL C 227      -8.430 -13.800  10.665  1.00 66.81           O  
ANISOU 4731  O   VAL C 227    11271   4366   9746   -199  -1462   2496       O  
ATOM   4732  CB  VAL C 227      -6.606 -11.572  11.713  1.00 70.82           C  
ANISOU 4732  CB  VAL C 227    11742   5186   9979   -235  -2016   2478       C  
ATOM   4733  CG1 VAL C 227      -5.701 -10.927  12.771  1.00 73.78           C  
ANISOU 4733  CG1 VAL C 227    12123   5715  10192   -288  -2389   2597       C  
ATOM   4734  CG2 VAL C 227      -6.378 -10.900  10.385  1.00 67.17           C  
ANISOU 4734  CG2 VAL C 227    11124   4646   9749   -163  -1836   2201       C  
ATOM   4735  N   TRP C 228      -6.584 -13.920   9.386  1.00 70.05           N  
ANISOU 4735  N   TRP C 228    11297   4500  10816    -18  -1515   2450       N  
ATOM   4736  CA  TRP C 228      -7.278 -14.409   8.169  1.00 70.44           C  
ANISOU 4736  CA  TRP C 228    11300   4434  11030     16  -1184   2206       C  
ATOM   4737  C   TRP C 228      -6.383 -15.431   7.472  1.00 72.97           C  
ANISOU 4737  C   TRP C 228    11374   4454  11896    133  -1119   2253       C  
ATOM   4738  O   TRP C 228      -5.475 -15.067   6.731  1.00 73.82           O  
ANISOU 4738  O   TRP C 228    11302   4513  12231    214  -1098   2146       O  
ATOM   4739  CB  TRP C 228      -7.594 -13.263   7.218  1.00 68.67           C  
ANISOU 4739  CB  TRP C 228    11081   4372  10638     14  -1033   1882       C  
ATOM   4740  CG  TRP C 228      -8.357 -13.642   5.984  1.00 68.11           C  
ANISOU 4740  CG  TRP C 228    10976   4259  10643     33   -731   1622       C  
ATOM   4741  CD1 TRP C 228      -8.702 -14.865   5.582  1.00 70.57           C  
ANISOU 4741  CD1 TRP C 228    11235   4382  11195     50   -574   1593       C  
ATOM   4742  CD2 TRP C 228      -8.866 -12.746   4.981  1.00 68.37           C  
ANISOU 4742  CD2 TRP C 228    11015   4456  10505     30   -566   1350       C  
ATOM   4743  NE1 TRP C 228      -9.408 -14.819   4.408  1.00 68.92           N  
ANISOU 4743  NE1 TRP C 228    11008   4231  10946     48   -334   1290       N  
ATOM   4744  CE2 TRP C 228      -9.493 -13.530   4.000  1.00 67.18           C  
ANISOU 4744  CE2 TRP C 228    10820   4238  10465     42   -332   1160       C  
ATOM   4745  CE3 TRP C 228      -8.841 -11.348   4.815  1.00 65.09           C  
ANISOU 4745  CE3 TRP C 228    10625   4231   9874     17   -602   1260       C  
ATOM   4746  CZ2 TRP C 228     -10.093 -12.986   2.876  1.00 65.49           C  
ANISOU 4746  CZ2 TRP C 228    10596   4180  10104     40   -156    905       C  
ATOM   4747  CZ3 TRP C 228      -9.424 -10.818   3.703  1.00 63.15           C  
ANISOU 4747  CZ3 TRP C 228    10360   4105   9529     27   -412   1043       C  
ATOM   4748  CH2 TRP C 228     -10.068 -11.632   2.751  1.00 63.53           C  
ANISOU 4748  CH2 TRP C 228    10376   4125   9635     36   -201    876       C  
ATOM   4749  N   PRO C 229      -6.636 -16.714   7.720  1.00 75.86           N  
ANISOU 4749  N   PRO C 229    11717   4601  12504    142  -1067   2416       N  
ATOM   4750  CA  PRO C 229      -5.684 -17.629   7.181  1.00 79.33           C  
ANISOU 4750  CA  PRO C 229    11901   4730  13508    259  -1023   2466       C  
ATOM   4751  C   PRO C 229      -5.691 -17.683   5.662  1.00 78.35           C  
ANISOU 4751  C   PRO C 229    11646   4536  13587    318   -717   2074       C  
ATOM   4752  O   PRO C 229      -6.724 -17.495   5.008  1.00 73.25           O  
ANISOU 4752  O   PRO C 229    11111   4014  12704    260   -509   1794       O  
ATOM   4753  CB  PRO C 229      -6.098 -18.955   7.820  1.00 82.72           C  
ANISOU 4753  CB  PRO C 229    12344   4927  14159    242  -1020   2731       C  
ATOM   4754  CG  PRO C 229      -6.586 -18.536   9.172  1.00 82.67           C  
ANISOU 4754  CG  PRO C 229    12571   5159  13680    135  -1243   3008       C  
ATOM   4755  CD  PRO C 229      -7.400 -17.324   8.828  1.00 78.36           C  
ANISOU 4755  CD  PRO C 229    12202   4927  12645     55  -1138   2682       C  
ATOM   4756  N   GLU C 230      -4.480 -17.915   5.149  1.00 81.90           N  
ANISOU 4756  N   GLU C 230    11846   4802  14468    434   -708   2072       N  
ATOM   4757  CA  GLU C 230      -4.125 -17.839   3.727  1.00 83.10           C  
ANISOU 4757  CA  GLU C 230    11839   4920  14812    504   -435   1724       C  
ATOM   4758  C   GLU C 230      -4.275 -16.434   3.040  1.00 76.25           C  
ANISOU 4758  C   GLU C 230    11047   4379  13544    472   -367   1496       C  
ATOM   4759  O   GLU C 230      -4.090 -16.355   1.817  1.00 75.07           O  
ANISOU 4759  O   GLU C 230    10790   4254  13478    518   -119   1219       O  
ATOM   4760  CB  GLU C 230      -4.850 -18.902   2.914  1.00 86.92           C  
ANISOU 4760  CB  GLU C 230    12298   5236  15488    501   -140   1460       C  
ATOM   4761  CG  GLU C 230      -4.569 -20.303   3.384  1.00 96.65           C  
ANISOU 4761  CG  GLU C 230    13395   6079  17246    551   -156   1660       C  
ATOM   4762  CD  GLU C 230      -4.375 -21.302   2.244  1.00102.43           C  
ANISOU 4762  CD  GLU C 230    13923   6538  18458    620    157   1333       C  
ATOM   4763  OE1 GLU C 230      -4.901 -22.439   2.338  1.00101.64           O  
ANISOU 4763  OE1 GLU C 230    13796   6168  18653    600    257   1321       O  
ATOM   4764  OE2 GLU C 230      -3.642 -20.895   1.304  1.00107.88           O  
ANISOU 4764  OE2 GLU C 230    14472   7287  19230    691    302   1100       O  
ATOM   4765  N   VAL C 231      -4.515 -15.372   3.802  1.00 70.38           N  
ANISOU 4765  N   VAL C 231    10463   3866  12410    400   -574   1618       N  
ATOM   4766  CA  VAL C 231      -4.814 -14.061   3.183  1.00 67.24           C  
ANISOU 4766  CA  VAL C 231    10136   3741  11669    366   -498   1423       C  
ATOM   4767  C   VAL C 231      -3.669 -13.471   2.347  1.00 66.07           C  
ANISOU 4767  C   VAL C 231     9774   3591  11737    448   -425   1353       C  
ATOM   4768  O   VAL C 231      -3.889 -13.025   1.242  1.00 63.95           O  
ANISOU 4768  O   VAL C 231     9486   3455  11357    457   -201   1132       O  
ATOM   4769  CB  VAL C 231      -5.256 -13.009   4.210  1.00 65.23           C  
ANISOU 4769  CB  VAL C 231    10074   3698  11013    273   -725   1541       C  
ATOM   4770  CG1 VAL C 231      -4.095 -12.512   5.067  1.00 65.49           C  
ANISOU 4770  CG1 VAL C 231    10014   3705  11163    288  -1021   1767       C  
ATOM   4771  CG2 VAL C 231      -5.936 -11.866   3.481  1.00 63.14           C  
ANISOU 4771  CG2 VAL C 231     9891   3668  10430    234   -587   1323       C  
ATOM   4772  N   GLU C 232      -2.443 -13.671   2.811  1.00 66.52           N  
ANISOU 4772  N   GLU C 232     9644   3476  12152    512   -592   1553       N  
ATOM   4773  CA  GLU C 232      -1.268 -13.122   2.160  1.00 66.13           C  
ANISOU 4773  CA  GLU C 232     9361   3400  12364    586   -536   1525       C  
ATOM   4774  C   GLU C 232      -0.994 -13.768   0.801  1.00 68.00           C  
ANISOU 4774  C   GLU C 232     9430   3540  12863    670   -177   1290       C  
ATOM   4775  O   GLU C 232      -0.073 -13.349   0.087  1.00 67.91           O  
ANISOU 4775  O   GLU C 232     9219   3525  13058    732    -51   1239       O  
ATOM   4776  CB  GLU C 232      -0.068 -13.214   3.102  1.00 67.64           C  
ANISOU 4776  CB  GLU C 232     9376   3429  12893    626   -841   1811       C  
ATOM   4777  CG  GLU C 232      -0.338 -12.511   4.424  1.00 68.45           C  
ANISOU 4777  CG  GLU C 232     9658   3683  12664    525  -1197   1997       C  
ATOM   4778  CD  GLU C 232       0.699 -12.827   5.534  1.00 71.88           C  
ANISOU 4778  CD  GLU C 232     9949   3985  13377    548  -1564   2313       C  
ATOM   4779  OE1 GLU C 232       1.895 -13.115   5.234  1.00 75.15           O  
ANISOU 4779  OE1 GLU C 232    10064   4207  14282    645  -1580   2394       O  
ATOM   4780  OE2 GLU C 232       0.334 -12.718   6.745  1.00 72.98           O  
ANISOU 4780  OE2 GLU C 232    10266   4238  13223    462  -1853   2488       O  
ATOM   4781  N   SER C 233      -1.737 -14.863   0.487  1.00 71.01           N  
ANISOU 4781  N   SER C 233     9877   3826  13279    670     -7   1142       N  
ATOM   4782  CA  SER C 233      -1.627 -15.594  -0.784  1.00 74.20           C  
ANISOU 4782  CA  SER C 233    10147   4149  13894    732    346    846       C  
ATOM   4783  C   SER C 233      -2.577 -15.133  -1.858  1.00 71.28           C  
ANISOU 4783  C   SER C 233     9918   4068  13095    673    582    548       C  
ATOM   4784  O   SER C 233      -2.496 -15.570  -2.996  1.00 71.52           O  
ANISOU 4784  O   SER C 233     9856   4114  13202    708    877    268       O  
ATOM   4785  CB  SER C 233      -1.913 -17.075  -0.532  1.00 79.09           C  
ANISOU 4785  CB  SER C 233    10736   4475  14837    753    392    821       C  
ATOM   4786  OG  SER C 233      -0.958 -17.570   0.390  1.00 83.11           O  
ANISOU 4786  OG  SER C 233    11079   4706  15792    823    173   1135       O  
ATOM   4787  N   LEU C 234      -3.499 -14.268  -1.493  1.00 69.40           N  
ANISOU 4787  N   LEU C 234     9898   4067  12404    583    451    601       N  
ATOM   4788  CA  LEU C 234      -4.435 -13.728  -2.461  1.00 68.11           C  
ANISOU 4788  CA  LEU C 234     9855   4195  11828    529    629    372       C  
ATOM   4789  C   LEU C 234      -3.703 -12.853  -3.483  1.00 69.59           C  
ANISOU 4789  C   LEU C 234     9915   4554  11971    575    796    317       C  
ATOM   4790  O   LEU C 234      -2.642 -12.270  -3.197  1.00 68.24           O  
ANISOU 4790  O   LEU C 234     9605   4315  12006    621    710    501       O  
ATOM   4791  CB  LEU C 234      -5.505 -12.932  -1.750  1.00 64.55           C  
ANISOU 4791  CB  LEU C 234     9628   3921  10975    435    443    476       C  
ATOM   4792  CG  LEU C 234      -6.309 -13.710  -0.751  1.00 63.44           C  
ANISOU 4792  CG  LEU C 234     9625   3653  10826    376    309    548       C  
ATOM   4793  CD1 LEU C 234      -7.332 -12.854  -0.063  1.00 60.67           C  
ANISOU 4793  CD1 LEU C 234     9478   3489  10081    286    164    628       C  
ATOM   4794  CD2 LEU C 234      -6.999 -14.844  -1.478  1.00 66.43           C  
ANISOU 4794  CD2 LEU C 234    10000   3968  11272    360    520    284       C  
ATOM   4795  N   GLN C 235      -4.259 -12.825  -4.692  1.00 72.83           N  
ANISOU 4795  N   GLN C 235    10358   5190  12123    558   1039     66       N  
ATOM   4796  CA  GLN C 235      -3.575 -12.262  -5.888  1.00 76.93           C  
ANISOU 4796  CA  GLN C 235    10745   5891  12594    603   1281    -14       C  
ATOM   4797  C   GLN C 235      -3.223 -10.769  -5.747  1.00 71.25           C  
ANISOU 4797  C   GLN C 235    10012   5315  11742    597   1176    236       C  
ATOM   4798  O   GLN C 235      -2.135 -10.312  -6.156  1.00 72.78           O  
ANISOU 4798  O   GLN C 235    10024   5497  12131    652   1286    320       O  
ATOM   4799  CB  GLN C 235      -4.370 -12.549  -7.194  1.00 81.84           C  
ANISOU 4799  CB  GLN C 235    11431   6787  12876    568   1535   -332       C  
ATOM   4800  CG  GLN C 235      -5.739 -11.891  -7.315  1.00 85.48           C  
ANISOU 4800  CG  GLN C 235    12094   7533  12850    480   1438   -336       C  
ATOM   4801  CD  GLN C 235      -6.334 -11.974  -8.732  1.00 91.03           C  
ANISOU 4801  CD  GLN C 235    12825   8575  13186    447   1665   -610       C  
ATOM   4802  OE1 GLN C 235      -5.654 -11.678  -9.724  1.00 96.96           O  
ANISOU 4802  OE1 GLN C 235    13471   9500  13867    486   1886   -660       O  
ATOM   4803  NE2 GLN C 235      -7.609 -12.352  -8.823  1.00 91.24           N  
ANISOU 4803  NE2 GLN C 235    12987   8715  12962    368   1608   -781       N  
ATOM   4804  N   ASP C 236      -4.116 -10.054  -5.070  1.00 64.66           N  
ANISOU 4804  N   ASP C 236     9353   4573  10640    528    962    357       N  
ATOM   4805  CA  ASP C 236      -3.948  -8.643  -4.790  1.00 59.60           C  
ANISOU 4805  CA  ASP C 236     8712   4024   9907    509    837    572       C  
ATOM   4806  C   ASP C 236      -3.616  -8.326  -3.308  1.00 58.12           C  
ANISOU 4806  C   ASP C 236     8545   3637   9898    486    522    771       C  
ATOM   4807  O   ASP C 236      -3.708  -7.176  -2.888  1.00 59.38           O  
ANISOU 4807  O   ASP C 236     8740   3856   9964    447    385    901       O  
ATOM   4808  CB  ASP C 236      -5.221  -7.921  -5.213  1.00 56.38           C  
ANISOU 4808  CB  ASP C 236     8465   3888   9067    449    850    539       C  
ATOM   4809  CG  ASP C 236      -5.562  -8.114  -6.682  1.00 56.62           C  
ANISOU 4809  CG  ASP C 236     8479   4180   8851    459   1120    365       C  
ATOM   4810  OD1 ASP C 236      -4.634  -8.050  -7.522  1.00 55.99           O  
ANISOU 4810  OD1 ASP C 236     8247   4152   8876    511   1327    359       O  
ATOM   4811  OD2 ASP C 236      -6.778  -8.365  -6.973  1.00 56.00           O  
ANISOU 4811  OD2 ASP C 236     8538   4267   8469    408   1122    225       O  
ATOM   4812  N   TYR C 237      -3.207  -9.291  -2.510  1.00 58.23           N  
ANISOU 4812  N   TYR C 237     8529   3422  10171    505    398    801       N  
ATOM   4813  CA  TYR C 237      -2.659  -8.959  -1.213  1.00 57.51           C  
ANISOU 4813  CA  TYR C 237     8424   3186  10241    486     96   1004       C  
ATOM   4814  C   TYR C 237      -1.330  -8.343  -1.501  1.00 59.56           C  
ANISOU 4814  C   TYR C 237     8443   3378  10806    536    115   1107       C  
ATOM   4815  O   TYR C 237      -0.690  -8.691  -2.514  1.00 61.70           O  
ANISOU 4815  O   TYR C 237     8543   3632  11268    606    370   1030       O  
ATOM   4816  CB  TYR C 237      -2.433 -10.182  -0.325  1.00 58.31           C  
ANISOU 4816  CB  TYR C 237     8519   3061  10572    504    -51   1073       C  
ATOM   4817  CG  TYR C 237      -1.884  -9.687   1.050  1.00 57.98           C  
ANISOU 4817  CG  TYR C 237     8476   2943  10608    468   -408   1300       C  
ATOM   4818  CD1 TYR C 237      -2.761  -9.285   2.067  1.00 56.22           C  
ANISOU 4818  CD1 TYR C 237     8480   2822  10058    375   -611   1349       C  
ATOM   4819  CD2 TYR C 237      -0.528  -9.602   1.294  1.00 59.08           C  
ANISOU 4819  CD2 TYR C 237     8382   2932  11131    519   -531   1441       C  
ATOM   4820  CE1 TYR C 237      -2.299  -8.850   3.293  1.00 56.55           C  
ANISOU 4820  CE1 TYR C 237     8537   2839  10108    328   -930   1512       C  
ATOM   4821  CE2 TYR C 237      -0.053  -9.170   2.531  1.00 60.17           C  
ANISOU 4821  CE2 TYR C 237     8518   3035  11308    472   -885   1623       C  
ATOM   4822  CZ  TYR C 237      -0.947  -8.777   3.529  1.00 59.07           C  
ANISOU 4822  CZ  TYR C 237     8629   3026  10789    372  -1086   1647       C  
ATOM   4823  OH  TYR C 237      -0.507  -8.533   4.812  1.00 62.30           O  
ANISOU 4823  OH  TYR C 237     9054   3426  11189    316  -1444   1806       O  
ATOM   4824  N   LYS C 238      -0.884  -7.444  -0.614  1.00 59.80           N  
ANISOU 4824  N   LYS C 238     8447   3370  10902    495   -141   1262       N  
ATOM   4825  CA  LYS C 238       0.525  -6.971  -0.612  1.00 61.53           C  
ANISOU 4825  CA  LYS C 238     8398   3464  11515    532   -194   1386       C  
ATOM   4826  C   LYS C 238       1.023  -6.677   0.790  1.00 62.67           C  
ANISOU 4826  C   LYS C 238     8525   3498  11786    481   -585   1534       C  
ATOM   4827  O   LYS C 238       0.290  -6.182   1.650  1.00 60.53           O  
ANISOU 4827  O   LYS C 238     8456   3315  11228    396   -789   1535       O  
ATOM   4828  CB  LYS C 238       0.729  -5.711  -1.406  1.00 61.71           C  
ANISOU 4828  CB  LYS C 238     8330   3602  11512    518    -40   1404       C  
ATOM   4829  CG  LYS C 238       0.068  -5.629  -2.774  1.00 61.44           C  
ANISOU 4829  CG  LYS C 238     8351   3773  11217    541    307   1291       C  
ATOM   4830  CD  LYS C 238       0.906  -6.228  -3.920  1.00 63.12           C  
ANISOU 4830  CD  LYS C 238     8355   3972  11655    627    628   1233       C  
ATOM   4831  CE  LYS C 238       0.118  -6.080  -5.234  1.00 62.75           C  
ANISOU 4831  CE  LYS C 238     8404   4203  11235    627    940   1115       C  
ATOM   4832  NZ  LYS C 238       0.942  -5.884  -6.450  1.00 64.92           N  
ANISOU 4832  NZ  LYS C 238     8475   4566  11626    679   1273   1124       N  
ATOM   4833  N   ASN C 239       2.301  -7.014   0.997  1.00 66.48           N  
ANISOU 4833  N   ASN C 239     8750   3798  12710    535   -684   1648       N  
ATOM   4834  CA  ASN C 239       2.912  -6.815   2.284  1.00 69.60           C  
ANISOU 4834  CA  ASN C 239     9092   4106  13246    488  -1085   1797       C  
ATOM   4835  C   ASN C 239       3.212  -5.344   2.486  1.00 69.04           C  
ANISOU 4835  C   ASN C 239     8963   4093  13175    408  -1208   1800       C  
ATOM   4836  O   ASN C 239       3.761  -4.966   3.523  1.00 72.58           O  
ANISOU 4836  O   ASN C 239     9353   4497  13725    347  -1557   1881       O  
ATOM   4837  CB  ASN C 239       4.195  -7.618   2.422  1.00 73.83           C  
ANISOU 4837  CB  ASN C 239     9332   4421  14300    575  -1175   1935       C  
ATOM   4838  CG  ASN C 239       5.166  -7.336   1.301  1.00 76.80           C  
ANISOU 4838  CG  ASN C 239     9404   4715  15061    648   -893   1909       C  
ATOM   4839  OD1 ASN C 239       5.298  -8.150   0.411  1.00 81.72           O  
ANISOU 4839  OD1 ASN C 239     9934   5273  15842    741   -586   1833       O  
ATOM   4840  ND2 ASN C 239       5.848  -6.200   1.331  1.00 77.60           N  
ANISOU 4840  ND2 ASN C 239     9341   4817  15327    601   -978   1960       N  
ATOM   4841  N   THR C 240       2.945  -4.519   1.481  1.00 66.86           N  
ANISOU 4841  N   THR C 240     8673   3904  12824    406   -930   1723       N  
ATOM   4842  CA  THR C 240       3.262  -3.096   1.511  1.00 64.86           C  
ANISOU 4842  CA  THR C 240     8324   3658  12660    337   -991   1738       C  
ATOM   4843  C   THR C 240       2.070  -2.264   1.995  1.00 63.62           C  
ANISOU 4843  C   THR C 240     8438   3640  12096    243  -1075   1641       C  
ATOM   4844  O   THR C 240       2.215  -1.054   2.277  1.00 64.61           O  
ANISOU 4844  O   THR C 240     8509   3742  12296    168  -1179   1626       O  
ATOM   4845  CB  THR C 240       3.694  -2.659   0.118  1.00 63.72           C  
ANISOU 4845  CB  THR C 240     7984   3520  12704    394   -622   1763       C  
ATOM   4846  OG1 THR C 240       2.858  -3.287  -0.874  1.00 61.00           O  
ANISOU 4846  OG1 THR C 240     7786   3320  12071    452   -300   1679       O  
ATOM   4847  CG2 THR C 240       5.122  -3.019  -0.114  1.00 65.64           C  
ANISOU 4847  CG2 THR C 240     7888   3591  13461    457   -593   1860       C  
ATOM   4848  N   PHE C 241       0.913  -2.902   2.155  1.00 61.88           N  
ANISOU 4848  N   PHE C 241     8485   3535  11490    241  -1036   1565       N  
ATOM   4849  CA  PHE C 241      -0.272  -2.237   2.703  1.00 60.31           C  
ANISOU 4849  CA  PHE C 241     8537   3459  10919    158  -1108   1464       C  
ATOM   4850  C   PHE C 241       0.021  -1.481   3.980  1.00 61.24           C  
ANISOU 4850  C   PHE C 241     8670   3542  11055     54  -1448   1436       C  
ATOM   4851  O   PHE C 241       0.906  -1.876   4.747  1.00 61.89           O  
ANISOU 4851  O   PHE C 241     8654   3548  11313     39  -1710   1507       O  
ATOM   4852  CB  PHE C 241      -1.342  -3.258   3.098  1.00 59.83           C  
ANISOU 4852  CB  PHE C 241     8732   3489  10510    156  -1109   1411       C  
ATOM   4853  CG  PHE C 241      -2.092  -3.931   1.944  1.00 59.00           C  
ANISOU 4853  CG  PHE C 241     8689   3466  10262    223   -788   1356       C  
ATOM   4854  CD1 PHE C 241      -2.005  -3.513   0.622  1.00 58.53           C  
ANISOU 4854  CD1 PHE C 241     8512   3462  10264    274   -510   1348       C  
ATOM   4855  CD2 PHE C 241      -2.929  -5.001   2.222  1.00 59.00           C  
ANISOU 4855  CD2 PHE C 241     8869   3503  10043    223   -774   1311       C  
ATOM   4856  CE1 PHE C 241      -2.735  -4.136  -0.380  1.00 57.25           C  
ANISOU 4856  CE1 PHE C 241     8421   3419   9912    318   -252   1267       C  
ATOM   4857  CE2 PHE C 241      -3.650  -5.621   1.220  1.00 57.51           C  
ANISOU 4857  CE2 PHE C 241     8732   3392   9725    265   -510   1219       C  
ATOM   4858  CZ  PHE C 241      -3.580  -5.164  -0.082  1.00 56.70           C  
ANISOU 4858  CZ  PHE C 241     8525   3377   9642    309   -260   1181       C  
ATOM   4859  N   PRO C 242      -0.732  -0.397   4.240  1.00 61.72           N  
ANISOU 4859  N   PRO C 242     8849   3662  10938    -20  -1455   1320       N  
ATOM   4860  CA  PRO C 242      -0.542   0.283   5.522  1.00 63.94           C  
ANISOU 4860  CA  PRO C 242     9172   3932  11190   -134  -1774   1225       C  
ATOM   4861  C   PRO C 242      -0.988  -0.634   6.653  1.00 63.12           C  
ANISOU 4861  C   PRO C 242     9293   3937  10751   -174  -1982   1213       C  
ATOM   4862  O   PRO C 242      -1.876  -1.419   6.459  1.00 61.64           O  
ANISOU 4862  O   PRO C 242     9278   3831  10308   -136  -1833   1225       O  
ATOM   4863  CB  PRO C 242      -1.473   1.543   5.428  1.00 62.80           C  
ANISOU 4863  CB  PRO C 242     9118   3815  10926   -190  -1658   1075       C  
ATOM   4864  CG  PRO C 242      -1.865   1.670   4.026  1.00 60.61           C  
ANISOU 4864  CG  PRO C 242     8779   3547  10703   -101  -1317   1159       C  
ATOM   4865  CD  PRO C 242      -1.828   0.250   3.491  1.00 60.74           C  
ANISOU 4865  CD  PRO C 242     8826   3622  10629    -11  -1201   1256       C  
ATOM   4866  N   LYS C 243      -0.353  -0.470   7.802  1.00 66.33           N  
ANISOU 4866  N   LYS C 243     9682   4350  11169   -259  -2327   1195       N  
ATOM   4867  CA  LYS C 243      -0.451  -1.348   8.969  1.00 68.91           C  
ANISOU 4867  CA  LYS C 243    10176   4790  11216   -303  -2587   1256       C  
ATOM   4868  C   LYS C 243      -1.205  -0.688  10.108  1.00 70.08           C  
ANISOU 4868  C   LYS C 243    10559   5099  10968   -437  -2737   1060       C  
ATOM   4869  O   LYS C 243      -0.606   0.005  10.956  1.00 74.30           O  
ANISOU 4869  O   LYS C 243    11043   5661  11526   -540  -3027    954       O  
ATOM   4870  CB  LYS C 243       0.961  -1.755   9.440  1.00 71.46           C  
ANISOU 4870  CB  LYS C 243    10276   5034  11840   -299  -2907   1418       C  
ATOM   4871  CG  LYS C 243       1.936  -2.162   8.334  1.00 71.63           C  
ANISOU 4871  CG  LYS C 243     9994   4865  12356   -175  -2756   1570       C  
ATOM   4872  CD  LYS C 243       1.575  -3.508   7.694  1.00 70.22           C  
ANISOU 4872  CD  LYS C 243     9864   4653  12161    -55  -2525   1704       C  
ATOM   4873  CE  LYS C 243       2.657  -3.980   6.734  1.00 70.31           C  
ANISOU 4873  CE  LYS C 243     9560   4479  12673     62  -2388   1828       C  
ATOM   4874  NZ  LYS C 243       2.014  -4.422   5.476  1.00 68.54           N  
ANISOU 4874  NZ  LYS C 243     9380   4248  12414    153  -1966   1778       N  
ATOM   4875  N   TRP C 244      -2.516  -0.881  10.072  1.00 68.63           N  
ANISOU 4875  N   TRP C 244    10613   5019  10443   -437  -2524    987       N  
ATOM   4876  CA  TRP C 244      -3.406  -0.456  11.099  1.00 71.25           C  
ANISOU 4876  CA  TRP C 244    11189   5517  10364   -549  -2587    802       C  
ATOM   4877  C   TRP C 244      -3.720  -1.599  12.013  1.00 74.68           C  
ANISOU 4877  C   TRP C 244    11823   6106  10444   -576  -2717    946       C  
ATOM   4878  O   TRP C 244      -3.972  -2.703  11.581  1.00 75.46           O  
ANISOU 4878  O   TRP C 244    11947   6172  10550   -494  -2589   1134       O  
ATOM   4879  CB  TRP C 244      -4.694   0.073  10.473  1.00 68.69           C  
ANISOU 4879  CB  TRP C 244    10971   5199   9929   -529  -2251    651       C  
ATOM   4880  CG  TRP C 244      -4.480   1.359   9.726  1.00 68.14           C  
ANISOU 4880  CG  TRP C 244    10718   4985  10186   -518  -2138    527       C  
ATOM   4881  CD1 TRP C 244      -4.089   2.532  10.260  1.00 69.35           C  
ANISOU 4881  CD1 TRP C 244    10798   5087  10461   -611  -2284    331       C  
ATOM   4882  CD2 TRP C 244      -4.662   1.602   8.336  1.00 65.64           C  
ANISOU 4882  CD2 TRP C 244    10264   4560  10113   -416  -1857    602       C  
ATOM   4883  NE1 TRP C 244      -4.017   3.477   9.299  1.00 68.24           N  
ANISOU 4883  NE1 TRP C 244    10475   4782  10670   -568  -2102    307       N  
ATOM   4884  CE2 TRP C 244      -4.370   2.933   8.107  1.00 65.25           C  
ANISOU 4884  CE2 TRP C 244    10061   4386  10344   -447  -1841    490       C  
ATOM   4885  CE3 TRP C 244      -5.055   0.822   7.268  1.00 64.26           C  
ANISOU 4885  CE3 TRP C 244    10083   4394   9938   -310  -1619    746       C  
ATOM   4886  CZ2 TRP C 244      -4.443   3.509   6.862  1.00 64.18           C  
ANISOU 4886  CZ2 TRP C 244     9768   4145  10472   -370  -1599    572       C  
ATOM   4887  CZ3 TRP C 244      -5.144   1.423   6.000  1.00 62.65           C  
ANISOU 4887  CZ3 TRP C 244     9732   4119   9953   -239  -1383    790       C  
ATOM   4888  CH2 TRP C 244      -4.826   2.733   5.817  1.00 61.73           C  
ANISOU 4888  CH2 TRP C 244     9466   3889  10097   -266  -1377    732       C  
ATOM   4889  N   LYS C 245      -3.717  -1.318  13.302  1.00 82.24           N  
ANISOU 4889  N   LYS C 245    12923   7239  11085   -702  -2970    850       N  
ATOM   4890  CA  LYS C 245      -4.199  -2.242  14.329  1.00 86.82           C  
ANISOU 4890  CA  LYS C 245    13737   8020  11229   -755  -3077    985       C  
ATOM   4891  C   LYS C 245      -5.733  -2.276  14.278  1.00 86.41           C  
ANISOU 4891  C   LYS C 245    13913   8054  10863   -769  -2750    863       C  
ATOM   4892  O   LYS C 245      -6.343  -1.391  13.732  1.00 83.57           O  
ANISOU 4892  O   LYS C 245    13540   7634  10575   -763  -2528    634       O  
ATOM   4893  CB  LYS C 245      -3.769  -1.765  15.737  1.00 91.87           C  
ANISOU 4893  CB  LYS C 245    14472   8879  11553   -905  -3441    877       C  
ATOM   4894  CG  LYS C 245      -2.274  -1.853  16.067  1.00 95.55           C  
ANISOU 4894  CG  LYS C 245    14724   9315  12264   -917  -3849   1025       C  
ATOM   4895  CD  LYS C 245      -2.065  -1.732  17.576  1.00102.31           C  
ANISOU 4895  CD  LYS C 245    15738  10473  12659  -1074  -4223    977       C  
ATOM   4896  CE  LYS C 245      -0.702  -2.222  18.059  1.00108.71           C  
ANISOU 4896  CE  LYS C 245    16363  11310  13630  -1078  -4677   1242       C  
ATOM   4897  NZ  LYS C 245       0.210  -1.089  18.383  1.00111.98           N  
ANISOU 4897  NZ  LYS C 245    16605  11731  14212  -1184  -4975    976       N  
ATOM   4898  N   PRO C 246      -6.351  -3.304  14.857  1.00 92.26           N  
ANISOU 4898  N   PRO C 246    14843   8923  11286   -786  -2723   1039       N  
ATOM   4899  CA  PRO C 246      -7.780  -3.188  15.108  1.00 93.98           C  
ANISOU 4899  CA  PRO C 246    15280   9262  11165   -836  -2455    888       C  
ATOM   4900  C   PRO C 246      -7.976  -2.234  16.286  1.00101.77           C  
ANISOU 4900  C   PRO C 246    16422  10468  11777   -983  -2580    618       C  
ATOM   4901  O   PRO C 246      -7.379  -2.470  17.335  1.00105.04           O  
ANISOU 4901  O   PRO C 246    16914  11063  11933  -1068  -2881    711       O  
ATOM   4902  CB  PRO C 246      -8.187  -4.619  15.474  1.00 95.11           C  
ANISOU 4902  CB  PRO C 246    15550   9464  11120   -825  -2424   1196       C  
ATOM   4903  CG  PRO C 246      -7.061  -5.487  15.000  1.00 94.39           C  
ANISOU 4903  CG  PRO C 246    15263   9202  11398   -725  -2593   1490       C  
ATOM   4904  CD  PRO C 246      -5.840  -4.655  15.175  1.00 94.29           C  
ANISOU 4904  CD  PRO C 246    15093   9179  11554   -747  -2888   1407       C  
ATOM   4905  N   GLY C 247      -8.832  -1.210  16.200  1.00110.85           N  
ANISOU 4905  N   GLY C 247    17625  11625  12868  -1021  -2358    288       N  
ATOM   4906  CA  GLY C 247     -10.035  -1.166  15.358  1.00112.47           C  
ANISOU 4906  CA  GLY C 247    17840  11731  13161   -953  -1979    217       C  
ATOM   4907  C   GLY C 247     -11.120  -1.886  16.146  1.00116.89           C  
ANISOU 4907  C   GLY C 247    18640  12486  13287  -1016  -1833    273       C  
ATOM   4908  O   GLY C 247     -11.412  -3.029  15.803  1.00118.07           O  
ANISOU 4908  O   GLY C 247    18806  12595  13460   -960  -1742    538       O  
ATOM   4909  N   SER C 248     -11.757  -1.292  17.165  1.00118.80           N  
ANISOU 4909  N   SER C 248    19058  12926  13152  -1135  -1780     26       N  
ATOM   4910  CA  SER C 248     -12.124   0.122  17.303  1.00120.18           C  
ANISOU 4910  CA  SER C 248    19217  13088  13357  -1186  -1678   -388       C  
ATOM   4911  C   SER C 248     -13.250   0.389  16.307  1.00117.51           C  
ANISOU 4911  C   SER C 248    18798  12584  13264  -1096  -1318   -468       C  
ATOM   4912  O   SER C 248     -13.083   1.111  15.300  1.00118.14           O  
ANISOU 4912  O   SER C 248    18681  12450  13757  -1013  -1260   -541       O  
ATOM   4913  CB  SER C 248     -10.976   1.119  17.174  1.00123.33           C  
ANISOU 4913  CB  SER C 248    19446  13373  14040  -1198  -1923   -555       C  
ATOM   4914  OG  SER C 248     -11.458   2.441  17.355  1.00129.98           O  
ANISOU 4914  OG  SER C 248    20272  14172  14941  -1252  -1788   -966       O  
ATOM   4915  N   LEU C 249     -14.391  -0.238  16.609  1.00112.46           N  
ANISOU 4915  N   LEU C 249    18306  12058  12366  -1118  -1085   -420       N  
ATOM   4916  CA  LEU C 249     -15.552  -0.256  15.727  1.00103.96           C  
ANISOU 4916  CA  LEU C 249    17155  10859  11484  -1040   -765   -440       C  
ATOM   4917  C   LEU C 249     -16.723   0.550  16.258  1.00102.00           C  
ANISOU 4917  C   LEU C 249    16979  10679  11095  -1100   -503   -758       C  
ATOM   4918  O   LEU C 249     -17.399   1.202  15.469  1.00101.39           O  
ANISOU 4918  O   LEU C 249    16759  10446  11316  -1028   -308   -883       O  
ATOM   4919  CB  LEU C 249     -15.993  -1.685  15.481  1.00 99.07           C  
ANISOU 4919  CB  LEU C 249    16589  10260  10793  -1010   -678   -128       C  
ATOM   4920  CG  LEU C 249     -17.094  -1.879  14.436  1.00 96.85           C  
ANISOU 4920  CG  LEU C 249    16201   9854  10741   -930   -400   -119       C  
ATOM   4921  CD1 LEU C 249     -16.568  -1.623  13.032  1.00 92.64           C  
ANISOU 4921  CD1 LEU C 249    15449   9125  10623   -808   -448    -66       C  
ATOM   4922  CD2 LEU C 249     -17.676  -3.292  14.546  1.00100.37           C  
ANISOU 4922  CD2 LEU C 249    16733  10345  11056   -947   -296    128       C  
ATOM   4923  N   ALA C 250     -17.000   0.462  17.553  1.00102.44           N  
ANISOU 4923  N   ALA C 250    17244  10973  10703  -1225   -484   -869       N  
ATOM   4924  CA  ALA C 250     -17.975   1.366  18.197  1.00106.81           C  
ANISOU 4924  CA  ALA C 250    17862  11602  11118  -1294   -230  -1246       C  
ATOM   4925  C   ALA C 250     -17.610   2.815  17.907  1.00106.40           C  
ANISOU 4925  C   ALA C 250    17654  11373  11400  -1274   -270  -1580       C  
ATOM   4926  O   ALA C 250     -18.468   3.678  17.707  1.00110.12           O  
ANISOU 4926  O   ALA C 250    18035  11726  12079  -1248    -19  -1841       O  
ATOM   4927  CB  ALA C 250     -18.007   1.135  19.697  1.00111.01           C  
ANISOU 4927  CB  ALA C 250    18652  12460  11064  -1449   -259  -1336       C  
ATOM   4928  N   SER C 251     -16.304   3.051  17.879  1.00104.17           N  
ANISOU 4928  N   SER C 251    17316  11049  11212  -1283   -592  -1549       N  
ATOM   4929  CA  SER C 251     -15.697   4.272  17.343  1.00 99.28           C  
ANISOU 4929  CA  SER C 251    16493  10196  11032  -1246   -679  -1756       C  
ATOM   4930  C   SER C 251     -16.394   4.744  16.068  1.00 94.07           C  
ANISOU 4930  C   SER C 251    15618   9269  10853  -1109   -445  -1717       C  
ATOM   4931  O   SER C 251     -16.838   5.885  15.982  1.00 95.07           O  
ANISOU 4931  O   SER C 251    15635   9243  11245  -1100   -294  -2001       O  
ATOM   4932  CB  SER C 251     -14.217   3.980  17.055  1.00 97.06           C  
ANISOU 4932  CB  SER C 251    16127   9869  10880  -1230  -1038  -1535       C  
ATOM   4933  OG  SER C 251     -13.580   5.025  16.367  1.00 92.16           O  
ANISOU 4933  OG  SER C 251    15279   8994  10742  -1184  -1108  -1650       O  
ATOM   4934  N   HIS C 252     -16.514   3.828  15.108  1.00 88.90           N  
ANISOU 4934  N   HIS C 252    14905   8570  10302  -1007   -418  -1365       N  
ATOM   4935  CA  HIS C 252     -17.043   4.127  13.776  1.00 83.27           C  
ANISOU 4935  CA  HIS C 252    13985   7652   9999   -876   -255  -1260       C  
ATOM   4936  C   HIS C 252     -18.570   4.114  13.655  1.00 82.76           C  
ANISOU 4936  C   HIS C 252    13920   7598   9926   -849     56  -1331       C  
ATOM   4937  O   HIS C 252     -19.082   4.292  12.546  1.00 80.58           O  
ANISOU 4937  O   HIS C 252    13470   7187   9958   -742    168  -1217       O  
ATOM   4938  CB  HIS C 252     -16.425   3.182  12.715  1.00 79.74           C  
ANISOU 4938  CB  HIS C 252    13459   7166   9673   -784   -372   -893       C  
ATOM   4939  CG  HIS C 252     -14.971   3.450  12.410  1.00 80.03           C  
ANISOU 4939  CG  HIS C 252    13386   7107   9915   -767   -626   -808       C  
ATOM   4940  ND1 HIS C 252     -13.931   2.918  13.153  1.00 81.36           N  
ANISOU 4940  ND1 HIS C 252    13649   7379   9883   -836   -884   -743       N  
ATOM   4941  CD2 HIS C 252     -14.388   4.167  11.417  1.00 78.78           C  
ANISOU 4941  CD2 HIS C 252    13012   6759  10162   -689   -657   -748       C  
ATOM   4942  CE1 HIS C 252     -12.775   3.320  12.649  1.00 79.09           C  
ANISOU 4942  CE1 HIS C 252    13197   6958   9894   -803  -1060   -677       C  
ATOM   4943  NE2 HIS C 252     -13.025   4.064  11.588  1.00 78.61           N  
ANISOU 4943  NE2 HIS C 252    12953   6719  10197   -716   -913   -674       N  
ATOM   4944  N   VAL C 253     -19.308   3.926  14.749  1.00 86.22           N  
ANISOU 4944  N   VAL C 253    14534   8204  10021   -945    200  -1507       N  
ATOM   4945  CA  VAL C 253     -20.763   3.795  14.631  1.00 87.71           C  
ANISOU 4945  CA  VAL C 253    14700   8401  10226   -921    507  -1549       C  
ATOM   4946  C   VAL C 253     -21.492   3.988  15.941  1.00 90.94           C  
ANISOU 4946  C   VAL C 253    15273   8972  10305  -1036    705  -1838       C  
ATOM   4947  O   VAL C 253     -21.164   3.338  16.930  1.00 94.46           O  
ANISOU 4947  O   VAL C 253    15940   9645  10305  -1144    628  -1815       O  
ATOM   4948  CB  VAL C 253     -21.160   2.431  13.995  1.00 88.22           C  
ANISOU 4948  CB  VAL C 253    14777   8522  10218   -878    536  -1211       C  
ATOM   4949  CG1 VAL C 253     -20.241   1.303  14.423  1.00 89.36           C  
ANISOU 4949  CG1 VAL C 253    15086   8804  10061   -932    320   -983       C  
ATOM   4950  CG2 VAL C 253     -22.618   2.045  14.287  1.00 90.57           C  
ANISOU 4950  CG2 VAL C 253    15105   8894  10412   -905    836  -1261       C  
ATOM   4951  N   LYS C 254     -22.525   4.823  15.901  1.00 91.75           N  
ANISOU 4951  N   LYS C 254    15258   8965  10635  -1007    975  -2081       N  
ATOM   4952  CA  LYS C 254     -23.383   5.074  17.037  1.00 97.32           C  
ANISOU 4952  CA  LYS C 254    16084   9807  11083  -1104   1241  -2392       C  
ATOM   4953  C   LYS C 254     -24.799   4.597  16.814  1.00 92.14           C  
ANISOU 4953  C   LYS C 254    15364   9159  10484  -1070   1550  -2319       C  
ATOM   4954  O   LYS C 254     -25.218   4.356  15.704  1.00 87.73           O  
ANISOU 4954  O   LYS C 254    14624   8461  10245   -963   1561  -2096       O  
ATOM   4955  CB  LYS C 254     -23.393   6.565  17.362  1.00107.96           C  
ANISOU 4955  CB  LYS C 254    17329  10997  12694  -1112   1330  -2823       C  
ATOM   4956  CG  LYS C 254     -22.304   6.998  18.354  1.00120.05           C  
ANISOU 4956  CG  LYS C 254    19021  12650  13942  -1237   1121  -3084       C  
ATOM   4957  CD  LYS C 254     -20.936   7.231  17.707  1.00124.23           C  
ANISOU 4957  CD  LYS C 254    19456  13037  14708  -1196    760  -2927       C  
ATOM   4958  CE  LYS C 254     -19.898   7.649  18.748  1.00129.51           C  
ANISOU 4958  CE  LYS C 254    20265  13840  15099  -1335    532  -3207       C  
ATOM   4959  NZ  LYS C 254     -18.505   7.673  18.216  1.00129.36           N  
ANISOU 4959  NZ  LYS C 254    20160  13720  15270  -1311    165  -3012       N  
ATOM   4960  N   ASN C 255     -25.524   4.468  17.919  1.00 94.38           N  
ANISOU 4960  N   ASN C 255    15798   9628  10433  -1175   1804  -2521       N  
ATOM   4961  CA  ASN C 255     -26.920   3.944  17.999  1.00 94.80           C  
ANISOU 4961  CA  ASN C 255    15813   9730  10477  -1179   2143  -2481       C  
ATOM   4962  C   ASN C 255     -27.061   2.424  17.922  1.00 89.44           C  
ANISOU 4962  C   ASN C 255    15245   9197   9538  -1215   2110  -2091       C  
ATOM   4963  O   ASN C 255     -28.005   1.926  17.324  1.00 86.01           O  
ANISOU 4963  O   ASN C 255    14672   8691   9317  -1168   2270  -1943       O  
ATOM   4964  CB  ASN C 255     -27.853   4.584  16.965  1.00 96.64           C  
ANISOU 4964  CB  ASN C 255    15727   9694  11294  -1044   2302  -2512       C  
ATOM   4965  CG  ASN C 255     -27.751   6.079  16.952  1.00100.40           C  
ANISOU 4965  CG  ASN C 255    16052   9964  12132   -994   2346  -2855       C  
ATOM   4966  OD1 ASN C 255     -27.302   6.673  15.978  1.00 99.98           O  
ANISOU 4966  OD1 ASN C 255    15810   9690  12488   -886   2168  -2761       O  
ATOM   4967  ND2 ASN C 255     -28.155   6.701  18.053  1.00106.07           N  
ANISOU 4967  ND2 ASN C 255    16848  10748  12703  -1079   2599  -3262       N  
ATOM   4968  N   LEU C 256     -26.136   1.712  18.557  1.00 86.85           N  
ANISOU 4968  N   LEU C 256    15152   9065   8780  -1301   1900  -1932       N  
ATOM   4969  CA  LEU C 256     -26.289   0.295  18.780  1.00 84.70           C  
ANISOU 4969  CA  LEU C 256    15010   8937   8234  -1359   1910  -1586       C  
ATOM   4970  C   LEU C 256     -25.870  -0.091  20.184  1.00 87.34           C  
ANISOU 4970  C   LEU C 256    15639   9582   7964  -1507   1890  -1581       C  
ATOM   4971  O   LEU C 256     -24.775   0.239  20.617  1.00 87.31           O  
ANISOU 4971  O   LEU C 256    15752   9672   7749  -1544   1621  -1645       O  
ATOM   4972  CB  LEU C 256     -25.443  -0.472  17.792  1.00 81.08           C  
ANISOU 4972  CB  LEU C 256    14491   8361   7954  -1280   1598  -1239       C  
ATOM   4973  CG  LEU C 256     -25.840  -0.393  16.320  1.00 77.72           C  
ANISOU 4973  CG  LEU C 256    13797   7692   8040  -1146   1593  -1159       C  
ATOM   4974  CD1 LEU C 256     -24.824  -1.152  15.487  1.00 73.97           C  
ANISOU 4974  CD1 LEU C 256    13300   7143   7661  -1087   1291   -862       C  
ATOM   4975  CD2 LEU C 256     -27.234  -0.951  16.013  1.00 77.91           C  
ANISOU 4975  CD2 LEU C 256    13704   7682   8215  -1145   1877  -1098       C  
ATOM   4976  N   ASP C 257     -26.738  -0.807  20.887  1.00 89.32           N  
ANISOU 4976  N   ASP C 257    15999  10003   7934  -1597   2168  -1486       N  
ATOM   4977  CA  ASP C 257     -26.327  -1.435  22.138  1.00 93.63           C  
ANISOU 4977  CA  ASP C 257    16833  10875   7866  -1738   2127  -1347       C  
ATOM   4978  C   ASP C 257     -25.171  -2.411  21.900  1.00 91.65           C  
ANISOU 4978  C   ASP C 257    16653  10625   7543  -1722   1735   -923       C  
ATOM   4979  O   ASP C 257     -24.836  -2.727  20.753  1.00 89.37           O  
ANISOU 4979  O   ASP C 257    16193  10085   7678  -1607   1561   -746       O  
ATOM   4980  CB  ASP C 257     -27.506  -2.133  22.839  1.00 97.57           C  
ANISOU 4980  CB  ASP C 257    17414  11539   8117  -1835   2525  -1243       C  
ATOM   4981  CG  ASP C 257     -28.219  -3.152  21.971  1.00 95.32           C  
ANISOU 4981  CG  ASP C 257    16960  11049   8206  -1778   2633   -915       C  
ATOM   4982  OD1 ASP C 257     -27.768  -3.465  20.869  1.00 91.03           O  
ANISOU 4982  OD1 ASP C 257    16267  10274   8044  -1671   2390   -743       O  
ATOM   4983  OD2 ASP C 257     -29.255  -3.662  22.425  1.00100.45           O  
ANISOU 4983  OD2 ASP C 257    17624  11782   8759  -1851   2979   -841       O  
ATOM   4984  N   GLU C 258     -24.569  -2.912  22.971  1.00 93.69           N  
ANISOU 4984  N   GLU C 258    17154  11173   7268  -1835   1598   -752       N  
ATOM   4985  CA  GLU C 258     -23.453  -3.846  22.826  1.00 91.82           C  
ANISOU 4985  CA  GLU C 258    16966  10928   6992  -1814   1222   -331       C  
ATOM   4986  C   GLU C 258     -23.728  -5.097  21.986  1.00 86.54           C  
ANISOU 4986  C   GLU C 258    16173  10036   6669  -1744   1249     79       C  
ATOM   4987  O   GLU C 258     -22.809  -5.644  21.364  1.00 84.57           O  
ANISOU 4987  O   GLU C 258    15853   9635   6642  -1669    949    330       O  
ATOM   4988  CB  GLU C 258     -22.942  -4.291  24.195  1.00 97.89           C  
ANISOU 4988  CB  GLU C 258    18010  12076   7106  -1955   1097   -147       C  
ATOM   4989  CG  GLU C 258     -22.011  -3.267  24.838  1.00101.07           C  
ANISOU 4989  CG  GLU C 258    18519  12675   7207  -2013    832   -469       C  
ATOM   4990  CD  GLU C 258     -20.736  -3.006  24.023  1.00 98.77           C  
ANISOU 4990  CD  GLU C 258    18078  12161   7288  -1909    408   -436       C  
ATOM   4991  OE1 GLU C 258     -20.558  -3.582  22.918  1.00 96.30           O  
ANISOU 4991  OE1 GLU C 258    17585  11550   7453  -1783    333   -183       O  
ATOM   4992  OE2 GLU C 258     -19.903  -2.219  24.482  1.00100.22           O  
ANISOU 4992  OE2 GLU C 258    18315  12471   7293  -1958    158   -681       O  
ATOM   4993  N   ASN C 259     -24.988  -5.517  21.977  1.00 84.55           N  
ANISOU 4993  N   ASN C 259    15879   9756   6486  -1774   1618    114       N  
ATOM   4994  CA  ASN C 259     -25.468  -6.582  21.104  1.00 81.12           C  
ANISOU 4994  CA  ASN C 259    15289   9081   6451  -1719   1695    402       C  
ATOM   4995  C   ASN C 259     -25.359  -6.282  19.614  1.00 75.81           C  
ANISOU 4995  C   ASN C 259    14363   8098   6341  -1574   1582    284       C  
ATOM   4996  O   ASN C 259     -24.799  -7.077  18.849  1.00 73.10           O  
ANISOU 4996  O   ASN C 259    13933   7579   6262  -1508   1387    529       O  
ATOM   4997  CB  ASN C 259     -26.917  -6.871  21.402  1.00 82.27           C  
ANISOU 4997  CB  ASN C 259    15407   9259   6590  -1790   2130    383       C  
ATOM   4998  CG  ASN C 259     -27.106  -7.487  22.744  1.00 86.18           C  
ANISOU 4998  CG  ASN C 259    16137  10047   6559  -1936   2280    619       C  
ATOM   4999  OD1 ASN C 259     -26.182  -8.074  23.307  1.00 87.19           O  
ANISOU 4999  OD1 ASN C 259    16426  10309   6392  -1975   2027    929       O  
ATOM   5000  ND2 ASN C 259     -28.307  -7.358  23.276  1.00 88.26           N  
ANISOU 5000  ND2 ASN C 259    16412  10422   6702  -2017   2699    494       N  
ATOM   5001  N   GLY C 260     -25.877  -5.128  19.224  1.00 74.21           N  
ANISOU 5001  N   GLY C 260    14041   7838   6317  -1526   1710    -87       N  
ATOM   5002  CA  GLY C 260     -25.715  -4.629  17.876  1.00 69.77           C  
ANISOU 5002  CA  GLY C 260    13251   7034   6225  -1392   1588   -203       C  
ATOM   5003  C   GLY C 260     -24.267  -4.605  17.442  1.00 68.14           C  
ANISOU 5003  C   GLY C 260    13049   6763   6078  -1325   1207    -99       C  
ATOM   5004  O   GLY C 260     -23.913  -5.128  16.384  1.00 65.03           O  
ANISOU 5004  O   GLY C 260    12520   6192   5997  -1239   1072     54       O  
ATOM   5005  N   LEU C 261     -23.407  -4.056  18.281  1.00 70.74           N  
ANISOU 5005  N   LEU C 261    13528   7248   6100  -1373   1035   -185       N  
ATOM   5006  CA  LEU C 261     -21.997  -3.909  17.913  1.00 71.27           C  
ANISOU 5006  CA  LEU C 261    13571   7250   6257  -1314    671   -111       C  
ATOM   5007  C   LEU C 261     -21.297  -5.239  17.754  1.00 72.50           C  
ANISOU 5007  C   LEU C 261    13750   7360   6435  -1299    480    290       C  
ATOM   5008  O   LEU C 261     -20.434  -5.440  16.866  1.00 72.58           O  
ANISOU 5008  O   LEU C 261    13635   7202   6738  -1204    266    399       O  
ATOM   5009  CB  LEU C 261     -21.260  -3.097  18.972  1.00 74.64           C  
ANISOU 5009  CB  LEU C 261    14152   7876   6331  -1393    512   -299       C  
ATOM   5010  CG  LEU C 261     -21.730  -1.630  19.080  1.00 75.14           C  
ANISOU 5010  CG  LEU C 261    14162   7929   6457  -1398    668   -755       C  
ATOM   5011  CD1 LEU C 261     -21.207  -0.967  20.334  1.00 79.06           C  
ANISOU 5011  CD1 LEU C 261    14843   8670   6526  -1517    565   -990       C  
ATOM   5012  CD2 LEU C 261     -21.339  -0.818  17.846  1.00 71.86           C  
ANISOU 5012  CD2 LEU C 261    13511   7246   6543  -1270    563   -870       C  
ATOM   5013  N   ASP C 262     -21.703  -6.163  18.609  1.00 75.40           N  
ANISOU 5013  N   ASP C 262    14266   7865   6517  -1391    585    521       N  
ATOM   5014  CA  ASP C 262     -21.203  -7.513  18.600  1.00 75.44           C  
ANISOU 5014  CA  ASP C 262    14290   7807   6567  -1387    451    934       C  
ATOM   5015  C   ASP C 262     -21.656  -8.257  17.328  1.00 72.26           C  
ANISOU 5015  C   ASP C 262    13687   7125   6641  -1302    555   1019       C  
ATOM   5016  O   ASP C 262     -20.824  -8.813  16.598  1.00 70.84           O  
ANISOU 5016  O   ASP C 262    13405   6774   6737  -1220    358   1175       O  
ATOM   5017  CB  ASP C 262     -21.687  -8.229  19.872  1.00 79.49           C  
ANISOU 5017  CB  ASP C 262    15004   8543   6655  -1518    586   1171       C  
ATOM   5018  CG  ASP C 262     -21.078  -9.601  20.046  1.00 80.14           C  
ANISOU 5018  CG  ASP C 262    15111   8559   6776  -1519    422   1651       C  
ATOM   5019  OD1 ASP C 262     -19.893  -9.659  20.387  1.00 80.81           O  
ANISOU 5019  OD1 ASP C 262    15247   8709   6748  -1506     94   1808       O  
ATOM   5020  OD2 ASP C 262     -21.780 -10.588  19.786  1.00 78.53           O  
ANISOU 5020  OD2 ASP C 262    14848   8212   6775  -1530    616   1857       O  
ATOM   5021  N   LEU C 263     -22.965  -8.287  17.092  1.00 71.14           N  
ANISOU 5021  N   LEU C 263    13482   6948   6596  -1327    864    904       N  
ATOM   5022  CA  LEU C 263     -23.517  -8.924  15.889  1.00 67.77           C  
ANISOU 5022  CA  LEU C 263    12859   6291   6599  -1265    960    927       C  
ATOM   5023  C   LEU C 263     -22.805  -8.419  14.663  1.00 64.87           C  
ANISOU 5023  C   LEU C 263    12333   5781   6530  -1141    771    791       C  
ATOM   5024  O   LEU C 263     -22.323  -9.177  13.822  1.00 63.56           O  
ANISOU 5024  O   LEU C 263    12062   5451   6637  -1079    663    916       O  
ATOM   5025  CB  LEU C 263     -25.008  -8.595  15.767  1.00 67.08           C  
ANISOU 5025  CB  LEU C 263    12690   6213   6581  -1303   1285    729       C  
ATOM   5026  CG  LEU C 263     -25.706  -9.112  14.503  1.00 63.92           C  
ANISOU 5026  CG  LEU C 263    12066   5611   6606  -1253   1371    694       C  
ATOM   5027  CD1 LEU C 263     -25.414 -10.577  14.257  1.00 63.38           C  
ANISOU 5027  CD1 LEU C 263    11974   5388   6717  -1269   1313    977       C  
ATOM   5028  CD2 LEU C 263     -27.202  -8.891  14.591  1.00 64.62           C  
ANISOU 5028  CD2 LEU C 263    12068   5726   6755  -1308   1684    545       C  
ATOM   5029  N   LEU C 264     -22.745  -7.090  14.587  1.00 65.64           N  
ANISOU 5029  N   LEU C 264    12410   5945   6583  -1108    751    525       N  
ATOM   5030  CA  LEU C 264     -22.024  -6.350  13.515  1.00 62.93           C  
ANISOU 5030  CA  LEU C 264    11922   5496   6490   -994    582    399       C  
ATOM   5031  C   LEU C 264     -20.579  -6.815  13.354  1.00 62.26           C  
ANISOU 5031  C   LEU C 264    11846   5350   6460   -948    301    586       C  
ATOM   5032  O   LEU C 264     -20.157  -7.141  12.268  1.00 56.70           O  
ANISOU 5032  O   LEU C 264    11002   4506   6033   -864    229    628       O  
ATOM   5033  CB  LEU C 264     -22.056  -4.840  13.790  1.00 61.85           C  
ANISOU 5033  CB  LEU C 264    11788   5433   6280   -988    595    122       C  
ATOM   5034  CG  LEU C 264     -21.352  -3.985  12.728  1.00 59.37           C  
ANISOU 5034  CG  LEU C 264    11313   5003   6241   -879    445     26       C  
ATOM   5035  CD1 LEU C 264     -21.974  -4.111  11.351  1.00 56.44           C  
ANISOU 5035  CD1 LEU C 264    10746   4517   6178   -796    534     21       C  
ATOM   5036  CD2 LEU C 264     -21.351  -2.524  13.149  1.00 61.11           C  
ANISOU 5036  CD2 LEU C 264    11532   5257   6428   -886    462   -237       C  
ATOM   5037  N   SER C 265     -19.865  -6.875  14.477  1.00 66.65           N  
ANISOU 5037  N   SER C 265    12560   6028   6734  -1009    151    698       N  
ATOM   5038  CA  SER C 265     -18.481  -7.313  14.453  1.00 68.91           C  
ANISOU 5038  CA  SER C 265    12835   6259   7086   -968   -131    896       C  
ATOM   5039  C   SER C 265     -18.366  -8.701  13.835  1.00 69.32           C  
ANISOU 5039  C   SER C 265    12804   6135   7396   -925   -125   1143       C  
ATOM   5040  O   SER C 265     -17.442  -8.965  13.059  1.00 69.62           O  
ANISOU 5040  O   SER C 265    12719   6032   7702   -837   -272   1206       O  
ATOM   5041  CB  SER C 265     -17.870  -7.319  15.841  1.00 72.55           C  
ANISOU 5041  CB  SER C 265    13480   6912   7173  -1056   -306   1020       C  
ATOM   5042  OG  SER C 265     -18.270  -8.492  16.529  1.00 75.82           O  
ANISOU 5042  OG  SER C 265    14004   7373   7429  -1123   -233   1309       O  
ATOM   5043  N   LYS C 266     -19.342  -9.558  14.134  1.00 69.88           N  
ANISOU 5043  N   LYS C 266    12925   6200   7425   -989     72   1256       N  
ATOM   5044  CA  LYS C 266     -19.345 -10.920  13.607  1.00 69.88           C  
ANISOU 5044  CA  LYS C 266    12837   6001   7712   -964    105   1465       C  
ATOM   5045  C   LYS C 266     -19.727 -11.025  12.158  1.00 66.22           C  
ANISOU 5045  C   LYS C 266    12184   5378   7597   -891    208   1282       C  
ATOM   5046  O   LYS C 266     -19.287 -11.952  11.470  1.00 66.03           O  
ANISOU 5046  O   LYS C 266    12053   5169   7866   -841    169   1376       O  
ATOM   5047  CB  LYS C 266     -20.274 -11.793  14.410  1.00 73.76           C  
ANISOU 5047  CB  LYS C 266    13424   6518   8080  -1068    293   1655       C  
ATOM   5048  CG  LYS C 266     -19.761 -12.057  15.807  1.00 78.38           C  
ANISOU 5048  CG  LYS C 266    14195   7262   8321  -1141    166   1942       C  
ATOM   5049  CD  LYS C 266     -20.822 -12.776  16.615  1.00 82.20           C  
ANISOU 5049  CD  LYS C 266    14779   7806   8644  -1256    407   2130       C  
ATOM   5050  CE  LYS C 266     -20.261 -13.419  17.866  1.00 87.58           C  
ANISOU 5050  CE  LYS C 266    15622   8614   9039  -1323    272   2537       C  
ATOM   5051  NZ  LYS C 266     -20.095 -12.396  18.927  1.00 91.17           N  
ANISOU 5051  NZ  LYS C 266    16272   9414   8955  -1393    195   2432       N  
ATOM   5052  N   MET C 267     -20.527 -10.072  11.690  1.00 64.06           N  
ANISOU 5052  N   MET C 267    11863   5180   7297   -885    335   1018       N  
ATOM   5053  CA  MET C 267     -20.757  -9.923  10.246  1.00 61.25           C  
ANISOU 5053  CA  MET C 267    11325   4734   7211   -808    378    839       C  
ATOM   5054  C   MET C 267     -19.551  -9.423   9.455  1.00 57.59           C  
ANISOU 5054  C   MET C 267    10775   4232   6875   -704    197    798       C  
ATOM   5055  O   MET C 267     -19.541  -9.573   8.261  1.00 54.00           O  
ANISOU 5055  O   MET C 267    10181   3711   6624   -643    220    707       O  
ATOM   5056  CB  MET C 267     -21.929  -9.016   9.972  1.00 60.98           C  
ANISOU 5056  CB  MET C 267    11239   4792   7135   -822    540    619       C  
ATOM   5057  CG  MET C 267     -23.244  -9.684  10.097  1.00 62.85           C  
ANISOU 5057  CG  MET C 267    11452   5012   7415   -901    754    613       C  
ATOM   5058  SD  MET C 267     -24.493  -8.489  10.499  1.00 66.23           S  
ANISOU 5058  SD  MET C 267    11873   5577   7712   -936    944    410       S  
ATOM   5059  CE  MET C 267     -26.038  -9.239   9.989  1.00 65.50           C  
ANISOU 5059  CE  MET C 267    11630   5425   7831   -996   1167    356       C  
ATOM   5060  N   LEU C 268     -18.578  -8.814  10.109  1.00 58.47           N  
ANISOU 5060  N   LEU C 268    10958   4399   6856   -693     25    853       N  
ATOM   5061  CA  LEU C 268     -17.424  -8.247   9.422  1.00 59.12           C  
ANISOU 5061  CA  LEU C 268    10939   4439   7082   -603   -132    820       C  
ATOM   5062  C   LEU C 268     -16.105  -8.915   9.794  1.00 60.36           C  
ANISOU 5062  C   LEU C 268    11100   4513   7319   -578   -333   1030       C  
ATOM   5063  O   LEU C 268     -15.028  -8.293   9.739  1.00 59.22           O  
ANISOU 5063  O   LEU C 268    10905   4366   7229   -533   -501   1032       O  
ATOM   5064  CB  LEU C 268     -17.327  -6.751   9.751  1.00 59.91           C  
ANISOU 5064  CB  LEU C 268    11064   4647   7052   -608   -181    668       C  
ATOM   5065  CG  LEU C 268     -18.550  -5.905   9.431  1.00 59.35           C  
ANISOU 5065  CG  LEU C 268    10959   4637   6953   -616      1    470       C  
ATOM   5066  CD1 LEU C 268     -18.353  -4.492   9.953  1.00 59.34           C  
ANISOU 5066  CD1 LEU C 268    10982   4697   6865   -628    -48    323       C  
ATOM   5067  CD2 LEU C 268     -18.839  -5.883   7.934  1.00 58.16           C  
ANISOU 5067  CD2 LEU C 268    10634   4434   7028   -536     75    410       C  
ATOM   5068  N   ILE C 269     -16.188 -10.185  10.164  1.00 60.47           N  
ANISOU 5068  N   ILE C 269    11150   4440   7385   -607   -315   1222       N  
ATOM   5069  CA  ILE C 269     -14.995 -10.978  10.304  1.00 61.09           C  
ANISOU 5069  CA  ILE C 269    11178   4389   7643   -561   -488   1442       C  
ATOM   5070  C   ILE C 269     -14.373 -11.171   8.898  1.00 57.53           C  
ANISOU 5070  C   ILE C 269    10532   3788   7536   -453   -462   1340       C  
ATOM   5071  O   ILE C 269     -15.090 -11.406   7.927  1.00 53.64           O  
ANISOU 5071  O   ILE C 269     9968   3259   7152   -439   -283   1180       O  
ATOM   5072  CB  ILE C 269     -15.337 -12.326  10.969  1.00 66.06           C  
ANISOU 5072  CB  ILE C 269    11869   4923   8306   -613   -446   1695       C  
ATOM   5073  CG1 ILE C 269     -15.753 -12.071  12.439  1.00 68.26           C  
ANISOU 5073  CG1 ILE C 269    12352   5401   8180   -722   -486   1831       C  
ATOM   5074  CG2 ILE C 269     -14.149 -13.319  10.874  1.00 67.57           C  
ANISOU 5074  CG2 ILE C 269    11948   4908   8817   -540   -598   1931       C  
ATOM   5075  CD1 ILE C 269     -16.543 -13.194  13.076  1.00 70.40           C  
ANISOU 5075  CD1 ILE C 269    12702   5625   8421   -800   -352   2058       C  
ATOM   5076  N   TYR C 270     -13.050 -11.026   8.826  1.00 57.19           N  
ANISOU 5076  N   TYR C 270    10401   3686   7643   -386   -641   1425       N  
ATOM   5077  CA  TYR C 270     -12.324 -11.097   7.574  1.00 56.42           C  
ANISOU 5077  CA  TYR C 270    10117   3474   7845   -286   -603   1330       C  
ATOM   5078  C   TYR C 270     -12.467 -12.484   6.974  1.00 58.35           C  
ANISOU 5078  C   TYR C 270    10277   3527   8367   -256   -472   1351       C  
ATOM   5079  O   TYR C 270     -13.049 -12.649   5.922  1.00 56.82           O  
ANISOU 5079  O   TYR C 270    10018   3324   8245   -242   -293   1150       O  
ATOM   5080  CB  TYR C 270     -10.845 -10.752   7.776  1.00 57.72           C  
ANISOU 5080  CB  TYR C 270    10184   3592   8152   -228   -819   1446       C  
ATOM   5081  CG  TYR C 270     -10.508  -9.271   7.835  1.00 59.12           C  
ANISOU 5081  CG  TYR C 270    10360   3906   8195   -236   -912   1336       C  
ATOM   5082  CD1 TYR C 270     -10.939  -8.390   6.822  1.00 59.23           C  
ANISOU 5082  CD1 TYR C 270    10318   3987   8199   -210   -757   1130       C  
ATOM   5083  CD2 TYR C 270      -9.669  -8.747   8.846  1.00 61.22           C  
ANISOU 5083  CD2 TYR C 270    10652   4222   8384   -268  -1169   1445       C  
ATOM   5084  CE1 TYR C 270     -10.592  -7.040   6.859  1.00 60.01           C  
ANISOU 5084  CE1 TYR C 270    10388   4162   8252   -215   -832   1051       C  
ATOM   5085  CE2 TYR C 270      -9.279  -7.430   8.884  1.00 60.93           C  
ANISOU 5085  CE2 TYR C 270    10584   4265   8299   -282  -1256   1323       C  
ATOM   5086  CZ  TYR C 270      -9.749  -6.557   7.892  1.00 61.26           C  
ANISOU 5086  CZ  TYR C 270    10567   4335   8373   -254  -1075   1129       C  
ATOM   5087  OH  TYR C 270      -9.403  -5.228   7.887  1.00 58.08           O  
ANISOU 5087  OH  TYR C 270    10113   3971   7983   -266  -1140   1021       O  
ATOM   5088  N   ASP C 271     -11.930 -13.487   7.687  1.00 60.46           N  
ANISOU 5088  N   ASP C 271    10535   3636   8798   -252   -576   1601       N  
ATOM   5089  CA  ASP C 271     -11.995 -14.860   7.287  1.00 60.39           C  
ANISOU 5089  CA  ASP C 271    10432   3390   9122   -227   -462   1644       C  
ATOM   5090  C   ASP C 271     -13.453 -15.239   7.027  1.00 58.32           C  
ANISOU 5090  C   ASP C 271    10237   3149   8772   -307   -249   1495       C  
ATOM   5091  O   ASP C 271     -14.247 -15.296   7.967  1.00 58.88           O  
ANISOU 5091  O   ASP C 271    10450   3294   8626   -397   -243   1622       O  
ATOM   5092  CB  ASP C 271     -11.406 -15.699   8.422  1.00 64.42           C  
ANISOU 5092  CB  ASP C 271    10959   3762   9755   -230   -633   2015       C  
ATOM   5093  CG  ASP C 271     -11.244 -17.199   8.094  1.00 66.39           C  
ANISOU 5093  CG  ASP C 271    11067   3684  10472   -187   -536   2112       C  
ATOM   5094  OD1 ASP C 271     -11.541 -17.670   6.952  1.00 65.25           O  
ANISOU 5094  OD1 ASP C 271    10809   3411  10569   -159   -328   1845       O  
ATOM   5095  OD2 ASP C 271     -10.763 -17.873   9.040  1.00 69.41           O  
ANISOU 5095  OD2 ASP C 271    11449   3946  10975   -184   -690   2470       O  
ATOM   5096  N   PRO C 272     -13.807 -15.513   5.756  1.00 55.86           N  
ANISOU 5096  N   PRO C 272     9814   2786   8622   -282    -72   1221       N  
ATOM   5097  CA  PRO C 272     -15.176 -15.962   5.384  1.00 55.28           C  
ANISOU 5097  CA  PRO C 272     9760   2717   8525   -363    112   1049       C  
ATOM   5098  C   PRO C 272     -15.667 -17.268   6.014  1.00 58.55           C  
ANISOU 5098  C   PRO C 272    10182   2907   9154   -428    178   1217       C  
ATOM   5099  O   PRO C 272     -16.860 -17.409   6.365  1.00 58.85           O  
ANISOU 5099  O   PRO C 272    10294   2992   9074   -527    282   1205       O  
ATOM   5100  CB  PRO C 272     -15.127 -16.084   3.854  1.00 53.73           C  
ANISOU 5100  CB  PRO C 272     9419   2513   8482   -314    240    727       C  
ATOM   5101  CG  PRO C 272     -13.787 -15.614   3.433  1.00 53.14           C  
ANISOU 5101  CG  PRO C 272     9259   2444   8486   -207    156    740       C  
ATOM   5102  CD  PRO C 272     -12.885 -15.517   4.608  1.00 54.71           C  
ANISOU 5102  CD  PRO C 272     9502   2574   8708   -181    -38   1059       C  
ATOM   5103  N   ALA C 273     -14.754 -18.234   6.177  1.00 62.01           N  
ANISOU 5103  N   ALA C 273    10525   3082   9951   -371    127   1395       N  
ATOM   5104  CA  ALA C 273     -15.067 -19.487   6.866  1.00 64.83           C  
ANISOU 5104  CA  ALA C 273    10873   3185  10573   -423    173   1635       C  
ATOM   5105  C   ALA C 273     -15.535 -19.215   8.281  1.00 66.47           C  
ANISOU 5105  C   ALA C 273    11267   3538  10450   -507     91   1958       C  
ATOM   5106  O   ALA C 273     -16.346 -19.971   8.831  1.00 68.46           O  
ANISOU 5106  O   ALA C 273    11555   3684  10771   -595    197   2112       O  
ATOM   5107  CB  ALA C 273     -13.864 -20.391   6.891  1.00 67.32           C  
ANISOU 5107  CB  ALA C 273    11040   3198  11339   -327     97   1823       C  
ATOM   5108  N   LYS C 274     -14.995 -18.147   8.877  1.00 66.64           N  
ANISOU 5108  N   LYS C 274    11399   3801  10119   -487    -87   2054       N  
ATOM   5109  CA  LYS C 274     -15.221 -17.809  10.308  1.00 68.62           C  
ANISOU 5109  CA  LYS C 274    11841   4236   9994   -565   -194   2351       C  
ATOM   5110  C   LYS C 274     -16.340 -16.761  10.486  1.00 64.80           C  
ANISOU 5110  C   LYS C 274    11501   4039   9079   -650    -87   2145       C  
ATOM   5111  O   LYS C 274     -16.780 -16.456  11.585  1.00 65.51           O  
ANISOU 5111  O   LYS C 274    11755   4307   8828   -733   -102   2306       O  
ATOM   5112  CB  LYS C 274     -13.894 -17.330  10.914  1.00 70.81           C  
ANISOU 5112  CB  LYS C 274    12134   4592  10176   -501   -479   2558       C  
ATOM   5113  CG  LYS C 274     -13.513 -17.863  12.301  1.00 77.08           C  
ANISOU 5113  CG  LYS C 274    13021   5398  10865   -539   -658   3023       C  
ATOM   5114  CD  LYS C 274     -12.123 -18.529  12.324  1.00 81.65           C  
ANISOU 5114  CD  LYS C 274    13435   5752  11834   -431   -871   3288       C  
ATOM   5115  CE  LYS C 274     -12.024 -19.615  13.392  1.00 85.70           C  
ANISOU 5115  CE  LYS C 274    13973   6143  12445   -462   -965   3796       C  
ATOM   5116  NZ  LYS C 274     -10.654 -20.210  13.459  1.00 89.67           N  
ANISOU 5116  NZ  LYS C 274    14289   6424  13357   -346  -1199   4082       N  
ATOM   5117  N   ARG C 275     -16.806 -16.195   9.401  1.00 61.03           N  
ANISOU 5117  N   ARG C 275    10953   3617   8616   -630     26   1791       N  
ATOM   5118  CA  ARG C 275     -17.773 -15.120   9.531  1.00 58.47           C  
ANISOU 5118  CA  ARG C 275    10729   3541   7945   -689    110   1607       C  
ATOM   5119  C   ARG C 275     -19.087 -15.782   9.856  1.00 58.98           C  
ANISOU 5119  C   ARG C 275    10824   3566   8018   -796    314   1637       C  
ATOM   5120  O   ARG C 275     -19.340 -16.861   9.405  1.00 59.22           O  
ANISOU 5120  O   ARG C 275    10748   3377   8373   -809    412   1644       O  
ATOM   5121  CB  ARG C 275     -17.852 -14.292   8.233  1.00 54.51           C  
ANISOU 5121  CB  ARG C 275    10121   3115   7473   -627    149   1270       C  
ATOM   5122  CG  ARG C 275     -18.685 -13.000   8.319  1.00 51.63           C  
ANISOU 5122  CG  ARG C 275     9825   2985   6805   -661    205   1096       C  
ATOM   5123  CD  ARG C 275     -18.646 -12.236   6.978  1.00 48.09           C  
ANISOU 5123  CD  ARG C 275     9252   2601   6417   -588    220    838       C  
ATOM   5124  NE  ARG C 275     -17.277 -12.029   6.525  1.00 46.01           N  
ANISOU 5124  NE  ARG C 275     8921   2292   6265   -493     79    866       N  
ATOM   5125  CZ  ARG C 275     -16.871 -12.034   5.245  1.00 44.68           C  
ANISOU 5125  CZ  ARG C 275     8616   2099   6261   -419    105    718       C  
ATOM   5126  NH1 ARG C 275     -17.709 -12.204   4.211  1.00 43.59           N  
ANISOU 5126  NH1 ARG C 275     8395   2002   6165   -430    236    515       N  
ATOM   5127  NH2 ARG C 275     -15.567 -11.916   4.991  1.00 44.68           N  
ANISOU 5127  NH2 ARG C 275     8550   2042   6383   -339     -1    777       N  
ATOM   5128  N   ILE C 276     -19.907 -15.071  10.605  1.00 60.00           N  
ANISOU 5128  N   ILE C 276    11082   3902   7812   -873    389   1624       N  
ATOM   5129  CA  ILE C 276     -21.238 -15.481  10.940  1.00 62.04           C  
ANISOU 5129  CA  ILE C 276    11360   4160   8051   -980    609   1629       C  
ATOM   5130  C   ILE C 276     -22.060 -15.857   9.732  1.00 62.34           C  
ANISOU 5130  C   ILE C 276    11225   4080   8381   -986    752   1367       C  
ATOM   5131  O   ILE C 276     -21.840 -15.370   8.633  1.00 60.56           O  
ANISOU 5131  O   ILE C 276    10898   3881   8229   -913    701   1118       O  
ATOM   5132  CB  ILE C 276     -21.974 -14.405  11.788  1.00 62.50           C  
ANISOU 5132  CB  ILE C 276    11560   4486   7700  -1045    692   1569       C  
ATOM   5133  CG1 ILE C 276     -23.097 -15.057  12.616  1.00 65.67           C  
ANISOU 5133  CG1 ILE C 276    12017   4887   8045  -1171    917   1726       C  
ATOM   5134  CG2 ILE C 276     -22.551 -13.291  10.953  1.00 59.42           C  
ANISOU 5134  CG2 ILE C 276    11090   4208   7276  -1009    747   1225       C  
ATOM   5135  CD1 ILE C 276     -23.537 -14.239  13.807  1.00 66.62           C  
ANISOU 5135  CD1 ILE C 276    12317   5273   7721  -1244    998   1756       C  
ATOM   5136  N   SER C 277     -22.982 -16.786   9.946  1.00 67.49           N  
ANISOU 5136  N   SER C 277    11834   4601   9205  -1081    927   1440       N  
ATOM   5137  CA  SER C 277     -23.901 -17.216   8.910  1.00 68.66           C  
ANISOU 5137  CA  SER C 277    11809   4645   9632  -1117   1058   1181       C  
ATOM   5138  C   SER C 277     -25.199 -16.423   9.093  1.00 69.75           C  
ANISOU 5138  C   SER C 277    11952   4975   9573  -1186   1205   1038       C  
ATOM   5139  O   SER C 277     -25.427 -15.829  10.146  1.00 69.27           O  
ANISOU 5139  O   SER C 277    12033   5073   9210  -1222   1257   1169       O  
ATOM   5140  CB  SER C 277     -24.168 -18.679   9.071  1.00 70.87           C  
ANISOU 5140  CB  SER C 277    12010   4637  10278  -1192   1167   1338       C  
ATOM   5141  OG  SER C 277     -25.194 -18.857  10.034  1.00 73.92           O  
ANISOU 5141  OG  SER C 277    12455   5058  10573  -1311   1349   1510       O  
ATOM   5142  N   GLY C 278     -26.046 -16.436   8.071  1.00 70.28           N  
ANISOU 5142  N   GLY C 278    11852   5032   9819  -1206   1271    761       N  
ATOM   5143  CA  GLY C 278     -27.375 -15.862   8.168  1.00 70.71           C  
ANISOU 5143  CA  GLY C 278    11851   5218   9795  -1273   1420    635       C  
ATOM   5144  C   GLY C 278     -28.174 -16.419   9.325  1.00 75.84           C  
ANISOU 5144  C   GLY C 278    12554   5814  10448  -1396   1630    850       C  
ATOM   5145  O   GLY C 278     -28.780 -15.644  10.064  1.00 75.71           O  
ANISOU 5145  O   GLY C 278    12609   5967  10187  -1427   1747    868       O  
ATOM   5146  N   LYS C 279     -28.174 -17.752   9.474  1.00 82.03           N  
ANISOU 5146  N   LYS C 279    13290   6350  11527  -1465   1697   1011       N  
ATOM   5147  CA  LYS C 279     -28.976 -18.449  10.500  1.00 88.74           C  
ANISOU 5147  CA  LYS C 279    14161   7115  12441  -1596   1924   1259       C  
ATOM   5148  C   LYS C 279     -28.572 -18.104  11.900  1.00 87.67           C  
ANISOU 5148  C   LYS C 279    14261   7136  11914  -1607   1955   1576       C  
ATOM   5149  O   LYS C 279     -29.414 -17.812  12.730  1.00 92.06           O  
ANISOU 5149  O   LYS C 279    14872   7822  12281  -1690   2160   1652       O  
ATOM   5150  CB  LYS C 279     -28.813 -19.967  10.412  1.00100.00           C  
ANISOU 5150  CB  LYS C 279    15491   8201  14301  -1655   1964   1424       C  
ATOM   5151  CG  LYS C 279     -29.412 -20.643   9.184  1.00105.50           C  
ANISOU 5151  CG  LYS C 279    15935   8697  15450  -1698   1987   1110       C  
ATOM   5152  CD  LYS C 279     -28.532 -21.803   8.688  1.00107.49           C  
ANISOU 5152  CD  LYS C 279    16113   8630  16094  -1669   1897   1143       C  
ATOM   5153  CE  LYS C 279     -29.083 -22.467   7.426  1.00108.14           C  
ANISOU 5153  CE  LYS C 279    15949   8532  16604  -1724   1912    759       C  
ATOM   5154  NZ  LYS C 279     -30.274 -23.328   7.670  1.00111.73           N  
ANISOU 5154  NZ  LYS C 279    16244   8777  17428  -1887   2124    788       N  
ATOM   5155  N   MET C 280     -27.280 -18.171  12.178  1.00 83.54           N  
ANISOU 5155  N   MET C 280    13867   6607  11267  -1528   1756   1761       N  
ATOM   5156  CA  MET C 280     -26.769 -17.779  13.495  1.00 82.87           C  
ANISOU 5156  CA  MET C 280    14016   6720  10752  -1539   1724   2048       C  
ATOM   5157  C   MET C 280     -27.161 -16.351  13.847  1.00 78.64           C  
ANISOU 5157  C   MET C 280    13580   6495   9805  -1531   1770   1838       C  
ATOM   5158  O   MET C 280     -27.573 -16.062  14.980  1.00 77.96           O  
ANISOU 5158  O   MET C 280    13640   6595   9384  -1609   1918   1973       O  
ATOM   5159  CB  MET C 280     -25.258 -17.760  13.530  1.00 84.17           C  
ANISOU 5159  CB  MET C 280    14266   6871  10841  -1433   1439   2187       C  
ATOM   5160  CG  MET C 280     -24.459 -18.849  12.875  1.00 85.80           C  
ANISOU 5160  CG  MET C 280    14347   6766  11484  -1376   1315   2288       C  
ATOM   5161  SD  MET C 280     -24.134 -20.246  13.929  1.00 91.19           S  
ANISOU 5161  SD  MET C 280    15078   7241  12329  -1438   1343   2844       S  
ATOM   5162  CE  MET C 280     -25.377 -20.255  15.229  1.00 94.11           C  
ANISOU 5162  CE  MET C 280    15580   7796  12380  -1602   1629   3087       C  
ATOM   5163  N   ALA C 281     -26.952 -15.454  12.882  1.00 73.67           N  
ANISOU 5163  N   ALA C 281    12871   5919   9200  -1434   1641   1515       N  
ATOM   5164  CA  ALA C 281     -27.235 -14.049  13.077  1.00 71.42           C  
ANISOU 5164  CA  ALA C 281    12644   5873   8617  -1408   1666   1295       C  
ATOM   5165  C   ALA C 281     -28.682 -13.879  13.531  1.00 72.81           C  
ANISOU 5165  C   ALA C 281    12776   6123   8764  -1508   1970   1222       C  
ATOM   5166  O   ALA C 281     -28.943 -13.087  14.439  1.00 74.93           O  
ANISOU 5166  O   ALA C 281    13173   6595   8700  -1540   2083   1194       O  
ATOM   5167  CB  ALA C 281     -26.966 -13.268  11.813  1.00 68.17           C  
ANISOU 5167  CB  ALA C 281    12102   5460   8339  -1295   1513   1002       C  
ATOM   5168  N   LEU C 282     -29.616 -14.659  12.985  1.00 71.45           N  
ANISOU 5168  N   LEU C 282    12419   5785   8942  -1567   2116   1189       N  
ATOM   5169  CA  LEU C 282     -30.996 -14.588  13.484  1.00 72.88           C  
ANISOU 5169  CA  LEU C 282    12532   6018   9138  -1671   2426   1152       C  
ATOM   5170  C   LEU C 282     -31.182 -14.945  14.979  1.00 75.41           C  
ANISOU 5170  C   LEU C 282    13040   6442   9168  -1782   2640   1452       C  
ATOM   5171  O   LEU C 282     -32.246 -14.700  15.536  1.00 76.92           O  
ANISOU 5171  O   LEU C 282    13202   6725   9296  -1864   2927   1411       O  
ATOM   5172  CB  LEU C 282     -31.915 -15.436  12.607  1.00 73.59           C  
ANISOU 5172  CB  LEU C 282    12365   5896   9699  -1728   2517   1064       C  
ATOM   5173  CG  LEU C 282     -32.211 -14.864  11.235  1.00 71.29           C  
ANISOU 5173  CG  LEU C 282    11866   5601   9618  -1650   2381    727       C  
ATOM   5174  CD1 LEU C 282     -32.568 -15.932  10.235  1.00 71.28           C  
ANISOU 5174  CD1 LEU C 282    11651   5381  10051  -1696   2344    645       C  
ATOM   5175  CD2 LEU C 282     -33.363 -13.886  11.332  1.00 72.09           C  
ANISOU 5175  CD2 LEU C 282    11856   5840   9692  -1662   2557    538       C  
ATOM   5176  N   ASN C 283     -30.186 -15.583  15.607  1.00 76.08           N  
ANISOU 5176  N   ASN C 283    13298   6513   9095  -1789   2512   1772       N  
ATOM   5177  CA  ASN C 283     -30.261 -15.960  17.050  1.00 79.54           C  
ANISOU 5177  CA  ASN C 283    13934   7094   9192  -1897   2683   2118       C  
ATOM   5178  C   ASN C 283     -29.479 -15.054  17.974  1.00 80.20           C  
ANISOU 5178  C   ASN C 283    14273   7482   8715  -1873   2565   2137       C  
ATOM   5179  O   ASN C 283     -29.417 -15.308  19.175  1.00 83.19           O  
ANISOU 5179  O   ASN C 283    14841   8038   8726  -1961   2666   2422       O  
ATOM   5180  CB  ASN C 283     -29.758 -17.398  17.284  1.00 81.16           C  
ANISOU 5180  CB  ASN C 283    14151   7084   9603  -1938   2627   2549       C  
ATOM   5181  CG  ASN C 283     -30.491 -18.425  16.439  1.00 80.69           C  
ANISOU 5181  CG  ASN C 283    13833   6688  10137  -1983   2747   2527       C  
ATOM   5182  OD1 ASN C 283     -31.711 -18.378  16.296  1.00 80.35           O  
ANISOU 5182  OD1 ASN C 283    13646   6623  10260  -2060   3004   2374       O  
ATOM   5183  ND2 ASN C 283     -29.730 -19.357  15.844  1.00 80.05           N  
ANISOU 5183  ND2 ASN C 283    13671   6329  10412  -1936   2557   2652       N  
ATOM   5184  N   HIS C 284     -28.897 -13.989  17.432  1.00 77.74           N  
ANISOU 5184  N   HIS C 284    13963   7244   8329  -1764   2355   1835       N  
ATOM   5185  CA  HIS C 284     -28.139 -13.063  18.276  1.00 78.88           C  
ANISOU 5185  CA  HIS C 284    14329   7663   7977  -1750   2226   1794       C  
ATOM   5186  C   HIS C 284     -29.015 -12.321  19.306  1.00 81.31           C  
ANISOU 5186  C   HIS C 284    14753   8242   7898  -1845   2529   1659       C  
ATOM   5187  O   HIS C 284     -30.117 -11.909  18.996  1.00 79.48           O  
ANISOU 5187  O   HIS C 284    14378   7979   7841  -1858   2783   1416       O  
ATOM   5188  CB  HIS C 284     -27.387 -12.050  17.427  1.00 75.12           C  
ANISOU 5188  CB  HIS C 284    13795   7170   7575  -1620   1964   1491       C  
ATOM   5189  CG  HIS C 284     -26.186 -11.488  18.110  1.00 76.15           C  
ANISOU 5189  CG  HIS C 284    14120   7487   7326  -1599   1709   1533       C  
ATOM   5190  ND1 HIS C 284     -26.255 -10.438  18.992  1.00 78.19           N  
ANISOU 5190  ND1 HIS C 284    14530   8013   7164  -1644   1772   1341       N  
ATOM   5191  CD2 HIS C 284     -24.887 -11.861  18.074  1.00 76.02           C  
ANISOU 5191  CD2 HIS C 284    14155   7426   7303  -1546   1389   1738       C  
ATOM   5192  CE1 HIS C 284     -25.046 -10.163  19.442  1.00 79.10           C  
ANISOU 5192  CE1 HIS C 284    14784   8251   7020  -1626   1477   1410       C  
ATOM   5193  NE2 HIS C 284     -24.195 -11.009  18.894  1.00 77.19           N  
ANISOU 5193  NE2 HIS C 284    14475   7821   7031  -1562   1237   1666       N  
ATOM   5194  N   PRO C 285     -28.515 -12.152  20.531  1.00 86.13           N  
ANISOU 5194  N   PRO C 285    15614   9128   7983  -1912   2502   1807       N  
ATOM   5195  CA  PRO C 285     -29.261 -11.448  21.608  1.00 90.43           C  
ANISOU 5195  CA  PRO C 285    16297   9971   8088  -2013   2808   1651       C  
ATOM   5196  C   PRO C 285     -29.955 -10.116  21.196  1.00 89.06           C  
ANISOU 5196  C   PRO C 285    16003   9811   8021  -1962   2966   1135       C  
ATOM   5197  O   PRO C 285     -31.046  -9.798  21.685  1.00 89.50           O  
ANISOU 5197  O   PRO C 285    16040   9972   7994  -2034   3338    984       O  
ATOM   5198  CB  PRO C 285     -28.171 -11.157  22.661  1.00 93.10           C  
ANISOU 5198  CB  PRO C 285    16914  10614   7845  -2050   2578   1766       C  
ATOM   5199  CG  PRO C 285     -26.889 -11.730  22.135  1.00 91.44           C  
ANISOU 5199  CG  PRO C 285    16683  10239   7818  -1963   2155   2014       C  
ATOM   5200  CD  PRO C 285     -27.237 -12.690  21.042  1.00 88.41           C  
ANISOU 5200  CD  PRO C 285    16066   9484   8039  -1909   2188   2151       C  
ATOM   5201  N   TYR C 286     -29.272  -9.370  20.317  1.00 86.25           N  
ANISOU 5201  N   TYR C 286    15559   9341   7869  -1837   2685    898       N  
ATOM   5202  CA  TYR C 286     -29.797  -8.201  19.598  1.00 84.22           C  
ANISOU 5202  CA  TYR C 286    15125   9002   7871  -1753   2758    477       C  
ATOM   5203  C   TYR C 286     -31.285  -8.341  19.260  1.00 84.49           C  
ANISOU 5203  C   TYR C 286    14947   8928   8226  -1779   3114    384       C  
ATOM   5204  O   TYR C 286     -32.063  -7.458  19.570  1.00 86.46           O  
ANISOU 5204  O   TYR C 286    15148   9255   8446  -1790   3368     97       O  
ATOM   5205  CB  TYR C 286     -28.973  -7.939  18.324  1.00 80.73           C  
ANISOU 5205  CB  TYR C 286    14542   8356   7774  -1613   2414    409       C  
ATOM   5206  CG  TYR C 286     -29.347  -6.666  17.616  1.00 79.32           C  
ANISOU 5206  CG  TYR C 286    14191   8105   7839  -1520   2443     37       C  
ATOM   5207  CD1 TYR C 286     -29.005  -5.427  18.141  1.00 79.64           C  
ANISOU 5207  CD1 TYR C 286    14319   8271   7668  -1508   2425   -240       C  
ATOM   5208  CD2 TYR C 286     -30.088  -6.699  16.411  1.00 77.12           C  
ANISOU 5208  CD2 TYR C 286    13644   7629   8026  -1447   2487    -35       C  
ATOM   5209  CE1 TYR C 286     -29.392  -4.244  17.501  1.00 78.61           C  
ANISOU 5209  CE1 TYR C 286    14006   8035   7827  -1418   2470   -554       C  
ATOM   5210  CE2 TYR C 286     -30.480  -5.514  15.766  1.00 76.48           C  
ANISOU 5210  CE2 TYR C 286    13386   7483   8187  -1356   2510   -323       C  
ATOM   5211  CZ  TYR C 286     -30.129  -4.276  16.314  1.00 76.14           C  
ANISOU 5211  CZ  TYR C 286    13424   7529   7973  -1336   2510   -571       C  
ATOM   5212  OH  TYR C 286     -30.507  -3.101  15.679  1.00 74.19           O  
ANISOU 5212  OH  TYR C 286    12981   7178   8028  -1239   2537   -825       O  
ATOM   5213  N   PHE C 287     -31.685  -9.465  18.663  1.00 83.13           N  
ANISOU 5213  N   PHE C 287    14636   8567   8382  -1795   3139    615       N  
ATOM   5214  CA  PHE C 287     -33.080  -9.681  18.349  1.00 83.22           C  
ANISOU 5214  CA  PHE C 287    14423   8471   8725  -1833   3451    542       C  
ATOM   5215  C   PHE C 287     -33.724 -10.310  19.556  1.00 89.29           C  
ANISOU 5215  C   PHE C 287    15313   9383   9228  -1983   3796    750       C  
ATOM   5216  O   PHE C 287     -33.864 -11.536  19.645  1.00 94.04           O  
ANISOU 5216  O   PHE C 287    15904   9887   9939  -2059   3849   1082       O  
ATOM   5217  CB  PHE C 287     -33.236 -10.580  17.124  1.00 80.55           C  
ANISOU 5217  CB  PHE C 287    13861   7865   8879  -1797   3313    648       C  
ATOM   5218  CG  PHE C 287     -32.480 -10.122  15.933  1.00 76.56           C  
ANISOU 5218  CG  PHE C 287    13261   7251   8575  -1660   2969    503       C  
ATOM   5219  CD1 PHE C 287     -32.957  -9.061  15.179  1.00 75.71           C  
ANISOU 5219  CD1 PHE C 287    12967   7118   8678  -1570   2963    203       C  
ATOM   5220  CD2 PHE C 287     -31.291 -10.715  15.565  1.00 74.17           C  
ANISOU 5220  CD2 PHE C 287    13043   6872   8264  -1615   2663    681       C  
ATOM   5221  CE1 PHE C 287     -32.244  -8.580  14.095  1.00 72.30           C  
ANISOU 5221  CE1 PHE C 287    12456   6614   8398  -1446   2661    101       C  
ATOM   5222  CE2 PHE C 287     -30.591 -10.254  14.470  1.00 71.78           C  
ANISOU 5222  CE2 PHE C 287    12652   6491   8129  -1492   2382    545       C  
ATOM   5223  CZ  PHE C 287     -31.064  -9.183  13.733  1.00 70.41           C  
ANISOU 5223  CZ  PHE C 287    12313   6319   8121  -1411   2382    265       C  
ATOM   5224  N   ASN C 288     -34.139  -9.491  20.504  1.00 93.46           N  
ANISOU 5224  N   ASN C 288    15951  10141   9418  -2033   4058    559       N  
ATOM   5225  CA  ASN C 288     -35.079  -9.955  21.546  1.00 98.18           C  
ANISOU 5225  CA  ASN C 288    16604  10883   9815  -2179   4494    696       C  
ATOM   5226  C   ASN C 288     -36.291  -9.046  21.681  1.00100.70           C  
ANISOU 5226  C   ASN C 288    16757  11237  10266  -2184   4878    333       C  
ATOM   5227  O   ASN C 288     -36.976  -9.116  22.676  1.00106.38           O  
ANISOU 5227  O   ASN C 288    17553  12138  10728  -2297   5270    357       O  
ATOM   5228  CB  ASN C 288     -34.359 -10.101  22.882  1.00100.98           C  
ANISOU 5228  CB  ASN C 288    17310  11559   9498  -2275   4497    902       C  
ATOM   5229  CG  ASN C 288     -33.422 -11.282  22.904  1.00100.94           C  
ANISOU 5229  CG  ASN C 288    17426  11496   9430  -2294   4208   1374       C  
ATOM   5230  OD1 ASN C 288     -33.597 -12.238  22.150  1.00100.12           O  
ANISOU 5230  OD1 ASN C 288    17147  11112   9782  -2281   4150   1589       O  
ATOM   5231  ND2 ASN C 288     -32.398 -11.221  23.745  1.00102.46           N  
ANISOU 5231  ND2 ASN C 288    17901  11942   9086  -2324   4007   1526       N  
ATOM   5232  N   ASP C 289     -36.577  -8.202  20.679  1.00 98.19           N  
ANISOU 5232  N   ASP C 289    16197  10747  10364  -2059   4781     14       N  
ATOM   5233  CA  ASP C 289     -37.672  -7.232  20.812  1.00 98.57           C  
ANISOU 5233  CA  ASP C 289    16062  10805  10584  -2043   5129   -339       C  
ATOM   5234  C   ASP C 289     -38.192  -6.703  19.470  1.00 93.34           C  
ANISOU 5234  C   ASP C 289    15044   9885  10535  -1910   5001   -540       C  
ATOM   5235  O   ASP C 289     -39.206  -7.179  18.972  1.00 90.77           O  
ANISOU 5235  O   ASP C 289    14448   9410  10628  -1932   5155   -491       O  
ATOM   5236  CB  ASP C 289     -37.298  -6.089  21.813  1.00101.48           C  
ANISOU 5236  CB  ASP C 289    16653  11424  10480  -2051   5244   -642       C  
ATOM   5237  CG  ASP C 289     -35.756  -5.852  21.980  1.00100.35           C  
ANISOU 5237  CG  ASP C 289    16791  11400   9936  -2017   4823   -607       C  
ATOM   5238  OD1 ASP C 289     -35.081  -6.700  22.573  1.00100.98           O  
ANISOU 5238  OD1 ASP C 289    17110  11628   9627  -2101   4709   -283       O  
ATOM   5239  OD2 ASP C 289     -35.233  -4.784  21.561  1.00 97.82           O  
ANISOU 5239  OD2 ASP C 289    16436  11021   9708  -1911   4616   -895       O  
TER    5240      ASP C 289                                                      
ATOM   5241  N   GLN D   5      -8.547  15.493 -15.780  1.00 85.86           N  
ANISOU 5241  N   GLN D   5    12316   8499  11805    861  -2164   1555       N  
ATOM   5242  CA  GLN D   5      -7.490  15.913 -14.791  1.00 84.10           C  
ANISOU 5242  CA  GLN D   5    12094   8044  11814    833  -1845   1535       C  
ATOM   5243  C   GLN D   5      -7.334  15.023 -13.567  1.00 77.27           C  
ANISOU 5243  C   GLN D   5    10959   7270  11127    839  -1507   1167       C  
ATOM   5244  O   GLN D   5      -8.245  14.316 -13.161  1.00 80.70           O  
ANISOU 5244  O   GLN D   5    11136   7868  11655    925  -1522    914       O  
ATOM   5245  CB  GLN D   5      -7.746  17.324 -14.300  1.00 91.15           C  
ANISOU 5245  CB  GLN D   5    12998   8534  13098   1057  -2111   1662       C  
ATOM   5246  CG  GLN D   5      -7.697  18.348 -15.432  1.00101.66           C  
ANISOU 5246  CG  GLN D   5    14667   9666  14291   1017  -2466   2131       C  
ATOM   5247  CD  GLN D   5      -6.967  19.648 -15.068  1.00106.80           C  
ANISOU 5247  CD  GLN D   5    15522   9834  15220    997  -2532   2369       C  
ATOM   5248  OE1 GLN D   5      -6.547  19.858 -13.918  1.00107.70           O  
ANISOU 5248  OE1 GLN D   5    15520   9754  15644   1042  -2349   2134       O  
ATOM   5249  NE2 GLN D   5      -6.796  20.518 -16.064  1.00113.20           N  
ANISOU 5249  NE2 GLN D   5    16676  10440  15893    887  -2819   2856       N  
ATOM   5250  N   ILE D   6      -6.167  15.110 -12.960  1.00 70.90           N  
ANISOU 5250  N   ILE D   6    10205   6352  10381    721  -1231   1181       N  
ATOM   5251  CA  ILE D   6      -5.713  14.172 -11.953  1.00 65.26           C  
ANISOU 5251  CA  ILE D   6     9319   5733   9741    665   -919    927       C  
ATOM   5252  C   ILE D   6      -6.325  14.392 -10.559  1.00 64.12           C  
ANISOU 5252  C   ILE D   6     8964   5499   9900    845   -932    682       C  
ATOM   5253  O   ILE D   6      -6.288  15.507 -10.081  1.00 69.22           O  
ANISOU 5253  O   ILE D   6     9662   5886  10752    964  -1060    709       O  
ATOM   5254  CB  ILE D   6      -4.202  14.313 -11.817  1.00 63.26           C  
ANISOU 5254  CB  ILE D   6     9162   5397   9476    482   -688   1070       C  
ATOM   5255  CG1 ILE D   6      -3.549  13.905 -13.126  1.00 65.18           C  
ANISOU 5255  CG1 ILE D   6     9568   5821   9375    305   -539   1251       C  
ATOM   5256  CG2 ILE D   6      -3.671  13.489 -10.646  1.00 59.48           C  
ANISOU 5256  CG2 ILE D   6     8512   4962   9124    453   -458    858       C  
ATOM   5257  CD1 ILE D   6      -2.030  13.921 -13.111  1.00 65.42           C  
ANISOU 5257  CD1 ILE D   6     9587   5852   9416    120   -246   1393       C  
ATOM   5258  N   TYR D   7      -6.861  13.342  -9.906  1.00 60.71           N  
ANISOU 5258  N   TYR D   7     8325   5265   9475    844   -785    443       N  
ATOM   5259  CA  TYR D   7      -7.453  13.439  -8.550  1.00 59.13           C  
ANISOU 5259  CA  TYR D   7     7929   5070   9466    976   -713    208       C  
ATOM   5260  C   TYR D   7      -6.415  13.002  -7.500  1.00 52.96           C  
ANISOU 5260  C   TYR D   7     7203   4263   8656    838   -486    157       C  
ATOM   5261  O   TYR D   7      -5.636  12.110  -7.740  1.00 53.68           O  
ANISOU 5261  O   TYR D   7     7344   4417   8632    668   -355    231       O  
ATOM   5262  CB  TYR D   7      -8.809  12.702  -8.475  1.00 63.43           C  
ANISOU 5262  CB  TYR D   7     8184   5868  10047   1025   -715     42       C  
ATOM   5263  CG  TYR D   7      -9.325  12.330  -7.078  1.00 72.94           C  
ANISOU 5263  CG  TYR D   7     9168   7209  11334   1050   -493   -183       C  
ATOM   5264  CD1 TYR D   7      -8.841  11.148  -6.421  1.00 79.86           C  
ANISOU 5264  CD1 TYR D   7    10069   8193  12081    817   -259   -203       C  
ATOM   5265  CD2 TYR D   7     -10.324  13.084  -6.414  1.00 78.31           C  
ANISOU 5265  CD2 TYR D   7     9617   7930  12208   1306   -498   -372       C  
ATOM   5266  CE1 TYR D   7      -9.319  10.762  -5.151  1.00 84.89           C  
ANISOU 5266  CE1 TYR D   7    10551   8989  12711    781    -45   -348       C  
ATOM   5267  CE2 TYR D   7     -10.789  12.733  -5.124  1.00 83.39           C  
ANISOU 5267  CE2 TYR D   7    10073   8769  12839   1301   -217   -583       C  
ATOM   5268  CZ  TYR D   7     -10.292  11.581  -4.492  1.00 89.96           C  
ANISOU 5268  CZ  TYR D   7    10976   9730  13474   1010      5   -544       C  
ATOM   5269  OH  TYR D   7     -10.734  11.171  -3.239  1.00 99.69           O  
ANISOU 5269  OH  TYR D   7    12074  11186  14614    942    286   -684       O  
ATOM   5270  N   TYR D   8      -6.339  13.712  -6.383  1.00 49.07           N  
ANISOU 5270  N   TYR D   8     6725   3650   8269    929   -478     27       N  
ATOM   5271  CA  TYR D   8      -5.347  13.500  -5.351  1.00 44.80           C  
ANISOU 5271  CA  TYR D   8     6269   3069   7683    797   -368      0       C  
ATOM   5272  C   TYR D   8      -6.181  13.196  -4.113  1.00 47.27           C  
ANISOU 5272  C   TYR D   8     6466   3552   7941    867   -230   -247       C  
ATOM   5273  O   TYR D   8      -7.071  13.946  -3.791  1.00 53.32           O  
ANISOU 5273  O   TYR D   8     7160   4304   8793   1078   -252   -437       O  
ATOM   5274  CB  TYR D   8      -4.476  14.746  -5.098  1.00 43.58           C  
ANISOU 5274  CB  TYR D   8     6301   2611   7644    791   -523     48       C  
ATOM   5275  CG  TYR D   8      -3.486  15.073  -6.193  1.00 41.47           C  
ANISOU 5275  CG  TYR D   8     6132   2208   7416    642   -600    346       C  
ATOM   5276  CD1 TYR D   8      -3.910  15.685  -7.347  1.00 42.31           C  
ANISOU 5276  CD1 TYR D   8     6305   2221   7548    711   -733    504       C  
ATOM   5277  CD2 TYR D   8      -2.143  14.772  -6.092  1.00 39.68           C  
ANISOU 5277  CD2 TYR D   8     5907   1974   7194    428   -536    493       C  
ATOM   5278  CE1 TYR D   8      -3.043  15.933  -8.381  1.00 42.66           C  
ANISOU 5278  CE1 TYR D   8     6455   2206   7547    534   -744    807       C  
ATOM   5279  CE2 TYR D   8      -1.244  15.016  -7.138  1.00 39.81           C  
ANISOU 5279  CE2 TYR D   8     5949   1944   7232    271   -518    772       C  
ATOM   5280  CZ  TYR D   8      -1.720  15.555  -8.289  1.00 41.67           C  
ANISOU 5280  CZ  TYR D   8     6289   2129   7414    310   -590    928       C  
ATOM   5281  OH  TYR D   8      -0.906  15.876  -9.374  1.00 44.59           O  
ANISOU 5281  OH  TYR D   8     6724   2488   7727    123   -538   1238       O  
ATOM   5282  N   SER D   9      -5.894  12.112  -3.393  1.00 46.41           N  
ANISOU 5282  N   SER D   9     6339   3602   7690    698    -76   -238       N  
ATOM   5283  CA  SER D   9      -6.701  11.732  -2.229  1.00 46.96           C  
ANISOU 5283  CA  SER D   9     6318   3891   7631    698    102   -415       C  
ATOM   5284  C   SER D   9      -6.264  12.604  -1.102  1.00 47.60           C  
ANISOU 5284  C   SER D   9     6584   3880   7620    750     74   -575       C  
ATOM   5285  O   SER D   9      -5.158  13.148  -1.135  1.00 46.23           O  
ANISOU 5285  O   SER D   9     6592   3476   7495    695   -103   -493       O  
ATOM   5286  CB  SER D   9      -6.470  10.223  -1.844  1.00 46.65           C  
ANISOU 5286  CB  SER D   9     6268   4000   7454    452    231   -273       C  
ATOM   5287  OG  SER D   9      -5.146   9.944  -1.367  1.00 45.23           O  
ANISOU 5287  OG  SER D   9     6273   3698   7213    327    150   -129       O  
ATOM   5288  N   ASP D  10      -7.081  12.647  -0.084  1.00 50.35           N  
ANISOU 5288  N   ASP D  10     6882   4435   7812    813    263   -801       N  
ATOM   5289  CA  ASP D  10      -6.592  13.074   1.178  1.00 54.24           C  
ANISOU 5289  CA  ASP D  10     7617   4919   8072    776    269   -960       C  
ATOM   5290  C   ASP D  10      -5.446  12.190   1.617  1.00 52.68           C  
ANISOU 5290  C   ASP D  10     7579   4727   7707    493    175   -705       C  
ATOM   5291  O   ASP D  10      -5.197  11.135   1.030  1.00 51.64           O  
ANISOU 5291  O   ASP D  10     7345   4624   7651    358    181   -444       O  
ATOM   5292  CB  ASP D  10      -7.694  13.034   2.221  1.00 60.28           C  
ANISOU 5292  CB  ASP D  10     8298   6008   8597    854    583  -1236       C  
ATOM   5293  CG  ASP D  10      -8.683  14.148   2.050  1.00 64.84           C  
ANISOU 5293  CG  ASP D  10     8723   6536   9376   1220    652  -1572       C  
ATOM   5294  OD1 ASP D  10      -8.317  15.218   1.474  1.00 69.98           O  
ANISOU 5294  OD1 ASP D  10     9493   6808  10286   1406    388  -1631       O  
ATOM   5295  OD2 ASP D  10      -9.832  13.976   2.511  1.00 68.50           O  
ANISOU 5295  OD2 ASP D  10     8932   7328   9765   1326    972  -1767       O  
ATOM   5296  N   LYS D  11      -4.757  12.619   2.659  1.00 54.09           N  
ANISOU 5296  N   LYS D  11     8016   4863   7672    418     57   -800       N  
ATOM   5297  CA  LYS D  11      -3.666  11.858   3.187  1.00 54.25           C  
ANISOU 5297  CA  LYS D  11     8169   4891   7552    177   -104   -549       C  
ATOM   5298  C   LYS D  11      -4.123  10.982   4.348  1.00 58.13           C  
ANISOU 5298  C   LYS D  11     8760   5697   7627     24     75   -517       C  
ATOM   5299  O   LYS D  11      -5.177  11.231   4.953  1.00 62.59           O  
ANISOU 5299  O   LYS D  11     9330   6502   7949     95    351   -770       O  
ATOM   5300  CB  LYS D  11      -2.552  12.761   3.651  1.00 54.52           C  
ANISOU 5300  CB  LYS D  11     8424   4705   7585    117   -427   -612       C  
ATOM   5301  CG  LYS D  11      -1.911  13.510   2.525  1.00 51.83           C  
ANISOU 5301  CG  LYS D  11     7989   4051   7652    167   -610   -530       C  
ATOM   5302  CD  LYS D  11      -0.732  14.298   3.055  1.00 54.16           C  
ANISOU 5302  CD  LYS D  11     8466   4130   7980     17   -962   -550       C  
ATOM   5303  CE  LYS D  11      -0.213  15.283   2.027  1.00 54.02           C  
ANISOU 5303  CE  LYS D  11     8386   3783   8355     23  -1118   -481       C  
ATOM   5304  NZ  LYS D  11       0.507  16.439   2.657  1.00 58.56           N  
ANISOU 5304  NZ  LYS D  11     9197   4079   8972   -108  -1458   -644       N  
ATOM   5305  N   TYR D  12      -3.356   9.932   4.617  1.00 57.86           N  
ANISOU 5305  N   TYR D  12     8785   5667   7530   -178    -64   -186       N  
ATOM   5306  CA  TYR D  12      -3.680   8.987   5.697  1.00 61.50           C  
ANISOU 5306  CA  TYR D  12     9393   6387   7584   -383     52    -36       C  
ATOM   5307  C   TYR D  12      -2.367   8.395   6.187  1.00 63.61           C  
ANISOU 5307  C   TYR D  12     9828   6531   7807   -545   -319    286       C  
ATOM   5308  O   TYR D  12      -1.321   8.552   5.525  1.00 61.78           O  
ANISOU 5308  O   TYR D  12     9487   6046   7941   -485   -587    391       O  
ATOM   5309  CB  TYR D  12      -4.702   7.893   5.251  1.00 59.91           C  
ANISOU 5309  CB  TYR D  12     8976   6323   7461   -459    352    116       C  
ATOM   5310  CG  TYR D  12      -4.459   7.296   3.869  1.00 55.75           C  
ANISOU 5310  CG  TYR D  12     8223   5550   7406   -399    277    278       C  
ATOM   5311  CD1 TYR D  12      -3.622   6.175   3.691  1.00 54.47           C  
ANISOU 5311  CD1 TYR D  12     8102   5197   7397   -507     94    608       C  
ATOM   5312  CD2 TYR D  12      -5.017   7.853   2.742  1.00 52.42           C  
ANISOU 5312  CD2 TYR D  12     7577   5073   7265   -215    365     92       C  
ATOM   5313  CE1 TYR D  12      -3.383   5.625   2.437  1.00 51.23           C  
ANISOU 5313  CE1 TYR D  12     7523   4568   7370   -427     66    680       C  
ATOM   5314  CE2 TYR D  12      -4.776   7.286   1.486  1.00 50.41           C  
ANISOU 5314  CE2 TYR D  12     7182   4632   7338   -183    302    216       C  
ATOM   5315  CZ  TYR D  12      -3.966   6.168   1.346  1.00 49.94           C  
ANISOU 5315  CZ  TYR D  12     7179   4405   7390   -287    182    477       C  
ATOM   5316  OH  TYR D  12      -3.708   5.659   0.071  1.00 50.61           O  
ANISOU 5316  OH  TYR D  12     7155   4310   7765   -219    160    516       O  
ATOM   5317  N   ASP D  13      -2.389   7.780   7.376  1.00 68.82           N  
ANISOU 5317  N   ASP D  13    10742   7391   8014   -753   -348    454       N  
ATOM   5318  CA  ASP D  13      -1.142   7.269   7.981  1.00 70.93           C  
ANISOU 5318  CA  ASP D  13    11182   7549   8219   -892   -791    784       C  
ATOM   5319  C   ASP D  13      -1.253   6.126   9.009  1.00 73.89           C  
ANISOU 5319  C   ASP D  13    11811   8083   8179  -1144   -836   1158       C  
ATOM   5320  O   ASP D  13      -2.232   5.985   9.739  1.00 74.01           O  
ANISOU 5320  O   ASP D  13    11998   8409   7710  -1293   -520   1110       O  
ATOM   5321  CB  ASP D  13      -0.331   8.458   8.576  1.00 74.29           C  
ANISOU 5321  CB  ASP D  13    11799   7943   8484   -893  -1129    555       C  
ATOM   5322  CG  ASP D  13      -1.225   9.532   9.206  1.00 78.02           C  
ANISOU 5322  CG  ASP D  13    12491   8631   8522   -852   -872     76       C  
ATOM   5323  OD1 ASP D  13      -1.566   9.433  10.409  1.00 81.44           O  
ANISOU 5323  OD1 ASP D  13    13260   9357   8325  -1009   -808     25       O  
ATOM   5324  OD2 ASP D  13      -1.592  10.476   8.465  1.00 78.37           O  
ANISOU 5324  OD2 ASP D  13    12378   8541   8857   -644   -727   -250       O  
ATOM   5325  N   ASP D  14      -0.156   5.377   9.038  1.00 75.81           N  
ANISOU 5325  N   ASP D  14    12054   8101   8648  -1177  -1252   1542       N  
ATOM   5326  CA  ASP D  14       0.247   4.450  10.083  1.00 81.41           C  
ANISOU 5326  CA  ASP D  14    13057   8849   9024  -1393  -1549   1982       C  
ATOM   5327  C   ASP D  14       0.857   5.163  11.246  1.00 88.28           C  
ANISOU 5327  C   ASP D  14    14257   9902   9381  -1521  -1915   1924       C  
ATOM   5328  O   ASP D  14       0.849   6.388  11.316  1.00 94.66           O  
ANISOU 5328  O   ASP D  14    15101  10802  10062  -1458  -1888   1491       O  
ATOM   5329  CB  ASP D  14       1.439   3.652   9.600  1.00 81.02           C  
ANISOU 5329  CB  ASP D  14    12812   8430   9539  -1274  -1972   2345       C  
ATOM   5330  CG  ASP D  14       1.133   2.750   8.498  1.00 78.47           C  
ANISOU 5330  CG  ASP D  14    12231   7846   9737  -1146  -1740   2439       C  
ATOM   5331  OD1 ASP D  14       0.071   2.101   8.535  1.00 80.25           O  
ANISOU 5331  OD1 ASP D  14    12552   8138   9798  -1293  -1414   2514       O  
ATOM   5332  OD2 ASP D  14       2.022   2.601   7.646  1.00 78.01           O  
ANISOU 5332  OD2 ASP D  14    11877   7511  10251   -920  -1909   2465       O  
ATOM   5333  N   GLU D  15       1.428   4.394  12.162  1.00 93.87           N  
ANISOU 5333  N   GLU D  15    15239  10624   9803  -1705  -2320   2369       N  
ATOM   5334  CA  GLU D  15       2.482   4.907  12.997  1.00 98.25           C  
ANISOU 5334  CA  GLU D  15    16003  11222  10104  -1790  -2910   2412       C  
ATOM   5335  C   GLU D  15       3.809   5.036  12.228  1.00 97.07           C  
ANISOU 5335  C   GLU D  15    15429  10731  10721  -1585  -3360   2492       C  
ATOM   5336  O   GLU D  15       4.600   5.905  12.569  1.00101.81           O  
ANISOU 5336  O   GLU D  15    16049  11354  11279  -1628  -3762   2332       O  
ATOM   5337  CB  GLU D  15       2.613   4.072  14.250  1.00105.10           C  
ANISOU 5337  CB  GLU D  15    17325  12249  10359  -2067  -3236   2895       C  
ATOM   5338  CG  GLU D  15       1.437   4.279  15.207  1.00109.48           C  
ANISOU 5338  CG  GLU D  15    18338  13267   9990  -2324  -2786   2730       C  
ATOM   5339  CD  GLU D  15       1.441   3.305  16.390  1.00117.62           C  
ANISOU 5339  CD  GLU D  15    19860  14479  10350  -2658  -3034   3311       C  
ATOM   5340  OE1 GLU D  15       2.375   3.367  17.222  1.00122.91           O  
ANISOU 5340  OE1 GLU D  15    20827  15184  10689  -2778  -3689   3533       O  
ATOM   5341  OE2 GLU D  15       0.515   2.468  16.511  1.00118.76           O  
ANISOU 5341  OE2 GLU D  15    20105  14733  10282  -2838  -2610   3586       O  
ATOM   5342  N   GLU D  16       4.054   4.218  11.205  1.00 93.45           N  
ANISOU 5342  N   GLU D  16    14583   9973  10949  -1378  -3280   2705       N  
ATOM   5343  CA  GLU D  16       5.318   4.260  10.413  1.00 93.01           C  
ANISOU 5343  CA  GLU D  16    14051   9641  11646  -1158  -3607   2781       C  
ATOM   5344  C   GLU D  16       5.413   5.225   9.212  1.00 85.68           C  
ANISOU 5344  C   GLU D  16    12735   8637  11182   -989  -3317   2379       C  
ATOM   5345  O   GLU D  16       6.367   5.991   9.122  1.00 86.65           O  
ANISOU 5345  O   GLU D  16    12640   8723  11557   -991  -3632   2300       O  
ATOM   5346  CB  GLU D  16       5.710   2.858   9.914  1.00 96.94           C  
ANISOU 5346  CB  GLU D  16    14325   9826  12680   -972  -3693   3193       C  
ATOM   5347  CG  GLU D  16       5.719   1.715  10.969  1.00105.31           C  
ANISOU 5347  CG  GLU D  16    15753  10836  13422  -1118  -4046   3722       C  
ATOM   5348  CD  GLU D  16       6.875   1.765  11.972  1.00112.12           C  
ANISOU 5348  CD  GLU D  16    16696  11734  14171  -1195  -4814   4043       C  
ATOM   5349  OE1 GLU D  16       7.673   2.719  11.914  1.00114.50           O  
ANISOU 5349  OE1 GLU D  16    16753  12117  14635  -1172  -5081   3829       O  
ATOM   5350  OE2 GLU D  16       6.989   0.841  12.809  1.00116.32           O  
ANISOU 5350  OE2 GLU D  16    17534  12196  14466  -1302  -5189   4540       O  
ATOM   5351  N   PHE D  17       4.504   5.138   8.250  1.00 78.41           N  
ANISOU 5351  N   PHE D  17    11704   7675  10413   -868  -2769   2180       N  
ATOM   5352  CA  PHE D  17       4.501   6.073   7.099  1.00 71.01           C  
ANISOU 5352  CA  PHE D  17    10469   6677   9835   -732  -2501   1845       C  
ATOM   5353  C   PHE D  17       3.291   6.996   7.044  1.00 66.87           C  
ANISOU 5353  C   PHE D  17    10139   6309   8957   -769  -2112   1446       C  
ATOM   5354  O   PHE D  17       2.345   6.848   7.795  1.00 65.04           O  
ANISOU 5354  O   PHE D  17    10212   6272   8226   -878  -1938   1385       O  
ATOM   5355  CB  PHE D  17       4.446   5.315   5.782  1.00 68.09           C  
ANISOU 5355  CB  PHE D  17     9777   6118   9975   -513  -2196   1897       C  
ATOM   5356  CG  PHE D  17       5.606   4.421   5.525  1.00 70.20           C  
ANISOU 5356  CG  PHE D  17     9750   6182  10739   -360  -2464   2202       C  
ATOM   5357  CD1 PHE D  17       6.744   4.913   4.903  1.00 70.80           C  
ANISOU 5357  CD1 PHE D  17     9411   6202  11287   -252  -2591   2187       C  
ATOM   5358  CD2 PHE D  17       5.562   3.086   5.878  1.00 70.76           C  
ANISOU 5358  CD2 PHE D  17     9933   6100  10852   -315  -2575   2512       C  
ATOM   5359  CE1 PHE D  17       7.827   4.087   4.636  1.00 73.71           C  
ANISOU 5359  CE1 PHE D  17     9420   6407  12177    -52  -2793   2434       C  
ATOM   5360  CE2 PHE D  17       6.628   2.276   5.621  1.00 72.72           C  
ANISOU 5360  CE2 PHE D  17     9886   6114  11628    -99  -2827   2759       C  
ATOM   5361  CZ  PHE D  17       7.751   2.755   4.987  1.00 73.88           C  
ANISOU 5361  CZ  PHE D  17     9562   6245  12262     61  -2914   2700       C  
ATOM   5362  N   GLU D  18       3.366   7.989   6.141  1.00 64.21           N  
ANISOU 5362  N   GLU D  18     9602   5885   8907   -673  -1981   1189       N  
ATOM   5363  CA  GLU D  18       2.181   8.672   5.673  1.00 60.40           C  
ANISOU 5363  CA  GLU D  18     9182   5464   8300   -598  -1582    856       C  
ATOM   5364  C   GLU D  18       2.025   8.300   4.256  1.00 55.89           C  
ANISOU 5364  C   GLU D  18     8310   4771   8151   -437  -1315    895       C  
ATOM   5365  O   GLU D  18       2.967   7.884   3.567  1.00 55.11           O  
ANISOU 5365  O   GLU D  18     7951   4536   8452   -372  -1411   1083       O  
ATOM   5366  CB  GLU D  18       2.220  10.158   5.854  1.00 62.28           C  
ANISOU 5366  CB  GLU D  18     9541   5662   8460   -621  -1678    529       C  
ATOM   5367  CG  GLU D  18       3.251  10.897   5.024  1.00 63.30           C  
ANISOU 5367  CG  GLU D  18     9415   5569   9066   -620  -1872    562       C  
ATOM   5368  CD  GLU D  18       3.110  12.434   5.075  1.00 65.93           C  
ANISOU 5368  CD  GLU D  18     9913   5761   9375   -652  -1950    227       C  
ATOM   5369  OE1 GLU D  18       1.980  12.966   5.254  1.00 65.49           O  
ANISOU 5369  OE1 GLU D  18    10071   5743   9069   -541  -1712    -87       O  
ATOM   5370  OE2 GLU D  18       4.178  13.093   4.956  1.00 68.92           O  
ANISOU 5370  OE2 GLU D  18    10184   5971  10031   -793  -2272    289       O  
ATOM   5371  N   TYR D  19       0.794   8.429   3.825  1.00 54.15           N  
ANISOU 5371  N   TYR D  19     8117   4630   7826   -365   -969    700       N  
ATOM   5372  CA  TYR D  19       0.354   7.891   2.542  1.00 52.13           C  
ANISOU 5372  CA  TYR D  19     7651   4307   7846   -244   -711    720       C  
ATOM   5373  C   TYR D  19      -0.617   8.857   1.831  1.00 50.31           C  
ANISOU 5373  C   TYR D  19     7385   4108   7621   -136   -496    446       C  
ATOM   5374  O   TYR D  19      -1.363   9.640   2.486  1.00 48.36           O  
ANISOU 5374  O   TYR D  19     7277   3969   7128   -123   -435    213       O  
ATOM   5375  CB  TYR D  19      -0.471   6.578   2.741  1.00 52.80           C  
ANISOU 5375  CB  TYR D  19     7787   4466   7806   -306   -535    844       C  
ATOM   5376  CG  TYR D  19       0.254   5.429   3.354  1.00 55.58           C  
ANISOU 5376  CG  TYR D  19     8208   4724   8184   -388   -744   1164       C  
ATOM   5377  CD1 TYR D  19       0.955   4.525   2.559  1.00 55.40           C  
ANISOU 5377  CD1 TYR D  19     8018   4475   8556   -275   -793   1325       C  
ATOM   5378  CD2 TYR D  19       0.236   5.229   4.731  1.00 58.37           C  
ANISOU 5378  CD2 TYR D  19     8815   5206   8153   -560   -900   1305       C  
ATOM   5379  CE1 TYR D  19       1.653   3.481   3.123  1.00 58.49           C  
ANISOU 5379  CE1 TYR D  19     8460   4714   9050   -292  -1033   1629       C  
ATOM   5380  CE2 TYR D  19       0.924   4.195   5.309  1.00 60.91           C  
ANISOU 5380  CE2 TYR D  19     9225   5408   8509   -628  -1167   1660       C  
ATOM   5381  CZ  TYR D  19       1.639   3.286   4.528  1.00 61.13           C  
ANISOU 5381  CZ  TYR D  19     9057   5150   9020   -478  -1258   1839       C  
ATOM   5382  OH  TYR D  19       2.333   2.187   5.089  1.00 60.25           O  
ANISOU 5382  OH  TYR D  19     9020   4842   9028   -486  -1568   2214       O  
ATOM   5383  N   ARG D  20      -0.651   8.700   0.508  1.00 48.17           N  
ANISOU 5383  N   ARG D  20     6938   3752   7612    -40   -377    471       N  
ATOM   5384  CA  ARG D  20      -1.793   9.085  -0.271  1.00 48.42           C  
ANISOU 5384  CA  ARG D  20     6916   3835   7645     59   -189    302       C  
ATOM   5385  C   ARG D  20      -1.809   8.370  -1.556  1.00 45.75           C  
ANISOU 5385  C   ARG D  20     6448   3448   7484    102    -85    380       C  
ATOM   5386  O   ARG D  20      -0.789   7.805  -1.994  1.00 47.85           O  
ANISOU 5386  O   ARG D  20     6650   3613   7915    101   -120    525       O  
ATOM   5387  CB  ARG D  20      -1.759  10.603  -0.569  1.00 52.26           C  
ANISOU 5387  CB  ARG D  20     7436   4216   8202    148   -276    156       C  
ATOM   5388  CG  ARG D  20      -0.960  10.976  -1.808  1.00 51.85           C  
ANISOU 5388  CG  ARG D  20     7289   4015   8395    163   -325    290       C  
ATOM   5389  CD  ARG D  20      -1.482  12.260  -2.470  1.00 54.79           C  
ANISOU 5389  CD  ARG D  20     7708   4270   8839    263   -363    192       C  
ATOM   5390  NE  ARG D  20      -0.401  13.235  -2.200  1.00 55.74           N  
ANISOU 5390  NE  ARG D  20     7899   4192   9085    156   -569    253       N  
ATOM   5391  CZ  ARG D  20      -0.538  14.401  -1.629  1.00 54.30           C  
ANISOU 5391  CZ  ARG D  20     7881   3834   8914    175   -732     90       C  
ATOM   5392  NH1 ARG D  20      -1.747  14.923  -1.325  1.00 54.69           N  
ANISOU 5392  NH1 ARG D  20     8026   3873   8878    368   -685   -169       N  
ATOM   5393  NH2 ARG D  20       0.562  15.053  -1.420  1.00 55.69           N  
ANISOU 5393  NH2 ARG D  20     8098   3830   9231      3   -944    179       N  
ATOM   5394  N   HIS D  21      -2.931   8.451  -2.230  1.00 44.20           N  
ANISOU 5394  N   HIS D  21     6198   3328   7266    160     31    260       N  
ATOM   5395  CA  HIS D  21      -2.997   7.959  -3.610  1.00 44.14           C  
ANISOU 5395  CA  HIS D  21     6123   3283   7362    194     92    284       C  
ATOM   5396  C   HIS D  21      -3.527   9.027  -4.622  1.00 44.70           C  
ANISOU 5396  C   HIS D  21     6174   3362   7447    299     57    212       C  
ATOM   5397  O   HIS D  21      -4.266   9.940  -4.249  1.00 45.67           O  
ANISOU 5397  O   HIS D  21     6287   3516   7550    382     10    102       O  
ATOM   5398  CB  HIS D  21      -3.843   6.649  -3.694  1.00 43.63           C  
ANISOU 5398  CB  HIS D  21     6032   3274   7270    104    184    263       C  
ATOM   5399  CG  HIS D  21      -5.252   6.774  -3.187  1.00 42.69           C  
ANISOU 5399  CG  HIS D  21     5826   3339   7053     58    250    152       C  
ATOM   5400  ND1 HIS D  21      -5.567   6.618  -1.855  1.00 44.52           N  
ANISOU 5400  ND1 HIS D  21     6080   3689   7146    -38    322    168       N  
ATOM   5401  CD2 HIS D  21      -6.422   6.982  -3.829  1.00 43.07           C  
ANISOU 5401  CD2 HIS D  21     5731   3509   7122     89    263     34       C  
ATOM   5402  CE1 HIS D  21      -6.879   6.730  -1.696  1.00 46.46           C  
ANISOU 5402  CE1 HIS D  21     6162   4141   7346    -61    442     48       C  
ATOM   5403  NE2 HIS D  21      -7.430   6.943  -2.883  1.00 45.68           N  
ANISOU 5403  NE2 HIS D  21     5932   4040   7383     24    383    -32       N  
ATOM   5404  N   VAL D  22      -3.193   8.814  -5.885  1.00 44.80           N  
ANISOU 5404  N   VAL D  22     6196   3347   7479    309     83    269       N  
ATOM   5405  CA  VAL D  22      -3.495   9.692  -6.938  1.00 47.54           C  
ANISOU 5405  CA  VAL D  22     6577   3691   7793    371     16    290       C  
ATOM   5406  C   VAL D  22      -4.117   8.949  -8.097  1.00 49.50           C  
ANISOU 5406  C   VAL D  22     6843   4034   7930    355     38    240       C  
ATOM   5407  O   VAL D  22      -3.548   7.974  -8.580  1.00 50.79           O  
ANISOU 5407  O   VAL D  22     7050   4191   8057    305    155    228       O  
ATOM   5408  CB  VAL D  22      -2.193  10.314  -7.464  1.00 50.25           C  
ANISOU 5408  CB  VAL D  22     6969   3940   8181    334     31    459       C  
ATOM   5409  CG1 VAL D  22      -2.482  11.353  -8.520  1.00 52.02           C  
ANISOU 5409  CG1 VAL D  22     7290   4135   8341    359    -65    560       C  
ATOM   5410  CG2 VAL D  22      -1.431  11.019  -6.344  1.00 51.46           C  
ANISOU 5410  CG2 VAL D  22     7109   3975   8466    295    -55    504       C  
ATOM   5411  N   MET D  23      -5.259   9.435  -8.563  1.00 50.58           N  
ANISOU 5411  N   MET D  23     6948   4243   8027    414   -102    193       N  
ATOM   5412  CA  MET D  23      -5.978   8.815  -9.625  1.00 52.90           C  
ANISOU 5412  CA  MET D  23     7262   4642   8193    369   -172    133       C  
ATOM   5413  C   MET D  23      -5.706   9.534 -10.924  1.00 53.44           C  
ANISOU 5413  C   MET D  23     7499   4718   8087    393   -273    265       C  
ATOM   5414  O   MET D  23      -6.073  10.694 -11.088  1.00 53.13           O  
ANISOU 5414  O   MET D  23     7467   4632   8086    490   -455    377       O  
ATOM   5415  CB  MET D  23      -7.475   8.738  -9.289  1.00 58.75           C  
ANISOU 5415  CB  MET D  23     7794   5507   9022    388   -300     16       C  
ATOM   5416  CG  MET D  23      -7.782   7.865  -8.053  1.00 63.34           C  
ANISOU 5416  CG  MET D  23     8231   6130   9705    285   -145    -71       C  
ATOM   5417  SD  MET D  23      -9.474   7.715  -7.404  1.00 80.14           S  
ANISOU 5417  SD  MET D  23    10003   8481  11965    251   -165   -191       S  
ATOM   5418  CE  MET D  23     -10.496   8.194  -8.825  1.00 84.26           C  
ANISOU 5418  CE  MET D  23    10406   9105  12502    335   -492   -210       C  
ATOM   5419  N   LEU D  24      -5.058   8.820 -11.859  1.00 54.45           N  
ANISOU 5419  N   LEU D  24     7784   4892   8008    308   -145    251       N  
ATOM   5420  CA  LEU D  24      -4.803   9.289 -13.219  1.00 55.39           C  
ANISOU 5420  CA  LEU D  24     8117   5094   7832    276   -186    378       C  
ATOM   5421  C   LEU D  24      -5.965   9.061 -14.165  1.00 59.73           C  
ANISOU 5421  C   LEU D  24     8757   5778   8160    244   -453    304       C  
ATOM   5422  O   LEU D  24      -6.749   8.145 -13.962  1.00 57.58           O  
ANISOU 5422  O   LEU D  24     8385   5541   7949    197   -528     97       O  
ATOM   5423  CB  LEU D  24      -3.633   8.602 -13.840  1.00 54.63           C  
ANISOU 5423  CB  LEU D  24     8148   5048   7559    218    121    338       C  
ATOM   5424  CG  LEU D  24      -2.342   8.476 -13.068  1.00 53.53           C  
ANISOU 5424  CG  LEU D  24     7868   4816   7653    240    387    384       C  
ATOM   5425  CD1 LEU D  24      -1.290   7.819 -13.936  1.00 55.56           C  
ANISOU 5425  CD1 LEU D  24     8203   5174   7731    233    716    317       C  
ATOM   5426  CD2 LEU D  24      -1.838   9.799 -12.595  1.00 54.64           C  
ANISOU 5426  CD2 LEU D  24     7938   4870   7949    223    329    640       C  
ATOM   5427  N   PRO D  25      -6.110   9.951 -15.185  1.00 67.03           N  
ANISOU 5427  N   PRO D  25     9867   6767   8833    240   -648    513       N  
ATOM   5428  CA  PRO D  25      -7.067   9.703 -16.256  1.00 74.04           C  
ANISOU 5428  CA  PRO D  25    10892   7815   9424    183   -955    469       C  
ATOM   5429  C   PRO D  25      -6.676   8.466 -17.027  1.00 80.79           C  
ANISOU 5429  C   PRO D  25    11971   8790   9934     46   -767    225       C  
ATOM   5430  O   PRO D  25      -5.484   8.237 -17.224  1.00 80.74           O  
ANISOU 5430  O   PRO D  25    12096   8790   9791     27   -393    215       O  
ATOM   5431  CB  PRO D  25      -6.934  10.949 -17.141  1.00 75.68           C  
ANISOU 5431  CB  PRO D  25    11331   8035   9389    190  -1152    825       C  
ATOM   5432  CG  PRO D  25      -5.664  11.583 -16.710  1.00 72.37           C  
ANISOU 5432  CG  PRO D  25    10932   7480   9085    180   -834   1012       C  
ATOM   5433  CD  PRO D  25      -5.620  11.342 -15.264  1.00 67.23           C  
ANISOU 5433  CD  PRO D  25     9971   6679   8892    280   -703    835       C  
ATOM   5434  N   LYS D  26      -7.678   7.743 -17.534  1.00 90.74           N  
ANISOU 5434  N   LYS D  26    13272  10148  11057    -44  -1045     23       N  
ATOM   5435  CA  LYS D  26      -7.547   6.297 -17.833  1.00 95.58           C  
ANISOU 5435  CA  LYS D  26    14033  10754  11528   -164   -902   -340       C  
ATOM   5436  C   LYS D  26      -6.460   5.961 -18.866  1.00 99.95           C  
ANISOU 5436  C   LYS D  26    14974  11403  11598   -193   -583   -443       C  
ATOM   5437  O   LYS D  26      -5.396   5.485 -18.463  1.00 99.71           O  
ANISOU 5437  O   LYS D  26    14913  11268  11704   -116   -159   -545       O  
ATOM   5438  CB  LYS D  26      -8.900   5.684 -18.157  1.00 98.13           C  
ANISOU 5438  CB  LYS D  26    14306  11140  11836   -311  -1332   -525       C  
ATOM   5439  CG  LYS D  26      -9.831   5.707 -16.960  1.00 96.54           C  
ANISOU 5439  CG  LYS D  26    13636  10869  12174   -295  -1472   -494       C  
ATOM   5440  CD  LYS D  26      -9.698   4.478 -16.086  1.00 95.65           C  
ANISOU 5440  CD  LYS D  26    13417  10573  12351   -398  -1238   -718       C  
ATOM   5441  CE  LYS D  26     -10.723   4.518 -14.959  1.00 96.65           C  
ANISOU 5441  CE  LYS D  26    13082  10715  12926   -438  -1345   -660       C  
ATOM   5442  NZ  LYS D  26     -12.123   4.243 -15.415  1.00100.59           N  
ANISOU 5442  NZ  LYS D  26    13381  11365  13473   -623  -1777   -743       N  
ATOM   5443  N  AASP D  27      -6.748   6.378 -20.121  0.50102.94           N  
ANISOU 5443  N  AASP D  27    15674  12003  11433   -284   -804   -360       N  
ATOM   5444  N  BASP D  27      -6.718   5.959 -20.159  0.50108.37           N  
ANISOU 5444  N  BASP D  27    16398  12674  12104   -302   -758   -492       N  
ATOM   5445  CA AASP D  27      -5.845   6.921 -21.198  0.50107.14           C  
ANISOU 5445  CA AASP D  27    16565  12748  11394   -322   -561   -193       C  
ATOM   5446  CA BASP D  27      -5.605   5.428 -21.042  0.50116.46           C  
ANISOU 5446  CA BASP D  27    17780  13814  12652   -312   -316   -696       C  
ATOM   5447  C  AASP D  27      -4.349   6.864 -21.075  0.50105.34           C  
ANISOU 5447  C  AASP D  27    16324  12527  11171   -252     57   -188       C  
ATOM   5448  C  BASP D  27      -4.281   6.471 -21.028  0.50110.51           C  
ANISOU 5448  C  BASP D  27    16981  13157  11851   -237    125   -322       C  
ATOM   5449  O  AASP D  27      -3.620   6.680 -22.039  0.50108.18           O  
ANISOU 5449  O  AASP D  27    16981  13103  11017   -303    383   -269       O  
ATOM   5450  O  BASP D  27      -3.626   6.671 -22.046  0.50112.89           O  
ANISOU 5450  O  BASP D  27    17581  13700  11610   -303    382   -272       O  
ATOM   5451  CB AASP D  27      -6.260   8.349 -21.628  1.00111.06           C  
ANISOU 5451  CB AASP D  27    17133  13340  11723   -350   -918    295       C  
ATOM   5452  CB BASP D  27      -6.142   4.662 -22.404  1.00131.70           C  
ANISOU 5452  CB BASP D  27    20194  15926  13919   -477   -535  -1047       C  
ATOM   5453  CG AASP D  27      -6.863   8.397 -23.024  1.00118.25           C  
ANISOU 5453  CG AASP D  27    18479  14512  11937   -506  -1285    331       C  
ATOM   5454  CG BASP D  27      -6.130   3.079 -22.307  1.00135.97           C  
ANISOU 5454  CG BASP D  27    20838  16247  14577   -488   -412  -1621       C  
ATOM   5455  OD1AASP D  27      -6.541   7.540 -23.894  1.00126.40           O  
ANISOU 5455  OD1AASP D  27    19873  15729  12422   -616  -1092     10       O  
ATOM   5456  OD1BASP D  27      -5.292   2.483 -21.599  1.00135.44           O  
ANISOU 5456  OD1BASP D  27    20610  15956  14894   -332      4  -1770       O  
ATOM   5457  OD2AASP D  27      -7.649   9.329 -23.264  1.00121.25           O  
ANISOU 5457  OD2AASP D  27    18861  14906  12303   -503  -1790    681       O  
ATOM   5458  OD2BASP D  27      -6.962   2.426 -22.984  1.00144.46           O  
ANISOU 5458  OD2BASP D  27    22182  17344  15360   -663   -782  -1922       O  
ATOM   5459  N   ILE D  28      -3.934   7.146 -19.881  1.00101.78           N  
ANISOU 5459  N   ILE D  28    15505  11873  11291   -143    194    -59       N  
ATOM   5460  CA  ILE D  28      -2.521   7.410 -19.523  1.00 98.09           C  
ANISOU 5460  CA  ILE D  28    14881  11396  10992    -82    683     70       C  
ATOM   5461  C   ILE D  28      -1.928   6.162 -18.867  1.00 97.62           C  
ANISOU 5461  C   ILE D  28    14646  11177  11266     53    988   -289       C  
ATOM   5462  O   ILE D  28      -0.758   5.848 -19.066  1.00101.73           O  
ANISOU 5462  O   ILE D  28    15119  11768  11766    129   1444   -368       O  
ATOM   5463  CB  ILE D  28      -2.379   8.608 -18.545  1.00 93.05           C  
ANISOU 5463  CB  ILE D  28    13963  10597  10795    -63    563    455       C  
ATOM   5464  CG1 ILE D  28      -2.366   9.919 -19.312  1.00 93.80           C  
ANISOU 5464  CG1 ILE D  28    14258  10799  10580   -191    426    884       C  
ATOM   5465  CG2 ILE D  28      -1.109   8.516 -17.711  1.00 92.21           C  
ANISOU 5465  CG2 ILE D  28    13563  10396  11074      1    948    480       C  
ATOM   5466  CD1 ILE D  28      -2.205  11.167 -18.455  1.00 91.50           C  
ANISOU 5466  CD1 ILE D  28    13769  10278  10719   -183    278   1236       C  
ATOM   5467  N   ALA D  29      -2.730   5.479 -18.056  1.00 94.69           N  
ANISOU 5467  N   ALA D  29    14150  10587  11239     85    733   -471       N  
ATOM   5468  CA  ALA D  29      -2.373   4.190 -17.481  1.00 96.50           C  
ANISOU 5468  CA  ALA D  29    14292  10595  11776    190    912   -786       C  
ATOM   5469  C   ALA D  29      -1.903   3.118 -18.462  1.00103.14           C  
ANISOU 5469  C   ALA D  29    15418  11462  12306    251   1188  -1195       C  
ATOM   5470  O   ALA D  29      -1.294   2.113 -18.023  1.00110.76           O  
ANISOU 5470  O   ALA D  29    16303  12195  13586    408   1406  -1435       O  
ATOM   5471  CB  ALA D  29      -3.537   3.652 -16.665  1.00 98.43           C  
ANISOU 5471  CB  ALA D  29    14435  10639  12324    119    553   -873       C  
ATOM   5472  N   LYS D  30      -2.220   3.264 -19.760  1.00103.94           N  
ANISOU 5472  N   LYS D  30    15882  11815  11795    143   1150  -1301       N  
ATOM   5473  CA  LYS D  30      -1.562   2.447 -20.807  1.00107.02           C  
ANISOU 5473  CA  LYS D  30    16586  12308  11769    224   1526  -1712       C  
ATOM   5474  C   LYS D  30      -0.056   2.452 -20.567  1.00102.97           C  
ANISOU 5474  C   LYS D  30    15808  11831  11484    441   2107  -1677       C  
ATOM   5475  O   LYS D  30       0.639   1.468 -20.879  1.00113.47           O  
ANISOU 5475  O   LYS D  30    17206  13084  12822    642   2476  -2088       O  
ATOM   5476  CB  LYS D  30      -1.869   2.951 -22.250  1.00113.35           C  
ANISOU 5476  CB  LYS D  30    17826  13494  11746     53   1475  -1706       C  
ATOM   5477  CG  LYS D  30      -2.750   2.044 -23.122  1.00120.65           C  
ANISOU 5477  CG  LYS D  30    19210  14408  12222    -63   1185  -2171       C  
ATOM   5478  CD  LYS D  30      -1.985   1.158 -24.108  1.00128.40           C  
ANISOU 5478  CD  LYS D  30    20570  15491  12724     52   1660  -2706       C  
ATOM   5479  CE  LYS D  30      -2.926   0.148 -24.755  1.00132.09           C  
ANISOU 5479  CE  LYS D  30    21496  15824  12867    -82   1277  -3231       C  
ATOM   5480  NZ  LYS D  30      -2.263  -0.704 -25.778  1.00138.81           N  
ANISOU 5480  NZ  LYS D  30    22802  16761  13178     42   1720  -3841       N  
ATOM   5481  N   LEU D  31       0.426   3.562 -20.029  1.00 93.29           N  
ANISOU 5481  N   LEU D  31    14267  10707  10470    404   2162  -1206       N  
ATOM   5482  CA  LEU D  31       1.809   3.926 -20.076  1.00 93.97           C  
ANISOU 5482  CA  LEU D  31    14089  10968  10648    501   2674  -1061       C  
ATOM   5483  C   LEU D  31       2.400   4.010 -18.698  1.00 85.95           C  
ANISOU 5483  C   LEU D  31    12591   9710  10356    617   2653   -862       C  
ATOM   5484  O   LEU D  31       3.504   4.507 -18.539  1.00 85.17           O  
ANISOU 5484  O   LEU D  31    12170   9745  10446    646   2969   -647       O  
ATOM   5485  CB  LEU D  31       1.927   5.274 -20.818  1.00 97.74           C  
ANISOU 5485  CB  LEU D  31    14675  11797  10662    263   2728   -630       C  
ATOM   5486  CG  LEU D  31       0.996   5.399 -22.059  1.00102.47           C  
ANISOU 5486  CG  LEU D  31    15818  12622  10494     83   2510   -699       C  
ATOM   5487  CD1 LEU D  31       0.946   6.824 -22.578  1.00104.62           C  
ANISOU 5487  CD1 LEU D  31    16209  13132  10409   -166   2404   -148       C  
ATOM   5488  CD2 LEU D  31       1.355   4.435 -23.189  1.00108.59           C  
ANISOU 5488  CD2 LEU D  31    16935  13613  10708    164   2920  -1197       C  
ATOM   5489  N   VAL D  32       1.693   3.476 -17.716  1.00 81.37           N  
ANISOU 5489  N   VAL D  32    11958   8795  10162    657   2284   -935       N  
ATOM   5490  CA  VAL D  32       2.268   3.268 -16.395  1.00 78.39           C  
ANISOU 5490  CA  VAL D  32    11197   8171  10413    786   2251   -814       C  
ATOM   5491  C   VAL D  32       2.952   1.914 -16.419  1.00 81.28           C  
ANISOU 5491  C   VAL D  32    11516   8339  11025   1065   2514  -1185       C  
ATOM   5492  O   VAL D  32       2.286   0.910 -16.707  1.00 81.36           O  
ANISOU 5492  O   VAL D  32    11823   8142  10947   1103   2401  -1536       O  
ATOM   5493  CB  VAL D  32       1.206   3.219 -15.310  1.00 74.52           C  
ANISOU 5493  CB  VAL D  32    10703   7433  10177    692   1784   -718       C  
ATOM   5494  CG1 VAL D  32       1.779   2.735 -13.986  1.00 74.45           C  
ANISOU 5494  CG1 VAL D  32    10401   7163  10723    822   1738   -638       C  
ATOM   5495  CG2 VAL D  32       0.626   4.592 -15.125  1.00 72.71           C  
ANISOU 5495  CG2 VAL D  32    10454   7343   9828    504   1536   -378       C  
ATOM   5496  N   PRO D  33       4.268   1.867 -16.108  1.00 81.97           N  
ANISOU 5496  N   PRO D  33    11216   8456  11472   1264   2829  -1115       N  
ATOM   5497  CA  PRO D  33       4.983   0.578 -16.122  1.00 85.40           C  
ANISOU 5497  CA  PRO D  33    11559   8658  12229   1614   3073  -1475       C  
ATOM   5498  C   PRO D  33       4.308  -0.443 -15.210  1.00 84.06           C  
ANISOU 5498  C   PRO D  33    11521   7995  12421   1673   2674  -1579       C  
ATOM   5499  O   PRO D  33       3.929  -0.112 -14.092  1.00 79.01           O  
ANISOU 5499  O   PRO D  33    10764   7230  12025   1531   2314  -1259       O  
ATOM   5500  CB  PRO D  33       6.359   0.924 -15.580  1.00 85.89           C  
ANISOU 5500  CB  PRO D  33    11056   8824  12754   1773   3303  -1234       C  
ATOM   5501  CG  PRO D  33       6.129   2.125 -14.752  1.00 82.19           C  
ANISOU 5501  CG  PRO D  33    10438   8439  12352   1480   2972   -754       C  
ATOM   5502  CD  PRO D  33       5.059   2.910 -15.444  1.00 79.57           C  
ANISOU 5502  CD  PRO D  33    10498   8293  11441   1184   2845   -690       C  
ATOM   5503  N   LYS D  34       4.091  -1.641 -15.743  1.00 89.09           N  
ANISOU 5503  N   LYS D  34    12454   8362  13032   1840   2741  -2034       N  
ATOM   5504  CA  LYS D  34       3.334  -2.682 -15.046  1.00 89.25           C  
ANISOU 5504  CA  LYS D  34    12684   7875  13349   1820   2357  -2135       C  
ATOM   5505  C   LYS D  34       4.211  -3.553 -14.183  1.00 88.96           C  
ANISOU 5505  C   LYS D  34    12397   7432  13971   2148   2347  -2110       C  
ATOM   5506  O   LYS D  34       3.787  -3.978 -13.125  1.00 84.77           O  
ANISOU 5506  O   LYS D  34    11885   6561  13762   2058   1971  -1894       O  
ATOM   5507  CB  LYS D  34       2.507  -3.519 -16.049  1.00 96.02           C  
ANISOU 5507  CB  LYS D  34    14055   8570  13854   1756   2323  -2633       C  
ATOM   5508  CG  LYS D  34       1.145  -2.883 -16.340  1.00 96.23           C  
ANISOU 5508  CG  LYS D  34    14329   8818  13415   1337   1996  -2524       C  
ATOM   5509  CD  LYS D  34       0.573  -3.186 -17.719  1.00101.95           C  
ANISOU 5509  CD  LYS D  34    15516   9658  13559   1238   2034  -2973       C  
ATOM   5510  CE  LYS D  34      -0.640  -2.291 -17.996  1.00100.10           C  
ANISOU 5510  CE  LYS D  34    15399   9736  12896    857   1682  -2753       C  
ATOM   5511  NZ  LYS D  34      -1.330  -2.618 -19.277  1.00105.65           N  
ANISOU 5511  NZ  LYS D  34    16579  10547  13015    704   1579  -3158       N  
ATOM   5512  N   THR D  35       5.433  -3.796 -14.634  1.00 92.94           N  
ANISOU 5512  N   THR D  35    12648   7995  14669   2528   2761  -2305       N  
ATOM   5513  CA  THR D  35       6.350  -4.660 -13.927  1.00 96.96           C  
ANISOU 5513  CA  THR D  35    12876   8105  15859   2923   2740  -2302       C  
ATOM   5514  C   THR D  35       7.415  -3.945 -13.076  1.00 94.56           C  
ANISOU 5514  C   THR D  35    11963   8016  15950   3016   2738  -1850       C  
ATOM   5515  O   THR D  35       8.383  -4.568 -12.675  1.00 98.50           O  
ANISOU 5515  O   THR D  35    12127   8277  17019   3405   2772  -1857       O  
ATOM   5516  CB  THR D  35       7.074  -5.564 -14.936  1.00106.80           C  
ANISOU 5516  CB  THR D  35    14169   9214  17194   3382   3198  -2885       C  
ATOM   5517  OG1 THR D  35       7.828  -4.731 -15.814  1.00111.27           O  
ANISOU 5517  OG1 THR D  35    14457  10385  17435   3439   3743  -2948       O  
ATOM   5518  CG2 THR D  35       6.081  -6.426 -15.758  1.00109.76           C  
ANISOU 5518  CG2 THR D  35    15204   9283  17216   3300   3139  -3411       C  
ATOM   5519  N   HIS D  36       7.267  -2.656 -12.823  1.00 89.87           N  
ANISOU 5519  N   HIS D  36    11216   7840  15089   2677   2668  -1475       N  
ATOM   5520  CA  HIS D  36       8.105  -1.956 -11.837  1.00 89.07           C  
ANISOU 5520  CA  HIS D  36    10607   7879  15355   2662   2517  -1026       C  
ATOM   5521  C   HIS D  36       7.499  -0.659 -11.346  1.00 83.66           C  
ANISOU 5521  C   HIS D  36     9965   7467  14352   2219   2268   -653       C  
ATOM   5522  O   HIS D  36       6.668  -0.013 -12.037  1.00 84.05           O  
ANISOU 5522  O   HIS D  36    10312   7743  13880   1956   2341   -711       O  
ATOM   5523  CB  HIS D  36       9.509  -1.652 -12.372  1.00 95.52           C  
ANISOU 5523  CB  HIS D  36    10870   9019  16402   2918   2978  -1060       C  
ATOM   5524  CG  HIS D  36       9.569  -0.575 -13.420  1.00 97.71           C  
ANISOU 5524  CG  HIS D  36    11129   9834  16159   2678   3393  -1064       C  
ATOM   5525  ND1 HIS D  36       9.609  -0.858 -14.774  1.00103.90           N  
ANISOU 5525  ND1 HIS D  36    12103  10819  16552   2802   3915  -1477       N  
ATOM   5526  CD2 HIS D  36       9.666   0.775 -13.322  1.00 95.92           C  
ANISOU 5526  CD2 HIS D  36    10736   9968  15740   2319   3364   -690       C  
ATOM   5527  CE1 HIS D  36       9.700   0.270 -15.461  1.00104.41           C  
ANISOU 5527  CE1 HIS D  36    12128  11371  16171   2506   4185  -1304       C  
ATOM   5528  NE2 HIS D  36       9.727   1.277 -14.602  1.00100.19           N  
ANISOU 5528  NE2 HIS D  36    11377  10906  15784   2210   3844   -820       N  
ATOM   5529  N   LEU D  37       7.970  -0.233 -10.183  1.00 79.75           N  
ANISOU 5529  N   LEU D  37     9170   6955  14176   2156   1959   -280       N  
ATOM   5530  CA  LEU D  37       7.565   1.064  -9.592  1.00 73.14           C  
ANISOU 5530  CA  LEU D  37     8342   6340  13107   1779   1717     43       C  
ATOM   5531  C   LEU D  37       8.448   2.197 -10.082  1.00 74.10           C  
ANISOU 5531  C   LEU D  37     8098   6846  13210   1675   1973    190       C  
ATOM   5532  O   LEU D  37       9.570   1.961 -10.542  1.00 79.91           O  
ANISOU 5532  O   LEU D  37     8426   7706  14228   1899   2293    131       O  
ATOM   5533  CB  LEU D  37       7.656   0.994  -8.077  1.00 69.54           C  
ANISOU 5533  CB  LEU D  37     7800   5687  12933   1724   1240    344       C  
ATOM   5534  CG  LEU D  37       6.878  -0.153  -7.435  1.00 66.61           C  
ANISOU 5534  CG  LEU D  37     7767   4922  12618   1773    970    306       C  
ATOM   5535  CD1 LEU D  37       7.275  -0.298  -5.972  1.00 65.60           C  
ANISOU 5535  CD1 LEU D  37     7518   4639  12768   1755    530    649       C  
ATOM   5536  CD2 LEU D  37       5.379   0.079  -7.584  1.00 62.14           C  
ANISOU 5536  CD2 LEU D  37     7636   4386  11586   1483    917    219       C  
ATOM   5537  N   MET D  38       7.959   3.429  -9.931  1.00 70.22           N  
ANISOU 5537  N   MET D  38     7723   6522  12434   1335   1826    396       N  
ATOM   5538  CA  MET D  38       8.437   4.576 -10.707  1.00 69.60           C  
ANISOU 5538  CA  MET D  38     7483   6774  12188   1138   2092    529       C  
ATOM   5539  C   MET D  38       9.292   5.405  -9.830  1.00 68.90           C  
ANISOU 5539  C   MET D  38     7004   6734  12438    976   1863    849       C  
ATOM   5540  O   MET D  38       8.969   5.615  -8.652  1.00 63.89           O  
ANISOU 5540  O   MET D  38     6456   5923  11895    876   1413    979       O  
ATOM   5541  CB  MET D  38       7.286   5.447 -11.164  1.00 66.77           C  
ANISOU 5541  CB  MET D  38     7553   6487  11329    871   2013    561       C  
ATOM   5542  CG  MET D  38       6.340   4.770 -12.104  1.00 67.81           C  
ANISOU 5542  CG  MET D  38     8089   6608  11066    954   2163    260       C  
ATOM   5543  SD  MET D  38       4.901   5.797 -12.490  1.00 66.53           S  
ANISOU 5543  SD  MET D  38     8364   6508  10403    674   1932    345       S  
ATOM   5544  CE  MET D  38       5.465   6.283 -14.097  1.00 70.04           C  
ANISOU 5544  CE  MET D  38     8846   7307  10458    595   2397    367       C  
ATOM   5545  N   SER D  39      10.375   5.909 -10.427  1.00 73.49           N  
ANISOU 5545  N   SER D  39     7164   7584  13173    914   2183    971       N  
ATOM   5546  CA  SER D  39      11.173   6.969  -9.796  1.00 75.08           C  
ANISOU 5546  CA  SER D  39     6998   7866  13660    634   1964   1302       C  
ATOM   5547  C   SER D  39      10.378   8.264  -9.712  1.00 73.79           C  
ANISOU 5547  C   SER D  39     7218   7656  13162    261   1728   1463       C  
ATOM   5548  O   SER D  39       9.305   8.405 -10.309  1.00 69.35           O  
ANISOU 5548  O   SER D  39     7122   7070  12158    233   1792   1354       O  
ATOM   5549  CB  SER D  39      12.465   7.209 -10.557  1.00 80.53           C  
ANISOU 5549  CB  SER D  39     7111   8886  14598    600   2416   1414       C  
ATOM   5550  OG  SER D  39      12.231   7.188 -11.940  1.00 82.13           O  
ANISOU 5550  OG  SER D  39     7506   9325  14373    609   2960   1278       O  
ATOM   5551  N   GLU D  40      10.920   9.195  -8.937  1.00 76.33           N  
ANISOU 5551  N   GLU D  40     7330   7934  13736     -8   1406   1711       N  
ATOM   5552  CA  GLU D  40      10.327  10.496  -8.800  1.00 75.04           C  
ANISOU 5552  CA  GLU D  40     7494   7655  13360   -339   1159   1853       C  
ATOM   5553  C   GLU D  40      10.213  11.130 -10.180  1.00 75.36           C  
ANISOU 5553  C   GLU D  40     7662   7873  13096   -509   1552   1964       C  
ATOM   5554  O   GLU D  40       9.141  11.581 -10.577  1.00 71.10           O  
ANISOU 5554  O   GLU D  40     7599   7238  12175   -558   1488   1933       O  
ATOM   5555  CB  GLU D  40      11.158  11.353  -7.859  1.00 80.69           C  
ANISOU 5555  CB  GLU D  40     7924   8289  14446   -627    776   2073       C  
ATOM   5556  CG  GLU D  40      10.507  12.693  -7.525  1.00 82.51           C  
ANISOU 5556  CG  GLU D  40     8556   8284  14509   -931    441   2155       C  
ATOM   5557  CD  GLU D  40      10.902  13.207  -6.154  1.00 86.96           C  
ANISOU 5557  CD  GLU D  40     9054   8656  15329  -1113   -102   2191       C  
ATOM   5558  OE1 GLU D  40      10.958  12.403  -5.179  1.00 90.77           O  
ANISOU 5558  OE1 GLU D  40     9479   9117  15890   -923   -345   2075       O  
ATOM   5559  OE2 GLU D  40      11.146  14.424  -6.044  1.00 91.07           O  
ANISOU 5559  OE2 GLU D  40     9625   9024  15951  -1466   -317   2341       O  
ATOM   5560  N   SER D  41      11.319  11.150 -10.914  1.00 79.99           N  
ANISOU 5560  N   SER D  41     7804   8742  13844   -598   1961   2110       N  
ATOM   5561  CA  SER D  41      11.296  11.624 -12.307  1.00 83.72           C  
ANISOU 5561  CA  SER D  41     8408   9457  13942   -773   2414   2243       C  
ATOM   5562  C   SER D  41      10.155  10.961 -13.099  1.00 81.18           C  
ANISOU 5562  C   SER D  41     8604   9161  13079   -527   2581   1968       C  
ATOM   5563  O   SER D  41       9.339  11.656 -13.723  1.00 79.67           O  
ANISOU 5563  O   SER D  41     8860   8937  12474   -692   2523   2077       O  
ATOM   5564  CB  SER D  41      12.660  11.436 -12.994  1.00 90.01           C  
ANISOU 5564  CB  SER D  41     8592  10647  14959   -832   2964   2366       C  
ATOM   5565  OG  SER D  41      13.320  10.290 -12.513  1.00 91.77           O  
ANISOU 5565  OG  SER D  41     8355  10925  15585   -459   3047   2138       O  
ATOM   5566  N   GLU D  42      10.073   9.631 -13.008  1.00 79.93           N  
ANISOU 5566  N   GLU D  42     8393   9010  12965   -140   2708   1623       N  
ATOM   5567  CA  GLU D  42       9.109   8.858 -13.796  1.00 77.45           C  
ANISOU 5567  CA  GLU D  42     8524   8720  12181     71   2868   1317       C  
ATOM   5568  C   GLU D  42       7.663   9.284 -13.571  1.00 72.03           C  
ANISOU 5568  C   GLU D  42     8368   7803  11194     -5   2439   1304       C  
ATOM   5569  O   GLU D  42       6.959   9.566 -14.536  1.00 72.75           O  
ANISOU 5569  O   GLU D  42     8831   7996  10811    -87   2518   1307       O  
ATOM   5570  CB  GLU D  42       9.306   7.373 -13.584  1.00 78.62           C  
ANISOU 5570  CB  GLU D  42     8531   8802  12537    477   2998    954       C  
ATOM   5571  CG  GLU D  42      10.392   6.796 -14.465  1.00 85.53           C  
ANISOU 5571  CG  GLU D  42     9041   9985  13471    655   3611    817       C  
ATOM   5572  CD  GLU D  42      10.687   5.371 -14.169  1.00 87.58           C  
ANISOU 5572  CD  GLU D  42     9131  10084  14061   1105   3692    463       C  
ATOM   5573  OE1 GLU D  42       9.761   4.567 -14.280  1.00 88.38           O  
ANISOU 5573  OE1 GLU D  42     9670   9969  13937   1273   3576    163       O  
ATOM   5574  OE2 GLU D  42      11.839   5.039 -13.817  1.00 93.53           O  
ANISOU 5574  OE2 GLU D  42     9298  10897  15340   1290   3839    493       O  
ATOM   5575  N   TRP D  43       7.242   9.439 -12.320  1.00 67.78           N  
ANISOU 5575  N   TRP D  43     7850   6989  10914      2   1982   1317       N  
ATOM   5576  CA  TRP D  43       5.873   9.903 -12.054  1.00 64.12           C  
ANISOU 5576  CA  TRP D  43     7803   6338  10218    -42   1619   1288       C  
ATOM   5577  C   TRP D  43       5.644  11.433 -12.259  1.00 63.63           C  
ANISOU 5577  C   TRP D  43     7908   6208  10057   -319   1433   1587       C  
ATOM   5578  O   TRP D  43       4.578  11.847 -12.724  1.00 61.78           O  
ANISOU 5578  O   TRP D  43     8025   5922   9525   -331   1282   1590       O  
ATOM   5579  CB  TRP D  43       5.326   9.440 -10.696  1.00 61.54           C  
ANISOU 5579  CB  TRP D  43     7499   5779  10103     82   1266   1146       C  
ATOM   5580  CG  TRP D  43       6.124   9.708  -9.407  1.00 64.84           C  
ANISOU 5580  CG  TRP D  43     7637   6079  10919     20   1025   1267       C  
ATOM   5581  CD1 TRP D  43       6.861   8.794  -8.724  1.00 69.14           C  
ANISOU 5581  CD1 TRP D  43     7903   6601  11765    166   1009   1221       C  
ATOM   5582  CD2 TRP D  43       6.180  10.911  -8.618  1.00 66.23           C  
ANISOU 5582  CD2 TRP D  43     7838   6113  11213   -190    701   1426       C  
ATOM   5583  NE1 TRP D  43       7.395   9.344  -7.582  1.00 69.35           N  
ANISOU 5583  NE1 TRP D  43     7768   6530  12049     35    680   1365       N  
ATOM   5584  CE2 TRP D  43       6.983  10.638  -7.488  1.00 67.68           C  
ANISOU 5584  CE2 TRP D  43     7757   6239  11719   -191    497   1460       C  
ATOM   5585  CE3 TRP D  43       5.631  12.190  -8.753  1.00 66.11           C  
ANISOU 5585  CE3 TRP D  43     8066   5973  11077   -364    528   1533       C  
ATOM   5586  CZ2 TRP D  43       7.236  11.580  -6.508  1.00 68.09           C  
ANISOU 5586  CZ2 TRP D  43     7809   6146  11915   -390    136   1553       C  
ATOM   5587  CZ3 TRP D  43       5.911  13.142  -7.776  1.00 65.63           C  
ANISOU 5587  CZ3 TRP D  43     7999   5714  11220   -535    195   1611       C  
ATOM   5588  CH2 TRP D  43       6.694  12.833  -6.674  1.00 67.10           C  
ANISOU 5588  CH2 TRP D  43     7949   5878  11666   -562      6   1600       C  
ATOM   5589  N   ARG D  44       6.618  12.266 -11.955  1.00 64.01           N  
ANISOU 5589  N   ARG D  44     7708   6230  10382   -546   1408   1847       N  
ATOM   5590  CA  ARG D  44       6.476  13.682 -12.317  1.00 65.57           C  
ANISOU 5590  CA  ARG D  44     8104   6305  10502   -834   1253   2156       C  
ATOM   5591  C   ARG D  44       6.154  13.820 -13.787  1.00 68.65           C  
ANISOU 5591  C   ARG D  44     8754   6902  10425   -904   1518   2288       C  
ATOM   5592  O   ARG D  44       5.265  14.594 -14.118  1.00 68.72           O  
ANISOU 5592  O   ARG D  44     9128   6752  10228   -962   1263   2416       O  
ATOM   5593  CB  ARG D  44       7.724  14.512 -11.996  1.00 67.86           C  
ANISOU 5593  CB  ARG D  44     8062   6559  11163  -1156   1241   2454       C  
ATOM   5594  CG  ARG D  44       7.829  14.796 -10.522  1.00 65.60           C  
ANISOU 5594  CG  ARG D  44     7682   5991  11251  -1168    806   2365       C  
ATOM   5595  CD  ARG D  44       8.920  15.756 -10.153  1.00 69.18           C  
ANISOU 5595  CD  ARG D  44     7866   6339  12079  -1545    662   2644       C  
ATOM   5596  NE  ARG D  44       9.046  15.844  -8.696  1.00 68.43           N  
ANISOU 5596  NE  ARG D  44     7707   6019  12274  -1535    223   2488       N  
ATOM   5597  CZ  ARG D  44       8.189  16.455  -7.861  1.00 65.67           C  
ANISOU 5597  CZ  ARG D  44     7738   5336  11877  -1495   -186   2325       C  
ATOM   5598  NH1 ARG D  44       7.109  17.076  -8.304  1.00 63.58           N  
ANISOU 5598  NH1 ARG D  44     7899   4880  11377  -1430   -254   2307       N  
ATOM   5599  NH2 ARG D  44       8.439  16.436  -6.541  1.00 66.42           N  
ANISOU 5599  NH2 ARG D  44     7773   5303  12159  -1506   -541   2169       N  
ATOM   5600  N   ASN D  45       6.844  13.061 -14.642  1.00 72.28           N  
ANISOU 5600  N   ASN D  45     9042   7713  10708   -871   2010   2240       N  
ATOM   5601  CA  ASN D  45       6.583  13.048 -16.087  1.00 77.08           C  
ANISOU 5601  CA  ASN D  45     9944   8593  10748   -939   2309   2319       C  
ATOM   5602  C   ASN D  45       5.172  12.771 -16.493  1.00 74.14           C  
ANISOU 5602  C   ASN D  45    10035   8158   9976   -774   2059   2132       C  
ATOM   5603  O   ASN D  45       4.740  13.236 -17.535  1.00 78.31           O  
ANISOU 5603  O   ASN D  45    10909   8806  10040   -909   2066   2322       O  
ATOM   5604  CB  ASN D  45       7.468  12.060 -16.807  1.00 82.27           C  
ANISOU 5604  CB  ASN D  45    10351   9643  11265   -835   2912   2140       C  
ATOM   5605  CG  ASN D  45       8.860  12.586 -17.002  1.00 90.56           C  
ANISOU 5605  CG  ASN D  45    10956  10915  12535  -1106   3288   2455       C  
ATOM   5606  OD1 ASN D  45       9.385  13.364 -16.183  1.00 93.52           O  
ANISOU 5606  OD1 ASN D  45    11058  11093  13380  -1319   3044   2710       O  
ATOM   5607  ND2 ASN D  45       9.474  12.209 -18.110  1.00 97.19           N  
ANISOU 5607  ND2 ASN D  45    11717  12186  13023  -1134   3894   2438       N  
ATOM   5608  N   LEU D  46       4.453  12.028 -15.682  1.00 69.71           N  
ANISOU 5608  N   LEU D  46     9473   7424   9588   -514   1817   1796       N  
ATOM   5609  CA  LEU D  46       3.018  11.822 -15.920  1.00 68.65           C  
ANISOU 5609  CA  LEU D  46     9694   7214   9174   -387   1511   1630       C  
ATOM   5610  C   LEU D  46       2.160  12.993 -15.515  1.00 66.80           C  
ANISOU 5610  C   LEU D  46     9630   6706   9044   -445   1040   1839       C  
ATOM   5611  O   LEU D  46       0.954  13.038 -15.823  1.00 67.44           O  
ANISOU 5611  O   LEU D  46     9956   6746   8920   -352    755   1774       O  
ATOM   5612  CB  LEU D  46       2.500  10.582 -15.188  1.00 65.27           C  
ANISOU 5612  CB  LEU D  46     9184   6701   8912   -135   1439   1223       C  
ATOM   5613  CG  LEU D  46       3.099   9.256 -15.651  1.00 67.97           C  
ANISOU 5613  CG  LEU D  46     9442   7219   9163      5   1838    927       C  
ATOM   5614  CD1 LEU D  46       2.558   8.197 -14.741  1.00 65.72           C  
ANISOU 5614  CD1 LEU D  46     9100   6734   9134    198   1666    625       C  
ATOM   5615  CD2 LEU D  46       2.801   8.898 -17.101  1.00 71.17           C  
ANISOU 5615  CD2 LEU D  46    10176   7881   8984    -18   2044    804       C  
ATOM   5616  N   GLY D  47       2.773  13.940 -14.825  1.00 65.69           N  
ANISOU 5616  N   GLY D  47     9344   6360   9255   -586    935   2069       N  
ATOM   5617  CA  GLY D  47       2.102  15.144 -14.427  1.00 64.43           C  
ANISOU 5617  CA  GLY D  47     9359   5871   9251   -620    509   2243       C  
ATOM   5618  C   GLY D  47       1.618  15.063 -13.012  1.00 59.24           C  
ANISOU 5618  C   GLY D  47     8579   4980   8946   -436    254   1973       C  
ATOM   5619  O   GLY D  47       0.665  15.741 -12.651  1.00 62.93           O  
ANISOU 5619  O   GLY D  47     9197   5211   9501   -323    -80   1944       O  
ATOM   5620  N   VAL D  48       2.322  14.361 -12.179  1.00 55.61           N  
ANISOU 5620  N   VAL D  48     7850   4574   8704   -409    399   1806       N  
ATOM   5621  CA  VAL D  48       1.930  14.304 -10.803  1.00 52.56           C  
ANISOU 5621  CA  VAL D  48     7395   4006   8569   -280    172   1583       C  
ATOM   5622  C   VAL D  48       2.685  15.384 -10.066  1.00 54.45           C  
ANISOU 5622  C   VAL D  48     7581   3995   9110   -465    -10   1735       C  
ATOM   5623  O   VAL D  48       3.883  15.508 -10.239  1.00 55.86           O  
ANISOU 5623  O   VAL D  48     7566   4237   9420   -679    134   1930       O  
ATOM   5624  CB  VAL D  48       2.233  12.899 -10.191  1.00 49.94           C  
ANISOU 5624  CB  VAL D  48     6849   3829   8295   -158    343   1346       C  
ATOM   5625  CG1 VAL D  48       2.068  12.882  -8.683  1.00 47.49           C  
ANISOU 5625  CG1 VAL D  48     6482   3371   8190    -99    125   1191       C  
ATOM   5626  CG2 VAL D  48       1.289  11.889 -10.809  1.00 48.49           C  
ANISOU 5626  CG2 VAL D  48     6777   3796   7850     -2    438   1151       C  
ATOM   5627  N   GLN D  49       1.974  16.102  -9.193  1.00 54.54           N  
ANISOU 5627  N   GLN D  49     7741   3735   9247   -376   -321   1601       N  
ATOM   5628  CA  GLN D  49       2.493  17.248  -8.485  1.00 56.04           C  
ANISOU 5628  CA  GLN D  49     7984   3601   9705   -544   -574   1674       C  
ATOM   5629  C   GLN D  49       2.334  17.013  -7.020  1.00 53.85           C  
ANISOU 5629  C   GLN D  49     7676   3262   9520   -435   -724   1360       C  
ATOM   5630  O   GLN D  49       1.210  16.984  -6.514  1.00 53.17           O  
ANISOU 5630  O   GLN D  49     7719   3136   9346   -195   -806   1101       O  
ATOM   5631  CB  GLN D  49       1.737  18.528  -8.893  1.00 59.21           C  
ANISOU 5631  CB  GLN D  49     8693   3656  10149   -512   -836   1783       C  
ATOM   5632  CG  GLN D  49       1.410  18.613 -10.379  1.00 61.71           C  
ANISOU 5632  CG  GLN D  49     9136   4080  10230   -537   -740   2075       C  
ATOM   5633  CD  GLN D  49       1.422  20.053 -10.910  1.00 67.39           C  
ANISOU 5633  CD  GLN D  49    10129   4396  11078   -698  -1006   2414       C  
ATOM   5634  OE1 GLN D  49       0.391  20.616 -11.246  1.00 67.37           O  
ANISOU 5634  OE1 GLN D  49    10354   4184  11057   -495  -1251   2436       O  
ATOM   5635  NE2 GLN D  49       2.620  20.642 -10.994  1.00 71.32           N  
ANISOU 5635  NE2 GLN D  49    10580   4771  11748  -1080   -978   2708       N  
ATOM   5636  N   GLN D  50       3.453  17.056  -6.335  1.00 54.86           N  
ANISOU 5636  N   GLN D  50     7646   3365   9834   -640   -797   1407       N  
ATOM   5637  CA  GLN D  50       3.571  16.704  -4.962  1.00 55.79           C  
ANISOU 5637  CA  GLN D  50     7734   3490   9973   -602   -949   1169       C  
ATOM   5638  C   GLN D  50       4.955  17.172  -4.441  1.00 58.11           C  
ANISOU 5638  C   GLN D  50     7864   3679  10535   -920  -1153   1312       C  
ATOM   5639  O   GLN D  50       5.886  17.300  -5.222  1.00 59.08           O  
ANISOU 5639  O   GLN D  50     7756   3862  10830  -1139  -1038   1607       O  
ATOM   5640  CB  GLN D  50       3.629  15.192  -5.000  1.00 59.15           C  
ANISOU 5640  CB  GLN D  50     7946   4250  10275   -468   -701   1138       C  
ATOM   5641  CG  GLN D  50       2.824  14.413  -3.992  1.00 59.57           C  
ANISOU 5641  CG  GLN D  50     8086   4402  10146   -281   -723    878       C  
ATOM   5642  CD  GLN D  50       2.885  12.980  -4.278  1.00 60.41           C  
ANISOU 5642  CD  GLN D  50     8024   4740  10189   -179   -497    907       C  
ATOM   5643  OE1 GLN D  50       3.500  12.499  -5.277  1.00 60.72           O  
ANISOU 5643  OE1 GLN D  50     7879   4885  10303   -193   -288   1059       O  
ATOM   5644  NE2 GLN D  50       2.272  12.246  -3.415  1.00 63.61           N  
ANISOU 5644  NE2 GLN D  50     8499   5220  10447    -82   -515    756       N  
ATOM   5645  N   SER D  51       5.141  17.279  -3.138  1.00 58.47           N  
ANISOU 5645  N   SER D  51     7981   3642  10592   -964  -1432   1114       N  
ATOM   5646  CA  SER D  51       6.478  17.503  -2.607  1.00 62.89           C  
ANISOU 5646  CA  SER D  51     8320   4165  11406  -1275  -1679   1250       C  
ATOM   5647  C   SER D  51       7.463  16.334  -2.810  1.00 65.03           C  
ANISOU 5647  C   SER D  51     8124   4774  11808  -1289  -1508   1456       C  
ATOM   5648  O   SER D  51       7.104  15.240  -3.210  1.00 61.84           O  
ANISOU 5648  O   SER D  51     7627   4601  11267  -1042  -1213   1442       O  
ATOM   5649  CB  SER D  51       6.388  17.862  -1.115  1.00 64.57           C  
ANISOU 5649  CB  SER D  51     8787   4229  11514  -1317  -2070    954       C  
ATOM   5650  OG  SER D  51       5.326  17.163  -0.475  1.00 61.58           O  
ANISOU 5650  OG  SER D  51     8612   4007  10777  -1015  -1957    681       O  
ATOM   5651  N   GLN D  52       8.704  16.563  -2.411  1.00 72.48           N  
ANISOU 5651  N   GLN D  52     8771   5713  13052  -1570  -1751   1613       N  
ATOM   5652  CA  GLN D  52       9.745  15.544  -2.467  1.00 75.85           C  
ANISOU 5652  CA  GLN D  52     8684   6429  13704  -1552  -1657   1796       C  
ATOM   5653  C   GLN D  52       9.537  14.341  -1.581  1.00 73.25           C  
ANISOU 5653  C   GLN D  52     8367   6246  13216  -1291  -1748   1667       C  
ATOM   5654  O   GLN D  52       8.791  14.381  -0.610  1.00 71.19           O  
ANISOU 5654  O   GLN D  52     8493   5899  12656  -1225  -1968   1447       O  
ATOM   5655  CB  GLN D  52      11.090  16.140  -2.111  1.00 84.05           C  
ANISOU 5655  CB  GLN D  52     9352   7431  15152  -1933  -1984   1995       C  
ATOM   5656  CG  GLN D  52      12.036  16.258  -3.300  1.00 92.01           C  
ANISOU 5656  CG  GLN D  52     9849   8607  16501  -2119  -1642   2322       C  
ATOM   5657  CD  GLN D  52      13.044  15.103  -3.372  1.00 99.84           C  
ANISOU 5657  CD  GLN D  52    10205   9941  17789  -1968  -1486   2454       C  
ATOM   5658  OE1 GLN D  52      12.737  13.936  -3.007  1.00100.73           O  
ANISOU 5658  OE1 GLN D  52    10335  10163  17773  -1596  -1443   2318       O  
ATOM   5659  NE2 GLN D  52      14.280  15.425  -3.830  1.00106.38           N  
ANISOU 5659  NE2 GLN D  52    10433  10922  19063  -2260  -1407   2736       N  
ATOM   5660  N   GLY D  53      10.206  13.254  -1.956  1.00 73.17           N  
ANISOU 5660  N   GLY D  53     7935   6456  13411  -1135  -1547   1814       N  
ATOM   5661  CA  GLY D  53      10.306  12.058  -1.115  1.00 73.34           C  
ANISOU 5661  CA  GLY D  53     7894   6565  13404   -921  -1708   1795       C  
ATOM   5662  C   GLY D  53       9.075  11.189  -0.918  1.00 69.11           C  
ANISOU 5662  C   GLY D  53     7744   6028  12486   -647  -1548   1619       C  
ATOM   5663  O   GLY D  53       9.104  10.292  -0.120  1.00 68.11           O  
ANISOU 5663  O   GLY D  53     7646   5925  12305   -530  -1729   1647       O  
ATOM   5664  N   TRP D  54       7.989  11.467  -1.650  1.00 67.21           N  
ANISOU 5664  N   TRP D  54     7788   5752  11994   -572  -1237   1472       N  
ATOM   5665  CA  TRP D  54       6.897  10.530  -1.771  1.00 62.85           C  
ANISOU 5665  CA  TRP D  54     7467   5236  11176   -337  -1014   1339       C  
ATOM   5666  C   TRP D  54       7.460   9.416  -2.642  1.00 62.91           C  
ANISOU 5666  C   TRP D  54     7155   5330  11416   -145   -728   1430       C  
ATOM   5667  O   TRP D  54       8.109   9.687  -3.654  1.00 66.18           O  
ANISOU 5667  O   TRP D  54     7298   5820  12025   -169   -490   1510       O  
ATOM   5668  CB  TRP D  54       5.638  11.120  -2.427  1.00 60.79           C  
ANISOU 5668  CB  TRP D  54     7507   4937  10651   -301   -799   1171       C  
ATOM   5669  CG  TRP D  54       4.872  12.061  -1.530  1.00 62.78           C  
ANISOU 5669  CG  TRP D  54     8095   5083  10675   -380  -1021    994       C  
ATOM   5670  CD1 TRP D  54       4.920  13.409  -1.569  1.00 64.85           C  
ANISOU 5670  CD1 TRP D  54     8473   5178  10986   -523  -1167    950       C  
ATOM   5671  CD2 TRP D  54       3.967  11.730  -0.473  1.00 62.62           C  
ANISOU 5671  CD2 TRP D  54     8340   5105  10347   -316  -1095    820       C  
ATOM   5672  NE1 TRP D  54       4.149  13.943  -0.587  1.00 64.87           N  
ANISOU 5672  NE1 TRP D  54     8796   5099  10752   -506  -1333    706       N  
ATOM   5673  CE2 TRP D  54       3.539  12.948   0.101  1.00 62.53           C  
ANISOU 5673  CE2 TRP D  54     8583   4971  10203   -385  -1260    621       C  
ATOM   5674  CE3 TRP D  54       3.485  10.525   0.048  1.00 62.83           C  
ANISOU 5674  CE3 TRP D  54     8423   5249  10197   -224  -1024    824       C  
ATOM   5675  CZ2 TRP D  54       2.679  13.017   1.159  1.00 63.52           C  
ANISOU 5675  CZ2 TRP D  54     8986   5151   9996   -341  -1302    389       C  
ATOM   5676  CZ3 TRP D  54       2.604  10.586   1.120  1.00 64.00           C  
ANISOU 5676  CZ3 TRP D  54     8850   5467   9999   -239  -1073    660       C  
ATOM   5677  CH2 TRP D  54       2.213  11.835   1.667  1.00 64.71           C  
ANISOU 5677  CH2 TRP D  54     9162   5496   9929   -283  -1184    424       C  
ATOM   5678  N   VAL D  55       7.174   8.167  -2.252  1.00 60.58           N  
ANISOU 5678  N   VAL D  55     6922   5012  11083     40   -730   1410       N  
ATOM   5679  CA  VAL D  55       7.644   6.946  -2.970  1.00 58.53           C  
ANISOU 5679  CA  VAL D  55     6419   4749  11068    288   -486   1430       C  
ATOM   5680  C   VAL D  55       6.505   6.122  -3.524  1.00 53.98           C  
ANISOU 5680  C   VAL D  55     6129   4117  10262    426   -234   1254       C  
ATOM   5681  O   VAL D  55       5.581   5.778  -2.776  1.00 51.63           O  
ANISOU 5681  O   VAL D  55     6129   3754   9732    387   -369   1219       O  
ATOM   5682  CB  VAL D  55       8.470   6.019  -2.068  1.00 60.17           C  
ANISOU 5682  CB  VAL D  55     6425   4875  11562    411   -783   1595       C  
ATOM   5683  CG1 VAL D  55       9.263   5.117  -2.958  1.00 62.59           C  
ANISOU 5683  CG1 VAL D  55     6361   5167  12252    694   -508   1586       C  
ATOM   5684  CG2 VAL D  55       9.410   6.800  -1.149  1.00 62.52           C  
ANISOU 5684  CG2 VAL D  55     6511   5223  12019    213  -1207   1773       C  
ATOM   5685  N   HIS D  56       6.551   5.861  -4.832  1.00 53.26           N  
ANISOU 5685  N   HIS D  56     5955   4079  10202    547    133   1140       N  
ATOM   5686  CA  HIS D  56       5.593   4.933  -5.474  1.00 51.68           C  
ANISOU 5686  CA  HIS D  56     6005   3804   9825    671    337    944       C  
ATOM   5687  C   HIS D  56       5.943   3.553  -4.901  1.00 54.04           C  
ANISOU 5687  C   HIS D  56     6259   3890  10382    862    221    977       C  
ATOM   5688  O   HIS D  56       7.079   3.102  -5.069  1.00 56.40           O  
ANISOU 5688  O   HIS D  56     6233   4153  11043   1057    273   1025       O  
ATOM   5689  CB  HIS D  56       5.760   4.934  -6.987  1.00 52.92           C  
ANISOU 5689  CB  HIS D  56     6103   4080   9921    756    729    799       C  
ATOM   5690  CG  HIS D  56       4.740   4.114  -7.708  1.00 52.83           C  
ANISOU 5690  CG  HIS D  56     6389   3999   9683    830    877    561       C  
ATOM   5691  ND1 HIS D  56       3.500   3.842  -7.176  1.00 51.29           N  
ANISOU 5691  ND1 HIS D  56     6475   3705   9307    732    692    512       N  
ATOM   5692  CD2 HIS D  56       4.761   3.504  -8.927  1.00 55.43           C  
ANISOU 5692  CD2 HIS D  56     6779   4355   9924    965   1185    338       C  
ATOM   5693  CE1 HIS D  56       2.786   3.129  -8.041  1.00 50.88           C  
ANISOU 5693  CE1 HIS D  56     6621   3605   9103    773    830    292       C  
ATOM   5694  NE2 HIS D  56       3.523   2.920  -9.118  1.00 53.74           N  
ANISOU 5694  NE2 HIS D  56     6897   4033   9488    919   1115    163       N  
ATOM   5695  N   TYR D  57       5.040   2.979  -4.122  1.00 52.11           N  
ANISOU 5695  N   TYR D  57     6301   3507   9988    793     38    997       N  
ATOM   5696  CA  TYR D  57       5.377   1.884  -3.253  1.00 54.44           C  
ANISOU 5696  CA  TYR D  57     6609   3567  10505    894   -197   1152       C  
ATOM   5697  C   TYR D  57       4.614   0.564  -3.535  1.00 56.22           C  
ANISOU 5697  C   TYR D  57     7093   3521  10745    965   -122   1040       C  
ATOM   5698  O   TYR D  57       5.022  -0.466  -3.047  1.00 59.39           O  
ANISOU 5698  O   TYR D  57     7506   3641  11418   1100   -298   1172       O  
ATOM   5699  CB  TYR D  57       5.219   2.271  -1.783  1.00 54.55           C  
ANISOU 5699  CB  TYR D  57     6752   3628  10345    690   -560   1381       C  
ATOM   5700  CG  TYR D  57       3.792   2.285  -1.258  1.00 53.88           C  
ANISOU 5700  CG  TYR D  57     7028   3589   9853    469   -557   1344       C  
ATOM   5701  CD1 TYR D  57       2.982   3.433  -1.404  1.00 51.58           C  
ANISOU 5701  CD1 TYR D  57     6823   3524   9252    319   -439   1191       C  
ATOM   5702  CD2 TYR D  57       3.237   1.161  -0.597  1.00 55.51           C  
ANISOU 5702  CD2 TYR D  57     7467   3609  10013    405   -669   1482       C  
ATOM   5703  CE1 TYR D  57       1.678   3.471  -0.908  1.00 50.78           C  
ANISOU 5703  CE1 TYR D  57     6956   3512   8825    152   -396   1136       C  
ATOM   5704  CE2 TYR D  57       1.922   1.191  -0.089  1.00 54.36           C  
ANISOU 5704  CE2 TYR D  57     7580   3573   9501    162   -610   1467       C  
ATOM   5705  CZ  TYR D  57       1.147   2.338  -0.245  1.00 51.71           C  
ANISOU 5705  CZ  TYR D  57     7253   3513   8881     56   -455   1274       C  
ATOM   5706  OH  TYR D  57      -0.135   2.394   0.222  1.00 50.10           O  
ANISOU 5706  OH  TYR D  57     7206   3458   8369   -138   -353   1231       O  
ATOM   5707  N   MET D  58       3.528   0.602  -4.297  1.00 54.32           N  
ANISOU 5707  N   MET D  58     7058   3335  10243    861     82    819       N  
ATOM   5708  CA  MET D  58       2.816  -0.586  -4.704  1.00 54.91           C  
ANISOU 5708  CA  MET D  58     7368   3144  10351    875    137    674       C  
ATOM   5709  C   MET D  58       1.848  -0.309  -5.843  1.00 54.47           C  
ANISOU 5709  C   MET D  58     7447   3231  10018    778    354    390       C  
ATOM   5710  O   MET D  58       1.534   0.854  -6.133  1.00 57.53           O  
ANISOU 5710  O   MET D  58     7780   3921  10156    677    425    366       O  
ATOM   5711  CB  MET D  58       2.020  -1.167  -3.545  1.00 54.70           C  
ANISOU 5711  CB  MET D  58     7570   2971  10241    650   -100    892       C  
ATOM   5712  CG  MET D  58       0.821  -0.363  -3.124  1.00 51.72           C  
ANISOU 5712  CG  MET D  58     7293   2885   9473    355    -85    905       C  
ATOM   5713  SD  MET D  58      -0.289  -1.236  -1.995  1.00 53.78           S  
ANISOU 5713  SD  MET D  58     7808   3027   9599     37   -224   1129       S  
ATOM   5714  CE  MET D  58      -1.572  -1.792  -3.144  1.00 53.05           C  
ANISOU 5714  CE  MET D  58     7812   2865   9477   -105    -57    838       C  
ATOM   5715  N   ILE D  59       1.345  -1.376  -6.445  1.00 55.52           N  
ANISOU 5715  N   ILE D  59     7779   3112  10201    793    402    188       N  
ATOM   5716  CA  ILE D  59       0.391  -1.319  -7.537  1.00 53.83           C  
ANISOU 5716  CA  ILE D  59     7727   3000   9724    679    523    -91       C  
ATOM   5717  C   ILE D  59      -0.786  -2.191  -7.172  1.00 55.53           C  
ANISOU 5717  C   ILE D  59     8160   3002   9937    427    358    -92       C  
ATOM   5718  O   ILE D  59      -0.589  -3.354  -6.769  1.00 61.25           O  
ANISOU 5718  O   ILE D  59     9012   3322  10936    456    249    -42       O  
ATOM   5719  CB  ILE D  59       1.007  -1.861  -8.840  1.00 55.82           C  
ANISOU 5719  CB  ILE D  59     8036   3145  10026    924    754   -427       C  
ATOM   5720  CG1 ILE D  59       2.140  -0.944  -9.272  1.00 55.27           C  
ANISOU 5720  CG1 ILE D  59     7699   3360   9941   1115    983   -395       C  
ATOM   5721  CG2 ILE D  59      -0.043  -2.001  -9.940  1.00 56.23           C  
ANISOU 5721  CG2 ILE D  59     8339   3262   9764    769    790   -730       C  
ATOM   5722  CD1 ILE D  59       2.856  -1.362 -10.537  1.00 59.20           C  
ANISOU 5722  CD1 ILE D  59     8205   3858  10429   1369   1316   -726       C  
ATOM   5723  N   HIS D  60      -1.990  -1.651  -7.293  1.00 52.91           N  
ANISOU 5723  N   HIS D  60     7845   2916   9342    176    322   -121       N  
ATOM   5724  CA  HIS D  60      -3.128  -2.460  -7.316  1.00 53.75           C  
ANISOU 5724  CA  HIS D  60     8098   2872   9452    -89    208   -187       C  
ATOM   5725  C   HIS D  60      -3.366  -2.850  -8.786  1.00 56.30           C  
ANISOU 5725  C   HIS D  60     8588   3125   9678    -54    249   -572       C  
ATOM   5726  O   HIS D  60      -3.924  -2.109  -9.535  1.00 54.04           O  
ANISOU 5726  O   HIS D  60     8267   3140   9124   -110    259   -695       O  
ATOM   5727  CB  HIS D  60      -4.291  -1.741  -6.677  1.00 51.89           C  
ANISOU 5727  CB  HIS D  60     7722   2961   9033   -354    155    -39       C  
ATOM   5728  CG  HIS D  60      -5.443  -2.638  -6.310  1.00 55.19           C  
ANISOU 5728  CG  HIS D  60     8199   3248   9523   -708     46     10       C  
ATOM   5729  ND1 HIS D  60      -5.302  -3.770  -5.510  1.00 58.59           N  
ANISOU 5729  ND1 HIS D  60     8781   3308  10170   -851    -38    213       N  
ATOM   5730  CD2 HIS D  60      -6.762  -2.564  -6.614  1.00 56.14           C  
ANISOU 5730  CD2 HIS D  60     8215   3557   9557   -978    -10    -75       C  
ATOM   5731  CE1 HIS D  60      -6.475  -4.364  -5.370  1.00 61.16           C  
ANISOU 5731  CE1 HIS D  60     9114   3596  10528  -1233   -111    251       C  
ATOM   5732  NE2 HIS D  60      -7.380  -3.659  -6.034  1.00 60.38           N  
ANISOU 5732  NE2 HIS D  60     8826   3852  10262  -1315    -94     62       N  
ATOM   5733  N   GLU D  61      -3.091  -4.107  -9.147  1.00 62.23           N  
ANISOU 5733  N   GLU D  61     9566   3435  10640      1    219   -767       N  
ATOM   5734  CA  GLU D  61      -3.177  -4.508 -10.562  1.00 66.11           C  
ANISOU 5734  CA  GLU D  61    10283   3852  10982     64    273  -1206       C  
ATOM   5735  C   GLU D  61      -4.507  -4.194 -11.265  1.00 63.51           C  
ANISOU 5735  C   GLU D  61    10007   3775  10349   -247    116  -1352       C  
ATOM   5736  O   GLU D  61      -4.484  -3.826 -12.444  1.00 64.15           O  
ANISOU 5736  O   GLU D  61    10202   4059  10111   -170    178  -1620       O  
ATOM   5737  CB  GLU D  61      -2.781  -5.982 -10.840  1.00 73.82           C  
ANISOU 5737  CB  GLU D  61    11553   4232  12260    178    239  -1474       C  
ATOM   5738  CG  GLU D  61      -1.417  -6.387 -10.304  1.00 78.52           C  
ANISOU 5738  CG  GLU D  61    12069   4540  13225    566    358  -1369       C  
ATOM   5739  CD  GLU D  61      -1.562  -7.120  -8.972  1.00 84.43           C  
ANISOU 5739  CD  GLU D  61    12842   4898  14339    415    110   -987       C  
ATOM   5740  OE1 GLU D  61      -1.610  -8.407  -9.020  1.00 88.96           O  
ANISOU 5740  OE1 GLU D  61    13700   4867  15232    412    -35  -1120       O  
ATOM   5741  OE2 GLU D  61      -1.736  -6.400  -7.905  1.00 83.19           O  
ANISOU 5741  OE2 GLU D  61    12469   5033  14106    257     47   -562       O  
ATOM   5742  N   PRO D  62      -5.651  -4.414 -10.597  1.00 60.78           N  
ANISOU 5742  N   PRO D  62     9577   3419  10097   -608    -91  -1179       N  
ATOM   5743  CA  PRO D  62      -6.884  -4.145 -11.323  1.00 61.14           C  
ANISOU 5743  CA  PRO D  62     9596   3713   9919   -880   -281  -1327       C  
ATOM   5744  C   PRO D  62      -7.223  -2.647 -11.455  1.00 57.64           C  
ANISOU 5744  C   PRO D  62     8884   3808   9205   -812   -256  -1186       C  
ATOM   5745  O   PRO D  62      -8.182  -2.319 -12.102  1.00 58.78           O  
ANISOU 5745  O   PRO D  62     8973   4180   9179   -976   -450  -1281       O  
ATOM   5746  CB  PRO D  62      -7.940  -4.860 -10.484  1.00 62.81           C  
ANISOU 5746  CB  PRO D  62     9713   3766  10385  -1294   -466  -1151       C  
ATOM   5747  CG  PRO D  62      -7.364  -5.017  -9.121  1.00 60.99           C  
ANISOU 5747  CG  PRO D  62     9405   3389  10379  -1239   -339   -792       C  
ATOM   5748  CD  PRO D  62      -5.894  -4.833  -9.207  1.00 59.64           C  
ANISOU 5748  CD  PRO D  62     9329   3109  10222   -799   -156   -824       C  
ATOM   5749  N   GLU D  63      -6.467  -1.766 -10.804  1.00 53.64           N  
ANISOU 5749  N   GLU D  63     8214   3463   8701   -584    -69   -952       N  
ATOM   5750  CA  GLU D  63      -6.665  -0.326 -10.905  1.00 50.94           C  
ANISOU 5750  CA  GLU D  63     7672   3523   8158   -489    -57   -823       C  
ATOM   5751  C   GLU D  63      -5.317   0.366 -11.156  1.00 49.02           C  
ANISOU 5751  C   GLU D  63     7470   3336   7820   -190    160   -776       C  
ATOM   5752  O   GLU D  63      -4.743   1.001 -10.258  1.00 45.49           O  
ANISOU 5752  O   GLU D  63     6864   2939   7479    -85    253   -551       O  
ATOM   5753  CB  GLU D  63      -7.292   0.186  -9.603  1.00 48.48           C  
ANISOU 5753  CB  GLU D  63     7071   3365   7983   -592    -68   -563       C  
ATOM   5754  CG  GLU D  63      -8.738  -0.163  -9.493  1.00 50.19           C  
ANISOU 5754  CG  GLU D  63     7119   3679   8269   -896   -241   -584       C  
ATOM   5755  CD  GLU D  63      -9.326   0.302  -8.189  1.00 49.28           C  
ANISOU 5755  CD  GLU D  63     6707   3764   8253   -980   -154   -363       C  
ATOM   5756  OE1 GLU D  63      -8.578   0.523  -7.247  1.00 48.01           O  
ANISOU 5756  OE1 GLU D  63     6571   3562   8106   -866      0   -202       O  
ATOM   5757  OE2 GLU D  63     -10.552   0.470  -8.082  1.00 50.91           O  
ANISOU 5757  OE2 GLU D  63     6632   4201   8511  -1157   -237   -362       O  
ATOM   5758  N   PRO D  64      -4.774   0.123 -12.337  1.00 51.69           N  
ANISOU 5758  N   PRO D  64     8026   3651   7961    -81    252  -1004       N  
ATOM   5759  CA  PRO D  64      -3.401   0.464 -12.604  1.00 53.06           C  
ANISOU 5759  CA  PRO D  64     8206   3853   8102    169    527   -982       C  
ATOM   5760  C   PRO D  64      -3.175   1.974 -12.758  1.00 52.80           C  
ANISOU 5760  C   PRO D  64     8040   4135   7886    218    569   -753       C  
ATOM   5761  O   PRO D  64      -2.032   2.449 -12.703  1.00 53.50           O  
ANISOU 5761  O   PRO D  64     8032   4271   8021    365    783   -637       O  
ATOM   5762  CB  PRO D  64      -3.112  -0.285 -13.920  1.00 56.22           C  
ANISOU 5762  CB  PRO D  64     8905   4187   8268    236    645  -1351       C  
ATOM   5763  CG  PRO D  64      -4.421  -0.364 -14.599  1.00 56.96           C  
ANISOU 5763  CG  PRO D  64     9158   4377   8105     -5    353  -1497       C  
ATOM   5764  CD  PRO D  64      -5.394  -0.553 -13.488  1.00 55.29           C  
ANISOU 5764  CD  PRO D  64     8742   4066   8198   -208    116  -1322       C  
ATOM   5765  N   HIS D  65      -4.270   2.696 -12.965  1.00 53.41           N  
ANISOU 5765  N   HIS D  65     8094   4398   7801     90    339   -685       N  
ATOM   5766  CA  HIS D  65      -4.259   4.180 -12.982  1.00 52.39           C  
ANISOU 5766  CA  HIS D  65     7859   4474   7572    132    294   -441       C  
ATOM   5767  C   HIS D  65      -4.156   4.852 -11.618  1.00 48.79           C  
ANISOU 5767  C   HIS D  65     7168   3978   7389    170    277   -232       C  
ATOM   5768  O   HIS D  65      -4.249   6.023 -11.556  1.00 48.37           O  
ANISOU 5768  O   HIS D  65     7055   4015   7306    205    202    -75       O  
ATOM   5769  CB  HIS D  65      -5.524   4.679 -13.675  1.00 53.72           C  
ANISOU 5769  CB  HIS D  65     8070   4811   7530     36     -3   -448       C  
ATOM   5770  CG  HIS D  65      -6.772   4.321 -12.963  1.00 54.73           C  
ANISOU 5770  CG  HIS D  65     8004   4922   7867    -79   -218   -492       C  
ATOM   5771  ND1 HIS D  65      -7.429   3.122 -13.172  1.00 58.01           N  
ANISOU 5771  ND1 HIS D  65     8480   5254   8308   -253   -327   -705       N  
ATOM   5772  CD2 HIS D  65      -7.479   4.978 -12.021  1.00 54.09           C  
ANISOU 5772  CD2 HIS D  65     7654   4904   7993    -62   -313   -364       C  
ATOM   5773  CE1 HIS D  65      -8.512   3.074 -12.414  1.00 58.31           C  
ANISOU 5773  CE1 HIS D  65     8249   5340   8563   -375   -476   -658       C  
ATOM   5774  NE2 HIS D  65      -8.575   4.191 -11.713  1.00 56.27           N  
ANISOU 5774  NE2 HIS D  65     7780   5196   8402   -238   -444   -471       N  
ATOM   5775  N   ILE D  66      -4.091   4.098 -10.525  1.00 47.82           N  
ANISOU 5775  N   ILE D  66     6954   3704   7508    143    308   -236       N  
ATOM   5776  CA  ILE D  66      -4.140   4.669  -9.200  1.00 44.41           C  
ANISOU 5776  CA  ILE D  66     6358   3276   7236    146    274    -77       C  
ATOM   5777  C   ILE D  66      -2.758   4.530  -8.616  1.00 45.82           C  
ANISOU 5777  C   ILE D  66     6508   3334   7566    233    399     29       C  
ATOM   5778  O   ILE D  66      -2.324   3.438  -8.282  1.00 48.09           O  
ANISOU 5778  O   ILE D  66     6823   3450   7998    243    446      4       O  
ATOM   5779  CB  ILE D  66      -5.162   3.989  -8.301  1.00 42.99           C  
ANISOU 5779  CB  ILE D  66     6098   3081   7155      2    202   -100       C  
ATOM   5780  CG1 ILE D  66      -6.565   4.162  -8.856  1.00 43.17           C  
ANISOU 5780  CG1 ILE D  66     6039   3263   7099    -90     52   -198       C  
ATOM   5781  CG2 ILE D  66      -5.048   4.542  -6.890  1.00 42.17           C  
ANISOU 5781  CG2 ILE D  66     5886   3014   7122     12    222     37       C  
ATOM   5782  CD1 ILE D  66      -7.720   3.872  -7.872  1.00 43.30           C  
ANISOU 5782  CD1 ILE D  66     5848   3375   7226   -248     28   -183       C  
ATOM   5783  N   LEU D  67      -2.055   5.643  -8.485  1.00 46.53           N  
ANISOU 5783  N   LEU D  67     6530   3482   7664    291    413    163       N  
ATOM   5784  CA  LEU D  67      -0.690   5.593  -8.038  1.00 47.59           C  
ANISOU 5784  CA  LEU D  67     6569   3538   7975    353    492    277       C  
ATOM   5785  C   LEU D  67      -0.683   5.697  -6.535  1.00 48.16           C  
ANISOU 5785  C   LEU D  67     6585   3558   8154    307    352    381       C  
ATOM   5786  O   LEU D  67      -1.427   6.537  -5.996  1.00 50.43           O  
ANISOU 5786  O   LEU D  67     6889   3921   8348    258    253    379       O  
ATOM   5787  CB  LEU D  67       0.085   6.704  -8.667  1.00 48.81           C  
ANISOU 5787  CB  LEU D  67     6670   3780   8094    363    559    390       C  
ATOM   5788  CG  LEU D  67       0.104   6.709 -10.197  1.00 50.33           C  
ANISOU 5788  CG  LEU D  67     6968   4087   8065    375    724    325       C  
ATOM   5789  CD1 LEU D  67       0.941   7.896 -10.667  1.00 50.56           C  
ANISOU 5789  CD1 LEU D  67     6937   4204   8068    316    801    532       C  
ATOM   5790  CD2 LEU D  67       0.636   5.400 -10.790  1.00 53.35           C  
ANISOU 5790  CD2 LEU D  67     7370   4433   8466    478    943    145       C  
ATOM   5791  N   LEU D  68       0.079   4.818  -5.863  1.00 48.49           N  
ANISOU 5791  N   LEU D  68     6581   3470   8373    339    333    457       N  
ATOM   5792  CA  LEU D  68       0.048   4.742  -4.417  1.00 49.23           C  
ANISOU 5792  CA  LEU D  68     6690   3534   8480    263    172    580       C  
ATOM   5793  C   LEU D  68       1.358   5.177  -3.885  1.00 49.79           C  
ANISOU 5793  C   LEU D  68     6629   3578   8708    301     61    730       C  
ATOM   5794  O   LEU D  68       2.441   4.719  -4.297  1.00 51.19           O  
ANISOU 5794  O   LEU D  68     6649   3678   9121    417    109    785       O  
ATOM   5795  CB  LEU D  68      -0.352   3.361  -3.913  1.00 52.44           C  
ANISOU 5795  CB  LEU D  68     7196   3795   8934    211    140    617       C  
ATOM   5796  CG  LEU D  68      -1.835   3.079  -4.272  1.00 53.06           C  
ANISOU 5796  CG  LEU D  68     7359   3941   8860     84    208    479       C  
ATOM   5797  CD1 LEU D  68      -1.977   1.884  -5.175  1.00 56.79           C  
ANISOU 5797  CD1 LEU D  68     7912   4220   9443     97    264    361       C  
ATOM   5798  CD2 LEU D  68      -2.706   2.900  -3.041  1.00 53.59           C  
ANISOU 5798  CD2 LEU D  68     7476   4091   8792   -101    163    575       C  
ATOM   5799  N   PHE D  69       1.246   6.097  -2.938  1.00 49.33           N  
ANISOU 5799  N   PHE D  69     6616   3595   8532    204    -93    771       N  
ATOM   5800  CA  PHE D  69       2.399   6.846  -2.487  1.00 50.24           C  
ANISOU 5800  CA  PHE D  69     6611   3702   8776    174   -261    887       C  
ATOM   5801  C   PHE D  69       2.475   6.856  -0.988  1.00 53.25           C  
ANISOU 5801  C   PHE D  69     7107   4092   9031     72   -517    968       C  
ATOM   5802  O   PHE D  69       1.449   6.825  -0.294  1.00 56.76           O  
ANISOU 5802  O   PHE D  69     7751   4612   9200      3   -503    891       O  
ATOM   5803  CB  PHE D  69       2.335   8.283  -2.957  1.00 48.58           C  
ANISOU 5803  CB  PHE D  69     6402   3530   8523    121   -253    823       C  
ATOM   5804  CG  PHE D  69       2.612   8.468  -4.420  1.00 45.65           C  
ANISOU 5804  CG  PHE D  69     5922   3181   8239    171    -41    831       C  
ATOM   5805  CD1 PHE D  69       3.896   8.400  -4.894  1.00 46.22           C  
ANISOU 5805  CD1 PHE D  69     5748   3264   8548    178     28    959       C  
ATOM   5806  CD2 PHE D  69       1.565   8.737  -5.288  1.00 43.85           C  
ANISOU 5806  CD2 PHE D  69     5827   2998   7836    202     81    719       C  
ATOM   5807  CE1 PHE D  69       4.164   8.577  -6.227  1.00 46.98           C  
ANISOU 5807  CE1 PHE D  69     5766   3439   8643    197    284    971       C  
ATOM   5808  CE2 PHE D  69       1.799   8.917  -6.632  1.00 44.69           C  
ANISOU 5808  CE2 PHE D  69     5900   3157   7921    218    257    748       C  
ATOM   5809  CZ  PHE D  69       3.112   8.839  -7.102  1.00 46.69           C  
ANISOU 5809  CZ  PHE D  69     5945   3444   8347    206    391    872       C  
ATOM   5810  N   ARG D  70       3.701   6.956  -0.511  1.00 53.99           N  
ANISOU 5810  N   ARG D  70     7055   4146   9310     48   -747   1123       N  
ATOM   5811  CA  ARG D  70       4.004   6.680   0.852  1.00 54.86           C  
ANISOU 5811  CA  ARG D  70     7278   4261   9303    -42  -1055   1258       C  
ATOM   5812  C   ARG D  70       5.268   7.404   1.140  1.00 55.62           C  
ANISOU 5812  C   ARG D  70     7175   4348   9606   -115  -1343   1357       C  
ATOM   5813  O   ARG D  70       6.192   7.389   0.299  1.00 55.32           O  
ANISOU 5813  O   ARG D  70     6797   4279   9943    -36  -1275   1434       O  
ATOM   5814  CB  ARG D  70       4.189   5.168   0.981  1.00 57.82           C  
ANISOU 5814  CB  ARG D  70     7629   4519   9818     58  -1083   1442       C  
ATOM   5815  CG  ARG D  70       5.171   4.688   2.053  1.00 62.16           C  
ANISOU 5815  CG  ARG D  70     8141   5010  10464     36  -1495   1715       C  
ATOM   5816  CD  ARG D  70       6.201   3.720   1.487  1.00 64.54           C  
ANISOU 5816  CD  ARG D  70     8119   5130  11272    272  -1532   1869       C  
ATOM   5817  NE  ARG D  70       5.882   2.377   1.932  1.00 68.34           N  
ANISOU 5817  NE  ARG D  70     8790   5414  11758    333  -1620   2046       N  
ATOM   5818  CZ  ARG D  70       6.724   1.342   1.942  1.00 70.71           C  
ANISOU 5818  CZ  ARG D  70     8915   5475  12473    552  -1805   2247       C  
ATOM   5819  NH1 ARG D  70       7.972   1.471   1.473  1.00 73.09           N  
ANISOU 5819  NH1 ARG D  70     8762   5765  13243    762  -1866   2267       N  
ATOM   5820  NH2 ARG D  70       6.297   0.166   2.403  1.00 71.44           N  
ANISOU 5820  NH2 ARG D  70     9271   5327  12546    562  -1916   2436       N  
ATOM   5821  N   ARG D  71       5.351   7.963   2.339  1.00 56.83           N  
ANISOU 5821  N   ARG D  71     7525   4550   9515   -280  -1662   1355       N  
ATOM   5822  CA  ARG D  71       6.559   8.645   2.771  1.00 61.04           C  
ANISOU 5822  CA  ARG D  71     7884   5067  10240   -414  -2041   1450       C  
ATOM   5823  C   ARG D  71       6.745   8.524   4.276  1.00 65.07           C  
ANISOU 5823  C   ARG D  71     8647   5637  10437   -561  -2479   1534       C  
ATOM   5824  O   ARG D  71       5.781   8.648   5.016  1.00 64.45           O  
ANISOU 5824  O   ARG D  71     8968   5646   9873   -629  -2430   1385       O  
ATOM   5825  CB  ARG D  71       6.458  10.120   2.391  1.00 63.14           C  
ANISOU 5825  CB  ARG D  71     8195   5289  10506   -542  -2005   1248       C  
ATOM   5826  CG  ARG D  71       7.580  11.035   2.908  1.00 67.21           C  
ANISOU 5826  CG  ARG D  71     8588   5751  11197   -777  -2439   1302       C  
ATOM   5827  CD  ARG D  71       7.035  12.381   3.355  1.00 68.02           C  
ANISOU 5827  CD  ARG D  71     9055   5750  11036   -935  -2552   1014       C  
ATOM   5828  NE  ARG D  71       7.033  13.339   2.263  1.00 67.72           N  
ANISOU 5828  NE  ARG D  71     8909   5563  11259   -974  -2361    969       N  
ATOM   5829  CZ  ARG D  71       6.204  14.379   2.141  1.00 67.03           C  
ANISOU 5829  CZ  ARG D  71     9127   5316  11024   -974  -2283    717       C  
ATOM   5830  NH1 ARG D  71       5.247  14.662   3.025  1.00 66.15           N  
ANISOU 5830  NH1 ARG D  71     9424   5201  10508   -907  -2312    411       N  
ATOM   5831  NH2 ARG D  71       6.339  15.138   1.067  1.00 67.91           N  
ANISOU 5831  NH2 ARG D  71     9121   5271  11410  -1027  -2151    786       N  
ATOM   5832  N   PRO D  72       7.995   8.255   4.745  1.00 70.86           N  
ANISOU 5832  N   PRO D  72     9133   6356  11433   -610  -2916   1782       N  
ATOM   5833  CA  PRO D  72       8.215   7.971   6.163  1.00 76.11           C  
ANISOU 5833  CA  PRO D  72    10066   7091  11758   -751  -3401   1928       C  
ATOM   5834  C   PRO D  72       7.910   9.164   7.009  1.00 81.13           C  
ANISOU 5834  C   PRO D  72    11086   7802  11934   -999  -3605   1659       C  
ATOM   5835  O   PRO D  72       7.990  10.280   6.528  1.00 82.82           O  
ANISOU 5835  O   PRO D  72    11233   7941  12293  -1078  -3538   1434       O  
ATOM   5836  CB  PRO D  72       9.718   7.654   6.230  1.00 78.39           C  
ANISOU 5836  CB  PRO D  72     9881   7338  12564   -732  -3855   2229       C  
ATOM   5837  CG  PRO D  72      10.148   7.293   4.865  1.00 75.77           C  
ANISOU 5837  CG  PRO D  72     9035   6926  12826   -496  -3479   2271       C  
ATOM   5838  CD  PRO D  72       9.235   8.037   3.953  1.00 72.22           C  
ANISOU 5838  CD  PRO D  72     8728   6476  12236   -508  -2961   1969       C  
ATOM   5839  N   LEU D  73       7.675   8.921   8.281  1.00 90.03           N  
ANISOU 5839  N   LEU D  73    12626   9057  12522  -1132  -3893   1701       N  
ATOM   5840  CA  LEU D  73       7.541   9.970   9.257  1.00 98.75           C  
ANISOU 5840  CA  LEU D  73    14144  10244  13132  -1368  -4162   1416       C  
ATOM   5841  C   LEU D  73       8.874  10.174   9.979  1.00114.12           C  
ANISOU 5841  C   LEU D  73    15980  12187  15192  -1581  -4898   1602       C  
ATOM   5842  O   LEU D  73       9.821   9.471   9.718  1.00115.42           O  
ANISOU 5842  O   LEU D  73    15704  12306  15842  -1506  -5153   1967       O  
ATOM   5843  CB  LEU D  73       6.457   9.577  10.254  1.00 98.83           C  
ANISOU 5843  CB  LEU D  73    14702  10470  12378  -1416  -4000   1334       C  
ATOM   5844  CG  LEU D  73       5.125   9.106   9.666  1.00 93.37           C  
ANISOU 5844  CG  LEU D  73    14049   9831  11593  -1237  -3325   1239       C  
ATOM   5845  CD1 LEU D  73       4.202   8.568  10.752  1.00 95.64           C  
ANISOU 5845  CD1 LEU D  73    14805  10388  11146  -1350  -3183   1263       C  
ATOM   5846  CD2 LEU D  73       4.437  10.213   8.915  1.00 90.38           C  
ANISOU 5846  CD2 LEU D  73    13635   9372  11332  -1134  -2941    807       C  
ATOM   5847  N   PRO D  74       8.964  11.169  10.869  1.00 72.90           N  
ATOM   5848  CA  PRO D  74       9.991  11.259  11.905  1.00 80.87           C  
ATOM   5849  C   PRO D  74      10.595   9.942  12.463  1.00 85.37           C  
ATOM   5850  O   PRO D  74      11.255   9.942  13.526  1.00 88.93           O  
ATOM   5851  CB  PRO D  74       9.229  12.006  13.011  1.00 88.95           C  
ATOM   5852  CG  PRO D  74       8.109  12.763  12.302  1.00 85.12           C  
ATOM   5853  CD  PRO D  74       8.184  12.425  10.845  1.00 79.90           C  
TER    5854      PRO D  74                                                      
ATOM   5855  N   MET E   1       4.836 -18.878 -15.078  1.00144.25           N  
ANISOU 5855  N   MET E   1    20628  17243  16937    994   -900  -2125       N  
ATOM   5856  CA  MET E   1       6.037 -18.001 -15.333  1.00151.28           C  
ANISOU 5856  CA  MET E   1    20870  18759  17847    737  -1041  -2416       C  
ATOM   5857  C   MET E   1       7.378 -18.508 -14.807  1.00150.18           C  
ANISOU 5857  C   MET E   1    20220  19725  17115   1300  -1042  -2293       C  
ATOM   5858  O   MET E   1       8.401 -17.830 -14.975  1.00154.43           O  
ANISOU 5858  O   MET E   1    20150  20907  17617   1050  -1152  -2549       O  
ATOM   5859  CB  MET E   1       5.812 -16.552 -14.802  1.00162.32           C  
ANISOU 5859  CB  MET E   1    21877  20271  19526     61  -1246  -3005       C  
ATOM   5860  CG  MET E   1       5.998 -15.455 -15.855  1.00168.56           C  
ANISOU 5860  CG  MET E   1    22581  20637  20826   -583  -1229  -3251       C  
ATOM   5861  SD  MET E   1       4.493 -15.091 -16.765  1.00175.20           S  
ANISOU 5861  SD  MET E   1    24078  20250  22238   -919  -1126  -3149       S  
ATOM   5862  CE  MET E   1       4.071 -16.678 -17.563  1.00168.91           C  
ANISOU 5862  CE  MET E   1    23883  19001  21291   -384   -970  -2543       C  
ATOM   5863  N   GLU E   2       7.378 -19.640 -14.122  1.00145.82           N  
ANISOU 5863  N   GLU E   2    19873  19461  16067   2051   -894  -1913       N  
ATOM   5864  CA  GLU E   2       8.611 -20.316 -13.777  1.00147.77           C  
ANISOU 5864  CA  GLU E   2    19728  20740  15676   2787   -810  -1638       C  
ATOM   5865  C   GLU E   2       9.385 -20.588 -15.033  1.00143.71           C  
ANISOU 5865  C   GLU E   2    19274  20098  15231   2892   -664  -1382       C  
ATOM   5866  O   GLU E   2      10.548 -20.210 -15.160  1.00145.93           O  
ANISOU 5866  O   GLU E   2    18883  21264  15298   2902   -762  -1488       O  
ATOM   5867  CB  GLU E   2       8.313 -21.635 -13.046  1.00150.89           C  
ANISOU 5867  CB  GLU E   2    20592  21163  15577   3681   -523  -1131       C  
ATOM   5868  CG  GLU E   2       8.180 -21.515 -11.535  1.00155.03           C  
ANISOU 5868  CG  GLU E   2    20741  22474  15687   3935   -659  -1290       C  
ATOM   5869  CD  GLU E   2       7.403 -20.285 -11.087  1.00153.54           C  
ANISOU 5869  CD  GLU E   2    20332  22080  15926   3081   -982  -1905       C  
ATOM   5870  OE1 GLU E   2       6.342 -19.988 -11.685  1.00149.47           O  
ANISOU 5870  OE1 GLU E   2    20326  20466  15997   2532   -965  -1991       O  
ATOM   5871  OE2 GLU E   2       7.873 -19.592 -10.163  1.00157.47           O  
ANISOU 5871  OE2 GLU E   2    20133  23558  16140   2961  -1236  -2316       O  
ATOM   5872  N   ASP E   3       8.721 -21.247 -15.966  1.00137.11           N  
ANISOU 5872  N   ASP E   3    19230  18192  14671   2940   -421  -1067       N  
ATOM   5873  CA  ASP E   3       9.352 -21.677 -17.202  1.00137.00           C  
ANISOU 5873  CA  ASP E   3    19422  17944  14687   3133   -228   -768       C  
ATOM   5874  C   ASP E   3       9.638 -20.549 -18.243  1.00132.90           C  
ANISOU 5874  C   ASP E   3    18572  17245  14677   2384   -408  -1091       C  
ATOM   5875  O   ASP E   3      10.306 -20.827 -19.257  1.00135.10           O  
ANISOU 5875  O   ASP E   3    18913  17472  14943   2565   -264   -850       O  
ATOM   5876  CB  ASP E   3       8.507 -22.791 -17.862  1.00134.56           C  
ANISOU 5876  CB  ASP E   3    20122  16537  14468   3377    123   -384       C  
ATOM   5877  CG  ASP E   3       8.454 -24.079 -17.040  1.00137.76           C  
ANISOU 5877  CG  ASP E   3    20976  17038  14328   4235    473     52       C  
ATOM   5878  OD1 ASP E   3       9.264 -24.299 -16.108  1.00141.53           O  
ANISOU 5878  OD1 ASP E   3    20993  18530  14249   4878    488    202       O  
ATOM   5879  OD2 ASP E   3       7.609 -24.920 -17.396  1.00137.79           O  
ANISOU 5879  OD2 ASP E   3    21830  16092  14432   4279    787    264       O  
ATOM   5880  N   TYR E   4       9.151 -19.322 -18.009  1.00126.68           N  
ANISOU 5880  N   TYR E   4    17491  16332  14309   1613   -658  -1591       N  
ATOM   5881  CA  TYR E   4       9.164 -18.239 -19.005  1.00120.83           C  
ANISOU 5881  CA  TYR E   4    16624  15173  14114    900   -726  -1860       C  
ATOM   5882  C   TYR E   4       9.622 -16.882 -18.468  1.00122.14           C  
ANISOU 5882  C   TYR E   4    16077  15901  14428    261   -926  -2418       C  
ATOM   5883  O   TYR E   4       9.142 -16.423 -17.443  1.00122.11           O  
ANISOU 5883  O   TYR E   4    15934  16053  14406     37  -1067  -2748       O  
ATOM   5884  CB  TYR E   4       7.764 -18.060 -19.571  1.00114.10           C  
ANISOU 5884  CB  TYR E   4    16409  13199  13745    524   -693  -1879       C  
ATOM   5885  CG  TYR E   4       7.213 -19.263 -20.294  1.00111.12           C  
ANISOU 5885  CG  TYR E   4    16766  12155  13298    917   -474  -1448       C  
ATOM   5886  CD1 TYR E   4       7.507 -19.483 -21.620  1.00109.78           C  
ANISOU 5886  CD1 TYR E   4    16837  11616  13258    944   -333  -1238       C  
ATOM   5887  CD2 TYR E   4       6.385 -20.181 -19.653  1.00110.10           C  
ANISOU 5887  CD2 TYR E   4    17117  11749  12965   1220   -371  -1276       C  
ATOM   5888  CE1 TYR E   4       7.009 -20.599 -22.299  1.00108.34           C  
ANISOU 5888  CE1 TYR E   4    17367  10817  12979   1238   -103   -915       C  
ATOM   5889  CE2 TYR E   4       5.873 -21.304 -20.327  1.00109.32           C  
ANISOU 5889  CE2 TYR E   4    17748  10989  12798   1471   -104   -946       C  
ATOM   5890  CZ  TYR E   4       6.185 -21.517 -21.666  1.00108.25           C  
ANISOU 5890  CZ  TYR E   4    17860  10496  12774   1462     25   -790       C  
ATOM   5891  OH  TYR E   4       5.642 -22.612 -22.375  1.00107.20           O  
ANISOU 5891  OH  TYR E   4    18491   9681  12560   1618    309   -546       O  
ATOM   5892  N   THR E   5      10.524 -16.232 -19.200  1.00123.42           N  
ANISOU 5892  N   THR E   5    15835  16311  14748    -72   -898  -2540       N  
ATOM   5893  CA  THR E   5      10.869 -14.821 -18.972  1.00124.87           C  
ANISOU 5893  CA  THR E   5    15489  16746  15210   -877   -979  -3117       C  
ATOM   5894  C   THR E   5      10.049 -13.929 -19.889  1.00119.63           C  
ANISOU 5894  C   THR E   5    15268  14969  15215  -1449   -854  -3226       C  
ATOM   5895  O   THR E   5       9.973 -14.180 -21.093  1.00115.82           O  
ANISOU 5895  O   THR E   5    15132  13925  14948  -1328   -708  -2889       O  
ATOM   5896  CB  THR E   5      12.337 -14.506 -19.318  1.00130.82           C  
ANISOU 5896  CB  THR E   5    15526  18385  15792  -1026   -947  -3210       C  
ATOM   5897  OG1 THR E   5      12.584 -14.824 -20.698  1.00129.03           O  
ANISOU 5897  OG1 THR E   5    15588  17671  15765   -846   -760  -2799       O  
ATOM   5898  CG2 THR E   5      13.261 -15.284 -18.439  1.00136.67           C  
ANISOU 5898  CG2 THR E   5    15697  20436  15794   -419  -1059  -3094       C  
ATOM   5899  N   LYS E   6       9.492 -12.866 -19.315  1.00119.42           N  
ANISOU 5899  N   LYS E   6    15215  14688  15470  -2031   -882  -3695       N  
ATOM   5900  CA  LYS E   6       8.883 -11.762 -20.090  1.00116.30           C  
ANISOU 5900  CA  LYS E   6    15144  13367  15676  -2590   -690  -3845       C  
ATOM   5901  C   LYS E   6      10.021 -10.999 -20.727  1.00119.13           C  
ANISOU 5901  C   LYS E   6    15076  13981  16205  -3056   -520  -4031       C  
ATOM   5902  O   LYS E   6      11.020 -10.748 -20.056  1.00124.66           O  
ANISOU 5902  O   LYS E   6    15133  15590  16639  -3315   -593  -4385       O  
ATOM   5903  CB  LYS E   6       8.050 -10.828 -19.195  1.00116.93           C  
ANISOU 5903  CB  LYS E   6    15336  13141  15947  -3022   -697  -4296       C  
ATOM   5904  CG  LYS E   6       6.631 -11.348 -18.847  1.00113.03           C  
ANISOU 5904  CG  LYS E   6    15379  12121  15446  -2660   -786  -4070       C  
ATOM   5905  CD  LYS E   6       5.768 -10.405 -17.980  1.00113.29           C  
ANISOU 5905  CD  LYS E   6    15546  11850  15649  -3015   -765  -4475       C  
ATOM   5906  CE  LYS E   6       4.614 -11.198 -17.331  1.00109.79           C  
ANISOU 5906  CE  LYS E   6    15433  11271  15010  -2567   -916  -4245       C  
ATOM   5907  NZ  LYS E   6       3.362 -10.487 -16.964  1.00108.04           N  
ANISOU 5907  NZ  LYS E   6    15558  10472  15020  -2727   -845  -4381       N  
ATOM   5908  N   ILE E   7       9.949 -10.814 -22.041  1.00116.32           N  
ANISOU 5908  N   ILE E   7    15024  12973  16199  -3081   -305  -3741       N  
ATOM   5909  CA  ILE E   7      10.947 -10.041 -22.802  1.00120.38           C  
ANISOU 5909  CA  ILE E   7    15212  13581  16945  -3537    -66  -3857       C  
ATOM   5910  C   ILE E