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***  Oligopeptidase B from Trypanosoma brucei with covalently bound antipain - closed form  ***

elNémo ID: 21032523424327926

Job options:

ID        	=	 21032523424327926
JOBID     	=	 Oligopeptidase B from Trypanosoma brucei with covalently bound antipain - closed form
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 10
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER Oligopeptidase B from Trypanosoma brucei with covalently bound antipain - closed form

HEADER    HYDROLASE                               23-MAY-13   4BP9              
TITLE     OLIGOPEPTIDASE B FROM TRYPANOSOMA BRUCEI WITH COVALENTLY BOUND        
TITLE    2 ANTIPAIN - CLOSED FORM                                               
CAVEAT     4BP9    OAR G 4 HAS WRONG CHIRALITY AT ATOM CA OAR H 4 HAS WRONG     
CAVEAT   2 4BP9    CHIRALITY AT ATOM CA OAR I 4 HAS WRONG CHIRALITY AT ATOM CA  
CAVEAT   3 4BP9    OAR J 4 HAS WRONG CHIRALITY AT ATOM CA OAR K 4 HAS WRONG     
CAVEAT   4 4BP9    CHIRALITY AT ATOM CA OAR L 4 HAS WRONG CHIRALITY AT ATOM CA  
CAVEAT   5 4BP9    OAR G 4 CA HAS THE WRONG CHIRALITY OAR H 4 CA HAS THE WRONG  
CAVEAT   6 4BP9    CHIRALITY OAR I 4 CA HAS THE WRONG CHIRALITY OAR J 4 CA HAS  
CAVEAT   7 4BP9    THE WRONG CHIRALITY OAR K 4 CA HAS THE WRONG CHIRALITY OAR   
CAVEAT   8 4BP9    L 4 CA HAS THE WRONG CHIRALITY                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: OLIGOPEPTIDASSE B;                                         
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 EC: 3.4.21.83;                                                       
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: ANTIPAIN;                                                  
COMPND   8 CHAIN: G, H, I, J, K, L                                              
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: TRYPANOSOMA BRUCEI;                             
SOURCE   3 ORGANISM_TAXID: 5691;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   7 EXPRESSION_SYSTEM_VARIANT: PRARE;                                    
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: ACTINOBACTERIA;                                 
SOURCE  11 ORGANISM_TAXID: 1760                                                 
KEYWDS    HYDROLASE, PROLYL OLIGOPEPTIDASE                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.CANNING,D.REA,R.MORTY,V.FULOP                                       
REVDAT   6   10-JUL-19 4BP9    1       REMARK                                   
REVDAT   5   15-MAY-19 4BP9    1       CAVEAT REMARK SEQRES LINK                
REVDAT   4   13-SEP-17 4BP9    1       REMARK                                   
REVDAT   3   18-JUN-14 4BP9    1       HETATM                                   
REVDAT   2   19-MAR-14 4BP9    1       JRNL   HETATM                            
REVDAT   1   12-FEB-14 4BP9    0                                                
JRNL        AUTH   P.CANNING,D.REA,R.E.MORTY,V.FULOP                            
JRNL        TITL   CRYSTAL STRUCTURES OF TRYPANOSOMA BRUCEI OLIGOPEPTIDASE B    
JRNL        TITL 2 BROADEN THE PARADIGM OF CATALYTIC REGULATION IN PROLYL       
JRNL        TITL 3 OLIGOPEPTIDASE FAMILY ENZYMES.                               
JRNL        REF    PLOS ONE                      V.   8 79349 2013              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   24265767                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0079349                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 58.59                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 121891                         
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) : 0.216                           
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.281                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5162                            
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) : 2.85                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.92                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8894                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.86                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2920                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 379                          
REMARK   3   BIN FREE R VALUE                    : 0.3650                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 34062                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 344                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 45.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 59.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.97000                                             
REMARK   3    B22 (A**2) : 1.49000                                              
REMARK   3    B33 (A**2) : 0.51000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.69000                                              
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): 0.436         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.381         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 43.636        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.882                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 34896 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 47322 ; 1.697 ; 1.966       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  4254 ; 8.110 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1614 ;35.788 ;23.234       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  5814 ;20.883 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   276 ;20.513 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  5136 ; 0.115 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 26730 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 21210 ; 0.392 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 34344 ; 0.774 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 13686 ; 1.381 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 12978 ; 2.302 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 18                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     5        A    86                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.5900 121.8250 223.9420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4167 T22:   0.6717                                     
REMARK   3      T33:   0.3381 T12:   0.1220                                     
REMARK   3      T13:   0.1576 T23:   0.0634                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6990 L22:   2.1497                                     
REMARK   3      L33:   2.5552 L12:   0.6199                                     
REMARK   3      L13:  -0.2926 L23:  -0.7631                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1958 S12:   0.1253 S13:   0.4175                       
REMARK   3      S21:   0.3655 S22:   0.1841 S23:   0.5994                       
REMARK   3      S31:  -0.5691 S32:  -0.5266 S33:  -0.3799                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    87        A   441                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.7330 106.1900 248.7460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4345 T22:   0.5750                                     
REMARK   3      T33:   0.1617 T12:   0.0175                                     
REMARK   3      T13:   0.0165 T23:   0.0290                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7974 L22:   0.9615                                     
REMARK   3      L33:   1.3416 L12:   0.0510                                     
REMARK   3      L13:   0.0312 L23:  -0.1461                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0236 S12:  -0.1981 S13:   0.0613                       
REMARK   3      S21:   0.2644 S22:   0.0492 S23:   0.0167                       
REMARK   3      S31:   0.0564 S32:   0.1057 S33:  -0.0728                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   442        A   714                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.6600 109.6620 220.1640              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3974 T22:   0.5619                                     
REMARK   3      T33:   0.2233 T12:  -0.0135                                     
REMARK   3      T13:   0.0302 T23:   0.0224                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6979 L22:   1.3464                                     
REMARK   3      L33:   1.2312 L12:   0.2719                                     
REMARK   3      L13:  -0.1035 L23:  -0.0608                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0431 S12:   0.0166 S13:   0.0967                       
REMARK   3      S21:   0.1000 S22:   0.0223 S23:   0.0333                       
REMARK   3      S31:   0.1256 S32:  -0.0731 S33:  -0.0654                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     5        B    86                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.3490 140.4630 194.0850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5018 T22:   0.5705                                     
REMARK   3      T33:   0.1958 T12:   0.0926                                     
REMARK   3      T13:   0.0635 T23:   0.0622                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7073 L22:   2.2222                                     
REMARK   3      L33:   1.7304 L12:   0.8004                                     
REMARK   3      L13:  -0.1787 L23:  -0.3574                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1091 S12:   0.1983 S13:   0.2519                       
REMARK   3      S21:  -0.0253 S22:  -0.0500 S23:   0.3722                       
REMARK   3      S31:  -0.5191 S32:  -0.2990 S33:  -0.0591                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    87        B   441                          
REMARK   3    ORIGIN FOR THE GROUP (A):  60.2030 124.7900 182.9270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2849 T22:   0.9500                                     
REMARK   3      T33:   0.1952 T12:  -0.0171                                     
REMARK   3      T13:   0.0462 T23:  -0.0040                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6099 L22:   0.6688                                     
REMARK   3      L33:   2.0683 L12:   0.1180                                     
REMARK   3      L13:  -0.1344 L23:   0.0305                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0452 S12:   0.1562 S13:  -0.0498                       
REMARK   3      S21:  -0.0502 S22:  -0.0286 S23:  -0.0325                       
REMARK   3      S31:   0.0113 S32:   0.7632 S33:  -0.0166                       
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 :   B   442        B   714                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.7200 136.6320 204.7970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5128 T22:   0.6435                                     
REMARK   3      T33:   0.2551 T12:  -0.0916                                     
REMARK   3      T13:   0.0492 T23:   0.0073                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9062 L22:   0.6838                                     
REMARK   3      L33:   1.5649 L12:   0.3395                                     
REMARK   3      L13:   0.0004 L23:  -0.0698                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0318 S12:   0.0404 S13:   0.0281                       
REMARK   3      S21:   0.0167 S22:   0.0346 S23:   0.0325                       
REMARK   3      S31:  -0.4014 S32:   0.2819 S33:  -0.0665                       
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 :   C     5        C    86                          
REMARK   3    ORIGIN FOR THE GROUP (A):  54.7850  42.3530 216.1690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7079 T22:   0.7692                                     
REMARK   3      T33:   0.3170 T12:  -0.0160                                     
REMARK   3      T13:   0.1993 T23:  -0.1079                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9413 L22:   0.9072                                     
REMARK   3      L33:   3.3626 L12:   0.4730                                     
REMARK   3      L13:   1.5078 L23:   0.1774                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0703 S12:   0.0353 S13:  -0.5749                       
REMARK   3      S21:  -0.1498 S22:  -0.2024 S23:  -0.1314                       
REMARK   3      S31:   0.7459 S32:  -0.4066 S33:   0.1321                       
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    87        C   441                          
REMARK   3    ORIGIN FOR THE GROUP (A):  60.3880  72.6490 198.3050              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8187 T22:   0.8194                                     
REMARK   3      T33:   0.2041 T12:   0.2483                                     
REMARK   3      T13:   0.0521 T23:   0.0232                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9881 L22:   0.6715                                     
REMARK   3      L33:   1.8239 L12:   0.2944                                     
REMARK   3      L13:  -0.3279 L23:  -0.1156                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0195 S12:   0.3042 S13:   0.0102                       
REMARK   3      S21:  -0.1385 S22:  -0.0436 S23:   0.0142                       
REMARK   3      S31:  -0.4683 S32:  -0.5338 S33:   0.0241                       
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   442        C   714                          
REMARK   3    ORIGIN FOR THE GROUP (A):  48.1420  57.7610 221.1940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6350 T22:   0.9659                                     
REMARK   3      T33:   0.2986 T12:   0.1006                                     
REMARK   3      T13:   0.0615 T23:  -0.0421                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8321 L22:   0.5125                                     
REMARK   3      L33:   1.7825 L12:   0.1390                                     
REMARK   3      L13:  -0.3256 L23:   0.2134                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0449 S12:   0.2659 S13:  -0.0686                       
REMARK   3      S21:  -0.1575 S22:  -0.1292 S23:  -0.0214                       
REMARK   3      S31:  -0.0504 S32:  -0.6442 S33:   0.0843                       
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 :   D     5        D    86                          
REMARK   3    ORIGIN FOR THE GROUP (A):  65.6170  42.5170 255.1530              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6980 T22:   0.6300                                     
REMARK   3      T33:   0.2937 T12:   0.1245                                     
REMARK   3      T13:   0.2327 T23:   0.1211                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6422 L22:   1.1404                                     
REMARK   3      L33:   3.2490 L12:   0.4076                                     
REMARK   3      L13:   1.2411 L23:   0.1890                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0071 S12:  -0.1410 S13:  -0.4821                       
REMARK   3      S21:   0.1323 S22:  -0.2149 S23:   0.1114                       
REMARK   3      S31:   0.9723 S32:   0.0914 S33:   0.2078                       
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 :   D    87        D   441                          
REMARK   3    ORIGIN FOR THE GROUP (A):  60.0250  72.8510 272.8470              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5627 T22:   0.6474                                     
REMARK   3      T33:   0.1901 T12:  -0.0724                                     
REMARK   3      T13:   0.0417 T23:   0.0124                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9444 L22:   0.9860                                     
REMARK   3      L33:   1.8714 L12:  -0.0542                                     
REMARK   3      L13:  -0.3010 L23:  -0.1905                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0269 S12:  -0.2001 S13:   0.0299                       
REMARK   3      S21:   0.1758 S22:  -0.0754 S23:   0.0910                       
REMARK   3      S31:  -0.3145 S32:   0.2250 S33:   0.0485                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   442        D   714                          
REMARK   3    ORIGIN FOR THE GROUP (A):  72.2920  57.8150 250.0510              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5541 T22:   0.7766                                     
REMARK   3      T33:   0.3074 T12:   0.0411                                     
REMARK   3      T13:   0.1055 T23:   0.1021                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6143 L22:   0.5319                                     
REMARK   3      L33:   2.1111 L12:   0.1707                                     
REMARK   3      L13:  -0.5368 L23:   0.0843                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0079 S12:  -0.0999 S13:  -0.0787                       
REMARK   3      S21:   0.0000 S22:  -0.1351 S23:   0.0047                       
REMARK   3      S31:   0.0555 S32:   0.3940 S33:   0.1272                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     5        E    86                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.0760  47.4680 159.1150              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3635 T22:   1.2215                                     
REMARK   3      T33:   0.2785 T12:   0.1284                                     
REMARK   3      T13:   0.0073 T23:   0.0586                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2776 L22:   0.9642                                     
REMARK   3      L33:   6.0542 L12:   0.0100                                     
REMARK   3      L13:  -1.2905 L23:  -0.2890                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1614 S12:   0.1644 S13:   0.0061                       
REMARK   3      S21:   0.1345 S22:   0.0118 S23:   0.3237                       
REMARK   3      S31:  -0.5452 S32:  -1.9389 S33:  -0.1732                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E    87        E   441                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.4720  31.2900 183.9780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7986 T22:   0.6169                                     
REMARK   3      T33:   0.2453 T12:   0.1113                                     
REMARK   3      T13:   0.0987 T23:   0.0521                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1442 L22:   0.6682                                     
REMARK   3      L33:   4.7127 L12:  -0.0342                                     
REMARK   3      L13:  -1.0401 L23:  -0.0614                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2468 S12:  -0.3082 S13:  -0.1246                       
REMARK   3      S21:   0.2348 S22:   0.0687 S23:  -0.0271                       
REMARK   3      S31:   1.0113 S32:   0.4200 S33:   0.1781                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   442        E   714                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.8330  35.1570 155.3530              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6198 T22:   0.6742                                     
REMARK   3      T33:   0.2601 T12:  -0.1532                                     
REMARK   3      T13:   0.1086 T23:  -0.0524                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0216 L22:   0.6808                                     
REMARK   3      L33:   5.1965 L12:   0.1705                                     
REMARK   3      L13:  -1.1195 L23:  -0.2129                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2581 S12:   0.1592 S13:  -0.0979                       
REMARK   3      S21:   0.0656 S22:   0.0642 S23:   0.0201                       
REMARK   3      S31:   0.8737 S32:  -0.6651 S33:   0.1939                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F     5        F    86                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.4370  65.9230 129.6430              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8811 T22:   0.6564                                     
REMARK   3      T33:   0.2072 T12:   0.1066                                     
REMARK   3      T13:   0.0490 T23:   0.0488                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1089 L22:   2.5497                                     
REMARK   3      L33:   4.8052 L12:   0.1485                                     
REMARK   3      L13:  -0.7594 L23:  -0.0812                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1890 S12:   0.4240 S13:   0.2735                       
REMARK   3      S21:  -0.0147 S22:  -0.0471 S23:   0.2624                       
REMARK   3      S31:  -1.5659 S32:  -0.5421 S33:  -0.1419                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F    87        F   441                          
REMARK   3    ORIGIN FOR THE GROUP (A):  46.9830  49.4520 118.5030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2921 T22:   1.4549                                     
REMARK   3      T33:   0.2573 T12:  -0.1609                                     
REMARK   3      T13:   0.0550 T23:  -0.0606                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5034 L22:   0.8560                                     
REMARK   3      L33:   4.5782 L12:  -0.0053                                     
REMARK   3      L13:  -0.2308 L23:  -0.1363                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0072 S12:  -0.0150 S13:  -0.0005                       
REMARK   3      S21:  -0.0182 S22:   0.0026 S23:  -0.0323                       
REMARK   3      S31:  -0.1926 S32:   1.8657 S33:   0.0046                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F   442        F   714                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.6280  61.7550 140.3490              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7467 T22:   0.7807                                     
REMARK   3      T33:   0.2763 T12:  -0.2802                                     
REMARK   3      T13:   0.0675 T23:  -0.0409                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8171 L22:   0.6648                                     
REMARK   3      L33:   4.4124 L12:   0.0084                                     
REMARK   3      L13:  -0.4684 L23:  -0.2158                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1334 S12:  -0.0515 S13:   0.0705                       
REMARK   3      S21:   0.0852 S22:   0.0178 S23:  -0.0570                       
REMARK   3      S31:  -1.1722 S32:   0.8420 S33:  -0.1512                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. U VALUES WITH TLS ADDED                                  
REMARK   4                                                                      
REMARK   4 4BP9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-MAY-13.                  
REMARK 100 THE DEPOSITION ID IS D_1290056998.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-OCT-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9778                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 127053                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 59.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : 0.22000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.12000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: STARTING MODEL IS ALSO BEING CURRENTLY DEPOSITED             
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 % PEG 4000, 0.2 M CALCIUM ACETATE,    
REMARK 280  0.1 M SODIUM ACETATE PH 5                                           
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       74.40000            
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, 5, 6                                        
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, G                                  
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 APPLY THE FOLLOWING TO CHAINS: B, 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, I                                  
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 APPLY THE FOLLOWING TO CHAINS: D, J                                  
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: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, K                                  
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: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, L                                  
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ANTIPAIN HYDROCHLORIDE IS A REVERSIBLE INHIBITOR OF SERINE/CYSTEINE  
REMARK 400 PROTEASES AND SOME TRYPSIN-LIKE SERINE PROTEASES. ITS ACTION         
REMARK 400 RESEMBLES LEUPEPTIN; HOWEVER, ITS PLASMIN INHIBITION IS LESS AND     
REMARK 400 ITS CATHEPSIN A INHIBITION IS MORE THAN THAT OBSERVED WITH           
REMARK 400 LEUPEPTIN. IT IS AN INHIBITOR OF TRYPSIN-LIKE PROTEASES              
REMARK 400 (E.G. TRYPSIN, PAPAIN, CATHEPSIN B); CATHEPSIN A, A CARBOXYPEPTIDASE 
REMARK 400 IS INHIBITED TOO, WHICH IS NOT TRUE FOR OTHER INHIBITORS FROM        
REMARK 400 ACTINOMYCES.THE NAME IS DERIVED FROM ANTI-PAPAIN.                    
REMARK 400                                                                      
REMARK 400  GROUP: 1                                                            
REMARK 400   NAME: ANTIPAIN                                                     
REMARK 400   CHAIN: G, H, I, J, K, L                                            
REMARK 400   COMPONENT_1: PEPTIDE LIKE SEQUENCE RESIDUES 1 TO 4                 
REMARK 400   DESCRIPTION: ANTIPAIN FORMS A COVALENT LINKAGE BETWEEN THE ARGINAL 
REMARK 400                RESIDUE OF THE INHIBITOR AND SER RESIDUE OF THE       
REMARK 400                PROTEIN.THE PROTEASE INHIBITOR ANTIPAIN INCREASES THE 
REMARK 400                EFFECTIVENESSOF UV IRRADIATION ON CESSATION OF        
REMARK 400                RESPIRATION AND CELL KILLING IN ESCHERICHIA COLI B/R  
REMARK 400                CULTURES WITHOUT AFFECTING EXCISION OF PYRIMIDINE     
REMARK 400                DIMERS. THE ACTIONS ARE SIMILAR TO THOSE CAUSED BY    
REMARK 400                CYCLIC AMP IN IRRADIATED CULTURES.                    
REMARK 400                                                                      
REMARK 400 THE ANTIPAIN IS OLIGOPEPTIDE, A MEMBER OF ENZYME INHIBITOR CLASS.    
REMARK 400                                                                      
REMARK 400  GROUP: 1                                                            
REMARK 400   NAME: ANTIPAIN                                                     
REMARK 400   CHAIN: G, H, I, J, K, L                                            
REMARK 400   COMPONENT_1: PEPTIDE LIKE POLYMER                                  
REMARK 400   COMPONENT_2: PEPTIDE LIKE POLYMER                                  
REMARK 400   COMPONENT_3: PEPTIDE LIKE POLYMER                                  
REMARK 400   COMPONENT_4: PEPTIDE LIKE POLYMER                                  
REMARK 400   COMPONENT_5: PEPTIDE LIKE POLYMER                                  
REMARK 400   COMPONENT_6: PEPTIDE LIKE POLYMER                                  
REMARK 400   DESCRIPTION: NULL                                                  
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLN A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     LYS A   715                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLN B     2                                                      
REMARK 465     THR B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     LYS B   715                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLN C     2                                                      
REMARK 465     THR C     3                                                      
REMARK 465     GLU C     4                                                      
REMARK 465     LYS C   715                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLN D     2                                                      
REMARK 465     THR D     3                                                      
REMARK 465     GLU D     4                                                      
REMARK 465     LYS D   715                                                      
REMARK 465     MET E     1                                                      
REMARK 465     GLN E     2                                                      
REMARK 465     THR E     3                                                      
REMARK 465     GLU E     4                                                      
REMARK 465     LYS E   715                                                      
REMARK 465     MET F     1                                                      
REMARK 465     GLN F     2                                                      
REMARK 465     THR F     3                                                      
REMARK 465     GLU F     4                                                      
REMARK 465     LYS F   715                                                      
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   OG   SER A   563     C    OAR G     4              1.35            
REMARK 500   OG   SER D   563     C    OAR J     4              1.35            
REMARK 500   OG   SER C   563     C    OAR I     4              1.35            
REMARK 500   OG   SER F   563     C    OAR L     4              1.35            
REMARK 500   OG   SER B   563     C    OAR H     4              1.36            
REMARK 500   OG   SER E   563     C    OAR K     4              1.38            
REMARK 500   OH   TYR E   444     OD1  ASP E   502              2.06            
REMARK 500   OG   SER C   563     O    OAR I     4              2.06            
REMARK 500   OG   SER A   563     O    OAR G     4              2.07            
REMARK 500   OD1  ASP D   455     OG1  THR D   457              2.11            
REMARK 500   OG   SER D   563     O    OAR J     4              2.11            
REMARK 500   O    GLY C   367     N    ASP C   369              2.13            
REMARK 500   NH2  ARG F   664     O    VAL F   673              2.14            
REMARK 500   ND2  ASN C   312     OG1  THR C   338              2.15            
REMARK 500   O    HIS B   381     NH2  ARG B   427              2.15            
REMARK 500   OG   SER F   563     O    OAR L     4              2.16            
REMARK 500   OG1  THR B   477     OG1  THR B   552              2.16            
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  49   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    PRO A 157   C   -  N   -  CD  ANGL. DEV. = -17.3 DEGREES          
REMARK 500    VAL A 350   CB  -  CA  -  C   ANGL. DEV. = -12.1 DEGREES          
REMARK 500    TYR A 482   CA  -  C   -  N   ANGL. DEV. =  12.1 DEGREES          
REMARK 500    GLY A 483   N   -  CA  -  C   ANGL. DEV. = -16.4 DEGREES          
REMARK 500    ARG A 496   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 664   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ARG B  49   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG B  49   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    PRO B 157   C   -  N   -  CA  ANGL. DEV. =  12.2 DEGREES          
REMARK 500    PRO B 157   C   -  N   -  CD  ANGL. DEV. = -18.5 DEGREES          
REMARK 500    LEU B 463   CA  -  CB  -  CG  ANGL. DEV. =  16.6 DEGREES          
REMARK 500    GLY B 483   N   -  CA  -  C   ANGL. DEV. = -15.1 DEGREES          
REMARK 500    ARG B 533   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    PRO C 157   C   -  N   -  CA  ANGL. DEV. =  10.7 DEGREES          
REMARK 500    PRO C 157   C   -  N   -  CD  ANGL. DEV. = -17.2 DEGREES          
REMARK 500    PRO D 156   C   -  N   -  CA  ANGL. DEV. =  10.9 DEGREES          
REMARK 500    PRO D 157   C   -  N   -  CD  ANGL. DEV. = -16.9 DEGREES          
REMARK 500    PRO E 157   C   -  N   -  CD  ANGL. DEV. = -13.1 DEGREES          
REMARK 500    LEU E 279   CA  -  CB  -  CG  ANGL. DEV. =  15.4 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    ASP A  32      112.98   -160.89                                   
REMARK 500    GLU A  88       89.02     60.71                                   
REMARK 500    ASP A  99     -129.36     60.90                                   
REMARK 500    ALA A 121      -57.64    -27.72                                   
REMARK 500    GLU A 142      101.87    -27.60                                   
REMARK 500    PRO A 156      162.68    -26.97                                   
REMARK 500    PRO A 157      -74.67     29.46                                   
REMARK 500    ARG A 180       26.25     38.32                                   
REMARK 500    ASN A 199       39.26     37.94                                   
REMARK 500    LYS A 208     -165.38    -67.25                                   
REMARK 500    ALA A 210      126.45    -37.14                                   
REMARK 500    MET A 281      140.22    -38.27                                   
REMARK 500    VAL A 282      -76.17   -100.86                                   
REMARK 500    PHE A 348      178.26    177.18                                   
REMARK 500    PRO A 368      -32.80    -38.50                                   
REMARK 500    SER A 394        8.46    -66.86                                   
REMARK 500    MET A 411       -9.00    -50.75                                   
REMARK 500    THR A 467      -10.40    -48.05                                   
REMARK 500    TYR A 482      -91.72   -107.00                                   
REMARK 500    TYR A 485      -14.94     63.44                                   
REMARK 500    HIS A 511       59.36    -93.69                                   
REMARK 500    TYR A 529     -136.05     44.47                                   
REMARK 500    LEU A 530       22.77    -74.12                                   
REMARK 500    SER A 563     -122.95     61.27                                   
REMARK 500    VAL A 587       56.74     30.30                                   
REMARK 500    ASP A 591       62.18   -102.00                                   
REMARK 500    GLU A 610      -70.23   -125.56                                   
REMARK 500    PHE A 620      -74.01    -37.44                                   
REMARK 500    ALA A 634       96.84    -63.11                                   
REMARK 500    HIS A 647       34.05    -97.82                                   
REMARK 500    SER A 685      -91.55    -59.83                                   
REMARK 500    ALA A 686      -69.42     65.62                                   
REMARK 500    SER A 687     -174.41   -170.70                                   
REMARK 500    ARG A 689     -150.04   -134.92                                   
REMARK 500    ASN A 708       47.73     75.38                                   
REMARK 500    ASN B  29       58.07   -153.34                                   
REMARK 500    GLU B  88       87.23     56.32                                   
REMARK 500    SER B  93      179.22    -52.68                                   
REMARK 500    ASP B  99     -127.54     42.38                                   
REMARK 500    ALA B 121       90.29    -59.18                                   
REMARK 500    GLU B 142       96.10    -27.81                                   
REMARK 500    CYS B 147      100.38   -160.06                                   
REMARK 500    PRO B 156      180.00    -54.85                                   
REMARK 500    PRO B 157      -75.21     29.55                                   
REMARK 500    ASN B 199       55.26     27.68                                   
REMARK 500    ASP B 214       96.23    -66.14                                   
REMARK 500    ILE B 222      132.67    -39.56                                   
REMARK 500    VAL B 274      -20.01    -33.66                                   
REMARK 500    VAL B 282      -74.63    -95.28                                   
REMARK 500    ASP B 308       32.17     72.67                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     263 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 PRO A  156     PRO A  157                 -129.12                    
REMARK 500 SER A  685     ALA A  686                 -137.48                    
REMARK 500 PRO B  156     PRO B  157                 -129.96                    
REMARK 500 TYR B  482     GLY B  483                  -48.31                    
REMARK 500 SER B  685     ALA B  686                 -135.86                    
REMARK 500 ASP B  688     ARG B  689                 -147.02                    
REMARK 500 GLY C  110     LEU C  111                 -149.94                    
REMARK 500 PRO C  156     PRO C  157                 -126.69                    
REMARK 500 TYR C  482     GLY C  483                  -30.80                    
REMARK 500 SER C  685     ALA C  686                 -145.30                    
REMARK 500 PRO D  156     PRO D  157                 -122.91                    
REMARK 500 TYR D  482     GLY D  483                  -39.14                    
REMARK 500 PHE D  684     SER D  685                 -148.12                    
REMARK 500 SER D  685     ALA D  686                 -142.45                    
REMARK 500 PRO E  156     PRO E  157                 -126.69                    
REMARK 500 SER E  685     ALA E  686                 -134.11                    
REMARK 500 PRO F  156     PRO F  157                 -132.58                    
REMARK 500 SER F  685     ALA F  686                 -131.61                    
REMARK 500 ARG G    2     VAL G    3                 -132.88                    
REMARK 500 ARG L    2     VAL L    3                 -146.49                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG G   2         0.25    SIDE CHAIN                              
REMARK 500    ARG H   2         0.29    SIDE CHAIN                              
REMARK 500    ARG I   2         0.12    SIDE CHAIN                              
REMARK 500    ARG J   2         0.15    SIDE CHAIN                              
REMARK 500    ARG K   2         0.27    SIDE CHAIN                              
REMARK 500    ARG L   2         0.29    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 ANTIPAIN: COVALENTLY BOUND TO THE CATALYTIC SER563                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN G OF ANTIPAIN               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN H OF ANTIPAIN               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN I OF ANTIPAIN               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN J OF ANTIPAIN               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN K OF ANTIPAIN               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN L OF ANTIPAIN               
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4BP8   RELATED DB: PDB                                   
REMARK 900 OLIGOPEPTIDASE B FROM TRYPANOSOMA BRUCEI - OPEN FORM                 
DBREF  4BP9 A    1   715  UNP    O76728   O76728_TRYBB     1    715             
DBREF  4BP9 B    1   715  UNP    O76728   O76728_TRYBB     1    715             
DBREF  4BP9 C    1   715  UNP    O76728   O76728_TRYBB     1    715             
DBREF  4BP9 D    1   715  UNP    O76728   O76728_TRYBB     1    715             
DBREF  4BP9 E    1   715  UNP    O76728   O76728_TRYBB     1    715             
DBREF  4BP9 F    1   715  UNP    O76728   O76728_TRYBB     1    715             
DBREF  4BP9 G    1     4  NOR    NOR00664 NOR00664         1      4             
DBREF  4BP9 H    1     4  NOR    NOR00664 NOR00664         1      4             
DBREF  4BP9 I    1     4  NOR    NOR00664 NOR00664         1      4             
DBREF  4BP9 J    1     4  NOR    NOR00664 NOR00664         1      4             
DBREF  4BP9 K    1     4  NOR    NOR00664 NOR00664         1      4             
DBREF  4BP9 L    1     4  NOR    NOR00664 NOR00664         1      4             
SEQADV 4BP9 OAR G    4  NOR  NOR00664  RGL     4 CONFLICT                       
SEQADV 4BP9 OAR H    4  NOR  NOR00664  RGL     4 CONFLICT                       
SEQADV 4BP9 OAR I    4  NOR  NOR00664  RGL     4 CONFLICT                       
SEQADV 4BP9 OAR J    4  NOR  NOR00664  RGL     4 CONFLICT                       
SEQADV 4BP9 OAR K    4  NOR  NOR00664  RGL     4 CONFLICT                       
SEQADV 4BP9 OAR L    4  NOR  NOR00664  RGL     4 CONFLICT                       
SEQRES   1 A  715  MET GLN THR GLU ARG GLY PRO ILE ALA ALA HIS ARG PRO          
SEQRES   2 A  715  HIS GLU VAL VAL PHE GLY LYS VAL GLU GLY GLU ASP ARG          
SEQRES   3 A  715  GLY ALA ASN PRO MET ASP PRO PRO ARG ARG ARG VAL ASP          
SEQRES   4 A  715  PRO LEU PHE TRP LEU ARG ASP ASP ASN ARG ALA ASP PRO          
SEQRES   5 A  715  GLU VAL LEU ALA HIS LEU HIS LEU GLU LYS ASP TYR TYR          
SEQRES   6 A  715  GLU LYS ARG ALA VAL ASP ILE LYS ASP LEU ALA GLU THR          
SEQRES   7 A  715  ILE TYR GLN GLU HIS ILE SER HIS ILE GLU GLU THR ASP          
SEQRES   8 A  715  MET SER ALA PRO TYR VAL TYR ASP ARG PHE LEU TYR TYR          
SEQRES   9 A  715  THR ARG ASP VAL LYS GLY LEU SER TYR LYS LEU HIS CYS          
SEQRES  10 A  715  ARG VAL PRO ALA GLY LYS THR PRO GLY GLU GLY GLU ASP          
SEQRES  11 A  715  GLU GLU ILE VAL LEU ASP GLU ASN LYS LEU ALA GLU GLY          
SEQRES  12 A  715  LYS SER PHE CYS VAL VAL GLY CYS VAL ALA PRO ALA PRO          
SEQRES  13 A  715  PRO GLU HIS ALA LEU VAL ALA TYR SER VAL ASP TYR CYS          
SEQRES  14 A  715  GLY ASP GLU VAL TYR SER ILE ARG PHE VAL ARG ASP VAL          
SEQRES  15 A  715  VAL ALA ASP LYS VAL GLU GLY THR ASN GLY SER VAL VAL          
SEQRES  16 A  715  TRP GLY PRO ASN ALA GLU CYS PHE PHE TYR ILE THR LYS          
SEQRES  17 A  715  ASP ALA SER LYS ARG ASP ASN LYS VAL TRP ARG HIS ILE          
SEQRES  18 A  715  ILE GLY GLN PRO GLN SER GLU ASP VAL CYS LEU TYR THR          
SEQRES  19 A  715  ASP ASP ASP PRO LEU PHE SER VAL GLY VAL GLY ARG SER          
SEQRES  20 A  715  GLY ASP GLY LYS THR LEU ILE ILE CYS SER MET SER SER          
SEQRES  21 A  715  GLU THR SER GLU SER HIS LEU LEU ASP LEU ARG LYS GLY          
SEQRES  22 A  715  VAL LYS HIS ASN THR LEU GLU MET VAL ARG PRO ARG GLU          
SEQRES  23 A  715  LYS GLY VAL ARG TYR THR VAL GLU MET HIS GLY THR ASP          
SEQRES  24 A  715  THR LEU ILE VAL LEU THR ASN LYS ASP LYS CYS VAL ASN          
SEQRES  25 A  715  GLY LYS VAL VAL LEU THR LYS ARG SER ALA PRO THR ASP          
SEQRES  26 A  715  TRP GLY THR VAL LEU ILE PRO HIS ASP ASP LYS VAL THR          
SEQRES  27 A  715  ILE ASP ASP VAL ALA VAL PHE ALA LYS PHE ALA VAL LEU          
SEQRES  28 A  715  SER GLY ARG ARG ASP GLY LEU THR ARG VAL TRP THR VAL          
SEQRES  29 A  715  ARG LEU GLY PRO ASP ASN LEU PHE SER SER ALA THR LEU          
SEQRES  30 A  715  LYS GLU LEU HIS PHE ASP GLU PRO VAL PHE THR ALA HIS          
SEQRES  31 A  715  VAL VAL CYS SER GLN MET LYS THR TYR ASP ALA SER LEU          
SEQRES  32 A  715  LEU ARG LEU ARG TYR SER SER MET THR THR PRO THR VAL          
SEQRES  33 A  715  TRP TYR ASP GLU ASP VAL LEU SER GLY GLU ARG LYS VAL          
SEQRES  34 A  715  VAL LYS ALA ARG LYS VAL GLY GLY GLY PHE GLU SER LYS          
SEQRES  35 A  715  ASN TYR VAL CYS ARG ARG GLU LEU ALA THR ALA PRO ASP          
SEQRES  36 A  715  GLY THR LYS VAL PRO ILE SER LEU VAL TYR ASP THR SER          
SEQRES  37 A  715  ILE ASP LEU LYS LYS PRO ASN PRO THR MET LEU TYR GLY          
SEQRES  38 A  715  TYR GLY SER TYR GLY ILE CYS ILE GLU PRO GLU PHE ASN          
SEQRES  39 A  715  SER ARG PHE LEU PRO TYR VAL ASP ARG GLY MET ILE TYR          
SEQRES  40 A  715  ALA ILE ALA HIS VAL ARG GLY GLY GLY GLU MET GLY ARG          
SEQRES  41 A  715  THR TRP TYR GLU VAL GLY GLY LYS TYR LEU THR LYS ARG          
SEQRES  42 A  715  ASN THR PHE MET ASP PHE ILE ALA CYS ALA GLU HIS LEU          
SEQRES  43 A  715  ILE SER SER GLY LEU THR THR PRO ALA GLN LEU SER CYS          
SEQRES  44 A  715  GLU GLY ARG SER ALA GLY GLY LEU LEU VAL GLY ALA VAL          
SEQRES  45 A  715  LEU ASN MET ARG PRO ASP LEU PHE HIS VAL ALA LEU ALA          
SEQRES  46 A  715  GLY VAL PRO PHE VAL ASP VAL MET THR THR MET CYS ASP          
SEQRES  47 A  715  PRO SER ILE PRO LEU THR THR GLY GLU TRP GLU GLU TRP          
SEQRES  48 A  715  GLY ASN PRO ASN GLU TYR LYS PHE PHE ASP TYR MET ASN          
SEQRES  49 A  715  SER TYR SER PRO ILE ASP ASN VAL ARG ALA GLN ASP TYR          
SEQRES  50 A  715  PRO HIS LEU MET ILE GLN ALA GLY LEU HIS ASP PRO ARG          
SEQRES  51 A  715  VAL ALA TYR TRP GLU PRO ALA LYS TRP ALA SER LYS LEU          
SEQRES  52 A  715  ARG GLU LEU LYS THR ASP SER ASN GLU VAL LEU LEU LYS          
SEQRES  53 A  715  MET ASP LEU GLU SER GLY HIS PHE SER ALA SER ASP ARG          
SEQRES  54 A  715  TYR LYS TYR LEU ARG GLU ASN ALA ILE GLN GLN ALA PHE          
SEQRES  55 A  715  VAL LEU LYS HIS LEU ASN VAL ARG GLN LEU LEU ARG LYS          
SEQRES   1 B  715  MET GLN THR GLU ARG GLY PRO ILE ALA ALA HIS ARG PRO          
SEQRES   2 B  715  HIS GLU VAL VAL PHE GLY LYS VAL GLU GLY GLU ASP ARG          
SEQRES   3 B  715  GLY ALA ASN PRO MET ASP PRO PRO ARG ARG ARG VAL ASP          
SEQRES   4 B  715  PRO LEU PHE TRP LEU ARG ASP ASP ASN ARG ALA ASP PRO          
SEQRES   5 B  715  GLU VAL LEU ALA HIS LEU HIS LEU GLU LYS ASP TYR TYR          
SEQRES   6 B  715  GLU LYS ARG ALA VAL ASP ILE LYS ASP LEU ALA GLU THR          
SEQRES   7 B  715  ILE TYR GLN GLU HIS ILE SER HIS ILE GLU GLU THR ASP          
SEQRES   8 B  715  MET SER ALA PRO TYR VAL TYR ASP ARG PHE LEU TYR TYR          
SEQRES   9 B  715  THR ARG ASP VAL LYS GLY LEU SER TYR LYS LEU HIS CYS          
SEQRES  10 B  715  ARG VAL PRO ALA GLY LYS THR PRO GLY GLU GLY GLU ASP          
SEQRES  11 B  715  GLU GLU ILE VAL LEU ASP GLU ASN LYS LEU ALA GLU GLY          
SEQRES  12 B  715  LYS SER PHE CYS VAL VAL GLY CYS VAL ALA PRO ALA PRO          
SEQRES  13 B  715  PRO GLU HIS ALA LEU VAL ALA TYR SER VAL ASP TYR CYS          
SEQRES  14 B  715  GLY ASP GLU VAL TYR SER ILE ARG PHE VAL ARG ASP VAL          
SEQRES  15 B  715  VAL ALA ASP LYS VAL GLU GLY THR ASN GLY SER VAL VAL          
SEQRES  16 B  715  TRP GLY PRO ASN ALA GLU CYS PHE PHE TYR ILE THR LYS          
SEQRES  17 B  715  ASP ALA SER LYS ARG ASP ASN LYS VAL TRP ARG HIS ILE          
SEQRES  18 B  715  ILE GLY GLN PRO GLN SER GLU ASP VAL CYS LEU TYR THR          
SEQRES  19 B  715  ASP ASP ASP PRO LEU PHE SER VAL GLY VAL GLY ARG SER          
SEQRES  20 B  715  GLY ASP GLY LYS THR LEU ILE ILE CYS SER MET SER SER          
SEQRES  21 B  715  GLU THR SER GLU SER HIS LEU LEU ASP LEU ARG LYS GLY          
SEQRES  22 B  715  VAL LYS HIS ASN THR LEU GLU MET VAL ARG PRO ARG GLU          
SEQRES  23 B  715  LYS GLY VAL ARG TYR THR VAL GLU MET HIS GLY THR ASP          
SEQRES  24 B  715  THR LEU ILE VAL LEU THR ASN LYS ASP LYS CYS VAL ASN          
SEQRES  25 B  715  GLY LYS VAL VAL LEU THR LYS ARG SER ALA PRO THR ASP          
SEQRES  26 B  715  TRP GLY THR VAL LEU ILE PRO HIS ASP ASP LYS VAL THR          
SEQRES  27 B  715  ILE ASP ASP VAL ALA VAL PHE ALA LYS PHE ALA VAL LEU          
SEQRES  28 B  715  SER GLY ARG ARG ASP GLY LEU THR ARG VAL TRP THR VAL          
SEQRES  29 B  715  ARG LEU GLY PRO ASP ASN LEU PHE SER SER ALA THR LEU          
SEQRES  30 B  715  LYS GLU LEU HIS PHE ASP GLU PRO VAL PHE THR ALA HIS          
SEQRES  31 B  715  VAL VAL CYS SER GLN MET LYS THR TYR ASP ALA SER LEU          
SEQRES  32 B  715  LEU ARG LEU ARG TYR SER SER MET THR THR PRO THR VAL          
SEQRES  33 B  715  TRP TYR ASP GLU ASP VAL LEU SER GLY GLU ARG LYS VAL          
SEQRES  34 B  715  VAL LYS ALA ARG LYS VAL GLY GLY GLY PHE GLU SER LYS          
SEQRES  35 B  715  ASN TYR VAL CYS ARG ARG GLU LEU ALA THR ALA PRO ASP          
SEQRES  36 B  715  GLY THR LYS VAL PRO ILE SER LEU VAL TYR ASP THR SER          
SEQRES  37 B  715  ILE ASP LEU LYS LYS PRO ASN PRO THR MET LEU TYR GLY          
SEQRES  38 B  715  TYR GLY SER TYR GLY ILE CYS ILE GLU PRO GLU PHE ASN          
SEQRES  39 B  715  SER ARG PHE LEU PRO TYR VAL ASP ARG GLY MET ILE TYR          
SEQRES  40 B  715  ALA ILE ALA HIS VAL ARG GLY GLY GLY GLU MET GLY ARG          
SEQRES  41 B  715  THR TRP TYR GLU VAL GLY GLY LYS TYR LEU THR LYS ARG          
SEQRES  42 B  715  ASN THR PHE MET ASP PHE ILE ALA CYS ALA GLU HIS LEU          
SEQRES  43 B  715  ILE SER SER GLY LEU THR THR PRO ALA GLN LEU SER CYS          
SEQRES  44 B  715  GLU GLY ARG SER ALA GLY GLY LEU LEU VAL GLY ALA VAL          
SEQRES  45 B  715  LEU ASN MET ARG PRO ASP LEU PHE HIS VAL ALA LEU ALA          
SEQRES  46 B  715  GLY VAL PRO PHE VAL ASP VAL MET THR THR MET CYS ASP          
SEQRES  47 B  715  PRO SER ILE PRO LEU THR THR GLY GLU TRP GLU GLU TRP          
SEQRES  48 B  715  GLY ASN PRO ASN GLU TYR LYS PHE PHE ASP TYR MET ASN          
SEQRES  49 B  715  SER TYR SER PRO ILE ASP ASN VAL ARG ALA GLN ASP TYR          
SEQRES  50 B  715  PRO HIS LEU MET ILE GLN ALA GLY LEU HIS ASP PRO ARG          
SEQRES  51 B  715  VAL ALA TYR TRP GLU PRO ALA LYS TRP ALA SER LYS LEU          
SEQRES  52 B  715  ARG GLU LEU LYS THR ASP SER ASN GLU VAL LEU LEU LYS          
SEQRES  53 B  715  MET ASP LEU GLU SER GLY HIS PHE SER ALA SER ASP ARG          
SEQRES  54 B  715  TYR LYS TYR LEU ARG GLU ASN ALA ILE GLN GLN ALA PHE          
SEQRES  55 B  715  VAL LEU LYS HIS LEU ASN VAL ARG GLN LEU LEU ARG LYS          
SEQRES   1 C  715  MET GLN THR GLU ARG GLY PRO ILE ALA ALA HIS ARG PRO          
SEQRES   2 C  715  HIS GLU VAL VAL PHE GLY LYS VAL GLU GLY GLU ASP ARG          
SEQRES   3 C  715  GLY ALA ASN PRO MET ASP PRO PRO ARG ARG ARG VAL ASP          
SEQRES   4 C  715  PRO LEU PHE TRP LEU ARG ASP ASP ASN ARG ALA ASP PRO          
SEQRES   5 C  715  GLU VAL LEU ALA HIS LEU HIS LEU GLU LYS ASP TYR TYR          
SEQRES   6 C  715  GLU LYS ARG ALA VAL ASP ILE LYS ASP LEU ALA GLU THR          
SEQRES   7 C  715  ILE TYR GLN GLU HIS ILE SER HIS ILE GLU GLU THR ASP          
SEQRES   8 C  715  MET SER ALA PRO TYR VAL TYR ASP ARG PHE LEU TYR TYR          
SEQRES   9 C  715  THR ARG ASP VAL LYS GLY LEU SER TYR LYS LEU HIS CYS          
SEQRES  10 C  715  ARG VAL PRO ALA GLY LYS THR PRO GLY GLU GLY GLU ASP          
SEQRES  11 C  715  GLU GLU ILE VAL LEU ASP GLU ASN LYS LEU ALA GLU GLY          
SEQRES  12 C  715  LYS SER PHE CYS VAL VAL GLY CYS VAL ALA PRO ALA PRO          
SEQRES  13 C  715  PRO GLU HIS ALA LEU VAL ALA TYR SER VAL ASP TYR CYS          
SEQRES  14 C  715  GLY ASP GLU VAL TYR SER ILE ARG PHE VAL ARG ASP VAL          
SEQRES  15 C  715  VAL ALA ASP LYS VAL GLU GLY THR ASN GLY SER VAL VAL          
SEQRES  16 C  715  TRP GLY PRO ASN ALA GLU CYS PHE PHE TYR ILE THR LYS          
SEQRES  17 C  715  ASP ALA SER LYS ARG ASP ASN LYS VAL TRP ARG HIS ILE          
SEQRES  18 C  715  ILE GLY GLN PRO GLN SER GLU ASP VAL CYS LEU TYR THR          
SEQRES  19 C  715  ASP ASP ASP PRO LEU PHE SER VAL GLY VAL GLY ARG SER          
SEQRES  20 C  715  GLY ASP GLY LYS THR LEU ILE ILE CYS SER MET SER SER          
SEQRES  21 C  715  GLU THR SER GLU SER HIS LEU LEU ASP LEU ARG LYS GLY          
SEQRES  22 C  715  VAL LYS HIS ASN THR LEU GLU MET VAL ARG PRO ARG GLU          
SEQRES  23 C  715  LYS GLY VAL ARG TYR THR VAL GLU MET HIS GLY THR ASP          
SEQRES  24 C  715  THR LEU ILE VAL LEU THR ASN LYS ASP LYS CYS VAL ASN          
SEQRES  25 C  715  GLY LYS VAL VAL LEU THR LYS ARG SER ALA PRO THR ASP          
SEQRES  26 C  715  TRP GLY THR VAL LEU ILE PRO HIS ASP ASP LYS VAL THR          
SEQRES  27 C  715  ILE ASP ASP VAL ALA VAL PHE ALA LYS PHE ALA VAL LEU          
SEQRES  28 C  715  SER GLY ARG ARG ASP GLY LEU THR ARG VAL TRP THR VAL          
SEQRES  29 C  715  ARG LEU GLY PRO ASP ASN LEU PHE SER SER ALA THR LEU          
SEQRES  30 C  715  LYS GLU LEU HIS PHE ASP GLU PRO VAL PHE THR ALA HIS          
SEQRES  31 C  715  VAL VAL CYS SER GLN MET LYS THR TYR ASP ALA SER LEU          
SEQRES  32 C  715  LEU ARG LEU ARG TYR SER SER MET THR THR PRO THR VAL          
SEQRES  33 C  715  TRP TYR ASP GLU ASP VAL LEU SER GLY GLU ARG LYS VAL          
SEQRES  34 C  715  VAL LYS ALA ARG LYS VAL GLY GLY GLY PHE GLU SER LYS          
SEQRES  35 C  715  ASN TYR VAL CYS ARG ARG GLU LEU ALA THR ALA PRO ASP          
SEQRES  36 C  715  GLY THR LYS VAL PRO ILE SER LEU VAL TYR ASP THR SER          
SEQRES  37 C  715  ILE ASP LEU LYS LYS PRO ASN PRO THR MET LEU TYR GLY          
SEQRES  38 C  715  TYR GLY SER TYR GLY ILE CYS ILE GLU PRO GLU PHE ASN          
SEQRES  39 C  715  SER ARG PHE LEU PRO TYR VAL ASP ARG GLY MET ILE TYR          
SEQRES  40 C  715  ALA ILE ALA HIS VAL ARG GLY GLY GLY GLU MET GLY ARG          
SEQRES  41 C  715  THR TRP TYR GLU VAL GLY GLY LYS TYR LEU THR LYS ARG          
SEQRES  42 C  715  ASN THR PHE MET ASP PHE ILE ALA CYS ALA GLU HIS LEU          
SEQRES  43 C  715  ILE SER SER GLY LEU THR THR PRO ALA GLN LEU SER CYS          
SEQRES  44 C  715  GLU GLY ARG SER ALA GLY GLY LEU LEU VAL GLY ALA VAL          
SEQRES  45 C  715  LEU ASN MET ARG PRO ASP LEU PHE HIS VAL ALA LEU ALA          
SEQRES  46 C  715  GLY VAL PRO PHE VAL ASP VAL MET THR THR MET CYS ASP          
SEQRES  47 C  715  PRO SER ILE PRO LEU THR THR GLY GLU TRP GLU GLU TRP          
SEQRES  48 C  715  GLY ASN PRO ASN GLU TYR LYS PHE PHE ASP TYR MET ASN          
SEQRES  49 C  715  SER TYR SER PRO ILE ASP ASN VAL ARG ALA GLN ASP TYR          
SEQRES  50 C  715  PRO HIS LEU MET ILE GLN ALA GLY LEU HIS ASP PRO ARG          
SEQRES  51 C  715  VAL ALA TYR TRP GLU PRO ALA LYS TRP ALA SER LYS LEU          
SEQRES  52 C  715  ARG GLU LEU LYS THR ASP SER ASN GLU VAL LEU LEU LYS          
SEQRES  53 C  715  MET ASP LEU GLU SER GLY HIS PHE SER ALA SER ASP ARG          
SEQRES  54 C  715  TYR LYS TYR LEU ARG GLU ASN ALA ILE GLN GLN ALA PHE          
SEQRES  55 C  715  VAL LEU LYS HIS LEU ASN VAL ARG GLN LEU LEU ARG LYS          
SEQRES   1 D  715  MET GLN THR GLU ARG GLY PRO ILE ALA ALA HIS ARG PRO          
SEQRES   2 D  715  HIS GLU VAL VAL PHE GLY LYS VAL GLU GLY GLU ASP ARG          
SEQRES   3 D  715  GLY ALA ASN PRO MET ASP PRO PRO ARG ARG ARG VAL ASP          
SEQRES   4 D  715  PRO LEU PHE TRP LEU ARG ASP ASP ASN ARG ALA ASP PRO          
SEQRES   5 D  715  GLU VAL LEU ALA HIS LEU HIS LEU GLU LYS ASP TYR TYR          
SEQRES   6 D  715  GLU LYS ARG ALA VAL ASP ILE LYS ASP LEU ALA GLU THR          
SEQRES   7 D  715  ILE TYR GLN GLU HIS ILE SER HIS ILE GLU GLU THR ASP          
SEQRES   8 D  715  MET SER ALA PRO TYR VAL TYR ASP ARG PHE LEU TYR TYR          
SEQRES   9 D  715  THR ARG ASP VAL LYS GLY LEU SER TYR LYS LEU HIS CYS          
SEQRES  10 D  715  ARG VAL PRO ALA GLY LYS THR PRO GLY GLU GLY GLU ASP          
SEQRES  11 D  715  GLU GLU ILE VAL LEU ASP GLU ASN LYS LEU ALA GLU GLY          
SEQRES  12 D  715  LYS SER PHE CYS VAL VAL GLY CYS VAL ALA PRO ALA PRO          
SEQRES  13 D  715  PRO GLU HIS ALA LEU VAL ALA TYR SER VAL ASP TYR CYS          
SEQRES  14 D  715  GLY ASP GLU VAL TYR SER ILE ARG PHE VAL ARG ASP VAL          
SEQRES  15 D  715  VAL ALA ASP LYS VAL GLU GLY THR ASN GLY SER VAL VAL          
SEQRES  16 D  715  TRP GLY PRO ASN ALA GLU CYS PHE PHE TYR ILE THR LYS          
SEQRES  17 D  715  ASP ALA SER LYS ARG ASP ASN LYS VAL TRP ARG HIS ILE          
SEQRES  18 D  715  ILE GLY GLN PRO GLN SER GLU ASP VAL CYS LEU TYR THR          
SEQRES  19 D  715  ASP ASP ASP PRO LEU PHE SER VAL GLY VAL GLY ARG SER          
SEQRES  20 D  715  GLY ASP GLY LYS THR LEU ILE ILE CYS SER MET SER SER          
SEQRES  21 D  715  GLU THR SER GLU SER HIS LEU LEU ASP LEU ARG LYS GLY          
SEQRES  22 D  715  VAL LYS HIS ASN THR LEU GLU MET VAL ARG PRO ARG GLU          
SEQRES  23 D  715  LYS GLY VAL ARG TYR THR VAL GLU MET HIS GLY THR ASP          
SEQRES  24 D  715  THR LEU ILE VAL LEU THR ASN LYS ASP LYS CYS VAL ASN          
SEQRES  25 D  715  GLY LYS VAL VAL LEU THR LYS ARG SER ALA PRO THR ASP          
SEQRES  26 D  715  TRP GLY THR VAL LEU ILE PRO HIS ASP ASP LYS VAL THR          
SEQRES  27 D  715  ILE ASP ASP VAL ALA VAL PHE ALA LYS PHE ALA VAL LEU          
SEQRES  28 D  715  SER GLY ARG ARG ASP GLY LEU THR ARG VAL TRP THR VAL          
SEQRES  29 D  715  ARG LEU GLY PRO ASP ASN LEU PHE SER SER ALA THR LEU          
SEQRES  30 D  715  LYS GLU LEU HIS PHE ASP GLU PRO VAL PHE THR ALA HIS          
SEQRES  31 D  715  VAL VAL CYS SER GLN MET LYS THR TYR ASP ALA SER LEU          
SEQRES  32 D  715  LEU ARG LEU ARG TYR SER SER MET THR THR PRO THR VAL          
SEQRES  33 D  715  TRP TYR ASP GLU ASP VAL LEU SER GLY GLU ARG LYS VAL          
SEQRES  34 D  715  VAL LYS ALA ARG LYS VAL GLY GLY GLY PHE GLU SER LYS          
SEQRES  35 D  715  ASN TYR VAL CYS ARG ARG GLU LEU ALA THR ALA PRO ASP          
SEQRES  36 D  715  GLY THR LYS VAL PRO ILE SER LEU VAL TYR ASP THR SER          
SEQRES  37 D  715  ILE ASP LEU LYS LYS PRO ASN PRO THR MET LEU TYR GLY          
SEQRES  38 D  715  TYR GLY SER TYR GLY ILE CYS ILE GLU PRO GLU PHE ASN          
SEQRES  39 D  715  SER ARG PHE LEU PRO TYR VAL ASP ARG GLY MET ILE TYR          
SEQRES  40 D  715  ALA ILE ALA HIS VAL ARG GLY GLY GLY GLU MET GLY ARG          
SEQRES  41 D  715  THR TRP TYR GLU VAL GLY GLY LYS TYR LEU THR LYS ARG          
SEQRES  42 D  715  ASN THR PHE MET ASP PHE ILE ALA CYS ALA GLU HIS LEU          
SEQRES  43 D  715  ILE SER SER GLY LEU THR THR PRO ALA GLN LEU SER CYS          
SEQRES  44 D  715  GLU GLY ARG SER ALA GLY GLY LEU LEU VAL GLY ALA VAL          
SEQRES  45 D  715  LEU ASN MET ARG PRO ASP LEU PHE HIS VAL ALA LEU ALA          
SEQRES  46 D  715  GLY VAL PRO PHE VAL ASP VAL MET THR THR MET CYS ASP          
SEQRES  47 D  715  PRO SER ILE PRO LEU THR THR GLY GLU TRP GLU GLU TRP          
SEQRES  48 D  715  GLY ASN PRO ASN GLU TYR LYS PHE PHE ASP TYR MET ASN          
SEQRES  49 D  715  SER TYR SER PRO ILE ASP ASN VAL ARG ALA GLN ASP TYR          
SEQRES  50 D  715  PRO HIS LEU MET ILE GLN ALA GLY LEU HIS ASP PRO ARG          
SEQRES  51 D  715  VAL ALA TYR TRP GLU PRO ALA LYS TRP ALA SER LYS LEU          
SEQRES  52 D  715  ARG GLU LEU LYS THR ASP SER ASN GLU VAL LEU LEU LYS          
SEQRES  53 D  715  MET ASP LEU GLU SER GLY HIS PHE SER ALA SER ASP ARG          
SEQRES  54 D  715  TYR LYS TYR LEU ARG GLU ASN ALA ILE GLN GLN ALA PHE          
SEQRES  55 D  715  VAL LEU LYS HIS LEU ASN VAL ARG GLN LEU LEU ARG LYS          
SEQRES   1 E  715  MET GLN THR GLU ARG GLY PRO ILE ALA ALA HIS ARG PRO          
SEQRES   2 E  715  HIS GLU VAL VAL PHE GLY LYS VAL GLU GLY GLU ASP ARG          
SEQRES   3 E  715  GLY ALA ASN PRO MET ASP PRO PRO ARG ARG ARG VAL ASP          
SEQRES   4 E  715  PRO LEU PHE TRP LEU ARG ASP ASP ASN ARG ALA ASP PRO          
SEQRES   5 E  715  GLU VAL LEU ALA HIS LEU HIS LEU GLU LYS ASP TYR TYR          
SEQRES   6 E  715  GLU LYS ARG ALA VAL ASP ILE LYS ASP LEU ALA GLU THR          
SEQRES   7 E  715  ILE TYR GLN GLU HIS ILE SER HIS ILE GLU GLU THR ASP          
SEQRES   8 E  715  MET SER ALA PRO TYR VAL TYR ASP ARG PHE LEU TYR TYR          
SEQRES   9 E  715  THR ARG ASP VAL LYS GLY LEU SER TYR LYS LEU HIS CYS          
SEQRES  10 E  715  ARG VAL PRO ALA GLY LYS THR PRO GLY GLU GLY GLU ASP          
SEQRES  11 E  715  GLU GLU ILE VAL LEU ASP GLU ASN LYS LEU ALA GLU GLY          
SEQRES  12 E  715  LYS SER PHE CYS VAL VAL GLY CYS VAL ALA PRO ALA PRO          
SEQRES  13 E  715  PRO GLU HIS ALA LEU VAL ALA TYR SER VAL ASP TYR CYS          
SEQRES  14 E  715  GLY ASP GLU VAL TYR SER ILE ARG PHE VAL ARG ASP VAL          
SEQRES  15 E  715  VAL ALA ASP LYS VAL GLU GLY THR ASN GLY SER VAL VAL          
SEQRES  16 E  715  TRP GLY PRO ASN ALA GLU CYS PHE PHE TYR ILE THR LYS          
SEQRES  17 E  715  ASP ALA SER LYS ARG ASP ASN LYS VAL TRP ARG HIS ILE          
SEQRES  18 E  715  ILE GLY GLN PRO GLN SER GLU ASP VAL CYS LEU TYR THR          
SEQRES  19 E  715  ASP ASP ASP PRO LEU PHE SER VAL GLY VAL GLY ARG SER          
SEQRES  20 E  715  GLY ASP GLY LYS THR LEU ILE ILE CYS SER MET SER SER          
SEQRES  21 E  715  GLU THR SER GLU SER HIS LEU LEU ASP LEU ARG LYS GLY          
SEQRES  22 E  715  VAL LYS HIS ASN THR LEU GLU MET VAL ARG PRO ARG GLU          
SEQRES  23 E  715  LYS GLY VAL ARG TYR THR VAL GLU MET HIS GLY THR ASP          
SEQRES  24 E  715  THR LEU ILE VAL LEU THR ASN LYS ASP LYS CYS VAL ASN          
SEQRES  25 E  715  GLY LYS VAL VAL LEU THR LYS ARG SER ALA PRO THR ASP          
SEQRES  26 E  715  TRP GLY THR VAL LEU ILE PRO HIS ASP ASP LYS VAL THR          
SEQRES  27 E  715  ILE ASP ASP VAL ALA VAL PHE ALA LYS PHE ALA VAL LEU          
SEQRES  28 E  715  SER GLY ARG ARG ASP GLY LEU THR ARG VAL TRP THR VAL          
SEQRES  29 E  715  ARG LEU GLY PRO ASP ASN LEU PHE SER SER ALA THR LEU          
SEQRES  30 E  715  LYS GLU LEU HIS PHE ASP GLU PRO VAL PHE THR ALA HIS          
SEQRES  31 E  715  VAL VAL CYS SER GLN MET LYS THR TYR ASP ALA SER LEU          
SEQRES  32 E  715  LEU ARG LEU ARG TYR SER SER MET THR THR PRO THR VAL          
SEQRES  33 E  715  TRP TYR ASP GLU ASP VAL LEU SER GLY GLU ARG LYS VAL          
SEQRES  34 E  715  VAL LYS ALA ARG LYS VAL GLY GLY GLY PHE GLU SER LYS          
SEQRES  35 E  715  ASN TYR VAL CYS ARG ARG GLU LEU ALA THR ALA PRO ASP          
SEQRES  36 E  715  GLY THR LYS VAL PRO ILE SER LEU VAL TYR ASP THR SER          
SEQRES  37 E  715  ILE ASP LEU LYS LYS PRO ASN PRO THR MET LEU TYR GLY          
SEQRES  38 E  715  TYR GLY SER TYR GLY ILE CYS ILE GLU PRO GLU PHE ASN          
SEQRES  39 E  715  SER ARG PHE LEU PRO TYR VAL ASP ARG GLY MET ILE TYR          
SEQRES  40 E  715  ALA ILE ALA HIS VAL ARG GLY GLY GLY GLU MET GLY ARG          
SEQRES  41 E  715  THR TRP TYR GLU VAL GLY GLY LYS TYR LEU THR LYS ARG          
SEQRES  42 E  715  ASN THR PHE MET ASP PHE ILE ALA CYS ALA GLU HIS LEU          
SEQRES  43 E  715  ILE SER SER GLY LEU THR THR PRO ALA GLN LEU SER CYS          
SEQRES  44 E  715  GLU GLY ARG SER ALA GLY GLY LEU LEU VAL GLY ALA VAL          
SEQRES  45 E  715  LEU ASN MET ARG PRO ASP LEU PHE HIS VAL ALA LEU ALA          
SEQRES  46 E  715  GLY VAL PRO PHE VAL ASP VAL MET THR THR MET CYS ASP          
SEQRES  47 E  715  PRO SER ILE PRO LEU THR THR GLY GLU TRP GLU GLU TRP          
SEQRES  48 E  715  GLY ASN PRO ASN GLU TYR LYS PHE PHE ASP TYR MET ASN          
SEQRES  49 E  715  SER TYR SER PRO ILE ASP ASN VAL ARG ALA GLN ASP TYR          
SEQRES  50 E  715  PRO HIS LEU MET ILE GLN ALA GLY LEU HIS ASP PRO ARG          
SEQRES  51 E  715  VAL ALA TYR TRP GLU PRO ALA LYS TRP ALA SER LYS LEU          
SEQRES  52 E  715  ARG GLU LEU LYS THR ASP SER ASN GLU VAL LEU LEU LYS          
SEQRES  53 E  715  MET ASP LEU GLU SER GLY HIS PHE SER ALA SER ASP ARG          
SEQRES  54 E  715  TYR LYS TYR LEU ARG GLU ASN ALA ILE GLN GLN ALA PHE          
SEQRES  55 E  715  VAL LEU LYS HIS LEU ASN VAL ARG GLN LEU LEU ARG LYS          
SEQRES   1 F  715  MET GLN THR GLU ARG GLY PRO ILE ALA ALA HIS ARG PRO          
SEQRES   2 F  715  HIS GLU VAL VAL PHE GLY LYS VAL GLU GLY GLU ASP ARG          
SEQRES   3 F  715  GLY ALA ASN PRO MET ASP PRO PRO ARG ARG ARG VAL ASP          
SEQRES   4 F  715  PRO LEU PHE TRP LEU ARG ASP ASP ASN ARG ALA ASP PRO          
SEQRES   5 F  715  GLU VAL LEU ALA HIS LEU HIS LEU GLU LYS ASP TYR TYR          
SEQRES   6 F  715  GLU LYS ARG ALA VAL ASP ILE LYS ASP LEU ALA GLU THR          
SEQRES   7 F  715  ILE TYR GLN GLU HIS ILE SER HIS ILE GLU GLU THR ASP          
SEQRES   8 F  715  MET SER ALA PRO TYR VAL TYR ASP ARG PHE LEU TYR TYR          
SEQRES   9 F  715  THR ARG ASP VAL LYS GLY LEU SER TYR LYS LEU HIS CYS          
SEQRES  10 F  715  ARG VAL PRO ALA GLY LYS THR PRO GLY GLU GLY GLU ASP          
SEQRES  11 F  715  GLU GLU ILE VAL LEU ASP GLU ASN LYS LEU ALA GLU GLY          
SEQRES  12 F  715  LYS SER PHE CYS VAL VAL GLY CYS VAL ALA PRO ALA PRO          
SEQRES  13 F  715  PRO GLU HIS ALA LEU VAL ALA TYR SER VAL ASP TYR CYS          
SEQRES  14 F  715  GLY ASP GLU VAL TYR SER ILE ARG PHE VAL ARG ASP VAL          
SEQRES  15 F  715  VAL ALA ASP LYS VAL GLU GLY THR ASN GLY SER VAL VAL          
SEQRES  16 F  715  TRP GLY PRO ASN ALA GLU CYS PHE PHE TYR ILE THR LYS          
SEQRES  17 F  715  ASP ALA SER LYS ARG ASP ASN LYS VAL TRP ARG HIS ILE          
SEQRES  18 F  715  ILE GLY GLN PRO GLN SER GLU ASP VAL CYS LEU TYR THR          
SEQRES  19 F  715  ASP ASP ASP PRO LEU PHE SER VAL GLY VAL GLY ARG SER          
SEQRES  20 F  715  GLY ASP GLY LYS THR LEU ILE ILE CYS SER MET SER SER          
SEQRES  21 F  715  GLU THR SER GLU SER HIS LEU LEU ASP LEU ARG LYS GLY          
SEQRES  22 F  715  VAL LYS HIS ASN THR LEU GLU MET VAL ARG PRO ARG GLU          
SEQRES  23 F  715  LYS GLY VAL ARG TYR THR VAL GLU MET HIS GLY THR ASP          
SEQRES  24 F  715  THR LEU ILE VAL LEU THR ASN LYS ASP LYS CYS VAL ASN          
SEQRES  25 F  715  GLY LYS VAL VAL LEU THR LYS ARG SER ALA PRO THR ASP          
SEQRES  26 F  715  TRP GLY THR VAL LEU ILE PRO HIS ASP ASP LYS VAL THR          
SEQRES  27 F  715  ILE ASP ASP VAL ALA VAL PHE ALA LYS PHE ALA VAL LEU          
SEQRES  28 F  715  SER GLY ARG ARG ASP GLY LEU THR ARG VAL TRP THR VAL          
SEQRES  29 F  715  ARG LEU GLY PRO ASP ASN LEU PHE SER SER ALA THR LEU          
SEQRES  30 F  715  LYS GLU LEU HIS PHE ASP GLU PRO VAL PHE THR ALA HIS          
SEQRES  31 F  715  VAL VAL CYS SER GLN MET LYS THR TYR ASP ALA SER LEU          
SEQRES  32 F  715  LEU ARG LEU ARG TYR SER SER MET THR THR PRO THR VAL          
SEQRES  33 F  715  TRP TYR ASP GLU ASP VAL LEU SER GLY GLU ARG LYS VAL          
SEQRES  34 F  715  VAL LYS ALA ARG LYS VAL GLY GLY GLY PHE GLU SER LYS          
SEQRES  35 F  715  ASN TYR VAL CYS ARG ARG GLU LEU ALA THR ALA PRO ASP          
SEQRES  36 F  715  GLY THR LYS VAL PRO ILE SER LEU VAL TYR ASP THR SER          
SEQRES  37 F  715  ILE ASP LEU LYS LYS PRO ASN PRO THR MET LEU TYR GLY          
SEQRES  38 F  715  TYR GLY SER TYR GLY ILE CYS ILE GLU PRO GLU PHE ASN          
SEQRES  39 F  715  SER ARG PHE LEU PRO TYR VAL ASP ARG GLY MET ILE TYR          
SEQRES  40 F  715  ALA ILE ALA HIS VAL ARG GLY GLY GLY GLU MET GLY ARG          
SEQRES  41 F  715  THR TRP TYR GLU VAL GLY GLY LYS TYR LEU THR LYS ARG          
SEQRES  42 F  715  ASN THR PHE MET ASP PHE ILE ALA CYS ALA GLU HIS LEU          
SEQRES  43 F  715  ILE SER SER GLY LEU THR THR PRO ALA GLN LEU SER CYS          
SEQRES  44 F  715  GLU GLY ARG SER ALA GLY GLY LEU LEU VAL GLY ALA VAL          
SEQRES  45 F  715  LEU ASN MET ARG PRO ASP LEU PHE HIS VAL ALA LEU ALA          
SEQRES  46 F  715  GLY VAL PRO PHE VAL ASP VAL MET THR THR MET CYS ASP          
SEQRES  47 F  715  PRO SER ILE PRO LEU THR THR GLY GLU TRP GLU GLU TRP          
SEQRES  48 F  715  GLY ASN PRO ASN GLU TYR LYS PHE PHE ASP TYR MET ASN          
SEQRES  49 F  715  SER TYR SER PRO ILE ASP ASN VAL ARG ALA GLN ASP TYR          
SEQRES  50 F  715  PRO HIS LEU MET ILE GLN ALA GLY LEU HIS ASP PRO ARG          
SEQRES  51 F  715  VAL ALA TYR TRP GLU PRO ALA LYS TRP ALA SER LYS LEU          
SEQRES  52 F  715  ARG GLU LEU LYS THR ASP SER ASN GLU VAL LEU LEU LYS          
SEQRES  53 F  715  MET ASP LEU GLU SER GLY HIS PHE SER ALA SER ASP ARG          
SEQRES  54 F  715  TYR LYS TYR LEU ARG GLU ASN ALA ILE GLN GLN ALA PHE          
SEQRES  55 F  715  VAL LEU LYS HIS LEU ASN VAL ARG GLN LEU LEU ARG LYS          
SEQRES   1 G    4  FC0 ARG VAL OAR                                              
SEQRES   1 H    4  FC0 ARG VAL OAR                                              
SEQRES   1 I    4  FC0 ARG VAL OAR                                              
SEQRES   1 J    4  FC0 ARG VAL OAR                                              
SEQRES   1 K    4  FC0 ARG VAL OAR                                              
SEQRES   1 L    4  FC0 ARG VAL OAR                                              
MODRES 4BP9 FC0 G    1  PHE  N-CARBOXY-L-PHENYLALANINE                          
MODRES 4BP9 OAR G    4  ARG  N-(4-AMINO-5-HYDROXY-PENTYL)-GUANIDINE             
MODRES 4BP9 FC0 H    1  PHE  N-CARBOXY-L-PHENYLALANINE                          
MODRES 4BP9 OAR H    4  ARG  N-(4-AMINO-5-HYDROXY-PENTYL)-GUANIDINE             
MODRES 4BP9 FC0 I    1  PHE  N-CARBOXY-L-PHENYLALANINE                          
MODRES 4BP9 OAR I    4  ARG  N-(4-AMINO-5-HYDROXY-PENTYL)-GUANIDINE             
MODRES 4BP9 FC0 J    1  PHE  N-CARBOXY-L-PHENYLALANINE                          
MODRES 4BP9 OAR J    4  ARG  N-(4-AMINO-5-HYDROXY-PENTYL)-GUANIDINE             
MODRES 4BP9 FC0 K    1  PHE  N-CARBOXY-L-PHENYLALANINE                          
MODRES 4BP9 OAR K    4  ARG  N-(4-AMINO-5-HYDROXY-PENTYL)-GUANIDINE             
MODRES 4BP9 FC0 L    1  PHE  N-CARBOXY-L-PHENYLALANINE                          
MODRES 4BP9 OAR L    4  ARG  N-(4-AMINO-5-HYDROXY-PENTYL)-GUANIDINE             
HET    FC0  G   1      14                                                       
HET    OAR  G   4      11                                                       
HET    FC0  H   1      14                                                       
HET    OAR  H   4      11                                                       
HET    FC0  I   1      14                                                       
HET    OAR  I   4      11                                                       
HET    FC0  J   1      14                                                       
HET    OAR  J   4      11                                                       
HET    FC0  K   1      14                                                       
HET    OAR  K   4      11                                                       
HET    FC0  L   1      14                                                       
HET    OAR  L   4      11                                                       
HETNAM     FC0 N-CARBOXY-L-PHENYLALANINE                                        
HETNAM     OAR N-(4-AMINO-5-HYDROXY-PENTYL)-GUANIDINE                           
FORMUL   7  FC0    6(C10 H11 N O4)                                              
FORMUL   7  OAR    6(C6 H16 N4 O)                                               
FORMUL  13  HOH   *344(H2 O)                                                    
HELIX    1   1 LEU A   41  ARG A   45  5                                   5    
HELIX    2   2 ASP A   51  ALA A   69  1                                  19    
HELIX    3   3 ILE A   72  HIS A   86  1                                  15    
HELIX    4   4 GLU A  137  GLU A  142  1                                   6    
HELIX    5   5 ARG A  180  VAL A  182  5                                   3    
HELIX    6   6 PRO A  198  ALA A  200  5                                   3    
HELIX    7   7 ASP A  209  ARG A  213  5                                   5    
HELIX    8   8 PRO A  225  ASP A  229  5                                   5    
HELIX    9   9 ARG A  271  GLY A  273  5                                   3    
HELIX   10  10 SER A  373  LEU A  377  5                                   5    
HELIX   11  11 CYS A  393  MET A  396  5                                   4    
HELIX   12  12 GLU A  440  LYS A  442  5                                   3    
HELIX   13  13 ASN A  494  ARG A  496  5                                   3    
HELIX   14  14 PHE A  497  ASP A  502  1                                   6    
HELIX   15  15 ARG A  520  VAL A  525  1                                   6    
HELIX   16  16 LYS A  528  THR A  531  5                                   4    
HELIX   17  17 LYS A  532  SER A  549  1                                  18    
HELIX   18  18 THR A  553  ALA A  555  5                                   3    
HELIX   19  19 SER A  563  ARG A  576  1                                  14    
HELIX   20  20 PRO A  577  PHE A  580  5                                   4    
HELIX   21  21 ASP A  591  ASP A  598  1                                   8    
HELIX   22  22 THR A  605  GLU A  610  5                                   6    
HELIX   23  23 PHE A  619  SER A  625  1                                   7    
HELIX   24  24 SER A  627  VAL A  632  1                                   6    
HELIX   25  25 TYR A  653  LYS A  667  1                                  15    
HELIX   26  26 TYR A  690  ASN A  708  1                                  19    
HELIX   27  27 LEU B   41  ARG B   45  5                                   5    
HELIX   28  28 ASP B   51  VAL B   70  1                                  20    
HELIX   29  29 ILE B   72  GLU B   88  1                                  17    
HELIX   30  30 GLU B  137  GLU B  142  1                                   6    
HELIX   31  31 ARG B  180  VAL B  182  5                                   3    
HELIX   32  32 PRO B  198  ALA B  200  5                                   3    
HELIX   33  33 ALA B  210  LYS B  212  5                                   3    
HELIX   34  34 PRO B  225  ASP B  229  5                                   5    
HELIX   35  35 CYS B  393  MET B  396  5                                   4    
HELIX   36  36 GLU B  440  LYS B  442  5                                   3    
HELIX   37  37 ASN B  494  ARG B  496  5                                   3    
HELIX   38  38 PHE B  497  ASP B  502  1                                   6    
HELIX   39  39 ARG B  520  VAL B  525  1                                   6    
HELIX   40  40 LYS B  528  LYS B  532  5                                   5    
HELIX   41  41 ARG B  533  SER B  549  1                                  17    
HELIX   42  42 THR B  553  ALA B  555  5                                   3    
HELIX   43  43 ALA B  564  ARG B  576  1                                  13    
HELIX   44  44 PRO B  577  PHE B  580  5                                   4    
HELIX   45  45 ASP B  591  CYS B  597  1                                   7    
HELIX   46  46 THR B  604  GLU B  609  5                                   6    
HELIX   47  47 PHE B  619  SER B  625  1                                   7    
HELIX   48  48 PRO B  628  VAL B  632  5                                   5    
HELIX   49  49 TYR B  653  LYS B  667  1                                  15    
HELIX   50  50 TYR B  690  LEU B  707  1                                  18    
HELIX   51  51 LEU C   41  ARG C   45  5                                   5    
HELIX   52  52 ASP C   51  VAL C   70  1                                  20    
HELIX   53  53 ASP C   71  LYS C   73  5                                   3    
HELIX   54  54 ASP C   74  GLU C   88  1                                  15    
HELIX   55  55 GLU C  137  GLU C  142  1                                   6    
HELIX   56  56 ARG C  180  VAL C  182  5                                   3    
HELIX   57  57 PRO C  198  ALA C  200  5                                   3    
HELIX   58  58 ASP C  209  ARG C  213  5                                   5    
HELIX   59  59 PRO C  225  ASP C  229  5                                   5    
HELIX   60  60 ARG C  271  GLY C  273  5                                   3    
HELIX   61  61 CYS C  393  MET C  396  5                                   4    
HELIX   62  62 GLU C  440  LYS C  442  5                                   3    
HELIX   63  63 ASN C  494  ARG C  496  5                                   3    
HELIX   64  64 PHE C  497  ASP C  502  1                                   6    
HELIX   65  65 ARG C  520  VAL C  525  1                                   6    
HELIX   66  66 LYS C  528  THR C  531  5                                   4    
HELIX   67  67 LYS C  532  SER C  549  1                                  18    
HELIX   68  68 THR C  553  ALA C  555  5                                   3    
HELIX   69  69 SER C  563  ARG C  576  1                                  14    
HELIX   70  70 PRO C  577  PHE C  580  5                                   4    
HELIX   71  71 ASP C  591  ASP C  598  1                                   8    
HELIX   72  72 LEU C  603  GLU C  610  5                                   8    
HELIX   73  73 GLU C  616  SER C  627  1                                  12    
HELIX   74  74 PRO C  628  VAL C  632  5                                   5    
HELIX   75  75 TYR C  653  LYS C  667  1                                  15    
HELIX   76  76 LYS C  691  ASN C  708  1                                  18    
HELIX   77  77 LEU D   41  ARG D   45  5                                   5    
HELIX   78  78 ASP D   51  ALA D   69  1                                  19    
HELIX   79  79 ILE D   72  HIS D   86  1                                  15    
HELIX   80  80 GLU D  137  ALA D  141  1                                   5    
HELIX   81  81 ARG D  180  VAL D  182  5                                   3    
HELIX   82  82 ALA D  210  LYS D  212  5                                   3    
HELIX   83  83 PRO D  225  ASP D  229  5                                   5    
HELIX   84  84 ARG D  271  GLY D  273  5                                   3    
HELIX   85  85 SER D  373  LEU D  377  5                                   5    
HELIX   86  86 CYS D  393  MET D  396  5                                   4    
HELIX   87  87 GLU D  440  LYS D  442  5                                   3    
HELIX   88  88 ASN D  494  ARG D  496  5                                   3    
HELIX   89  89 PHE D  497  ASP D  502  1                                   6    
HELIX   90  90 ARG D  520  VAL D  525  1                                   6    
HELIX   91  91 LYS D  528  THR D  531  5                                   4    
HELIX   92  92 LYS D  532  SER D  549  1                                  18    
HELIX   93  93 THR D  553  ALA D  555  5                                   3    
HELIX   94  94 SER D  563  ARG D  576  1                                  14    
HELIX   95  95 PRO D  577  PHE D  580  5                                   4    
HELIX   96  96 ASP D  591  CYS D  597  1                                   7    
HELIX   97  97 THR D  605  GLU D  610  5                                   6    
HELIX   98  98 PHE D  619  SER D  625  1                                   7    
HELIX   99  99 PRO D  628  VAL D  632  5                                   5    
HELIX  100 100 TYR D  653  LYS D  667  1                                  15    
HELIX  101 101 TYR D  690  ASN D  708  1                                  19    
HELIX  102 102 LEU E   41  ARG E   45  5                                   5    
HELIX  103 103 ASP E   51  VAL E   70  1                                  20    
HELIX  104 104 ILE E   72  GLU E   88  1                                  17    
HELIX  105 105 GLU E  137  GLU E  142  1                                   6    
HELIX  106 106 ARG E  180  VAL E  182  5                                   3    
HELIX  107 107 PRO E  198  ALA E  200  5                                   3    
HELIX  108 108 ASP E  209  ARG E  213  5                                   5    
HELIX  109 109 PRO E  225  ASP E  229  5                                   5    
HELIX  110 110 CYS E  393  MET E  396  5                                   4    
HELIX  111 111 GLU E  440  LYS E  442  5                                   3    
HELIX  112 112 ASN E  494  ARG E  496  5                                   3    
HELIX  113 113 PHE E  497  ASP E  502  1                                   6    
HELIX  114 114 ARG E  520  VAL E  525  1                                   6    
HELIX  115 115 LYS E  528  THR E  531  5                                   4    
HELIX  116 116 LYS E  532  SER E  549  1                                  18    
HELIX  117 117 THR E  553  ALA E  555  5                                   3    
HELIX  118 118 ALA E  564  ARG E  576  1                                  13    
HELIX  119 119 PRO E  577  PHE E  580  5                                   4    
HELIX  120 120 ASP E  591  ASP E  598  1                                   8    
HELIX  121 121 LEU E  603  TRP E  608  1                                   6    
HELIX  122 122 GLU E  616  SER E  625  1                                  10    
HELIX  123 123 PRO E  628  VAL E  632  5                                   5    
HELIX  124 124 TYR E  653  LYS E  667  1                                  15    
HELIX  125 125 TYR E  690  ASN E  708  1                                  19    
HELIX  126 126 LEU F   41  ARG F   45  5                                   5    
HELIX  127 127 ASP F   51  VAL F   70  1                                  20    
HELIX  128 128 ILE F   72  SER F   85  1                                  14    
HELIX  129 129 GLU F  137  ALA F  141  1                                   5    
HELIX  130 130 ARG F  180  VAL F  182  5                                   3    
HELIX  131 131 PRO F  198  ALA F  200  5                                   3    
HELIX  132 132 ALA F  210  LYS F  212  5                                   3    
HELIX  133 133 PRO F  225  ASP F  229  5                                   5    
HELIX  134 134 CYS F  393  MET F  396  5                                   4    
HELIX  135 135 GLU F  440  LYS F  442  5                                   3    
HELIX  136 136 ASN F  494  ARG F  496  5                                   3    
HELIX  137 137 PHE F  497  ASP F  502  1                                   6    
HELIX  138 138 ARG F  520  VAL F  525  1                                   6    
HELIX  139 139 LYS F  528  THR F  531  5                                   4    
HELIX  140 140 LYS F  532  SER F  549  1                                  18    
HELIX  141 141 THR F  553  ALA F  555  5                                   3    
HELIX  142 142 SER F  563  ARG F  576  1                                  14    
HELIX  143 143 PRO F  577  PHE F  580  5                                   4    
HELIX  144 144 ASP F  591  CYS F  597  1                                   7    
HELIX  145 145 LEU F  603  TRP F  608  1                                   6    
HELIX  146 146 PHE F  619  SER F  625  1                                   7    
HELIX  147 147 PRO F  628  VAL F  632  5                                   5    
HELIX  148 148 TYR F  653  LYS F  667  1                                  15    
HELIX  149 149 TYR F  690  LEU F  707  1                                  18    
SHEET    1  AA 2 GLU A  15  PHE A  18  0                                        
SHEET    2  AA 2 ARG A  35  VAL A  38 -1  O  ARG A  35   N  PHE A  18           
SHEET    1  AB 2 ASP A  91  MET A  92  0                                        
SHEET    2  AB 2 PHE A 101  ASP A 107 -1  O  ASP A 107   N  ASP A  91           
SHEET    1  AC 2 TYR A  96  TYR A  98  0                                        
SHEET    2  AC 2 PHE A 101  ASP A 107 -1  O  PHE A 101   N  TYR A  98           
SHEET    1  AD 4 GLU A 132  ASP A 136  0                                        
SHEET    2  AD 4 LEU A 115  PRO A 120 -1  O  HIS A 116   N  VAL A 134           
SHEET    3  AD 4 PHE A 101  ASP A 107 -1  O  LEU A 102   N  VAL A 119           
SHEET    4  AD 4 TYR A  96  TYR A  98 -1  O  TYR A  96   N  TYR A 103           
SHEET    1  AE 4 GLU A 132  ASP A 136  0                                        
SHEET    2  AE 4 LEU A 115  PRO A 120 -1  O  HIS A 116   N  VAL A 134           
SHEET    3  AE 4 PHE A 101  ASP A 107 -1  O  LEU A 102   N  VAL A 119           
SHEET    4  AE 4 ASP A  91  MET A  92 -1  O  ASP A  91   N  ASP A 107           
SHEET    1  AF 4 VAL A 148  PRO A 154  0                                        
SHEET    2  AF 4 VAL A 162  ASP A 167 -1  O  ALA A 163   N  ALA A 153           
SHEET    3  AF 4 TYR A 174  PHE A 178 -1  O  SER A 175   N  VAL A 166           
SHEET    4  AF 4 VAL A 187  THR A 190 -1  O  VAL A 187   N  ILE A 176           
SHEET    1  AG 4 VAL A 195  TRP A 196  0                                        
SHEET    2  AG 4 CYS A 202  THR A 207 -1  O  PHE A 204   N  VAL A 195           
SHEET    3  AG 4 LYS A 216  ILE A 221 -1  O  LYS A 216   N  THR A 207           
SHEET    4  AG 4 VAL A 230  THR A 234 -1  O  VAL A 230   N  ARG A 219           
SHEET    1  AH 4 SER A 241  ARG A 246  0                                        
SHEET    2  AH 4 THR A 252  SER A 259 -1  O  ILE A 254   N  GLY A 245           
SHEET    3  AH 4 THR A 262  ASP A 269 -1  O  THR A 262   N  SER A 259           
SHEET    4  AH 4 GLU A 280  MET A 281 -1  O  GLU A 280   N  LEU A 267           
SHEET    1  AI 4 TYR A 291  HIS A 296  0                                        
SHEET    2  AI 4 THR A 300  THR A 305 -1  O  THR A 300   N  HIS A 296           
SHEET    3  AI 4 LYS A 314  LYS A 319 -1  O  LYS A 314   N  THR A 305           
SHEET    4  AI 4 THR A 328  ILE A 331 -1  O  THR A 328   N  LEU A 317           
SHEET    1  AJ 4 THR A 338  VAL A 344  0                                        
SHEET    2  AJ 4 PHE A 348  ARG A 355 -1  O  VAL A 350   N  ALA A 343           
SHEET    3  AJ 4 LEU A 358  ARG A 365 -1  O  LEU A 358   N  ARG A 355           
SHEET    4  AJ 4 LYS A 378  GLU A 379 -1  O  LYS A 378   N  THR A 363           
SHEET    1  AK 4 THR A 388  VAL A 391  0                                        
SHEET    2  AK 4 LEU A 403  SER A 409 -1  O  ARG A 407   N  HIS A 390           
SHEET    3  AK 4 VAL A 416  ASP A 421 -1  O  VAL A 416   N  TYR A 408           
SHEET    4  AK 4 ARG A 427  ALA A 432 -1  O  LYS A 428   N  ASP A 419           
SHEET    1  AL 8 TYR A 444  THR A 452  0                                        
SHEET    2  AL 8 LYS A 458  ASP A 466 -1  O  VAL A 459   N  ALA A 451           
SHEET    3  AL 8 ILE A 506  ALA A 510 -1  O  TYR A 507   N  VAL A 464           
SHEET    4  AL 8 THR A 477  TYR A 480  1  O  MET A 478   N  ALA A 508           
SHEET    5  AL 8 LEU A 557  ARG A 562  1  O  SER A 558   N  LEU A 479           
SHEET    6  AL 8 VAL A 582  GLY A 586  1  O  VAL A 582   N  CYS A 559           
SHEET    7  AL 8 HIS A 639  GLY A 645  1  O  HIS A 639   N  ALA A 583           
SHEET    8  AL 8 VAL A 673  ASP A 678  1  O  LEU A 674   N  ILE A 642           
SHEET    1  BA 2 GLU B  15  PHE B  18  0                                        
SHEET    2  BA 2 ARG B  35  VAL B  38 -1  O  ARG B  35   N  PHE B  18           
SHEET    1  BB 2 ASP B  91  MET B  92  0                                        
SHEET    2  BB 2 PHE B 101  ASP B 107 -1  O  ASP B 107   N  ASP B  91           
SHEET    1  BC 2 TYR B  96  TYR B  98  0                                        
SHEET    2  BC 2 PHE B 101  ASP B 107 -1  O  PHE B 101   N  TYR B  98           
SHEET    1  BD 4 GLU B 132  ASP B 136  0                                        
SHEET    2  BD 4 LEU B 115  PRO B 120 -1  O  HIS B 116   N  LEU B 135           
SHEET    3  BD 4 PHE B 101  ASP B 107 -1  O  LEU B 102   N  VAL B 119           
SHEET    4  BD 4 TYR B  96  TYR B  98 -1  O  TYR B  96   N  TYR B 103           
SHEET    1  BE 4 GLU B 132  ASP B 136  0                                        
SHEET    2  BE 4 LEU B 115  PRO B 120 -1  O  HIS B 116   N  LEU B 135           
SHEET    3  BE 4 PHE B 101  ASP B 107 -1  O  LEU B 102   N  VAL B 119           
SHEET    4  BE 4 ASP B  91  MET B  92 -1  O  ASP B  91   N  ASP B 107           
SHEET    1  BF 4 VAL B 148  PRO B 154  0                                        
SHEET    2  BF 4 VAL B 162  ASP B 167 -1  O  ALA B 163   N  ALA B 153           
SHEET    3  BF 4 TYR B 174  PHE B 178 -1  O  SER B 175   N  VAL B 166           
SHEET    4  BF 4 VAL B 187  THR B 190 -1  O  VAL B 187   N  ILE B 176           
SHEET    1  BG 4 VAL B 195  TRP B 196  0                                        
SHEET    2  BG 4 CYS B 202  LYS B 208 -1  O  PHE B 204   N  VAL B 195           
SHEET    3  BG 4 ASP B 214  ILE B 221 -1  O  LYS B 216   N  THR B 207           
SHEET    4  BG 4 VAL B 230  THR B 234 -1  O  VAL B 230   N  ARG B 219           
SHEET    1  BH 4 SER B 241  ARG B 246  0                                        
SHEET    2  BH 4 THR B 252  MET B 258 -1  O  ILE B 254   N  GLY B 245           
SHEET    3  BH 4 SER B 263  ASP B 269 -1  O  GLU B 264   N  SER B 257           
SHEET    4  BH 4 GLU B 280  MET B 281 -1  O  GLU B 280   N  LEU B 267           
SHEET    1  BI 3 TYR B 291  HIS B 296  0                                        
SHEET    2  BI 3 THR B 300  THR B 305 -1  O  THR B 300   N  HIS B 296           
SHEET    3  BI 3 LYS B 314  LYS B 319 -1  O  LYS B 314   N  THR B 305           
SHEET    1  BJ 4 THR B 338  VAL B 344  0                                        
SHEET    2  BJ 4 PHE B 348  ARG B 355 -1  O  VAL B 350   N  ALA B 343           
SHEET    3  BJ 4 LEU B 358  LEU B 366 -1  O  LEU B 358   N  ARG B 355           
SHEET    4  BJ 4 PHE B 372  GLU B 379 -1  N  SER B 373   O  ARG B 365           
SHEET    1  BK 4 THR B 388  VAL B 391  0                                        
SHEET    2  BK 4 LEU B 403  SER B 409 -1  O  ARG B 407   N  HIS B 390           
SHEET    3  BK 4 VAL B 416  ASP B 421 -1  O  VAL B 416   N  TYR B 408           
SHEET    4  BK 4 ARG B 427  ALA B 432 -1  O  LYS B 428   N  ASP B 419           
SHEET    1  BL 8 TYR B 444  THR B 452  0                                        
SHEET    2  BL 8 LYS B 458  ASP B 466 -1  O  VAL B 459   N  ALA B 451           
SHEET    3  BL 8 ILE B 506  ALA B 510 -1  O  TYR B 507   N  VAL B 464           
SHEET    4  BL 8 THR B 477  GLY B 481  1  O  MET B 478   N  ALA B 508           
SHEET    5  BL 8 LEU B 557  ARG B 562  1  O  SER B 558   N  LEU B 479           
SHEET    6  BL 8 VAL B 582  GLY B 586  1  O  VAL B 582   N  CYS B 559           
SHEET    7  BL 8 HIS B 639  GLY B 645  1  O  HIS B 639   N  ALA B 583           
SHEET    8  BL 8 VAL B 673  ASP B 678  1  O  LEU B 674   N  ILE B 642           
SHEET    1  CA 2 GLU C  15  PHE C  18  0                                        
SHEET    2  CA 2 ARG C  35  VAL C  38 -1  O  ARG C  35   N  PHE C  18           
SHEET    1  CB 4 TYR C  96  TYR C  98  0                                        
SHEET    2  CB 4 PHE C 101  ARG C 106 -1  O  PHE C 101   N  TYR C  98           
SHEET    3  CB 4 LEU C 115  PRO C 120 -1  O  LEU C 115   N  ARG C 106           
SHEET    4  CB 4 GLU C 132  ASP C 136 -1  O  GLU C 132   N  ARG C 118           
SHEET    1  CC 4 VAL C 148  PRO C 154  0                                        
SHEET    2  CC 4 VAL C 162  ASP C 167 -1  O  ALA C 163   N  ALA C 153           
SHEET    3  CC 4 TYR C 174  PHE C 178 -1  O  SER C 175   N  VAL C 166           
SHEET    4  CC 4 VAL C 187  THR C 190 -1  O  VAL C 187   N  ILE C 176           
SHEET    1  CD 4 VAL C 195  TRP C 196  0                                        
SHEET    2  CD 4 CYS C 202  THR C 207 -1  O  PHE C 204   N  VAL C 195           
SHEET    3  CD 4 LYS C 216  ILE C 221 -1  O  LYS C 216   N  THR C 207           
SHEET    4  CD 4 VAL C 230  THR C 234 -1  O  VAL C 230   N  ARG C 219           
SHEET    1  CE 4 SER C 241  ARG C 246  0                                        
SHEET    2  CE 4 THR C 252  SER C 259 -1  O  ILE C 254   N  GLY C 245           
SHEET    3  CE 4 THR C 262  ASP C 269 -1  O  THR C 262   N  SER C 259           
SHEET    4  CE 4 GLU C 280  MET C 281 -1  O  GLU C 280   N  LEU C 267           
SHEET    1  CF 4 TYR C 291  HIS C 296  0                                        
SHEET    2  CF 4 THR C 300  THR C 305 -1  O  THR C 300   N  HIS C 296           
SHEET    3  CF 4 LYS C 314  LYS C 319 -1  O  LYS C 314   N  THR C 305           
SHEET    4  CF 4 THR C 328  ILE C 331 -1  O  THR C 328   N  LEU C 317           
SHEET    1  CG 4 VAL C 337  VAL C 344  0                                        
SHEET    2  CG 4 PHE C 348  ARG C 355 -1  O  VAL C 350   N  ALA C 343           
SHEET    3  CG 4 LEU C 358  GLY C 367 -1  O  LEU C 358   N  ARG C 355           
SHEET    4  CG 4 LEU C 371  PHE C 372  1  O  LEU C 371   N  GLY C 367           
SHEET    1  CH 4 VAL C 337  VAL C 344  0                                        
SHEET    2  CH 4 PHE C 348  ARG C 355 -1  O  VAL C 350   N  ALA C 343           
SHEET    3  CH 4 LEU C 358  GLY C 367 -1  O  LEU C 358   N  ARG C 355           
SHEET    4  CH 4 LYS C 378  GLU C 379 -1  O  LYS C 378   N  THR C 363           
SHEET    1  CI 2 LEU C 371  PHE C 372  0                                        
SHEET    2  CI 2 LEU C 358  GLY C 367  1  N  GLY C 367   O  LEU C 371           
SHEET    1  CJ 4 PHE C 387  VAL C 391  0                                        
SHEET    2  CJ 4 ARG C 405  SER C 410 -1  O  ARG C 407   N  HIS C 390           
SHEET    3  CJ 4 VAL C 416  GLU C 420 -1  O  VAL C 416   N  TYR C 408           
SHEET    4  CJ 4 ARG C 427  ALA C 432 -1  O  LYS C 428   N  ASP C 419           
SHEET    1  CK 8 TYR C 444  THR C 452  0                                        
SHEET    2  CK 8 LYS C 458  ASP C 466 -1  O  VAL C 459   N  ALA C 451           
SHEET    3  CK 8 ILE C 506  ALA C 510 -1  O  TYR C 507   N  VAL C 464           
SHEET    4  CK 8 THR C 477  GLY C 481  1  O  MET C 478   N  ALA C 508           
SHEET    5  CK 8 LEU C 557  ARG C 562  1  O  SER C 558   N  LEU C 479           
SHEET    6  CK 8 VAL C 582  GLY C 586  1  O  VAL C 582   N  CYS C 559           
SHEET    7  CK 8 HIS C 639  GLY C 645  1  O  HIS C 639   N  ALA C 583           
SHEET    8  CK 8 VAL C 673  ASP C 678  1  O  LEU C 674   N  ILE C 642           
SHEET    1  DA 2 GLU D  15  PHE D  18  0                                        
SHEET    2  DA 2 ARG D  35  VAL D  38 -1  O  ARG D  35   N  PHE D  18           
SHEET    1  DB 2 ASP D  91  MET D  92  0                                        
SHEET    2  DB 2 PHE D 101  ASP D 107 -1  O  ASP D 107   N  ASP D  91           
SHEET    1  DC 2 TYR D  96  TYR D  98  0                                        
SHEET    2  DC 2 PHE D 101  ASP D 107  1  O  PHE D 101   N  TYR D  98           
SHEET    1  DD 4 GLU D 132  ASP D 136  0                                        
SHEET    2  DD 4 LEU D 115  PRO D 120 -1  O  HIS D 116   N  VAL D 134           
SHEET    3  DD 4 PHE D 101  ASP D 107 -1  O  LEU D 102   N  VAL D 119           
SHEET    4  DD 4 TYR D  96  TYR D  98  1  O  TYR D  96   N  TYR D 103           
SHEET    1  DE 4 GLU D 132  ASP D 136  0                                        
SHEET    2  DE 4 LEU D 115  PRO D 120 -1  O  HIS D 116   N  VAL D 134           
SHEET    3  DE 4 PHE D 101  ASP D 107 -1  O  LEU D 102   N  VAL D 119           
SHEET    4  DE 4 ASP D  91  MET D  92 -1  O  ASP D  91   N  ASP D 107           
SHEET    1  DF 4 VAL D 148  PRO D 154  0                                        
SHEET    2  DF 4 VAL D 162  ASP D 167 -1  O  ALA D 163   N  ALA D 153           
SHEET    3  DF 4 TYR D 174  PHE D 178 -1  O  SER D 175   N  VAL D 166           
SHEET    4  DF 4 VAL D 187  THR D 190 -1  O  VAL D 187   N  ILE D 176           
SHEET    1  DG 4 VAL D 195  TRP D 196  0                                        
SHEET    2  DG 4 CYS D 202  LYS D 208 -1  O  PHE D 204   N  VAL D 195           
SHEET    3  DG 4 ASP D 214  ILE D 221 -1  N  ASN D 215   O  THR D 207           
SHEET    4  DG 4 VAL D 230  THR D 234 -1  O  VAL D 230   N  ARG D 219           
SHEET    1  DH 4 SER D 241  ARG D 246  0                                        
SHEET    2  DH 4 THR D 252  SER D 259 -1  O  ILE D 254   N  GLY D 245           
SHEET    3  DH 4 THR D 262  ASP D 269 -1  O  THR D 262   N  SER D 259           
SHEET    4  DH 4 GLU D 280  MET D 281 -1  O  GLU D 280   N  LEU D 267           
SHEET    1  DI 4 TYR D 291  HIS D 296  0                                        
SHEET    2  DI 4 THR D 300  THR D 305 -1  O  THR D 300   N  HIS D 296           
SHEET    3  DI 4 LYS D 314  LYS D 319 -1  O  LYS D 314   N  THR D 305           
SHEET    4  DI 4 THR D 328  ILE D 331 -1  O  THR D 328   N  LEU D 317           
SHEET    1  DJ 4 VAL D 337  VAL D 344  0                                        
SHEET    2  DJ 4 PHE D 348  ARG D 355 -1  O  VAL D 350   N  ALA D 343           
SHEET    3  DJ 4 LEU D 358  ARG D 365 -1  O  LEU D 358   N  ARG D 355           
SHEET    4  DJ 4 LYS D 378  GLU D 379 -1  O  LYS D 378   N  THR D 363           
SHEET    1  DK 4 THR D 388  VAL D 391  0                                        
SHEET    2  DK 4 LEU D 403  SER D 409 -1  O  ARG D 407   N  HIS D 390           
SHEET    3  DK 4 VAL D 416  ASP D 421 -1  O  VAL D 416   N  TYR D 408           
SHEET    4  DK 4 ARG D 427  ALA D 432 -1  O  LYS D 428   N  ASP D 419           
SHEET    1  DL 8 TYR D 444  THR D 452  0                                        
SHEET    2  DL 8 LYS D 458  ASP D 466 -1  O  VAL D 459   N  ALA D 451           
SHEET    3  DL 8 ILE D 506  ALA D 510 -1  O  TYR D 507   N  VAL D 464           
SHEET    4  DL 8 THR D 477  GLY D 481  1  O  MET D 478   N  ALA D 508           
SHEET    5  DL 8 LEU D 557  ARG D 562  1  O  SER D 558   N  LEU D 479           
SHEET    6  DL 8 VAL D 582  GLY D 586  1  O  VAL D 582   N  CYS D 559           
SHEET    7  DL 8 HIS D 639  GLY D 645  1  O  HIS D 639   N  ALA D 583           
SHEET    8  DL 8 VAL D 673  ASP D 678  1  O  LEU D 674   N  ILE D 642           
SHEET    1  EA 2 GLU E  15  PHE E  18  0                                        
SHEET    2  EA 2 ARG E  35  VAL E  38 -1  O  ARG E  35   N  PHE E  18           
SHEET    1  EB 2 ASP E  91  MET E  92  0                                        
SHEET    2  EB 2 PHE E 101  VAL E 108 -1  O  ASP E 107   N  ASP E  91           
SHEET    1  EC 2 TYR E  96  TYR E  98  0                                        
SHEET    2  EC 2 PHE E 101  VAL E 108  1  O  PHE E 101   N  TYR E  98           
SHEET    1  ED 4 GLU E 132  ASP E 136  0                                        
SHEET    2  ED 4 LEU E 111  PRO E 120 -1  O  HIS E 116   N  LEU E 135           
SHEET    3  ED 4 PHE E 101  VAL E 108 -1  O  LEU E 102   N  VAL E 119           
SHEET    4  ED 4 TYR E  96  TYR E  98  1  O  TYR E  96   N  TYR E 103           
SHEET    1  EE 4 GLU E 132  ASP E 136  0                                        
SHEET    2  EE 4 LEU E 111  PRO E 120 -1  O  HIS E 116   N  LEU E 135           
SHEET    3  EE 4 PHE E 101  VAL E 108 -1  O  LEU E 102   N  VAL E 119           
SHEET    4  EE 4 ASP E  91  MET E  92 -1  O  ASP E  91   N  ASP E 107           
SHEET    1  EF 4 VAL E 148  PRO E 154  0                                        
SHEET    2  EF 4 VAL E 162  ASP E 167 -1  O  ALA E 163   N  ALA E 153           
SHEET    3  EF 4 TYR E 174  PHE E 178 -1  O  SER E 175   N  VAL E 166           
SHEET    4  EF 4 VAL E 187  THR E 190 -1  O  VAL E 187   N  ILE E 176           
SHEET    1  EG 4 VAL E 195  TRP E 196  0                                        
SHEET    2  EG 4 CYS E 202  THR E 207 -1  O  PHE E 204   N  VAL E 195           
SHEET    3  EG 4 LYS E 216  ILE E 221 -1  O  LYS E 216   N  THR E 207           
SHEET    4  EG 4 VAL E 230  THR E 234 -1  O  VAL E 230   N  ARG E 219           
SHEET    1  EH 4 SER E 241  ARG E 246  0                                        
SHEET    2  EH 4 THR E 252  MET E 258 -1  O  ILE E 254   N  GLY E 245           
SHEET    3  EH 4 SER E 263  ASP E 269 -1  O  GLU E 264   N  SER E 257           
SHEET    4  EH 4 GLU E 280  MET E 281 -1  O  GLU E 280   N  LEU E 267           
SHEET    1  EI 4 TYR E 291  HIS E 296  0                                        
SHEET    2  EI 4 THR E 300  THR E 305 -1  O  THR E 300   N  HIS E 296           
SHEET    3  EI 4 LYS E 314  LYS E 319 -1  O  LYS E 314   N  THR E 305           
SHEET    4  EI 4 THR E 328  ILE E 331 -1  O  THR E 328   N  LEU E 317           
SHEET    1  EJ 4 VAL E 337  PHE E 345  0                                        
SHEET    2  EJ 4 PHE E 348  ARG E 355 -1  O  PHE E 348   N  PHE E 345           
SHEET    3  EJ 4 LEU E 358  LEU E 366 -1  O  LEU E 358   N  ARG E 355           
SHEET    4  EJ 4 PHE E 372  GLU E 379 -1  N  SER E 373   O  ARG E 365           
SHEET    1  EK 4 THR E 388  VAL E 391  0                                        
SHEET    2  EK 4 LEU E 406  SER E 409 -1  O  ARG E 407   N  HIS E 390           
SHEET    3  EK 4 VAL E 416  GLU E 420 -1  O  VAL E 416   N  TYR E 408           
SHEET    4  EK 4 ARG E 427  ALA E 432 -1  O  LYS E 428   N  ASP E 419           
SHEET    1  EL 8 TYR E 444  THR E 452  0                                        
SHEET    2  EL 8 LYS E 458  ASP E 466 -1  O  VAL E 459   N  ALA E 451           
SHEET    3  EL 8 ILE E 506  ALA E 510 -1  O  TYR E 507   N  VAL E 464           
SHEET    4  EL 8 THR E 477  GLY E 481  1  O  MET E 478   N  ALA E 508           
SHEET    5  EL 8 LEU E 557  ARG E 562  1  O  SER E 558   N  LEU E 479           
SHEET    6  EL 8 VAL E 582  GLY E 586  1  O  VAL E 582   N  CYS E 559           
SHEET    7  EL 8 HIS E 639  GLY E 645  1  O  HIS E 639   N  ALA E 583           
SHEET    8  EL 8 VAL E 673  ASP E 678  1  O  LEU E 674   N  ILE E 642           
SHEET    1  FA 2 HIS F  14  PHE F  18  0                                        
SHEET    2  FA 2 ARG F  35  ASP F  39 -1  O  ARG F  35   N  PHE F  18           
SHEET    1  FB 2 ASP F  91  MET F  92  0                                        
SHEET    2  FB 2 PHE F 101  ASP F 107 -1  O  ASP F 107   N  ASP F  91           
SHEET    1  FC 2 TYR F  96  TYR F  98  0                                        
SHEET    2  FC 2 PHE F 101  ASP F 107  1  O  PHE F 101   N  TYR F  98           
SHEET    1  FD 4 GLU F 132  ASP F 136  0                                        
SHEET    2  FD 4 LEU F 115  ARG F 118 -1  O  HIS F 116   N  VAL F 134           
SHEET    3  FD 4 PHE F 101  ASP F 107 -1  O  TYR F 104   N  CYS F 117           
SHEET    4  FD 4 TYR F  96  TYR F  98  1  O  TYR F  96   N  TYR F 103           
SHEET    1  FE 4 GLU F 132  ASP F 136  0                                        
SHEET    2  FE 4 LEU F 115  ARG F 118 -1  O  HIS F 116   N  VAL F 134           
SHEET    3  FE 4 PHE F 101  ASP F 107 -1  O  TYR F 104   N  CYS F 117           
SHEET    4  FE 4 ASP F  91  MET F  92 -1  O  ASP F  91   N  ASP F 107           
SHEET    1  FF 4 VAL F 148  PRO F 154  0                                        
SHEET    2  FF 4 VAL F 162  ASP F 167 -1  O  ALA F 163   N  ALA F 153           
SHEET    3  FF 4 TYR F 174  PHE F 178 -1  O  SER F 175   N  VAL F 166           
SHEET    4  FF 4 VAL F 187  THR F 190 -1  O  VAL F 187   N  ILE F 176           
SHEET    1  FG 4 VAL F 195  TRP F 196  0                                        
SHEET    2  FG 4 CYS F 202  LYS F 208 -1  O  PHE F 204   N  VAL F 195           
SHEET    3  FG 4 ASP F 214  ILE F 221 -1  O  LYS F 216   N  THR F 207           
SHEET    4  FG 4 VAL F 230  THR F 234 -1  O  VAL F 230   N  ARG F 219           
SHEET    1  FH 4 SER F 241  ARG F 246  0                                        
SHEET    2  FH 4 THR F 252  SER F 259 -1  O  ILE F 254   N  GLY F 245           
SHEET    3  FH 4 THR F 262  ASP F 269 -1  O  THR F 262   N  SER F 259           
SHEET    4  FH 4 GLU F 280  MET F 281 -1  O  GLU F 280   N  LEU F 267           
SHEET    1  FI 4 TYR F 291  HIS F 296  0                                        
SHEET    2  FI 4 THR F 300  THR F 305 -1  O  THR F 300   N  HIS F 296           
SHEET    3  FI 4 LYS F 314  LYS F 319 -1  O  LYS F 314   N  THR F 305           
SHEET    4  FI 4 VAL F 329  ILE F 331 -1  N  LEU F 330   O  VAL F 315           
SHEET    1  FJ 4 THR F 338  VAL F 344  0                                        
SHEET    2  FJ 4 PHE F 348  ARG F 355 -1  O  VAL F 350   N  ALA F 343           
SHEET    3  FJ 4 LEU F 358  ARG F 365 -1  O  LEU F 358   N  ARG F 355           
SHEET    4  FJ 4 LYS F 378  GLU F 379 -1  O  LYS F 378   N  THR F 363           
SHEET    1  FK 4 PHE F 387  VAL F 391  0                                        
SHEET    2  FK 4 LEU F 406  SER F 410 -1  O  ARG F 407   N  HIS F 390           
SHEET    3  FK 4 VAL F 416  GLU F 420 -1  O  VAL F 416   N  TYR F 408           
SHEET    4  FK 4 ARG F 427  ALA F 432 -1  O  LYS F 428   N  ASP F 419           
SHEET    1  FL 8 TYR F 444  THR F 452  0                                        
SHEET    2  FL 8 LYS F 458  ASP F 466 -1  O  VAL F 459   N  ALA F 451           
SHEET    3  FL 8 ILE F 506  ALA F 510 -1  O  TYR F 507   N  VAL F 464           
SHEET    4  FL 8 THR F 477  TYR F 480  1  O  MET F 478   N  ALA F 508           
SHEET    5  FL 8 LEU F 557  ARG F 562  1  O  SER F 558   N  LEU F 479           
SHEET    6  FL 8 VAL F 582  GLY F 586  1  O  VAL F 582   N  CYS F 559           
SHEET    7  FL 8 HIS F 639  GLY F 645  1  O  HIS F 639   N  ALA F 583           
SHEET    8  FL 8 VAL F 673  ASP F 678  1  O  LEU F 674   N  ILE F 642           
LINK         C1  FC0 G   1                 N   ARG G   2     1555   1555  1.37  
LINK         N1  OAR G   4                 C   VAL G   3     1555   1555  1.34  
LINK         C1  FC0 H   1                 N   ARG H   2     1555   1555  1.34  
LINK         N1  OAR H   4                 C   VAL H   3     1555   1555  1.33  
LINK         C1  FC0 I   1                 N   ARG I   2     1555   1555  1.34  
LINK         N1  OAR I   4                 C   VAL I   3     1555   1555  1.34  
LINK         C1  FC0 J   1                 N   ARG J   2     1555   1555  1.34  
LINK         N1  OAR J   4                 C   VAL J   3     1555   1555  1.35  
LINK         C1  FC0 K   1                 N   ARG K   2     1555   1555  1.36  
LINK         N1  OAR K   4                 C   VAL K   3     1555   1555  1.35  
LINK         C1  FC0 L   1                 N   ARG L   2     1555   1555  1.32  
LINK         N1  OAR L   4                 C   VAL L   3     1555   1555  1.32  
CISPEP   1 ASP A   32    PRO A   33          0         2.50                     
CISPEP   2 TYR A  482    GLY A  483          0       -15.32                     
CISPEP   3 ASP B   32    PRO B   33          0         1.67                     
CISPEP   4 ASP C   32    PRO C   33          0        -0.74                     
CISPEP   5 ASP D   32    PRO D   33          0        -1.21                     
CISPEP   6 ASP E   32    PRO E   33          0         2.44                     
CISPEP   7 TYR E  482    GLY E  483          0       -22.05                     
CISPEP   8 ASP F   32    PRO F   33          0        -4.87                     
CISPEP   9 TYR F  482    GLY F  483          0       -23.29                     
SITE     1 AC1 14 ASN A 191  LYS A 208  LYS A 212  ASP A 214                    
SITE     2 AC1 14 TYR A 482  TYR A 485  SER A 563  ALA A 564                    
SITE     3 AC1 14 PHE A 589  GLU A 607  ARG A 650  VAL A 651                    
SITE     4 AC1 14 HOH A2039  HOH A2105                                          
SITE     1 AC2 13 GLU B 172  LYS B 208  ASP B 214  TYR B 482                    
SITE     2 AC2 13 TYR B 485  SER B 563  ALA B 564  PHE B 589                    
SITE     3 AC2 13 LEU B 603  GLU B 607  ARG B 650  VAL B 651                    
SITE     4 AC2 13 GLU B 655                                                     
SITE     1 AC3 14 GLU C 172  ASN C 191  LYS C 208  ASP C 214                    
SITE     2 AC3 14 TYR C 482  TYR C 485  SER C 563  ALA C 564                    
SITE     3 AC3 14 PHE C 589  GLU C 607  ARG C 650  VAL C 651                    
SITE     4 AC3 14 GLU C 655  HOH C2008                                          
SITE     1 AC4 12 GLU D 172  LYS D 208  ASP D 214  TYR D 482                    
SITE     2 AC4 12 TYR D 485  SER D 563  ALA D 564  PHE D 589                    
SITE     3 AC4 12 LEU D 603  GLU D 607  ARG D 650  VAL D 651                    
SITE     1 AC5 13 ASN E 191  LYS E 208  LYS E 212  ASP E 214                    
SITE     2 AC5 13 TYR E 482  TYR E 485  SER E 563  ALA E 564                    
SITE     3 AC5 13 PHE E 589  GLU E 607  ARG E 650  VAL E 651                    
SITE     4 AC5 13 HOH E2015                                                     
SITE     1 AC6 13 GLU F 172  LYS F 208  LYS F 212  ASP F 214                    
SITE     2 AC6 13 TYR F 482  TYR F 485  SER F 563  ALA F 564                    
SITE     3 AC6 13 PHE F 589  GLU F 607  ARG F 650  HOH F2013                    
SITE     4 AC6 13 HOH F2039                                                     
CRYST1   71.800  148.800  268.000  90.00  91.00  90.00 P 1 21 1     12          
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      0.013928  0.000000  0.000243        0.00000                         
SCALE2      0.000000  0.006720  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003732        0.00000                         
ATOM      1  N   ARG A   5       0.375 116.084 208.516  1.00 55.86           N  
ANISOU    1  N   ARG A   5     3628  11937   5657    387   -935   2668       N  
ATOM      2  CA  ARG A   5       1.671 116.647 209.047  1.00 53.85           C  
ANISOU    2  CA  ARG A   5     3662  11416   5382    504   -741   2480       C  
ATOM      3  C   ARG A   5       1.747 116.484 210.544  1.00 53.32           C  
ANISOU    3  C   ARG A   5     3633  11184   5441    589   -523   2357       C  
ATOM      4  O   ARG A   5       1.183 115.539 211.079  1.00 54.70           O  
ANISOU    4  O   ARG A   5     3703  11428   5652    477   -543   2323       O  
ATOM      5  CB  ARG A   5       1.767 118.116 208.753  1.00 54.33           C  
ANISOU    5  CB  ARG A   5     3734  11404   5506    734   -658   2642       C  
ATOM      6  CG  ARG A   5       3.158 118.672 208.673  1.00 51.51           C  
ANISOU    6  CG  ARG A   5     3674  10843   5054    770   -562   2482       C  
ATOM      7  CD  ARG A   5       3.024 120.008 207.934  1.00 54.14           C  
ANISOU    7  CD  ARG A   5     3980  11173   5417    939   -566   2705       C  
ATOM      8  NE  ARG A   5       4.278 120.701 207.670  1.00 51.99           N  
ANISOU    8  NE  ARG A   5     3973  10729   5055    967   -490   2602       N  
ATOM      9  CZ  ARG A   5       4.365 122.005 207.406  1.00 52.86           C  
ANISOU    9  CZ  ARG A   5     4123  10738   5221   1144   -416   2757       C  
ATOM     10  NH1 ARG A   5       3.270 122.771 207.364  1.00 55.29           N  
ANISOU   10  NH1 ARG A   5     4227  11097   5685   1335   -404   3024       N  
ATOM     11  NH2 ARG A   5       5.556 122.548 207.192  1.00 51.62           N  
ANISOU   11  NH2 ARG A   5     4212  10428   4975   1134   -349   2650       N  
ATOM     12  N   GLY A   6       2.439 117.409 211.224  1.00 52.19           N  
ANISOU   12  N   GLY A   6     3652  10824   5356    773   -317   2294       N  
ATOM     13  CA  GLY A   6       2.657 117.357 212.696  1.00 49.26           C  
ANISOU   13  CA  GLY A   6     3366  10274   5075    853    -97   2160       C  
ATOM     14  C   GLY A   6       2.513 118.742 213.332  1.00 49.58           C  
ANISOU   14  C   GLY A   6     3417  10162   5257   1126    123   2257       C  
ATOM     15  O   GLY A   6       2.373 119.745 212.625  1.00 50.86           O  
ANISOU   15  O   GLY A   6     3545  10330   5450   1256    107   2418       O  
ATOM     16  N   PRO A   7       2.504 118.808 214.671  1.00 49.01           N  
ANISOU   16  N   PRO A   7     3402   9950   5270   1213    332   2167       N  
ATOM     17  CA  PRO A   7       2.406 120.086 215.361  1.00 49.81           C  
ANISOU   17  CA  PRO A   7     3555   9878   5494   1464    564   2225       C  
ATOM     18  C   PRO A   7       3.615 120.986 215.088  1.00 48.65           C  
ANISOU   18  C   PRO A   7     3677   9534   5272   1510    607   2134       C  
ATOM     19  O   PRO A   7       4.759 120.544 215.118  1.00 46.51           O  
ANISOU   19  O   PRO A   7     3615   9187   4871   1365    565   1934       O  
ATOM     20  CB  PRO A   7       2.365 119.683 216.853  1.00 49.09           C  
ANISOU   20  CB  PRO A   7     3526   9683   5443   1473    754   2087       C  
ATOM     21  CG  PRO A   7       1.849 118.338 216.868  1.00 48.99           C  
ANISOU   21  CG  PRO A   7     3362   9850   5403   1285    625   2073       C  
ATOM     22  CD  PRO A   7       2.371 117.683 215.612  1.00 48.13           C  
ANISOU   22  CD  PRO A   7     3283   9852   5153   1087    366   2037       C  
ATOM     23  N   ILE A   8       3.345 122.252 214.847  1.00 50.25           N  
ANISOU   23  N   ILE A   8     3870   9654   5569   1716    698   2289       N  
ATOM     24  CA  ILE A   8       4.375 123.250 214.692  1.00 49.59           C  
ANISOU   24  CA  ILE A   8     4038   9363   5439   1773    769   2226       C  
ATOM     25  C   ILE A   8       3.956 124.394 215.631  1.00 51.08           C  
ANISOU   25  C   ILE A   8     4275   9352   5783   2025   1032   2281       C  
ATOM     26  O   ILE A   8       2.847 124.914 215.501  1.00 53.50           O  
ANISOU   26  O   ILE A   8     4377   9715   6237   2213   1084   2498       O  
ATOM     27  CB  ILE A   8       4.394 123.712 213.226  1.00 50.59           C  
ANISOU   27  CB  ILE A   8     4114   9589   5520   1769    597   2396       C  
ATOM     28  CG1 ILE A   8       4.853 122.553 212.333  1.00 49.25           C  
ANISOU   28  CG1 ILE A   8     3931   9605   5175   1511    359   2310       C  
ATOM     29  CG2 ILE A   8       5.229 124.962 213.046  1.00 50.63           C  
ANISOU   29  CG2 ILE A   8     4348   9375   5516   1864    694   2393       C  
ATOM     30  CD1 ILE A   8       4.544 122.720 210.859  1.00 50.69           C  
ANISOU   30  CD1 ILE A   8     4002   9965   5294   1475    156   2502       C  
ATOM     31  N   ALA A   9       4.789 124.768 216.596  1.00 49.93           N  
ANISOU   31  N   ALA A   9     4388   8975   5607   2033   1201   2091       N  
ATOM     32  CA  ALA A   9       4.425 125.889 217.464  1.00 51.58           C  
ANISOU   32  CA  ALA A   9     4682   8971   5945   2265   1462   2124       C  
ATOM     33  C   ALA A   9       4.512 127.268 216.779  1.00 53.23           C  
ANISOU   33  C   ALA A   9     4973   9032   6219   2433   1506   2273       C  
ATOM     34  O   ALA A   9       5.183 127.439 215.781  1.00 52.61           O  
ANISOU   34  O   ALA A   9     4963   8972   6053   2338   1355   2299       O  
ATOM     35  CB  ALA A   9       5.225 125.859 218.728  1.00 50.17           C  
ANISOU   35  CB  ALA A   9     4763   8599   5699   2205   1620   1878       C  
ATOM     36  N   ALA A  10       3.821 128.248 217.338  1.00 55.51           N  
ANISOU   36  N   ALA A  10     5263   9165   6664   2686   1727   2371       N  
ATOM     37  CA  ALA A  10       3.729 129.569 216.732  1.00 57.57           C  
ANISOU   37  CA  ALA A  10     5586   9270   7018   2878   1785   2543       C  
ATOM     38  C   ALA A  10       4.885 130.449 217.133  1.00 56.91           C  
ANISOU   38  C   ALA A  10     5874   8879   6869   2851   1910   2377       C  
ATOM     39  O   ALA A  10       5.364 130.388 218.243  1.00 55.97           O  
ANISOU   39  O   ALA A  10     5951   8614   6703   2799   2056   2163       O  
ATOM     40  CB  ALA A  10       2.425 130.228 217.118  1.00 60.70           C  
ANISOU   40  CB  ALA A  10     5807   9629   7628   3185   1977   2737       C  
ATOM     41  N   HIS A  11       5.281 131.311 216.226  1.00 57.70           N  
ANISOU   41  N   HIS A  11     6070   8884   6968   2885   1852   2493       N  
ATOM     42  CA  HIS A  11       6.403 132.190 216.423  1.00 57.31           C  
ANISOU   42  CA  HIS A  11     6364   8554   6856   2831   1941   2363       C  
ATOM     43  C   HIS A  11       6.007 133.430 217.142  1.00 59.82           C  
ANISOU   43  C   HIS A  11     6842   8569   7320   3080   2214   2398       C  
ATOM     44  O   HIS A  11       5.143 134.127 216.695  1.00 62.39           O  
ANISOU   44  O   HIS A  11     7047   8862   7797   3317   2265   2632       O  
ATOM     45  CB  HIS A  11       6.932 132.563 215.057  1.00 57.35           C  
ANISOU   45  CB  HIS A  11     6391   8602   6797   2755   1760   2498       C  
ATOM     46  CG  HIS A  11       7.490 131.392 214.323  1.00 54.95           C  
ANISOU   46  CG  HIS A  11     5984   8568   6326   2496   1510   2431       C  
ATOM     47  ND1 HIS A  11       8.529 131.499 213.427  1.00 53.94           N  
ANISOU   47  ND1 HIS A  11     5980   8453   6063   2322   1375   2410       N  
ATOM     48  CD2 HIS A  11       7.189 130.073 214.408  1.00 53.46           C  
ANISOU   48  CD2 HIS A  11     5602   8631   6082   2377   1389   2364       C  
ATOM     49  CE1 HIS A  11       8.828 130.296 212.974  1.00 52.00           C  
ANISOU   49  CE1 HIS A  11     5618   8455   5686   2123   1189   2330       C  
ATOM     50  NE2 HIS A  11       8.031 129.414 213.555  1.00 51.67           N  
ANISOU   50  NE2 HIS A  11     5391   8552   5690   2149   1189   2299       N  
ATOM     51  N   ARG A  12       6.629 133.690 218.277  1.00 59.28           N  
ANISOU   51  N   ARG A  12     7048   8274   7201   3028   2389   2165       N  
ATOM     52  CA  ARG A  12       6.476 134.945 218.975  1.00 61.70           C  
ANISOU   52  CA  ARG A  12     7591   8240   7613   3229   2659   2151       C  
ATOM     53  C   ARG A  12       7.871 135.536 219.105  1.00 60.75           C  
ANISOU   53  C   ARG A  12     7835   7884   7364   3035   2664   1972       C  
ATOM     54  O   ARG A  12       8.779 134.860 219.625  1.00 58.36           O  
ANISOU   54  O   ARG A  12     7642   7628   6903   2787   2599   1747       O  
ATOM     55  CB  ARG A  12       5.850 134.718 220.335  1.00 62.37           C  
ANISOU   55  CB  ARG A  12     7684   8272   7743   3336   2887   2025       C  
ATOM     56  CG  ARG A  12       4.644 133.807 220.305  1.00 62.67           C  
ANISOU   56  CG  ARG A  12     7338   8605   7868   3437   2849   2159       C  
ATOM     57  CD  ARG A  12       3.532 134.374 221.144  1.00 65.64           C  
ANISOU   57  CD  ARG A  12     7670   8854   8416   3740   3145   2221       C  
ATOM     58  NE  ARG A  12       2.467 133.407 221.383  1.00 65.82           N  
ANISOU   58  NE  ARG A  12     7344   9160   8503   3795   3137   2303       N  
ATOM     59  CZ  ARG A  12       2.308 132.735 222.523  1.00 65.16           C  
ANISOU   59  CZ  ARG A  12     7274   9120   8364   3734   3262   2134       C  
ATOM     60  NH1 ARG A  12       3.152 132.916 223.535  1.00 64.27           N  
ANISOU   60  NH1 ARG A  12     7509   8792   8117   3618   3396   1870       N  
ATOM     61  NH2 ARG A  12       1.299 131.881 222.659  1.00 65.57           N  
ANISOU   61  NH2 ARG A  12     6992   9436   8485   3778   3250   2235       N  
ATOM     62  N   PRO A  13       8.073 136.781 218.605  1.00 62.73           N  
ANISOU   62  N   PRO A  13     8267   7887   7682   3135   2729   2085       N  
ATOM     63  CA  PRO A  13       9.435 137.348 218.580  1.00 61.97           C  
ANISOU   63  CA  PRO A  13     8497   7587   7462   2917   2707   1939       C  
ATOM     64  C   PRO A  13       9.939 137.657 219.995  1.00 62.09           C  
ANISOU   64  C   PRO A  13     8824   7351   7417   2848   2908   1670       C  
ATOM     65  O   PRO A  13       9.210 138.205 220.836  1.00 64.28           O  
ANISOU   65  O   PRO A  13     9193   7432   7797   3062   3153   1650       O  
ATOM     66  CB  PRO A  13       9.273 138.623 217.762  1.00 64.62           C  
ANISOU   66  CB  PRO A  13     8933   7708   7913   3081   2755   2158       C  
ATOM     67  CG  PRO A  13       7.873 139.073 218.074  1.00 67.48           C  
ANISOU   67  CG  PRO A  13     9169   7990   8481   3440   2947   2319       C  
ATOM     68  CD  PRO A  13       7.061 137.783 218.221  1.00 66.10           C  
ANISOU   68  CD  PRO A  13     8633   8172   8311   3460   2860   2337       C  
ATOM     69  N   HIS A  14      11.168 137.238 220.252  1.00 59.84           N  
ANISOU   69  N   HIS A  14     8685   7095   6958   2547   2800   1466       N  
ATOM     70  CA  HIS A  14      11.816 137.431 221.527  1.00 59.77           C  
ANISOU   70  CA  HIS A  14     8971   6887   6850   2418   2934   1206       C  
ATOM     71  C   HIS A  14      13.270 137.537 221.179  1.00 58.35           C  
ANISOU   71  C   HIS A  14     8959   6681   6529   2117   2784   1105       C  
ATOM     72  O   HIS A  14      13.779 136.729 220.400  1.00 56.15           O  
ANISOU   72  O   HIS A  14     8495   6663   6176   1960   2562   1137       O  
ATOM     73  CB  HIS A  14      11.585 136.229 222.427  1.00 58.00           C  
ANISOU   73  CB  HIS A  14     8617   6871   6551   2355   2922   1061       C  
ATOM     74  CG  HIS A  14      12.433 136.224 223.661  1.00 57.51           C  
ANISOU   74  CG  HIS A  14     8840   6670   6342   2159   2995    792       C  
ATOM     75  ND1 HIS A  14      11.948 136.579 224.901  1.00 59.23           N  
ANISOU   75  ND1 HIS A  14     9240   6700   6563   2266   3238    669       N  
ATOM     76  CD2 HIS A  14      13.733 135.896 223.848  1.00 55.69           C  
ANISOU   76  CD2 HIS A  14     8739   6473   5950   1859   2853    629       C  
ATOM     77  CE1 HIS A  14      12.913 136.475 225.797  1.00 58.47           C  
ANISOU   77  CE1 HIS A  14     9387   6530   6301   2026   3229    440       C  
ATOM     78  NE2 HIS A  14      14.006 136.057 225.185  1.00 56.33           N  
ANISOU   78  NE2 HIS A  14     9075   6394   5935   1779   2992    419       N  
ATOM     79  N   GLU A  15      13.961 138.535 221.714  1.00 59.77           N  
ANISOU   79  N   GLU A  15     9488   6549   6671   2028   2904    985       N  
ATOM     80  CA  GLU A  15      15.401 138.558 221.477  1.00 58.44           C  
ANISOU   80  CA  GLU A  15     9457   6384   6363   1711   2755    879       C  
ATOM     81  C   GLU A  15      16.146 137.919 222.639  1.00 56.97           C  
ANISOU   81  C   GLU A  15     9381   6242   6022   1486   2733    621       C  
ATOM     82  O   GLU A  15      15.784 138.068 223.817  1.00 58.02           O  
ANISOU   82  O   GLU A  15     9675   6230   6138   1544   2903    484       O  
ATOM     83  CB  GLU A  15      15.941 139.945 221.067  1.00 60.66           C  
ANISOU   83  CB  GLU A  15    10021   6351   6676   1672   2825    934       C  
ATOM     84  CG  GLU A  15      16.293 140.909 222.194  1.00 62.76           C  
ANISOU   84  CG  GLU A  15    10688   6250   6909   1611   3021    750       C  
ATOM     85  CD  GLU A  15      16.580 142.321 221.672  1.00 68.65           C  
ANISOU   85  CD  GLU A  15    11700   6661   7724   1621   3106    847       C  
ATOM     86  OE1 GLU A  15      17.106 142.460 220.531  1.00 67.64           O  
ANISOU   86  OE1 GLU A  15    11490   6615   7594   1522   2957    993       O  
ATOM     87  OE2 GLU A  15      16.265 143.295 222.411  1.00 74.09           O  
ANISOU   87  OE2 GLU A  15    12693   6994   8465   1729   3334    776       O  
ATOM     88  N   VAL A  16      17.159 137.153 222.267  1.00 54.63           N  
ANISOU   88  N   VAL A  16     8979   6167   5612   1239   2521    567       N  
ATOM     89  CA  VAL A  16      18.026 136.514 223.233  1.00 53.23           C  
ANISOU   89  CA  VAL A  16     8882   6058   5285   1003   2457    350       C  
ATOM     90  C   VAL A  16      19.378 137.182 223.061  1.00 53.62           C  
ANISOU   90  C   VAL A  16     9136   5985   5250    739   2388    283       C  
ATOM     91  O   VAL A  16      19.785 137.468 221.961  1.00 53.54           O  
ANISOU   91  O   VAL A  16     9061   6013   5267    691   2299    409       O  
ATOM     92  CB  VAL A  16      18.013 134.977 223.073  1.00 50.46           C  
ANISOU   92  CB  VAL A  16     8220   6065   4885    957   2281    342       C  
ATOM     93  CG1 VAL A  16      17.951 134.600 221.607  1.00 49.39           C  
ANISOU   93  CG1 VAL A  16     7828   6139   4800    992   2129    523       C  
ATOM     94  CG2 VAL A  16      19.191 134.351 223.745  1.00 48.99           C  
ANISOU   94  CG2 VAL A  16     8094   5971   4550    685   2161    161       C  
ATOM     95  N   VAL A  17      20.019 137.520 224.166  1.00 54.40           N  
ANISOU   95  N   VAL A  17     9501   5923   5247    565   2444     93       N  
ATOM     96  CA  VAL A  17      21.242 138.316 224.138  1.00 55.38           C  
ANISOU   96  CA  VAL A  17     9853   5891   5296    302   2401     26       C  
ATOM     97  C   VAL A  17      22.431 137.426 224.471  1.00 53.45           C  
ANISOU   97  C   VAL A  17     9522   5875   4911     16   2206    -99       C  
ATOM     98  O   VAL A  17      22.290 136.513 225.251  1.00 52.22           O  
ANISOU   98  O   VAL A  17     9285   5864   4691     12   2171   -198       O  
ATOM     99  CB  VAL A  17      21.154 139.483 225.158  1.00 58.25           C  
ANISOU   99  CB  VAL A  17    10620   5874   5637    287   2605   -102       C  
ATOM    100  CG1 VAL A  17      22.406 140.302 225.120  1.00 59.44           C  
ANISOU  100  CG1 VAL A  17    11009   5866   5711    -12   2549   -168       C  
ATOM    101  CG2 VAL A  17      19.914 140.340 224.911  1.00 60.44           C  
ANISOU  101  CG2 VAL A  17    10980   5912   6073    611   2822     23       C  
ATOM    102  N   PHE A  18      23.584 137.691 223.868  1.00 53.35           N  
ANISOU  102  N   PHE A  18     9517   5898   4858   -214   2083    -80       N  
ATOM    103  CA  PHE A  18      24.840 136.941 224.081  1.00 51.88           C  
ANISOU  103  CA  PHE A  18     9229   5929   4554   -490   1895   -176       C  
ATOM    104  C   PHE A  18      25.954 137.923 224.384  1.00 53.75           C  
ANISOU  104  C   PHE A  18     9726   5977   4719   -775   1885   -255       C  
ATOM    105  O   PHE A  18      26.268 138.799 223.555  1.00 54.97           O  
ANISOU  105  O   PHE A  18     9956   6008   4923   -828   1907   -153       O  
ATOM    106  CB  PHE A  18      25.228 136.164 222.818  1.00 49.92           C  
ANISOU  106  CB  PHE A  18     8659   5974   4336   -497   1738    -48       C  
ATOM    107  CG  PHE A  18      24.488 134.898 222.649  1.00 47.80           C  
ANISOU  107  CG  PHE A  18     8115   5952   4095   -317   1684    -14       C  
ATOM    108  CD1 PHE A  18      23.249 134.890 222.039  1.00 47.79           C  
ANISOU  108  CD1 PHE A  18     8010   5950   4198    -49   1761    120       C  
ATOM    109  CD2 PHE A  18      25.031 133.718 223.091  1.00 46.02           C  
ANISOU  109  CD2 PHE A  18     7733   5958   3795   -420   1549   -105       C  
ATOM    110  CE1 PHE A  18      22.561 133.733 221.876  1.00 46.04           C  
ANISOU  110  CE1 PHE A  18     7540   5954   3999     91   1703    153       C  
ATOM    111  CE2 PHE A  18      24.351 132.538 222.947  1.00 44.23           C  
ANISOU  111  CE2 PHE A  18     7272   5939   3594   -268   1500    -76       C  
ATOM    112  CZ  PHE A  18      23.109 132.541 222.346  1.00 44.22           C  
ANISOU  112  CZ  PHE A  18     7176   5936   3691    -23   1576     48       C  
ATOM    113  N   GLY A  19      26.554 137.787 225.553  1.00 54.14           N  
ANISOU  113  N   GLY A  19     9916   6008   4645   -973   1845   -425       N  
ATOM    114  CA  GLY A  19      27.498 138.794 226.003  1.00 56.36           C  
ANISOU  114  CA  GLY A  19    10486   6081   4848  -1257   1846   -516       C  
ATOM    115  C   GLY A  19      27.071 139.458 227.288  1.00 58.50           C  
ANISOU  115  C   GLY A  19    11118   6065   5046  -1267   1999   -676       C  
ATOM    116  O   GLY A  19      26.297 138.894 228.048  1.00 57.93           O  
ANISOU  116  O   GLY A  19    11039   6026   4946  -1111   2065   -745       O  
ATOM    117  N   LYS A  20      27.572 140.671 227.517  1.00 61.16           N  
ANISOU  117  N   LYS A  20    11782   6111   5346  -1458   2063   -735       N  
ATOM    118  CA  LYS A  20      27.382 141.373 228.802  1.00 63.64           C  
ANISOU  118  CA  LYS A  20    12494   6134   5554  -1535   2200   -921       C  
ATOM    119  C   LYS A  20      25.951 141.857 229.014  1.00 64.86           C  
ANISOU  119  C   LYS A  20    12811   6033   5800  -1190   2464   -914       C  
ATOM    120  O   LYS A  20      25.348 142.458 228.115  1.00 65.49           O  
ANISOU  120  O   LYS A  20    12879   5970   6033   -981   2576   -766       O  
ATOM    121  CB  LYS A  20      28.346 142.549 228.908  1.00 66.37           C  
ANISOU  121  CB  LYS A  20    13154   6228   5837  -1856   2190   -984       C  
ATOM    122  CG  LYS A  20      28.461 143.152 230.263  1.00 68.97           C  
ANISOU  122  CG  LYS A  20    13892   6303   6009  -2033   2275  -1201       C  
ATOM    123  CD  LYS A  20      29.479 144.276 230.269  1.00 71.72           C  
ANISOU  123  CD  LYS A  20    14533   6419   6298  -2386   2238  -1254       C  
ATOM    124  CE  LYS A  20      29.737 144.714 231.706  1.00 74.27           C  
ANISOU  124  CE  LYS A  20    15257   6542   6421  -2623   2277  -1494       C  
ATOM    125  NZ  LYS A  20      30.648 145.889 231.806  1.00 77.43           N  
ANISOU  125  NZ  LYS A  20    15996   6672   6753  -2986   2256  -1564       N  
ATOM    126  N   VAL A  21      25.415 141.572 230.200  1.00 65.32           N  
ANISOU  126  N   VAL A  21    13008   6050   5762  -1129   2562  -1064       N  
ATOM    127  CA  VAL A  21      24.088 142.042 230.610  1.00 66.92           C  
ANISOU  127  CA  VAL A  21    13386   6006   6034   -814   2839  -1086       C  
ATOM    128  C   VAL A  21      24.127 142.486 232.072  1.00 69.36           C  
ANISOU  128  C   VAL A  21    14098   6091   6166   -950   2966  -1324       C  
ATOM    129  O   VAL A  21      24.335 141.666 232.984  1.00 68.45           O  
ANISOU  129  O   VAL A  21    13949   6163   5895  -1066   2881  -1442       O  
ATOM    130  CB  VAL A  21      22.967 140.975 230.395  1.00 64.62           C  
ANISOU  130  CB  VAL A  21    12749   5963   5841   -482   2872   -980       C  
ATOM    131  CG1 VAL A  21      21.595 141.545 230.759  1.00 66.64           C  
ANISOU  131  CG1 VAL A  21    13164   5966   6192   -146   3174   -981       C  
ATOM    132  CG2 VAL A  21      22.959 140.465 228.949  1.00 62.28           C  
ANISOU  132  CG2 VAL A  21    12064   5909   5692   -375   2728   -757       C  
ATOM    133  N   GLU A  22      23.942 143.791 232.273  1.00 72.65           N  
ANISOU  133  N   GLU A  22    14908   6097   6599   -940   3169  -1391       N  
ATOM    134  CA  GLU A  22      23.906 144.392 233.598  1.00 75.57           C  
ANISOU  134  CA  GLU A  22    15723   6192   6799  -1056   3329  -1628       C  
ATOM    135  C   GLU A  22      22.962 143.654 234.530  1.00 75.11           C  
ANISOU  135  C   GLU A  22    15625   6238   6675   -849   3464  -1712       C  
ATOM    136  O   GLU A  22      21.806 143.434 234.188  1.00 74.54           O  
ANISOU  136  O   GLU A  22    15372   6188   6762   -478   3622  -1597       O  
ATOM    137  CB  GLU A  22      23.472 145.844 233.495  1.00 79.16           C  
ANISOU  137  CB  GLU A  22    16565   6168   7343   -943   3590  -1650       C  
ATOM    138  CG  GLU A  22      24.506 146.736 232.846  1.00 80.46           C  
ANISOU  138  CG  GLU A  22    16885   6161   7524  -1225   3478  -1613       C  
ATOM    139  CD  GLU A  22      25.525 147.317 233.838  1.00 82.98           C  
ANISOU  139  CD  GLU A  22    17619   6299   7611  -1657   3423  -1847       C  
ATOM    140  OE1 GLU A  22      25.113 148.035 234.789  1.00 86.12           O  
ANISOU  140  OE1 GLU A  22    18450   6358   7914  -1640   3651  -2036       O  
ATOM    141  OE2 GLU A  22      26.743 147.072 233.645  1.00 82.03           O  
ANISOU  141  OE2 GLU A  22    17390   6374   7401  -2019   3154  -1840       O  
ATOM    142  N   GLY A  23      23.480 143.276 235.701  1.00 75.52           N  
ANISOU  142  N   GLY A  23    15842   6366   6489  -1103   3391  -1902       N  
ATOM    143  CA  GLY A  23      22.693 142.667 236.790  1.00 75.68           C  
ANISOU  143  CA  GLY A  23    15907   6455   6394   -968   3531  -2015       C  
ATOM    144  C   GLY A  23      22.853 141.162 236.810  1.00 72.19           C  
ANISOU  144  C   GLY A  23    15055   6462   5911   -994   3302  -1940       C  
ATOM    145  O   GLY A  23      22.666 140.511 237.837  1.00 72.14           O  
ANISOU  145  O   GLY A  23    15094   6576   5741  -1033   3315  -2048       O  
ATOM    146  N   GLU A  24      23.202 140.624 235.645  1.00 69.43           N  
ANISOU  146  N   GLU A  24    14318   6350   5710   -972   3098  -1751       N  
ATOM    147  CA  GLU A  24      23.400 139.193 235.451  1.00 66.07           C  
ANISOU  147  CA  GLU A  24    13483   6338   5281   -982   2872  -1659       C  
ATOM    148  C   GLU A  24      24.874 138.849 235.421  1.00 65.12           C  
ANISOU  148  C   GLU A  24    13294   6405   5044  -1354   2565  -1681       C  
ATOM    149  O   GLU A  24      25.738 139.727 235.351  1.00 66.83           O  
ANISOU  149  O   GLU A  24    13729   6455   5211  -1603   2512  -1736       O  
ATOM    150  CB  GLU A  24      22.780 138.720 234.136  1.00 63.69           C  
ANISOU  150  CB  GLU A  24    12780   6200   5219   -700   2850  -1434       C  
ATOM    151  CG  GLU A  24      21.299 139.001 233.988  1.00 64.54           C  
ANISOU  151  CG  GLU A  24    12873   6169   5480   -312   3127  -1364       C  
ATOM    152  CD  GLU A  24      20.621 138.061 232.995  1.00 61.80           C  
ANISOU  152  CD  GLU A  24    12072   6100   5310    -67   3054  -1159       C  
ATOM    153  OE1 GLU A  24      21.067 136.889 232.855  1.00 59.17           O  
ANISOU  153  OE1 GLU A  24    11461   6087   4935   -170   2831  -1122       O  
ATOM    154  OE2 GLU A  24      19.625 138.502 232.373  1.00 62.51           O  
ANISOU  154  OE2 GLU A  24    12093   6080   5579    229   3222  -1034       O  
ATOM    155  N   ASP A  25      25.148 137.555 235.452  1.00 62.53           N  
ANISOU  155  N   ASP A  25    12649   6425   4684  -1387   2365  -1626       N  
ATOM    156  CA  ASP A  25      26.492 137.079 235.546  1.00 61.73           C  
ANISOU  156  CA  ASP A  25    12447   6534   4474  -1710   2078  -1640       C  
ATOM    157  C   ASP A  25      26.685 136.177 234.367  1.00 58.68           C  
ANISOU  157  C   ASP A  25    11612   6434   4248  -1607   1913  -1458       C  
ATOM    158  O   ASP A  25      26.120 135.094 234.303  1.00 56.60           O  
ANISOU  158  O   ASP A  25    11091   6382   4031  -1427   1887  -1391       O  
ATOM    159  CB  ASP A  25      26.703 136.353 236.886  1.00 62.01           C  
ANISOU  159  CB  ASP A  25    12572   6702   4289  -1863   1996  -1762       C  
ATOM    160  CG  ASP A  25      27.906 135.415 236.865  1.00 60.42           C  
ANISOU  160  CG  ASP A  25    12116   6819   4022  -2101   1673  -1714       C  
ATOM    161  OD1 ASP A  25      29.059 135.868 236.583  1.00 61.17           O  
ANISOU  161  OD1 ASP A  25    12229   6921   4091  -2371   1511  -1714       O  
ATOM    162  OD2 ASP A  25      27.679 134.206 237.111  1.00 58.54           O  
ANISOU  162  OD2 ASP A  25    11647   6825   3770  -2009   1587  -1666       O  
ATOM    163  N   ARG A  26      27.470 136.657 233.415  1.00 58.62           N  
ANISOU  163  N   ARG A  26    11528   6420   4323  -1728   1813  -1380       N  
ATOM    164  CA  ARG A  26      27.664 135.991 232.127  1.00 56.11           C  
ANISOU  164  CA  ARG A  26    10818   6339   4161  -1628   1687  -1208       C  
ATOM    165  C   ARG A  26      29.110 135.586 231.988  1.00 55.55           C  
ANISOU  165  C   ARG A  26    10593   6484   4028  -1922   1429  -1196       C  
ATOM    166  O   ARG A  26      29.590 135.380 230.895  1.00 54.30           O  
ANISOU  166  O   ARG A  26    10185   6469   3977  -1923   1332  -1076       O  
ATOM    167  CB  ARG A  26      27.272 136.920 231.000  1.00 56.69           C  
ANISOU  167  CB  ARG A  26    10915   6229   4394  -1487   1815  -1099       C  
ATOM    168  CG  ARG A  26      25.833 137.322 230.992  1.00 57.36           C  
ANISOU  168  CG  ARG A  26    11101   6117   4576  -1164   2066  -1075       C  
ATOM    169  CD  ARG A  26      24.941 136.155 230.717  1.00 54.97           C  
ANISOU  169  CD  ARG A  26    10482   6050   4355   -902   2061   -983       C  
ATOM    170  NE  ARG A  26      23.558 136.605 230.608  1.00 55.87           N  
ANISOU  170  NE  ARG A  26    10656   5988   4583   -588   2301   -932       N  
ATOM    171  CZ  ARG A  26      22.826 136.669 229.487  1.00 55.20           C  
ANISOU  171  CZ  ARG A  26    10376   5924   4672   -345   2353   -762       C  
ATOM    172  NH1 ARG A  26      23.286 136.290 228.307  1.00 53.50           N  
ANISOU  172  NH1 ARG A  26     9898   5898   4531   -371   2192   -629       N  
ATOM    173  NH2 ARG A  26      21.586 137.109 229.556  1.00 56.43           N  
ANISOU  173  NH2 ARG A  26    10596   5918   4927    -67   2573   -720       N  
ATOM    174  N   GLY A  27      29.809 135.491 233.115  1.00 56.72           N  
ANISOU  174  N   GLY A  27    10893   6661   3998  -2176   1321  -1319       N  
ATOM    175  CA  GLY A  27      31.165 134.976 233.151  1.00 56.38           C  
ANISOU  175  CA  GLY A  27    10672   6857   3891  -2448   1062  -1301       C  
ATOM    176  C   GLY A  27      32.194 136.067 233.299  1.00 58.91           C  
ANISOU  176  C   GLY A  27    11215   7036   4134  -2785   1001  -1361       C  
ATOM    177  O   GLY A  27      31.866 137.258 233.306  1.00 60.93           O  
ANISOU  177  O   GLY A  27    11781   6982   4389  -2807   1167  -1418       O  
ATOM    178  N   ALA A  28      33.446 135.638 233.396  1.00 58.95           N  
ANISOU  178  N   ALA A  28    11048   7269   4081  -3045    763  -1338       N  
ATOM    179  CA  ALA A  28      34.554 136.509 233.688  1.00 61.51           C  
ANISOU  179  CA  ALA A  28    11546   7517   4308  -3419    658  -1393       C  
ATOM    180  C   ALA A  28      34.848 137.493 232.564  1.00 62.27           C  
ANISOU  180  C   ALA A  28    11658   7472   4531  -3472    726  -1315       C  
ATOM    181  O   ALA A  28      35.307 138.595 232.819  1.00 64.93           O  
ANISOU  181  O   ALA A  28    12281   7593   4797  -3730    745  -1385       O  
ATOM    182  CB  ALA A  28      35.776 135.685 234.002  1.00 61.30           C  
ANISOU  182  CB  ALA A  28    11263   7813   4214  -3650    379  -1355       C  
ATOM    183  N   ASN A  29      34.608 137.115 231.319  1.00 60.16           N  
ANISOU  183  N   ASN A  29    11099   7320   4438  -3249    760  -1169       N  
ATOM    184  CA  ASN A  29      34.981 137.993 230.222  1.00 60.97           C  
ANISOU  184  CA  ASN A  29    11198   7320   4647  -3320    807  -1076       C  
ATOM    185  C   ASN A  29      34.000 137.956 229.020  1.00 59.22           C  
ANISOU  185  C   ASN A  29    10848   7056   4596  -2970    965   -950       C  
ATOM    186  O   ASN A  29      34.292 137.371 227.982  1.00 57.50           O  
ANISOU  186  O   ASN A  29    10304   7065   4479  -2891    899   -821       O  
ATOM    187  CB  ASN A  29      36.444 137.717 229.861  1.00 61.20           C  
ANISOU  187  CB  ASN A  29    10965   7616   4673  -3603    589  -1005       C  
ATOM    188  CG  ASN A  29      36.847 138.249 228.492  1.00 61.31           C  
ANISOU  188  CG  ASN A  29    10846   7631   4816  -3628    624   -866       C  
ATOM    189  OD1 ASN A  29      36.526 139.374 228.093  1.00 62.82           O  
ANISOU  189  OD1 ASN A  29    11285   7538   5045  -3642    768   -854       O  
ATOM    190  ND2 ASN A  29      37.587 137.431 227.774  1.00 59.89           N  
ANISOU  190  ND2 ASN A  29    10279   7774   4702  -3636    496   -757       N  
ATOM    191  N   PRO A  30      32.821 138.600 229.176  1.00 59.91           N  
ANISOU  191  N   PRO A  30    11198   6851   4712  -2760   1179   -988       N  
ATOM    192  CA  PRO A  30      31.738 138.487 228.211  1.00 58.40           C  
ANISOU  192  CA  PRO A  30    10886   6633   4672  -2408   1319   -867       C  
ATOM    193  C   PRO A  30      31.772 139.598 227.154  1.00 59.74           C  
ANISOU  193  C   PRO A  30    11152   6603   4944  -2416   1416   -756       C  
ATOM    194  O   PRO A  30      32.405 140.626 227.382  1.00 62.22           O  
ANISOU  194  O   PRO A  30    11724   6709   5207  -2673   1426   -806       O  
ATOM    195  CB  PRO A  30      30.495 138.596 229.108  1.00 58.88           C  
ANISOU  195  CB  PRO A  30    11178   6491   4703  -2191   1497   -966       C  
ATOM    196  CG  PRO A  30      30.923 139.440 230.270  1.00 61.69           C  
ANISOU  196  CG  PRO A  30    11923   6611   4908  -2455   1523  -1136       C  
ATOM    197  CD  PRO A  30      32.424 139.444 230.326  1.00 62.37           C  
ANISOU  197  CD  PRO A  30    11941   6848   4909  -2838   1304  -1149       C  
ATOM    198  N   MET A  31      31.093 139.373 226.020  1.00 58.26           N  
ANISOU  198  N   MET A  31    10766   6481   4889  -2148   1477   -604       N  
ATOM    199  CA  MET A  31      31.150 140.249 224.821  1.00 59.23           C  
ANISOU  199  CA  MET A  31    10915   6479   5112  -2137   1542   -456       C  
ATOM    200  C   MET A  31      30.422 141.578 224.991  1.00 61.80           C  
ANISOU  200  C   MET A  31    11619   6383   5479  -2055   1746   -466       C  
ATOM    201  O   MET A  31      29.340 141.616 225.589  1.00 62.01           O  
ANISOU  201  O   MET A  31    11780   6257   5523  -1821   1887   -523       O  
ATOM    202  CB  MET A  31      30.561 139.537 223.615  1.00 57.00           C  
ANISOU  202  CB  MET A  31    10313   6407   4936  -1868   1537   -292       C  
ATOM    203  CG  MET A  31      31.307 138.323 223.191  1.00 54.77           C  
ANISOU  203  CG  MET A  31     9667   6511   4632  -1934   1360   -262       C  
ATOM    204  SD  MET A  31      30.610 137.584 221.699  1.00 52.59           S  
ANISOU  204  SD  MET A  31     9066   6454   4461  -1645   1363    -80       S  
ATOM    205  CE  MET A  31      29.315 136.536 222.368  1.00 50.68           C  
ANISOU  205  CE  MET A  31     8735   6287   4236  -1344   1397   -139       C  
ATOM    206  N   ASP A  32      30.998 142.647 224.436  1.00 63.87           N  
ANISOU  206  N   ASP A  32    12044   6458   5765  -2235   1770   -401       N  
ATOM    207  CA  ASP A  32      30.596 144.032 224.738  1.00 66.96           C  
ANISOU  207  CA  ASP A  32    12858   6405   6180  -2240   1951   -435       C  
ATOM    208  C   ASP A  32      31.093 144.980 223.620  1.00 68.56           C  
ANISOU  208  C   ASP A  32    13118   6476   6454  -2361   1965   -275       C  
ATOM    209  O   ASP A  32      32.302 145.193 223.449  1.00 69.33           O  
ANISOU  209  O   ASP A  32    13198   6652   6494  -2702   1843   -274       O  
ATOM    210  CB  ASP A  32      31.103 144.446 226.146  1.00 69.00           C  
ANISOU  210  CB  ASP A  32    13442   6484   6290  -2513   1947   -660       C  
ATOM    211  CG  ASP A  32      30.725 145.899 226.561  1.00 72.59           C  
ANISOU  211  CG  ASP A  32    14386   6440   6754  -2537   2148   -729       C  
ATOM    212  OD1 ASP A  32      29.826 146.538 225.969  1.00 73.48           O  
ANISOU  212  OD1 ASP A  32    14602   6317   7000  -2267   2323   -616       O  
ATOM    213  OD2 ASP A  32      31.341 146.408 227.535  1.00 74.77           O  
ANISOU  213  OD2 ASP A  32    14961   6550   6896  -2836   2130   -903       O  
ATOM    214  N   PRO A  33      30.148 145.557 222.861  1.00 69.23           N  
ANISOU  214  N   PRO A  33    13269   6368   6668  -2082   2113   -125       N  
ATOM    215  CA  PRO A  33      28.709 145.391 223.054  1.00 68.74           C  
ANISOU  215  CA  PRO A  33    13219   6209   6689  -1681   2264   -109       C  
ATOM    216  C   PRO A  33      28.227 143.991 222.689  1.00 65.32           C  
ANISOU  216  C   PRO A  33    12369   6173   6278  -1462   2169    -50       C  
ATOM    217  O   PRO A  33      28.731 143.390 221.731  1.00 63.60           O  
ANISOU  217  O   PRO A  33    11852   6248   6066  -1514   2032     68       O  
ATOM    218  CB  PRO A  33      28.109 146.419 222.104  1.00 70.63           C  
ANISOU  218  CB  PRO A  33    13591   6179   7066  -1501   2401     84       C  
ATOM    219  CG  PRO A  33      29.131 146.571 221.042  1.00 70.58           C  
ANISOU  219  CG  PRO A  33    13454   6312   7049  -1739   2273    221       C  
ATOM    220  CD  PRO A  33      30.445 146.476 221.753  1.00 70.88           C  
ANISOU  220  CD  PRO A  33    13548   6432   6951  -2152   2144     55       C  
ATOM    221  N   PRO A  34      27.236 143.485 223.433  1.00 64.55           N  
ANISOU  221  N   PRO A  34    12260   6076   6189  -1219   2252   -130       N  
ATOM    222  CA  PRO A  34      26.676 142.144 223.227  1.00 61.54           C  
ANISOU  222  CA  PRO A  34    11515   6041   5827  -1014   2173    -90       C  
ATOM    223  C   PRO A  34      26.102 141.886 221.815  1.00 60.38           C  
ANISOU  223  C   PRO A  34    11098   6049   5796   -789   2151    141       C  
ATOM    224  O   PRO A  34      25.940 142.825 221.011  1.00 62.08           O  
ANISOU  224  O   PRO A  34    11421   6075   6091   -734   2223    290       O  
ATOM    225  CB  PRO A  34      25.583 142.039 224.310  1.00 61.96           C  
ANISOU  225  CB  PRO A  34    11699   5958   5885   -791   2327   -203       C  
ATOM    226  CG  PRO A  34      25.280 143.401 224.678  1.00 65.20           C  
ANISOU  226  CG  PRO A  34    12501   5940   6330   -765   2522   -237       C  
ATOM    227  CD  PRO A  34      26.521 144.216 224.486  1.00 66.81           C  
ANISOU  227  CD  PRO A  34    12899   6011   6474  -1114   2451   -259       C  
ATOM    228  N   ARG A  35      25.834 140.614 221.522  1.00 57.68           N  
ANISOU  228  N   ARG A  35    10419   6047   5450   -676   2043    171       N  
ATOM    229  CA  ARG A  35      25.238 140.241 220.242  1.00 56.58           C  
ANISOU  229  CA  ARG A  35    10019   6084   5395   -474   2007    373       C  
ATOM    230  C   ARG A  35      23.821 139.784 220.527  1.00 56.02           C  
ANISOU  230  C   ARG A  35     9854   6030   5401   -148   2095    400       C  
ATOM    231  O   ARG A  35      23.545 139.285 221.617  1.00 55.46           O  
ANISOU  231  O   ARG A  35     9812   5971   5291   -122   2128    252       O  
ATOM    232  CB  ARG A  35      26.035 139.121 219.542  1.00 54.17           C  
ANISOU  232  CB  ARG A  35     9396   6159   5025   -605   1816    394       C  
ATOM    233  CG  ARG A  35      27.451 139.505 219.118  1.00 54.78           C  
ANISOU  233  CG  ARG A  35     9506   6270   5037   -919   1730    395       C  
ATOM    234  CD  ARG A  35      28.302 138.288 218.762  1.00 52.53           C  
ANISOU  234  CD  ARG A  35     8919   6358   4683  -1047   1562    365       C  
ATOM    235  NE  ARG A  35      29.682 138.660 218.397  1.00 53.36           N  
ANISOU  235  NE  ARG A  35     9031   6511   4733  -1348   1492    371       N  
ATOM    236  CZ  ARG A  35      30.606 137.806 217.935  1.00 52.02           C  
ANISOU  236  CZ  ARG A  35     8606   6645   4513  -1480   1367    367       C  
ATOM    237  NH1 ARG A  35      30.317 136.512 217.773  1.00 49.74           N  
ANISOU  237  NH1 ARG A  35     8058   6623   4218  -1340   1293    348       N  
ATOM    238  NH2 ARG A  35      31.827 138.231 217.637  1.00 53.12           N  
ANISOU  238  NH2 ARG A  35     8749   6820   4612  -1752   1322    382       N  
ATOM    239  N   ARG A  36      22.917 139.967 219.564  1.00 56.37           N  
ANISOU  239  N   ARG A  36     9784   6082   5553     91   2132    599       N  
ATOM    240  CA  ARG A  36      21.507 139.589 219.733  1.00 56.17           C  
ANISOU  240  CA  ARG A  36     9637   6085   5620    407   2215    659       C  
ATOM    241  C   ARG A  36      21.060 138.699 218.573  1.00 54.43           C  
ANISOU  241  C   ARG A  36     9071   6183   5427    524   2082    824       C  
ATOM    242  O   ARG A  36      21.630 138.733 217.472  1.00 54.13           O  
ANISOU  242  O   ARG A  36     8944   6262   5361    422   1976    937       O  
ATOM    243  CB  ARG A  36      20.613 140.835 219.852  1.00 59.10           C  
ANISOU  243  CB  ARG A  36    10236   6102   6116    630   2420    750       C  
ATOM    244  CG  ARG A  36      21.350 142.079 220.356  1.00 61.50           C  
ANISOU  244  CG  ARG A  36    10926   6048   6393    454   2524    657       C  
ATOM    245  CD  ARG A  36      20.497 143.326 220.472  1.00 64.67           C  
ANISOU  245  CD  ARG A  36    11579   6066   6926    685   2743    741       C  
ATOM    246  NE  ARG A  36      19.856 143.427 221.794  1.00 65.71           N  
ANISOU  246  NE  ARG A  36    11884   6018   7065    810   2924    574       N  
ATOM    247  CZ  ARG A  36      20.355 144.069 222.856  1.00 67.37           C  
ANISOU  247  CZ  ARG A  36    12447   5952   7198    650   3035    371       C  
ATOM    248  NH1 ARG A  36      21.524 144.697 222.803  1.00 68.24           N  
ANISOU  248  NH1 ARG A  36    12778   5925   7226    342   2975    307       N  
ATOM    249  NH2 ARG A  36      19.667 144.094 223.982  1.00 68.37           N  
ANISOU  249  NH2 ARG A  36    12713   5942   7323    790   3211    232       N  
ATOM    250  N   ARG A  37      20.066 137.869 218.845  1.00 53.39           N  
ANISOU  250  N   ARG A  37     8751   6199   5336    717   2089    829       N  
ATOM    251  CA  ARG A  37      19.377 137.118 217.810  1.00 52.28           C  
ANISOU  251  CA  ARG A  37     8307   6323   5233    857   1983    993       C  
ATOM    252  C   ARG A  37      17.969 136.749 218.248  1.00 52.50           C  
ANISOU  252  C   ARG A  37     8209   6380   5359   1125   2067   1038       C  
ATOM    253  O   ARG A  37      17.640 136.852 219.436  1.00 53.05           O  
ANISOU  253  O   ARG A  37     8406   6307   5443   1181   2200    908       O  
ATOM    254  CB  ARG A  37      20.159 135.889 217.395  1.00 49.71           C  
ANISOU  254  CB  ARG A  37     7771   6321   4797    675   1794    928       C  
ATOM    255  CG  ARG A  37      20.996 135.334 218.465  1.00 48.48           C  
ANISOU  255  CG  ARG A  37     7678   6194   4548    487   1766    706       C  
ATOM    256  CD  ARG A  37      21.173 133.886 218.243  1.00 46.07           C  
ANISOU  256  CD  ARG A  37     7115   6207   4182    436   1615    660       C  
ATOM    257  NE  ARG A  37      22.170 133.660 217.227  1.00 45.34           N  
ANISOU  257  NE  ARG A  37     6931   6274   4022    271   1490    696       N  
ATOM    258  CZ  ARG A  37      22.626 132.461 216.887  1.00 43.45           C  
ANISOU  258  CZ  ARG A  37     6491   6300   3717    190   1357    646       C  
ATOM    259  NH1 ARG A  37      22.166 131.342 217.474  1.00 42.00           N  
ANISOU  259  NH1 ARG A  37     6178   6251   3529    251   1316    564       N  
ATOM    260  NH2 ARG A  37      23.557 132.394 215.945  1.00 43.19           N  
ANISOU  260  NH2 ARG A  37     6395   6391   3623     49   1275    682       N  
ATOM    261  N   VAL A  38      17.125 136.367 217.286  1.00 52.35           N  
ANISOU  261  N   VAL A  38     7946   6544   5401   1285   1994   1227       N  
ATOM    262  CA  VAL A  38      15.705 136.088 217.566  1.00 52.96           C  
ANISOU  262  CA  VAL A  38     7867   6665   5591   1548   2070   1312       C  
ATOM    263  C   VAL A  38      15.538 134.598 217.758  1.00 50.57           C  
ANISOU  263  C   VAL A  38     7322   6665   5227   1493   1947   1228       C  
ATOM    264  O   VAL A  38      16.114 133.796 217.014  1.00 48.82           O  
ANISOU  264  O   VAL A  38     6959   6676   4915   1343   1770   1226       O  
ATOM    265  CB  VAL A  38      14.688 136.663 216.473  1.00 54.87           C  
ANISOU  265  CB  VAL A  38     7979   6909   5959   1783   2070   1600       C  
ATOM    266  CG1 VAL A  38      14.554 138.188 216.594  1.00 57.79           C  
ANISOU  266  CG1 VAL A  38     8612   6913   6433   1913   2250   1683       C  
ATOM    267  CG2 VAL A  38      15.074 136.265 215.010  1.00 53.94           C  
ANISOU  267  CG2 VAL A  38     7695   7035   5767   1673   1861   1740       C  
ATOM    268  N   ASP A  39      14.812 134.237 218.807  1.00 50.63           N  
ANISOU  268  N   ASP A  39     7306   6655   5276   1601   2054   1148       N  
ATOM    269  CA  ASP A  39      14.386 132.876 219.001  1.00 48.83           C  
ANISOU  269  CA  ASP A  39     6842   6694   5019   1588   1959   1105       C  
ATOM    270  C   ASP A  39      12.875 132.954 219.035  1.00 50.38           C  
ANISOU  270  C   ASP A  39     6873   6910   5357   1857   2057   1261       C  
ATOM    271  O   ASP A  39      12.296 133.328 220.059  1.00 51.66           O  
ANISOU  271  O   ASP A  39     7131   6915   5584   1990   2248   1208       O  
ATOM    272  CB  ASP A  39      14.924 132.283 220.301  1.00 47.59           C  
ANISOU  272  CB  ASP A  39     6794   6520   4769   1451   1993    872       C  
ATOM    273  CG  ASP A  39      14.423 130.858 220.535  1.00 45.93           C  
ANISOU  273  CG  ASP A  39     6348   6566   4536   1443   1902    840       C  
ATOM    274  OD1 ASP A  39      13.345 130.514 219.998  1.00 48.27           O  
ANISOU  274  OD1 ASP A  39     6419   7002   4920   1593   1879    993       O  
ATOM    275  OD2 ASP A  39      15.097 130.064 221.239  1.00 44.76           O  
ANISOU  275  OD2 ASP A  39     6235   6485   4287   1280   1846    674       O  
ATOM    276  N   PRO A  40      12.223 132.581 217.916  1.00 50.43           N  
ANISOU  276  N   PRO A  40     6625   7125   5410   1934   1927   1455       N  
ATOM    277  CA  PRO A  40      10.764 132.762 217.843  1.00 52.32           C  
ANISOU  277  CA  PRO A  40     6679   7396   5804   2197   2009   1642       C  
ATOM    278  C   PRO A  40       9.997 131.809 218.780  1.00 51.75           C  
ANISOU  278  C   PRO A  40     6456   7451   5754   2242   2062   1565       C  
ATOM    279  O   PRO A  40       8.813 132.020 219.051  1.00 53.56           O  
ANISOU  279  O   PRO A  40     6555   7675   6119   2464   2186   1686       O  
ATOM    280  CB  PRO A  40      10.448 132.465 216.377  1.00 52.33           C  
ANISOU  280  CB  PRO A  40     6451   7626   5806   2200   1808   1852       C  
ATOM    281  CG  PRO A  40      11.729 131.785 215.785  1.00 49.93           C  
ANISOU  281  CG  PRO A  40     6188   7456   5327   1919   1620   1730       C  
ATOM    282  CD  PRO A  40      12.740 131.671 216.867  1.00 48.57           C  
ANISOU  282  CD  PRO A  40     6232   7152   5071   1764   1693   1477       C  
ATOM    283  N   LEU A  41      10.677 130.784 219.288  1.00 49.43           N  
ANISOU  283  N   LEU A  41     6179   7269   5334   2035   1978   1375       N  
ATOM    284  CA  LEU A  41      10.039 129.789 220.136  1.00 48.80           C  
ANISOU  284  CA  LEU A  41     5964   7319   5257   2043   2009   1305       C  
ATOM    285  C   LEU A  41      10.461 129.874 221.608  1.00 48.62           C  
ANISOU  285  C   LEU A  41     6174   7125   5174   1991   2172   1092       C  
ATOM    286  O   LEU A  41      10.250 128.944 222.374  1.00 47.70           O  
ANISOU  286  O   LEU A  41     5993   7116   5015   1934   2175    999       O  
ATOM    287  CB  LEU A  41      10.326 128.398 219.585  1.00 46.55           C  
ANISOU  287  CB  LEU A  41     5498   7310   4878   1860   1779   1273       C  
ATOM    288  CG  LEU A  41       9.857 128.070 218.181  1.00 46.69           C  
ANISOU  288  CG  LEU A  41     5280   7540   4920   1874   1597   1462       C  
ATOM    289  CD1 LEU A  41      10.235 126.644 217.870  1.00 44.54           C  
ANISOU  289  CD1 LEU A  41     4889   7497   4538   1675   1403   1374       C  
ATOM    290  CD2 LEU A  41       8.375 128.203 218.101  1.00 48.70           C  
ANISOU  290  CD2 LEU A  41     5309   7871   5323   2087   1661   1658       C  
ATOM    291  N   PHE A  42      11.056 130.999 221.991  1.00 49.68           N  
ANISOU  291  N   PHE A  42     6591   6990   5295   1998   2301   1019       N  
ATOM    292  CA  PHE A  42      11.513 131.197 223.367  1.00 49.84           C  
ANISOU  292  CA  PHE A  42     6870   6833   5235   1929   2450    811       C  
ATOM    293  C   PHE A  42      10.409 130.944 224.380  1.00 51.00           C  
ANISOU  293  C   PHE A  42     6955   6986   5438   2084   2636    800       C  
ATOM    294  O   PHE A  42      10.615 130.203 225.339  1.00 50.02           O  
ANISOU  294  O   PHE A  42     6876   6915   5213   1969   2646    652       O  
ATOM    295  CB  PHE A  42      12.071 132.595 223.568  1.00 51.52           C  
ANISOU  295  CB  PHE A  42     7397   6731   5448   1944   2587    762       C  
ATOM    296  CG  PHE A  42      12.807 132.758 224.848  1.00 51.54           C  
ANISOU  296  CG  PHE A  42     7690   6569   5323   1799   2684    531       C  
ATOM    297  CD1 PHE A  42      14.155 132.450 224.928  1.00 49.83           C  
ANISOU  297  CD1 PHE A  42     7591   6382   4961   1526   2529    392       C  
ATOM    298  CD2 PHE A  42      12.159 133.231 225.980  1.00 53.49           C  
ANISOU  298  CD2 PHE A  42     8094   6639   5590   1933   2933    456       C  
ATOM    299  CE1 PHE A  42      14.853 132.609 226.102  1.00 50.05           C  
ANISOU  299  CE1 PHE A  42     7882   6274   4861   1375   2594    191       C  
ATOM    300  CE2 PHE A  42      12.851 133.386 227.165  1.00 53.70           C  
ANISOU  300  CE2 PHE A  42     8410   6520   5473   1778   3012    239       C  
ATOM    301  CZ  PHE A  42      14.211 133.062 227.210  1.00 51.94           C  
ANISOU  301  CZ  PHE A  42     8293   6340   5100   1489   2826    112       C  
ATOM    302  N   TRP A  43       9.243 131.559 224.150  1.00 53.26           N  
ANISOU  302  N   TRP A  43     7128   7223   5887   2349   2783    969       N  
ATOM    303  CA  TRP A  43       8.037 131.345 224.962  1.00 54.76           C  
ANISOU  303  CA  TRP A  43     7199   7446   6159   2531   2975   1001       C  
ATOM    304  C   TRP A  43       7.839 129.912 225.499  1.00 53.01           C  
ANISOU  304  C   TRP A  43     6809   7472   5861   2401   2889    932       C  
ATOM    305  O   TRP A  43       7.471 129.745 226.653  1.00 53.75           O  
ANISOU  305  O   TRP A  43     6976   7524   5923   2431   3064    834       O  
ATOM    306  CB  TRP A  43       6.770 131.901 224.265  1.00 57.13           C  
ANISOU  306  CB  TRP A  43     7269   7770   6668   2824   3060   1256       C  
ATOM    307  CG  TRP A  43       6.297 131.138 223.092  1.00 56.23           C  
ANISOU  307  CG  TRP A  43     6805   7950   6610   2812   2828   1449       C  
ATOM    308  CD1 TRP A  43       6.731 131.268 221.797  1.00 55.52           C  
ANISOU  308  CD1 TRP A  43     6653   7928   6515   2749   2618   1564       C  
ATOM    309  CD2 TRP A  43       5.299 130.109 223.076  1.00 56.12           C  
ANISOU  309  CD2 TRP A  43     6461   8211   6653   2844   2775   1549       C  
ATOM    310  NE1 TRP A  43       6.066 130.378 220.976  1.00 55.00           N  
ANISOU  310  NE1 TRP A  43     6250   8160   6486   2737   2433   1721       N  
ATOM    311  CE2 TRP A  43       5.190 129.649 221.735  1.00 55.34           C  
ANISOU  311  CE2 TRP A  43     6121   8333   6572   2787   2518   1715       C  
ATOM    312  CE3 TRP A  43       4.482 129.527 224.059  1.00 56.78           C  
ANISOU  312  CE3 TRP A  43     6431   8377   6764   2901   2921   1518       C  
ATOM    313  CZ2 TRP A  43       4.300 128.642 221.359  1.00 55.23           C  
ANISOU  313  CZ2 TRP A  43     5769   8611   6605   2776   2394   1843       C  
ATOM    314  CZ3 TRP A  43       3.595 128.521 223.683  1.00 56.62           C  
ANISOU  314  CZ3 TRP A  43     6059   8652   6803   2893   2802   1656       C  
ATOM    315  CH2 TRP A  43       3.511 128.091 222.347  1.00 55.87           C  
ANISOU  315  CH2 TRP A  43     5737   8765   6727   2825   2536   1813       C  
ATOM    316  N   LEU A  44       8.116 128.883 224.697  1.00 50.84           N  
ANISOU  316  N   LEU A  44     6335   7439   5544   2247   2629    976       N  
ATOM    317  CA  LEU A  44       7.956 127.480 225.162  1.00 49.28           C  
ANISOU  317  CA  LEU A  44     5990   7457   5277   2113   2537    916       C  
ATOM    318  C   LEU A  44       8.572 127.191 226.536  1.00 48.66           C  
ANISOU  318  C   LEU A  44     6150   7285   5055   1980   2627    698       C  
ATOM    319  O   LEU A  44       8.206 126.220 227.216  1.00 48.16           O  
ANISOU  319  O   LEU A  44     5999   7351   4950   1921   2632    660       O  
ATOM    320  CB  LEU A  44       8.442 126.472 224.112  1.00 47.03           C  
ANISOU  320  CB  LEU A  44     5537   7393   4941   1938   2244    950       C  
ATOM    321  CG  LEU A  44       7.570 126.473 222.847  1.00 47.85           C  
ANISOU  321  CG  LEU A  44     5356   7656   5168   2053   2142   1179       C  
ATOM    322  CD1 LEU A  44       8.163 125.626 221.733  1.00 45.89           C  
ANISOU  322  CD1 LEU A  44     4999   7594   4844   1873   1865   1193       C  
ATOM    323  CD2 LEU A  44       6.174 125.994 223.171  1.00 49.23           C  
ANISOU  323  CD2 LEU A  44     5274   7977   5453   2180   2226   1301       C  
ATOM    324  N   ARG A  45       9.502 128.043 226.935  1.00 48.89           N  
ANISOU  324  N   ARG A  45     6484   7089   5002   1920   2690    565       N  
ATOM    325  CA  ARG A  45      10.017 127.990 228.278  1.00 48.92           C  
ANISOU  325  CA  ARG A  45     6741   6981   4865   1809   2795    370       C  
ATOM    326  C   ARG A  45       9.052 128.631 229.291  1.00 51.55           C  
ANISOU  326  C   ARG A  45     7172   7171   5243   2001   3106    355       C  
ATOM    327  O   ARG A  45       8.721 129.804 229.191  1.00 53.64           O  
ANISOU  327  O   ARG A  45     7546   7237   5597   2178   3281    396       O  
ATOM    328  CB  ARG A  45      11.400 128.641 228.368  1.00 48.41           C  
ANISOU  328  CB  ARG A  45     6969   6741   4682   1642   2734    228       C  
ATOM    329  CG  ARG A  45      11.889 128.759 229.811  1.00 48.99           C  
ANISOU  329  CG  ARG A  45     7336   6680   4599   1527   2853     30       C  
ATOM    330  CD  ARG A  45      13.323 129.097 229.872  1.00 48.19           C  
ANISOU  330  CD  ARG A  45     7464   6478   4370   1308   2729   -101       C  
ATOM    331  NE  ARG A  45      13.721 129.608 231.165  1.00 49.55           N  
ANISOU  331  NE  ARG A  45     7962   6465   4399   1219   2869   -278       N  
ATOM    332  CZ  ARG A  45      14.746 130.429 231.340  1.00 50.11           C  
ANISOU  332  CZ  ARG A  45     8304   6355   4380   1073   2851   -389       C  
ATOM    333  NH1 ARG A  45      15.473 130.839 230.318  1.00 49.41           N  
ANISOU  333  NH1 ARG A  45     8190   6245   4337   1007   2712   -337       N  
ATOM    334  NH2 ARG A  45      15.043 130.854 232.548  1.00 51.57           N  
ANISOU  334  NH2 ARG A  45     8793   6381   4418    979   2975   -554       N  
ATOM    335  N   ASP A  46       8.596 127.837 230.249  1.00 51.58           N  
ANISOU  335  N   ASP A  46     7137   7275   5186   1971   3181    302       N  
ATOM    336  CA  ASP A  46       8.001 128.360 231.481  1.00 53.95           C  
ANISOU  336  CA  ASP A  46     7614   7428   5457   2088   3485    221       C  
ATOM    337  C   ASP A  46       8.676 127.713 232.672  1.00 53.12           C  
ANISOU  337  C   ASP A  46     7712   7333   5139   1870   3467     36       C  
ATOM    338  O   ASP A  46       8.625 126.491 232.867  1.00 51.64           O  
ANISOU  338  O   ASP A  46     7371   7352   4898   1750   3338     48       O  
ATOM    339  CB  ASP A  46       6.479 128.161 231.574  1.00 55.73           C  
ANISOU  339  CB  ASP A  46     7571   7769   5835   2318   3667    374       C  
ATOM    340  CG  ASP A  46       5.953 128.419 232.976  1.00 57.96           C  
ANISOU  340  CG  ASP A  46     8033   7943   6047   2396   3976    266       C  
ATOM    341  OD1 ASP A  46       6.465 129.345 233.637  1.00 59.25           O  
ANISOU  341  OD1 ASP A  46     8546   7852   6115   2393   4131    112       O  
ATOM    342  OD2 ASP A  46       5.040 127.696 233.439  1.00 58.58           O  
ANISOU  342  OD2 ASP A  46     7916   8188   6154   2448   4070    329       O  
ATOM    343  N   ASP A  47       9.303 128.552 233.472  1.00 54.30           N  
ANISOU  343  N   ASP A  47     8218   7251   5162   1814   3593   -130       N  
ATOM    344  CA  ASP A  47      10.019 128.044 234.617  1.00 53.79           C  
ANISOU  344  CA  ASP A  47     8374   7190   4876   1594   3562   -303       C  
ATOM    345  C   ASP A  47       9.090 127.392 235.624  1.00 54.87           C  
ANISOU  345  C   ASP A  47     8454   7428   4966   1647   3738   -305       C  
ATOM    346  O   ASP A  47       9.445 126.417 236.267  1.00 53.74           O  
ANISOU  346  O   ASP A  47     8327   7413   4681   1467   3630   -363       O  
ATOM    347  CB  ASP A  47      10.834 129.151 235.252  1.00 55.22           C  
ANISOU  347  CB  ASP A  47     8959   7098   4922   1510   3662   -479       C  
ATOM    348  CG  ASP A  47      12.123 129.401 234.506  1.00 53.59           C  
ANISOU  348  CG  ASP A  47     8823   6851   4686   1332   3414   -510       C  
ATOM    349  OD1 ASP A  47      12.397 128.720 233.467  1.00 51.33           O  
ANISOU  349  OD1 ASP A  47     8275   6747   4481   1288   3175   -398       O  
ATOM    350  OD2 ASP A  47      12.866 130.281 234.989  1.00 56.91           O  
ANISOU  350  OD2 ASP A  47     9572   7058   4994   1227   3467   -651       O  
ATOM    351  N   ASN A  48       7.879 127.911 235.716  1.00 57.17           N  
ANISOU  351  N   ASN A  48     8661   7671   5391   1902   4008   -223       N  
ATOM    352  CA  ASN A  48       6.910 127.333 236.610  1.00 58.47           C  
ANISOU  352  CA  ASN A  48     8742   7946   5529   1967   4201   -206       C  
ATOM    353  C   ASN A  48       6.175 126.099 236.093  1.00 57.15           C  
ANISOU  353  C   ASN A  48     8170   8071   5474   1973   4068    -31       C  
ATOM    354  O   ASN A  48       5.432 125.503 236.846  1.00 58.12           O  
ANISOU  354  O   ASN A  48     8214   8304   5565   1990   4206    -11       O  
ATOM    355  CB  ASN A  48       5.959 128.418 237.086  1.00 61.91           C  
ANISOU  355  CB  ASN A  48     9280   8199   6045   2235   4581   -210       C  
ATOM    356  CG  ASN A  48       6.650 129.411 237.992  1.00 63.58           C  
ANISOU  356  CG  ASN A  48     9956   8124   6077   2173   4744   -429       C  
ATOM    357  OD1 ASN A  48       7.492 129.031 238.809  1.00 62.83           O  
ANISOU  357  OD1 ASN A  48    10098   8026   5749   1928   4655   -586       O  
ATOM    358  ND2 ASN A  48       6.304 130.690 237.857  1.00 66.04           N  
ANISOU  358  ND2 ASN A  48    10410   8188   6494   2391   4978   -439       N  
ATOM    359  N   ARG A  49       6.422 125.682 234.847  1.00 55.05           N  
ANISOU  359  N   ARG A  49     7668   7929   5320   1935   3798     85       N  
ATOM    360  CA  ARG A  49       5.721 124.545 234.203  1.00 53.94           C  
ANISOU  360  CA  ARG A  49     7147   8057   5293   1928   3651    253       C  
ATOM    361  C   ARG A  49       4.191 124.614 234.309  1.00 56.33           C  
ANISOU  361  C   ARG A  49     7196   8450   5755   2155   3886    406       C  
ATOM    362  O   ARG A  49       3.535 123.594 234.535  1.00 56.23           O  
ANISOU  362  O   ARG A  49     6969   8639   5757   2104   3869    484       O  
ATOM    363  CB  ARG A  49       6.200 123.190 234.735  1.00 52.11           C  
ANISOU  363  CB  ARG A  49     6914   7974   4910   1683   3476    194       C  
ATOM    364  CG  ARG A  49       7.605 123.134 235.303  1.00 50.76           C  
ANISOU  364  CG  ARG A  49     7058   7699   4532   1466   3347     12       C  
ATOM    365  CD  ARG A  49       8.671 122.507 234.450  1.00 48.03           C  
ANISOU  365  CD  ARG A  49     6656   7428   4167   1294   3015      7       C  
ATOM    366  NE  ARG A  49       9.870 123.212 234.858  1.00 47.88           N  
ANISOU  366  NE  ARG A  49     6954   7232   4004   1184   2987   -151       N  
ATOM    367  CZ  ARG A  49      11.117 123.000 234.430  1.00 50.22           C  
ANISOU  367  CZ  ARG A  49     7315   7530   4236   1018   2745   -210       C  
ATOM    368  NH1 ARG A  49      11.447 122.044 233.550  1.00 48.44           N  
ANISOU  368  NH1 ARG A  49     6877   7463   4064    939   2498   -139       N  
ATOM    369  NH2 ARG A  49      12.071 123.785 234.895  1.00 52.77           N  
ANISOU  369  NH2 ARG A  49     7925   7689   4436    925   2755   -345       N  
ATOM    370  N   ALA A  50       3.623 125.807 234.133  1.00 58.62           N  
ANISOU  370  N   ALA A  50     7504   8594   6177   2406   4107    458       N  
ATOM    371  CA  ALA A  50       2.186 126.002 234.350  1.00 61.39           C  
ANISOU  371  CA  ALA A  50     7625   9014   6687   2651   4373    600       C  
ATOM    372  C   ALA A  50       1.449 126.796 233.268  1.00 62.86           C  
ANISOU  372  C   ALA A  50     7575   9191   7118   2912   4408    797       C  
ATOM    373  O   ALA A  50       0.230 126.914 233.319  1.00 65.24           O  
ANISOU  373  O   ALA A  50     7627   9582   7580   3125   4601    948       O  
ATOM    374  CB  ALA A  50       1.931 126.633 235.746  1.00 64.01           C  
ANISOU  374  CB  ALA A  50     8238   9168   6915   2746   4740    456       C  
ATOM    375  N   ASP A  51       2.170 127.340 232.300  1.00 61.66           N  
ANISOU  375  N   ASP A  51     7491   8940   6997   2898   4225    809       N  
ATOM    376  CA  ASP A  51       1.538 128.149 231.268  1.00 63.19           C  
ANISOU  376  CA  ASP A  51     7489   9111   7410   3142   4246   1006       C  
ATOM    377  C   ASP A  51       0.509 127.335 230.474  1.00 63.28           C  
ANISOU  377  C   ASP A  51     7031   9432   7579   3187   4112   1246       C  
ATOM    378  O   ASP A  51       0.811 126.229 230.019  1.00 60.88           O  
ANISOU  378  O   ASP A  51     6588   9332   7211   2963   3835   1260       O  
ATOM    379  CB  ASP A  51       2.585 128.776 230.339  1.00 61.72           C  
ANISOU  379  CB  ASP A  51     7468   8781   7202   3076   4046    980       C  
ATOM    380  CG  ASP A  51       2.040 129.956 229.536  1.00 63.99           C  
ANISOU  380  CG  ASP A  51     7680   8943   7692   3358   4143   1152       C  
ATOM    381  OD1 ASP A  51       1.415 130.863 230.131  1.00 66.98           O  
ANISOU  381  OD1 ASP A  51     8152   9138   8158   3605   4460   1157       O  
ATOM    382  OD2 ASP A  51       2.254 129.986 228.301  1.00 62.95           O  
ANISOU  382  OD2 ASP A  51     7406   8886   7624   3336   3907   1285       O  
ATOM    383  N   PRO A  52      -0.724 127.874 230.338  1.00 66.29           N  
ANISOU  383  N   PRO A  52     7171   9849   8169   3476   4313   1436       N  
ATOM    384  CA  PRO A  52      -1.809 127.256 229.566  1.00 67.03           C  
ANISOU  384  CA  PRO A  52     6795  10239   8434   3539   4198   1691       C  
ATOM    385  C   PRO A  52      -1.492 127.101 228.068  1.00 65.38           C  
ANISOU  385  C   PRO A  52     6424  10146   8272   3457   3849   1828       C  
ATOM    386  O   PRO A  52      -1.655 126.012 227.523  1.00 63.93           O  
ANISOU  386  O   PRO A  52     5999  10220   8073   3277   3603   1904       O  
ATOM    387  CB  PRO A  52      -2.973 128.220 229.785  1.00 70.99           C  
ANISOU  387  CB  PRO A  52     7152  10675   9148   3905   4523   1845       C  
ATOM    388  CG  PRO A  52      -2.684 128.829 231.126  1.00 72.21           C  
ANISOU  388  CG  PRO A  52     7682  10565   9191   3971   4858   1623       C  
ATOM    389  CD  PRO A  52      -1.210 129.046 231.092  1.00 69.56           C  
ANISOU  389  CD  PRO A  52     7748  10025   8659   3758   4697   1406       C  
ATOM    390  N   GLU A  53      -1.033 128.167 227.420  1.00 65.74           N  
ANISOU  390  N   GLU A  53     6619   9997   8362   3575   3832   1853       N  
ATOM    391  CA  GLU A  53      -0.610 128.082 226.022  1.00 64.21           C  
ANISOU  391  CA  GLU A  53     6322   9895   8178   3483   3512   1965       C  
ATOM    392  C   GLU A  53       0.457 127.004 225.801  1.00 60.58           C  
ANISOU  392  C   GLU A  53     5962   9535   7519   3136   3225   1809       C  
ATOM    393  O   GLU A  53       0.409 126.268 224.815  1.00 59.36           O  
ANISOU  393  O   GLU A  53     5591   9598   7364   3006   2952   1914       O  
ATOM    394  CB  GLU A  53      -0.141 129.445 225.517  1.00 65.18           C  
ANISOU  394  CB  GLU A  53     6659   9753   8353   3643   3566   1989       C  
ATOM    395  CG  GLU A  53      -1.119 130.553 225.884  1.00 71.73           C  
ANISOU  395  CG  GLU A  53     7444  10430   9380   4007   3890   2115       C  
ATOM    396  CD  GLU A  53      -1.219 131.671 224.842  1.00 78.17           C  
ANISOU  396  CD  GLU A  53     8239  11120  10341   4216   3856   2308       C  
ATOM    397  OE1 GLU A  53      -1.589 131.408 223.666  1.00 78.87           O  
ANISOU  397  OE1 GLU A  53     8034  11424  10509   4214   3613   2532       O  
ATOM    398  OE2 GLU A  53      -0.952 132.836 225.216  1.00 82.35           O  
ANISOU  398  OE2 GLU A  53     9060  11326  10904   4384   4078   2241       O  
ATOM    399  N   VAL A  54       1.401 126.892 226.730  1.00 59.07           N  
ANISOU  399  N   VAL A  54     6099   9189   7157   2987   3289   1563       N  
ATOM    400  CA  VAL A  54       2.454 125.893 226.599  1.00 55.87           C  
ANISOU  400  CA  VAL A  54     5793   8863   6574   2681   3035   1417       C  
ATOM    401  C   VAL A  54       1.893 124.477 226.815  1.00 55.13           C  
ANISOU  401  C   VAL A  54     5458   9030   6459   2537   2936   1449       C  
ATOM    402  O   VAL A  54       2.027 123.607 225.948  1.00 53.57           O  
ANISOU  402  O   VAL A  54     5098   9018   6240   2378   2669   1503       O  
ATOM    403  CB  VAL A  54       3.671 126.181 227.534  1.00 54.67           C  
ANISOU  403  CB  VAL A  54     6049   8480   6242   2554   3110   1159       C  
ATOM    404  CG1 VAL A  54       4.784 125.177 227.297  1.00 51.57           C  
ANISOU  404  CG1 VAL A  54     5728   8177   5690   2263   2838   1035       C  
ATOM    405  CG2 VAL A  54       4.196 127.555 227.298  1.00 55.60           C  
ANISOU  405  CG2 VAL A  54     6405   8337   6383   2672   3202   1132       C  
ATOM    406  N   LEU A  55       1.252 124.260 227.959  1.00 56.46           N  
ANISOU  406  N   LEU A  55     5614   9206   6631   2588   3159   1415       N  
ATOM    407  CA  LEU A  55       0.687 122.952 228.291  1.00 56.06           C  
ANISOU  407  CA  LEU A  55     5356   9385   6561   2445   3094   1448       C  
ATOM    408  C   LEU A  55      -0.251 122.459 227.197  1.00 56.75           C  
ANISOU  408  C   LEU A  55     5044   9727   6793   2462   2923   1680       C  
ATOM    409  O   LEU A  55      -0.346 121.252 226.934  1.00 55.56           O  
ANISOU  409  O   LEU A  55     4741   9769   6600   2259   2726   1700       O  
ATOM    410  CB  LEU A  55      -0.042 123.008 229.639  1.00 58.11           C  
ANISOU  410  CB  LEU A  55     5637   9615   6826   2545   3409   1416       C  
ATOM    411  CG  LEU A  55       0.841 123.243 230.868  1.00 57.52           C  
ANISOU  411  CG  LEU A  55     5961   9327   6566   2470   3560   1175       C  
ATOM    412  CD1 LEU A  55       0.040 123.080 232.135  1.00 59.58           C  
ANISOU  412  CD1 LEU A  55     6215   9611   6812   2535   3850   1157       C  
ATOM    413  CD2 LEU A  55       2.046 122.305 230.860  1.00 54.39           C  
ANISOU  413  CD2 LEU A  55     5729   8949   5987   2175   3296   1026       C  
ATOM    414  N   ALA A  56      -0.935 123.416 226.571  1.00 58.89           N  
ANISOU  414  N   ALA A  56     5156   9989   7230   2702   2997   1858       N  
ATOM    415  CA  ALA A  56      -1.812 123.160 225.442  1.00 59.95           C  
ANISOU  415  CA  ALA A  56     4915  10360   7503   2738   2824   2102       C  
ATOM    416  C   ALA A  56      -1.006 122.625 224.291  1.00 57.52           C  
ANISOU  416  C   ALA A  56     4631  10127   7096   2526   2482   2079       C  
ATOM    417  O   ALA A  56      -1.397 121.638 223.669  1.00 57.13           O  
ANISOU  417  O   ALA A  56     4349  10310   7048   2369   2267   2168       O  
ATOM    418  CB  ALA A  56      -2.522 124.426 225.022  1.00 62.76           C  
ANISOU  418  CB  ALA A  56     5148  10652   8046   3053   2970   2292       C  
ATOM    419  N   HIS A  57       0.122 123.278 224.013  1.00 56.06           N  
ANISOU  419  N   HIS A  57     4735   9743   6822   2513   2440   1958       N  
ATOM    420  CA  HIS A  57       0.929 122.878 222.883  1.00 53.99           C  
ANISOU  420  CA  HIS A  57     4505   9543   6464   2333   2143   1936       C  
ATOM    421  C   HIS A  57       1.454 121.505 223.144  1.00 51.71           C  
ANISOU  421  C   HIS A  57     4261   9351   6035   2059   1989   1788       C  
ATOM    422  O   HIS A  57       1.603 120.716 222.228  1.00 50.63           O  
ANISOU  422  O   HIS A  57     4019   9369   5851   1894   1739   1818       O  
ATOM    423  CB  HIS A  57       2.084 123.822 222.592  1.00 52.97           C  
ANISOU  423  CB  HIS A  57     4675   9186   6264   2356   2141   1832       C  
ATOM    424  CG  HIS A  57       2.978 123.318 221.501  1.00 50.83           C  
ANISOU  424  CG  HIS A  57     4445   8991   5878   2156   1856   1793       C  
ATOM    425  ND1 HIS A  57       2.597 123.298 220.172  1.00 51.43           N  
ANISOU  425  ND1 HIS A  57     4316   9229   5995   2157   1661   1973       N  
ATOM    426  CD2 HIS A  57       4.217 122.765 221.549  1.00 48.30           C  
ANISOU  426  CD2 HIS A  57     4336   8619   5398   1947   1737   1597       C  
ATOM    427  CE1 HIS A  57       3.575 122.775 219.448  1.00 49.34           C  
ANISOU  427  CE1 HIS A  57     4155   9000   5593   1958   1451   1875       C  
ATOM    428  NE2 HIS A  57       4.565 122.437 220.260  1.00 47.43           N  
ANISOU  428  NE2 HIS A  57     4153   8631   5238   1836   1496   1650       N  
ATOM    429  N   LEU A  58       1.725 121.208 224.398  1.00 51.16           N  
ANISOU  429  N   LEU A  58     4359   9185   5895   2010   2141   1632       N  
ATOM    430  CA  LEU A  58       2.214 119.893 224.714  1.00 49.21           C  
ANISOU  430  CA  LEU A  58     4161   9014   5523   1762   2002   1504       C  
ATOM    431  C   LEU A  58       1.123 118.844 224.549  1.00 50.13           C  
ANISOU  431  C   LEU A  58     3969   9373   5707   1680   1920   1638       C  
ATOM    432  O   LEU A  58       1.409 117.711 224.214  1.00 48.73           O  
ANISOU  432  O   LEU A  58     3765   9298   5453   1466   1718   1591       O  
ATOM    433  CB  LEU A  58       2.835 119.853 226.108  1.00 48.52           C  
ANISOU  433  CB  LEU A  58     4346   8764   5326   1720   2169   1313       C  
ATOM    434  CG  LEU A  58       4.177 120.576 226.317  1.00 47.16           C  
ANISOU  434  CG  LEU A  58     4510   8367   5041   1702   2185   1140       C  
ATOM    435  CD1 LEU A  58       4.733 120.269 227.698  1.00 46.57           C  
ANISOU  435  CD1 LEU A  58     4674   8183   4836   1610   2300    963       C  
ATOM    436  CD2 LEU A  58       5.238 120.259 225.227  1.00 45.02           C  
ANISOU  436  CD2 LEU A  58     4294   8117   4694   1554   1918   1090       C  
ATOM    437  N   HIS A  59      -0.133 119.220 224.764  1.00 52.70           N  
ANISOU  437  N   HIS A  59     4055   9788   6181   1848   2079   1810       N  
ATOM    438  CA  HIS A  59      -1.233 118.304 224.477  1.00 53.94           C  
ANISOU  438  CA  HIS A  59     3879  10198   6417   1761   1984   1968       C  
ATOM    439  C   HIS A  59      -1.263 117.937 223.000  1.00 53.56           C  
ANISOU  439  C   HIS A  59     3668  10308   6372   1652   1683   2072       C  
ATOM    440  O   HIS A  59      -1.250 116.763 222.671  1.00 52.69           O  
ANISOU  440  O   HIS A  59     3492  10329   6198   1423   1487   2049       O  
ATOM    441  CB  HIS A  59      -2.568 118.892 224.885  1.00 57.08           C  
ANISOU  441  CB  HIS A  59     4018  10678   6992   1985   2213   2156       C  
ATOM    442  CG  HIS A  59      -3.611 117.858 225.141  1.00 60.47           C  
ANISOU  442  CG  HIS A  59     4158  11338   7480   1866   2194   2269       C  
ATOM    443  ND1 HIS A  59      -4.941 118.043 224.818  1.00 66.79           N  
ANISOU  443  ND1 HIS A  59     4577  12339   8460   1989   2237   2516       N  
ATOM    444  CD2 HIS A  59      -3.523 116.622 225.688  1.00 60.92           C  
ANISOU  444  CD2 HIS A  59     4245  11457   7443   1628   2134   2181       C  
ATOM    445  CE1 HIS A  59      -5.633 116.973 225.177  1.00 68.30           C  
ANISOU  445  CE1 HIS A  59     4573  12713   8664   1819   2210   2570       C  
ATOM    446  NE2 HIS A  59      -4.797 116.097 225.710  1.00 65.97           N  
ANISOU  446  NE2 HIS A  59     4533  12329   8203   1599   2150   2368       N  
ATOM    447  N   LEU A  60      -1.282 118.950 222.123  1.00 54.52           N  
ANISOU  447  N   LEU A  60     3750  10408   6559   1812   1651   2183       N  
ATOM    448  CA  LEU A  60      -1.196 118.770 220.662  1.00 54.52           C  
ANISOU  448  CA  LEU A  60     3640  10542   6533   1717   1368   2279       C  
ATOM    449  C   LEU A  60      -0.178 117.703 220.325  1.00 52.24           C  
ANISOU  449  C   LEU A  60     3530  10250   6069   1444   1155   2094       C  
ATOM    450  O   LEU A  60      -0.434 116.785 219.556  1.00 51.94           O  
ANISOU  450  O   LEU A  60     3354  10389   5992   1260    933   2139       O  
ATOM    451  CB  LEU A  60      -0.815 120.085 219.980  1.00 54.55           C  
ANISOU  451  CB  LEU A  60     3736  10423   6568   1906   1388   2342       C  
ATOM    452  CG  LEU A  60      -1.933 121.121 219.887  1.00 58.90           C  
ANISOU  452  CG  LEU A  60     4054  11012   7314   2187   1533   2585       C  
ATOM    453  CD1 LEU A  60      -1.404 122.561 219.875  1.00 59.59           C  
ANISOU  453  CD1 LEU A  60     4353  10852   7436   2414   1686   2577       C  
ATOM    454  CD2 LEU A  60      -2.821 120.850 218.678  1.00 61.63           C  
ANISOU  454  CD2 LEU A  60     4062  11629   7725   2150   1301   2830       C  
ATOM    455  N   GLU A  61       0.975 117.832 220.955  1.00 51.21           N  
ANISOU  455  N   GLU A  61     3711   9912   5834   1421   1235   1884       N  
ATOM    456  CA  GLU A  61       2.069 116.914 220.786  1.00 50.17           C  
ANISOU  456  CA  GLU A  61     3771   9743   5548   1201   1073   1698       C  
ATOM    457  C   GLU A  61       1.726 115.551 221.403  1.00 50.12           C  
ANISOU  457  C   GLU A  61     3703   9826   5513   1017   1034   1648       C  
ATOM    458  O   GLU A  61       2.048 114.517 220.838  1.00 49.15           O  
ANISOU  458  O   GLU A  61     3591   9776   5309    817    833   1588       O  
ATOM    459  CB  GLU A  61       3.326 117.524 221.410  1.00 48.65           C  
ANISOU  459  CB  GLU A  61     3900   9313   5271   1244   1186   1513       C  
ATOM    460  CG  GLU A  61       4.631 117.106 220.773  1.00 49.49           C  
ANISOU  460  CG  GLU A  61     4193   9372   5240   1090   1009   1364       C  
ATOM    461  CD  GLU A  61       5.054 117.942 219.535  1.00 53.77           C  
ANISOU  461  CD  GLU A  61     4755   9907   5768   1146    914   1425       C  
ATOM    462  OE1 GLU A  61       5.427 119.141 219.693  1.00 57.22           O  
ANISOU  462  OE1 GLU A  61     5319  10192   6229   1292   1043   1425       O  
ATOM    463  OE2 GLU A  61       5.068 117.377 218.409  1.00 52.43           O  
ANISOU  463  OE2 GLU A  61     4498   9876   5549   1029    709   1463       O  
ATOM    464  N   LYS A  62       1.045 115.541 222.544  1.00 51.92           N  
ANISOU  464  N   LYS A  62     3873  10047   5808   1084   1232   1676       N  
ATOM    465  CA  LYS A  62       0.676 114.273 223.138  1.00 52.36           C  
ANISOU  465  CA  LYS A  62     3869  10185   5839    904   1201   1649       C  
ATOM    466  C   LYS A  62      -0.340 113.566 222.269  1.00 54.56           C  
ANISOU  466  C   LYS A  62     3850  10700   6182    787   1026   1812       C  
ATOM    467  O   LYS A  62      -0.260 112.352 222.129  1.00 54.71           O  
ANISOU  467  O   LYS A  62     3873  10779   6137    563    871   1757       O  
ATOM    468  CB  LYS A  62       0.117 114.424 224.537  1.00 53.10           C  
ANISOU  468  CB  LYS A  62     3959  10238   5980    993   1464   1657       C  
ATOM    469  CG  LYS A  62      -0.005 113.068 225.223  1.00 53.55           C  
ANISOU  469  CG  LYS A  62     4023  10343   5980    781   1426   1603       C  
ATOM    470  CD  LYS A  62      -1.058 113.057 226.302  1.00 56.35           C  
ANISOU  470  CD  LYS A  62     4236  10762   6412    843   1657   1697       C  
ATOM    471  CE  LYS A  62      -2.367 112.625 225.735  1.00 59.60           C  
ANISOU  471  CE  LYS A  62     4282  11413   6949    793   1585   1903       C  
ATOM    472  NZ  LYS A  62      -3.384 113.679 225.953  1.00 64.31           N  
ANISOU  472  NZ  LYS A  62     4660  12077   7698   1041   1807   2069       N  
ATOM    473  N   ASP A  63      -1.298 114.323 221.715  1.00 57.10           N  
ANISOU  473  N   ASP A  63     3916  11148   6630    936   1048   2015       N  
ATOM    474  CA  ASP A  63      -2.295 113.812 220.765  1.00 58.91           C  
ANISOU  474  CA  ASP A  63     3837  11625   6922    829    858   2198       C  
ATOM    475  C   ASP A  63      -1.551 113.203 219.593  1.00 57.03           C  
ANISOU  475  C   ASP A  63     3708  11410   6552    636    577   2113       C  
ATOM    476  O   ASP A  63      -1.687 112.014 219.330  1.00 56.79           O  
ANISOU  476  O   ASP A  63     3642  11473   6463    397    411   2080       O  
ATOM    477  CB  ASP A  63      -3.231 114.936 220.254  1.00 61.72           C  
ANISOU  477  CB  ASP A  63     3929  12092   7430   1059    915   2437       C  
ATOM    478  CG  ASP A  63      -4.495 115.127 221.127  1.00 66.28           C  
ANISOU  478  CG  ASP A  63     4238  12773   8173   1192   1133   2599       C  
ATOM    479  OD1 ASP A  63      -5.062 114.112 221.606  1.00 68.14           O  
ANISOU  479  OD1 ASP A  63     4348  13125   8417   1020   1122   2614       O  
ATOM    480  OD2 ASP A  63      -4.943 116.296 221.308  1.00 68.39           O  
ANISOU  480  OD2 ASP A  63     4414  13004   8569   1470   1323   2720       O  
ATOM    481  N   TYR A  64      -0.734 114.016 218.923  1.00 55.57           N  
ANISOU  481  N   TYR A  64     3676  11127   6313    734    539   2068       N  
ATOM    482  CA  TYR A  64      -0.047 113.587 217.721  1.00 54.24           C  
ANISOU  482  CA  TYR A  64     3604  10991   6015    577    296   1999       C  
ATOM    483  C   TYR A  64       0.675 112.290 217.981  1.00 52.88           C  
ANISOU  483  C   TYR A  64     3616  10754   5722    350    208   1798       C  
ATOM    484  O   TYR A  64       0.624 111.353 217.191  1.00 52.62           O  
ANISOU  484  O   TYR A  64     3556  10823   5614    143      1   1777       O  
ATOM    485  CB  TYR A  64       0.964 114.634 217.257  1.00 52.56           C  
ANISOU  485  CB  TYR A  64     3591  10633   5747    713    323   1938       C  
ATOM    486  CG  TYR A  64       1.686 114.221 216.005  1.00 50.44           C  
ANISOU  486  CG  TYR A  64     3424  10407   5336    558     95   1868       C  
ATOM    487  CD1 TYR A  64       0.985 113.899 214.855  1.00 51.64           C  
ANISOU  487  CD1 TYR A  64     3385  10769   5465    449   -115   2007       C  
ATOM    488  CD2 TYR A  64       3.069 114.134 215.969  1.00 50.13           C  
ANISOU  488  CD2 TYR A  64     3666  10207   5175    512     90   1663       C  
ATOM    489  CE1 TYR A  64       1.629 113.506 213.681  1.00 51.73           C  
ANISOU  489  CE1 TYR A  64     3508  10824   5324    298   -314   1934       C  
ATOM    490  CE2 TYR A  64       3.755 113.739 214.786  1.00 49.98           C  
ANISOU  490  CE2 TYR A  64     3743  10232   5017    374    -99   1592       C  
ATOM    491  CZ  TYR A  64       3.009 113.431 213.635  1.00 51.46           C  
ANISOU  491  CZ  TYR A  64     3757  10624   5170    268   -296   1725       C  
ATOM    492  OH  TYR A  64       3.637 113.040 212.456  1.00 50.08           O  
ANISOU  492  OH  TYR A  64     3689  10498   4840    127   -471   1650       O  
ATOM    493  N   TYR A  65       1.355 112.256 219.110  1.00 52.21           N  
ANISOU  493  N   TYR A  65     3731  10491   5618    391    369   1651       N  
ATOM    494  CA  TYR A  65       2.135 111.113 219.486  1.00 51.28           C  
ANISOU  494  CA  TYR A  65     3805  10282   5398    212    308   1466       C  
ATOM    495  C   TYR A  65       1.275 109.853 219.622  1.00 53.14           C  
ANISOU  495  C   TYR A  65     3895  10641   5653     11    218   1515       C  
ATOM    496  O   TYR A  65       1.570 108.811 219.038  1.00 52.59           O  
ANISOU  496  O   TYR A  65     3891  10589   5500   -189     39   1433       O  
ATOM    497  CB  TYR A  65       2.895 111.396 220.780  1.00 49.60           C  
ANISOU  497  CB  TYR A  65     3805   9873   5166    303    501   1335       C  
ATOM    498  CG  TYR A  65       3.341 110.131 221.411  1.00 48.46           C  
ANISOU  498  CG  TYR A  65     3795   9665   4955    129    459   1204       C  
ATOM    499  CD1 TYR A  65       4.360 109.379 220.841  1.00 45.64           C  
ANISOU  499  CD1 TYR A  65     3606   9243   4492      0    302   1059       C  
ATOM    500  CD2 TYR A  65       2.697 109.645 222.561  1.00 49.49           C  
ANISOU  500  CD2 TYR A  65     3875   9801   5129     95    580   1238       C  
ATOM    501  CE1 TYR A  65       4.733 108.179 221.410  1.00 47.81           C  
ANISOU  501  CE1 TYR A  65     4000   9446   4719   -147    262    954       C  
ATOM    502  CE2 TYR A  65       3.068 108.462 223.150  1.00 47.92           C  
ANISOU  502  CE2 TYR A  65     3802   9536   4870    -66    537   1138       C  
ATOM    503  CZ  TYR A  65       4.081 107.720 222.572  1.00 49.21           C  
ANISOU  503  CZ  TYR A  65     4134   9622   4941   -183    372   1000       C  
ATOM    504  OH  TYR A  65       4.465 106.526 223.163  1.00 51.66           O  
ANISOU  504  OH  TYR A  65     4578   9849   5204   -328    330    910       O  
ATOM    505  N   GLU A  66       0.215 109.950 220.404  1.00 56.00           N  
ANISOU  505  N   GLU A  66     4068  11083   6127     61    353   1646       N  
ATOM    506  CA  GLU A  66      -0.639 108.801 220.627  1.00 58.69           C  
ANISOU  506  CA  GLU A  66     4262  11543   6496   -139    286   1706       C  
ATOM    507  C   GLU A  66      -1.223 108.356 219.318  1.00 60.23           C  
ANISOU  507  C   GLU A  66     4282  11924   6680   -296     44   1803       C  
ATOM    508  O   GLU A  66      -1.110 107.192 218.979  1.00 60.18           O  
ANISOU  508  O   GLU A  66     4339  11928   6601   -531   -118   1727       O  
ATOM    509  CB  GLU A  66      -1.712 109.086 221.678  1.00 60.75           C  
ANISOU  509  CB  GLU A  66     4323  11877   6883    -44    496   1847       C  
ATOM    510  CG  GLU A  66      -1.423 108.380 223.005  1.00 62.41           C  
ANISOU  510  CG  GLU A  66     4696  11962   7053   -117    629   1739       C  
ATOM    511  CD  GLU A  66      -1.685 109.254 224.237  1.00 67.65           C  
ANISOU  511  CD  GLU A  66     5360  12567   7778     94    925   1771       C  
ATOM    512  OE1 GLU A  66      -2.872 109.500 224.608  1.00 70.57           O  
ANISOU  512  OE1 GLU A  66     5470  13078   8267    159   1059   1940       O  
ATOM    513  OE2 GLU A  66      -0.677 109.670 224.861  1.00 68.50           O  
ANISOU  513  OE2 GLU A  66     5735  12484   7808    187   1029   1622       O  
ATOM    514  N   LYS A  67      -1.778 109.305 218.567  1.00 62.50           N  
ANISOU  514  N   LYS A  67     4374  12342   7030   -166     16   1964       N  
ATOM    515  CA  LYS A  67      -2.363 109.073 217.226  1.00 64.95           C  
ANISOU  515  CA  LYS A  67     4505  12856   7319   -301   -229   2084       C  
ATOM    516  C   LYS A  67      -1.442 108.285 216.290  1.00 63.81           C  
ANISOU  516  C   LYS A  67     4589  12653   7003   -499   -440   1909       C  
ATOM    517  O   LYS A  67      -1.899 107.521 215.440  1.00 65.03           O  
ANISOU  517  O   LYS A  67     4659  12949   7102   -719   -653   1945       O  
ATOM    518  CB  LYS A  67      -2.783 110.422 216.599  1.00 66.35           C  
ANISOU  518  CB  LYS A  67     4506  13130   7572    -76   -209   2268       C  
ATOM    519  CG  LYS A  67      -3.230 110.414 215.119  1.00 69.24           C  
ANISOU  519  CG  LYS A  67     4718  13702   7890   -186   -471   2401       C  
ATOM    520  CD  LYS A  67      -3.367 111.857 214.533  1.00 71.69           C  
ANISOU  520  CD  LYS A  67     4925  14052   8262     70   -437   2567       C  
ATOM    521  CE  LYS A  67      -4.697 112.530 214.934  1.00 74.88           C  
ANISOU  521  CE  LYS A  67     4969  14610   8871    249   -322   2835       C  
ATOM    522  NZ  LYS A  67      -4.727 114.005 214.699  1.00 75.03           N  
ANISOU  522  NZ  LYS A  67     4939  14590   8979    554   -214   2976       N  
ATOM    523  N   ARG A  68      -0.143 108.456 216.489  1.00 62.23           N  
ANISOU  523  N   ARG A  68     4681  12245   6718   -424   -372   1717       N  
ATOM    524  CA  ARG A  68       0.878 107.921 215.590  1.00 61.55           C  
ANISOU  524  CA  ARG A  68     4822  12088   6476   -551   -529   1546       C  
ATOM    525  C   ARG A  68       1.583 106.673 216.156  1.00 60.24           C  
ANISOU  525  C   ARG A  68     4878  11765   6243   -707   -536   1346       C  
ATOM    526  O   ARG A  68       2.289 105.962 215.442  1.00 59.00           O  
ANISOU  526  O   ARG A  68     4895  11556   5967   -842   -667   1202       O  
ATOM    527  CB  ARG A  68       1.877 109.035 215.277  1.00 60.05           C  
ANISOU  527  CB  ARG A  68     4782  11792   6244   -356   -458   1490       C  
ATOM    528  CG  ARG A  68       2.650 108.832 214.023  1.00 60.64           C  
ANISOU  528  CG  ARG A  68     5001  11873   6168   -452   -623   1391       C  
ATOM    529  CD  ARG A  68       1.837 109.086 212.782  1.00 64.84           C  
ANISOU  529  CD  ARG A  68     5345  12622   6669   -516   -799   1558       C  
ATOM    530  NE  ARG A  68       2.723 108.937 211.631  1.00 67.69           N  
ANISOU  530  NE  ARG A  68     5888  12970   6860   -600   -928   1439       N  
ATOM    531  CZ  ARG A  68       2.527 109.497 210.436  1.00 71.50           C  
ANISOU  531  CZ  ARG A  68     6306  13594   7268   -604  -1056   1549       C  
ATOM    532  NH1 ARG A  68       1.443 110.250 210.220  1.00 74.45           N  
ANISOU  532  NH1 ARG A  68     6418  14135   7736   -520  -1088   1796       N  
ATOM    533  NH2 ARG A  68       3.416 109.311 209.453  1.00 70.55           N  
ANISOU  533  NH2 ARG A  68     6378  13451   6976   -686  -1147   1420       N  
ATOM    534  N   ALA A  69       1.345 106.424 217.445  1.00 60.70           N  
ANISOU  534  N   ALA A  69     4928  11753   6382   -681   -386   1348       N  
ATOM    535  CA  ALA A  69       1.847 105.269 218.188  1.00 60.16           C  
ANISOU  535  CA  ALA A  69     5043  11538   6276   -813   -374   1203       C  
ATOM    536  C   ALA A  69       0.874 104.059 218.287  1.00 62.50           C  
ANISOU  536  C   ALA A  69     5224  11923   6599  -1057   -471   1263       C  
ATOM    537  O   ALA A  69       1.123 103.112 219.054  1.00 62.39           O  
ANISOU  537  O   ALA A  69     5345  11786   6576  -1163   -442   1177       O  
ATOM    538  CB  ALA A  69       2.207 105.730 219.576  1.00 59.13           C  
ANISOU  538  CB  ALA A  69     4996  11275   6196   -652   -153   1174       C  
ATOM    539  N   VAL A  70      -0.233 104.095 217.544  1.00 64.91           N  
ANISOU  539  N   VAL A  70     5280  12442   6940  -1154   -590   1423       N  
ATOM    540  CA  VAL A  70      -1.266 103.058 217.653  1.00 67.18           C  
ANISOU  540  CA  VAL A  70     5421  12839   7265  -1399   -680   1508       C  
ATOM    541  C   VAL A  70      -0.705 101.707 217.206  1.00 67.12           C  
ANISOU  541  C   VAL A  70     5648  12711   7144  -1645   -840   1333       C  
ATOM    542  O   VAL A  70      -0.810 100.702 217.914  1.00 67.39           O  
ANISOU  542  O   VAL A  70     5759  12653   7193  -1793   -822   1292       O  
ATOM    543  CB  VAL A  70      -2.537 103.400 216.801  1.00 69.94           C  
ANISOU  543  CB  VAL A  70     5438  13469   7669  -1469   -810   1725       C  
ATOM    544  CG1 VAL A  70      -3.637 102.323 216.964  1.00 72.47           C  
ANISOU  544  CG1 VAL A  70     5587  13914   8034  -1749   -905   1823       C  
ATOM    545  CG2 VAL A  70      -3.078 104.777 217.150  1.00 69.79           C  
ANISOU  545  CG2 VAL A  70     5187  13556   7775  -1195   -648   1904       C  
ATOM    546  N   ASP A  71      -0.089 101.707 216.028  1.00 66.74           N  
ANISOU  546  N   ASP A  71     5726  12653   6978  -1681   -984   1231       N  
ATOM    547  CA  ASP A  71       0.314 100.474 215.360  1.00 66.81           C  
ANISOU  547  CA  ASP A  71     5942  12571   6871  -1919  -1147   1072       C  
ATOM    548  C   ASP A  71       1.687  99.934 215.811  1.00 63.93           C  
ANISOU  548  C   ASP A  71     5907  11933   6452  -1860  -1070    850       C  
ATOM    549  O   ASP A  71       2.272  99.077 215.161  1.00 63.88           O  
ANISOU  549  O   ASP A  71     6109  11818   6343  -1993  -1178    692       O  
ATOM    550  CB  ASP A  71       0.265 100.685 213.845  1.00 67.79           C  
ANISOU  550  CB  ASP A  71     6048  12830   6877  -2001  -1335   1069       C  
ATOM    551  CG  ASP A  71       0.989 101.939 213.430  1.00 67.14           C  
ANISOU  551  CG  ASP A  71     5992  12754   6764  -1748  -1267   1063       C  
ATOM    552  OD1 ASP A  71       0.483 103.033 213.809  1.00 68.35           O  
ANISOU  552  OD1 ASP A  71     5934  13013   7022  -1563  -1166   1233       O  
ATOM    553  OD2 ASP A  71       2.061 101.824 212.766  1.00 64.13           O  
ANISOU  553  OD2 ASP A  71     5845  12262   6259  -1733  -1301    891       O  
ATOM    554  N   ILE A  72       2.205 100.429 216.923  1.00 61.75           N  
ANISOU  554  N   ILE A  72     5677  11544   6241  -1659   -884    841       N  
ATOM    555  CA  ILE A  72       3.317  99.723 217.569  1.00 59.78           C  
ANISOU  555  CA  ILE A  72     5700  11051   5963  -1637   -824    669       C  
ATOM    556  C   ILE A  72       2.955  99.237 218.976  1.00 60.04           C  
ANISOU  556  C   ILE A  72     5723  11009   6080  -1665   -709    726       C  
ATOM    557  O   ILE A  72       3.694  98.472 219.569  1.00 59.11           O  
ANISOU  557  O   ILE A  72     5815  10699   5946  -1683   -681    616       O  
ATOM    558  CB  ILE A  72       4.651 100.501 217.521  1.00 57.11           C  
ANISOU  558  CB  ILE A  72     5516  10603   5580  -1411   -740    553       C  
ATOM    559  CG1 ILE A  72       4.475 101.956 217.967  1.00 55.54           C  
ANISOU  559  CG1 ILE A  72     5165  10492   5443  -1190   -601    670       C  
ATOM    560  CG2 ILE A  72       5.214 100.457 216.120  1.00 56.88           C  
ANISOU  560  CG2 ILE A  72     5583  10592   5438  -1450   -867    445       C  
ATOM    561  CD1 ILE A  72       5.774 102.726 218.089  1.00 51.09           C  
ANISOU  561  CD1 ILE A  72     4756   9813   4844   -991   -511    564       C  
ATOM    562  N   LYS A  73       1.787  99.644 219.472  1.00 61.74           N  
ANISOU  562  N   LYS A  73     5689  11384   6384  -1673   -645    909       N  
ATOM    563  CA  LYS A  73       1.268  99.163 220.762  1.00 63.26           C  
ANISOU  563  CA  LYS A  73     5848  11541   6648  -1727   -531    985       C  
ATOM    564  C   LYS A  73       1.412  97.663 220.918  1.00 63.22           C  
ANISOU  564  C   LYS A  73     6022  11386   6613  -1956   -622    902       C  
ATOM    565  O   LYS A  73       1.621  97.169 222.024  1.00 63.16           O  
ANISOU  565  O   LYS A  73     6124  11249   6626  -1962   -526    895       O  
ATOM    566  CB  LYS A  73      -0.212  99.540 220.991  1.00 65.81           C  
ANISOU  566  CB  LYS A  73     5842  12092   7069  -1772   -485   1202       C  
ATOM    567  CG  LYS A  73      -0.478 101.051 221.205  1.00 69.34           C  
ANISOU  567  CG  LYS A  73     6107  12661   7580  -1509   -333   1312       C  
ATOM    568  CD  LYS A  73      -0.451 101.541 222.690  1.00 72.73           C  
ANISOU  568  CD  LYS A  73     6551  13025   8059  -1346    -86   1347       C  
ATOM    569  CE  LYS A  73      -0.367 103.089 222.704  1.00 74.39           C  
ANISOU  569  CE  LYS A  73     6672  13287   8306  -1064     53   1395       C  
ATOM    570  NZ  LYS A  73      -0.464 103.735 224.046  1.00 74.52           N  
ANISOU  570  NZ  LYS A  73     6692  13260   8363   -897    305   1432       N  
ATOM    571  N   ASP A  74       1.304  96.941 219.814  1.00 63.59           N  
ANISOU  571  N   ASP A  74     6116  11442   6604  -2148   -806    840       N  
ATOM    572  CA  ASP A  74       1.251  95.502 219.900  1.00 64.20           C  
ANISOU  572  CA  ASP A  74     6352  11376   6663  -2390   -897    777       C  
ATOM    573  C   ASP A  74       2.647  94.898 219.860  1.00 61.43           C  
ANISOU  573  C   ASP A  74     6331  10761   6247  -2327   -906    573       C  
ATOM    574  O   ASP A  74       2.934  93.942 220.571  1.00 61.44           O  
ANISOU  574  O   ASP A  74     6505  10577   6265  -2402   -885    532       O  
ATOM    575  CB  ASP A  74       0.259  94.919 218.872  1.00 67.43           C  
ANISOU  575  CB  ASP A  74     6644  11926   7049  -2672  -1086    825       C  
ATOM    576  CG  ASP A  74      -1.229  94.886 219.408  1.00 72.96           C  
ANISOU  576  CG  ASP A  74     7041  12830   7849  -2823  -1065   1049       C  
ATOM    577  OD1 ASP A  74      -1.552  95.510 220.464  1.00 75.57           O  
ANISOU  577  OD1 ASP A  74     7226  13222   8265  -2675   -887   1171       O  
ATOM    578  OD2 ASP A  74      -2.088  94.207 218.781  1.00 77.47           O  
ANISOU  578  OD2 ASP A  74     7520  13503   8411  -3103  -1224   1102       O  
ATOM    579  N   LEU A  75       3.541  95.491 219.085  1.00 58.77           N  
ANISOU  579  N   LEU A  75     6076  10409   5845  -2173   -925    459       N  
ATOM    580  CA  LEU A  75       4.937  95.074 219.148  1.00 56.07           C  
ANISOU  580  CA  LEU A  75     6011   9834   5460  -2065   -902    282       C  
ATOM    581  C   LEU A  75       5.644  95.492 220.448  1.00 53.94           C  
ANISOU  581  C   LEU A  75     5796   9464   5236  -1861   -744    297       C  
ATOM    582  O   LEU A  75       6.331  94.678 221.052  1.00 53.59           O  
ANISOU  582  O   LEU A  75     5947   9218   5198  -1860   -727    227       O  
ATOM    583  CB  LEU A  75       5.709  95.567 217.939  1.00 54.93           C  
ANISOU  583  CB  LEU A  75     5931   9712   5227  -1971   -957    158       C  
ATOM    584  CG  LEU A  75       7.217  95.304 217.945  1.00 52.54           C  
ANISOU  584  CG  LEU A  75     5874   9201   4889  -1823   -915    -15       C  
ATOM    585  CD1 LEU A  75       7.554  93.814 217.937  1.00 52.07           C  
ANISOU  585  CD1 LEU A  75     6048   8915   4821  -1963   -974   -133       C  
ATOM    586  CD2 LEU A  75       7.849  96.009 216.759  1.00 50.38           C  
ANISOU  586  CD2 LEU A  75     5614   9000   4528  -1725   -944   -105       C  
ATOM    587  N   ALA A  76       5.484  96.749 220.862  1.00 52.31           N  
ANISOU  587  N   ALA A  76     5428   9390   5056  -1691   -635    389       N  
ATOM    588  CA  ALA A  76       5.980  97.216 222.156  1.00 50.93           C  
ANISOU  588  CA  ALA A  76     5295   9145   4910  -1528   -485    416       C  
ATOM    589  C   ALA A  76       5.560  96.265 223.279  1.00 52.43           C  
ANISOU  589  C   ALA A  76     5539   9244   5138  -1653   -448    481       C  
ATOM    590  O   ALA A  76       6.281  96.071 224.253  1.00 51.61           O  
ANISOU  590  O   ALA A  76     5581   9002   5029  -1573   -378    456       O  
ATOM    591  CB  ALA A  76       5.469  98.587 222.435  1.00 50.04           C  
ANISOU  591  CB  ALA A  76     4984   9199   4828  -1384   -370    528       C  
ATOM    592  N   GLU A  77       4.375  95.672 223.124  1.00 54.82           N  
ANISOU  592  N   GLU A  77     5721   9634   5475  -1862   -502    577       N  
ATOM    593  CA  GLU A  77       3.867  94.646 224.033  1.00 55.79           C  
ANISOU  593  CA  GLU A  77     5893   9675   5631  -2029   -484    649       C  
ATOM    594  C   GLU A  77       4.693  93.343 223.963  1.00 55.48           C  
ANISOU  594  C   GLU A  77     6133   9380   5565  -2119   -576    524       C  
ATOM    595  O   GLU A  77       5.160  92.873 224.977  1.00 55.26           O  
ANISOU  595  O   GLU A  77     6248   9203   5544  -2090   -517    533       O  
ATOM    596  CB  GLU A  77       2.373  94.408 223.754  1.00 58.13           C  
ANISOU  596  CB  GLU A  77     5960  10152   5974  -2245   -529    790       C  
ATOM    597  CG  GLU A  77       1.623  93.496 224.733  1.00 61.25           C  
ANISOU  597  CG  GLU A  77     6350  10510   6412  -2437   -487    903       C  
ATOM    598  CD  GLU A  77       1.722  93.914 226.212  1.00 62.38           C  
ANISOU  598  CD  GLU A  77     6499  10635   6565  -2302   -295    983       C  
ATOM    599  OE1 GLU A  77       2.069  95.091 226.506  1.00 62.26           O  
ANISOU  599  OE1 GLU A  77     6427  10688   6539  -2070   -178    981       O  
ATOM    600  OE2 GLU A  77       1.436  93.050 227.084  1.00 62.93           O  
ANISOU  600  OE2 GLU A  77     6645  10619   6647  -2443   -260   1051       O  
ATOM    601  N   THR A  78       4.900  92.771 222.784  1.00 55.45           N  
ANISOU  601  N   THR A  78     6219   9320   5530  -2217   -713    409       N  
ATOM    602  CA  THR A  78       5.682  91.547 222.703  1.00 55.83           C  
ANISOU  602  CA  THR A  78     6541   9107   5564  -2280   -781    286       C  
ATOM    603  C   THR A  78       7.043  91.774 223.363  1.00 53.62           C  
ANISOU  603  C   THR A  78     6416   8678   5278  -2039   -702    216       C  
ATOM    604  O   THR A  78       7.673  90.842 223.875  1.00 53.46           O  
ANISOU  604  O   THR A  78     6601   8439   5274  -2044   -710    177       O  
ATOM    605  CB  THR A  78       5.871  91.093 221.229  1.00 56.85           C  
ANISOU  605  CB  THR A  78     6764   9199   5637  -2377   -917    139       C  
ATOM    606  OG1 THR A  78       4.919  91.763 220.397  1.00 58.65           O  
ANISOU  606  OG1 THR A  78     6766   9677   5841  -2465   -975    202       O  
ATOM    607  CG2 THR A  78       5.674  89.561 221.071  1.00 59.73           C  
ANISOU  607  CG2 THR A  78     7332   9356   6008  -2617  -1012     84       C  
ATOM    608  N   ILE A  79       7.469  93.038 223.365  1.00 51.89           N  
ANISOU  608  N   ILE A  79     6092   8585   5040  -1834   -629    214       N  
ATOM    609  CA  ILE A  79       8.822  93.442 223.747  1.00 49.85           C  
ANISOU  609  CA  ILE A  79     5950   8226   4765  -1609   -574    136       C  
ATOM    610  C   ILE A  79       8.942  93.756 225.247  1.00 49.10           C  
ANISOU  610  C   ILE A  79     5858   8116   4683  -1524   -464    238       C  
ATOM    611  O   ILE A  79       9.986  93.528 225.846  1.00 48.90           O  
ANISOU  611  O   ILE A  79     5980   7950   4651  -1414   -450    198       O  
ATOM    612  CB  ILE A  79       9.294  94.633 222.886  1.00 48.23           C  
ANISOU  612  CB  ILE A  79     5654   8150   4521  -1453   -562     70       C  
ATOM    613  CG1 ILE A  79      10.637  94.342 222.258  1.00 48.02           C  
ANISOU  613  CG1 ILE A  79     5793   7985   4468  -1344   -601    -87       C  
ATOM    614  CG2 ILE A  79       9.415  95.889 223.672  1.00 47.92           C  
ANISOU  614  CG2 ILE A  79     5509   8217   4483  -1291   -444    143       C  
ATOM    615  CD1 ILE A  79      10.530  94.046 220.800  1.00 50.47           C  
ANISOU  615  CD1 ILE A  79     6125   8318   4733  -1431   -693   -191       C  
ATOM    616  N   TYR A  80       7.877  94.276 225.845  1.00 49.30           N  
ANISOU  616  N   TYR A  80     5717   8292   4721  -1576   -383    372       N  
ATOM    617  CA  TYR A  80       7.792  94.441 227.296  1.00 49.27           C  
ANISOU  617  CA  TYR A  80     5730   8279   4710  -1540   -268    474       C  
ATOM    618  C   TYR A  80       7.984  93.088 227.987  1.00 50.25           C  
ANISOU  618  C   TYR A  80     6039   8208   4844  -1656   -311    498       C  
ATOM    619  O   TYR A  80       8.677  92.980 229.016  1.00 49.84           O  
ANISOU  619  O   TYR A  80     6115   8058   4766  -1577   -269    520       O  
ATOM    620  CB  TYR A  80       6.438  95.056 227.657  1.00 50.12           C  
ANISOU  620  CB  TYR A  80     5618   8585   4839  -1602   -167    613       C  
ATOM    621  CG  TYR A  80       6.156  95.267 229.128  1.00 51.60           C  
ANISOU  621  CG  TYR A  80     5811   8789   5005  -1582    -22    722       C  
ATOM    622  CD1 TYR A  80       6.675  96.369 229.822  1.00 52.06           C  
ANISOU  622  CD1 TYR A  80     5882   8884   5016  -1397     97    712       C  
ATOM    623  CD2 TYR A  80       5.326  94.386 229.830  1.00 54.21           C  
ANISOU  623  CD2 TYR A  80     6141   9104   5354  -1765      3    836       C  
ATOM    624  CE1 TYR A  80       6.384  96.562 231.204  1.00 51.83           C  
ANISOU  624  CE1 TYR A  80     5879   8872   4941  -1391    241    805       C  
ATOM    625  CE2 TYR A  80       5.043  94.574 231.196  1.00 54.77           C  
ANISOU  625  CE2 TYR A  80     6225   9199   5384  -1755    151    939       C  
ATOM    626  CZ  TYR A  80       5.568  95.660 231.859  1.00 52.58           C  
ANISOU  626  CZ  TYR A  80     5971   8960   5047  -1566    269    918       C  
ATOM    627  OH  TYR A  80       5.269  95.820 233.171  1.00 52.97           O  
ANISOU  627  OH  TYR A  80     6054   9035   5038  -1570    417   1009       O  
ATOM    628  N   GLN A  81       7.380  92.058 227.403  1.00 51.31           N  
ANISOU  628  N   GLN A  81     6198   8285   5014  -1853   -403    498       N  
ATOM    629  CA  GLN A  81       7.401  90.723 227.991  1.00 52.62           C  
ANISOU  629  CA  GLN A  81     6542   8252   5199  -1991   -444    535       C  
ATOM    630  C   GLN A  81       8.799  90.152 227.945  1.00 52.04           C  
ANISOU  630  C   GLN A  81     6696   7953   5125  -1863   -504    426       C  
ATOM    631  O   GLN A  81       9.258  89.559 228.930  1.00 52.64           O  
ANISOU  631  O   GLN A  81     6919   7881   5202  -1846   -492    482       O  
ATOM    632  CB  GLN A  81       6.403  89.789 227.291  1.00 54.55           C  
ANISOU  632  CB  GLN A  81     6765   8481   5480  -2252   -534    552       C  
ATOM    633  CG  GLN A  81       4.957  90.231 227.416  1.00 54.97           C  
ANISOU  633  CG  GLN A  81     6566   8769   5551  -2396   -479    691       C  
ATOM    634  CD  GLN A  81       4.545  90.432 228.868  1.00 56.48           C  
ANISOU  634  CD  GLN A  81     6712   9012   5736  -2391   -338    844       C  
ATOM    635  OE1 GLN A  81       5.145  89.860 229.781  1.00 56.30           O  
ANISOU  635  OE1 GLN A  81     6877   8820   5694  -2368   -316    865       O  
ATOM    636  NE2 GLN A  81       3.522  91.250 229.088  1.00 56.70           N  
ANISOU  636  NE2 GLN A  81     6491   9276   5776  -2406   -235    955       N  
ATOM    637  N   GLU A  82       9.463  90.337 226.795  1.00 51.24           N  
ANISOU  637  N   GLU A  82     6615   7832   5020  -1772   -565    279       N  
ATOM    638  CA  GLU A  82      10.882  89.979 226.630  1.00 50.18           C  
ANISOU  638  CA  GLU A  82     6658   7516   4894  -1608   -603    166       C  
ATOM    639  C   GLU A  82      11.636  90.659 227.748  1.00 47.88           C  
ANISOU  639  C   GLU A  82     6366   7249   4578  -1433   -533    225       C  
ATOM    640  O   GLU A  82      12.308  89.981 228.503  1.00 48.16           O  
ANISOU  640  O   GLU A  82     6551   7120   4629  -1389   -551    258       O  
ATOM    641  CB  GLU A  82      11.457  90.385 225.259  1.00 49.56           C  
ANISOU  641  CB  GLU A  82     6558   7473   4798  -1515   -642      8       C  
ATOM    642  CG  GLU A  82      11.088  89.478 224.071  1.00 52.89           C  
ANISOU  642  CG  GLU A  82     7067   7806   5225  -1674   -731    -95       C  
ATOM    643  CD  GLU A  82      11.653  90.003 222.737  1.00 55.61           C  
ANISOU  643  CD  GLU A  82     7389   8216   5524  -1579   -754   -247       C  
ATOM    644  OE1 GLU A  82      12.903  90.174 222.637  1.00 57.18           O  
ANISOU  644  OE1 GLU A  82     7659   8339   5726  -1379   -728   -333       O  
ATOM    645  OE2 GLU A  82      10.856  90.244 221.795  1.00 54.22           O  
ANISOU  645  OE2 GLU A  82     7118   8176   5307  -1707   -799   -271       O  
ATOM    646  N   HIS A  83      11.477  91.977 227.881  1.00 45.48           N  
ANISOU  646  N   HIS A  83     5901   7146   4233  -1346   -457    247       N  
ATOM    647  CA  HIS A  83      12.057  92.694 229.012  1.00 44.53           C  
ANISOU  647  CA  HIS A  83     5788   7062   4070  -1215   -387    305       C  
ATOM    648  C   HIS A  83      11.828  92.007 230.374  1.00 45.83           C  
ANISOU  648  C   HIS A  83     6055   7140   4219  -1295   -363    435       C  
ATOM    649  O   HIS A  83      12.778  91.629 231.064  1.00 45.28           O  
ANISOU  649  O   HIS A  83     6121   6945   4137  -1213   -395    452       O  
ATOM    650  CB  HIS A  83      11.580  94.143 229.053  1.00 42.96           C  
ANISOU  650  CB  HIS A  83     5413   7079   3831  -1155   -288    327       C  
ATOM    651  CG  HIS A  83      12.287  95.036 228.092  1.00 40.56           C  
ANISOU  651  CG  HIS A  83     5051   6842   3520  -1015   -301    215       C  
ATOM    652  ND1 HIS A  83      13.438  94.661 227.436  1.00 40.65           N  
ANISOU  652  ND1 HIS A  83     5156   6742   3548   -926   -377    103       N  
ATOM    653  CD2 HIS A  83      12.025  96.299 227.691  1.00 39.42           C  
ANISOU  653  CD2 HIS A  83     4764   6859   3356   -945   -239    204       C  
ATOM    654  CE1 HIS A  83      13.853  95.652 226.668  1.00 38.26           C  
ANISOU  654  CE1 HIS A  83     4770   6540   3227   -822   -361     29       C  
ATOM    655  NE2 HIS A  83      13.008  96.655 226.796  1.00 37.63           N  
ANISOU  655  NE2 HIS A  83     4553   6619   3125   -833   -284     90       N  
ATOM    656  N   ILE A  84      10.564  91.834 230.735  1.00 47.52           N  
ANISOU  656  N   ILE A  84     6196   7427   4432  -1459   -309    539       N  
ATOM    657  CA  ILE A  84      10.207  91.149 231.961  1.00 49.58           C  
ANISOU  657  CA  ILE A  84     6551   7618   4670  -1564   -276    674       C  
ATOM    658  C   ILE A  84      10.871  89.789 232.073  1.00 50.90           C  
ANISOU  658  C   ILE A  84     6928   7534   4877  -1597   -382    674       C  
ATOM    659  O   ILE A  84      11.467  89.491 233.098  1.00 51.46           O  
ANISOU  659  O   ILE A  84     7126   7514   4913  -1550   -385    748       O  
ATOM    660  CB  ILE A  84       8.689  90.998 232.073  1.00 51.44           C  
ANISOU  660  CB  ILE A  84     6658   7967   4920  -1763   -211    779       C  
ATOM    661  CG1 ILE A  84       8.063  92.359 232.389  1.00 52.13           C  
ANISOU  661  CG1 ILE A  84     6555   8289   4965  -1697    -70    819       C  
ATOM    662  CG2 ILE A  84       8.303  89.933 233.121  1.00 52.19           C  
ANISOU  662  CG2 ILE A  84     6880   7945   5005  -1920   -201    915       C  
ATOM    663  CD1 ILE A  84       8.054  92.707 233.888  1.00 54.37           C  
ANISOU  663  CD1 ILE A  84     6892   8605   5159  -1669     54    923       C  
ATOM    664  N   SER A  85      10.786  88.971 231.027  1.00 51.93           N  
ANISOU  664  N   SER A  85     7107   7548   5077  -1674   -469    593       N  
ATOM    665  CA  SER A  85      11.383  87.649 231.081  1.00 53.82           C  
ANISOU  665  CA  SER A  85     7561   7519   5367  -1695   -556    587       C  
ATOM    666  C   SER A  85      12.906  87.695 231.153  1.00 53.47           C  
ANISOU  666  C   SER A  85     7619   7365   5333  -1464   -599    522       C  
ATOM    667  O   SER A  85      13.546  86.679 231.353  1.00 54.60           O  
ANISOU  667  O   SER A  85     7936   7283   5525  -1433   -662    537       O  
ATOM    668  CB  SER A  85      10.934  86.806 229.906  1.00 54.74           C  
ANISOU  668  CB  SER A  85     7725   7528   5545  -1837   -628    496       C  
ATOM    669  OG  SER A  85      11.542  87.280 228.742  1.00 54.27           O  
ANISOU  669  OG  SER A  85     7624   7505   5492  -1710   -657    333       O  
ATOM    670  N   HIS A  86      13.482  88.884 231.016  1.00 53.00           N  
ANISOU  670  N   HIS A  86     7442   7463   5232  -1302   -564    462       N  
ATOM    671  CA  HIS A  86      14.936  89.047 231.114  1.00 53.39           C  
ANISOU  671  CA  HIS A  86     7550   7446   5290  -1090   -604    413       C  
ATOM    672  C   HIS A  86      15.368  89.693 232.415  1.00 54.07           C  
ANISOU  672  C   HIS A  86     7632   7616   5297  -1017   -574    519       C  
ATOM    673  O   HIS A  86      16.557  89.893 232.629  1.00 54.17           O  
ANISOU  673  O   HIS A  86     7673   7600   5308   -858   -616    501       O  
ATOM    674  CB  HIS A  86      15.494  89.886 229.949  1.00 51.42           C  
ANISOU  674  CB  HIS A  86     7191   7298   5047   -961   -600    259       C  
ATOM    675  CG  HIS A  86      15.495  89.180 228.625  1.00 50.93           C  
ANISOU  675  CG  HIS A  86     7180   7125   5048   -989   -645    129       C  
ATOM    676  ND1 HIS A  86      15.407  89.855 227.426  1.00 48.36           N  
ANISOU  676  ND1 HIS A  86     6747   6921   4706   -968   -631      6       N  
ATOM    677  CD2 HIS A  86      15.566  87.864 228.315  1.00 51.57           C  
ANISOU  677  CD2 HIS A  86     7424   6975   5194  -1043   -699    101       C  
ATOM    678  CE1 HIS A  86      15.425  88.983 226.436  1.00 50.95           C  
ANISOU  678  CE1 HIS A  86     7173   7111   5074  -1015   -675    -99       C  
ATOM    679  NE2 HIS A  86      15.519  87.767 226.949  1.00 52.66           N  
ANISOU  679  NE2 HIS A  86     7559   7104   5345  -1060   -713    -51       N  
ATOM    680  N   ILE A  87      14.424  90.013 233.290  1.00 49.26           N  
ANISOU  680  N   ILE A  87     6926   7396   4396   -960   -241    937       N  
ATOM    681  CA  ILE A  87      14.724  90.968 234.347  1.00 49.89           C  
ANISOU  681  CA  ILE A  87     6931   7536   4488   -876   -166    952       C  
ATOM    682  C   ILE A  87      14.885  90.340 235.728  1.00 50.95           C  
ANISOU  682  C   ILE A  87     7127   7628   4602   -872   -116    981       C  
ATOM    683  O   ILE A  87      15.639  90.827 236.554  1.00 50.64           O  
ANISOU  683  O   ILE A  87     7089   7607   4545   -779    -68    970       O  
ATOM    684  CB  ILE A  87      13.760  92.246 234.273  1.00 50.09           C  
ANISOU  684  CB  ILE A  87     6784   7675   4573   -889   -140    987       C  
ATOM    685  CG1 ILE A  87      14.461  93.507 234.787  1.00 50.29           C  
ANISOU  685  CG1 ILE A  87     6751   7756   4602   -772    -83    967       C  
ATOM    686  CG2 ILE A  87      12.352  92.010 234.874  1.00 49.86           C  
ANISOU  686  CG2 ILE A  87     6675   7683   4588   -996   -117   1057       C  
ATOM    687  CD1 ILE A  87      15.662  93.938 233.910  1.00 52.37           C  
ANISOU  687  CD1 ILE A  87     7056   8007   4834   -685   -112    905       C  
ATOM    688  N   GLU A  88      14.245  89.196 235.911  1.00 52.64           N  
ANISOU  688  N   GLU A  88     7406   7779   4814   -975   -135   1016       N  
ATOM    689  CA  GLU A  88      14.113  88.515 237.203  1.00 54.15           C  
ANISOU  689  CA  GLU A  88     7653   7932   4989  -1001    -89   1063       C  
ATOM    690  C   GLU A  88      13.397  89.282 238.303  1.00 54.00           C  
ANISOU  690  C   GLU A  88     7516   8004   4997  -1009    -10   1116       C  
ATOM    691  O   GLU A  88      13.994  89.999 239.071  1.00 53.65           O  
ANISOU  691  O   GLU A  88     7449   7999   4935   -914     42   1105       O  
ATOM    692  CB  GLU A  88      15.358  87.692 237.652  1.00 54.51           C  
ANISOU  692  CB  GLU A  88     7857   7879   4976   -922    -96   1036       C  
ATOM    693  CG  GLU A  88      16.631  88.384 238.172  1.00 56.09           C  
ANISOU  693  CG  GLU A  88     8061   8105   5144   -775    -64    997       C  
ATOM    694  CD  GLU A  88      17.656  87.388 238.847  1.00 60.97           C  
ANISOU  694  CD  GLU A  88     8831   8627   5706   -711    -70    992       C  
ATOM    695  OE1 GLU A  88      17.239  86.277 239.291  1.00 63.76           O  
ANISOU  695  OE1 GLU A  88     9279   8900   6048   -784    -76   1036       O  
ATOM    696  OE2 GLU A  88      18.877  87.721 238.946  1.00 60.36           O  
ANISOU  696  OE2 GLU A  88     8778   8558   5600   -589    -69    947       O  
ATOM    697  N   GLU A  89      12.081  89.109 238.339  1.00 55.17           N  
ANISOU  697  N   GLU A  89     7587   8189   5188  -1128     -2   1172       N  
ATOM    698  CA  GLU A  89      11.164  89.920 239.129  1.00 54.98           C  
ANISOU  698  CA  GLU A  89     7422   8269   5200  -1145     73   1222       C  
ATOM    699  C   GLU A  89      11.313  89.798 240.642  1.00 54.84           C  
ANISOU  699  C   GLU A  89     7437   8253   5147  -1119    155   1257       C  
ATOM    700  O   GLU A  89      11.325  90.810 241.330  1.00 54.96           O  
ANISOU  700  O   GLU A  89     7371   8345   5165  -1047    221   1255       O  
ATOM    701  CB  GLU A  89       9.722  89.632 238.706  1.00 56.16           C  
ANISOU  701  CB  GLU A  89     7476   8458   5404  -1287     54   1275       C  
ATOM    702  CG  GLU A  89       9.187  90.608 237.683  1.00 56.41           C  
ANISOU  702  CG  GLU A  89     7370   8575   5490  -1280     21   1262       C  
ATOM    703  CD  GLU A  89       8.054  90.034 236.846  1.00 60.32           C  
ANISOU  703  CD  GLU A  89     7812   9080   6025  -1425    -43   1297       C  
ATOM    704  OE1 GLU A  89       8.336  89.077 236.093  1.00 61.35           O  
ANISOU  704  OE1 GLU A  89     8060   9121   6130  -1483   -121   1271       O  
ATOM    705  OE2 GLU A  89       6.888  90.535 236.924  1.00 61.92           O  
ANISOU  705  OE2 GLU A  89     7858   9383   6286  -1479    -19   1348       O  
ATOM    706  N   THR A  90      11.396  88.587 241.175  1.00 54.71           N  
ANISOU  706  N   THR A  90     7544   8151   5094  -1177    150   1289       N  
ATOM    707  CA  THR A  90      11.690  88.461 242.582  1.00 54.30           C  
ANISOU  707  CA  THR A  90     7542   8097   4993  -1140    221   1320       C  
ATOM    708  C   THR A  90      13.186  88.322 242.677  1.00 53.36           C  
ANISOU  708  C   THR A  90     7547   7911   4818  -1019    192   1266       C  
ATOM    709  O   THR A  90      13.754  87.419 242.095  1.00 53.56           O  
ANISOU  709  O   THR A  90     7690   7836   4824  -1023    127   1244       O  
ATOM    710  CB  THR A  90      11.002  87.242 243.203  1.00 55.77           C  
ANISOU  710  CB  THR A  90     7799   8225   5164  -1266    236   1395       C  
ATOM    711  OG1 THR A  90       9.591  87.328 242.995  1.00 57.81           O  
ANISOU  711  OG1 THR A  90     7929   8552   5482  -1389    256   1446       O  
ATOM    712  CG2 THR A  90      11.239  87.161 244.717  1.00 56.47           C  
ANISOU  712  CG2 THR A  90     7937   8323   5194  -1230    315   1436       C  
ATOM    713  N   ASP A  91      13.841  89.218 243.403  1.00 52.97           N  
ANISOU  713  N   ASP A  91     7469   7917   4740   -910    238   1241       N  
ATOM    714  CA  ASP A  91      15.300  89.153 243.506  1.00 52.89           C  
ANISOU  714  CA  ASP A  91     7558   7858   4678   -792    208   1190       C  
ATOM    715  C   ASP A  91      15.867  89.674 244.836  1.00 52.35           C  
ANISOU  715  C   ASP A  91     7500   7834   4557   -710    267   1193       C  
ATOM    716  O   ASP A  91      15.204  90.433 245.554  1.00 51.77           O  
ANISOU  716  O   ASP A  91     7337   7844   4491   -720    338   1215       O  
ATOM    717  CB  ASP A  91      15.960  89.884 242.313  1.00 52.51           C  
ANISOU  717  CB  ASP A  91     7467   7828   4658   -722    159   1117       C  
ATOM    718  CG  ASP A  91      17.396  89.436 242.070  1.00 53.97           C  
ANISOU  718  CG  ASP A  91     7765   7944   4799   -626    110   1067       C  
ATOM    719  OD1 ASP A  91      17.674  88.229 242.298  1.00 57.33           O  
ANISOU  719  OD1 ASP A  91     8318   8275   5190   -642     83   1088       O  
ATOM    720  OD2 ASP A  91      18.236  90.280 241.653  1.00 53.93           O  
ANISOU  720  OD2 ASP A  91     7720   7976   4794   -535     99   1010       O  
ATOM    721  N   MET A  92      17.090  89.227 245.142  1.00 51.98           N  
ANISOU  721  N   MET A  92     7564   7729   4455   -626    234   1169       N  
ATOM    722  CA  MET A  92      17.924  89.799 246.195  1.00 51.85           C  
ANISOU  722  CA  MET A  92     7561   7756   4383   -530    265   1153       C  
ATOM    723  C   MET A  92      19.190  90.304 245.539  1.00 50.73           C  
ANISOU  723  C   MET A  92     7419   7615   4241   -423    215   1078       C  
ATOM    724  O   MET A  92      19.621  89.723 244.546  1.00 51.23           O  
ANISOU  724  O   MET A  92     7529   7615   4319   -414    156   1052       O  
ATOM    725  CB  MET A  92      18.300  88.746 247.222  1.00 52.89           C  
ANISOU  725  CB  MET A  92     7827   7825   4446   -525    264   1202       C  
ATOM    726  CG  MET A  92      18.886  89.306 248.502  1.00 53.82           C  
ANISOU  726  CG  MET A  92     7954   7999   4496   -450    303   1200       C  
ATOM    727  SD  MET A  92      18.853  88.080 249.823  1.00 58.10           S  
ANISOU  727  SD  MET A  92     8640   8481   4955   -479    319   1286       S  
ATOM    728  CE  MET A  92      17.212  87.351 249.544  1.00 57.90           C  
ANISOU  728  CE  MET A  92     8596   8424   4978   -645    357   1361       C  
ATOM    729  N   SER A  93      19.769  91.381 246.082  1.00 49.69           N  
ANISOU  729  N   SER A  93     7234   7555   4089   -346    242   1041       N  
ATOM    730  CA  SER A  93      21.044  91.942 245.612  1.00 47.95           C  
ANISOU  730  CA  SER A  93     7005   7348   3864   -246    201    973       C  
ATOM    731  C   SER A  93      22.210  91.229 246.261  1.00 47.42           C  
ANISOU  731  C   SER A  93     7045   7241   3733   -172    165    973       C  
ATOM    732  O   SER A  93      22.033  90.168 246.852  1.00 48.44           O  
ANISOU  732  O   SER A  93     7269   7310   3824   -198    162   1025       O  
ATOM    733  CB  SER A  93      21.129  93.431 245.938  1.00 47.57           C  
ANISOU  733  CB  SER A  93     6856   7391   3826   -207    242    935       C  
ATOM    734  OG  SER A  93      21.192  93.653 247.338  1.00 48.91           O  
ANISOU  734  OG  SER A  93     7048   7597   3938   -187    286    953       O  
ATOM    735  N   ALA A  94      23.397  91.828 246.170  1.00 46.25           N  
ANISOU  735  N   ALA A  94     6877   7126   3570    -80    139    917       N  
ATOM    736  CA  ALA A  94      24.614  91.258 246.774  1.00 45.86           C  
ANISOU  736  CA  ALA A  94     6910   7053   3461      5     98    913       C  
ATOM    737  C   ALA A  94      24.882  91.816 248.178  1.00 45.49           C  
ANISOU  737  C   ALA A  94     6862   7069   3353     36    126    921       C  
ATOM    738  O   ALA A  94      25.351  92.958 248.309  1.00 44.54           O  
ANISOU  738  O   ALA A  94     6668   7021   3235     73    135    873       O  
ATOM    739  CB  ALA A  94      25.785  91.507 245.885  1.00 45.53           C  
ANISOU  739  CB  ALA A  94     6845   7019   3437     84     50    852       C  
ATOM    740  N   PRO A  95      24.581  91.011 249.227  1.00 45.68           N  
ANISOU  740  N   PRO A  95     6974   7062   3320     16    139    984       N  
ATOM    741  CA  PRO A  95      24.523  91.449 250.626  1.00 45.56           C  
ANISOU  741  CA  PRO A  95     6969   7106   3237     22    178   1003       C  
ATOM    742  C   PRO A  95      25.888  91.771 251.159  1.00 45.35           C  
ANISOU  742  C   PRO A  95     6955   7118   3157    120    131    966       C  
ATOM    743  O   PRO A  95      26.821  90.995 250.980  1.00 45.89           O  
ANISOU  743  O   PRO A  95     7085   7144   3209    184     69    968       O  
ATOM    744  CB  PRO A  95      23.966  90.227 251.354  1.00 46.35           C  
ANISOU  744  CB  PRO A  95     7179   7143   3290    -24    190   1087       C  
ATOM    745  CG  PRO A  95      23.388  89.370 250.279  1.00 46.88           C  
ANISOU  745  CG  PRO A  95     7270   7125   3419    -83    173   1108       C  
ATOM    746  CD  PRO A  95      24.272  89.583 249.114  1.00 46.13           C  
ANISOU  746  CD  PRO A  95     7139   7019   3369    -19    117   1041       C  
ATOM    747  N   TYR A  96      26.004  92.903 251.827  1.00 45.24           N  
ANISOU  747  N   TYR A  96     6886   7188   3117    132    160    930       N  
ATOM    748  CA  TYR A  96      27.302  93.350 252.317  1.00 45.80           C  
ANISOU  748  CA  TYR A  96     6954   7308   3140    213    111    888       C  
ATOM    749  C   TYR A  96      27.355  93.635 253.854  1.00 46.71           C  
ANISOU  749  C   TYR A  96     7113   7477   3157    220    131    904       C  
ATOM    750  O   TYR A  96      26.346  94.005 254.473  1.00 47.30           O  
ANISOU  750  O   TYR A  96     7184   7577   3212    163    204    923       O  
ATOM    751  CB  TYR A  96      27.742  94.561 251.493  1.00 44.95           C  
ANISOU  751  CB  TYR A  96     6737   7249   3092    230    106    810       C  
ATOM    752  CG  TYR A  96      26.720  95.667 251.484  1.00 44.93           C  
ANISOU  752  CG  TYR A  96     6661   7284   3125    170    180    789       C  
ATOM    753  CD1 TYR A  96      25.671  95.683 250.570  1.00 45.36           C  
ANISOU  753  CD1 TYR A  96     6670   7310   3254    112    217    803       C  
ATOM    754  CD2 TYR A  96      26.797  96.699 252.410  1.00 45.68           C  
ANISOU  754  CD2 TYR A  96     6735   7445   3178    176    209    755       C  
ATOM    755  CE1 TYR A  96      24.726  96.713 250.593  1.00 46.01           C  
ANISOU  755  CE1 TYR A  96     6680   7430   3371     69    284    788       C  
ATOM    756  CE2 TYR A  96      25.871  97.729 252.434  1.00 45.37           C  
ANISOU  756  CE2 TYR A  96     6633   7435   3171    134    280    734       C  
ATOM    757  CZ  TYR A  96      24.842  97.730 251.535  1.00 45.44           C  
ANISOU  757  CZ  TYR A  96     6591   7417   3258     86    318    753       C  
ATOM    758  OH  TYR A  96      23.949  98.764 251.612  1.00 46.58           O  
ANISOU  758  OH  TYR A  96     6671   7594   3435     57    388    734       O  
ATOM    759  N   VAL A  97      28.518  93.434 254.470  1.00 46.58           N  
ANISOU  759  N   VAL A  97     7139   7485   3076    292     67    897       N  
ATOM    760  CA  VAL A  97      28.656  93.748 255.867  1.00 47.07           C  
ANISOU  760  CA  VAL A  97     7244   7604   3038    301     76    905       C  
ATOM    761  C   VAL A  97      28.688  95.271 255.952  1.00 46.40           C  
ANISOU  761  C   VAL A  97     7070   7594   2966    288    107    827       C  
ATOM    762  O   VAL A  97      29.425  95.907 255.201  1.00 45.69           O  
ANISOU  762  O   VAL A  97     6906   7526   2930    317     70    766       O  
ATOM    763  CB  VAL A  97      29.954  93.087 256.512  1.00 48.41           C  
ANISOU  763  CB  VAL A  97     7482   7783   3131    386    -16    924       C  
ATOM    764  CG1 VAL A  97      30.326  93.751 257.828  1.00 48.08           C  
ANISOU  764  CG1 VAL A  97     7459   7822   2986    398    -22    906       C  
ATOM    765  CG2 VAL A  97      29.798  91.554 256.740  1.00 49.18           C  
ANISOU  765  CG2 VAL A  97     7696   7795   3194    398    -37   1015       C  
ATOM    766  N   TYR A  98      27.831  95.820 256.816  1.00 46.73           N  
ANISOU  766  N   TYR A  98     7123   7671   2961    243    180    830       N  
ATOM    767  CA  TYR A  98      27.878  97.193 257.354  1.00 46.75           C  
ANISOU  767  CA  TYR A  98     7081   7743   2939    238    211    760       C  
ATOM    768  C   TYR A  98      27.727  97.028 258.857  1.00 48.23           C  
ANISOU  768  C   TYR A  98     7357   7968   2999    236    234    789       C  
ATOM    769  O   TYR A  98      26.613  96.805 259.363  1.00 48.24           O  
ANISOU  769  O   TYR A  98     7391   7964   2972    189    315    835       O  
ATOM    770  CB  TYR A  98      26.667  98.011 256.894  1.00 46.33           C  
ANISOU  770  CB  TYR A  98     6957   7689   2957    184    304    739       C  
ATOM    771  CG  TYR A  98      26.761  99.543 256.978  1.00 45.63           C  
ANISOU  771  CG  TYR A  98     6806   7648   2883    186    332    654       C  
ATOM    772  CD1 TYR A  98      27.681 100.188 257.812  1.00 44.10           C  
ANISOU  772  CD1 TYR A  98     6637   7505   2613    216    292    599       C  
ATOM    773  CD2 TYR A  98      25.904 100.347 256.205  1.00 44.99           C  
ANISOU  773  CD2 TYR A  98     6643   7556   2894    157    394    628       C  
ATOM    774  CE1 TYR A  98      27.765 101.599 257.854  1.00 43.78           C  
ANISOU  774  CE1 TYR A  98     6549   7494   2590    211    316    517       C  
ATOM    775  CE2 TYR A  98      25.970 101.756 256.249  1.00 44.61           C  
ANISOU  775  CE2 TYR A  98     6547   7536   2865    161    420    552       C  
ATOM    776  CZ  TYR A  98      26.905 102.373 257.078  1.00 43.83           C  
ANISOU  776  CZ  TYR A  98     6484   7480   2691    186    382    494       C  
ATOM    777  OH  TYR A  98      26.969 103.747 257.110  1.00 41.70           O  
ANISOU  777  OH  TYR A  98     6178   7225   2442    184    406    417       O  
ATOM    778  N   ASP A  99      28.838  97.143 259.575  1.00 49.62           N  
ANISOU  778  N   ASP A  99     7570   8189   3095    283    161    765       N  
ATOM    779  CA  ASP A  99      28.838  97.021 261.036  1.00 51.47           C  
ANISOU  779  CA  ASP A  99     7897   8467   3193    286    169    789       C  
ATOM    780  C   ASP A  99      28.347  95.644 261.475  1.00 52.86           C  
ANISOU  780  C   ASP A  99     8170   8597   3317    276    181    895       C  
ATOM    781  O   ASP A  99      28.802  94.616 260.965  1.00 53.00           O  
ANISOU  781  O   ASP A  99     8214   8560   3364    307    120    944       O  
ATOM    782  CB  ASP A  99      27.980  98.120 261.674  1.00 51.62           C  
ANISOU  782  CB  ASP A  99     7904   8530   3178    244    266    743       C  
ATOM    783  CG  ASP A  99      28.687  99.465 261.727  1.00 52.07           C  
ANISOU  783  CG  ASP A  99     7910   8637   3237    258    238    638       C  
ATOM    784  OD1 ASP A  99      29.511  99.649 262.644  1.00 54.52           O  
ANISOU  784  OD1 ASP A  99     8272   9000   3445    282    180    613       O  
ATOM    785  OD2 ASP A  99      28.395 100.354 260.891  1.00 51.99           O  
ANISOU  785  OD2 ASP A  99     7814   8615   3325    241    273    583       O  
ATOM    786  N   ARG A 100      27.386  95.650 262.396  1.00 54.69           N  
ANISOU  786  N   ARG A 100     8456   8849   3475    231    267    930       N  
ATOM    787  CA  ARG A 100      26.820  94.446 263.031  1.00 56.21           C  
ANISOU  787  CA  ARG A 100     8752   9008   3599    206    294   1036       C  
ATOM    788  C   ARG A 100      25.709  93.862 262.144  1.00 55.17           C  
ANISOU  788  C   ARG A 100     8587   8806   3569    146    358   1088       C  
ATOM    789  O   ARG A 100      24.861  93.101 262.606  1.00 55.57           O  
ANISOU  789  O   ARG A 100     8701   8832   3582     96    416   1170       O  
ATOM    790  CB  ARG A 100      26.297  94.830 264.437  1.00 58.06           C  
ANISOU  790  CB  ARG A 100     9052   9308   3701    181    366   1045       C  
ATOM    791  CG  ARG A 100      25.913  93.690 265.386  1.00 62.45           C  
ANISOU  791  CG  ARG A 100     9733   9847   4148    159    387   1156       C  
ATOM    792  CD  ARG A 100      24.373  93.489 265.552  1.00 66.60           C  
ANISOU  792  CD  ARG A 100    10258  10365   4683     75    523   1212       C  
ATOM    793  NE  ARG A 100      23.998  92.233 266.242  1.00 71.84           N  
ANISOU  793  NE  ARG A 100    11040  10992   5264     42    539   1333       N  
ATOM    794  CZ  ARG A 100      24.687  91.071 266.240  1.00 74.59           C  
ANISOU  794  CZ  ARG A 100    11478  11276   5589     73    447   1405       C  
ATOM    795  NH1 ARG A 100      25.832  90.923 265.566  1.00 74.09           N  
ANISOU  795  NH1 ARG A 100    11396  11178   5577    146    330   1371       N  
ATOM    796  NH2 ARG A 100      24.216  90.020 266.917  1.00 76.29           N  
ANISOU  796  NH2 ARG A 100    11805  11455   5726     33    476   1518       N  
ATOM    797  N   PHE A 101      25.732  94.211 260.860  1.00 53.52           N  
ANISOU  797  N   PHE A 101     8281   8568   3488    146    344   1041       N  
ATOM    798  CA  PHE A 101      24.649  93.817 259.969  1.00 53.20           C  
ANISOU  798  CA  PHE A 101     8196   8473   3546     83    401   1077       C  
ATOM    799  C   PHE A 101      25.123  93.386 258.583  1.00 52.13           C  
ANISOU  799  C   PHE A 101     8019   8270   3517    104    332   1065       C  
ATOM    800  O   PHE A 101      26.206  93.766 258.152  1.00 52.32           O  
ANISOU  800  O   PHE A 101     8010   8307   3562    166    259   1007       O  
ATOM    801  CB  PHE A 101      23.650  94.967 259.807  1.00 52.96           C  
ANISOU  801  CB  PHE A 101     8068   8489   3565     41    498   1030       C  
ATOM    802  CG  PHE A 101      22.961  95.376 261.085  1.00 53.61           C  
ANISOU  802  CG  PHE A 101     8185   8635   3549     16    589   1041       C  
ATOM    803  CD1 PHE A 101      21.917  94.618 261.608  1.00 53.68           C  
ANISOU  803  CD1 PHE A 101     8239   8634   3521    -47    666   1128       C  
ATOM    804  CD2 PHE A 101      23.351  96.527 261.758  1.00 52.76           C  
ANISOU  804  CD2 PHE A 101     8067   8595   3383     52    602    963       C  
ATOM    805  CE1 PHE A 101      21.279  95.012 262.770  1.00 53.08           C  
ANISOU  805  CE1 PHE A 101     8192   8625   3351    -68    759   1138       C  
ATOM    806  CE2 PHE A 101      22.715  96.914 262.923  1.00 52.28           C  
ANISOU  806  CE2 PHE A 101     8045   8593   3225     33    692    967       C  
ATOM    807  CZ  PHE A 101      21.683  96.160 263.422  1.00 52.56           C  
ANISOU  807  CZ  PHE A 101     8120   8626   3223    -23    773   1054       C  
ATOM    808  N   LEU A 102      24.317  92.579 257.900  1.00 51.11           N  
ANISOU  808  N   LEU A 102     7895   8074   3452     48    355   1119       N  
ATOM    809  CA  LEU A 102      24.481  92.365 256.474  1.00 49.79           C  
ANISOU  809  CA  LEU A 102     7674   7851   3393     52    312   1096       C  
ATOM    810  C   LEU A 102      23.330  93.102 255.863  1.00 48.71           C  
ANISOU  810  C   LEU A 102     7435   7736   3336    -14    388   1076       C  
ATOM    811  O   LEU A 102      22.182  92.846 256.255  1.00 49.29           O  
ANISOU  811  O   LEU A 102     7514   7811   3402    -85    462   1130       O  
ATOM    812  CB  LEU A 102      24.371  90.888 256.102  1.00 50.46           C  
ANISOU  812  CB  LEU A 102     7846   7836   3490     31    277   1169       C  
ATOM    813  CG  LEU A 102      25.644  90.042 256.146  1.00 51.30           C  
ANISOU  813  CG  LEU A 102     8040   7894   3559    117    180   1181       C  
ATOM    814  CD1 LEU A 102      25.353  88.566 256.402  1.00 52.04           C  
ANISOU  814  CD1 LEU A 102     8261   7891   3622     90    167   1275       C  
ATOM    815  CD2 LEU A 102      26.421  90.217 254.862  1.00 51.25           C  
ANISOU  815  CD2 LEU A 102     7971   7868   3635    170    121   1117       C  
ATOM    816  N   TYR A 103      23.631  94.027 254.940  1.00 46.50           N  
ANISOU  816  N   TYR A 103     7059   7477   3131     11    371   1002       N  
ATOM    817  CA  TYR A 103      22.603  94.818 254.234  1.00 45.20           C  
ANISOU  817  CA  TYR A 103     6789   7334   3053    -39    433    980       C  
ATOM    818  C   TYR A 103      22.381  94.341 252.790  1.00 44.56           C  
ANISOU  818  C   TYR A 103     6670   7193   3067    -67    397    986       C  
ATOM    819  O   TYR A 103      23.325  93.936 252.099  1.00 44.29           O  
ANISOU  819  O   TYR A 103     6660   7119   3049    -22    322    964       O  
ATOM    820  CB  TYR A 103      22.952  96.320 254.212  1.00 44.48           C  
ANISOU  820  CB  TYR A 103     6617   7305   2977      0    447    897       C  
ATOM    821  CG  TYR A 103      22.548  97.110 255.432  1.00 42.57           C  
ANISOU  821  CG  TYR A 103     6379   7128   2668      0    520    882       C  
ATOM    822  CD1 TYR A 103      23.186  96.911 256.651  1.00 43.70           C  
ANISOU  822  CD1 TYR A 103     6610   7297   2699     31    504    888       C  
ATOM    823  CD2 TYR A 103      21.566  98.069 255.364  1.00 41.15           C  
ANISOU  823  CD2 TYR A 103     6119   6984   2533    -25    601    861       C  
ATOM    824  CE1 TYR A 103      22.848  97.625 257.767  1.00 42.27           C  
ANISOU  824  CE1 TYR A 103     6441   7174   2445     31    571    868       C  
ATOM    825  CE2 TYR A 103      21.202  98.780 256.489  1.00 41.73           C  
ANISOU  825  CE2 TYR A 103     6203   7113   2540    -18    673    841       C  
ATOM    826  CZ  TYR A 103      21.858  98.551 257.682  1.00 41.96           C  
ANISOU  826  CZ  TYR A 103     6326   7165   2451      8    658    842       C  
ATOM    827  OH  TYR A 103      21.524  99.231 258.815  1.00 43.71           O  
ANISOU  827  OH  TYR A 103     6571   7444   2595     15    730    818       O  
ATOM    828  N   TYR A 104      21.136  94.402 252.336  1.00 43.90           N  
ANISOU  828  N   TYR A 104     6528   7110   3044   -139    451   1013       N  
ATOM    829  CA  TYR A 104      20.820  93.993 250.985  1.00 43.21           C  
ANISOU  829  CA  TYR A 104     6405   6972   3040   -175    417   1017       C  
ATOM    830  C   TYR A 104      19.518  94.589 250.531  1.00 43.44           C  
ANISOU  830  C   TYR A 104     6330   7036   3140   -239    477   1026       C  
ATOM    831  O   TYR A 104      18.697  95.000 251.346  1.00 43.28           O  
ANISOU  831  O   TYR A 104     6277   7066   3101   -266    555   1048       O  
ATOM    832  CB  TYR A 104      20.766  92.467 250.866  1.00 43.79           C  
ANISOU  832  CB  TYR A 104     6578   6960   3098   -214    379   1078       C  
ATOM    833  CG  TYR A 104      19.796  91.815 251.815  1.00 43.10           C  
ANISOU  833  CG  TYR A 104     6537   6870   2969   -287    439   1157       C  
ATOM    834  CD1 TYR A 104      20.195  91.453 253.104  1.00 43.26           C  
ANISOU  834  CD1 TYR A 104     6648   6896   2892   -261    451   1190       C  
ATOM    835  CD2 TYR A 104      18.487  91.566 251.434  1.00 41.67           C  
ANISOU  835  CD2 TYR A 104     6305   6684   2842   -386    482   1202       C  
ATOM    836  CE1 TYR A 104      19.311  90.853 254.005  1.00 43.09           C  
ANISOU  836  CE1 TYR A 104     6673   6874   2824   -332    513   1268       C  
ATOM    837  CE2 TYR A 104      17.596  90.964 252.309  1.00 43.14           C  
ANISOU  837  CE2 TYR A 104     6527   6873   2991   -461    543   1278       C  
ATOM    838  CZ  TYR A 104      18.013  90.600 253.603  1.00 43.28           C  
ANISOU  838  CZ  TYR A 104     6642   6894   2907   -435    562   1313       C  
ATOM    839  OH  TYR A 104      17.137  90.003 254.491  1.00 42.09           O  
ANISOU  839  OH  TYR A 104     6532   6749   2713   -513    629   1394       O  
ATOM    840  N   THR A 105      19.352  94.636 249.213  1.00 44.04           N  
ANISOU  840  N   THR A 105     6351   7088   3293   -257    441   1009       N  
ATOM    841  CA  THR A 105      18.109  95.108 248.595  1.00 45.32           C  
ANISOU  841  CA  THR A 105     6408   7280   3530   -318    482   1024       C  
ATOM    842  C   THR A 105      17.272  93.915 248.119  1.00 45.86           C  
ANISOU  842  C   THR A 105     6500   7297   3626   -412    467   1086       C  
ATOM    843  O   THR A 105      17.848  92.852 247.833  1.00 45.93           O  
ANISOU  843  O   THR A 105     6606   7232   3614   -416    407   1098       O  
ATOM    844  CB  THR A 105      18.385  96.150 247.456  1.00 44.56           C  
ANISOU  844  CB  THR A 105     6226   7204   3501   -280    453    964       C  
ATOM    845  OG1 THR A 105      17.480  97.252 247.618  1.00 46.29           O  
ANISOU  845  OG1 THR A 105     6342   7487   3760   -286    521    960       O  
ATOM    846  CG2 THR A 105      18.266  95.544 245.995  1.00 44.60           C  
ANISOU  846  CG2 THR A 105     6224   7159   3563   -320    388    969       C  
ATOM    847  N   ARG A 106      15.942  94.083 248.071  1.00 46.35           N  
ANISOU  847  N   ARG A 106     6478   7400   3734   -486    520   1127       N  
ATOM    848  CA  ARG A 106      15.025  93.029 247.566  1.00 47.71           C  
ANISOU  848  CA  ARG A 106     6656   7532   3941   -594    505   1186       C  
ATOM    849  C   ARG A 106      13.919  93.519 246.611  1.00 48.64           C  
ANISOU  849  C   ARG A 106     6642   7693   4147   -651    511   1195       C  
ATOM    850  O   ARG A 106      13.361  94.589 246.809  1.00 49.07           O  
ANISOU  850  O   ARG A 106     6589   7825   4232   -628    568   1186       O  
ATOM    851  CB  ARG A 106      14.371  92.271 248.728  1.00 48.48           C  
ANISOU  851  CB  ARG A 106     6800   7630   3989   -660    565   1260       C  
ATOM    852  CG  ARG A 106      15.280  91.295 249.462  1.00 47.15           C  
ANISOU  852  CG  ARG A 106     6786   7392   3738   -636    537   1278       C  
ATOM    853  CD  ARG A 106      14.521  90.112 249.960  1.00 45.78           C  
ANISOU  853  CD  ARG A 106     6676   7176   3543   -741    560   1364       C  
ATOM    854  NE  ARG A 106      13.518  90.483 250.945  1.00 47.43           N  
ANISOU  854  NE  ARG A 106     6819   7467   3735   -787    664   1411       N  
ATOM    855  CZ  ARG A 106      12.203  90.518 250.711  1.00 48.51           C  
ANISOU  855  CZ  ARG A 106     6851   7650   3930   -884    712   1455       C  
ATOM    856  NH1 ARG A 106      11.722  90.215 249.509  1.00 48.59           N  
ANISOU  856  NH1 ARG A 106     6812   7631   4019   -950    657   1456       N  
ATOM    857  NH2 ARG A 106      11.365  90.865 251.682  1.00 47.49           N  
ANISOU  857  NH2 ARG A 106     6662   7602   3778   -913    815   1496       N  
ATOM    858  N   ASP A 107      13.594  92.734 245.586  1.00 49.88           N  
ANISOU  858  N   ASP A 107     6811   7799   4343   -724    449   1211       N  
ATOM    859  CA  ASP A 107      12.459  93.037 244.714  1.00 51.18           C  
ANISOU  859  CA  ASP A 107     6854   8007   4586   -793    444   1231       C  
ATOM    860  C   ASP A 107      11.417  91.943 244.840  1.00 52.37           C  
ANISOU  860  C   ASP A 107     7013   8139   4749   -925    451   1304       C  
ATOM    861  O   ASP A 107      11.773  90.783 244.993  1.00 53.33           O  
ANISOU  861  O   ASP A 107     7258   8174   4830   -966    418   1325       O  
ATOM    862  CB  ASP A 107      12.924  93.101 243.275  1.00 51.16           C  
ANISOU  862  CB  ASP A 107     6853   7969   4617   -777    357   1184       C  
ATOM    863  CG  ASP A 107      13.946  94.207 243.040  1.00 54.66           C  
ANISOU  863  CG  ASP A 107     7281   8432   5054   -658    349   1116       C  
ATOM    864  OD1 ASP A 107      13.550  95.408 243.112  1.00 59.01           O  
ANISOU  864  OD1 ASP A 107     7724   9057   5641   -620    393   1105       O  
ATOM    865  OD2 ASP A 107      15.146  93.888 242.776  1.00 58.42           O  
ANISOU  865  OD2 ASP A 107     7853   8852   5492   -602    299   1073       O  
ATOM    866  N   VAL A 108      10.133  92.291 244.777  1.00 52.86           N  
ANISOU  866  N   VAL A 108     6941   8276   4866   -993    494   1346       N  
ATOM    867  CA  VAL A 108       9.076  91.269 244.773  1.00 53.47           C  
ANISOU  867  CA  VAL A 108     7008   8343   4966  -1136    494   1418       C  
ATOM    868  C   VAL A 108       8.311  91.357 243.478  1.00 53.07           C  
ANISOU  868  C   VAL A 108     6857   8315   4990  -1204    432   1420       C  
ATOM    869  O   VAL A 108       8.079  92.454 243.006  1.00 52.23           O  
ANISOU  869  O   VAL A 108     6634   8281   4931  -1147    438   1395       O  
ATOM    870  CB  VAL A 108       8.092  91.440 245.947  1.00 54.44           C  
ANISOU  870  CB  VAL A 108     7051   8548   5084  -1179    605   1481       C  
ATOM    871  CG1 VAL A 108       7.247  90.173 246.131  1.00 55.40           C  
ANISOU  871  CG1 VAL A 108     7202   8639   5210  -1334    607   1560       C  
ATOM    872  CG2 VAL A 108       8.843  91.730 247.205  1.00 54.18           C  
ANISOU  872  CG2 VAL A 108     7094   8518   4973  -1087    672   1467       C  
ATOM    873  N   LYS A 109       7.896  90.204 242.947  1.00 53.96           N  
ANISOU  873  N   LYS A 109     7022   8366   5115  -1328    373   1453       N  
ATOM    874  CA  LYS A 109       7.251  90.069 241.602  1.00 54.65           C  
ANISOU  874  CA  LYS A 109     7042   8460   5263  -1409    290   1451       C  
ATOM    875  C   LYS A 109       6.107  90.994 241.187  1.00 54.75           C  
ANISOU  875  C   LYS A 109     6856   8596   5352  -1431    308   1476       C  
ATOM    876  O   LYS A 109       5.956  91.253 240.013  1.00 55.36           O  
ANISOU  876  O   LYS A 109     6884   8685   5467  -1441    232   1452       O  
ATOM    877  CB  LYS A 109       6.824  88.623 241.261  1.00 55.86           C  
ANISOU  877  CB  LYS A 109     7283   8529   5414  -1562    231   1489       C  
ATOM    878  CG  LYS A 109       6.601  88.419 239.740  1.00 55.90           C  
ANISOU  878  CG  LYS A 109     7273   8511   5456  -1622    121   1459       C  
ATOM    879  CD  LYS A 109       5.956  87.100 239.358  1.00 57.77           C  
ANISOU  879  CD  LYS A 109     7572   8676   5700  -1792     62   1497       C  
ATOM    880  CE  LYS A 109       5.402  87.177 237.943  1.00 58.42           C  
ANISOU  880  CE  LYS A 109     7586   8784   5827  -1861    -35   1477       C  
ATOM    881  NZ  LYS A 109       4.346  86.155 237.667  1.00 59.58           N  
ANISOU  881  NZ  LYS A 109     7726   8909   6003  -2053    -82   1529       N  
ATOM    882  N   GLY A 110       5.280  91.474 242.087  1.00 55.04           N  
ANISOU  882  N   GLY A 110     6775   8726   5410  -1438    404   1524       N  
ATOM    883  CA  GLY A 110       4.257  92.391 241.609  1.00 54.96           C  
ANISOU  883  CA  GLY A 110     6573   8832   5478  -1439    415   1544       C  
ATOM    884  C   GLY A 110       4.610  93.859 241.718  1.00 53.59           C  
ANISOU  884  C   GLY A 110     6326   8718   5317  -1284    461   1500       C  
ATOM    885  O   GLY A 110       3.880  94.692 241.191  1.00 54.30           O  
ANISOU  885  O   GLY A 110     6267   8892   5473  -1264    458   1510       O  
ATOM    886  N   LEU A 111       5.734  94.161 242.378  1.00 52.19           N  
ANISOU  886  N   LEU A 111     6257   8494   5078  -1176    496   1451       N  
ATOM    887  CA  LEU A 111       6.003  95.473 243.006  1.00 50.88           C  
ANISOU  887  CA  LEU A 111     6037   8384   4910  -1042    574   1418       C  
ATOM    888  C   LEU A 111       7.091  96.287 242.343  1.00 49.54           C  
ANISOU  888  C   LEU A 111     5913   8177   4732   -928    524   1344       C  
ATOM    889  O   LEU A 111       8.125  95.751 241.922  1.00 48.71           O  
ANISOU  889  O   LEU A 111     5936   7987   4584   -919    457   1306       O  
ATOM    890  CB  LEU A 111       6.399  95.299 244.465  1.00 50.81           C  
ANISOU  890  CB  LEU A 111     6110   8366   4831  -1011    665   1422       C  
ATOM    891  CG  LEU A 111       5.525  94.382 245.313  1.00 52.79           C  
ANISOU  891  CG  LEU A 111     6350   8640   5068  -1124    727   1497       C  
ATOM    892  CD1 LEU A 111       5.637  94.723 246.825  1.00 51.66           C  
ANISOU  892  CD1 LEU A 111     6232   8535   4863  -1065    846   1503       C  
ATOM    893  CD2 LEU A 111       4.058  94.427 244.832  1.00 53.65           C  
ANISOU  893  CD2 LEU A 111     6285   8839   5262  -1215    735   1557       C  
ATOM    894  N   SER A 112       6.869  97.604 242.319  1.00 49.30           N  
ANISOU  894  N   SER A 112     5779   8210   4743   -837    564   1326       N  
ATOM    895  CA  SER A 112       7.609  98.526 241.447  1.00 47.88           C  
ANISOU  895  CA  SER A 112     5604   8011   4578   -746    512   1270       C  
ATOM    896  C   SER A 112       8.840  99.139 242.082  1.00 46.49           C  
ANISOU  896  C   SER A 112     5520   7797   4347   -638    544   1207       C  
ATOM    897  O   SER A 112       9.637  99.782 241.388  1.00 45.75           O  
ANISOU  897  O   SER A 112     5452   7675   4256   -573    498   1160       O  
ATOM    898  CB  SER A 112       6.686  99.643 240.959  1.00 48.36           C  
ANISOU  898  CB  SER A 112     5506   8152   4719   -707    527   1289       C  
ATOM    899  OG  SER A 112       5.493  99.112 240.410  1.00 49.50           O  
ANISOU  899  OG  SER A 112     5546   8345   4915   -809    495   1351       O  
ATOM    900  N   TYR A 113       8.975  98.951 243.392  1.00 45.94           N  
ANISOU  900  N   TYR A 113     5498   7731   4225   -626    622   1210       N  
ATOM    901  CA  TYR A 113      10.026  99.578 244.160  1.00 44.63           C  
ANISOU  901  CA  TYR A 113     5408   7543   4005   -530    658   1153       C  
ATOM    902  C   TYR A 113      10.793  98.604 245.040  1.00 45.47           C  
ANISOU  902  C   TYR A 113     5651   7600   4026   -548    662   1151       C  
ATOM    903  O   TYR A 113      10.232  97.646 245.600  1.00 46.38           O  
ANISOU  903  O   TYR A 113     5786   7718   4120   -627    689   1204       O  
ATOM    904  CB  TYR A 113       9.419 100.675 245.001  1.00 44.58           C  
ANISOU  904  CB  TYR A 113     5316   7605   4016   -466    759   1150       C  
ATOM    905  CG  TYR A 113       8.838 101.741 244.164  1.00 42.33           C  
ANISOU  905  CG  TYR A 113     4912   7359   3814   -423    751   1147       C  
ATOM    906  CD1 TYR A 113       9.651 102.737 243.647  1.00 41.87           C  
ANISOU  906  CD1 TYR A 113     4874   7270   3766   -339    719   1091       C  
ATOM    907  CD2 TYR A 113       7.486 101.754 243.861  1.00 41.61           C  
ANISOU  907  CD2 TYR A 113     4686   7334   3791   -467    772   1206       C  
ATOM    908  CE1 TYR A 113       9.140 103.750 242.856  1.00 40.69           C  
ANISOU  908  CE1 TYR A 113     4624   7147   3690   -295    709   1094       C  
ATOM    909  CE2 TYR A 113       6.953 102.743 243.058  1.00 41.22           C  
ANISOU  909  CE2 TYR A 113     4525   7319   3818   -419    757   1209       C  
ATOM    910  CZ  TYR A 113       7.793 103.739 242.556  1.00 41.27           C  
ANISOU  910  CZ  TYR A 113     4565   7285   3829   -331    725   1154       C  
ATOM    911  OH  TYR A 113       7.310 104.735 241.761  1.00 39.00           O  
ANISOU  911  OH  TYR A 113     4181   7024   3615   -279    708   1162       O  
ATOM    912  N   LYS A 114      12.089  98.848 245.173  1.00 45.45           N  
ANISOU  912  N   LYS A 114     5740   7553   3975   -478    634   1093       N  
ATOM    913  CA  LYS A 114      12.891  97.984 246.030  1.00 46.77           C  
ANISOU  913  CA  LYS A 114     6035   7676   4059   -480    632   1091       C  
ATOM    914  C   LYS A 114      12.500  98.073 247.516  1.00 47.26           C  
ANISOU  914  C   LYS A 114     6105   7781   4069   -474    730   1113       C  
ATOM    915  O   LYS A 114      11.878  99.034 247.960  1.00 47.44           O  
ANISOU  915  O   LYS A 114     6045   7868   4113   -440    805   1107       O  
ATOM    916  CB  LYS A 114      14.428  98.122 245.800  1.00 46.41           C  
ANISOU  916  CB  LYS A 114     6081   7579   3972   -408    572   1028       C  
ATOM    917  CG  LYS A 114      14.933  99.276 244.896  1.00 47.87           C  
ANISOU  917  CG  LYS A 114     6215   7772   4201   -343    539    973       C  
ATOM    918  CD  LYS A 114      16.180  98.884 244.020  1.00 49.05           C  
ANISOU  918  CD  LYS A 114     6439   7865   4334   -320    452    934       C  
ATOM    919  CE  LYS A 114      15.789  98.097 242.718  1.00 47.87           C  
ANISOU  919  CE  LYS A 114     6283   7683   4224   -385    385    959       C  
ATOM    920  NZ  LYS A 114      16.958  97.534 241.947  1.00 45.32           N  
ANISOU  920  NZ  LYS A 114     6044   7303   3874   -362    310    922       N  
ATOM    921  N   LEU A 115      12.832  97.027 248.254  1.00 47.53           N  
ANISOU  921  N   LEU A 115     6245   7781   4034   -508    730   1142       N  
ATOM    922  CA  LEU A 115      12.799  97.047 249.690  1.00 48.54           C  
ANISOU  922  CA  LEU A 115     6415   7940   4087   -492    809   1155       C  
ATOM    923  C   LEU A 115      14.258  97.144 250.105  1.00 48.42           C  
ANISOU  923  C   LEU A 115     6510   7887   3999   -415    767   1100       C  
ATOM    924  O   LEU A 115      15.131  96.630 249.386  1.00 48.27           O  
ANISOU  924  O   LEU A 115     6552   7807   3983   -405    679   1081       O  
ATOM    925  CB  LEU A 115      12.211  95.737 250.205  1.00 49.68           C  
ANISOU  925  CB  LEU A 115     6612   8067   4198   -589    829   1234       C  
ATOM    926  CG  LEU A 115      10.698  95.516 250.285  1.00 50.70           C  
ANISOU  926  CG  LEU A 115     6638   8252   4374   -681    896   1303       C  
ATOM    927  CD1 LEU A 115       9.976  95.918 249.035  1.00 51.84           C  
ANISOU  927  CD1 LEU A 115     6656   8419   4623   -708    863   1302       C  
ATOM    928  CD2 LEU A 115      10.442  94.061 250.551  1.00 52.04           C  
ANISOU  928  CD2 LEU A 115     6891   8373   4511   -785    883   1376       C  
ATOM    929  N   HIS A 116      14.527  97.795 251.241  1.00 48.74           N  
ANISOU  929  N   HIS A 116     6575   7967   3976   -359    827   1073       N  
ATOM    930  CA  HIS A 116      15.882  97.919 251.783  1.00 48.43           C  
ANISOU  930  CA  HIS A 116     6634   7906   3862   -291    787   1023       C  
ATOM    931  C   HIS A 116      15.915  97.150 253.087  1.00 49.92           C  
ANISOU  931  C   HIS A 116     6918   8099   3950   -310    824   1067       C  
ATOM    932  O   HIS A 116      15.358  97.610 254.079  1.00 50.78           O  
ANISOU  932  O   HIS A 116     7012   8265   4016   -306    913   1073       O  
ATOM    933  CB  HIS A 116      16.224  99.376 252.079  1.00 47.89           C  
ANISOU  933  CB  HIS A 116     6526   7879   3792   -214    819    949       C  
ATOM    934  CG  HIS A 116      16.244 100.257 250.873  1.00 46.83           C  
ANISOU  934  CG  HIS A 116     6305   7738   3749   -188    787    908       C  
ATOM    935  ND1 HIS A 116      17.411 100.720 250.316  1.00 45.36           N  
ANISOU  935  ND1 HIS A 116     6142   7525   3570   -138    717    849       N  
ATOM    936  CD2 HIS A 116      15.235 100.778 250.130  1.00 47.23           C  
ANISOU  936  CD2 HIS A 116     6246   7812   3888   -206    815    922       C  
ATOM    937  CE1 HIS A 116      17.121 101.476 249.267  1.00 46.23           C  
ANISOU  937  CE1 HIS A 116     6167   7635   3764   -129    705    830       C  
ATOM    938  NE2 HIS A 116      15.807 101.529 249.133  1.00 44.82           N  
ANISOU  938  NE2 HIS A 116     5908   7486   3636   -166    760    874       N  
ATOM    939  N   CYS A 117      16.564  95.986 253.102  1.00 50.42           N  
ANISOU  939  N   CYS A 117     7084   8101   3972   -327    760   1099       N  
ATOM    940  CA  CYS A 117      16.488  95.115 254.262  1.00 51.44           C  
ANISOU  940  CA  CYS A 117     7310   8226   4009   -357    791   1158       C  
ATOM    941  C   CYS A 117      17.836  94.915 254.866  1.00 51.45           C  
ANISOU  941  C   CYS A 117     7421   8204   3923   -288    732   1132       C  
ATOM    942  O   CYS A 117      18.862  95.309 254.303  1.00 50.66           O  
ANISOU  942  O   CYS A 117     7320   8087   3841   -225    661   1071       O  
ATOM    943  CB  CYS A 117      15.920  93.752 253.910  1.00 51.78           C  
ANISOU  943  CB  CYS A 117     7393   8210   4071   -447    772   1239       C  
ATOM    944  SG  CYS A 117      14.596  93.763 252.717  1.00 55.71           S  
ANISOU  944  SG  CYS A 117     7760   8715   4691   -535    788   1265       S  
ATOM    945  N   ARG A 118      17.804  94.231 256.006  1.00 52.79           N  
ANISOU  945  N   ARG A 118     7684   8376   3997   -306    761   1186       N  
ATOM    946  CA  ARG A 118      18.890  94.149 256.942  1.00 52.83           C  
ANISOU  946  CA  ARG A 118     7790   8385   3897   -242    725   1171       C  
ATOM    947  C   ARG A 118      18.762  92.784 257.622  1.00 53.90           C  
ANISOU  947  C   ARG A 118     8043   8475   3962   -288    722   1265       C  
ATOM    948  O   ARG A 118      17.659  92.299 257.825  1.00 54.38           O  
ANISOU  948  O   ARG A 118     8095   8538   4030   -371    790   1333       O  
ATOM    949  CB  ARG A 118      18.695  95.280 257.940  1.00 52.79           C  
ANISOU  949  CB  ARG A 118     7759   8466   3832   -211    803   1128       C  
ATOM    950  CG  ARG A 118      19.769  95.449 258.947  1.00 54.00           C  
ANISOU  950  CG  ARG A 118     8003   8642   3873   -147    767   1099       C  
ATOM    951  CD  ARG A 118      19.174  96.040 260.192  1.00 57.19           C  
ANISOU  951  CD  ARG A 118     8419   9121   4189   -152    869   1097       C  
ATOM    952  NE  ARG A 118      19.167  97.501 260.212  1.00 57.44           N  
ANISOU  952  NE  ARG A 118     8378   9206   4241   -109    907   1004       N  
ATOM    953  CZ  ARG A 118      18.720  98.224 261.242  1.00 60.15           C  
ANISOU  953  CZ  ARG A 118     8730   9615   4511    -98    997    979       C  
ATOM    954  NH1 ARG A 118      18.236  97.638 262.344  1.00 59.36           N  
ANISOU  954  NH1 ARG A 118     8703   9546   4306   -130   1063   1042       N  
ATOM    955  NH2 ARG A 118      18.758  99.544 261.174  1.00 60.97           N  
ANISOU  955  NH2 ARG A 118     8775   9750   4640    -56   1026    890       N  
ATOM    956  N   VAL A 119      19.892  92.165 257.949  1.00 54.49           N  
ANISOU  956  N   VAL A 119     8224   8508   3971   -234    642   1272       N  
ATOM    957  CA  VAL A 119      19.943  90.896 258.684  1.00 55.93           C  
ANISOU  957  CA  VAL A 119     8538   8639   4075   -261    630   1362       C  
ATOM    958  C   VAL A 119      21.168  91.005 259.598  1.00 56.96           C  
ANISOU  958  C   VAL A 119     8752   8793   4096   -172    575   1341       C  
ATOM    959  O   VAL A 119      22.177  91.576 259.194  1.00 56.86           O  
ANISOU  959  O   VAL A 119     8708   8792   4103    -96    507   1267       O  
ATOM    960  CB  VAL A 119      19.988  89.668 257.707  1.00 55.84           C  
ANISOU  960  CB  VAL A 119     8573   8515   4129   -295    563   1407       C  
ATOM    961  CG1 VAL A 119      20.960  88.591 258.154  1.00 56.75           C  
ANISOU  961  CG1 VAL A 119     8833   8559   4172   -246    485   1453       C  
ATOM    962  CG2 VAL A 119      18.605  89.086 257.506  1.00 55.29           C  
ANISOU  962  CG2 VAL A 119     8482   8421   4103   -416    630   1478       C  
ATOM    963  N   PRO A 120      21.079  90.506 260.845  1.00 58.81           N  
ANISOU  963  N   PRO A 120     9089   9042   4214   -184    604   1407       N  
ATOM    964  CA  PRO A 120      22.179  90.704 261.791  1.00 59.57           C  
ANISOU  964  CA  PRO A 120     9259   9176   4197   -103    551   1386       C  
ATOM    965  C   PRO A 120      23.422  89.945 261.373  1.00 59.88           C  
ANISOU  965  C   PRO A 120     9363   9146   4242    -29    427   1391       C  
ATOM    966  O   PRO A 120      23.318  88.909 260.725  1.00 60.26           O  
ANISOU  966  O   PRO A 120     9452   9100   4342    -52    394   1443       O  
ATOM    967  CB  PRO A 120      21.631  90.118 263.097  1.00 60.80           C  
ANISOU  967  CB  PRO A 120     9520   9351   4232   -148    614   1477       C  
ATOM    968  CG  PRO A 120      20.160  90.161 262.946  1.00 61.06           C  
ANISOU  968  CG  PRO A 120     9489   9397   4314   -249    729   1513       C  
ATOM    969  CD  PRO A 120      19.937  89.838 261.493  1.00 60.27           C  
ANISOU  969  CD  PRO A 120     9319   9223   4358   -278    692   1502       C  
ATOM    970  N   ALA A 121      24.580  90.465 261.763  1.00 60.19           N  
ANISOU  970  N   ALA A 121     9410   9234   4227     57    359   1336       N  
ATOM    971  CA  ALA A 121      25.884  89.973 261.317  1.00 60.34           C  
ANISOU  971  CA  ALA A 121     9458   9209   4259    144    240   1323       C  
ATOM    972  C   ALA A 121      25.972  88.474 260.917  1.00 61.08           C  
ANISOU  972  C   ALA A 121     9648   9186   4375    147    191   1406       C  
ATOM    973  O   ALA A 121      26.352  88.149 259.766  1.00 60.51           O  
ANISOU  973  O   ALA A 121     9544   9051   4396    175    140   1381       O  
ATOM    974  CB  ALA A 121      26.946  90.315 262.368  1.00 61.29           C  
ANISOU  974  CB  ALA A 121     9625   9400   4264    219    179   1303       C  
ATOM    975  N   GLY A 122      25.622  87.579 261.843  1.00 61.58           N  
ANISOU  975  N   GLY A 122     9834   9216   4349    118    209   1504       N  
ATOM    976  CA  GLY A 122      25.960  86.178 261.672  1.00 62.52           C  
ANISOU  976  CA  GLY A 122    10068   9219   4467    142    147   1583       C  
ATOM    977  C   GLY A 122      24.807  85.303 261.247  1.00 63.44           C  
ANISOU  977  C   GLY A 122    10226   9241   4636     36    204   1655       C  
ATOM    978  O   GLY A 122      24.781  84.109 261.554  1.00 64.57           O  
ANISOU  978  O   GLY A 122    10500   9290   4743     25    180   1746       O  
ATOM    979  N   LYS A 123      23.846  85.903 260.549  1.00 62.92           N  
ANISOU  979  N   LYS A 123    10050   9199   4658    -45    276   1615       N  
ATOM    980  CA  LYS A 123      22.639  85.210 260.098  1.00 63.12           C  
ANISOU  980  CA  LYS A 123    10088   9152   4741   -163    334   1676       C  
ATOM    981  C   LYS A 123      22.596  85.160 258.571  1.00 62.80           C  
ANISOU  981  C   LYS A 123     9976   9053   4833   -172    300   1620       C  
ATOM    982  O   LYS A 123      23.542  85.590 257.889  1.00 62.03           O  
ANISOU  982  O   LYS A 123     9827   8965   4776    -82    234   1542       O  
ATOM    983  CB  LYS A 123      21.390  85.904 260.650  1.00 62.97           C  
ANISOU  983  CB  LYS A 123     9997   9223   4706   -260    455   1689       C  
ATOM    984  CG  LYS A 123      21.408  86.155 262.144  1.00 62.47           C  
ANISOU  984  CG  LYS A 123     9993   9237   4504   -249    501   1727       C  
ATOM    985  CD  LYS A 123      21.353  84.845 262.926  1.00 62.46           C  
ANISOU  985  CD  LYS A 123    10156   9159   4418   -279    491   1849       C  
ATOM    986  CE  LYS A 123      20.933  85.085 264.367  1.00 61.58           C  
ANISOU  986  CE  LYS A 123    10094   9133   4172   -309    571   1900       C  
ATOM    987  NZ  LYS A 123      20.160  83.946 264.903  1.00 60.52           N  
ANISOU  987  NZ  LYS A 123    10072   8932   3990   -406    619   2030       N  
ATOM    988  N   THR A 124      21.498  84.643 258.026  1.00 63.45           N  
ANISOU  988  N   THR A 124    10051   9078   4979   -284    343   1661       N  
ATOM    989  CA  THR A 124      21.460  84.329 256.603  1.00 63.42           C  
ANISOU  989  CA  THR A 124    10013   8998   5085   -300    299   1623       C  
ATOM    990  C   THR A 124      20.510  85.265 255.827  1.00 62.35           C  
ANISOU  990  C   THR A 124     9721   8932   5038   -372    358   1571       C  
ATOM    991  O   THR A 124      19.312  85.296 256.115  1.00 63.20           O  
ANISOU  991  O   THR A 124     9792   9069   5154   -480    437   1618       O  
ATOM    992  CB  THR A 124      21.138  82.816 256.375  1.00 64.77           C  
ANISOU  992  CB  THR A 124    10321   9022   5267   -364    272   1705       C  
ATOM    993  OG1 THR A 124      21.968  82.005 257.226  1.00 66.86           O  
ANISOU  993  OG1 THR A 124    10734   9227   5442   -291    224   1763       O  
ATOM    994  CG2 THR A 124      21.368  82.415 254.920  1.00 64.49           C  
ANISOU  994  CG2 THR A 124    10278   8897   5328   -355    209   1653       C  
ATOM    995  N   PRO A 125      21.042  86.028 254.838  1.00 60.72           N  
ANISOU  995  N   PRO A 125     9419   8753   4898   -311    319   1478       N  
ATOM    996  CA  PRO A 125      20.212  87.054 254.208  1.00 59.65           C  
ANISOU  996  CA  PRO A 125     9134   8693   4838   -363    372   1430       C  
ATOM    997  C   PRO A 125      19.055  86.469 253.394  1.00 59.81           C  
ANISOU  997  C   PRO A 125     9132   8659   4934   -484    391   1467       C  
ATOM    998  O   PRO A 125      19.257  85.570 252.598  1.00 59.92           O  
ANISOU  998  O   PRO A 125     9212   8571   4983   -498    331   1473       O  
ATOM    999  CB  PRO A 125      21.202  87.803 253.298  1.00 58.37           C  
ANISOU  999  CB  PRO A 125     8904   8552   4721   -267    313   1333       C  
ATOM   1000  CG  PRO A 125      22.567  87.327 253.671  1.00 58.00           C  
ANISOU 1000  CG  PRO A 125     8954   8469   4613   -160    240   1327       C  
ATOM   1001  CD  PRO A 125      22.379  85.961 254.215  1.00 59.90           C  
ANISOU 1001  CD  PRO A 125     9337   8614   4807   -195    229   1417       C  
ATOM   1002  N   GLY A 126      17.853  86.986 253.608  1.00 60.12           N  
ANISOU 1002  N   GLY A 126     9077   8770   4997   -571    475   1490       N  
ATOM   1003  CA  GLY A 126      16.667  86.540 252.895  1.00 60.42           C  
ANISOU 1003  CA  GLY A 126     9069   8778   5109   -696    494   1528       C  
ATOM   1004  C   GLY A 126      15.436  86.829 253.719  1.00 61.36           C  
ANISOU 1004  C   GLY A 126     9122   8978   5214   -786    600   1586       C  
ATOM   1005  O   GLY A 126      15.505  86.851 254.957  1.00 61.47           O  
ANISOU 1005  O   GLY A 126     9185   9029   5140   -769    653   1624       O  
ATOM   1006  N   GLU A 127      14.318  87.067 253.030  1.00 61.61           N  
ANISOU 1006  N   GLU A 127     9037   9044   5328   -877    632   1592       N  
ATOM   1007  CA  GLU A 127      12.999  87.236 253.663  1.00 62.92           C  
ANISOU 1007  CA  GLU A 127     9120   9289   5497   -975    736   1655       C  
ATOM   1008  C   GLU A 127      12.751  86.165 254.733  1.00 64.27           C  
ANISOU 1008  C   GLU A 127     9415   9416   5589  -1046    774   1754       C  
ATOM   1009  O   GLU A 127      12.738  84.977 254.448  1.00 65.25           O  
ANISOU 1009  O   GLU A 127     9643   9430   5719  -1116    725   1804       O  
ATOM   1010  CB  GLU A 127      11.918  87.190 252.593  1.00 62.96           C  
ANISOU 1010  CB  GLU A 127     9013   9303   5608  -1080    732   1664       C  
ATOM   1011  CG  GLU A 127      10.510  87.473 253.072  1.00 64.75           C  
ANISOU 1011  CG  GLU A 127     9118   9628   5857  -1178    838   1722       C  
ATOM   1012  CD  GLU A 127       9.507  87.343 251.935  1.00 66.29           C  
ANISOU 1012  CD  GLU A 127     9201   9828   6158  -1284    814   1733       C  
ATOM   1013  OE1 GLU A 127       9.704  86.440 251.089  1.00 67.86           O  
ANISOU 1013  OE1 GLU A 127     9475   9922   6387  -1338    726   1736       O  
ATOM   1014  OE2 GLU A 127       8.540  88.139 251.873  1.00 65.64           O  
ANISOU 1014  OE2 GLU A 127     8957   9856   6128  -1310    880   1736       O  
ATOM   1015  N   GLY A 128      12.577  86.589 255.971  1.00 64.88           N  
ANISOU 1015  N   GLY A 128     9490   9574   5587  -1027    862   1781       N  
ATOM   1016  CA  GLY A 128      12.583  85.649 257.082  1.00 66.41           C  
ANISOU 1016  CA  GLY A 128     9821   9727   5684  -1071    892   1872       C  
ATOM   1017  C   GLY A 128      12.418  86.319 258.428  1.00 67.09           C  
ANISOU 1017  C   GLY A 128     9894   9923   5674  -1037    994   1887       C  
ATOM   1018  O   GLY A 128      11.982  87.473 258.520  1.00 66.60           O  
ANISOU 1018  O   GLY A 128     9700   9973   5633  -1006   1063   1837       O  
ATOM   1019  N   GLU A 129      12.767  85.587 259.475  1.00 68.58           N  
ANISOU 1019  N   GLU A 129    10228  10076   5754  -1040   1004   1956       N  
ATOM   1020  CA  GLU A 129      12.516  86.037 260.847  1.00 69.96           C  
ANISOU 1020  CA  GLU A 129    10413  10351   5819  -1027   1108   1986       C  
ATOM   1021  C   GLU A 129      13.573  87.007 261.301  1.00 68.93           C  
ANISOU 1021  C   GLU A 129    10295  10274   5623   -881   1083   1898       C  
ATOM   1022  O   GLU A 129      13.316  87.837 262.174  1.00 69.52           O  
ANISOU 1022  O   GLU A 129    10329  10456   5631   -852   1172   1879       O  
ATOM   1023  CB  GLU A 129      12.457  84.864 261.832  1.00 71.76           C  
ANISOU 1023  CB  GLU A 129    10800  10522   5945  -1093   1129   2103       C  
ATOM   1024  CG  GLU A 129      13.754  84.081 261.992  1.00 72.91           C  
ANISOU 1024  CG  GLU A 129    11122  10555   6027  -1014   1015   2114       C  
ATOM   1025  CD  GLU A 129      13.888  83.470 263.378  1.00 77.80           C  
ANISOU 1025  CD  GLU A 129    11889  11172   6501  -1026   1054   2209       C  
ATOM   1026  OE1 GLU A 129      13.586  84.172 264.379  1.00 79.23           O  
ANISOU 1026  OE1 GLU A 129    12039  11472   6594  -1012   1149   2210       O  
ATOM   1027  OE2 GLU A 129      14.299  82.288 263.468  1.00 79.10           O  
ANISOU 1027  OE2 GLU A 129    12207  11214   6635  -1045    989   2283       O  
ATOM   1028  N   ASP A 130      14.760  86.882 260.709  1.00 67.52           N  
ANISOU 1028  N   ASP A 130    10173  10021   5460   -792    964   1844       N  
ATOM   1029  CA  ASP A 130      15.907  87.705 261.072  1.00 66.37           C  
ANISOU 1029  CA  ASP A 130    10045   9917   5256   -659    920   1762       C  
ATOM   1030  C   ASP A 130      15.871  89.065 260.363  1.00 64.80           C  
ANISOU 1030  C   ASP A 130     9693   9790   5139   -607    930   1653       C  
ATOM   1031  O   ASP A 130      16.486  90.037 260.824  1.00 64.29           O  
ANISOU 1031  O   ASP A 130     9612   9790   5025   -518    933   1582       O  
ATOM   1032  CB  ASP A 130      17.210  86.970 260.725  1.00 66.04           C  
ANISOU 1032  CB  ASP A 130    10119   9771   5201   -584    789   1754       C  
ATOM   1033  CG  ASP A 130      17.412  85.700 261.538  1.00 67.52           C  
ANISOU 1033  CG  ASP A 130    10476   9883   5296   -611    770   1860       C  
ATOM   1034  OD1 ASP A 130      16.992  85.660 262.719  1.00 68.82           O  
ANISOU 1034  OD1 ASP A 130    10688  10102   5357   -644    847   1920       O  
ATOM   1035  OD2 ASP A 130      18.015  84.745 260.997  1.00 67.24           O  
ANISOU 1035  OD2 ASP A 130    10531   9731   5287   -593    678   1883       O  
ATOM   1036  N   GLU A 131      15.144  89.115 259.247  1.00 63.69           N  
ANISOU 1036  N   GLU A 131     9446   9634   5120   -666    933   1643       N  
ATOM   1037  CA  GLU A 131      15.185  90.244 258.331  1.00 61.91           C  
ANISOU 1037  CA  GLU A 131     9087   9449   4986   -617    921   1549       C  
ATOM   1038  C   GLU A 131      14.298  91.374 258.807  1.00 61.96           C  
ANISOU 1038  C   GLU A 131     8977   9571   4995   -620   1036   1524       C  
ATOM   1039  O   GLU A 131      13.086  91.193 258.982  1.00 62.95           O  
ANISOU 1039  O   GLU A 131     9041   9735   5142   -708   1123   1583       O  
ATOM   1040  CB  GLU A 131      14.788  89.820 256.901  1.00 61.34           C  
ANISOU 1040  CB  GLU A 131     8954   9314   5037   -675    868   1550       C  
ATOM   1041  CG  GLU A 131      14.409  90.981 255.965  1.00 59.66           C  
ANISOU 1041  CG  GLU A 131     8584   9158   4925   -654    879   1476       C  
ATOM   1042  CD  GLU A 131      13.969  90.527 254.583  1.00 60.11           C  
ANISOU 1042  CD  GLU A 131     8588   9160   5092   -718    825   1483       C  
ATOM   1043  OE1 GLU A 131      14.847  90.119 253.797  1.00 60.27           O  
ANISOU 1043  OE1 GLU A 131     8665   9102   5133   -682    727   1451       O  
ATOM   1044  OE2 GLU A 131      12.753  90.582 254.268  1.00 60.00           O  
ANISOU 1044  OE2 GLU A 131     8471   9184   5140   -805    878   1518       O  
ATOM   1045  N   GLU A 132      14.922  92.531 259.012  1.00 60.76           N  
ANISOU 1045  N   GLU A 132     8794   9471   4821   -523   1035   1436       N  
ATOM   1046  CA  GLU A 132      14.210  93.765 259.235  1.00 60.53           C  
ANISOU 1046  CA  GLU A 132     8649   9536   4813   -503   1131   1390       C  
ATOM   1047  C   GLU A 132      14.163  94.546 257.935  1.00 58.58           C  
ANISOU 1047  C   GLU A 132     8282   9283   4691   -476   1091   1324       C  
ATOM   1048  O   GLU A 132      15.198  94.817 257.337  1.00 57.99           O  
ANISOU 1048  O   GLU A 132     8227   9169   4638   -413   1001   1263       O  
ATOM   1049  CB  GLU A 132      14.897  94.581 260.314  1.00 61.01           C  
ANISOU 1049  CB  GLU A 132     8764   9650   4766   -418   1155   1331       C  
ATOM   1050  CG  GLU A 132      13.901  95.344 261.175  1.00 65.10           C  
ANISOU 1050  CG  GLU A 132     9223  10265   5246   -425   1295   1329       C  
ATOM   1051  CD  GLU A 132      14.533  96.492 261.927  1.00 67.50           C  
ANISOU 1051  CD  GLU A 132     9554  10621   5474   -333   1315   1238       C  
ATOM   1052  OE1 GLU A 132      15.495  96.236 262.697  1.00 67.36           O  
ANISOU 1052  OE1 GLU A 132     9657  10592   5344   -298   1266   1231       O  
ATOM   1053  OE2 GLU A 132      14.056  97.644 261.732  1.00 68.50           O  
ANISOU 1053  OE2 GLU A 132     9579  10794   5653   -296   1375   1175       O  
ATOM   1054  N   ILE A 133      12.958  94.867 257.477  1.00 57.78           N  
ANISOU 1054  N   ILE A 133     8054   9225   4674   -527   1158   1342       N  
ATOM   1055  CA  ILE A 133      12.767  95.688 256.291  1.00 55.64           C  
ANISOU 1055  CA  ILE A 133     7662   8959   4519   -502   1130   1288       C  
ATOM   1056  C   ILE A 133      12.973  97.142 256.695  1.00 54.74           C  
ANISOU 1056  C   ILE A 133     7503   8905   4391   -408   1179   1204       C  
ATOM   1057  O   ILE A 133      12.071  97.762 257.272  1.00 55.33           O  
ANISOU 1057  O   ILE A 133     7509   9053   4461   -405   1287   1207       O  
ATOM   1058  CB  ILE A 133      11.334  95.570 255.742  1.00 56.27           C  
ANISOU 1058  CB  ILE A 133     7614   9076   4691   -585   1186   1342       C  
ATOM   1059  CG1 ILE A 133      11.016  94.138 255.322  1.00 58.11           C  
ANISOU 1059  CG1 ILE A 133     7889   9246   4942   -695   1139   1424       C  
ATOM   1060  CG2 ILE A 133      11.121  96.508 254.569  1.00 55.32           C  
ANISOU 1060  CG2 ILE A 133     7368   8968   4682   -549   1157   1288       C  
ATOM   1061  CD1 ILE A 133       9.545  93.920 254.848  1.00 61.40           C  
ANISOU 1061  CD1 ILE A 133     8176   9708   5446   -798   1191   1486       C  
ATOM   1062  N   VAL A 134      14.151  97.682 256.383  1.00 52.78           N  
ANISOU 1062  N   VAL A 134     7294   8624   4137   -333   1101   1129       N  
ATOM   1063  CA  VAL A 134      14.502  99.056 256.749  1.00 51.57           C  
ANISOU 1063  CA  VAL A 134     7118   8510   3967   -248   1133   1043       C  
ATOM   1064  C   VAL A 134      13.615 100.086 256.036  1.00 50.81           C  
ANISOU 1064  C   VAL A 134     6881   8447   3977   -232   1182   1016       C  
ATOM   1065  O   VAL A 134      13.015 100.916 256.690  1.00 51.83           O  
ANISOU 1065  O   VAL A 134     6968   8633   4090   -200   1279    993       O  
ATOM   1066  CB  VAL A 134      16.019  99.360 256.551  1.00 50.58           C  
ANISOU 1066  CB  VAL A 134     7063   8343   3814   -183   1031    973       C  
ATOM   1067  CG1 VAL A 134      16.346 100.777 256.987  1.00 50.35           C  
ANISOU 1067  CG1 VAL A 134     7017   8349   3764   -110   1065    885       C  
ATOM   1068  CG2 VAL A 134      16.859  98.389 257.334  1.00 50.67           C  
ANISOU 1068  CG2 VAL A 134     7205   8329   3717   -186    984   1003       C  
ATOM   1069  N   LEU A 135      13.522 100.047 254.716  1.00 49.36           N  
ANISOU 1069  N   LEU A 135     6628   8230   3898   -250   1118   1020       N  
ATOM   1070  CA  LEU A 135      12.611 100.949 254.027  1.00 48.98           C  
ANISOU 1070  CA  LEU A 135     6445   8215   3950   -236   1160   1008       C  
ATOM   1071  C   LEU A 135      11.808 100.182 252.988  1.00 49.56           C  
ANISOU 1071  C   LEU A 135     6442   8277   4110   -316   1127   1075       C  
ATOM   1072  O   LEU A 135      12.363  99.348 252.271  1.00 49.61           O  
ANISOU 1072  O   LEU A 135     6498   8224   4128   -353   1034   1090       O  
ATOM   1073  CB  LEU A 135      13.376 102.100 253.367  1.00 47.12           C  
ANISOU 1073  CB  LEU A 135     6192   7953   3758   -159   1109    926       C  
ATOM   1074  CG  LEU A 135      12.551 103.284 252.839  1.00 45.96           C  
ANISOU 1074  CG  LEU A 135     5922   7837   3702   -119   1159    903       C  
ATOM   1075  CD1 LEU A 135      12.140 104.143 253.994  1.00 46.60           C  
ANISOU 1075  CD1 LEU A 135     6001   7969   3736    -64   1271    869       C  
ATOM   1076  CD2 LEU A 135      13.305 104.146 251.837  1.00 42.08           C  
ANISOU 1076  CD2 LEU A 135     5417   7302   3270    -69   1084    844       C  
ATOM   1077  N   ASP A 136      10.510 100.453 252.897  1.00 50.36           N  
ANISOU 1077  N   ASP A 136     6423   8439   4272   -341   1201   1112       N  
ATOM   1078  CA  ASP A 136       9.716  99.908 251.783  1.00 50.75           C  
ANISOU 1078  CA  ASP A 136     6382   8486   4415   -417   1160   1167       C  
ATOM   1079  C   ASP A 136       9.265 100.992 250.783  1.00 49.84           C  
ANISOU 1079  C   ASP A 136     6140   8393   4404   -370   1148   1139       C  
ATOM   1080  O   ASP A 136       8.226 101.614 250.964  1.00 50.23           O  
ANISOU 1080  O   ASP A 136     6076   8510   4498   -353   1230   1155       O  
ATOM   1081  CB  ASP A 136       8.516  99.108 252.321  1.00 52.35           C  
ANISOU 1081  CB  ASP A 136     6535   8742   4614   -509   1236   1253       C  
ATOM   1082  CG  ASP A 136       7.787  98.297 251.232  1.00 53.75           C  
ANISOU 1082  CG  ASP A 136     6640   8908   4874   -612   1176   1315       C  
ATOM   1083  OD1 ASP A 136       8.135  98.397 250.029  1.00 51.43           O  
ANISOU 1083  OD1 ASP A 136     6330   8571   4640   -606   1080   1290       O  
ATOM   1084  OD2 ASP A 136       6.842  97.554 251.608  1.00 57.08           O  
ANISOU 1084  OD2 ASP A 136     7022   9368   5297   -704   1228   1389       O  
ATOM   1085  N   GLU A 137      10.031 101.188 249.716  1.00 48.70           N  
ANISOU 1085  N   GLU A 137     6015   8193   4296   -347   1049   1102       N  
ATOM   1086  CA  GLU A 137       9.732 102.240 248.731  1.00 48.64           C  
ANISOU 1086  CA  GLU A 137     5905   8196   4379   -298   1028   1078       C  
ATOM   1087  C   GLU A 137       8.300 102.286 248.161  1.00 49.41           C  
ANISOU 1087  C   GLU A 137     5852   8355   4566   -340   1054   1137       C  
ATOM   1088  O   GLU A 137       7.776 103.360 247.860  1.00 48.70           O  
ANISOU 1088  O   GLU A 137     5663   8301   4540   -277   1085   1124       O  
ATOM   1089  CB  GLU A 137      10.755 102.221 247.613  1.00 47.54           C  
ANISOU 1089  CB  GLU A 137     5817   7991   4257   -287    915   1042       C  
ATOM   1090  CG  GLU A 137      12.168 102.517 248.098  1.00 48.14           C  
ANISOU 1090  CG  GLU A 137     6009   8021   4261   -227    892    975       C  
ATOM   1091  CD  GLU A 137      13.103 102.790 246.960  1.00 48.90           C  
ANISOU 1091  CD  GLU A 137     6128   8067   4386   -203    797    936       C  
ATOM   1092  OE1 GLU A 137      12.611 102.832 245.805  1.00 48.70           O  
ANISOU 1092  OE1 GLU A 137     6031   8042   4432   -227    754    959       O  
ATOM   1093  OE2 GLU A 137      14.320 102.955 247.220  1.00 49.72           O  
ANISOU 1093  OE2 GLU A 137     6318   8137   4437   -162    766    884       O  
ATOM   1094  N   ASN A 138       7.676 101.118 248.049  1.00 50.60           N  
ANISOU 1094  N   ASN A 138     5986   8518   4722   -446   1041   1205       N  
ATOM   1095  CA  ASN A 138       6.248 100.990 247.711  1.00 52.17           C  
ANISOU 1095  CA  ASN A 138     6037   8790   4997   -506   1072   1272       C  
ATOM   1096  C   ASN A 138       5.264 101.707 248.654  1.00 53.87           C  
ANISOU 1096  C   ASN A 138     6149   9096   5224   -461   1205   1287       C  
ATOM   1097  O   ASN A 138       4.246 102.254 248.187  1.00 54.80           O  
ANISOU 1097  O   ASN A 138     6116   9279   5427   -448   1229   1315       O  
ATOM   1098  CB  ASN A 138       5.880  99.511 247.622  1.00 52.34           C  
ANISOU 1098  CB  ASN A 138     6085   8797   5005   -642   1038   1338       C  
ATOM   1099  CG  ASN A 138       6.841  98.747 246.778  1.00 51.00           C  
ANISOU 1099  CG  ASN A 138     6029   8534   4816   -679    917   1319       C  
ATOM   1100  OD1 ASN A 138       6.835  98.852 245.552  1.00 51.97           O  
ANISOU 1100  OD1 ASN A 138     6112   8638   4995   -689    832   1312       O  
ATOM   1101  ND2 ASN A 138       7.709  98.002 247.421  1.00 50.94           N  
ANISOU 1101  ND2 ASN A 138     6165   8466   4725   -690    908   1309       N  
ATOM   1102  N   LYS A 139       5.566 101.678 249.960  1.00 54.43           N  
ANISOU 1102  N   LYS A 139     6299   9174   5207   -435   1290   1270       N  
ATOM   1103  CA  LYS A 139       4.801 102.391 250.995  1.00 55.92           C  
ANISOU 1103  CA  LYS A 139     6417   9444   5385   -378   1429   1269       C  
ATOM   1104  C   LYS A 139       5.084 103.878 250.946  1.00 55.21           C  
ANISOU 1104  C   LYS A 139     6307   9349   5320   -243   1454   1194       C  
ATOM   1105  O   LYS A 139       4.222 104.696 251.203  1.00 56.24           O  
ANISOU 1105  O   LYS A 139     6328   9545   5495   -182   1543   1195       O  
ATOM   1106  CB  LYS A 139       5.100 101.852 252.411  1.00 56.98           C  
ANISOU 1106  CB  LYS A 139     6663   9585   5401   -397   1507   1273       C  
ATOM   1107  CG  LYS A 139       4.690 100.372 252.664  1.00 59.03           C  
ANISOU 1107  CG  LYS A 139     6947   9852   5629   -535   1505   1359       C  
ATOM   1108  CD  LYS A 139       4.154 100.126 254.076  1.00 63.91           C  
ANISOU 1108  CD  LYS A 139     7578  10537   6167   -554   1640   1394       C  
ATOM   1109  CE  LYS A 139       5.191 100.359 255.192  1.00 65.42           C  
ANISOU 1109  CE  LYS A 139     7926  10696   6233   -485   1671   1336       C  
ATOM   1110  NZ  LYS A 139       4.527 100.370 256.539  1.00 66.53           N  
ANISOU 1110  NZ  LYS A 139     8060  10920   6297   -487   1819   1364       N  
ATOM   1111  N   LEU A 140       6.315 104.220 250.625  1.00 54.52           N  
ANISOU 1111  N   LEU A 140     6328   9181   5206   -198   1376   1129       N  
ATOM   1112  CA  LEU A 140       6.677 105.593 250.260  1.00 54.43           C  
ANISOU 1112  CA  LEU A 140     6302   9143   5234    -87   1370   1062       C  
ATOM   1113  C   LEU A 140       5.929 106.127 249.016  1.00 54.68           C  
ANISOU 1113  C   LEU A 140     6196   9194   5387    -70   1328   1090       C  
ATOM   1114  O   LEU A 140       5.502 107.277 248.998  1.00 55.08           O  
ANISOU 1114  O   LEU A 140     6176   9263   5487     23   1379   1066       O  
ATOM   1115  CB  LEU A 140       8.201 105.695 250.026  1.00 52.85           C  
ANISOU 1115  CB  LEU A 140     6241   8854   4985    -65   1280    997       C  
ATOM   1116  CG  LEU A 140       9.127 106.313 251.069  1.00 51.80           C  
ANISOU 1116  CG  LEU A 140     6223   8694   4764      3   1319    920       C  
ATOM   1117  CD1 LEU A 140      10.098 107.236 250.339  1.00 49.54           C  
ANISOU 1117  CD1 LEU A 140     5976   8342   4507     62   1245    854       C  
ATOM   1118  CD2 LEU A 140       8.371 107.093 252.124  1.00 51.80           C  
ANISOU 1118  CD2 LEU A 140     6184   8750   4745     68   1453    900       C  
ATOM   1119  N   ALA A 141       5.801 105.290 247.986  1.00 54.76           N  
ANISOU 1119  N   ALA A 141     6176   9194   5437   -157   1233   1140       N  
ATOM   1120  CA  ALA A 141       5.268 105.708 246.695  1.00 55.25           C  
ANISOU 1120  CA  ALA A 141     6127   9267   5599   -150   1168   1166       C  
ATOM   1121  C   ALA A 141       3.731 105.652 246.588  1.00 57.12           C  
ANISOU 1121  C   ALA A 141     6190   9602   5912   -176   1219   1238       C  
ATOM   1122  O   ALA A 141       3.149 106.118 245.599  1.00 57.34           O  
ANISOU 1122  O   ALA A 141     6107   9653   6026   -158   1172   1265       O  
ATOM   1123  CB  ALA A 141       5.915 104.903 245.598  1.00 54.30           C  
ANISOU 1123  CB  ALA A 141     6065   9088   5478   -226   1037   1176       C  
ATOM   1124  N   GLU A 142       3.094 105.076 247.608  1.00 58.71           N  
ANISOU 1124  N   GLU A 142     6365   9864   6079   -222   1313   1273       N  
ATOM   1125  CA  GLU A 142       1.636 105.050 247.778  1.00 60.76           C  
ANISOU 1125  CA  GLU A 142     6453  10232   6401   -243   1389   1340       C  
ATOM   1126  C   GLU A 142       0.807 106.214 247.149  1.00 60.96           C  
ANISOU 1126  C   GLU A 142     6321  10309   6532   -146   1402   1349       C  
ATOM   1127  O   GLU A 142       0.735 107.332 247.696  1.00 61.05           O  
ANISOU 1127  O   GLU A 142     6318  10330   6550    -20   1488   1305       O  
ATOM   1128  CB  GLU A 142       1.335 104.916 249.273  1.00 62.14           C  
ANISOU 1128  CB  GLU A 142     6647  10459   6506   -235   1530   1341       C  
ATOM   1129  CG  GLU A 142      -0.146 105.011 249.636  1.00 67.34           C  
ANISOU 1129  CG  GLU A 142     7122  11241   7221   -240   1637   1404       C  
ATOM   1130  CD  GLU A 142      -1.017 103.992 248.892  1.00 71.04           C  
ANISOU 1130  CD  GLU A 142     7476  11764   7752   -380   1576   1495       C  
ATOM   1131  OE1 GLU A 142      -0.448 103.132 248.172  1.00 71.00           O  
ANISOU 1131  OE1 GLU A 142     7553  11691   7734   -476   1455   1506       O  
ATOM   1132  OE2 GLU A 142      -2.266 104.048 249.047  1.00 73.43           O  
ANISOU 1132  OE2 GLU A 142     7606  12178   8115   -393   1650   1554       O  
ATOM   1133  N   GLY A 143       0.185 105.928 246.001  1.00 60.73           N  
ANISOU 1133  N   GLY A 143     6182  10311   6582   -204   1313   1406       N  
ATOM   1134  CA  GLY A 143      -0.696 106.873 245.318  1.00 60.94           C  
ANISOU 1134  CA  GLY A 143     6047  10396   6713   -125   1310   1432       C  
ATOM   1135  C   GLY A 143      -0.009 108.165 244.918  1.00 60.13           C  
ANISOU 1135  C   GLY A 143     5998  10220   6628     12   1286   1368       C  
ATOM   1136  O   GLY A 143      -0.579 109.258 245.082  1.00 60.92           O  
ANISOU 1136  O   GLY A 143     6009  10354   6784    132   1355   1362       O  
ATOM   1137  N   LYS A 144       1.218 108.026 244.402  1.00 58.10           N  
ANISOU 1137  N   LYS A 144     5890   9862   6325     -8   1192   1323       N  
ATOM   1138  CA  LYS A 144       2.039 109.138 243.908  1.00 56.69           C  
ANISOU 1138  CA  LYS A 144     5782   9602   6157     95   1153   1265       C  
ATOM   1139  C   LYS A 144       2.524 108.904 242.479  1.00 55.59           C  
ANISOU 1139  C   LYS A 144     5668   9415   6037     46   1007   1279       C  
ATOM   1140  O   LYS A 144       2.973 107.810 242.137  1.00 55.13           O  
ANISOU 1140  O   LYS A 144     5678   9335   5936    -63    935   1289       O  
ATOM   1141  CB  LYS A 144       3.237 109.363 244.817  1.00 55.43           C  
ANISOU 1141  CB  LYS A 144     5790   9365   5906    133   1195   1183       C  
ATOM   1142  CG  LYS A 144       3.076 110.571 245.673  1.00 56.72           C  
ANISOU 1142  CG  LYS A 144     5947   9528   6075    263   1307   1135       C  
ATOM   1143  CD  LYS A 144       3.689 110.397 247.042  1.00 57.11           C  
ANISOU 1143  CD  LYS A 144     6117   9559   6023    267   1392   1077       C  
ATOM   1144  CE  LYS A 144       2.890 111.219 248.028  1.00 59.13           C  
ANISOU 1144  CE  LYS A 144     6309   9866   6290    368   1533   1060       C  
ATOM   1145  NZ  LYS A 144       3.748 111.772 249.083  1.00 59.87           N  
ANISOU 1145  NZ  LYS A 144     6545   9905   6298    428   1596    971       N  
ATOM   1146  N   SER A 145       2.439 109.928 241.639  1.00 55.09           N  
ANISOU 1146  N   SER A 145     5560   9334   6036    128    965   1281       N  
ATOM   1147  CA  SER A 145       2.914 109.794 240.270  1.00 53.63           C  
ANISOU 1147  CA  SER A 145     5406   9108   5864     88    833   1294       C  
ATOM   1148  C   SER A 145       4.408 109.499 240.254  1.00 51.71           C  
ANISOU 1148  C   SER A 145     5341   8770   5538     60    789   1230       C  
ATOM   1149  O   SER A 145       4.860 108.621 239.517  1.00 51.55           O  
ANISOU 1149  O   SER A 145     5372   8727   5487    -30    697   1239       O  
ATOM   1150  CB  SER A 145       2.596 111.037 239.445  1.00 53.90           C  
ANISOU 1150  CB  SER A 145     5371   9135   5973    190    803   1310       C  
ATOM   1151  OG  SER A 145       2.761 112.215 240.210  1.00 55.37           O  
ANISOU 1151  OG  SER A 145     5583   9286   6170    317    896   1262       O  
ATOM   1152  N   PHE A 146       5.178 110.188 241.091  1.00 50.10           N  
ANISOU 1152  N   PHE A 146     5230   8512   5295    134    855   1163       N  
ATOM   1153  CA  PHE A 146       6.626 110.012 241.041  1.00 47.48           C  
ANISOU 1153  CA  PHE A 146     5052   8097   4891    115    810   1103       C  
ATOM   1154  C   PHE A 146       7.281 109.778 242.428  1.00 46.46           C  
ANISOU 1154  C   PHE A 146     5024   7947   4682    119    888   1047       C  
ATOM   1155  O   PHE A 146       6.897 110.409 243.423  1.00 46.67           O  
ANISOU 1155  O   PHE A 146     5031   7994   4709    187    988   1026       O  
ATOM   1156  CB  PHE A 146       7.269 111.199 240.292  1.00 46.92           C  
ANISOU 1156  CB  PHE A 146     5017   7962   4848    191    770   1074       C  
ATOM   1157  CG  PHE A 146       8.767 111.122 240.234  1.00 45.90           C  
ANISOU 1157  CG  PHE A 146     5031   7758   4651    174    728   1013       C  
ATOM   1158  CD1 PHE A 146       9.545 111.478 241.355  1.00 43.23           C  
ANISOU 1158  CD1 PHE A 146     4785   7381   4258    212    793    945       C  
ATOM   1159  CD2 PHE A 146       9.412 110.655 239.072  1.00 43.82           C  
ANISOU 1159  CD2 PHE A 146     4809   7467   4373    118    625   1023       C  
ATOM   1160  CE1 PHE A 146      10.933 111.366 241.326  1.00 41.92           C  
ANISOU 1160  CE1 PHE A 146     4738   7158   4032    193    751    893       C  
ATOM   1161  CE2 PHE A 146      10.797 110.543 239.038  1.00 41.16           C  
ANISOU 1161  CE2 PHE A 146     4591   7071   3975    105    593    969       C  
ATOM   1162  CZ  PHE A 146      11.566 110.907 240.172  1.00 40.61           C  
ANISOU 1162  CZ  PHE A 146     4602   6970   3859    142    654    905       C  
ATOM   1163  N   CYS A 147       8.279 108.889 242.481  1.00 44.62           N  
ANISOU 1163  N   CYS A 147     4901   7675   4376     54    840   1023       N  
ATOM   1164  CA  CYS A 147       8.987 108.597 243.740  1.00 43.77           C  
ANISOU 1164  CA  CYS A 147     4897   7549   4186     55    896    975       C  
ATOM   1165  C   CYS A 147      10.414 108.048 243.599  1.00 41.98           C  
ANISOU 1165  C   CYS A 147     4801   7260   3889     20    828    933       C  
ATOM   1166  O   CYS A 147      10.590 106.874 243.250  1.00 41.52           O  
ANISOU 1166  O   CYS A 147     4773   7198   3804    -58    771    959       O  
ATOM   1167  CB  CYS A 147       8.162 107.632 244.610  1.00 44.89           C  
ANISOU 1167  CB  CYS A 147     5003   7751   4301     -4    959   1017       C  
ATOM   1168  SG  CYS A 147       8.939 107.209 246.226  1.00 45.14           S  
ANISOU 1168  SG  CYS A 147     5164   7769   4218     -5   1029    969       S  
ATOM   1169  N   VAL A 148      11.416 108.881 243.905  1.00 40.80           N  
ANISOU 1169  N   VAL A 148     4729   7063   3710     80    834    867       N  
ATOM   1170  CA  VAL A 148      12.825 108.432 243.985  1.00 39.68           C  
ANISOU 1170  CA  VAL A 148     4704   6874   3498     58    781    823       C  
ATOM   1171  C   VAL A 148      13.502 108.686 245.343  1.00 39.94           C  
ANISOU 1171  C   VAL A 148     4821   6897   3457     91    838    764       C  
ATOM   1172  O   VAL A 148      13.423 109.795 245.909  1.00 40.36           O  
ANISOU 1172  O   VAL A 148     4874   6944   3518    156    897    724       O  
ATOM   1173  CB  VAL A 148      13.713 108.973 242.802  1.00 38.70           C  
ANISOU 1173  CB  VAL A 148     4603   6702   3399     71    701    800       C  
ATOM   1174  CG1 VAL A 148      15.235 108.803 243.080  1.00 37.07           C  
ANISOU 1174  CG1 VAL A 148     4506   6456   3123     69    665    743       C  
ATOM   1175  CG2 VAL A 148      13.369 108.249 241.499  1.00 38.69           C  
ANISOU 1175  CG2 VAL A 148     4558   6709   3432     14    624    852       C  
ATOM   1176  N   VAL A 149      14.163 107.654 245.863  1.00 39.57           N  
ANISOU 1176  N   VAL A 149     4853   6846   3336     48    816    760       N  
ATOM   1177  CA  VAL A 149      14.948 107.803 247.082  1.00 40.21           C  
ANISOU 1177  CA  VAL A 149     5023   6920   3335     74    849    707       C  
ATOM   1178  C   VAL A 149      16.424 108.060 246.735  1.00 40.36           C  
ANISOU 1178  C   VAL A 149     5116   6894   3327     86    778    653       C  
ATOM   1179  O   VAL A 149      17.053 107.272 246.047  1.00 39.67           O  
ANISOU 1179  O   VAL A 149     5053   6789   3230     51    704    667       O  
ATOM   1180  CB  VAL A 149      14.820 106.573 248.008  1.00 39.98           C  
ANISOU 1180  CB  VAL A 149     5041   6916   3232     28    872    738       C  
ATOM   1181  CG1 VAL A 149      15.632 106.751 249.279  1.00 39.30           C  
ANISOU 1181  CG1 VAL A 149     5050   6829   3053     57    900    685       C  
ATOM   1182  CG2 VAL A 149      13.387 106.346 248.363  1.00 41.67           C  
ANISOU 1182  CG2 VAL A 149     5177   7182   3474      8    949    793       C  
ATOM   1183  N   GLY A 150      16.980 109.157 247.232  1.00 41.41           N  
ANISOU 1183  N   GLY A 150     5281   7008   3444    135    801    591       N  
ATOM   1184  CA  GLY A 150      18.374 109.448 246.997  1.00 41.97           C  
ANISOU 1184  CA  GLY A 150     5412   7046   3489    139    738    540       C  
ATOM   1185  C   GLY A 150      19.327 108.596 247.798  1.00 42.83           C  
ANISOU 1185  C   GLY A 150     5602   7163   3506    121    709    522       C  
ATOM   1186  O   GLY A 150      20.348 108.176 247.281  1.00 42.17           O  
ANISOU 1186  O   GLY A 150     5548   7066   3410    106    637    513       O  
ATOM   1187  N   CYS A 151      18.998 108.363 249.068  1.00 44.83           N  
ANISOU 1187  N   CYS A 151     5894   7444   3696    127    766    518       N  
ATOM   1188  CA  CYS A 151      19.945 107.807 250.040  1.00 46.68           C  
ANISOU 1188  CA  CYS A 151     6216   7689   3833    122    743    493       C  
ATOM   1189  C   CYS A 151      19.211 107.096 251.147  1.00 47.59           C  
ANISOU 1189  C   CYS A 151     6358   7840   3885    110    805    527       C  
ATOM   1190  O   CYS A 151      18.137 107.535 251.547  1.00 48.97           O  
ANISOU 1190  O   CYS A 151     6494   8036   4077    123    888    536       O  
ATOM   1191  CB  CYS A 151      20.784 108.918 250.685  1.00 47.22           C  
ANISOU 1191  CB  CYS A 151     6330   7748   3863    155    744    412       C  
ATOM   1192  SG  CYS A 151      22.499 108.433 251.168  1.00 51.24           S  
ANISOU 1192  SG  CYS A 151     6921   8263   4284    147    657    374       S  
ATOM   1193  N   VAL A 152      19.784 105.997 251.635  1.00 47.57           N  
ANISOU 1193  N   VAL A 152     6422   7844   3809     88    767    549       N  
ATOM   1194  CA  VAL A 152      19.276 105.324 252.822  1.00 48.08           C  
ANISOU 1194  CA  VAL A 152     6533   7941   3795     74    823    581       C  
ATOM   1195  C   VAL A 152      20.443 105.132 253.825  1.00 48.23           C  
ANISOU 1195  C   VAL A 152     6651   7968   3705     90    784    544       C  
ATOM   1196  O   VAL A 152      21.290 104.226 253.715  1.00 47.78           O  
ANISOU 1196  O   VAL A 152     6642   7898   3615     81    710    564       O  
ATOM   1197  CB  VAL A 152      18.523 104.023 252.480  1.00 48.02           C  
ANISOU 1197  CB  VAL A 152     6508   7932   3804     21    823    666       C  
ATOM   1198  CG1 VAL A 152      18.039 103.353 253.749  1.00 50.36           C  
ANISOU 1198  CG1 VAL A 152     6858   8261   4013      1    885    704       C  
ATOM   1199  CG2 VAL A 152      17.334 104.323 251.634  1.00 47.75           C  
ANISOU 1199  CG2 VAL A 152     6369   7904   3869      4    861    698       C  
ATOM   1200  N   ALA A 153      20.478 106.035 254.789  1.00 48.23           N  
ANISOU 1200  N   ALA A 153     6683   7990   3652    119    834    488       N  
ATOM   1201  CA  ALA A 153      21.638 106.203 255.626  1.00 48.07           C  
ANISOU 1201  CA  ALA A 153     6745   7981   3539    137    788    436       C  
ATOM   1202  C   ALA A 153      21.330 105.853 257.092  1.00 48.80           C  
ANISOU 1202  C   ALA A 153     6913   8115   3512    137    846    447       C  
ATOM   1203  O   ALA A 153      20.684 106.622 257.807  1.00 49.53           O  
ANISOU 1203  O   ALA A 153     7012   8230   3577    154    932    413       O  
ATOM   1204  CB  ALA A 153      22.156 107.638 255.485  1.00 47.77           C  
ANISOU 1204  CB  ALA A 153     6695   7927   3528    164    781    349       C  
ATOM   1205  N   PRO A 154      21.762 104.670 257.537  1.00 48.59           N  
ANISOU 1205  N   PRO A 154     6950   8099   3414    120    802    497       N  
ATOM   1206  CA  PRO A 154      21.639 104.332 258.959  1.00 49.48           C  
ANISOU 1206  CA  PRO A 154     7149   8252   3398    120    844    509       C  
ATOM   1207  C   PRO A 154      22.735 105.042 259.761  1.00 49.55           C  
ANISOU 1207  C   PRO A 154     7226   8281   3319    148    799    428       C  
ATOM   1208  O   PRO A 154      23.753 105.404 259.180  1.00 49.27           O  
ANISOU 1208  O   PRO A 154     7174   8228   3320    160    714    385       O  
ATOM   1209  CB  PRO A 154      21.869 102.816 258.976  1.00 49.78           C  
ANISOU 1209  CB  PRO A 154     7234   8279   3402     94    793    593       C  
ATOM   1210  CG  PRO A 154      21.870 102.363 257.521  1.00 48.32           C  
ANISOU 1210  CG  PRO A 154     6979   8046   3335     78    741    625       C  
ATOM   1211  CD  PRO A 154      22.289 103.552 256.736  1.00 47.98           C  
ANISOU 1211  CD  PRO A 154     6871   7990   3369    103    717    550       C  
ATOM   1212  N   ALA A 155      22.556 105.236 261.064  1.00 50.02           N  
ANISOU 1212  N   ALA A 155     7361   8383   3262    155    852    409       N  
ATOM   1213  CA  ALA A 155      23.578 105.959 261.850  1.00 50.53           C  
ANISOU 1213  CA  ALA A 155     7493   8470   3237    175    803    326       C  
ATOM   1214  C   ALA A 155      24.584 105.059 262.574  1.00 50.87           C  
ANISOU 1214  C   ALA A 155     7621   8541   3166    175    713    354       C  
ATOM   1215  O   ALA A 155      24.190 104.351 263.510  1.00 52.43           O  
ANISOU 1215  O   ALA A 155     7889   8770   3263    168    752    406       O  
ATOM   1216  CB  ALA A 155      22.939 106.950 262.838  1.00 51.08           C  
ANISOU 1216  CB  ALA A 155     7602   8566   3238    190    904    262       C  
ATOM   1217  N   PRO A 156      25.877 105.099 262.150  1.00 50.19           N  
ANISOU 1217  N   PRO A 156     7526   8447   3097    185    596    324       N  
ATOM   1218  CA  PRO A 156      27.015 104.418 262.734  1.00 50.49           C  
ANISOU 1218  CA  PRO A 156     7628   8515   3040    197    493    340       C  
ATOM   1219  C   PRO A 156      26.968 104.086 264.230  1.00 51.61           C  
ANISOU 1219  C   PRO A 156     7882   8709   3019    199    510    354       C  
ATOM   1220  O   PRO A 156      26.236 104.711 265.012  1.00 52.86           O  
ANISOU 1220  O   PRO A 156     8079   8889   3115    193    602    319       O  
ATOM   1221  CB  PRO A 156      28.165 105.344 262.374  1.00 50.81           C  
ANISOU 1221  CB  PRO A 156     7634   8560   3112    203    409    254       C  
ATOM   1222  CG  PRO A 156      27.842 105.725 260.959  1.00 48.88           C  
ANISOU 1222  CG  PRO A 156     7287   8264   3021    196    428    249       C  
ATOM   1223  CD  PRO A 156      26.305 105.763 260.897  1.00 49.40           C  
ANISOU 1223  CD  PRO A 156     7337   8310   3125    186    553    282       C  
ATOM   1224  N   PRO A 157      27.845 103.163 264.640  1.00 51.53           N  
ANISOU 1224  N   PRO A 157     7927   8720   2934    214    416    400       N  
ATOM   1225  CA  PRO A 157      27.565 101.993 265.419  1.00 51.48           C  
ANISOU 1225  CA  PRO A 157     8005   8727   2828    215    425    492       C  
ATOM   1226  C   PRO A 157      26.165 101.400 265.238  1.00 50.58           C  
ANISOU 1226  C   PRO A 157     7882   8583   2752    186    540    568       C  
ATOM   1227  O   PRO A 157      26.023 100.376 264.602  1.00 49.25           O  
ANISOU 1227  O   PRO A 157     7699   8372   2643    180    520    646       O  
ATOM   1228  CB  PRO A 157      27.824 102.487 266.854  1.00 52.90           C  
ANISOU 1228  CB  PRO A 157     8282   8972   2846    218    428    446       C  
ATOM   1229  CG  PRO A 157      28.979 103.451 266.695  1.00 52.56           C  
ANISOU 1229  CG  PRO A 157     8207   8948   2815    228    334    346       C  
ATOM   1230  CD  PRO A 157      29.062 103.793 265.183  1.00 52.65           C  
ANISOU 1230  CD  PRO A 157     8096   8905   3003    226    322    326       C  
ATOM   1231  N   GLU A 158      25.147 102.032 265.799  1.00 50.88           N  
ANISOU 1231  N   GLU A 158     7930   8645   2757    168    659    544       N  
ATOM   1232  CA  GLU A 158      23.949 101.287 266.159  1.00 51.35           C  
ANISOU 1232  CA  GLU A 158     8014   8706   2789    138    762    630       C  
ATOM   1233  C   GLU A 158      23.029 100.883 265.034  1.00 49.58           C  
ANISOU 1233  C   GLU A 158     7698   8433   2708    109    812    684       C  
ATOM   1234  O   GLU A 158      22.591  99.731 265.000  1.00 49.54           O  
ANISOU 1234  O   GLU A 158     7717   8406   2700     80    823    782       O  
ATOM   1235  CB  GLU A 158      23.188 102.015 267.252  1.00 52.92           C  
ANISOU 1235  CB  GLU A 158     8259   8961   2889    133    878    591       C  
ATOM   1236  CG  GLU A 158      24.086 102.376 268.451  1.00 57.40           C  
ANISOU 1236  CG  GLU A 158     8933   9580   3295    155    824    537       C  
ATOM   1237  CD  GLU A 158      24.790 101.161 269.078  1.00 60.80           C  
ANISOU 1237  CD  GLU A 158     9460  10024   3616    158    736    621       C  
ATOM   1238  OE1 GLU A 158      25.817 100.690 268.517  1.00 59.35           O  
ANISOU 1238  OE1 GLU A 158     9261   9814   3475    178    610    636       O  
ATOM   1239  OE2 GLU A 158      24.304 100.688 270.140  1.00 62.54           O  
ANISOU 1239  OE2 GLU A 158     9772  10284   3705    143    797    674       O  
ATOM   1240  N   HIS A 159      22.762 101.813 264.114  1.00 47.72           N  
ANISOU 1240  N   HIS A 159     7361   8177   2593    115    835    622       N  
ATOM   1241  CA  HIS A 159      21.754 101.637 263.048  1.00 46.11           C  
ANISOU 1241  CA  HIS A 159     7059   7937   2525     87    890    663       C  
ATOM   1242  C   HIS A 159      20.354 101.623 263.664  1.00 47.19           C  
ANISOU 1242  C   HIS A 159     7189   8109   2632     58   1031    703       C  
ATOM   1243  O   HIS A 159      19.453 100.925 263.187  1.00 47.29           O  
ANISOU 1243  O   HIS A 159     7153   8105   2707     16   1075    779       O  
ATOM   1244  CB  HIS A 159      21.994 100.366 262.190  1.00 45.23           C  
ANISOU 1244  CB  HIS A 159     6940   7772   2474     65    816    744       C  
ATOM   1245  CG  HIS A 159      23.331 100.328 261.516  1.00 41.86           C  
ANISOU 1245  CG  HIS A 159     6507   7315   2082    100    688    709       C  
ATOM   1246  ND1 HIS A 159      23.473 100.335 260.152  1.00 40.58           N  
ANISOU 1246  ND1 HIS A 159     6263   7107   2047     99    645    702       N  
ATOM   1247  CD2 HIS A 159      24.584 100.323 262.021  1.00 41.54           C  
ANISOU 1247  CD2 HIS A 159     6526   7292   1964    136    596    678       C  
ATOM   1248  CE1 HIS A 159      24.757 100.346 259.843  1.00 40.94           C  
ANISOU 1248  CE1 HIS A 159     6317   7145   2094    135    540    667       C  
ATOM   1249  NE2 HIS A 159      25.453 100.340 260.963  1.00 40.60           N  
ANISOU 1249  NE2 HIS A 159     6354   7142   1931    158    507    653       N  
ATOM   1250  N   ALA A 160      20.171 102.389 264.738  1.00 48.06           N  
ANISOU 1250  N   ALA A 160     7346   8272   2643     78   1101    650       N  
ATOM   1251  CA  ALA A 160      18.841 102.552 265.321  1.00 48.82           C  
ANISOU 1251  CA  ALA A 160     7424   8413   2714     62   1248    674       C  
ATOM   1252  C   ALA A 160      18.100 103.594 264.498  1.00 48.15           C  
ANISOU 1252  C   ALA A 160     7219   8317   2760     81   1311    623       C  
ATOM   1253  O   ALA A 160      17.076 103.289 263.874  1.00 48.24           O  
ANISOU 1253  O   ALA A 160     7139   8325   2864     52   1370    680       O  
ATOM   1254  CB  ALA A 160      18.920 102.961 266.766  1.00 50.00           C  
ANISOU 1254  CB  ALA A 160     7676   8622   2701     82   1305    634       C  
ATOM   1255  N   LEU A 161      18.636 104.812 264.463  1.00 47.49           N  
ANISOU 1255  N   LEU A 161     7134   8224   2685    128   1292    517       N  
ATOM   1256  CA  LEU A 161      18.129 105.817 263.526  1.00 46.50           C  
ANISOU 1256  CA  LEU A 161     6900   8071   2695    153   1326    469       C  
ATOM   1257  C   LEU A 161      18.555 105.433 262.104  1.00 44.48           C  
ANISOU 1257  C   LEU A 161     6572   7758   2568    135   1224    499       C  
ATOM   1258  O   LEU A 161      19.719 105.086 261.865  1.00 42.93           O  
ANISOU 1258  O   LEU A 161     6418   7537   2357    132   1108    490       O  
ATOM   1259  CB  LEU A 161      18.648 107.226 263.850  1.00 46.61           C  
ANISOU 1259  CB  LEU A 161     6947   8076   2686    203   1327    347       C  
ATOM   1260  CG  LEU A 161      18.586 107.864 265.240  1.00 48.98           C  
ANISOU 1260  CG  LEU A 161     7343   8421   2845    231   1402    280       C  
ATOM   1261  CD1 LEU A 161      19.272 109.247 265.276  1.00 49.70           C  
ANISOU 1261  CD1 LEU A 161     7465   8478   2939    269   1371    154       C  
ATOM   1262  CD2 LEU A 161      17.154 107.999 265.710  1.00 52.37           C  
ANISOU 1262  CD2 LEU A 161     7735   8895   3267    245   1562    304       C  
ATOM   1263  N   VAL A 162      17.603 105.470 261.177  1.00 43.71           N  
ANISOU 1263  N   VAL A 162     6366   7649   2594    124   1267    535       N  
ATOM   1264  CA  VAL A 162      17.937 105.477 259.755  1.00 42.42           C  
ANISOU 1264  CA  VAL A 162     6128   7432   2557    117   1183    540       C  
ATOM   1265  C   VAL A 162      17.223 106.632 259.040  1.00 42.61           C  
ANISOU 1265  C   VAL A 162     6052   7444   2693    150   1237    500       C  
ATOM   1266  O   VAL A 162      15.998 106.823 259.168  1.00 43.67           O  
ANISOU 1266  O   VAL A 162     6123   7610   2859    155   1341    526       O  
ATOM   1267  CB  VAL A 162      17.741 104.126 259.046  1.00 41.38           C  
ANISOU 1267  CB  VAL A 162     5971   7281   2470     63   1136    636       C  
ATOM   1268  CG1 VAL A 162      16.669 103.316 259.692  1.00 43.39           C  
ANISOU 1268  CG1 VAL A 162     6227   7575   2683     20   1225    716       C  
ATOM   1269  CG2 VAL A 162      17.403 104.347 257.611  1.00 40.85           C  
ANISOU 1269  CG2 VAL A 162     5798   7179   2545     56   1107    645       C  
ATOM   1270  N   ALA A 163      18.019 107.420 258.320  1.00 41.38           N  
ANISOU 1270  N   ALA A 163     5885   7244   2595    175   1165    438       N  
ATOM   1271  CA  ALA A 163      17.506 108.538 257.571  1.00 40.57           C  
ANISOU 1271  CA  ALA A 163     5700   7116   2598    210   1199    402       C  
ATOM   1272  C   ALA A 163      17.438 108.165 256.095  1.00 39.55           C  
ANISOU 1272  C   ALA A 163     5486   6954   2586    184   1133    452       C  
ATOM   1273  O   ALA A 163      18.131 107.229 255.645  1.00 39.10           O  
ANISOU 1273  O   ALA A 163     5451   6883   2524    148   1046    487       O  
ATOM   1274  CB  ALA A 163      18.390 109.723 257.783  1.00 40.02           C  
ANISOU 1274  CB  ALA A 163     5681   7015   2508    247   1170    303       C  
ATOM   1275  N   TYR A 164      16.596 108.886 255.348  1.00 39.04           N  
ANISOU 1275  N   TYR A 164     5328   6879   2625    208   1174    455       N  
ATOM   1276  CA  TYR A 164      16.474 108.721 253.880  1.00 38.18           C  
ANISOU 1276  CA  TYR A 164     5137   6741   2630    188   1112    495       C  
ATOM   1277  C   TYR A 164      16.028 110.045 253.211  1.00 38.19           C  
ANISOU 1277  C   TYR A 164     5069   6714   2726    239   1140    461       C  
ATOM   1278  O   TYR A 164      15.592 111.001 253.893  1.00 38.96           O  
ANISOU 1278  O   TYR A 164     5173   6817   2812    291   1222    414       O  
ATOM   1279  CB  TYR A 164      15.503 107.576 253.525  1.00 38.32           C  
ANISOU 1279  CB  TYR A 164     5093   6789   2679    137   1128    589       C  
ATOM   1280  CG  TYR A 164      14.076 107.913 253.837  1.00 39.26           C  
ANISOU 1280  CG  TYR A 164     5130   6954   2833    154   1240    617       C  
ATOM   1281  CD1 TYR A 164      13.627 107.950 255.157  1.00 40.30           C  
ANISOU 1281  CD1 TYR A 164     5298   7132   2882    169   1339    607       C  
ATOM   1282  CD2 TYR A 164      13.174 108.240 252.820  1.00 39.21           C  
ANISOU 1282  CD2 TYR A 164     5007   6951   2941    160   1248    652       C  
ATOM   1283  CE1 TYR A 164      12.316 108.280 255.472  1.00 41.29           C  
ANISOU 1283  CE1 TYR A 164     5341   7308   3038    192   1451    632       C  
ATOM   1284  CE2 TYR A 164      11.836 108.582 253.131  1.00 40.22           C  
ANISOU 1284  CE2 TYR A 164     5045   7131   3105    184   1354    679       C  
ATOM   1285  CZ  TYR A 164      11.424 108.598 254.459  1.00 41.25           C  
ANISOU 1285  CZ  TYR A 164     5210   7310   3155    201   1459    667       C  
ATOM   1286  OH  TYR A 164      10.123 108.933 254.790  1.00 42.73           O  
ANISOU 1286  OH  TYR A 164     5303   7557   3377    231   1572    693       O  
ATOM   1287  N   SER A 165      16.147 110.115 251.893  1.00 37.42           N  
ANISOU 1287  N   SER A 165     4914   6585   2718    227   1074    483       N  
ATOM   1288  CA  SER A 165      15.817 111.341 251.200  1.00 37.43           C  
ANISOU 1288  CA  SER A 165     4861   6553   2807    275   1088    458       C  
ATOM   1289  C   SER A 165      14.941 110.993 250.027  1.00 37.21           C  
ANISOU 1289  C   SER A 165     4727   6536   2875    256   1070    532       C  
ATOM   1290  O   SER A 165      15.137 109.955 249.377  1.00 36.63           O  
ANISOU 1290  O   SER A 165     4644   6468   2807    199   1004    580       O  
ATOM   1291  CB  SER A 165      17.078 112.102 250.743  1.00 36.79           C  
ANISOU 1291  CB  SER A 165     4831   6414   2733    283   1015    397       C  
ATOM   1292  OG  SER A 165      17.907 111.341 249.867  1.00 35.86           O  
ANISOU 1292  OG  SER A 165     4718   6286   2622    235    917    423       O  
ATOM   1293  N   VAL A 166      13.976 111.852 249.745  1.00 37.75           N  
ANISOU 1293  N   VAL A 166     4718   6607   3019    306   1125    540       N  
ATOM   1294  CA  VAL A 166      12.999 111.493 248.734  1.00 37.76           C  
ANISOU 1294  CA  VAL A 166     4608   6633   3106    287   1111    615       C  
ATOM   1295  C   VAL A 166      12.618 112.685 247.819  1.00 37.85           C  
ANISOU 1295  C   VAL A 166     4554   6611   3215    345   1106    613       C  
ATOM   1296  O   VAL A 166      12.466 113.820 248.280  1.00 38.43           O  
ANISOU 1296  O   VAL A 166     4640   6660   3302    418   1166    565       O  
ATOM   1297  CB  VAL A 166      11.793 110.777 249.407  1.00 38.65           C  
ANISOU 1297  CB  VAL A 166     4659   6820   3208    268   1192    669       C  
ATOM   1298  CG1 VAL A 166      11.142 111.676 250.461  1.00 39.75           C  
ANISOU 1298  CG1 VAL A 166     4789   6981   3333    343   1311    631       C  
ATOM   1299  CG2 VAL A 166      10.791 110.281 248.399  1.00 38.76           C  
ANISOU 1299  CG2 VAL A 166     4553   6868   3305    232   1167    750       C  
ATOM   1300  N   ASP A 167      12.539 112.424 246.522  1.00 37.31           N  
ANISOU 1300  N   ASP A 167     4431   6535   3209    314   1029    662       N  
ATOM   1301  CA  ASP A 167      12.067 113.416 245.576  1.00 37.73           C  
ANISOU 1301  CA  ASP A 167     4418   6564   3355    365   1017    678       C  
ATOM   1302  C   ASP A 167      10.745 112.919 245.040  1.00 38.55           C  
ANISOU 1302  C   ASP A 167     4395   6730   3521    350   1024    759       C  
ATOM   1303  O   ASP A 167      10.670 111.792 244.563  1.00 38.01           O  
ANISOU 1303  O   ASP A 167     4307   6692   3444    272    970    806       O  
ATOM   1304  CB  ASP A 167      13.056 113.597 244.398  1.00 36.91           C  
ANISOU 1304  CB  ASP A 167     4349   6406   3268    340    915    673       C  
ATOM   1305  CG  ASP A 167      12.590 114.664 243.372  1.00 37.25           C  
ANISOU 1305  CG  ASP A 167     4333   6419   3403    392    898    698       C  
ATOM   1306  OD1 ASP A 167      11.732 115.530 243.682  1.00 41.94           O  
ANISOU 1306  OD1 ASP A 167     4877   7012   4046    467    966    699       O  
ATOM   1307  OD2 ASP A 167      13.106 114.665 242.246  1.00 36.42           O  
ANISOU 1307  OD2 ASP A 167     4233   6287   3318    364    817    717       O  
ATOM   1308  N   TYR A 168       9.724 113.773 245.076  1.00 40.35           N  
ANISOU 1308  N   TYR A 168     4540   6976   3817    424   1087    775       N  
ATOM   1309  CA  TYR A 168       8.379 113.382 244.644  1.00 42.11           C  
ANISOU 1309  CA  TYR A 168     4624   7272   4105    415   1099    854       C  
ATOM   1310  C   TYR A 168       7.964 113.906 243.285  1.00 43.06           C  
ANISOU 1310  C   TYR A 168     4665   7382   4315    438   1031    902       C  
ATOM   1311  O   TYR A 168       6.902 113.532 242.805  1.00 43.83           O  
ANISOU 1311  O   TYR A 168     4642   7545   4467    421   1022    971       O  
ATOM   1312  CB  TYR A 168       7.330 113.771 245.684  1.00 42.89           C  
ANISOU 1312  CB  TYR A 168     4656   7424   4216    481   1223    853       C  
ATOM   1313  CG  TYR A 168       7.371 112.887 246.881  1.00 43.94           C  
ANISOU 1313  CG  TYR A 168     4834   7600   4263    431   1286    841       C  
ATOM   1314  CD1 TYR A 168       7.078 111.535 246.752  1.00 46.13           C  
ANISOU 1314  CD1 TYR A 168     5078   7930   4520    329   1254    900       C  
ATOM   1315  CD2 TYR A 168       7.738 113.378 248.155  1.00 43.77           C  
ANISOU 1315  CD2 TYR A 168     4898   7561   4171    482   1373    769       C  
ATOM   1316  CE1 TYR A 168       7.111 110.666 247.878  1.00 48.16           C  
ANISOU 1316  CE1 TYR A 168     5383   8223   4692    279   1312    898       C  
ATOM   1317  CE2 TYR A 168       7.766 112.522 249.294  1.00 44.75           C  
ANISOU 1317  CE2 TYR A 168     5069   7730   4205    435   1431    764       C  
ATOM   1318  CZ  TYR A 168       7.446 111.158 249.141  1.00 46.63           C  
ANISOU 1318  CZ  TYR A 168     5271   8020   4427    333   1401    834       C  
ATOM   1319  OH  TYR A 168       7.448 110.244 250.190  1.00 45.71           O  
ANISOU 1319  OH  TYR A 168     5203   7944   4222    278   1452    843       O  
ATOM   1320  N   CYS A 169       8.764 114.777 242.669  1.00 43.71           N  
ANISOU 1320  N   CYS A 169     4809   7387   4411    474    983    870       N  
ATOM   1321  CA  CYS A 169       8.415 115.255 241.326  1.00 44.94           C  
ANISOU 1321  CA  CYS A 169     4899   7532   4643    493    912    922       C  
ATOM   1322  C   CYS A 169       9.531 115.081 240.309  1.00 43.69           C  
ANISOU 1322  C   CYS A 169     4819   7323   4461    437    809    916       C  
ATOM   1323  O   CYS A 169       9.305 115.181 239.089  1.00 43.60           O  
ANISOU 1323  O   CYS A 169     4760   7313   4493    428    735    967       O  
ATOM   1324  CB  CYS A 169       7.888 116.700 241.343  1.00 46.36           C  
ANISOU 1324  CB  CYS A 169     5045   7676   4894    613    963    917       C  
ATOM   1325  SG  CYS A 169       9.086 117.909 241.847  1.00 48.00           S  
ANISOU 1325  SG  CYS A 169     5398   7768   5071    670    991    823       S  
ATOM   1326  N   GLY A 170      10.736 114.838 240.811  1.00 42.88           N  
ANISOU 1326  N   GLY A 170     4830   7179   4284    403    804    854       N  
ATOM   1327  CA  GLY A 170      11.873 114.558 239.928  1.00 41.97           C  
ANISOU 1327  CA  GLY A 170     4785   7025   4137    347    715    845       C  
ATOM   1328  C   GLY A 170      12.733 115.743 239.533  1.00 41.54           C  
ANISOU 1328  C   GLY A 170     4795   6892   4095    388    698    809       C  
ATOM   1329  O   GLY A 170      13.581 115.608 238.677  1.00 41.57           O  
ANISOU 1329  O   GLY A 170     4841   6873   4082    346    628    810       O  
ATOM   1330  N   ASP A 171      12.513 116.903 240.139  1.00 41.90           N  
ANISOU 1330  N   ASP A 171     4852   6897   4172    467    763    777       N  
ATOM   1331  CA  ASP A 171      13.325 118.068 239.858  1.00 41.59           C  
ANISOU 1331  CA  ASP A 171     4884   6773   4146    499    751    740       C  
ATOM   1332  C   ASP A 171      14.611 117.948 240.656  1.00 40.74           C  
ANISOU 1332  C   ASP A 171     4882   6636   3962    461    757    662       C  
ATOM   1333  O   ASP A 171      15.508 118.815 240.590  1.00 40.18           O  
ANISOU 1333  O   ASP A 171     4884   6495   3887    466    747    619       O  
ATOM   1334  CB  ASP A 171      12.578 119.335 240.215  1.00 43.12           C  
ANISOU 1334  CB  ASP A 171     5057   6923   4402    600    818    734       C  
ATOM   1335  CG  ASP A 171      12.344 119.475 241.688  1.00 46.25           C  
ANISOU 1335  CG  ASP A 171     5480   7326   4767    641    914    673       C  
ATOM   1336  OD1 ASP A 171      12.369 118.466 242.437  1.00 48.95           O  
ANISOU 1336  OD1 ASP A 171     5822   7727   5048    596    935    659       O  
ATOM   1337  OD2 ASP A 171      12.124 120.624 242.109  1.00 50.85           O  
ANISOU 1337  OD2 ASP A 171     6089   7848   5383    723    970    638       O  
ATOM   1338  N   GLU A 172      14.675 116.845 241.401  1.00 39.59           N  
ANISOU 1338  N   GLU A 172     4742   6544   3755    418    771    649       N  
ATOM   1339  CA  GLU A 172      15.872 116.428 242.118  1.00 38.77           C  
ANISOU 1339  CA  GLU A 172     4727   6433   3571    375    762    587       C  
ATOM   1340  C   GLU A 172      16.266 117.275 243.327  1.00 38.66           C  
ANISOU 1340  C   GLU A 172     4786   6378   3524    414    824    509       C  
ATOM   1341  O   GLU A 172      17.440 117.367 243.663  1.00 38.28           O  
ANISOU 1341  O   GLU A 172     4816   6304   3425    383    799    454       O  
ATOM   1342  CB  GLU A 172      17.037 116.221 241.157  1.00 37.93           C  
ANISOU 1342  CB  GLU A 172     4658   6306   3447    320    679    587       C  
ATOM   1343  CG  GLU A 172      16.960 114.853 240.514  1.00 38.59           C  
ANISOU 1343  CG  GLU A 172     4709   6443   3510    263    625    635       C  
ATOM   1344  CD  GLU A 172      17.977 114.643 239.407  1.00 38.14           C  
ANISOU 1344  CD  GLU A 172     4679   6373   3441    218    549    641       C  
ATOM   1345  OE1 GLU A 172      19.204 114.576 239.720  1.00 36.46           O  
ANISOU 1345  OE1 GLU A 172     4530   6146   3178    195    531    592       O  
ATOM   1346  OE2 GLU A 172      17.511 114.516 238.243  1.00 36.52           O  
ANISOU 1346  OE2 GLU A 172     4425   6177   3272    207    507    697       O  
ATOM   1347  N   VAL A 173      15.266 117.873 243.967  1.00 38.86           N  
ANISOU 1347  N   VAL A 173     4783   6402   3580    483    903    503       N  
ATOM   1348  CA  VAL A 173      15.395 118.488 245.274  1.00 38.80           C  
ANISOU 1348  CA  VAL A 173     4842   6369   3529    523    976    427       C  
ATOM   1349  C   VAL A 173      14.786 117.498 246.277  1.00 39.21           C  
ANISOU 1349  C   VAL A 173     4872   6500   3526    514   1032    435       C  
ATOM   1350  O   VAL A 173      13.671 116.987 246.061  1.00 38.91           O  
ANISOU 1350  O   VAL A 173     4741   6518   3526    524   1058    498       O  
ATOM   1351  CB  VAL A 173      14.631 119.831 245.326  1.00 40.31           C  
ANISOU 1351  CB  VAL A 173     5022   6505   3790    616   1039    414       C  
ATOM   1352  CG1 VAL A 173      14.726 120.493 246.739  1.00 40.64           C  
ANISOU 1352  CG1 VAL A 173     5145   6516   3779    663   1122    324       C  
ATOM   1353  CG2 VAL A 173      15.090 120.765 244.212  1.00 38.13           C  
ANISOU 1353  CG2 VAL A 173     4762   6149   3577    623    982    426       C  
ATOM   1354  N   TYR A 174      15.510 117.256 247.376  1.00 39.40           N  
ANISOU 1354  N   TYR A 174     4982   6530   3460    492   1049    373       N  
ATOM   1355  CA  TYR A 174      15.150 116.202 248.351  1.00 39.59           C  
ANISOU 1355  CA  TYR A 174     5004   6626   3412    470   1092    383       C  
ATOM   1356  C   TYR A 174      14.759 116.726 249.738  1.00 41.05           C  
ANISOU 1356  C   TYR A 174     5235   6817   3544    524   1195    325       C  
ATOM   1357  O   TYR A 174      15.278 117.748 250.204  1.00 41.70           O  
ANISOU 1357  O   TYR A 174     5394   6841   3609    557   1212    248       O  
ATOM   1358  CB  TYR A 174      16.287 115.177 248.471  1.00 38.07           C  
ANISOU 1358  CB  TYR A 174     4872   6452   3143    394   1020    377       C  
ATOM   1359  CG  TYR A 174      16.575 114.419 247.172  1.00 37.57           C  
ANISOU 1359  CG  TYR A 174     4764   6393   3117    341    930    437       C  
ATOM   1360  CD1 TYR A 174      17.249 115.031 246.099  1.00 35.46           C  
ANISOU 1360  CD1 TYR A 174     4499   6076   2898    335    866    431       C  
ATOM   1361  CD2 TYR A 174      16.161 113.075 247.006  1.00 36.61           C  
ANISOU 1361  CD2 TYR A 174     4604   6326   2981    294    912    499       C  
ATOM   1362  CE1 TYR A 174      17.489 114.332 244.911  1.00 34.72           C  
ANISOU 1362  CE1 TYR A 174     4370   5992   2830    290    790    483       C  
ATOM   1363  CE2 TYR A 174      16.409 112.376 245.829  1.00 35.02           C  
ANISOU 1363  CE2 TYR A 174     4373   6124   2808    247    832    545       C  
ATOM   1364  CZ  TYR A 174      17.077 113.015 244.807  1.00 34.51           C  
ANISOU 1364  CZ  TYR A 174     4312   6017   2784    249    774    535       C  
ATOM   1365  OH  TYR A 174      17.319 112.334 243.657  1.00 35.20           O  
ANISOU 1365  OH  TYR A 174     4376   6108   2890    206    701    576       O  
ATOM   1366  N   SER A 175      13.812 116.047 250.385  1.00 41.88           N  
ANISOU 1366  N   SER A 175     5294   6993   3625    529   1265    360       N  
ATOM   1367  CA  SER A 175      13.656 116.179 251.838  1.00 42.48           C  
ANISOU 1367  CA  SER A 175     5431   7093   3614    559   1356    305       C  
ATOM   1368  C   SER A 175      14.337 115.007 252.518  1.00 41.61           C  
ANISOU 1368  C   SER A 175     5385   7027   3399    487   1324    309       C  
ATOM   1369  O   SER A 175      14.452 113.941 251.947  1.00 40.67           O  
ANISOU 1369  O   SER A 175     5231   6935   3285    426   1263    372       O  
ATOM   1370  CB  SER A 175      12.188 116.330 252.298  1.00 44.01           C  
ANISOU 1370  CB  SER A 175     5542   7340   3838    621   1474    333       C  
ATOM   1371  OG  SER A 175      11.225 116.108 251.274  1.00 44.89           O  
ANISOU 1371  OG  SER A 175     5523   7482   4053    625   1464    417       O  
ATOM   1372  N   ILE A 176      14.841 115.215 253.719  1.00 42.55           N  
ANISOU 1372  N   ILE A 176     5603   7147   3417    496   1359    240       N  
ATOM   1373  CA  ILE A 176      15.420 114.112 254.458  1.00 42.49           C  
ANISOU 1373  CA  ILE A 176     5658   7184   3302    438   1333    250       C  
ATOM   1374  C   ILE A 176      14.539 113.845 255.657  1.00 44.99           C  
ANISOU 1374  C   ILE A 176     5983   7564   3549    459   1447    255       C  
ATOM   1375  O   ILE A 176      14.087 114.770 256.338  1.00 46.66           O  
ANISOU 1375  O   ILE A 176     6216   7769   3744    524   1536    198       O  
ATOM   1376  CB  ILE A 176      16.835 114.392 254.905  1.00 41.83           C  
ANISOU 1376  CB  ILE A 176     5687   7065   3142    417   1265    175       C  
ATOM   1377  CG1 ILE A 176      17.747 114.648 253.693  1.00 38.81           C  
ANISOU 1377  CG1 ILE A 176     5290   6627   2829    391   1158    174       C  
ATOM   1378  CG2 ILE A 176      17.355 113.224 255.702  1.00 40.77           C  
ANISOU 1378  CG2 ILE A 176     5613   6981   2897    368   1238    194       C  
ATOM   1379  CD1 ILE A 176      18.822 115.666 253.973  1.00 38.90           C  
ANISOU 1379  CD1 ILE A 176     5385   6583   2811    396   1121     82       C  
ATOM   1380  N   ARG A 177      14.283 112.569 255.894  1.00 45.76           N  
ANISOU 1380  N   ARG A 177     6065   7719   3603    405   1446    324       N  
ATOM   1381  CA  ARG A 177      13.300 112.144 256.848  1.00 47.58           C  
ANISOU 1381  CA  ARG A 177     6280   8020   3779    411   1557    355       C  
ATOM   1382  C   ARG A 177      13.877 110.902 257.509  1.00 47.40           C  
ANISOU 1382  C   ARG A 177     6333   8029   3646    344   1520    388       C  
ATOM   1383  O   ARG A 177      14.956 110.443 257.139  1.00 46.02           O  
ANISOU 1383  O   ARG A 177     6209   7823   3455    304   1411    386       O  
ATOM   1384  CB  ARG A 177      11.971 111.888 256.105  1.00 48.04           C  
ANISOU 1384  CB  ARG A 177     6193   8115   3944    412   1603    437       C  
ATOM   1385  CG  ARG A 177      11.182 113.188 255.856  1.00 52.18           C  
ANISOU 1385  CG  ARG A 177     6648   8624   4554    503   1677    403       C  
ATOM   1386  CD  ARG A 177       9.913 113.069 254.998  1.00 57.07           C  
ANISOU 1386  CD  ARG A 177     7110   9282   5292    512   1707    483       C  
ATOM   1387  NE  ARG A 177       9.586 114.384 254.408  1.00 63.06           N  
ANISOU 1387  NE  ARG A 177     7820   9993   6146    602   1724    447       N  
ATOM   1388  CZ  ARG A 177       9.165 114.588 253.143  1.00 65.09           C  
ANISOU 1388  CZ  ARG A 177     7974  10235   6523    610   1672    497       C  
ATOM   1389  NH1 ARG A 177       8.990 113.558 252.301  1.00 63.65           N  
ANISOU 1389  NH1 ARG A 177     7722  10083   6379    531   1599    579       N  
ATOM   1390  NH2 ARG A 177       8.921 115.834 252.705  1.00 64.38           N  
ANISOU 1390  NH2 ARG A 177     7857  10094   6512    699   1689    464       N  
ATOM   1391  N   PHE A 178      13.179 110.362 258.497  1.00 48.99           N  
ANISOU 1391  N   PHE A 178     6545   8296   3773    333   1612    420       N  
ATOM   1392  CA  PHE A 178      13.650 109.154 259.150  1.00 49.70           C  
ANISOU 1392  CA  PHE A 178     6713   8414   3757    271   1581    462       C  
ATOM   1393  C   PHE A 178      12.631 108.072 259.074  1.00 50.78           C  
ANISOU 1393  C   PHE A 178     6778   8603   3915    216   1628    566       C  
ATOM   1394  O   PHE A 178      11.439 108.343 259.164  1.00 52.39           O  
ANISOU 1394  O   PHE A 178     6892   8853   4162    236   1732    591       O  
ATOM   1395  CB  PHE A 178      13.993 109.462 260.597  1.00 50.60           C  
ANISOU 1395  CB  PHE A 178     6943   8555   3727    297   1637    401       C  
ATOM   1396  CG  PHE A 178      15.240 110.250 260.724  1.00 50.34           C  
ANISOU 1396  CG  PHE A 178     7001   8471   3656    323   1561    305       C  
ATOM   1397  CD1 PHE A 178      15.216 111.633 260.593  1.00 50.26           C  
ANISOU 1397  CD1 PHE A 178     6985   8420   3691    386   1590    219       C  
ATOM   1398  CD2 PHE A 178      16.458 109.610 260.882  1.00 50.62           C  
ANISOU 1398  CD2 PHE A 178     7121   8493   3621    283   1451    304       C  
ATOM   1399  CE1 PHE A 178      16.376 112.373 260.665  1.00 49.30           C  
ANISOU 1399  CE1 PHE A 178     6944   8247   3540    397   1515    132       C  
ATOM   1400  CE2 PHE A 178      17.635 110.344 260.960  1.00 50.91           C  
ANISOU 1400  CE2 PHE A 178     7227   8489   3628    299   1374    217       C  
ATOM   1401  CZ  PHE A 178      17.592 111.734 260.844  1.00 50.07           C  
ANISOU 1401  CZ  PHE A 178     7116   8343   3565    350   1405    131       C  
ATOM   1402  N   VAL A 179      13.097 106.843 258.915  1.00 51.03           N  
ANISOU 1402  N   VAL A 179     6848   8625   3916    146   1551    627       N  
ATOM   1403  CA  VAL A 179      12.217 105.679 258.907  1.00 52.69           C  
ANISOU 1403  CA  VAL A 179     7010   8876   4134     76   1586    730       C  
ATOM   1404  C   VAL A 179      11.228 105.672 260.091  1.00 55.63           C  
ANISOU 1404  C   VAL A 179     7377   9326   4434     80   1732    752       C  
ATOM   1405  O   VAL A 179      11.549 106.159 261.204  1.00 56.25           O  
ANISOU 1405  O   VAL A 179     7545   9426   4402    122   1786    694       O  
ATOM   1406  CB  VAL A 179      13.028 104.386 258.913  1.00 51.77           C  
ANISOU 1406  CB  VAL A 179     6981   8729   3960     11   1491    779       C  
ATOM   1407  CG1 VAL A 179      12.105 103.178 258.803  1.00 52.30           C  
ANISOU 1407  CG1 VAL A 179     7003   8822   4046    -72   1521    887       C  
ATOM   1408  CG2 VAL A 179      14.002 104.402 257.771  1.00 50.46           C  
ANISOU 1408  CG2 VAL A 179     6817   8494   3861     14   1359    754       C  
ATOM   1409  N   ARG A 180      10.025 105.141 259.834  1.00 57.46           N  
ANISOU 1409  N   ARG A 180     7501   9605   4725     33   1796    834       N  
ATOM   1410  CA  ARG A 180       8.976 105.005 260.852  1.00 60.36           C  
ANISOU 1410  CA  ARG A 180     7842  10059   5034     25   1942    871       C  
ATOM   1411  C   ARG A 180       8.909 106.196 261.814  1.00 61.34           C  
ANISOU 1411  C   ARG A 180     8002  10214   5090    119   2046    782       C  
ATOM   1412  O   ARG A 180       8.490 106.034 262.963  1.00 63.07           O  
ANISOU 1412  O   ARG A 180     8263  10498   5204    117   2155    793       O  
ATOM   1413  CB  ARG A 180       9.179 103.731 261.680  1.00 61.11           C  
ANISOU 1413  CB  ARG A 180     8037  10170   5012    -56   1943    941       C  
ATOM   1414  CG  ARG A 180       8.976 102.400 260.981  1.00 63.35           C  
ANISOU 1414  CG  ARG A 180     8293  10431   5347   -161   1875   1043       C  
ATOM   1415  CD  ARG A 180       9.591 101.351 261.889  1.00 68.76           C  
ANISOU 1415  CD  ARG A 180     9124  11104   5897   -212   1854   1086       C  
ATOM   1416  NE  ARG A 180       9.471  99.967 261.428  1.00 73.88           N  
ANISOU 1416  NE  ARG A 180     9783  11717   6570   -316   1793   1185       N  
ATOM   1417  CZ  ARG A 180      10.383  99.320 260.688  1.00 75.92           C  
ANISOU 1417  CZ  ARG A 180    10101  11891   6853   -338   1656   1192       C  
ATOM   1418  NH1 ARG A 180      11.499  99.928 260.260  1.00 74.65           N  
ANISOU 1418  NH1 ARG A 180     9982  11679   6703   -268   1561   1109       N  
ATOM   1419  NH2 ARG A 180      10.173  98.047 260.365  1.00 76.97           N  
ANISOU 1419  NH2 ARG A 180    10253  11989   7003   -433   1615   1281       N  
ATOM   1420  N   ASP A 181       9.349 107.370 261.360  1.00 60.69           N  
ANISOU 1420  N   ASP A 181     7915  10084   5062    199   2012    692       N  
ATOM   1421  CA  ASP A 181       9.310 108.593 262.161  1.00 61.81           C  
ANISOU 1421  CA  ASP A 181     8097  10237   5150    293   2102    596       C  
ATOM   1422  C   ASP A 181       9.839 108.431 263.560  1.00 62.02           C  
ANISOU 1422  C   ASP A 181     8272  10291   5003    292   2142    560       C  
ATOM   1423  O   ASP A 181       9.335 109.061 264.484  1.00 63.15           O  
ANISOU 1423  O   ASP A 181     8435  10480   5078    348   2266    513       O  
ATOM   1424  CB  ASP A 181       7.882 109.125 262.243  1.00 63.66           C  
ANISOU 1424  CB  ASP A 181     8201  10540   5449    343   2247    612       C  
ATOM   1425  CG  ASP A 181       7.462 109.828 260.970  1.00 66.15           C  
ANISOU 1425  CG  ASP A 181     8386  10820   5928    387   2212    609       C  
ATOM   1426  OD1 ASP A 181       7.236 109.135 259.946  1.00 68.59           O  
ANISOU 1426  OD1 ASP A 181     8608  11123   6331    323   2137    686       O  
ATOM   1427  OD2 ASP A 181       7.383 111.079 260.986  1.00 68.69           O  
ANISOU 1427  OD2 ASP A 181     8703  11116   6283    486   2255    529       O  
ATOM   1428  N   VAL A 182      10.842 107.572 263.720  1.00 60.96           N  
ANISOU 1428  N   VAL A 182     8241  10128   4793    233   2037    582       N  
ATOM   1429  CA  VAL A 182      11.458 107.322 265.027  1.00 60.62           C  
ANISOU 1429  CA  VAL A 182     8347  10110   4575    227   2053    557       C  
ATOM   1430  C   VAL A 182      11.820 108.656 265.685  1.00 60.60           C  
ANISOU 1430  C   VAL A 182     8416  10097   4511    312   2094    429       C  
ATOM   1431  O   VAL A 182      11.713 108.804 266.891  1.00 61.88           O  
ANISOU 1431  O   VAL A 182     8664  10308   4537    331   2179    398       O  
ATOM   1432  CB  VAL A 182      12.689 106.393 264.886  1.00 59.68           C  
ANISOU 1432  CB  VAL A 182     8323   9945   4408    170   1903    586       C  
ATOM   1433  CG1 VAL A 182      13.562 106.420 266.138  1.00 60.11           C  
ANISOU 1433  CG1 VAL A 182     8536  10016   4288    182   1889    536       C  
ATOM   1434  CG2 VAL A 182      12.233 104.963 264.567  1.00 59.41           C  
ANISOU 1434  CG2 VAL A 182     8251   9923   4397     83   1888    713       C  
ATOM   1435  N   VAL A 183      12.242 109.616 264.866  1.00 59.17           N  
ANISOU 1435  N   VAL A 183     8204   9848   4428    358   2032    358       N  
ATOM   1436  CA  VAL A 183      12.367 111.013 265.257  1.00 58.84           C  
ANISOU 1436  CA  VAL A 183     8207   9782   4368    441   2079    239       C  
ATOM   1437  C   VAL A 183      11.683 111.893 264.210  1.00 58.41           C  
ANISOU 1437  C   VAL A 183     8024   9689   4478    498   2107    224       C  
ATOM   1438  O   VAL A 183      11.303 111.430 263.123  1.00 57.36           O  
ANISOU 1438  O   VAL A 183     7777   9549   4470    467   2064    300       O  
ATOM   1439  CB  VAL A 183      13.838 111.454 265.432  1.00 58.49           C  
ANISOU 1439  CB  VAL A 183     8288   9676   4259    440   1958    150       C  
ATOM   1440  CG1 VAL A 183      14.560 110.562 266.448  1.00 59.00           C  
ANISOU 1440  CG1 VAL A 183     8477   9782   4159    389   1917    171       C  
ATOM   1441  CG2 VAL A 183      14.575 111.467 264.112  1.00 55.75           C  
ANISOU 1441  CG2 VAL A 183     7889   9257   4036    417   1819    159       C  
ATOM   1442  N   ALA A 184      11.534 113.169 264.539  1.00 58.97           N  
ANISOU 1442  N   ALA A 184     8124   9735   4549    582   2174    125       N  
ATOM   1443  CA  ALA A 184      10.622 114.049 263.804  1.00 58.92           C  
ANISOU 1443  CA  ALA A 184     7998   9706   4682    656   2239    116       C  
ATOM   1444  C   ALA A 184      11.335 115.028 262.880  1.00 57.75           C  
ANISOU 1444  C   ALA A 184     7858   9453   4631    688   2141     51       C  
ATOM   1445  O   ALA A 184      10.695 115.889 262.259  1.00 58.00           O  
ANISOU 1445  O   ALA A 184     7807   9451   4777    758   2183     36       O  
ATOM   1446  CB  ALA A 184       9.710 114.806 264.799  1.00 60.51           C  
ANISOU 1446  CB  ALA A 184     8211   9954   4828    744   2410     59       C  
ATOM   1447  N   ASP A 185      12.655 114.904 262.799  1.00 56.17           N  
ANISOU 1447  N   ASP A 185     7754   9204   4385    637   2013     17       N  
ATOM   1448  CA  ASP A 185      13.453 115.860 262.054  1.00 55.25           C  
ANISOU 1448  CA  ASP A 185     7661   8990   4341    656   1923    -50       C  
ATOM   1449  C   ASP A 185      13.168 115.756 260.550  1.00 54.00           C  
ANISOU 1449  C   ASP A 185     7372   8801   4346    646   1862     22       C  
ATOM   1450  O   ASP A 185      12.977 114.660 260.018  1.00 53.15           O  
ANISOU 1450  O   ASP A 185     7192   8733   4270    587   1821    117       O  
ATOM   1451  CB  ASP A 185      14.959 115.655 262.311  1.00 54.64           C  
ANISOU 1451  CB  ASP A 185     7702   8882   4176    595   1796    -95       C  
ATOM   1452  CG  ASP A 185      15.317 115.590 263.784  1.00 55.71           C  
ANISOU 1452  CG  ASP A 185     7971   9060   4138    591   1835   -155       C  
ATOM   1453  OD1 ASP A 185      14.610 114.880 264.526  1.00 57.38           O  
ANISOU 1453  OD1 ASP A 185     8178   9350   4273    587   1923   -106       O  
ATOM   1454  OD2 ASP A 185      16.328 116.213 264.191  1.00 54.98           O  
ANISOU 1454  OD2 ASP A 185     7988   8924   3980    584   1774   -247       O  
ATOM   1455  N   LYS A 186      13.155 116.911 259.886  1.00 53.63           N  
ANISOU 1455  N   LYS A 186     7305   8676   4395    703   1854    -27       N  
ATOM   1456  CA  LYS A 186      12.936 117.016 258.453  1.00 52.57           C  
ANISOU 1456  CA  LYS A 186     7060   8505   4409    703   1793     31       C  
ATOM   1457  C   LYS A 186      13.963 117.987 257.904  1.00 51.60           C  
ANISOU 1457  C   LYS A 186     7002   8280   4324    707   1705    -39       C  
ATOM   1458  O   LYS A 186      14.284 118.970 258.555  1.00 52.34           O  
ANISOU 1458  O   LYS A 186     7191   8323   4372    749   1738   -136       O  
ATOM   1459  CB  LYS A 186      11.537 117.560 258.172  1.00 53.71           C  
ANISOU 1459  CB  LYS A 186     7091   8666   4649    787   1901     59       C  
ATOM   1460  CG  LYS A 186      10.427 116.518 258.306  1.00 56.24           C  
ANISOU 1460  CG  LYS A 186     7302   9093   4975    766   1971    156       C  
ATOM   1461  CD  LYS A 186       9.124 117.090 258.927  1.00 59.93           C  
ANISOU 1461  CD  LYS A 186     7707   9608   5455    862   2130    146       C  
ATOM   1462  CE  LYS A 186       8.322 115.954 259.612  1.00 63.66           C  
ANISOU 1462  CE  LYS A 186     8123  10198   5865    817   2213    220       C  
ATOM   1463  NZ  LYS A 186       7.136 116.402 260.460  1.00 68.25           N  
ANISOU 1463  NZ  LYS A 186     8656  10847   6428    905   2385    205       N  
ATOM   1464  N   VAL A 187      14.504 117.705 256.719  1.00 50.05           N  
ANISOU 1464  N   VAL A 187     6759   8053   4205    659   1594      8       N  
ATOM   1465  CA  VAL A 187      15.449 118.632 256.081  1.00 49.13           C  
ANISOU 1465  CA  VAL A 187     6691   7842   4134    655   1513    -47       C  
ATOM   1466  C   VAL A 187      15.054 118.877 254.631  1.00 48.12           C  
ANISOU 1466  C   VAL A 187     6458   7679   4147    669   1474     17       C  
ATOM   1467  O   VAL A 187      14.996 117.957 253.830  1.00 46.78           O  
ANISOU 1467  O   VAL A 187     6213   7547   4016    620   1417     98       O  
ATOM   1468  CB  VAL A 187      16.929 118.181 256.197  1.00 47.81           C  
ANISOU 1468  CB  VAL A 187     6605   7668   3892    573   1400    -75       C  
ATOM   1469  CG1 VAL A 187      17.799 119.119 255.445  1.00 48.50           C  
ANISOU 1469  CG1 VAL A 187     6723   7667   4039    562   1324   -119       C  
ATOM   1470  CG2 VAL A 187      17.393 118.236 257.626  1.00 49.24           C  
ANISOU 1470  CG2 VAL A 187     6904   7871   3934    568   1430   -152       C  
ATOM   1471  N   GLU A 188      14.777 120.129 254.309  1.00 48.72           N  
ANISOU 1471  N   GLU A 188     6538   7679   4296    737   1504    -22       N  
ATOM   1472  CA  GLU A 188      14.206 120.460 253.006  1.00 49.31           C  
ANISOU 1472  CA  GLU A 188     6511   7723   4501    766   1481     43       C  
ATOM   1473  C   GLU A 188      15.250 121.025 252.047  1.00 47.68           C  
ANISOU 1473  C   GLU A 188     6342   7432   4342    728   1377     29       C  
ATOM   1474  O   GLU A 188      16.203 121.680 252.496  1.00 48.64           O  
ANISOU 1474  O   GLU A 188     6572   7493   4416    710   1353    -54       O  
ATOM   1475  CB  GLU A 188      13.060 121.475 253.159  1.00 51.01           C  
ANISOU 1475  CB  GLU A 188     6691   7909   4781    881   1587     28       C  
ATOM   1476  CG  GLU A 188      11.952 121.039 254.097  1.00 54.73           C  
ANISOU 1476  CG  GLU A 188     7114   8469   5212    928   1707     41       C  
ATOM   1477  CD  GLU A 188      11.163 119.814 253.608  1.00 58.74           C  
ANISOU 1477  CD  GLU A 188     7487   9079   5753    887   1701    153       C  
ATOM   1478  OE1 GLU A 188      10.789 119.754 252.407  1.00 59.98           O  
ANISOU 1478  OE1 GLU A 188     7545   9233   6013    885   1648    226       O  
ATOM   1479  OE2 GLU A 188      10.884 118.922 254.450  1.00 61.79           O  
ANISOU 1479  OE2 GLU A 188     7870   9549   6058    855   1752    168       O  
ATOM   1480  N   GLY A 189      15.070 120.770 250.748  1.00 45.30           N  
ANISOU 1480  N   GLY A 189     5952   7132   4129    710   1316    109       N  
ATOM   1481  CA  GLY A 189      15.901 121.393 249.694  1.00 42.69           C  
ANISOU 1481  CA  GLY A 189     5643   6722   3854    682   1230    109       C  
ATOM   1482  C   GLY A 189      17.361 120.984 249.576  1.00 40.40           C  
ANISOU 1482  C   GLY A 189     5416   6427   3507    589   1135     83       C  
ATOM   1483  O   GLY A 189      18.240 121.836 249.450  1.00 40.43           O  
ANISOU 1483  O   GLY A 189     5491   6356   3515    570   1098     30       O  
ATOM   1484  N   THR A 190      17.608 119.674 249.564  1.00 38.66           N  
ANISOU 1484  N   THR A 190     5166   6286   3239    530   1094    126       N  
ATOM   1485  CA  THR A 190      18.952 119.094 249.616  1.00 37.87           C  
ANISOU 1485  CA  THR A 190     5117   6200   3073    452   1012    104       C  
ATOM   1486  C   THR A 190      19.235 118.343 248.322  1.00 36.84           C  
ANISOU 1486  C   THR A 190     4919   6090   2987    404    932    178       C  
ATOM   1487  O   THR A 190      18.301 118.062 247.568  1.00 36.73           O  
ANISOU 1487  O   THR A 190     4823   6095   3038    423    942    248       O  
ATOM   1488  CB  THR A 190      19.065 118.094 250.790  1.00 37.98           C  
ANISOU 1488  CB  THR A 190     5166   6285   2979    430   1031     89       C  
ATOM   1489  OG1 THR A 190      18.753 116.781 250.333  1.00 37.33           O  
ANISOU 1489  OG1 THR A 190     5017   6267   2899    397   1005    170       O  
ATOM   1490  CG2 THR A 190      18.125 118.455 251.924  1.00 39.09           C  
ANISOU 1490  CG2 THR A 190     5329   6440   3085    491   1140     55       C  
ATOM   1491  N   ASN A 191      20.503 117.997 248.074  1.00 36.16           N  
ANISOU 1491  N   ASN A 191     4868   6007   2865    343    853    162       N  
ATOM   1492  CA  ASN A 191      20.886 117.241 246.864  1.00 35.24           C  
ANISOU 1492  CA  ASN A 191     4698   5911   2779    300    779    224       C  
ATOM   1493  C   ASN A 191      20.624 115.747 247.023  1.00 34.84           C  
ANISOU 1493  C   ASN A 191     4618   5933   2685    277    768    272       C  
ATOM   1494  O   ASN A 191      20.674 114.991 246.063  1.00 34.43           O  
ANISOU 1494  O   ASN A 191     4523   5902   2658    248    719    327       O  
ATOM   1495  CB  ASN A 191      22.363 117.460 246.494  1.00 34.79           C  
ANISOU 1495  CB  ASN A 191     4680   5834   2703    249    705    189       C  
ATOM   1496  CG  ASN A 191      23.323 116.815 247.494  1.00 35.77           C  
ANISOU 1496  CG  ASN A 191     4858   6000   2731    217    677    144       C  
ATOM   1497  OD1 ASN A 191      22.913 116.398 248.579  1.00 41.63           O  
ANISOU 1497  OD1 ASN A 191     5628   6775   3413    234    718    129       O  
ATOM   1498  ND2 ASN A 191      24.606 116.753 247.148  1.00 34.34           N  
ANISOU 1498  ND2 ASN A 191     4691   5824   2533    171    608    125       N  
ATOM   1499  N   GLY A 192      20.374 115.315 248.243  1.00 35.28           N  
ANISOU 1499  N   GLY A 192     4709   6024   2672    286    813    251       N  
ATOM   1500  CA  GLY A 192      20.057 113.937 248.479  1.00 35.07           C  
ANISOU 1500  CA  GLY A 192     4665   6056   2604    262    810    300       C  
ATOM   1501  C   GLY A 192      21.057 113.246 249.361  1.00 34.98           C  
ANISOU 1501  C   GLY A 192     4725   6073   2494    234    776    269       C  
ATOM   1502  O   GLY A 192      20.674 112.365 250.128  1.00 35.24           O  
ANISOU 1502  O   GLY A 192     4773   6149   2469    229    803    292       O  
ATOM   1503  N   SER A 193      22.333 113.617 249.254  1.00 34.70           N  
ANISOU 1503  N   SER A 193     4729   6018   2438    215    715    222       N  
ATOM   1504  CA  SER A 193      23.368 112.987 250.091  1.00 34.71           C  
ANISOU 1504  CA  SER A 193     4791   6053   2345    193    671    193       C  
ATOM   1505  C   SER A 193      23.148 113.231 251.595  1.00 35.58           C  
ANISOU 1505  C   SER A 193     4967   6179   2371    212    727    146       C  
ATOM   1506  O   SER A 193      22.967 114.362 252.009  1.00 36.15           O  
ANISOU 1506  O   SER A 193     5066   6220   2449    234    770     90       O  
ATOM   1507  CB  SER A 193      24.750 113.478 249.691  1.00 34.41           C  
ANISOU 1507  CB  SER A 193     4768   5997   2309    167    598    149       C  
ATOM   1508  OG  SER A 193      24.839 113.628 248.283  1.00 35.03           O  
ANISOU 1508  OG  SER A 193     4789   6052   2469    155    566    183       O  
ATOM   1509  N   VAL A 194      23.130 112.165 252.388  1.00 35.75           N  
ANISOU 1509  N   VAL A 194     5021   6248   2313    204    728    170       N  
ATOM   1510  CA  VAL A 194      23.224 112.277 253.845  1.00 36.58           C  
ANISOU 1510  CA  VAL A 194     5204   6380   2314    214    762    124       C  
ATOM   1511  C   VAL A 194      24.515 111.652 254.356  1.00 36.51           C  
ANISOU 1511  C   VAL A 194     5250   6403   2220    190    679    108       C  
ATOM   1512  O   VAL A 194      24.759 110.479 254.117  1.00 36.11           O  
ANISOU 1512  O   VAL A 194     5190   6376   2154    178    636    164       O  
ATOM   1513  CB  VAL A 194      22.075 111.510 254.542  1.00 37.08           C  
ANISOU 1513  CB  VAL A 194     5270   6482   2337    226    840    175       C  
ATOM   1514  CG1 VAL A 194      22.029 111.808 256.043  1.00 38.10           C  
ANISOU 1514  CG1 VAL A 194     5483   6638   2355    242    894    122       C  
ATOM   1515  CG2 VAL A 194      20.742 111.817 253.887  1.00 37.12           C  
ANISOU 1515  CG2 VAL A 194     5195   6472   2436    247    913    214       C  
ATOM   1516  N   VAL A 195      25.338 112.403 255.064  1.00 36.99           N  
ANISOU 1516  N   VAL A 195     5369   6464   2224    185    654     31       N  
ATOM   1517  CA  VAL A 195      26.541 111.795 255.669  1.00 37.11           C  
ANISOU 1517  CA  VAL A 195     5430   6521   2150    166    571     18       C  
ATOM   1518  C   VAL A 195      26.545 111.944 257.208  1.00 38.16           C  
ANISOU 1518  C   VAL A 195     5654   6686   2157    173    599    -29       C  
ATOM   1519  O   VAL A 195      26.320 113.040 257.737  1.00 38.81           O  
ANISOU 1519  O   VAL A 195     5777   6746   2223    180    645    -99       O  
ATOM   1520  CB  VAL A 195      27.855 112.355 255.039  1.00 36.77           C  
ANISOU 1520  CB  VAL A 195     5364   6466   2141    139    483    -24       C  
ATOM   1521  CG1 VAL A 195      29.116 111.871 255.811  1.00 37.13           C  
ANISOU 1521  CG1 VAL A 195     5452   6566   2090    125    396    -47       C  
ATOM   1522  CG2 VAL A 195      27.944 112.003 253.553  1.00 35.80           C  
ANISOU 1522  CG2 VAL A 195     5158   6323   2121    133    453     29       C  
ATOM   1523  N   TRP A 196      26.808 110.852 257.920  1.00 38.40           N  
ANISOU 1523  N   TRP A 196     5727   6767   2097    173    569     10       N  
ATOM   1524  CA  TRP A 196      26.652 110.862 259.367  1.00 39.45           C  
ANISOU 1524  CA  TRP A 196     5950   6937   2102    180    604    -20       C  
ATOM   1525  C   TRP A 196      27.854 111.346 260.164  1.00 40.08           C  
ANISOU 1525  C   TRP A 196     6093   7043   2091    163    527    -95       C  
ATOM   1526  O   TRP A 196      28.989 111.159 259.766  1.00 39.72           O  
ANISOU 1526  O   TRP A 196     6023   7012   2058    146    427    -98       O  
ATOM   1527  CB  TRP A 196      26.227 109.485 259.854  1.00 39.61           C  
ANISOU 1527  CB  TRP A 196     5997   6997   2058    187    619     64       C  
ATOM   1528  CG  TRP A 196      24.745 109.242 259.703  1.00 39.65           C  
ANISOU 1528  CG  TRP A 196     5969   6991   2104    197    729    117       C  
ATOM   1529  CD1 TRP A 196      24.113 108.547 258.703  1.00 38.93           C  
ANISOU 1529  CD1 TRP A 196     5805   6880   2106    191    742    194       C  
ATOM   1530  CD2 TRP A 196      23.702 109.727 260.573  1.00 40.55           C  
ANISOU 1530  CD2 TRP A 196     6118   7119   2170    214    843     96       C  
ATOM   1531  NE1 TRP A 196      22.761 108.543 258.917  1.00 39.34           N  
ANISOU 1531  NE1 TRP A 196     5838   6939   2173    198    851    225       N  
ATOM   1532  CE2 TRP A 196      22.478 109.264 260.049  1.00 40.34           C  
ANISOU 1532  CE2 TRP A 196     6025   7087   2215    216    920    167       C  
ATOM   1533  CE3 TRP A 196      23.690 110.479 261.769  1.00 41.63           C  
ANISOU 1533  CE3 TRP A 196     6337   7276   2202    228    889     22       C  
ATOM   1534  CZ2 TRP A 196      21.247 109.535 260.676  1.00 41.17           C  
ANISOU 1534  CZ2 TRP A 196     6132   7213   2298    235   1044    171       C  
ATOM   1535  CZ3 TRP A 196      22.454 110.746 262.388  1.00 42.44           C  
ANISOU 1535  CZ3 TRP A 196     6453   7395   2279    252   1019     21       C  
ATOM   1536  CH2 TRP A 196      21.262 110.270 261.840  1.00 42.21           C  
ANISOU 1536  CH2 TRP A 196     6344   7366   2328    257   1096     98       C  
ATOM   1537  N   GLY A 197      27.581 111.998 261.295  1.00 42.11           N  
ANISOU 1537  N   GLY A 197     6433   7312   2256    168    577   -159       N  
ATOM   1538  CA  GLY A 197      28.590 112.280 262.302  1.00 43.42           C  
ANISOU 1538  CA  GLY A 197     6676   7516   2304    148    506   -224       C  
ATOM   1539  C   GLY A 197      28.659 111.036 263.152  1.00 45.07           C  
ANISOU 1539  C   GLY A 197     6938   7790   2398    158    485   -161       C  
ATOM   1540  O   GLY A 197      28.020 110.021 262.824  1.00 45.24           O  
ANISOU 1540  O   GLY A 197     6929   7813   2446    174    519    -70       O  
ATOM   1541  N   PRO A 198      29.461 111.077 264.230  1.00 46.86           N  
ANISOU 1541  N   PRO A 198     7245   8067   2494    146    421   -204       N  
ATOM   1542  CA  PRO A 198      29.495 110.002 265.221  1.00 47.86           C  
ANISOU 1542  CA  PRO A 198     7442   8254   2488    158    404   -147       C  
ATOM   1543  C   PRO A 198      28.199 109.844 266.008  1.00 48.82           C  
ANISOU 1543  C   PRO A 198     7625   8384   2539    177    534   -125       C  
ATOM   1544  O   PRO A 198      27.370 110.761 266.045  1.00 49.09           O  
ANISOU 1544  O   PRO A 198     7664   8386   2603    185    635   -179       O  
ATOM   1545  CB  PRO A 198      30.629 110.432 266.168  1.00 49.00           C  
ANISOU 1545  CB  PRO A 198     7658   8448   2512    136    307   -221       C  
ATOM   1546  CG  PRO A 198      30.938 111.852 265.820  1.00 48.86           C  
ANISOU 1546  CG  PRO A 198     7621   8387   2556    106    302   -327       C  
ATOM   1547  CD  PRO A 198      30.628 111.963 264.376  1.00 47.40           C  
ANISOU 1547  CD  PRO A 198     7327   8141   2543    111    328   -294       C  
ATOM   1548  N   ASN A 199      28.056 108.664 266.616  1.00 49.60           N  
ANISOU 1548  N   ASN A 199     7771   8527   2549    186    532    -42       N  
ATOM   1549  CA  ASN A 199      27.022 108.351 267.602  1.00 50.69           C  
ANISOU 1549  CA  ASN A 199     7983   8694   2583    195    642    -12       C  
ATOM   1550  C   ASN A 199      25.669 108.975 267.300  1.00 50.09           C  
ANISOU 1550  C   ASN A 199     7866   8583   2582    208    788    -27       C  
ATOM   1551  O   ASN A 199      24.983 109.453 268.210  1.00 52.21           O  
ANISOU 1551  O   ASN A 199     8200   8874   2762    219    887    -67       O  
ATOM   1552  CB  ASN A 199      27.451 108.784 269.008  1.00 52.56           C  
ANISOU 1552  CB  ASN A 199     8342   8986   2644    191    625    -81       C  
ATOM   1553  CG  ASN A 199      28.958 108.780 269.200  1.00 55.16           C  
ANISOU 1553  CG  ASN A 199     8692   9346   2921    176    466   -114       C  
ATOM   1554  OD1 ASN A 199      29.650 107.778 268.913  1.00 54.97           O  
ANISOU 1554  OD1 ASN A 199     8642   9339   2905    182    370    -38       O  
ATOM   1555  ND2 ASN A 199      29.483 109.908 269.717  1.00 57.92           N  
ANISOU 1555  ND2 ASN A 199     9090   9703   3213    158    436   -230       N  
ATOM   1556  N   ALA A 200      25.287 108.998 266.034  1.00 47.68           N  
ANISOU 1556  N   ALA A 200     7453   8226   2436    209    803      3       N  
ATOM   1557  CA  ALA A 200      23.978 109.491 265.660  1.00 46.52           C  
ANISOU 1557  CA  ALA A 200     7252   8052   2373    226    934      3       C  
ATOM   1558  C   ALA A 200      23.657 110.852 266.234  1.00 46.79           C  
ANISOU 1558  C   ALA A 200     7330   8075   2373    248   1009   -106       C  
ATOM   1559  O   ALA A 200      22.501 111.185 266.393  1.00 47.36           O  
ANISOU 1559  O   ALA A 200     7386   8146   2462    273   1135   -107       O  
ATOM   1560  CB  ALA A 200      22.919 108.498 266.072  1.00 46.34           C  
ANISOU 1560  CB  ALA A 200     7234   8063   2308    224   1025     98       C  
ATOM   1561  N   GLU A 201      24.660 111.649 266.548  1.00 47.00           N  
ANISOU 1561  N   GLU A 201     7411   8092   2354    238    933   -200       N  
ATOM   1562  CA  GLU A 201      24.366 112.914 267.173  1.00 48.65           C  
ANISOU 1562  CA  GLU A 201     7683   8282   2520    257   1003   -309       C  
ATOM   1563  C   GLU A 201      23.966 113.986 266.155  1.00 48.21           C  
ANISOU 1563  C   GLU A 201     7552   8146   2618    276   1043   -354       C  
ATOM   1564  O   GLU A 201      23.276 114.950 266.518  1.00 49.42           O  
ANISOU 1564  O   GLU A 201     7738   8272   2766    311   1142   -425       O  
ATOM   1565  CB  GLU A 201      25.521 113.359 268.061  1.00 49.71           C  
ANISOU 1565  CB  GLU A 201     7922   8439   2526    230    910   -397       C  
ATOM   1566  CG  GLU A 201      25.221 113.198 269.539  1.00 53.47           C  
ANISOU 1566  CG  GLU A 201     8521   8979   2817    240    969   -419       C  
ATOM   1567  CD  GLU A 201      26.324 112.449 270.316  1.00 57.80           C  
ANISOU 1567  CD  GLU A 201     9142   9593   3224    208    845   -400       C  
ATOM   1568  OE1 GLU A 201      27.514 112.552 269.918  1.00 57.75           O  
ANISOU 1568  OE1 GLU A 201     9113   9581   3248    178    708   -423       O  
ATOM   1569  OE2 GLU A 201      25.987 111.755 271.329  1.00 59.26           O  
ANISOU 1569  OE2 GLU A 201     9406   9842   3267    215    886   -357       O  
ATOM   1570  N   CYS A 202      24.379 113.793 264.895  1.00 46.36           N  
ANISOU 1570  N   CYS A 202     7222   7877   2517    259    969   -311       N  
ATOM   1571  CA  CYS A 202      24.197 114.767 263.829  1.00 45.48           C  
ANISOU 1571  CA  CYS A 202     7042   7689   2551    270    982   -345       C  
ATOM   1572  C   CYS A 202      24.560 114.172 262.473  1.00 43.79           C  
ANISOU 1572  C   CYS A 202     6720   7457   2461    249    905   -269       C  
ATOM   1573  O   CYS A 202      25.119 113.065 262.419  1.00 43.33           O  
ANISOU 1573  O   CYS A 202     6651   7440   2371    226    832   -204       O  
ATOM   1574  CB  CYS A 202      25.159 115.906 264.033  1.00 46.20           C  
ANISOU 1574  CB  CYS A 202     7194   7739   2621    246    918   -456       C  
ATOM   1575  SG  CYS A 202      26.836 115.435 263.521  1.00 47.71           S  
ANISOU 1575  SG  CYS A 202     7356   7951   2820    184    741   -442       S  
ATOM   1576  N   PHE A 203      24.288 114.925 261.398  1.00 42.39           N  
ANISOU 1576  N   PHE A 203     6473   7214   2419    259    920   -278       N  
ATOM   1577  CA  PHE A 203      24.686 114.524 260.049  1.00 41.13           C  
ANISOU 1577  CA  PHE A 203     6219   7035   2375    238    848   -218       C  
ATOM   1578  C   PHE A 203      24.863 115.700 259.077  1.00 40.78           C  
ANISOU 1578  C   PHE A 203     6134   6913   2446    236    835   -262       C  
ATOM   1579  O   PHE A 203      24.565 116.865 259.406  1.00 41.51           O  
ANISOU 1579  O   PHE A 203     6272   6957   2543    256    889   -338       O  
ATOM   1580  CB  PHE A 203      23.719 113.505 259.445  1.00 40.53           C  
ANISOU 1580  CB  PHE A 203     6065   6978   2358    252    893   -113       C  
ATOM   1581  CG  PHE A 203      22.372 114.082 259.014  1.00 40.67           C  
ANISOU 1581  CG  PHE A 203     6026   6963   2464    292   1001   -100       C  
ATOM   1582  CD1 PHE A 203      22.267 114.941 257.930  1.00 40.67           C  
ANISOU 1582  CD1 PHE A 203     5966   6899   2587    303    995   -113       C  
ATOM   1583  CD2 PHE A 203      21.202 113.713 259.672  1.00 41.68           C  
ANISOU 1583  CD2 PHE A 203     6153   7129   2553    320   1107    -66       C  
ATOM   1584  CE1 PHE A 203      21.028 115.463 257.535  1.00 41.28           C  
ANISOU 1584  CE1 PHE A 203     5986   6951   2747    349   1089    -96       C  
ATOM   1585  CE2 PHE A 203      19.965 114.210 259.277  1.00 42.66           C  
ANISOU 1585  CE2 PHE A 203     6211   7235   2763    362   1205    -50       C  
ATOM   1586  CZ  PHE A 203      19.880 115.095 258.200  1.00 41.95           C  
ANISOU 1586  CZ  PHE A 203     6061   7080   2797    381   1192    -65       C  
ATOM   1587  N   PHE A 204      25.313 115.385 257.868  1.00 39.73           N  
ANISOU 1587  N   PHE A 204     5923   6766   2406    213    768   -213       N  
ATOM   1588  CA  PHE A 204      25.737 116.417 256.968  1.00 39.42           C  
ANISOU 1588  CA  PHE A 204     5856   6662   2461    198    738   -250       C  
ATOM   1589  C   PHE A 204      25.015 116.326 255.615  1.00 38.58           C  
ANISOU 1589  C   PHE A 204     5653   6523   2484    216    761   -178       C  
ATOM   1590  O   PHE A 204      24.837 115.223 255.027  1.00 37.84           O  
ANISOU 1590  O   PHE A 204     5500   6465   2415    212    740    -97       O  
ATOM   1591  CB  PHE A 204      27.270 116.381 256.795  1.00 39.16           C  
ANISOU 1591  CB  PHE A 204     5828   6644   2407    143    620   -276       C  
ATOM   1592  CG  PHE A 204      28.042 116.438 258.096  1.00 40.05           C  
ANISOU 1592  CG  PHE A 204     6030   6797   2390    121    580   -343       C  
ATOM   1593  CD1 PHE A 204      28.378 117.667 258.680  1.00 41.04           C  
ANISOU 1593  CD1 PHE A 204     6228   6880   2484    101    581   -444       C  
ATOM   1594  CD2 PHE A 204      28.440 115.267 258.752  1.00 40.09           C  
ANISOU 1594  CD2 PHE A 204     6054   6880   2300    118    535   -306       C  
ATOM   1595  CE1 PHE A 204      29.090 117.733 259.897  1.00 41.89           C  
ANISOU 1595  CE1 PHE A 204     6423   7030   2464     74    537   -510       C  
ATOM   1596  CE2 PHE A 204      29.137 115.330 259.970  1.00 41.02           C  
ANISOU 1596  CE2 PHE A 204     6256   7040   2290     99    492   -364       C  
ATOM   1597  CZ  PHE A 204      29.465 116.566 260.530  1.00 41.91           C  
ANISOU 1597  CZ  PHE A 204     6437   7118   2370     74    491   -468       C  
ATOM   1598  N   TYR A 205      24.626 117.491 255.106  1.00 38.77           N  
ANISOU 1598  N   TYR A 205     5667   6476   2589    235    799   -209       N  
ATOM   1599  CA  TYR A 205      23.882 117.522 253.874  1.00 38.15           C  
ANISOU 1599  CA  TYR A 205     5502   6367   2626    256    821   -144       C  
ATOM   1600  C   TYR A 205      24.246 118.757 253.054  1.00 38.14           C  
ANISOU 1600  C   TYR A 205     5496   6284   2709    246    800   -177       C  
ATOM   1601  O   TYR A 205      25.025 119.606 253.456  1.00 38.64           O  
ANISOU 1601  O   TYR A 205     5626   6311   2747    220    773   -253       O  
ATOM   1602  CB  TYR A 205      22.370 117.441 254.176  1.00 38.62           C  
ANISOU 1602  CB  TYR A 205     5536   6436   2701    315    928   -112       C  
ATOM   1603  CG  TYR A 205      21.861 118.675 254.867  1.00 39.71           C  
ANISOU 1603  CG  TYR A 205     5732   6522   2833    363   1008   -188       C  
ATOM   1604  CD1 TYR A 205      21.955 118.823 256.248  1.00 40.65           C  
ANISOU 1604  CD1 TYR A 205     5943   6662   2840    372   1046   -257       C  
ATOM   1605  CD2 TYR A 205      21.335 119.728 254.130  1.00 39.89           C  
ANISOU 1605  CD2 TYR A 205     5727   6470   2958    402   1041   -193       C  
ATOM   1606  CE1 TYR A 205      21.518 119.972 256.884  1.00 41.75           C  
ANISOU 1606  CE1 TYR A 205     6148   6748   2968    419   1121   -336       C  
ATOM   1607  CE2 TYR A 205      20.905 120.897 254.768  1.00 41.94           C  
ANISOU 1607  CE2 TYR A 205     6051   6669   3213    454   1114   -269       C  
ATOM   1608  CZ  TYR A 205      20.992 120.999 256.144  1.00 41.93           C  
ANISOU 1608  CZ  TYR A 205     6144   6690   3099    462   1156   -343       C  
ATOM   1609  OH  TYR A 205      20.552 122.162 256.732  1.00 43.12           O  
ANISOU 1609  OH  TYR A 205     6364   6774   3245    519   1233   -423       O  
ATOM   1610  N   ILE A 206      23.643 118.857 251.893  1.00 37.64           N  
ANISOU 1610  N   ILE A 206     5360   6193   2748    265    811   -117       N  
ATOM   1611  CA  ILE A 206      24.068 119.785 250.899  1.00 37.46           C  
ANISOU 1611  CA  ILE A 206     5324   6102   2807    247    777   -123       C  
ATOM   1612  C   ILE A 206      22.862 120.423 250.273  1.00 37.69           C  
ANISOU 1612  C   ILE A 206     5313   6080   2929    307    841    -89       C  
ATOM   1613  O   ILE A 206      22.123 119.748 249.541  1.00 37.17           O  
ANISOU 1613  O   ILE A 206     5167   6046   2911    325    849     -9       O  
ATOM   1614  CB  ILE A 206      24.811 119.014 249.811  1.00 36.43           C  
ANISOU 1614  CB  ILE A 206     5132   6006   2705    199    696    -65       C  
ATOM   1615  CG1 ILE A 206      26.244 118.739 250.281  1.00 36.37           C  
ANISOU 1615  CG1 ILE A 206     5161   6033   2624    141    621   -109       C  
ATOM   1616  CG2 ILE A 206      24.750 119.743 248.423  1.00 36.13           C  
ANISOU 1616  CG2 ILE A 206     5049   5906   2771    195    680    -29       C  
ATOM   1617  CD1 ILE A 206      27.089 117.940 249.330  1.00 35.50           C  
ANISOU 1617  CD1 ILE A 206     4992   5965   2531    102    546    -60       C  
ATOM   1618  N   THR A 207      22.663 121.715 250.535  1.00 38.55           N  
ANISOU 1618  N   THR A 207     5477   6106   3065    338    883   -147       N  
ATOM   1619  CA  THR A 207      21.618 122.459 249.816  1.00 38.86           C  
ANISOU 1619  CA  THR A 207     5477   6085   3204    402    934   -111       C  
ATOM   1620  C   THR A 207      21.979 122.912 248.403  1.00 38.36           C  
ANISOU 1620  C   THR A 207     5375   5969   3228    375    878    -64       C  
ATOM   1621  O   THR A 207      23.123 123.252 248.078  1.00 38.14           O  
ANISOU 1621  O   THR A 207     5382   5913   3197    310    814    -89       O  
ATOM   1622  CB  THR A 207      21.045 123.691 250.576  1.00 40.14           C  
ANISOU 1622  CB  THR A 207     5713   6167   3373    468   1015   -183       C  
ATOM   1623  OG1 THR A 207      22.015 124.750 250.642  1.00 40.59           O  
ANISOU 1623  OG1 THR A 207     5858   6135   3428    427    978   -256       O  
ATOM   1624  CG2 THR A 207      20.518 123.291 251.943  1.00 40.80           C  
ANISOU 1624  CG2 THR A 207     5830   6305   3366    505   1087   -226       C  
ATOM   1625  N   LYS A 208      20.936 122.908 247.581  1.00 38.27           N  
ANISOU 1625  N   LYS A 208     5290   5955   3296    427    905      9       N  
ATOM   1626  CA  LYS A 208      20.910 123.573 246.280  1.00 38.13           C  
ANISOU 1626  CA  LYS A 208     5243   5875   3369    429    873     59       C  
ATOM   1627  C   LYS A 208      20.965 125.085 246.443  1.00 40.07           C  
ANISOU 1627  C   LYS A 208     5569   6001   3655    459    902      3       C  
ATOM   1628  O   LYS A 208      21.286 125.599 247.523  1.00 40.78           O  
ANISOU 1628  O   LYS A 208     5745   6055   3693    460    932    -85       O  
ATOM   1629  CB  LYS A 208      19.659 123.153 245.511  1.00 37.97           C  
ANISOU 1629  CB  LYS A 208     5124   5891   3414    484    895    149       C  
ATOM   1630  CG  LYS A 208      19.957 122.232 244.375  1.00 37.56           C  
ANISOU 1630  CG  LYS A 208     5003   5894   3374    429    823    224       C  
ATOM   1631  CD  LYS A 208      20.069 120.780 244.734  1.00 38.02           C  
ANISOU 1631  CD  LYS A 208     5029   6051   3366    392    805    240       C  
ATOM   1632  CE  LYS A 208      20.307 120.004 243.428  1.00 40.14           C  
ANISOU 1632  CE  LYS A 208     5237   6357   3657    346    735    313       C  
ATOM   1633  NZ  LYS A 208      20.457 118.544 243.687  1.00 42.92           N  
ANISOU 1633  NZ  LYS A 208     5566   6793   3949    309    712    330       N  
ATOM   1634  N   ASP A 209      20.644 125.776 245.358  1.00 42.00           N  
ANISOU 1634  N   ASP A 209     5789   6181   3987    483    891     57       N  
ATOM   1635  CA  ASP A 209      20.882 127.206 245.213  1.00 45.07           C  
ANISOU 1635  CA  ASP A 209     6260   6441   4424    496    899     20       C  
ATOM   1636  C   ASP A 209      20.088 127.717 244.003  1.00 44.56           C  
ANISOU 1636  C   ASP A 209     6143   6328   4459    553    898    107       C  
ATOM   1637  O   ASP A 209      19.305 126.974 243.392  1.00 43.63           O  
ANISOU 1637  O   ASP A 209     5925   6283   4367    584    894    187       O  
ATOM   1638  CB  ASP A 209      22.406 127.466 245.020  1.00 46.30           C  
ANISOU 1638  CB  ASP A 209     6474   6568   4550    384    829    -17       C  
ATOM   1639  CG  ASP A 209      22.853 128.998 245.239  1.00 53.77           C  
ANISOU 1639  CG  ASP A 209     7536   7368   5525    374    839    -84       C  
ATOM   1640  OD1 ASP A 209      22.029 129.970 245.082  1.00 59.44           O  
ANISOU 1640  OD1 ASP A 209     8286   7986   6311    456    887    -77       O  
ATOM   1641  OD2 ASP A 209      24.081 129.223 245.536  1.00 58.10           O  
ANISOU 1641  OD2 ASP A 209     8144   7901   6031    278    793   -142       O  
ATOM   1642  N   ALA A 210      20.258 129.019 243.747  1.00 44.89           N  
ANISOU 1642  N   ALA A 210     6261   6243   4554    568    903     88       N  
ATOM   1643  CA  ALA A 210      19.981 129.680 242.500  1.00 44.52           C  
ANISOU 1643  CA  ALA A 210     6197   6128   4592    590    878    168       C  
ATOM   1644  C   ALA A 210      20.369 128.723 241.406  1.00 43.11           C  
ANISOU 1644  C   ALA A 210     5934   6040   4404    521    808    249       C  
ATOM   1645  O   ALA A 210      21.504 128.205 241.413  1.00 43.04           O  
ANISOU 1645  O   ALA A 210     5937   6076   4340    422    761    225       O  
ATOM   1646  CB  ALA A 210      20.836 130.954 242.403  1.00 45.28           C  
ANISOU 1646  CB  ALA A 210     6409   6085   4709    545    862    124       C  
ATOM   1647  N   SER A 211      19.431 128.458 240.490  1.00 41.54           N  
ANISOU 1647  N   SER A 211     5650   5875   4259    575    800    343       N  
ATOM   1648  CA  SER A 211      19.696 127.599 239.339  1.00 39.34           C  
ANISOU 1648  CA  SER A 211     5298   5675   3973    516    733    422       C  
ATOM   1649  C   SER A 211      20.131 126.199 239.732  1.00 38.01           C  
ANISOU 1649  C   SER A 211     5086   5627   3728    456    713    403       C  
ATOM   1650  O   SER A 211      20.765 125.492 238.927  1.00 37.17           O  
ANISOU 1650  O   SER A 211     4948   5578   3597    387    655    441       O  
ATOM   1651  CB  SER A 211      20.773 128.205 238.451  1.00 39.65           C  
ANISOU 1651  CB  SER A 211     5390   5653   4021    437    681    441       C  
ATOM   1652  OG  SER A 211      20.515 129.578 238.232  1.00 43.62           O  
ANISOU 1652  OG  SER A 211     5959   6025   4590    484    700    449       O  
ATOM   1653  N   LYS A 212      19.814 125.817 240.972  1.00 38.15           N  
ANISOU 1653  N   LYS A 212     5110   5681   3705    485    763    343       N  
ATOM   1654  CA  LYS A 212      19.889 124.434 241.430  1.00 37.35           C  
ANISOU 1654  CA  LYS A 212     4962   5693   3538    451    754    338       C  
ATOM   1655  C   LYS A 212      21.300 123.940 241.545  1.00 36.65           C  
ANISOU 1655  C   LYS A 212     4910   5634   3383    356    703    299       C  
ATOM   1656  O   LYS A 212      21.521 122.728 241.519  1.00 35.88           O  
ANISOU 1656  O   LYS A 212     4770   5625   3238    320    675    315       O  
ATOM   1657  CB  LYS A 212      19.039 123.508 240.537  1.00 36.86           C  
ANISOU 1657  CB  LYS A 212     4796   5708   3501    465    730    430       C  
ATOM   1658  CG  LYS A 212      17.683 123.161 241.133  1.00 37.33           C  
ANISOU 1658  CG  LYS A 212     4793   5813   3577    539    790    446       C  
ATOM   1659  CD  LYS A 212      16.531 123.026 240.130  1.00 37.50           C  
ANISOU 1659  CD  LYS A 212     4718   5865   3667    583    777    541       C  
ATOM   1660  CE  LYS A 212      15.261 123.562 240.806  1.00 38.58           C  
ANISOU 1660  CE  LYS A 212     4819   5991   3850    688    858    539       C  
ATOM   1661  NZ  LYS A 212      14.007 123.253 240.097  1.00 38.89           N  
ANISOU 1661  NZ  LYS A 212     4742   6086   3948    733    851    627       N  
ATOM   1662  N   ARG A 213      22.247 124.870 241.699  1.00 37.03           N  
ANISOU 1662  N   ARG A 213     5034   5606   3427    316    692    246       N  
ATOM   1663  CA  ARG A 213      23.651 124.495 241.993  1.00 36.57           C  
ANISOU 1663  CA  ARG A 213     5008   5582   3304    227    646    198       C  
ATOM   1664  C   ARG A 213      23.926 123.920 243.421  1.00 36.59           C  
ANISOU 1664  C   ARG A 213     5041   5635   3226    221    665    123       C  
ATOM   1665  O   ARG A 213      23.372 124.364 244.416  1.00 37.30           O  
ANISOU 1665  O   ARG A 213     5176   5693   3305    270    720     72       O  
ATOM   1666  CB  ARG A 213      24.573 125.673 241.748  1.00 37.09           C  
ANISOU 1666  CB  ARG A 213     5142   5558   3394    174    626    166       C  
ATOM   1667  CG  ARG A 213      26.047 125.309 241.657  1.00 36.64           C  
ANISOU 1667  CG  ARG A 213     5088   5546   3287     75    569    140       C  
ATOM   1668  CD  ARG A 213      26.837 126.513 241.282  1.00 37.27           C  
ANISOU 1668  CD  ARG A 213     5225   5535   3400     16    552    122       C  
ATOM   1669  NE  ARG A 213      27.604 127.066 242.400  1.00 37.92           N  
ANISOU 1669  NE  ARG A 213     5383   5583   3443    -30    551     26       N  
ATOM   1670  CZ  ARG A 213      27.238 128.118 243.103  1.00 38.92           C  
ANISOU 1670  CZ  ARG A 213     5594   5608   3587     -1    590    -32       C  
ATOM   1671  NH1 ARG A 213      26.086 128.711 242.877  1.00 39.40           N  
ANISOU 1671  NH1 ARG A 213     5669   5593   3707     85    639     -2       N  
ATOM   1672  NH2 ARG A 213      28.017 128.562 244.036  1.00 39.53           N  
ANISOU 1672  NH2 ARG A 213     5740   5659   3621    -56    578   -120       N  
ATOM   1673  N   ASP A 214      24.792 122.937 243.544  1.00 35.91           N  
ANISOU 1673  N   ASP A 214     4936   5628   3079    165    619    116       N  
ATOM   1674  CA  ASP A 214      25.114 122.480 244.877  1.00 36.06           C  
ANISOU 1674  CA  ASP A 214     4993   5690   3017    158    629     50       C  
ATOM   1675  C   ASP A 214      26.190 123.356 245.473  1.00 36.65           C  
ANISOU 1675  C   ASP A 214     5144   5717   3065    104    608    -31       C  
ATOM   1676  O   ASP A 214      27.379 123.202 245.190  1.00 36.36           O  
ANISOU 1676  O   ASP A 214     5101   5708   3008     32    549    -40       O  
ATOM   1677  CB  ASP A 214      25.496 121.009 244.855  1.00 35.21           C  
ANISOU 1677  CB  ASP A 214     4838   5686   2856    133    589     79       C  
ATOM   1678  CG  ASP A 214      24.321 120.129 244.520  1.00 34.83           C  
ANISOU 1678  CG  ASP A 214     4728   5681   2826    181    616    147       C  
ATOM   1679  OD1 ASP A 214      23.183 120.683 244.395  1.00 35.27           O  
ANISOU 1679  OD1 ASP A 214     4769   5697   2936    237    667    169       O  
ATOM   1680  OD2 ASP A 214      24.530 118.895 244.380  1.00 34.19           O  
ANISOU 1680  OD2 ASP A 214     4611   5671   2708    162    584    178       O  
ATOM   1681  N   ASN A 215      25.775 124.294 246.303  1.00 37.59           N  
ANISOU 1681  N   ASN A 215     5334   5764   3183    138    657    -93       N  
ATOM   1682  CA  ASN A 215      26.718 125.296 246.733  1.00 38.31           C  
ANISOU 1682  CA  ASN A 215     5506   5790   3260     80    635   -169       C  
ATOM   1683  C   ASN A 215      26.983 125.333 248.223  1.00 38.96           C  
ANISOU 1683  C   ASN A 215     5663   5887   3255     74    648   -262       C  
ATOM   1684  O   ASN A 215      27.843 126.096 248.641  1.00 39.63           O  
ANISOU 1684  O   ASN A 215     5814   5924   3318     14    619   -332       O  
ATOM   1685  CB  ASN A 215      26.260 126.662 246.275  1.00 39.09           C  
ANISOU 1685  CB  ASN A 215     5653   5762   3439    106    669   -171       C  
ATOM   1686  CG  ASN A 215      25.101 127.142 247.056  1.00 39.90           C  
ANISOU 1686  CG  ASN A 215     5801   5813   3547    200    750   -206       C  
ATOM   1687  OD1 ASN A 215      24.129 126.408 247.264  1.00 39.63           O  
ANISOU 1687  OD1 ASN A 215     5714   5839   3504    269    792   -172       O  
ATOM   1688  ND2 ASN A 215      25.183 128.371 247.527  1.00 41.01           N  
ANISOU 1688  ND2 ASN A 215     6040   5842   3701    203    774   -277       N  
ATOM   1689  N   LYS A 216      26.270 124.535 249.023  1.00 38.88           N  
ANISOU 1689  N   LYS A 216     5643   5940   3190    129    689   -264       N  
ATOM   1690  CA  LYS A 216      26.473 124.574 250.465  1.00 39.60           C  
ANISOU 1690  CA  LYS A 216     5813   6048   3187    127    705   -351       C  
ATOM   1691  C   LYS A 216      26.402 123.281 251.225  1.00 39.21           C  
ANISOU 1691  C   LYS A 216     5740   6109   3049    139    703   -339       C  
ATOM   1692  O   LYS A 216      25.526 122.454 250.994  1.00 38.70           O  
ANISOU 1692  O   LYS A 216     5614   6092   2997    188    738   -272       O  
ATOM   1693  CB  LYS A 216      25.504 125.529 251.109  1.00 40.68           C  
ANISOU 1693  CB  LYS A 216     6021   6101   3335    200    791   -403       C  
ATOM   1694  CG  LYS A 216      26.157 126.799 251.476  1.00 41.69           C  
ANISOU 1694  CG  LYS A 216     6252   6129   3460    157    777   -493       C  
ATOM   1695  CD  LYS A 216      25.217 127.757 252.141  1.00 42.89           C  
ANISOU 1695  CD  LYS A 216     6487   6190   3620    238    867   -553       C  
ATOM   1696  CE  LYS A 216      24.356 128.451 251.140  1.00 43.00           C  
ANISOU 1696  CE  LYS A 216     6470   6117   3751    303    909   -497       C  
ATOM   1697  NZ  LYS A 216      23.783 129.619 251.807  1.00 44.41           N  
ANISOU 1697  NZ  LYS A 216     6754   6183   3938    368    982   -576       N  
ATOM   1698  N   VAL A 217      27.315 123.161 252.188  1.00 39.60           N  
ANISOU 1698  N   VAL A 217     5846   6194   3005     90    660   -405       N  
ATOM   1699  CA  VAL A 217      27.403 122.038 253.121  1.00 39.48           C  
ANISOU 1699  CA  VAL A 217     5834   6278   2888     95    651   -405       C  
ATOM   1700  C   VAL A 217      27.039 122.532 254.516  1.00 40.63           C  
ANISOU 1700  C   VAL A 217     6082   6407   2949    123    706   -490       C  
ATOM   1701  O   VAL A 217      27.567 123.556 254.979  1.00 41.51           O  
ANISOU 1701  O   VAL A 217     6274   6457   3039     89    692   -577       O  
ATOM   1702  CB  VAL A 217      28.831 121.453 253.144  1.00 39.13           C  
ANISOU 1702  CB  VAL A 217     5772   6301   2793     20    548   -410       C  
ATOM   1703  CG1 VAL A 217      28.898 120.206 253.958  1.00 38.96           C  
ANISOU 1703  CG1 VAL A 217     5751   6378   2676     34    533   -391       C  
ATOM   1704  CG2 VAL A 217      29.270 121.120 251.745  1.00 38.16           C  
ANISOU 1704  CG2 VAL A 217     5558   6188   2753     -7    501   -338       C  
ATOM   1705  N   TRP A 218      26.143 121.778 255.162  1.00 40.69           N  
ANISOU 1705  N   TRP A 218     6086   6469   2905    180    768   -465       N  
ATOM   1706  CA  TRP A 218      25.603 122.074 256.485  1.00 41.80           C  
ANISOU 1706  CA  TRP A 218     6316   6610   2955    219    839   -534       C  
ATOM   1707  C   TRP A 218      25.636 120.859 257.394  1.00 41.75           C  
ANISOU 1707  C   TRP A 218     6319   6709   2836    218    834   -512       C  
ATOM   1708  O   TRP A 218      25.572 119.735 256.912  1.00 40.85           O  
ANISOU 1708  O   TRP A 218     6129   6656   2736    215    809   -426       O  
ATOM   1709  CB  TRP A 218      24.117 122.383 256.401  1.00 42.14           C  
ANISOU 1709  CB  TRP A 218     6340   6619   3054    308    955   -511       C  
ATOM   1710  CG  TRP A 218      23.657 123.433 255.486  1.00 42.25           C  
ANISOU 1710  CG  TRP A 218     6332   6532   3187    341    985   -507       C  
ATOM   1711  CD1 TRP A 218      23.548 123.356 254.124  1.00 41.35           C  
ANISOU 1711  CD1 TRP A 218     6128   6399   3185    337    955   -427       C  
ATOM   1712  CD2 TRP A 218      23.140 124.713 255.866  1.00 43.43           C  
ANISOU 1712  CD2 TRP A 218     6559   6585   3357    394   1056   -582       C  
ATOM   1713  NE1 TRP A 218      23.034 124.534 253.626  1.00 41.90           N  
ANISOU 1713  NE1 TRP A 218     6212   6364   3343    381    998   -443       N  
ATOM   1714  CE2 TRP A 218      22.760 125.379 254.672  1.00 43.18           C  
ANISOU 1714  CE2 TRP A 218     6476   6473   3456    421   1062   -537       C  
ATOM   1715  CE3 TRP A 218      22.955 125.361 257.096  1.00 44.76           C  
ANISOU 1715  CE3 TRP A 218     6840   6723   3442    425   1117   -683       C  
ATOM   1716  CZ2 TRP A 218      22.201 126.655 254.679  1.00 44.22           C  
ANISOU 1716  CZ2 TRP A 218     6666   6491   3643    482   1125   -587       C  
ATOM   1717  CZ3 TRP A 218      22.426 126.628 257.098  1.00 45.78           C  
ANISOU 1717  CZ3 TRP A 218     7030   6739   3626    484   1182   -740       C  
ATOM   1718  CH2 TRP A 218      22.043 127.259 255.904  1.00 45.51           C  
ANISOU 1718  CH2 TRP A 218     6943   6623   3728    515   1186   -690       C  
ATOM   1719  N   ARG A 219      25.637 121.127 258.703  1.00 42.85           N  
ANISOU 1719  N   ARG A 219     6558   6860   2861    226    865   -589       N  
ATOM   1720  CA  ARG A 219      25.514 120.141 259.774  1.00 43.15           C  
ANISOU 1720  CA  ARG A 219     6630   6991   2774    234    879   -577       C  
ATOM   1721  C   ARG A 219      24.061 120.145 260.252  1.00 43.75           C  
ANISOU 1721  C   ARG A 219     6712   7071   2840    313   1014   -565       C  
ATOM   1722  O   ARG A 219      23.460 121.209 260.459  1.00 44.60           O  
ANISOU 1722  O   ARG A 219     6864   7111   2971    358   1091   -627       O  
ATOM   1723  CB  ARG A 219      26.402 120.549 260.977  1.00 44.21           C  
ANISOU 1723  CB  ARG A 219     6882   7139   2778    193    832   -678       C  
ATOM   1724  CG  ARG A 219      26.805 119.414 261.914  1.00 44.36           C  
ANISOU 1724  CG  ARG A 219     6931   7263   2662    176    792   -654       C  
ATOM   1725  CD  ARG A 219      27.484 119.886 263.198  1.00 45.64           C  
ANISOU 1725  CD  ARG A 219     7217   7442   2683    144    758   -757       C  
ATOM   1726  NE  ARG A 219      28.829 120.472 263.093  1.00 45.81           N  
ANISOU 1726  NE  ARG A 219     7260   7445   2702     68    639   -820       N  
ATOM   1727  CZ  ARG A 219      29.976 119.849 263.411  1.00 45.78           C  
ANISOU 1727  CZ  ARG A 219     7254   7516   2625     14    523   -812       C  
ATOM   1728  NH1 ARG A 219      29.998 118.582 263.832  1.00 45.53           N  
ANISOU 1728  NH1 ARG A 219     7207   7577   2517     31    502   -741       N  
ATOM   1729  NH2 ARG A 219      31.125 120.508 263.304  1.00 46.09           N  
ANISOU 1729  NH2 ARG A 219     7304   7539   2671    -59    424   -874       N  
ATOM   1730  N   HIS A 220      23.484 118.973 260.464  1.00 43.45           N  
ANISOU 1730  N   HIS A 220     6631   7111   2766    330   1046   -486       N  
ATOM   1731  CA  HIS A 220      22.214 118.951 261.157  1.00 44.28           C  
ANISOU 1731  CA  HIS A 220     6750   7238   2835    394   1176   -482       C  
ATOM   1732  C   HIS A 220      22.302 118.105 262.412  1.00 44.90           C  
ANISOU 1732  C   HIS A 220     6897   7403   2759    382   1188   -480       C  
ATOM   1733  O   HIS A 220      22.706 116.932 262.332  1.00 44.23           O  
ANISOU 1733  O   HIS A 220     6783   7379   2643    345   1125   -407       O  
ATOM   1734  CB  HIS A 220      21.079 118.440 260.277  1.00 43.64           C  
ANISOU 1734  CB  HIS A 220     6550   7169   2863    431   1236   -382       C  
ATOM   1735  CG  HIS A 220      19.784 118.330 261.016  1.00 44.59           C  
ANISOU 1735  CG  HIS A 220     6668   7329   2944    492   1372   -370       C  
ATOM   1736  ND1 HIS A 220      19.007 119.427 261.317  1.00 45.63           N  
ANISOU 1736  ND1 HIS A 220     6825   7414   3098    563   1475   -433       N  
ATOM   1737  CD2 HIS A 220      19.165 117.264 261.569  1.00 44.78           C  
ANISOU 1737  CD2 HIS A 220     6673   7438   2904    492   1424   -305       C  
ATOM   1738  CE1 HIS A 220      17.947 119.037 261.996  1.00 46.41           C  
ANISOU 1738  CE1 HIS A 220     6908   7575   3150    607   1590   -407       C  
ATOM   1739  NE2 HIS A 220      18.015 117.727 262.158  1.00 45.91           N  
ANISOU 1739  NE2 HIS A 220     6818   7592   3034    559   1561   -326       N  
ATOM   1740  N   ILE A 221      21.911 118.706 263.539  1.00 46.24           N  
ANISOU 1740  N   ILE A 221     7163   7575   2832    416   1271   -559       N  
ATOM   1741  CA  ILE A 221      21.905 118.045 264.831  1.00 47.09           C  
ANISOU 1741  CA  ILE A 221     7351   7764   2778    410   1297   -565       C  
ATOM   1742  C   ILE A 221      20.510 117.530 265.188  1.00 47.59           C  
ANISOU 1742  C   ILE A 221     7376   7879   2827    463   1436   -504       C  
ATOM   1743  O   ILE A 221      19.525 118.273 265.179  1.00 48.24           O  
ANISOU 1743  O   ILE A 221     7441   7930   2959    528   1550   -533       O  
ATOM   1744  CB  ILE A 221      22.420 119.012 265.941  1.00 48.45           C  
ANISOU 1744  CB  ILE A 221     7667   7913   2828    408   1299   -698       C  
ATOM   1745  CG1 ILE A 221      23.858 119.468 265.636  1.00 48.08           C  
ANISOU 1745  CG1 ILE A 221     7651   7826   2790    340   1153   -754       C  
ATOM   1746  CG2 ILE A 221      22.216 118.423 267.386  1.00 49.61           C  
ANISOU 1746  CG2 ILE A 221     7910   8149   2790    413   1351   -707       C  
ATOM   1747  CD1 ILE A 221      24.317 120.617 266.476  1.00 49.39           C  
ANISOU 1747  CD1 ILE A 221     7950   7946   2871    329   1150   -891       C  
ATOM   1748  N   ILE A 222      20.437 116.253 265.515  1.00 47.38           N  
ANISOU 1748  N   ILE A 222     7335   7932   2734    436   1427   -418       N  
ATOM   1749  CA  ILE A 222      19.201 115.631 265.961  1.00 47.97           C  
ANISOU 1749  CA  ILE A 222     7378   8069   2779    467   1553   -352       C  
ATOM   1750  C   ILE A 222      18.604 116.351 267.175  1.00 49.64           C  
ANISOU 1750  C   ILE A 222     7682   8299   2878    519   1678   -436       C  
ATOM   1751  O   ILE A 222      19.292 116.715 268.138  1.00 50.48           O  
ANISOU 1751  O   ILE A 222     7917   8413   2852    507   1651   -521       O  
ATOM   1752  CB  ILE A 222      19.426 114.136 266.301  1.00 47.68           C  
ANISOU 1752  CB  ILE A 222     7347   8109   2662    416   1509   -253       C  
ATOM   1753  CG1 ILE A 222      20.407 113.482 265.313  1.00 46.23           C  
ANISOU 1753  CG1 ILE A 222     7112   7903   2551    366   1361   -199       C  
ATOM   1754  CG2 ILE A 222      18.110 113.385 266.325  1.00 47.96           C  
ANISOU 1754  CG2 ILE A 222     7308   8197   2719    430   1625   -158       C  
ATOM   1755  CD1 ILE A 222      19.994 113.554 263.827  1.00 45.06           C  
ANISOU 1755  CD1 ILE A 222     6832   7704   2585    371   1350   -149       C  
ATOM   1756  N   GLY A 223      17.308 116.575 267.123  1.00 50.21           N  
ANISOU 1756  N   GLY A 223     7690   8383   3004    579   1817   -415       N  
ATOM   1757  CA  GLY A 223      16.677 117.331 268.183  1.00 51.86           C  
ANISOU 1757  CA  GLY A 223     7979   8606   3119    641   1949   -500       C  
ATOM   1758  C   GLY A 223      16.471 118.773 267.785  1.00 52.23           C  
ANISOU 1758  C   GLY A 223     8030   8557   3259    708   1987   -596       C  
ATOM   1759  O   GLY A 223      15.998 119.565 268.606  1.00 53.69           O  
ANISOU 1759  O   GLY A 223     8291   8734   3374    772   2097   -684       O  
ATOM   1760  N   GLN A 224      16.782 119.118 266.527  1.00 51.03           N  
ANISOU 1760  N   GLN A 224     7798   8329   3260    699   1905   -578       N  
ATOM   1761  CA  GLN A 224      16.723 120.518 266.101  1.00 51.38           C  
ANISOU 1761  CA  GLN A 224     7860   8266   3394    756   1924   -667       C  
ATOM   1762  C   GLN A 224      15.999 120.908 264.824  1.00 50.74           C  
ANISOU 1762  C   GLN A 224     7645   8132   3501    804   1946   -613       C  
ATOM   1763  O   GLN A 224      15.926 120.133 263.868  1.00 49.48           O  
ANISOU 1763  O   GLN A 224     7371   7997   3433    767   1889   -508       O  
ATOM   1764  CB  GLN A 224      18.101 121.111 266.080  1.00 51.10           C  
ANISOU 1764  CB  GLN A 224     7924   8159   3330    698   1793   -752       C  
ATOM   1765  CG  GLN A 224      18.573 121.474 267.448  1.00 52.45           C  
ANISOU 1765  CG  GLN A 224     8257   8345   3326    690   1809   -861       C  
ATOM   1766  CD  GLN A 224      19.851 122.215 267.372  1.00 52.35           C  
ANISOU 1766  CD  GLN A 224     8333   8255   3301    633   1684   -952       C  
ATOM   1767  OE1 GLN A 224      19.900 123.394 267.702  1.00 56.18           O  
ANISOU 1767  OE1 GLN A 224     8914   8658   3774    664   1716  -1067       O  
ATOM   1768  NE2 GLN A 224      20.897 121.557 266.887  1.00 51.14           N  
ANISOU 1768  NE2 GLN A 224     8147   8124   3160    548   1541   -902       N  
ATOM   1769  N   PRO A 225      15.452 122.137 264.818  1.00 51.71           N  
ANISOU 1769  N   PRO A 225     7792   8179   3678    892   2028   -688       N  
ATOM   1770  CA  PRO A 225      14.843 122.699 263.647  1.00 51.31           C  
ANISOU 1770  CA  PRO A 225     7632   8064   3799    947   2042   -649       C  
ATOM   1771  C   PRO A 225      15.907 122.960 262.622  1.00 50.03           C  
ANISOU 1771  C   PRO A 225     7469   7821   3720    882   1894   -646       C  
ATOM   1772  O   PRO A 225      16.951 123.490 262.945  1.00 50.16           O  
ANISOU 1772  O   PRO A 225     7600   7780   3678    837   1822   -732       O  
ATOM   1773  CB  PRO A 225      14.290 124.033 264.150  1.00 52.91           C  
ANISOU 1773  CB  PRO A 225     7909   8191   4004   1054   2153   -756       C  
ATOM   1774  CG  PRO A 225      14.057 123.822 265.533  1.00 54.19           C  
ANISOU 1774  CG  PRO A 225     8160   8423   4006   1071   2247   -811       C  
ATOM   1775  CD  PRO A 225      15.234 123.010 265.979  1.00 53.46           C  
ANISOU 1775  CD  PRO A 225     8142   8377   3792    955   2130   -810       C  
ATOM   1776  N   GLN A 226      15.636 122.587 261.386  1.00 48.89           N  
ANISOU 1776  N   GLN A 226     7193   7676   3707    872   1850   -546       N  
ATOM   1777  CA  GLN A 226      16.570 122.884 260.319  1.00 47.76           C  
ANISOU 1777  CA  GLN A 226     7041   7457   3648    816   1722   -538       C  
ATOM   1778  C   GLN A 226      17.077 124.333 260.427  1.00 48.54           C  
ANISOU 1778  C   GLN A 226     7253   7431   3761    841   1713   -652       C  
ATOM   1779  O   GLN A 226      18.264 124.622 260.131  1.00 48.00           O  
ANISOU 1779  O   GLN A 226     7241   7308   3689    765   1602   -688       O  
ATOM   1780  CB  GLN A 226      15.954 122.555 258.942  1.00 46.78           C  
ANISOU 1780  CB  GLN A 226     6765   7337   3672    828   1701   -425       C  
ATOM   1781  CG  GLN A 226      16.276 123.507 257.812  1.00 46.37           C  
ANISOU 1781  CG  GLN A 226     6700   7176   3743    837   1641   -431       C  
ATOM   1782  CD  GLN A 226      16.440 122.785 256.512  1.00 44.93           C  
ANISOU 1782  CD  GLN A 226     6405   7015   3650    784   1551   -325       C  
ATOM   1783  OE1 GLN A 226      15.555 122.036 256.076  1.00 44.61           O  
ANISOU 1783  OE1 GLN A 226     6250   7043   3657    801   1580   -233       O  
ATOM   1784  NE2 GLN A 226      17.602 122.980 255.878  1.00 44.10           N  
ANISOU 1784  NE2 GLN A 226     6334   6858   3564    714   1438   -337       N  
ATOM   1785  N   SER A 227      16.188 125.222 260.888  1.00 49.93           N  
ANISOU 1785  N   SER A 227     7462   7563   3948    944   1833   -709       N  
ATOM   1786  CA  SER A 227      16.513 126.625 261.000  1.00 50.88           C  
ANISOU 1786  CA  SER A 227     7696   7550   4087    978   1839   -818       C  
ATOM   1787  C   SER A 227      17.706 126.828 261.878  1.00 51.24           C  
ANISOU 1787  C   SER A 227     7891   7576   4003    899   1774   -922       C  
ATOM   1788  O   SER A 227      18.307 127.867 261.802  1.00 51.73           O  
ANISOU 1788  O   SER A 227     8048   7524   4084    885   1735  -1004       O  
ATOM   1789  CB  SER A 227      15.335 127.433 261.500  1.00 52.49           C  
ANISOU 1789  CB  SER A 227     7919   7719   4307   1113   1990   -868       C  
ATOM   1790  OG  SER A 227      15.084 127.238 262.898  1.00 53.67           O  
ANISOU 1790  OG  SER A 227     8152   7934   4308   1138   2082   -936       O  
ATOM   1791  N   GLU A 228      18.082 125.825 262.671  1.00 51.03           N  
ANISOU 1791  N   GLU A 228     7884   7658   3847    840   1752   -913       N  
ATOM   1792  CA  GLU A 228      19.207 125.968 263.633  1.00 51.55           C  
ANISOU 1792  CA  GLU A 228     8093   7721   3771    765   1685  -1012       C  
ATOM   1793  C   GLU A 228      20.506 125.382 263.116  1.00 50.22           C  
ANISOU 1793  C   GLU A 228     7902   7577   3603    646   1527   -975       C  
ATOM   1794  O   GLU A 228      21.547 125.536 263.778  1.00 50.61           O  
ANISOU 1794  O   GLU A 228     8055   7624   3549    575   1451  -1051       O  
ATOM   1795  CB  GLU A 228      18.910 125.355 265.033  1.00 52.50           C  
ANISOU 1795  CB  GLU A 228     8280   7946   3721    778   1759  -1043       C  
ATOM   1796  CG  GLU A 228      18.099 126.206 266.029  1.00 54.38           C  
ANISOU 1796  CG  GLU A 228     8619   8152   3891    876   1903  -1145       C  
ATOM   1797  CD  GLU A 228      18.822 127.490 266.475  1.00 55.51           C  
ANISOU 1797  CD  GLU A 228     8926   8173   3992    862   1871  -1294       C  
ATOM   1798  OE1 GLU A 228      20.075 127.532 266.373  1.00 58.82           O  
ANISOU 1798  OE1 GLU A 228     9396   8569   4384    756   1734  -1324       O  
ATOM   1799  OE2 GLU A 228      18.150 128.462 266.916  1.00 56.99           O  
ANISOU 1799  OE2 GLU A 228     9191   8288   4176    956   1983  -1381       O  
ATOM   1800  N   ASP A 229      20.439 124.719 261.958  1.00 48.78           N  
ANISOU 1800  N   ASP A 229     7585   7420   3530    627   1479   -860       N  
ATOM   1801  CA  ASP A 229      21.615 124.078 261.305  1.00 47.46           C  
ANISOU 1801  CA  ASP A 229     7375   7280   3378    526   1335   -811       C  
ATOM   1802  C   ASP A 229      22.701 125.093 261.018  1.00 47.63           C  
ANISOU 1802  C   ASP A 229     7467   7204   3426    465   1247   -888       C  
ATOM   1803  O   ASP A 229      22.412 126.249 260.850  1.00 48.38           O  
ANISOU 1803  O   ASP A 229     7610   7191   3580    504   1290   -946       O  
ATOM   1804  CB  ASP A 229      21.235 123.388 259.975  1.00 46.05           C  
ANISOU 1804  CB  ASP A 229     7046   7125   3327    528   1312   -684       C  
ATOM   1805  CG  ASP A 229      20.224 122.254 260.143  1.00 45.80           C  
ANISOU 1805  CG  ASP A 229     6932   7193   3278    567   1383   -594       C  
ATOM   1806  OD1 ASP A 229      20.162 121.621 261.222  1.00 46.32           O  
ANISOU 1806  OD1 ASP A 229     7046   7336   3218    561   1415   -606       O  
ATOM   1807  OD2 ASP A 229      19.466 122.003 259.186  1.00 45.17           O  
ANISOU 1807  OD2 ASP A 229     6739   7115   3309    598   1407   -508       O  
ATOM   1808  N   VAL A 230      23.943 124.645 260.956  1.00 47.01           N  
ANISOU 1808  N   VAL A 230     7391   7163   3306    370   1125   -886       N  
ATOM   1809  CA  VAL A 230      25.091 125.500 260.739  1.00 47.22           C  
ANISOU 1809  CA  VAL A 230     7476   7117   3349    292   1032   -955       C  
ATOM   1810  C   VAL A 230      25.614 125.148 259.355  1.00 45.81           C  
ANISOU 1810  C   VAL A 230     7182   6939   3286    245    950   -865       C  
ATOM   1811  O   VAL A 230      25.890 123.968 259.054  1.00 44.76           O  
ANISOU 1811  O   VAL A 230     6966   6901   3142    220    900   -783       O  
ATOM   1812  CB  VAL A 230      26.171 125.248 261.823  1.00 47.80           C  
ANISOU 1812  CB  VAL A 230     7637   7251   3275    216    952  -1025       C  
ATOM   1813  CG1 VAL A 230      27.333 126.191 261.685  1.00 48.25           C  
ANISOU 1813  CG1 VAL A 230     7754   7235   3345    126    857  -1104       C  
ATOM   1814  CG2 VAL A 230      25.593 125.391 263.160  1.00 49.12           C  
ANISOU 1814  CG2 VAL A 230     7912   7437   3315    265   1036  -1100       C  
ATOM   1815  N   CYS A 231      25.713 126.171 258.502  1.00 45.87           N  
ANISOU 1815  N   CYS A 231     7189   6836   3402    236    941   -878       N  
ATOM   1816  CA  CYS A 231      26.331 126.038 257.183  1.00 44.74           C  
ANISOU 1816  CA  CYS A 231     6954   6683   3361    182    863   -805       C  
ATOM   1817  C   CYS A 231      27.838 126.092 257.334  1.00 44.77           C  
ANISOU 1817  C   CYS A 231     6986   6708   3318     69    745   -849       C  
ATOM   1818  O   CYS A 231      28.373 127.049 257.897  1.00 45.86           O  
ANISOU 1818  O   CYS A 231     7226   6779   3419     24    725   -948       O  
ATOM   1819  CB  CYS A 231      25.916 127.176 256.275  1.00 44.98           C  
ANISOU 1819  CB  CYS A 231     6987   6586   3517    210    896   -802       C  
ATOM   1820  SG  CYS A 231      27.000 127.261 254.820  1.00 43.96           S  
ANISOU 1820  SG  CYS A 231     6780   6436   3487    115    788   -740       S  
ATOM   1821  N   LEU A 232      28.524 125.074 256.827  1.00 43.69           N  
ANISOU 1821  N   LEU A 232     6757   6663   3181     24    669   -778       N  
ATOM   1822  CA  LEU A 232      29.949 124.925 257.099  1.00 43.79           C  
ANISOU 1822  CA  LEU A 232     6778   6725   3135    -74    557   -813       C  
ATOM   1823  C   LEU A 232      30.790 125.526 256.022  1.00 43.49           C  
ANISOU 1823  C   LEU A 232     6697   6637   3192   -148    493   -799       C  
ATOM   1824  O   LEU A 232      31.914 125.971 256.277  1.00 44.07           O  
ANISOU 1824  O   LEU A 232     6802   6709   3234   -239    414   -857       O  
ATOM   1825  CB  LEU A 232      30.331 123.454 257.257  1.00 42.97           C  
ANISOU 1825  CB  LEU A 232     6605   6754   2969    -77    506   -747       C  
ATOM   1826  CG  LEU A 232      29.882 122.790 258.561  1.00 43.50           C  
ANISOU 1826  CG  LEU A 232     6731   6889   2906    -34    542   -769       C  
ATOM   1827  CD1 LEU A 232      29.891 121.266 258.425  1.00 42.52           C  
ANISOU 1827  CD1 LEU A 232     6528   6874   2756    -13    516   -673       C  
ATOM   1828  CD2 LEU A 232      30.713 123.226 259.777  1.00 44.72           C  
ANISOU 1828  CD2 LEU A 232     6991   7061   2940    -90    487   -873       C  
ATOM   1829  N   TYR A 233      30.225 125.542 254.817  1.00 42.68           N  
ANISOU 1829  N   TYR A 233     6521   6496   3201   -113    527   -720       N  
ATOM   1830  CA  TYR A 233      30.971 125.830 253.595  1.00 42.16           C  
ANISOU 1830  CA  TYR A 233     6389   6405   3225   -178    471   -677       C  
ATOM   1831  C   TYR A 233      30.057 126.303 252.496  1.00 41.79           C  
ANISOU 1831  C   TYR A 233     6310   6274   3293   -124    532   -616       C  
ATOM   1832  O   TYR A 233      29.128 125.582 252.152  1.00 41.07           O  
ANISOU 1832  O   TYR A 233     6160   6219   3225    -49    579   -546       O  
ATOM   1833  CB  TYR A 233      31.600 124.531 253.117  1.00 41.06           C  
ANISOU 1833  CB  TYR A 233     6143   6386   3072   -197    408   -602       C  
ATOM   1834  CG  TYR A 233      32.590 124.735 252.014  1.00 40.67           C  
ANISOU 1834  CG  TYR A 233     6026   6337   3091   -274    344   -567       C  
ATOM   1835  CD1 TYR A 233      33.815 125.365 252.268  1.00 41.42           C  
ANISOU 1835  CD1 TYR A 233     6145   6427   3165   -375    273   -629       C  
ATOM   1836  CD2 TYR A 233      32.321 124.301 250.722  1.00 39.66           C  
ANISOU 1836  CD2 TYR A 233     5808   6218   3044   -251    354   -474       C  
ATOM   1837  CE1 TYR A 233      34.736 125.559 251.269  1.00 41.18           C  
ANISOU 1837  CE1 TYR A 233     6045   6404   3196   -449    221   -594       C  
ATOM   1838  CE2 TYR A 233      33.241 124.485 249.700  1.00 39.39           C  
ANISOU 1838  CE2 TYR A 233     5712   6189   3064   -321    303   -441       C  
ATOM   1839  CZ  TYR A 233      34.447 125.117 249.979  1.00 40.15           C  
ANISOU 1839  CZ  TYR A 233     5829   6285   3142   -419    240   -500       C  
ATOM   1840  OH  TYR A 233      35.372 125.304 248.977  1.00 40.63           O  
ANISOU 1840  OH  TYR A 233     5822   6359   3256   -493    196   -465       O  
ATOM   1841  N   THR A 234      30.284 127.496 251.947  1.00 42.35           N  
ANISOU 1841  N   THR A 234     6420   6234   3435   -164    529   -638       N  
ATOM   1842  CA  THR A 234      29.630 127.884 250.666  1.00 41.91           C  
ANISOU 1842  CA  THR A 234     6320   6110   3495   -125    565   -560       C  
ATOM   1843  C   THR A 234      30.738 128.020 249.659  1.00 41.54           C  
ANISOU 1843  C   THR A 234     6221   6069   3495   -222    492   -523       C  
ATOM   1844  O   THR A 234      31.853 128.231 250.030  1.00 41.98           O  
ANISOU 1844  O   THR A 234     6298   6142   3511   -314    431   -575       O  
ATOM   1845  CB  THR A 234      28.860 129.222 250.730  1.00 42.98           C  
ANISOU 1845  CB  THR A 234     6548   6096   3686    -78    631   -602       C  
ATOM   1846  OG1 THR A 234      28.126 129.311 251.952  1.00 43.74           O  
ANISOU 1846  OG1 THR A 234     6720   6183   3717     -7    695   -672       O  
ATOM   1847  CG2 THR A 234      27.880 129.320 249.640  1.00 42.52           C  
ANISOU 1847  CG2 THR A 234     6433   5996   3726     -3    677   -512       C  
ATOM   1848  N   ASP A 235      30.456 127.804 248.394  1.00 40.75           N  
ANISOU 1848  N   ASP A 235     6043   5969   3471   -204    497   -430       N  
ATOM   1849  CA  ASP A 235      31.342 128.223 247.324  1.00 40.65           C  
ANISOU 1849  CA  ASP A 235     5995   5934   3514   -290    449   -392       C  
ATOM   1850  C   ASP A 235      30.450 129.122 246.519  1.00 40.93           C  
ANISOU 1850  C   ASP A 235     6059   5851   3642   -240    500   -349       C  
ATOM   1851  O   ASP A 235      29.334 128.770 246.202  1.00 40.49           O  
ANISOU 1851  O   ASP A 235     5970   5799   3616   -146    548   -296       O  
ATOM   1852  CB  ASP A 235      31.778 127.045 246.468  1.00 39.46           C  
ANISOU 1852  CB  ASP A 235     5728   5902   3363   -303    409   -311       C  
ATOM   1853  CG  ASP A 235      33.004 127.349 245.617  1.00 40.72           C  
ANISOU 1853  CG  ASP A 235     5847   6071   3552   -408    353   -290       C  
ATOM   1854  OD1 ASP A 235      33.359 128.546 245.377  1.00 44.09           O  
ANISOU 1854  OD1 ASP A 235     6330   6398   4023   -472    350   -313       O  
ATOM   1855  OD2 ASP A 235      33.631 126.355 245.176  1.00 42.54           O  
ANISOU 1855  OD2 ASP A 235     5989   6413   3762   -427    314   -248       O  
ATOM   1856  N   ASP A 236      30.903 130.323 246.242  1.00 41.82           N  
ANISOU 1856  N   ASP A 236     6237   5852   3799   -303    490   -374       N  
ATOM   1857  CA  ASP A 236      30.029 131.256 245.578  1.00 42.29           C  
ANISOU 1857  CA  ASP A 236     6339   5784   3944   -246    539   -336       C  
ATOM   1858  C   ASP A 236      30.271 131.271 244.072  1.00 41.75           C  
ANISOU 1858  C   ASP A 236     6204   5717   3942   -281    515   -233       C  
ATOM   1859  O   ASP A 236      29.474 131.832 243.297  1.00 41.94           O  
ANISOU 1859  O   ASP A 236     6240   5657   4038   -224    548   -173       O  
ATOM   1860  CB  ASP A 236      30.151 132.637 246.239  1.00 43.80           C  
ANISOU 1860  CB  ASP A 236     6667   5827   4147   -275    555   -425       C  
ATOM   1861  CG  ASP A 236      29.071 132.863 247.300  1.00 48.32           C  
ANISOU 1861  CG  ASP A 236     7313   6352   4695   -164    625   -490       C  
ATOM   1862  OD1 ASP A 236      27.914 132.379 247.096  1.00 51.96           O  
ANISOU 1862  OD1 ASP A 236     7722   6843   5179    -48    678   -436       O  
ATOM   1863  OD2 ASP A 236      29.376 133.506 248.338  1.00 53.88           O  
ANISOU 1863  OD2 ASP A 236     8124   6994   5353   -194    628   -597       O  
ATOM   1864  N   ASP A 237      31.365 130.617 243.680  1.00 41.13           N  
ANISOU 1864  N   ASP A 237     6053   5741   3835   -369    458   -212       N  
ATOM   1865  CA  ASP A 237      31.770 130.537 242.294  1.00 40.66           C  
ANISOU 1865  CA  ASP A 237     5928   5702   3820   -414    435   -121       C  
ATOM   1866  C   ASP A 237      30.888 129.587 241.463  1.00 39.58           C  
ANISOU 1866  C   ASP A 237     5706   5635   3699   -326    453    -30       C  
ATOM   1867  O   ASP A 237      30.969 128.351 241.587  1.00 38.67           O  
ANISOU 1867  O   ASP A 237     5517   5642   3535   -307    437    -19       O  
ATOM   1868  CB  ASP A 237      33.246 130.177 242.218  1.00 40.54           C  
ANISOU 1868  CB  ASP A 237     5860   5777   3766   -532    375   -137       C  
ATOM   1869  CG  ASP A 237      33.795 130.244 240.820  1.00 40.30           C  
ANISOU 1869  CG  ASP A 237     5772   5764   3777   -592    359    -52       C  
ATOM   1870  OD1 ASP A 237      33.006 130.328 239.864  1.00 40.01           O  
ANISOU 1870  OD1 ASP A 237     5725   5690   3787   -535    386     27       O  
ATOM   1871  OD2 ASP A 237      35.030 130.187 240.699  1.00 40.47           O  
ANISOU 1871  OD2 ASP A 237     5754   5845   3780   -696    317    -63       O  
ATOM   1872  N   PRO A 238      30.039 130.195 240.604  1.00 39.80           N  
ANISOU 1872  N   PRO A 238     5749   5577   3794   -274    482     36       N  
ATOM   1873  CA  PRO A 238      29.066 129.564 239.676  1.00 39.05           C  
ANISOU 1873  CA  PRO A 238     5586   5523   3727   -194    497    129       C  
ATOM   1874  C   PRO A 238      29.664 128.430 238.826  1.00 38.01           C  
ANISOU 1874  C   PRO A 238     5358   5520   3565   -234    457    186       C  
ATOM   1875  O   PRO A 238      28.946 127.525 238.388  1.00 37.26           O  
ANISOU 1875  O   PRO A 238     5200   5491   3464   -173    461    239       O  
ATOM   1876  CB  PRO A 238      28.619 130.731 238.780  1.00 39.80           C  
ANISOU 1876  CB  PRO A 238     5730   5492   3900   -179    512    188       C  
ATOM   1877  CG  PRO A 238      29.539 131.868 239.100  1.00 40.83           C  
ANISOU 1877  CG  PRO A 238     5949   5522   4042   -271    502    132       C  
ATOM   1878  CD  PRO A 238      30.008 131.663 240.482  1.00 40.99           C  
ANISOU 1878  CD  PRO A 238     5999   5572   4003   -297    499     24       C  
ATOM   1879  N   LEU A 239      30.980 128.461 238.642  1.00 38.07           N  
ANISOU 1879  N   LEU A 239     5353   5562   3549   -337    421    170       N  
ATOM   1880  CA  LEU A 239      31.648 127.325 238.056  1.00 37.20           C  
ANISOU 1880  CA  LEU A 239     5155   5581   3399   -368    389    204       C  
ATOM   1881  C   LEU A 239      31.749 126.103 238.969  1.00 36.54           C  
ANISOU 1881  C   LEU A 239     5031   5603   3250   -338    376    158       C  
ATOM   1882  O   LEU A 239      32.223 125.089 238.513  1.00 35.86           O  
ANISOU 1882  O   LEU A 239     4876   5617   3131   -348    352    185       O  
ATOM   1883  CB  LEU A 239      33.030 127.704 237.535  1.00 37.56           C  
ANISOU 1883  CB  LEU A 239     5185   5645   3442   -482    360    206       C  
ATOM   1884  CG  LEU A 239      33.155 128.759 236.432  1.00 38.19           C  
ANISOU 1884  CG  LEU A 239     5296   5639   3577   -533    368    268       C  
ATOM   1885  CD1 LEU A 239      34.622 129.068 236.263  1.00 38.68           C  
ANISOU 1885  CD1 LEU A 239     5337   5733   3625   -658    342    251       C  
ATOM   1886  CD2 LEU A 239      32.477 128.364 235.105  1.00 37.65           C  
ANISOU 1886  CD2 LEU A 239     5188   5593   3526   -483    376    368       C  
ATOM   1887  N   PHE A 240      31.315 126.151 240.231  1.00 36.80           N  
ANISOU 1887  N   PHE A 240     5109   5614   3259   -298    394     92       N  
ATOM   1888  CA  PHE A 240      31.634 125.038 241.121  1.00 36.32           C  
ANISOU 1888  CA  PHE A 240     5018   5655   3128   -287    374     51       C  
ATOM   1889  C   PHE A 240      30.457 124.383 241.816  1.00 36.00           C  
ANISOU 1889  C   PHE A 240     4982   5631   3067   -194    409     47       C  
ATOM   1890  O   PHE A 240      29.442 125.007 242.089  1.00 36.43           O  
ANISOU 1890  O   PHE A 240     5079   5608   3153   -138    454     42       O  
ATOM   1891  CB  PHE A 240      32.622 125.478 242.194  1.00 37.01           C  
ANISOU 1891  CB  PHE A 240     5147   5741   3175   -354    348    -37       C  
ATOM   1892  CG  PHE A 240      34.009 125.753 241.702  1.00 37.28           C  
ANISOU 1892  CG  PHE A 240     5150   5806   3211   -458    303    -39       C  
ATOM   1893  CD1 PHE A 240      34.292 126.891 240.932  1.00 37.91           C  
ANISOU 1893  CD1 PHE A 240     5256   5800   3348   -520    309    -17       C  
ATOM   1894  CD2 PHE A 240      35.052 124.924 242.075  1.00 37.07           C  
ANISOU 1894  CD2 PHE A 240     5067   5891   3128   -495    257    -63       C  
ATOM   1895  CE1 PHE A 240      35.579 127.168 240.522  1.00 38.29           C  
ANISOU 1895  CE1 PHE A 240     5269   5881   3397   -626    273    -17       C  
ATOM   1896  CE2 PHE A 240      36.351 125.194 241.681  1.00 37.47           C  
ANISOU 1896  CE2 PHE A 240     5075   5980   3181   -591    218    -67       C  
ATOM   1897  CZ  PHE A 240      36.610 126.314 240.898  1.00 38.07           C  
ANISOU 1897  CZ  PHE A 240     5173   5977   3315   -661    229    -44       C  
ATOM   1898  N   SER A 241      30.626 123.118 242.164  1.00 35.36           N  
ANISOU 1898  N   SER A 241     4856   5649   2930   -178    389     48       N  
ATOM   1899  CA  SER A 241      29.707 122.501 243.064  1.00 35.23           C  
ANISOU 1899  CA  SER A 241     4852   5654   2880   -109    421     34       C  
ATOM   1900  C   SER A 241      30.430 122.027 244.292  1.00 35.40           C  
ANISOU 1900  C   SER A 241     4896   5732   2822   -131    396    -32       C  
ATOM   1901  O   SER A 241      31.600 121.677 244.211  1.00 35.28           O  
ANISOU 1901  O   SER A 241     4853   5775   2777   -185    344    -44       O  
ATOM   1902  CB  SER A 241      29.102 121.327 242.369  1.00 34.39           C  
ANISOU 1902  CB  SER A 241     4681   5610   2776    -68    420    104       C  
ATOM   1903  OG  SER A 241      28.226 121.826 241.400  1.00 34.39           O  
ANISOU 1903  OG  SER A 241     4667   5556   2844    -38    445    162       O  
ATOM   1904  N   VAL A 242      29.745 121.993 245.430  1.00 35.75           N  
ANISOU 1904  N   VAL A 242     4987   5768   2829    -85    432    -73       N  
ATOM   1905  CA  VAL A 242      30.344 121.454 246.660  1.00 35.96           C  
ANISOU 1905  CA  VAL A 242     5042   5856   2767   -100    407   -130       C  
ATOM   1906  C   VAL A 242      30.001 119.951 246.845  1.00 35.27           C  
ANISOU 1906  C   VAL A 242     4913   5856   2634    -57    403    -87       C  
ATOM   1907  O   VAL A 242      28.904 119.493 246.491  1.00 34.89           O  
ANISOU 1907  O   VAL A 242     4840   5805   2613     -5    444    -34       O  
ATOM   1908  CB  VAL A 242      30.011 122.334 247.951  1.00 36.97           C  
ANISOU 1908  CB  VAL A 242     5263   5925   2858    -87    444   -214       C  
ATOM   1909  CG1 VAL A 242      30.182 123.847 247.693  1.00 37.74           C  
ANISOU 1909  CG1 VAL A 242     5414   5914   3013   -123    454   -253       C  
ATOM   1910  CG2 VAL A 242      28.616 122.096 248.443  1.00 37.03           C  
ANISOU 1910  CG2 VAL A 242     5287   5923   2861     -4    517   -201       C  
ATOM   1911  N   GLY A 243      30.958 119.188 247.376  1.00 35.20           N  
ANISOU 1911  N   GLY A 243     4896   5922   2557    -82    350   -106       N  
ATOM   1912  CA  GLY A 243      30.755 117.780 247.731  1.00 34.74           C  
ANISOU 1912  CA  GLY A 243     4818   5936   2444    -45    341    -72       C  
ATOM   1913  C   GLY A 243      31.020 117.555 249.218  1.00 35.44           C  
ANISOU 1913  C   GLY A 243     4965   6061   2439    -43    331   -127       C  
ATOM   1914  O   GLY A 243      31.531 118.464 249.915  1.00 36.65           O  
ANISOU 1914  O   GLY A 243     5169   6192   2565    -78    319   -197       O  
ATOM   1915  N   VAL A 244      30.681 116.358 249.723  1.00 35.09           N  
ANISOU 1915  N   VAL A 244     4922   6071   2339     -6    333    -95       N  
ATOM   1916  CA  VAL A 244      30.956 116.013 251.123  1.00 35.69           C  
ANISOU 1916  CA  VAL A 244     5056   6190   2313     -1    319   -136       C  
ATOM   1917  C   VAL A 244      30.994 114.513 251.400  1.00 35.35           C  
ANISOU 1917  C   VAL A 244     5003   6214   2215     28    294    -85       C  
ATOM   1918  O   VAL A 244      30.115 113.746 251.007  1.00 34.87           O  
ANISOU 1918  O   VAL A 244     4922   6151   2177     60    331    -24       O  
ATOM   1919  CB  VAL A 244      30.012 116.763 252.088  1.00 36.41           C  
ANISOU 1919  CB  VAL A 244     5220   6238   2376     22    391   -183       C  
ATOM   1920  CG1 VAL A 244      28.607 116.200 252.041  1.00 36.15           C  
ANISOU 1920  CG1 VAL A 244     5176   6199   2360     76    467   -127       C  
ATOM   1921  CG2 VAL A 244      30.546 116.747 253.501  1.00 37.23           C  
ANISOU 1921  CG2 VAL A 244     5396   6380   2369      9    366   -244       C  
ATOM   1922  N   GLY A 245      32.035 114.098 252.106  1.00 36.00           N  
ANISOU 1922  N   GLY A 245     5102   6354   2222     14    228   -109       N  
ATOM   1923  CA  GLY A 245      32.234 112.679 252.456  1.00 36.16           C  
ANISOU 1923  CA  GLY A 245     5123   6433   2182     45    195    -62       C  
ATOM   1924  C   GLY A 245      32.923 112.388 253.782  1.00 36.33           C  
ANISOU 1924  C   GLY A 245     5200   6511   2093     43    146    -95       C  
ATOM   1925  O   GLY A 245      33.497 113.274 254.408  1.00 37.01           O  
ANISOU 1925  O   GLY A 245     5316   6603   2144      9    120   -164       O  
ATOM   1926  N   ARG A 246      32.879 111.122 254.169  1.00 36.29           N  
ANISOU 1926  N   ARG A 246     5211   6546   2033     79    128    -44       N  
ATOM   1927  CA  ARG A 246      33.404 110.652 255.436  1.00 37.97           C  
ANISOU 1927  CA  ARG A 246     5482   6814   2131     88     81    -58       C  
ATOM   1928  C   ARG A 246      34.685 109.851 255.254  1.00 37.69           C  
ANISOU 1928  C   ARG A 246     5404   6838   2077    101    -16    -36       C  
ATOM   1929  O   ARG A 246      34.773 109.040 254.326  1.00 36.81           O  
ANISOU 1929  O   ARG A 246     5243   6723   2019    127    -27     19       O  
ATOM   1930  CB  ARG A 246      32.361 109.766 256.106  1.00 38.63           C  
ANISOU 1930  CB  ARG A 246     5625   6896   2158    123    137     -7       C  
ATOM   1931  CG  ARG A 246      32.423 109.869 257.597  1.00 43.10           C  
ANISOU 1931  CG  ARG A 246     6278   7499   2600    122    132    -43       C  
ATOM   1932  CD  ARG A 246      31.535 108.838 258.288  1.00 48.73           C  
ANISOU 1932  CD  ARG A 246     7049   8220   3245    153    180     20       C  
ATOM   1933  NE  ARG A 246      31.435 109.160 259.715  1.00 51.29           N  
ANISOU 1933  NE  ARG A 246     7465   8576   3448    149    195    -22       N  
ATOM   1934  CZ  ARG A 246      31.205 108.273 260.676  1.00 54.49           C  
ANISOU 1934  CZ  ARG A 246     7940   9016   3748    168    200     21       C  
ATOM   1935  NH1 ARG A 246      31.073 106.976 260.397  1.00 55.38           N  
ANISOU 1935  NH1 ARG A 246     8046   9131   3866    193    186    109       N  
ATOM   1936  NH2 ARG A 246      31.114 108.690 261.927  1.00 56.07           N  
ANISOU 1936  NH2 ARG A 246     8225   9246   3833    162    217    -25       N  
ATOM   1937  N   SER A 247      35.666 110.051 256.147  1.00 38.15           N  
ANISOU 1937  N   SER A 247     5484   6954   2057     86    -89    -79       N  
ATOM   1938  CA  SER A 247      36.938 109.313 256.049  1.00 38.09           C  
ANISOU 1938  CA  SER A 247     5427   7016   2031    106   -186    -58       C  
ATOM   1939  C   SER A 247      36.749 107.860 256.442  1.00 38.31           C  
ANISOU 1939  C   SER A 247     5494   7062   2002    168   -200     15       C  
ATOM   1940  O   SER A 247      35.791 107.514 257.158  1.00 39.27           O  
ANISOU 1940  O   SER A 247     5693   7160   2067    182   -148     38       O  
ATOM   1941  CB  SER A 247      38.016 109.948 256.912  1.00 39.09           C  
ANISOU 1941  CB  SER A 247     5558   7204   2089     68   -267   -121       C  
ATOM   1942  OG  SER A 247      37.647 110.001 258.279  1.00 39.90           O  
ANISOU 1942  OG  SER A 247     5761   7321   2079     68   -263   -145       O  
ATOM   1943  N   GLY A 248      37.658 107.005 256.002  1.00 38.24           N  
ANISOU 1943  N   GLY A 248     5432   7093   2005    208   -269     52       N  
ATOM   1944  CA  GLY A 248      37.529 105.586 256.285  1.00 39.53           C  
ANISOU 1944  CA  GLY A 248     5637   7260   2122    271   -286    125       C  
ATOM   1945  C   GLY A 248      37.280 105.316 257.750  1.00 41.13           C  
ANISOU 1945  C   GLY A 248     5938   7487   2201    280   -297    131       C  
ATOM   1946  O   GLY A 248      36.300 104.675 258.123  1.00 41.68           O  
ANISOU 1946  O   GLY A 248     6080   7519   2236    296   -242    179       O  
ATOM   1947  N   ASP A 249      38.163 105.835 258.590  1.00 42.63           N  
ANISOU 1947  N   ASP A 249     6133   7743   2320    262   -369     83       N  
ATOM   1948  CA  ASP A 249      38.022 105.693 260.019  1.00 44.31           C  
ANISOU 1948  CA  ASP A 249     6445   7990   2403    264   -387     81       C  
ATOM   1949  C   ASP A 249      36.880 106.544 260.607  1.00 44.41           C  
ANISOU 1949  C   ASP A 249     6532   7962   2382    219   -292     38       C  
ATOM   1950  O   ASP A 249      36.542 106.428 261.797  1.00 45.48           O  
ANISOU 1950  O   ASP A 249     6761   8118   2401    221   -283     38       O  
ATOM   1951  CB  ASP A 249      39.363 105.992 260.707  1.00 45.79           C  
ANISOU 1951  CB  ASP A 249     6610   8267   2521    256   -504     40       C  
ATOM   1952  CG  ASP A 249      39.749 107.470 260.657  1.00 48.07           C  
ANISOU 1952  CG  ASP A 249     6861   8568   2836    178   -512    -57       C  
ATOM   1953  OD1 ASP A 249      39.118 108.268 259.891  1.00 49.17           O  
ANISOU 1953  OD1 ASP A 249     6976   8643   3065    139   -433    -88       O  
ATOM   1954  OD2 ASP A 249      40.714 107.818 261.391  1.00 50.35           O  
ANISOU 1954  OD2 ASP A 249     7145   8932   3055    154   -605    -98       O  
ATOM   1955  N   GLY A 250      36.299 107.408 259.787  1.00 43.30           N  
ANISOU 1955  N   GLY A 250     6350   7764   2337    184   -220      3       N  
ATOM   1956  CA  GLY A 250      35.103 108.131 260.201  1.00 44.06           C  
ANISOU 1956  CA  GLY A 250     6507   7814   2419    158   -118    -30       C  
ATOM   1957  C   GLY A 250      35.326 109.273 261.182  1.00 44.81           C  
ANISOU 1957  C   GLY A 250     6658   7931   2437    115   -127   -121       C  
ATOM   1958  O   GLY A 250      34.377 109.888 261.648  1.00 44.62           O  
ANISOU 1958  O   GLY A 250     6694   7871   2387    103    -41   -155       O  
ATOM   1959  N   LYS A 251      36.589 109.561 261.458  1.00 45.83           N  
ANISOU 1959  N   LYS A 251     6765   8118   2532     92   -233   -163       N  
ATOM   1960  CA  LYS A 251      37.000 110.634 262.343  1.00 47.45           C  
ANISOU 1960  CA  LYS A 251     7020   8347   2662     41   -264   -256       C  
ATOM   1961  C   LYS A 251      37.224 111.982 261.621  1.00 47.13           C  
ANISOU 1961  C   LYS A 251     6929   8259   2717    -20   -253   -332       C  
ATOM   1962  O   LYS A 251      37.416 113.030 262.258  1.00 48.26           O  
ANISOU 1962  O   LYS A 251     7124   8398   2813    -72   -264   -419       O  
ATOM   1963  CB  LYS A 251      38.268 110.180 263.069  1.00 48.76           C  
ANISOU 1963  CB  LYS A 251     7185   8609   2734     42   -396   -255       C  
ATOM   1964  CG  LYS A 251      37.998 109.348 264.366  1.00 52.66           C  
ANISOU 1964  CG  LYS A 251     7785   9146   3075     81   -408   -217       C  
ATOM   1965  CD  LYS A 251      37.841 107.834 264.120  1.00 55.31           C  
ANISOU 1965  CD  LYS A 251     8111   9489   3416    153   -412   -103       C  
ATOM   1966  CE  LYS A 251      39.201 107.101 264.122  1.00 56.99           C  
ANISOU 1966  CE  LYS A 251     8266   9779   3608    185   -548    -67       C  
ATOM   1967  NZ  LYS A 251      40.063 107.340 265.340  1.00 58.39           N  
ANISOU 1967  NZ  LYS A 251     8490  10044   3649    166   -653   -108       N  
ATOM   1968  N   THR A 252      37.176 111.945 260.290  1.00 45.71           N  
ANISOU 1968  N   THR A 252     6658   8042   2669    -15   -229   -297       N  
ATOM   1969  CA  THR A 252      37.516 113.084 259.449  1.00 45.03           C  
ANISOU 1969  CA  THR A 252     6513   7914   2681    -72   -227   -350       C  
ATOM   1970  C   THR A 252      36.410 113.260 258.424  1.00 43.40           C  
ANISOU 1970  C   THR A 252     6283   7622   2583    -53   -123   -318       C  
ATOM   1971  O   THR A 252      35.952 112.282 257.827  1.00 43.20           O  
ANISOU 1971  O   THR A 252     6225   7593   2596     -4    -95   -241       O  
ATOM   1972  CB  THR A 252      38.872 112.851 258.678  1.00 45.14           C  
ANISOU 1972  CB  THR A 252     6413   7986   2751    -90   -325   -333       C  
ATOM   1973  OG1 THR A 252      39.863 112.269 259.553  1.00 46.24           O  
ANISOU 1973  OG1 THR A 252     6556   8221   2792    -82   -430   -332       O  
ATOM   1974  CG2 THR A 252      39.401 114.155 258.032  1.00 44.37           C  
ANISOU 1974  CG2 THR A 252     6268   7858   2734   -169   -335   -396       C  
ATOM   1975  N   LEU A 253      35.993 114.510 258.216  1.00 42.54           N  
ANISOU 1975  N   LEU A 253     6195   7445   2524    -92    -70   -378       N  
ATOM   1976  CA  LEU A 253      35.007 114.852 257.187  1.00 40.24           C  
ANISOU 1976  CA  LEU A 253     5875   7073   2342    -76     20   -351       C  
ATOM   1977  C   LEU A 253      35.670 115.634 256.072  1.00 39.51           C  
ANISOU 1977  C   LEU A 253     5707   6951   2353   -126     -7   -367       C  
ATOM   1978  O   LEU A 253      36.566 116.439 256.302  1.00 39.90           O  
ANISOU 1978  O   LEU A 253     5759   7010   2392   -188    -64   -430       O  
ATOM   1979  CB  LEU A 253      33.875 115.685 257.781  1.00 40.50           C  
ANISOU 1979  CB  LEU A 253     5991   7039   2356    -68    114   -399       C  
ATOM   1980  CG  LEU A 253      32.553 115.827 257.033  1.00 39.33           C  
ANISOU 1980  CG  LEU A 253     5825   6821   2296    -29    219   -359       C  
ATOM   1981  CD1 LEU A 253      31.737 114.571 257.178  1.00 38.91           C  
ANISOU 1981  CD1 LEU A 253     5770   6799   2215     25    260   -280       C  
ATOM   1982  CD2 LEU A 253      31.775 117.026 257.560  1.00 40.04           C  
ANISOU 1982  CD2 LEU A 253     5991   6843   2381    -28    296   -430       C  
ATOM   1983  N   ILE A 254      35.195 115.393 254.855  1.00 38.49           N  
ANISOU 1983  N   ILE A 254     5516   6786   2322   -104     34   -308       N  
ATOM   1984  CA  ILE A 254      35.864 115.872 253.639  1.00 37.86           C  
ANISOU 1984  CA  ILE A 254     5355   6692   2337   -145      8   -301       C  
ATOM   1985  C   ILE A 254      34.931 116.769 252.824  1.00 37.48           C  
ANISOU 1985  C   ILE A 254     5311   6549   2382   -148     87   -299       C  
ATOM   1986  O   ILE A 254      33.920 116.324 252.302  1.00 36.82           O  
ANISOU 1986  O   ILE A 254     5216   6437   2338   -100    147   -244       O  
ATOM   1987  CB  ILE A 254      36.504 114.685 252.828  1.00 37.19           C  
ANISOU 1987  CB  ILE A 254     5182   6671   2276   -117    -39   -231       C  
ATOM   1988  CG1 ILE A 254      37.532 113.968 253.737  1.00 37.81           C  
ANISOU 1988  CG1 ILE A 254     5261   6842   2263   -111   -126   -240       C  
ATOM   1989  CG2 ILE A 254      37.154 115.183 251.550  1.00 36.84           C  
ANISOU 1989  CG2 ILE A 254     5056   6618   2325   -158    -54   -222       C  
ATOM   1990  CD1 ILE A 254      37.912 112.542 253.321  1.00 37.58           C  
ANISOU 1990  CD1 ILE A 254     5178   6870   2230    -53   -162   -170       C  
ATOM   1991  N   ILE A 255      35.273 118.045 252.753  1.00 38.03           N  
ANISOU 1991  N   ILE A 255     5398   6568   2483   -207     83   -358       N  
ATOM   1992  CA  ILE A 255      34.470 118.991 252.020  1.00 37.85           C  
ANISOU 1992  CA  ILE A 255     5387   6448   2547   -208    151   -356       C  
ATOM   1993  C   ILE A 255      35.243 119.373 250.779  1.00 37.54           C  
ANISOU 1993  C   ILE A 255     5273   6402   2589   -260    119   -332       C  
ATOM   1994  O   ILE A 255      36.434 119.660 250.880  1.00 38.03           O  
ANISOU 1994  O   ILE A 255     5310   6503   2637   -325     52   -366       O  
ATOM   1995  CB  ILE A 255      34.234 120.201 252.877  1.00 38.85           C  
ANISOU 1995  CB  ILE A 255     5607   6507   2647   -235    177   -441       C  
ATOM   1996  CG1 ILE A 255      33.181 119.843 253.916  1.00 39.10           C  
ANISOU 1996  CG1 ILE A 255     5710   6538   2608   -169    238   -453       C  
ATOM   1997  CG2 ILE A 255      33.825 121.384 252.029  1.00 38.90           C  
ANISOU 1997  CG2 ILE A 255     5622   6408   2752   -254    222   -447       C  
ATOM   1998  CD1 ILE A 255      32.776 120.974 254.710  1.00 40.10           C  
ANISOU 1998  CD1 ILE A 255     5934   6592   2708   -177    280   -536       C  
ATOM   1999  N   CYS A 256      34.617 119.381 249.603  1.00 36.82           N  
ANISOU 1999  N   CYS A 256     5141   6269   2581   -236    163   -273       N  
ATOM   2000  CA  CYS A 256      35.362 119.808 248.445  1.00 36.65           C  
ANISOU 2000  CA  CYS A 256     5057   6241   2628   -289    137   -251       C  
ATOM   2001  C   CYS A 256      34.583 120.708 247.506  1.00 36.50           C  
ANISOU 2001  C   CYS A 256     5048   6125   2697   -289    194   -226       C  
ATOM   2002  O   CYS A 256      33.407 120.902 247.666  1.00 36.44           O  
ANISOU 2002  O   CYS A 256     5083   6060   2704   -236    254   -219       O  
ATOM   2003  CB  CYS A 256      35.830 118.574 247.728  1.00 35.91           C  
ANISOU 2003  CB  CYS A 256     4879   6231   2535   -265    106   -188       C  
ATOM   2004  SG  CYS A 256      34.500 117.748 246.921  1.00 34.93           S  
ANISOU 2004  SG  CYS A 256     4739   6083   2448   -187    165   -110       S  
ATOM   2005  N   SER A 257      35.269 121.247 246.513  1.00 36.52           N  
ANISOU 2005  N   SER A 257     5007   6114   2756   -347    175   -207       N  
ATOM   2006  CA  SER A 257      34.690 122.054 245.442  1.00 36.41           C  
ANISOU 2006  CA  SER A 257     4995   6014   2824   -351    218   -169       C  
ATOM   2007  C   SER A 257      35.219 121.478 244.157  1.00 35.78           C  
ANISOU 2007  C   SER A 257     4828   5989   2777   -364    198   -102       C  
ATOM   2008  O   SER A 257      36.384 121.089 244.091  1.00 35.86           O  
ANISOU 2008  O   SER A 257     4784   6078   2763   -407    149   -109       O  
ATOM   2009  CB  SER A 257      35.154 123.514 245.544  1.00 37.37           C  
ANISOU 2009  CB  SER A 257     5169   6052   2978   -429    213   -220       C  
ATOM   2010  OG  SER A 257      34.224 124.309 246.259  1.00 37.92           O  
ANISOU 2010  OG  SER A 257     5332   6027   3051   -396    260   -265       O  
ATOM   2011  N   MET A 258      34.383 121.409 243.134  1.00 35.23           N  
ANISOU 2011  N   MET A 258     4744   5885   2759   -326    236    -38       N  
ATOM   2012  CA  MET A 258      34.747 120.734 241.915  1.00 34.63           C  
ANISOU 2012  CA  MET A 258     4594   5863   2701   -327    223     25       C  
ATOM   2013  C   MET A 258      34.170 121.555 240.816  1.00 34.64           C  
ANISOU 2013  C   MET A 258     4604   5788   2771   -335    256     72       C  
ATOM   2014  O   MET A 258      32.953 121.667 240.630  1.00 34.44           O  
ANISOU 2014  O   MET A 258     4605   5708   2774   -280    294    102       O  
ATOM   2015  CB  MET A 258      34.121 119.326 241.814  1.00 33.83           C  
ANISOU 2015  CB  MET A 258     4465   5817   2571   -253    228     65       C  
ATOM   2016  CG  MET A 258      34.479 118.297 242.917  1.00 39.21           C  
ANISOU 2016  CG  MET A 258     5147   6571   3180   -225    198     33       C  
ATOM   2017  SD  MET A 258      33.087 117.453 243.828  1.00 50.41           S  
ANISOU 2017  SD  MET A 258     6611   7982   4562   -144    233     41       S  
ATOM   2018  CE  MET A 258      31.600 118.503 243.674  1.00 45.65           C  
ANISOU 2018  CE  MET A 258     6051   7275   4019   -118    301     52       C  
ATOM   2019  N   SER A 259      35.053 122.180 240.082  1.00 34.99           N  
ANISOU 2019  N   SER A 259     4625   5829   2842   -407    242     83       N  
ATOM   2020  CA  SER A 259      34.661 122.643 238.790  1.00 34.90           C  
ANISOU 2020  CA  SER A 259     4606   5771   2882   -412    266    149       C  
ATOM   2021  C   SER A 259      35.309 121.639 237.893  1.00 34.37           C  
ANISOU 2021  C   SER A 259     4464   5803   2793   -414    247    190       C  
ATOM   2022  O   SER A 259      35.899 120.637 238.343  1.00 34.10           O  
ANISOU 2022  O   SER A 259     4390   5857   2711   -399    220    168       O  
ATOM   2023  CB  SER A 259      35.114 124.068 238.499  1.00 35.75           C  
ANISOU 2023  CB  SER A 259     4751   5798   3036   -491    271    142       C  
ATOM   2024  OG  SER A 259      36.408 124.078 237.984  1.00 36.01           O  
ANISOU 2024  OG  SER A 259     4728   5893   3060   -571    246    148       O  
ATOM   2025  N   SER A 260      35.149 121.902 236.609  1.00 34.29           N  
ANISOU 2025  N   SER A 260     4439   5775   2816   -426    263    253       N  
ATOM   2026  CA  SER A 260      35.402 120.904 235.610  1.00 33.76           C  
ANISOU 2026  CA  SER A 260     4314   5787   2726   -408    257    299       C  
ATOM   2027  C   SER A 260      36.900 120.730 235.528  1.00 34.09           C  
ANISOU 2027  C   SER A 260     4297   5912   2743   -467    235    277       C  
ATOM   2028  O   SER A 260      37.378 119.612 235.352  1.00 33.72           O  
ANISOU 2028  O   SER A 260     4200   5955   2658   -437    221    279       O  
ATOM   2029  CB  SER A 260      34.794 121.327 234.295  1.00 33.73           C  
ANISOU 2029  CB  SER A 260     4320   5740   2756   -407    279    370       C  
ATOM   2030  OG  SER A 260      35.149 120.414 233.305  1.00 33.35           O  
ANISOU 2030  OG  SER A 260     4223   5770   2678   -397    274    407       O  
ATOM   2031  N   GLU A 261      37.638 121.816 235.751  1.00 34.87           N  
ANISOU 2031  N   GLU A 261     4403   5982   2864   -550    231    253       N  
ATOM   2032  CA  GLU A 261      39.085 121.735 235.685  1.00 35.34           C  
ANISOU 2032  CA  GLU A 261     4393   6128   2905   -616    210    234       C  
ATOM   2033  C   GLU A 261      39.889 122.177 236.894  1.00 36.01           C  
ANISOU 2033  C   GLU A 261     4477   6226   2980   -672    176    164       C  
ATOM   2034  O   GLU A 261      41.051 122.504 236.738  1.00 36.67           O  
ANISOU 2034  O   GLU A 261     4504   6363   3065   -752    160    155       O  
ATOM   2035  CB  GLU A 261      39.611 122.385 234.405  1.00 35.79           C  
ANISOU 2035  CB  GLU A 261     4423   6185   2988   -685    234    288       C  
ATOM   2036  CG  GLU A 261      39.108 123.770 234.048  1.00 38.15           C  
ANISOU 2036  CG  GLU A 261     4793   6363   3340   -738    257    315       C  
ATOM   2037  CD  GLU A 261      39.276 124.039 232.549  1.00 41.94           C  
ANISOU 2037  CD  GLU A 261     5254   6849   3832   -772    286    392       C  
ATOM   2038  OE1 GLU A 261      39.171 123.061 231.770  1.00 43.75           O  
ANISOU 2038  OE1 GLU A 261     5443   7151   4029   -719    294    427       O  
ATOM   2039  OE2 GLU A 261      39.521 125.201 232.144  1.00 44.32           O  
ANISOU 2039  OE2 GLU A 261     5587   7084   4170   -854    300    418       O  
ATOM   2040  N   THR A 262      39.286 122.102 238.087  1.00 35.90           N  
ANISOU 2040  N   THR A 262     4518   6174   2948   -631    163    115       N  
ATOM   2041  CA  THR A 262      39.815 122.687 239.334  1.00 36.64           C  
ANISOU 2041  CA  THR A 262     4638   6256   3026   -685    129     42       C  
ATOM   2042  C   THR A 262      39.135 122.138 240.568  1.00 36.34           C  
ANISOU 2042  C   THR A 262     4649   6212   2945   -613    119     -2       C  
ATOM   2043  O   THR A 262      37.922 121.999 240.595  1.00 35.83           O  
ANISOU 2043  O   THR A 262     4636   6089   2890   -543    152     15       O  
ATOM   2044  CB  THR A 262      39.594 124.195 239.380  1.00 37.41           C  
ANISOU 2044  CB  THR A 262     4811   6232   3172   -757    146     26       C  
ATOM   2045  OG1 THR A 262      39.684 124.757 238.044  1.00 37.55           O  
ANISOU 2045  OG1 THR A 262     4812   6217   3236   -800    176     91       O  
ATOM   2046  CG2 THR A 262      40.591 124.847 240.313  1.00 38.42           C  
ANISOU 2046  CG2 THR A 262     4943   6370   3285   -850    103    -45       C  
ATOM   2047  N   SER A 263      39.931 121.874 241.607  1.00 36.77           N  
ANISOU 2047  N   SER A 263     4686   6331   2953   -635     71    -58       N  
ATOM   2048  CA  SER A 263      39.462 121.266 242.864  1.00 36.61           C  
ANISOU 2048  CA  SER A 263     4710   6324   2876   -572     55   -100       C  
ATOM   2049  C   SER A 263      39.930 122.012 244.079  1.00 37.56           C  
ANISOU 2049  C   SER A 263     4877   6427   2966   -633     19   -179       C  
ATOM   2050  O   SER A 263      40.890 122.759 244.012  1.00 38.35           O  
ANISOU 2050  O   SER A 263     4953   6536   3082   -729    -11   -203       O  
ATOM   2051  CB  SER A 263      39.962 119.831 242.992  1.00 36.17           C  
ANISOU 2051  CB  SER A 263     4586   6385   2771   -515     21    -84       C  
ATOM   2052  OG  SER A 263      39.369 119.008 242.006  1.00 35.65           O  
ANISOU 2052  OG  SER A 263     4496   6326   2722   -448     54    -20       O  
ATOM   2053  N   GLU A 264      39.244 121.793 245.195  1.00 37.55           N  
ANISOU 2053  N   GLU A 264     4946   6404   2917   -581     22   -218       N  
ATOM   2054  CA  GLU A 264      39.680 122.255 246.494  1.00 38.45           C  
ANISOU 2054  CA  GLU A 264     5112   6521   2979   -626    -20   -298       C  
ATOM   2055  C   GLU A 264      39.016 121.375 247.555  1.00 38.17           C  
ANISOU 2055  C   GLU A 264     5120   6512   2869   -540    -17   -314       C  
ATOM   2056  O   GLU A 264      37.861 120.981 247.405  1.00 37.49           O  
ANISOU 2056  O   GLU A 264     5065   6387   2793   -462     38   -279       O  
ATOM   2057  CB  GLU A 264      39.323 123.724 246.701  1.00 39.23           C  
ANISOU 2057  CB  GLU A 264     5301   6494   3112   -685      7   -346       C  
ATOM   2058  CG  GLU A 264      40.079 124.363 247.858  1.00 40.41           C  
ANISOU 2058  CG  GLU A 264     5496   6647   3210   -764    -49   -435       C  
ATOM   2059  CD  GLU A 264      39.818 125.848 248.008  1.00 41.56           C  
ANISOU 2059  CD  GLU A 264     5742   6658   3393   -830    -25   -487       C  
ATOM   2060  OE1 GLU A 264      38.825 126.203 248.693  1.00 42.46           O  
ANISOU 2060  OE1 GLU A 264     5957   6687   3487   -777     19   -527       O  
ATOM   2061  OE2 GLU A 264      40.628 126.654 247.478  1.00 41.98           O  
ANISOU 2061  OE2 GLU A 264     5771   6687   3492   -935    -49   -491       O  
ATOM   2062  N   SER A 265      39.756 121.083 248.625  1.00 38.77           N  
ANISOU 2062  N   SER A 265     5199   6661   2872   -560    -79   -362       N  
ATOM   2063  CA  SER A 265      39.272 120.251 249.706  1.00 38.67           C  
ANISOU 2063  CA  SER A 265     5233   6683   2778   -489    -84   -376       C  
ATOM   2064  C   SER A 265      39.501 120.940 251.013  1.00 39.76           C  
ANISOU 2064  C   SER A 265     5451   6806   2848   -536   -116   -462       C  
ATOM   2065  O   SER A 265      40.351 121.796 251.117  1.00 40.61           O  
ANISOU 2065  O   SER A 265     5555   6909   2964   -629   -161   -510       O  
ATOM   2066  CB  SER A 265      40.017 118.917 249.732  1.00 38.37           C  
ANISOU 2066  CB  SER A 265     5115   6767   2698   -450   -139   -338       C  
ATOM   2067  OG  SER A 265      39.435 117.977 248.831  1.00 37.33           O  
ANISOU 2067  OG  SER A 265     4944   6641   2600   -376    -99   -262       O  
ATOM   2068  N   HIS A 266      38.725 120.548 252.014  1.00 39.80           N  
ANISOU 2068  N   HIS A 266     5533   6806   2783   -474    -93   -482       N  
ATOM   2069  CA  HIS A 266      38.967 120.895 253.391  1.00 40.84           C  
ANISOU 2069  CA  HIS A 266     5745   6951   2823   -503   -130   -562       C  
ATOM   2070  C   HIS A 266      38.663 119.686 254.219  1.00 40.63           C  
ANISOU 2070  C   HIS A 266     5736   6996   2706   -426   -139   -538       C  
ATOM   2071  O   HIS A 266      37.959 118.778 253.776  1.00 39.70           O  
ANISOU 2071  O   HIS A 266     5593   6886   2607   -349    -94   -469       O  
ATOM   2072  CB  HIS A 266      38.046 122.013 253.820  1.00 41.37           C  
ANISOU 2072  CB  HIS A 266     5925   6898   2895   -508    -63   -621       C  
ATOM   2073  CG  HIS A 266      38.043 123.170 252.874  1.00 42.25           C  
ANISOU 2073  CG  HIS A 266     6034   6911   3108   -565    -35   -627       C  
ATOM   2074  ND1 HIS A 266      38.685 124.361 253.154  1.00 43.92           N  
ANISOU 2074  ND1 HIS A 266     6293   7069   3324   -664    -70   -702       N  
ATOM   2075  CD2 HIS A 266      37.489 123.312 251.644  1.00 41.48           C  
ANISOU 2075  CD2 HIS A 266     5896   6756   3107   -539     20   -563       C  
ATOM   2076  CE1 HIS A 266      38.500 125.197 252.146  1.00 45.08           C  
ANISOU 2076  CE1 HIS A 266     6435   7124   3569   -695    -31   -681       C  
ATOM   2077  NE2 HIS A 266      37.794 124.579 251.211  1.00 44.21           N  
ANISOU 2077  NE2 HIS A 266     6269   7014   3514   -619     22   -595       N  
ATOM   2078  N   LEU A 267      39.175 119.731 255.445  1.00 41.61           N  
ANISOU 2078  N   LEU A 267     5912   7168   2729   -452   -197   -598       N  
ATOM   2079  CA  LEU A 267      38.983 118.722 256.441  1.00 41.72           C  
ANISOU 2079  CA  LEU A 267     5963   7250   2639   -391   -215   -585       C  
ATOM   2080  C   LEU A 267      38.336 119.294 257.694  1.00 42.61           C  
ANISOU 2080  C   LEU A 267     6207   7320   2662   -391   -181   -660       C  
ATOM   2081  O   LEU A 267      38.655 120.412 258.117  1.00 43.71           O  
ANISOU 2081  O   LEU A 267     6403   7417   2786   -462   -200   -744       O  
ATOM   2082  CB  LEU A 267      40.334 118.168 256.828  1.00 42.28           C  
ANISOU 2082  CB  LEU A 267     5972   7437   2653   -421   -330   -586       C  
ATOM   2083  CG  LEU A 267      41.162 117.503 255.732  1.00 41.64           C  
ANISOU 2083  CG  LEU A 267     5757   7420   2644   -414   -372   -519       C  
ATOM   2084  CD1 LEU A 267      42.422 116.912 256.391  1.00 42.44           C  
ANISOU 2084  CD1 LEU A 267     5807   7647   2672   -427   -488   -524       C  
ATOM   2085  CD2 LEU A 267      40.345 116.446 254.918  1.00 40.36           C  
ANISOU 2085  CD2 LEU A 267     5564   7244   2529   -321   -306   -429       C  
ATOM   2086  N   LEU A 268      37.448 118.502 258.304  1.00 42.39           N  
ANISOU 2086  N   LEU A 268     6230   7306   2569   -313   -131   -629       N  
ATOM   2087  CA  LEU A 268      36.887 118.778 259.624  1.00 43.32           C  
ANISOU 2087  CA  LEU A 268     6470   7412   2576   -300   -100   -691       C  
ATOM   2088  C   LEU A 268      37.040 117.584 260.578  1.00 43.75           C  
ANISOU 2088  C   LEU A 268     6549   7565   2510   -256   -142   -656       C  
ATOM   2089  O   LEU A 268      36.720 116.437 260.236  1.00 42.76           O  
ANISOU 2089  O   LEU A 268     6378   7473   2396   -194   -126   -568       O  
ATOM   2090  CB  LEU A 268      35.417 119.103 259.469  1.00 42.96           C  
ANISOU 2090  CB  LEU A 268     6475   7277   2570   -243     29   -684       C  
ATOM   2091  CG  LEU A 268      34.685 119.697 260.667  1.00 44.00           C  
ANISOU 2091  CG  LEU A 268     6738   7374   2609   -228     90   -760       C  
ATOM   2092  CD1 LEU A 268      35.004 121.183 260.847  1.00 45.89           C  
ANISOU 2092  CD1 LEU A 268     7043   7532   2860   -296     82   -867       C  
ATOM   2093  CD2 LEU A 268      33.203 119.486 260.507  1.00 43.50           C  
ANISOU 2093  CD2 LEU A 268     6689   7263   2577   -147    217   -718       C  
ATOM   2094  N   ASP A 269      37.507 117.869 261.791  1.00 45.77           N  
ANISOU 2094  N   ASP A 269     6885   7861   2643   -290   -197   -726       N  
ATOM   2095  CA  ASP A 269      37.689 116.832 262.814  1.00 46.82           C  
ANISOU 2095  CA  ASP A 269     7057   8086   2645   -253   -243   -696       C  
ATOM   2096  C   ASP A 269      36.394 116.478 263.515  1.00 46.79           C  
ANISOU 2096  C   ASP A 269     7147   8059   2571   -188   -138   -680       C  
ATOM   2097  O   ASP A 269      35.820 117.310 264.227  1.00 48.38           O  
ANISOU 2097  O   ASP A 269     7450   8216   2718   -198    -79   -757       O  
ATOM   2098  CB  ASP A 269      38.709 117.259 263.874  1.00 48.38           C  
ANISOU 2098  CB  ASP A 269     7307   8347   2727   -317   -351   -776       C  
ATOM   2099  CG  ASP A 269      39.081 116.115 264.824  1.00 50.80           C  
ANISOU 2099  CG  ASP A 269     7639   8761   2903   -277   -421   -731       C  
ATOM   2100  OD1 ASP A 269      38.542 114.984 264.639  1.00 50.30           O  
ANISOU 2100  OD1 ASP A 269     7556   8713   2842   -201   -381   -637       O  
ATOM   2101  OD2 ASP A 269      39.921 116.348 265.747  1.00 52.93           O  
ANISOU 2101  OD2 ASP A 269     7950   9096   3064   -325   -521   -787       O  
ATOM   2102  N   LEU A 270      35.964 115.230 263.356  1.00 45.64           N  
ANISOU 2102  N   LEU A 270     6971   7948   2423   -123   -114   -582       N  
ATOM   2103  CA  LEU A 270      34.742 114.767 263.993  1.00 45.12           C  
ANISOU 2103  CA  LEU A 270     6981   7871   2292    -67    -12   -553       C  
ATOM   2104  C   LEU A 270      34.989 114.264 265.446  1.00 46.88           C  
ANISOU 2104  C   LEU A 270     7303   8172   2338    -60    -56   -564       C  
ATOM   2105  O   LEU A 270      34.063 113.912 266.196  1.00 47.23           O  
ANISOU 2105  O   LEU A 270     7426   8221   2299    -22     26   -545       O  
ATOM   2106  CB  LEU A 270      34.047 113.737 263.088  1.00 43.51           C  
ANISOU 2106  CB  LEU A 270     6705   7653   2175    -13     42   -443       C  
ATOM   2107  CG  LEU A 270      33.579 114.116 261.654  1.00 42.36           C  
ANISOU 2107  CG  LEU A 270     6469   7432   2193    -10     97   -420       C  
ATOM   2108  CD1 LEU A 270      33.087 112.898 260.910  1.00 41.34           C  
ANISOU 2108  CD1 LEU A 270     6279   7308   2121     36    122   -312       C  
ATOM   2109  CD2 LEU A 270      32.497 115.191 261.600  1.00 42.49           C  
ANISOU 2109  CD2 LEU A 270     6525   7367   2254     -6    209   -471       C  
ATOM   2110  N   ARG A 271      36.243 114.279 265.864  1.00 48.05           N  
ANISOU 2110  N   ARG A 271     7446   8387   2424   -100   -184   -594       N  
ATOM   2111  CA  ARG A 271      36.577 113.829 267.208  1.00 50.36           C  
ANISOU 2111  CA  ARG A 271     7831   8759   2544    -96   -242   -602       C  
ATOM   2112  C   ARG A 271      36.311 114.922 268.263  1.00 52.37           C  
ANISOU 2112  C   ARG A 271     8212   8996   2691   -134   -210   -718       C  
ATOM   2113  O   ARG A 271      36.354 114.661 269.476  1.00 53.32           O  
ANISOU 2113  O   ARG A 271     8433   9175   2651   -130   -234   -734       O  
ATOM   2114  CB  ARG A 271      38.026 113.336 267.240  1.00 50.56           C  
ANISOU 2114  CB  ARG A 271     7793   8874   2544   -116   -400   -582       C  
ATOM   2115  CG  ARG A 271      38.317 112.289 266.138  1.00 50.79           C  
ANISOU 2115  CG  ARG A 271     7700   8914   2685    -70   -426   -475       C  
ATOM   2116  CD  ARG A 271      39.790 112.111 265.819  1.00 51.49           C  
ANISOU 2116  CD  ARG A 271     7689   9077   2798    -92   -568   -470       C  
ATOM   2117  NE  ARG A 271      40.465 113.395 265.788  1.00 53.92           N  
ANISOU 2117  NE  ARG A 271     7979   9379   3127   -180   -616   -572       N  
ATOM   2118  CZ  ARG A 271      41.781 113.548 265.750  1.00 56.74           C  
ANISOU 2118  CZ  ARG A 271     8261   9811   3486   -225   -744   -594       C  
ATOM   2119  NH1 ARG A 271      42.587 112.496 265.715  1.00 57.95           N  
ANISOU 2119  NH1 ARG A 271     8343  10051   3623   -178   -836   -521       N  
ATOM   2120  NH2 ARG A 271      42.297 114.763 265.740  1.00 58.63           N  
ANISOU 2120  NH2 ARG A 271     8495  10037   3747   -317   -779   -689       N  
ATOM   2121  N   LYS A 272      36.008 116.134 267.786  1.00 53.20           N  
ANISOU 2121  N   LYS A 272     8319   9014   2882   -169   -153   -797       N  
ATOM   2122  CA  LYS A 272      35.820 117.314 268.649  1.00 55.00           C  
ANISOU 2122  CA  LYS A 272     8667   9204   3025   -208   -124   -921       C  
ATOM   2123  C   LYS A 272      34.350 117.744 268.816  1.00 55.38           C  
ANISOU 2123  C   LYS A 272     8788   9176   3079   -157     43   -943       C  
ATOM   2124  O   LYS A 272      34.055 118.749 269.480  1.00 55.79           O  
ANISOU 2124  O   LYS A 272     8946   9182   3068   -175     88  -1050       O  
ATOM   2125  CB  LYS A 272      36.714 118.475 268.185  1.00 55.09           C  
ANISOU 2125  CB  LYS A 272     8649   9172   3109   -294   -198  -1009       C  
ATOM   2126  CG  LYS A 272      38.173 118.073 268.160  1.00 55.67           C  
ANISOU 2126  CG  LYS A 272     8648   9340   3164   -346   -362   -992       C  
ATOM   2127  CD  LYS A 272      39.149 119.231 268.046  1.00 58.49           C  
ANISOU 2127  CD  LYS A 272     8997   9676   3551   -451   -450  -1091       C  
ATOM   2128  CE  LYS A 272      40.557 118.731 268.426  1.00 61.00           C  
ANISOU 2128  CE  LYS A 272     9258  10118   3801   -498   -618  -1078       C  
ATOM   2129  NZ  LYS A 272      41.687 119.487 267.798  1.00 61.33           N  
ANISOU 2129  NZ  LYS A 272     9210  10162   3931   -598   -715  -1122       N  
ATOM   2130  N   GLY A 273      33.440 116.973 268.217  1.00 54.67           N  
ANISOU 2130  N   GLY A 273     8638   9073   3063    -92    132   -844       N  
ATOM   2131  CA  GLY A 273      32.019 117.114 268.521  1.00 55.68           C  
ANISOU 2131  CA  GLY A 273     8823   9159   3176    -34    288   -845       C  
ATOM   2132  C   GLY A 273      31.295 118.232 267.793  1.00 55.86           C  
ANISOU 2132  C   GLY A 273     8828   9071   3326    -24    384   -897       C  
ATOM   2133  O   GLY A 273      31.920 119.037 267.070  1.00 56.14           O  
ANISOU 2133  O   GLY A 273     8824   9051   3458    -70    330   -942       O  
ATOM   2134  N   VAL A 274      29.980 118.288 268.005  1.00 55.80           N  
ANISOU 2134  N   VAL A 274     8851   9035   3316     39    528   -887       N  
ATOM   2135  CA  VAL A 274      29.085 119.061 267.146  1.00 55.41           C  
ANISOU 2135  CA  VAL A 274     8757   8889   3407     74    630   -898       C  
ATOM   2136  C   VAL A 274      29.312 120.561 267.107  1.00 56.68           C  
ANISOU 2136  C   VAL A 274     8978   8954   3602     46    633  -1019       C  
ATOM   2137  O   VAL A 274      29.022 121.195 266.091  1.00 55.85           O  
ANISOU 2137  O   VAL A 274     8813   8764   3641     55    664  -1016       O  
ATOM   2138  CB  VAL A 274      27.602 118.796 267.435  1.00 55.61           C  
ANISOU 2138  CB  VAL A 274     8793   8916   3421    151    786   -860       C  
ATOM   2139  CG1 VAL A 274      27.211 117.410 266.945  1.00 54.41           C  
ANISOU 2139  CG1 VAL A 274     8545   8821   3307    173    794   -722       C  
ATOM   2140  CG2 VAL A 274      27.285 118.984 268.903  1.00 56.03           C  
ANISOU 2140  CG2 VAL A 274     8983   9006   3298    168    846   -931       C  
ATOM   2141  N   LYS A 275      29.820 121.142 268.189  1.00 58.64           N  
ANISOU 2141  N   LYS A 275     9351   9212   3718     10    597  -1125       N  
ATOM   2142  CA  LYS A 275      30.085 122.585 268.154  1.00 59.86           C  
ANISOU 2142  CA  LYS A 275     9575   9264   3906    -26    592  -1246       C  
ATOM   2143  C   LYS A 275      31.452 123.013 267.550  1.00 59.71           C  
ANISOU 2143  C   LYS A 275     9514   9226   3949   -125    447  -1273       C  
ATOM   2144  O   LYS A 275      31.768 124.199 267.545  1.00 61.54           O  
ANISOU 2144  O   LYS A 275     9810   9370   4204   -171    431  -1373       O  
ATOM   2145  CB  LYS A 275      29.810 123.241 269.513  1.00 61.44           C  
ANISOU 2145  CB  LYS A 275     9941   9455   3950    -16    645  -1366       C  
ATOM   2146  CG  LYS A 275      28.304 123.372 269.811  1.00 62.34           C  
ANISOU 2146  CG  LYS A 275    10090   9540   4057     87    824  -1366       C  
ATOM   2147  CD  LYS A 275      27.947 124.672 270.545  1.00 64.08           C  
ANISOU 2147  CD  LYS A 275    10459   9672   4217    106    899  -1512       C  
ATOM   2148  CE  LYS A 275      28.508 124.706 271.976  1.00 65.24           C  
ANISOU 2148  CE  LYS A 275    10755   9882   4153     64    851  -1606       C  
ATOM   2149  NZ  LYS A 275      28.942 126.081 272.320  1.00 64.38           N  
ANISOU 2149  NZ  LYS A 275    10775   9669   4019     18    825  -1759       N  
ATOM   2150  N   HIS A 276      32.243 122.072 267.030  1.00 57.78           N  
ANISOU 2150  N   HIS A 276     9161   9059   3733   -156    345  -1185       N  
ATOM   2151  CA  HIS A 276      33.524 122.414 266.453  1.00 56.55           C  
ANISOU 2151  CA  HIS A 276     8949   8901   3636   -246    215  -1202       C  
ATOM   2152  C   HIS A 276      33.311 122.533 264.970  1.00 54.93           C  
ANISOU 2152  C   HIS A 276     8626   8632   3614   -235    243  -1134       C  
ATOM   2153  O   HIS A 276      32.974 121.566 264.300  1.00 53.28           O  
ANISOU 2153  O   HIS A 276     8318   8462   3464   -188    263  -1026       O  
ATOM   2154  CB  HIS A 276      34.543 121.324 266.754  1.00 56.69           C  
ANISOU 2154  CB  HIS A 276     8915   9048   3577   -277     90  -1146       C  
ATOM   2155  CG  HIS A 276      35.753 121.365 265.870  1.00 57.25           C  
ANISOU 2155  CG  HIS A 276     8876   9137   3740   -349    -29  -1124       C  
ATOM   2156  ND1 HIS A 276      36.842 122.176 266.126  1.00 57.14           N  
ANISOU 2156  ND1 HIS A 276     8889   9121   3701   -449   -133  -1211       N  
ATOM   2157  CD2 HIS A 276      36.041 120.698 264.722  1.00 57.42           C  
ANISOU 2157  CD2 HIS A 276     8759   9180   3877   -339    -56  -1025       C  
ATOM   2158  CE1 HIS A 276      37.747 122.005 265.179  1.00 58.38           C  
ANISOU 2158  CE1 HIS A 276     8919   9305   3956   -496   -215  -1163       C  
ATOM   2159  NE2 HIS A 276      37.284 121.118 264.309  1.00 58.85           N  
ANISOU 2159  NE2 HIS A 276     8881   9379   4102   -427   -168  -1052       N  
ATOM   2160  N   ASN A 277      33.501 123.723 264.429  1.00 55.04           N  
ANISOU 2160  N   ASN A 277     8654   8542   3715   -281    242  -1196       N  
ATOM   2161  CA  ASN A 277      33.187 123.914 263.009  1.00 53.23           C  
ANISOU 2161  CA  ASN A 277     8324   8246   3656   -265    279  -1129       C  
ATOM   2162  C   ASN A 277      34.313 124.409 262.119  1.00 52.64           C  
ANISOU 2162  C   ASN A 277     8180   8147   3672   -359    182  -1132       C  
ATOM   2163  O   ASN A 277      34.072 124.632 260.915  1.00 51.45           O  
ANISOU 2163  O   ASN A 277     7954   7938   3658   -349    212  -1077       O  
ATOM   2164  CB  ASN A 277      31.973 124.841 262.834  1.00 53.48           C  
ANISOU 2164  CB  ASN A 277     8414   8154   3750   -202    409  -1165       C  
ATOM   2165  CG  ASN A 277      30.673 124.211 263.298  1.00 52.83           C  
ANISOU 2165  CG  ASN A 277     8346   8101   3624    -96    526  -1125       C  
ATOM   2166  OD1 ASN A 277      30.521 122.984 263.340  1.00 50.65           O  
ANISOU 2166  OD1 ASN A 277     8008   7922   3316    -66    522  -1038       O  
ATOM   2167  ND2 ASN A 277      29.716 125.060 263.636  1.00 53.15           N  
ANISOU 2167  ND2 ASN A 277     8470   8055   3668    -39    635  -1186       N  
ATOM   2168  N   THR A 278      35.511 124.602 262.678  1.00 52.79           N  
ANISOU 2168  N   THR A 278     8223   8214   3619   -450     68  -1192       N  
ATOM   2169  CA  THR A 278      36.602 125.153 261.866  1.00 53.02           C  
ANISOU 2169  CA  THR A 278     8185   8225   3735   -551    -19  -1197       C  
ATOM   2170  C   THR A 278      37.254 124.116 260.956  1.00 51.40           C  
ANISOU 2170  C   THR A 278     7824   8116   3591   -552    -81  -1088       C  
ATOM   2171  O   THR A 278      37.636 123.010 261.384  1.00 51.06           O  
ANISOU 2171  O   THR A 278     7738   8189   3472   -529   -135  -1044       O  
ATOM   2172  CB  THR A 278      37.674 125.943 262.664  1.00 54.60           C  
ANISOU 2172  CB  THR A 278     8459   8429   3857   -666   -121  -1308       C  
ATOM   2173  OG1 THR A 278      38.318 125.060 263.584  1.00 56.03           O  
ANISOU 2173  OG1 THR A 278     8634   8747   3908   -675   -208  -1306       O  
ATOM   2174  CG2 THR A 278      37.053 127.160 263.428  1.00 56.22           C  
ANISOU 2174  CG2 THR A 278     8833   8511   4016   -671    -56  -1430       C  
ATOM   2175  N   LEU A 279      37.337 124.514 259.686  1.00 50.41           N  
ANISOU 2175  N   LEU A 279     7621   7931   3602   -575    -66  -1046       N  
ATOM   2176  CA  LEU A 279      37.913 123.745 258.589  1.00 48.81           C  
ANISOU 2176  CA  LEU A 279     7272   7796   3479   -579   -108   -949       C  
ATOM   2177  C   LEU A 279      39.435 123.875 258.513  1.00 49.68           C  
ANISOU 2177  C   LEU A 279     7315   7977   3584   -687   -231   -969       C  
ATOM   2178  O   LEU A 279      40.038 124.764 259.143  1.00 50.81           O  
ANISOU 2178  O   LEU A 279     7524   8097   3685   -777   -285  -1060       O  
ATOM   2179  CB  LEU A 279      37.318 124.219 257.250  1.00 47.57           C  
ANISOU 2179  CB  LEU A 279     7070   7541   3462   -562    -35   -898       C  
ATOM   2180  CG  LEU A 279      35.874 123.914 256.827  1.00 45.76           C  
ANISOU 2180  CG  LEU A 279     6847   7260   3281   -453     79   -840       C  
ATOM   2181  CD1 LEU A 279      35.296 122.689 257.555  1.00 44.82           C  
ANISOU 2181  CD1 LEU A 279     6733   7224   3073   -369    103   -802       C  
ATOM   2182  CD2 LEU A 279      34.988 125.098 257.041  1.00 46.47           C  
ANISOU 2182  CD2 LEU A 279     7043   7218   3396   -435    162   -903       C  
ATOM   2183  N   GLU A 280      40.035 122.998 257.703  1.00 48.81           N  
ANISOU 2183  N   GLU A 280     7072   7953   3521   -678   -273   -884       N  
ATOM   2184  CA  GLU A 280      41.475 122.967 257.475  1.00 49.20           C  
ANISOU 2184  CA  GLU A 280     7025   8089   3579   -766   -382   -885       C  
ATOM   2185  C   GLU A 280      41.724 122.866 255.979  1.00 47.88           C  
ANISOU 2185  C   GLU A 280     6737   7917   3538   -773   -363   -807       C  
ATOM   2186  O   GLU A 280      41.682 121.783 255.413  1.00 47.11           O  
ANISOU 2186  O   GLU A 280     6555   7884   3461   -702   -355   -725       O  
ATOM   2187  CB  GLU A 280      42.093 121.774 258.202  1.00 49.53           C  
ANISOU 2187  CB  GLU A 280     7022   8273   3523   -730   -463   -859       C  
ATOM   2188  CG  GLU A 280      41.495 121.560 259.606  1.00 52.84           C  
ANISOU 2188  CG  GLU A 280     7568   8700   3809   -685   -454   -907       C  
ATOM   2189  CD  GLU A 280      42.100 120.394 260.384  1.00 55.49           C  
ANISOU 2189  CD  GLU A 280     7873   9171   4038   -647   -540   -876       C  
ATOM   2190  OE1 GLU A 280      42.929 119.644 259.811  1.00 55.24           O  
ANISOU 2190  OE1 GLU A 280     7716   9229   4042   -639   -602   -812       O  
ATOM   2191  OE2 GLU A 280      41.727 120.229 261.578  1.00 56.90           O  
ANISOU 2191  OE2 GLU A 280     8157   9367   4095   -620   -542   -914       O  
ATOM   2192  N   MET A 281      41.953 124.009 255.337  1.00 47.53           N  
ANISOU 2192  N   MET A 281     6695   7789   3574   -859   -352   -834       N  
ATOM   2193  CA  MET A 281      42.367 124.075 253.940  1.00 45.55           C  
ANISOU 2193  CA  MET A 281     6334   7538   3433   -890   -342   -768       C  
ATOM   2194  C   MET A 281      43.353 122.943 253.612  1.00 44.08           C  
ANISOU 2194  C   MET A 281     6008   7503   3239   -875   -410   -707       C  
ATOM   2195  O   MET A 281      44.188 122.615 254.458  1.00 45.23           O  
ANISOU 2195  O   MET A 281     6131   7746   3307   -904   -498   -740       O  
ATOM   2196  CB  MET A 281      43.011 125.443 253.713  1.00 46.83           C  
ANISOU 2196  CB  MET A 281     6517   7631   3646  -1025   -368   -823       C  
ATOM   2197  CG  MET A 281      43.498 125.690 252.328  1.00 48.25           C  
ANISOU 2197  CG  MET A 281     6594   7806   3932  -1076   -356   -761       C  
ATOM   2198  SD  MET A 281      42.206 125.299 251.143  1.00 52.79           S  
ANISOU 2198  SD  MET A 281     7162   8308   4586   -959   -242   -668       S  
ATOM   2199  CE  MET A 281      41.447 126.925 250.931  1.00 53.51           C  
ANISOU 2199  CE  MET A 281     7382   8205   4742  -1007   -176   -712       C  
ATOM   2200  N   VAL A 282      43.248 122.316 252.430  1.00 42.98           N  
ANISOU 2200  N   VAL A 282     5776   7384   3170   -825   -371   -621       N  
ATOM   2201  CA  VAL A 282      44.242 121.300 252.044  1.00 42.76           C  
ANISOU 2201  CA  VAL A 282     5614   7494   3141   -807   -430   -569       C  
ATOM   2202  C   VAL A 282      45.231 121.895 251.092  1.00 43.15           C  
ANISOU 2202  C   VAL A 282     5563   7566   3266   -905   -452   -556       C  
ATOM   2203  O   VAL A 282      46.350 122.152 251.467  1.00 44.18           O  
ANISOU 2203  O   VAL A 282     5637   7774   3377   -988   -532   -590       O  
ATOM   2204  CB  VAL A 282      43.690 120.032 251.394  1.00 41.48           C  
ANISOU 2204  CB  VAL A 282     5406   7361   2992   -687   -385   -485       C  
ATOM   2205  CG1 VAL A 282      44.858 119.135 250.984  1.00 41.52           C  
ANISOU 2205  CG1 VAL A 282     5275   7501   3000   -674   -448   -441       C  
ATOM   2206  CG2 VAL A 282      42.782 119.276 252.334  1.00 41.15           C  
ANISOU 2206  CG2 VAL A 282     5451   7312   2872   -593   -366   -485       C  
ATOM   2207  N   ARG A 283      44.840 122.072 249.842  1.00 42.38           N  
ANISOU 2207  N   ARG A 283     5437   7413   3254   -895   -382   -501       N  
ATOM   2208  CA  ARG A 283      45.646 122.849 248.946  1.00 42.87           C  
ANISOU 2208  CA  ARG A 283     5426   7476   3388  -1001   -388   -490       C  
ATOM   2209  C   ARG A 283      44.728 123.831 248.296  1.00 42.60           C  
ANISOU 2209  C   ARG A 283     5475   7291   3419  -1022   -308   -484       C  
ATOM   2210  O   ARG A 283      43.726 123.444 247.727  1.00 41.55           O  
ANISOU 2210  O   ARG A 283     5369   7107   3312   -932   -240   -435       O  
ATOM   2211  CB  ARG A 283      46.339 121.990 247.915  1.00 42.38           C  
ANISOU 2211  CB  ARG A 283     5221   7521   3361   -970   -390   -418       C  
ATOM   2212  CG  ARG A 283      47.237 122.806 247.046  1.00 43.06           C  
ANISOU 2212  CG  ARG A 283     5226   7620   3513  -1088   -393   -406       C  
ATOM   2213  CD  ARG A 283      48.197 121.944 246.306  1.00 42.96           C  
ANISOU 2213  CD  ARG A 283     5060   7748   3516  -1065   -410   -352       C  
ATOM   2214  NE  ARG A 283      49.199 122.758 245.618  1.00 43.88           N  
ANISOU 2214  NE  ARG A 283     5088   7897   3688  -1194   -419   -345       N  
ATOM   2215  CZ  ARG A 283      49.010 123.394 244.459  1.00 43.69           C  
ANISOU 2215  CZ  ARG A 283     5062   7806   3732  -1242   -352   -302       C  
ATOM   2216  NH1 ARG A 283      47.846 123.343 243.801  1.00 43.23           N  
ANISOU 2216  NH1 ARG A 283     5083   7645   3699  -1169   -275   -263       N  
ATOM   2217  NH2 ARG A 283      49.997 124.107 243.953  1.00 44.69           N  
ANISOU 2217  NH2 ARG A 283     5106   7973   3901  -1369   -364   -296       N  
ATOM   2218  N   PRO A 284      45.041 125.120 248.423  1.00 43.64           N  
ANISOU 2218  N   PRO A 284     5655   7347   3578  -1140   -320   -534       N  
ATOM   2219  CA  PRO A 284      44.231 126.165 247.810  1.00 43.58           C  
ANISOU 2219  CA  PRO A 284     5735   7186   3638  -1163   -249   -528       C  
ATOM   2220  C   PRO A 284      44.014 125.918 246.312  1.00 42.67           C  
ANISOU 2220  C   PRO A 284     5550   7066   3596  -1131   -190   -434       C  
ATOM   2221  O   PRO A 284      44.935 125.489 245.611  1.00 42.65           O  
ANISOU 2221  O   PRO A 284     5426   7167   3611  -1163   -212   -390       O  
ATOM   2222  CB  PRO A 284      45.071 127.419 248.025  1.00 45.04           C  
ANISOU 2222  CB  PRO A 284     5943   7326   3843  -1320   -292   -585       C  
ATOM   2223  CG  PRO A 284      45.823 127.142 249.295  1.00 45.89           C  
ANISOU 2223  CG  PRO A 284     6042   7528   3866  -1355   -383   -657       C  
ATOM   2224  CD  PRO A 284      46.034 125.661 249.368  1.00 45.04           C  
ANISOU 2224  CD  PRO A 284     5834   7567   3712  -1251   -407   -611       C  
ATOM   2225  N   ARG A 285      42.803 126.176 245.833  1.00 42.01           N  
ANISOU 2225  N   ARG A 285     5541   6870   3550  -1065   -116   -403       N  
ATOM   2226  CA  ARG A 285      42.488 125.994 244.432  1.00 41.22           C  
ANISOU 2226  CA  ARG A 285     5392   6758   3511  -1034    -63   -315       C  
ATOM   2227  C   ARG A 285      43.489 126.749 243.570  1.00 41.96           C  
ANISOU 2227  C   ARG A 285     5427   6859   3658  -1158    -73   -291       C  
ATOM   2228  O   ARG A 285      43.914 127.875 243.920  1.00 43.10           O  
ANISOU 2228  O   ARG A 285     5623   6935   3820  -1270    -95   -340       O  
ATOM   2229  CB  ARG A 285      41.068 126.466 244.122  1.00 40.75           C  
ANISOU 2229  CB  ARG A 285     5432   6562   3490   -965      8   -294       C  
ATOM   2230  CG  ARG A 285      40.793 127.911 244.526  1.00 41.79           C  
ANISOU 2230  CG  ARG A 285     5680   6548   3651  -1031     22   -348       C  
ATOM   2231  CD  ARG A 285      39.383 128.356 244.152  1.00 41.41           C  
ANISOU 2231  CD  ARG A 285     5717   6369   3647   -948     94   -319       C  
ATOM   2232  NE  ARG A 285      38.357 127.700 244.966  1.00 40.84           N  
ANISOU 2232  NE  ARG A 285     5686   6301   3529   -831    119   -341       N  
ATOM   2233  CZ  ARG A 285      37.050 127.872 244.789  1.00 40.48           C  
ANISOU 2233  CZ  ARG A 285     5697   6169   3514   -740    181   -316       C  
ATOM   2234  NH1 ARG A 285      36.613 128.682 243.812  1.00 40.61           N  
ANISOU 2234  NH1 ARG A 285     5740   6085   3606   -746    218   -267       N  
ATOM   2235  NH2 ARG A 285      36.185 127.236 245.568  1.00 40.06           N  
ANISOU 2235  NH2 ARG A 285     5671   6134   3416   -643    205   -336       N  
ATOM   2236  N   GLU A 286      43.874 126.100 242.466  1.00 41.40           N  
ANISOU 2236  N   GLU A 286     5251   6871   3607  -1142    -57   -218       N  
ATOM   2237  CA  GLU A 286      44.750 126.655 241.444  1.00 41.99           C  
ANISOU 2237  CA  GLU A 286     5256   6967   3730  -1246    -50   -176       C  
ATOM   2238  C   GLU A 286      44.194 126.180 240.115  1.00 41.03           C  
ANISOU 2238  C   GLU A 286     5106   6847   3637  -1176     10    -88       C  
ATOM   2239  O   GLU A 286      44.101 124.976 239.836  1.00 40.15           O  
ANISOU 2239  O   GLU A 286     4932   6826   3497  -1081     15    -57       O  
ATOM   2240  CB  GLU A 286      46.205 126.205 241.658  1.00 42.64           C  
ANISOU 2240  CB  GLU A 286     5208   7205   3786  -1312   -110   -192       C  
ATOM   2241  CG  GLU A 286      47.195 126.551 240.498  1.00 43.48           C  
ANISOU 2241  CG  GLU A 286     5212   7371   3938  -1411    -93   -137       C  
ATOM   2242  CD  GLU A 286      48.673 126.305 240.872  1.00 46.42           C  
ANISOU 2242  CD  GLU A 286     5451   7895   4291  -1491   -158   -163       C  
ATOM   2243  OE1 GLU A 286      49.009 125.210 241.386  1.00 46.89           O  
ANISOU 2243  OE1 GLU A 286     5440   8073   4302  -1411   -197   -177       O  
ATOM   2244  OE2 GLU A 286      49.505 127.207 240.644  1.00 48.48           O  
ANISOU 2244  OE2 GLU A 286     5677   8158   4587  -1635   -170   -165       O  
ATOM   2245  N   LYS A 287      43.781 127.155 239.319  1.00 41.29           N  
ANISOU 2245  N   LYS A 287     5196   6768   3724  -1221     54    -49       N  
ATOM   2246  CA  LYS A 287      43.072 126.909 238.061  1.00 40.51           C  
ANISOU 2246  CA  LYS A 287     5096   6644   3651  -1158    110     35       C  
ATOM   2247  C   LYS A 287      43.850 125.890 237.251  1.00 40.13           C  
ANISOU 2247  C   LYS A 287     4921   6745   3582  -1142    112     81       C  
ATOM   2248  O   LYS A 287      45.072 125.959 237.179  1.00 40.87           O  
ANISOU 2248  O   LYS A 287     4927   6929   3673  -1227     89     73       O  
ATOM   2249  CB  LYS A 287      42.929 128.236 237.292  1.00 41.24           C  
ANISOU 2249  CB  LYS A 287     5253   6614   3804  -1244    143     74       C  
ATOM   2250  CG  LYS A 287      41.607 128.438 236.564  1.00 40.64           C  
ANISOU 2250  CG  LYS A 287     5252   6431   3756  -1161    193    133       C  
ATOM   2251  CD  LYS A 287      41.754 128.297 235.032  1.00 42.95           C  
ANISOU 2251  CD  LYS A 287     5494   6761   4064  -1172    229    228       C  
ATOM   2252  CE  LYS A 287      40.376 128.052 234.391  1.00 45.40           C  
ANISOU 2252  CE  LYS A 287     5856   7009   4386  -1059    263    285       C  
ATOM   2253  NZ  LYS A 287      40.281 128.612 232.990  1.00 49.22           N  
ANISOU 2253  NZ  LYS A 287     6352   7452   4898  -1095    298    376       N  
ATOM   2254  N   GLY A 288      43.148 124.932 236.668  1.00 39.07           N  
ANISOU 2254  N   GLY A 288     4776   6639   3431  -1031    139    124       N  
ATOM   2255  CA  GLY A 288      43.799 123.852 235.979  1.00 38.71           C  
ANISOU 2255  CA  GLY A 288     4624   6728   3358   -995    143    158       C  
ATOM   2256  C   GLY A 288      44.088 122.657 236.871  1.00 38.32           C  
ANISOU 2256  C   GLY A 288     4525   6776   3258   -919    101    114       C  
ATOM   2257  O   GLY A 288      44.271 121.549 236.379  1.00 37.80           O  
ANISOU 2257  O   GLY A 288     4397   6800   3165   -847    108    140       O  
ATOM   2258  N   VAL A 289      44.132 122.845 238.184  1.00 38.63           N  
ANISOU 2258  N   VAL A 289     4599   6799   3279   -931     57     48       N  
ATOM   2259  CA  VAL A 289      44.531 121.738 239.017  1.00 38.42           C  
ANISOU 2259  CA  VAL A 289     4525   6873   3201   -866     12     15       C  
ATOM   2260  C   VAL A 289      43.296 121.073 239.541  1.00 37.50           C  
ANISOU 2260  C   VAL A 289     4487   6703   3058   -756     22      9       C  
ATOM   2261  O   VAL A 289      42.436 121.726 240.093  1.00 37.49           O  
ANISOU 2261  O   VAL A 289     4580   6598   3065   -757     33    -15       O  
ATOM   2262  CB  VAL A 289      45.506 122.129 240.204  1.00 39.44           C  
ANISOU 2262  CB  VAL A 289     4627   7051   3308   -942    -54    -53       C  
ATOM   2263  CG1 VAL A 289      46.062 120.893 240.847  1.00 39.32           C  
ANISOU 2263  CG1 VAL A 289     4543   7158   3239   -869   -103    -71       C  
ATOM   2264  CG2 VAL A 289      46.681 122.955 239.750  1.00 40.54           C  
ANISOU 2264  CG2 VAL A 289     4689   7233   3481  -1073    -64    -50       C  
ATOM   2265  N   ARG A 290      43.213 119.764 239.354  1.00 36.82           N  
ANISOU 2265  N   ARG A 290     4362   6687   2939   -660     20     33       N  
ATOM   2266  CA  ARG A 290      42.178 118.910 239.972  1.00 36.04           C  
ANISOU 2266  CA  ARG A 290     4325   6560   2807   -559     22     28       C  
ATOM   2267  C   ARG A 290      42.867 117.931 240.913  1.00 36.20           C  
ANISOU 2267  C   ARG A 290     4305   6678   2773   -515    -33     -3       C  
ATOM   2268  O   ARG A 290      44.016 117.505 240.674  1.00 36.62           O  
ANISOU 2268  O   ARG A 290     4263   6835   2816   -524    -61      1       O  
ATOM   2269  CB  ARG A 290      41.376 118.120 238.909  1.00 35.14           C  
ANISOU 2269  CB  ARG A 290     4216   6434   2702   -483     64     88       C  
ATOM   2270  CG  ARG A 290      40.473 119.000 238.032  1.00 35.55           C  
ANISOU 2270  CG  ARG A 290     4319   6385   2803   -508    113    126       C  
ATOM   2271  CD  ARG A 290      39.987 118.331 236.770  1.00 39.53           C  
ANISOU 2271  CD  ARG A 290     4809   6898   3312   -457    145    186       C  
ATOM   2272  NE  ARG A 290      39.411 117.011 236.992  1.00 43.71           N  
ANISOU 2272  NE  ARG A 290     5350   7453   3806   -364    138    193       N  
ATOM   2273  CZ  ARG A 290      39.950 115.866 236.558  1.00 46.14           C  
ANISOU 2273  CZ  ARG A 290     5607   7841   4083   -316    129    205       C  
ATOM   2274  NH1 ARG A 290      41.091 115.852 235.865  1.00 44.56           N  
ANISOU 2274  NH1 ARG A 290     5331   7717   3882   -346    130    212       N  
ATOM   2275  NH2 ARG A 290      39.340 114.714 236.823  1.00 48.48           N  
ANISOU 2275  NH2 ARG A 290     5930   8141   4350   -237    122    211       N  
ATOM   2276  N   TYR A 291      42.171 117.571 241.984  1.00 35.97           N  
ANISOU 2276  N   TYR A 291     4345   6618   2705   -465    -47    -29       N  
ATOM   2277  CA  TYR A 291      42.699 116.591 242.913  1.00 36.14           C  
ANISOU 2277  CA  TYR A 291     4343   6723   2667   -414   -100    -50       C  
ATOM   2278  C   TYR A 291      41.626 116.143 243.858  1.00 35.73           C  
ANISOU 2278  C   TYR A 291     4383   6620   2574   -351    -94    -61       C  
ATOM   2279  O   TYR A 291      40.741 116.930 244.199  1.00 35.70           O  
ANISOU 2279  O   TYR A 291     4456   6526   2582   -372    -63    -79       O  
ATOM   2280  CB  TYR A 291      43.898 117.151 243.674  1.00 37.20           C  
ANISOU 2280  CB  TYR A 291     4431   6922   2783   -490   -162    -99       C  
ATOM   2281  CG  TYR A 291      43.561 118.148 244.718  1.00 37.72           C  
ANISOU 2281  CG  TYR A 291     4580   6920   2833   -548   -176   -156       C  
ATOM   2282  CD1 TYR A 291      43.310 117.730 246.015  1.00 37.88           C  
ANISOU 2282  CD1 TYR A 291     4657   6950   2786   -508   -211   -192       C  
ATOM   2283  CD2 TYR A 291      43.516 119.524 244.425  1.00 38.18           C  
ANISOU 2283  CD2 TYR A 291     4667   6900   2939   -645   -153   -176       C  
ATOM   2284  CE1 TYR A 291      43.029 118.648 247.023  1.00 38.48           C  
ANISOU 2284  CE1 TYR A 291     4818   6967   2837   -561   -222   -253       C  
ATOM   2285  CE2 TYR A 291      43.205 120.465 245.414  1.00 38.78           C  
ANISOU 2285  CE2 TYR A 291     4833   6904   2998   -696   -165   -238       C  
ATOM   2286  CZ  TYR A 291      42.963 120.001 246.720  1.00 38.93           C  
ANISOU 2286  CZ  TYR A 291     4906   6940   2943   -651   -198   -279       C  
ATOM   2287  OH  TYR A 291      42.683 120.849 247.750  1.00 39.61           O  
ANISOU 2287  OH  TYR A 291     5086   6964   3000   -694   -209   -347       O  
ATOM   2288  N   THR A 292      41.733 114.873 244.256  1.00 35.52           N  
ANISOU 2288  N   THR A 292     4345   6652   2500   -272   -121    -46       N  
ATOM   2289  CA  THR A 292      40.817 114.204 245.186  1.00 35.30           C  
ANISOU 2289  CA  THR A 292     4396   6593   2422   -208   -117    -47       C  
ATOM   2290  C   THR A 292      41.599 113.714 246.412  1.00 36.61           C  
ANISOU 2290  C   THR A 292     4558   6835   2517   -193   -187    -77       C  
ATOM   2291  O   THR A 292      42.733 113.259 246.284  1.00 36.93           O  
ANISOU 2291  O   THR A 292     4518   6964   2548   -184   -236    -74       O  
ATOM   2292  CB  THR A 292      40.141 112.999 244.493  1.00 34.40           C  
ANISOU 2292  CB  THR A 292     4288   6470   2313   -127    -87     10       C  
ATOM   2293  OG1 THR A 292      39.170 113.455 243.540  1.00 33.82           O  
ANISOU 2293  OG1 THR A 292     4236   6320   2294   -138    -27     38       O  
ATOM   2294  CG2 THR A 292      39.451 112.123 245.498  1.00 35.32           C  
ANISOU 2294  CG2 THR A 292     4472   6575   2371    -65    -93     15       C  
ATOM   2295  N   VAL A 293      40.969 113.787 247.583  1.00 37.70           N  
ANISOU 2295  N   VAL A 293     4780   6941   2603   -183   -190   -104       N  
ATOM   2296  CA  VAL A 293      41.593 113.443 248.869  1.00 39.38           C  
ANISOU 2296  CA  VAL A 293     5008   7220   2736   -174   -258   -135       C  
ATOM   2297  C   VAL A 293      40.955 112.229 249.561  1.00 39.99           C  
ANISOU 2297  C   VAL A 293     5144   7298   2750    -88   -257   -103       C  
ATOM   2298  O   VAL A 293      39.709 112.123 249.647  1.00 39.88           O  
ANISOU 2298  O   VAL A 293     5202   7213   2736    -63   -197    -87       O  
ATOM   2299  CB  VAL A 293      41.530 114.662 249.841  1.00 40.17           C  
ANISOU 2299  CB  VAL A 293     5169   7286   2808   -249   -268   -204       C  
ATOM   2300  CG1 VAL A 293      41.990 114.301 251.303  1.00 39.84           C  
ANISOU 2300  CG1 VAL A 293     5165   7307   2664   -237   -339   -238       C  
ATOM   2301  CG2 VAL A 293      42.326 115.828 249.254  1.00 40.92           C  
ANISOU 2301  CG2 VAL A 293     5206   7381   2960   -345   -282   -236       C  
ATOM   2302  N   GLU A 294      41.814 111.339 250.068  1.00 41.05           N  
ANISOU 2302  N   GLU A 294     5249   7517   2833    -44   -326    -92       N  
ATOM   2303  CA  GLU A 294      41.398 110.185 250.887  1.00 41.92           C  
ANISOU 2303  CA  GLU A 294     5422   7635   2870     32   -340    -60       C  
ATOM   2304  C   GLU A 294      42.336 110.070 252.074  1.00 42.89           C  
ANISOU 2304  C   GLU A 294     5544   7840   2912     31   -428    -88       C  
ATOM   2305  O   GLU A 294      43.558 110.132 251.889  1.00 44.01           O  
ANISOU 2305  O   GLU A 294     5594   8062   3064     18   -492    -99       O  
ATOM   2306  CB  GLU A 294      41.423 108.866 250.092  1.00 41.13           C  
ANISOU 2306  CB  GLU A 294     5291   7543   2792    114   -334      3       C  
ATOM   2307  CG  GLU A 294      40.393 108.760 248.957  1.00 43.28           C  
ANISOU 2307  CG  GLU A 294     5576   7737   3132    121   -255     36       C  
ATOM   2308  CD  GLU A 294      39.037 108.208 249.418  1.00 48.33           C  
ANISOU 2308  CD  GLU A 294     6312   8310   3744    152   -206     66       C  
ATOM   2309  OE1 GLU A 294      39.046 107.118 250.083  1.00 50.02           O  
ANISOU 2309  OE1 GLU A 294     6567   8541   3898    209   -235     97       O  
ATOM   2310  OE2 GLU A 294      37.980 108.862 249.105  1.00 46.45           O  
ANISOU 2310  OE2 GLU A 294     6102   8003   3544    118   -140     63       O  
ATOM   2311  N   MET A 295      41.766 109.889 253.270  1.00 42.97           N  
ANISOU 2311  N   MET A 295     5650   7837   2838     45   -432    -96       N  
ATOM   2312  CA  MET A 295      42.529 109.735 254.517  1.00 43.73           C  
ANISOU 2312  CA  MET A 295     5765   8011   2839     47   -519   -118       C  
ATOM   2313  C   MET A 295      42.928 108.296 254.757  1.00 43.71           C  
ANISOU 2313  C   MET A 295     5756   8060   2792    141   -569    -57       C  
ATOM   2314  O   MET A 295      42.247 107.352 254.313  1.00 42.79           O  
ANISOU 2314  O   MET A 295     5669   7895   2693    204   -523      0       O  
ATOM   2315  CB  MET A 295      41.712 110.176 255.733  1.00 44.16           C  
ANISOU 2315  CB  MET A 295     5938   8029   2810     23   -496   -154       C  
ATOM   2316  CG  MET A 295      41.117 111.568 255.656  1.00 45.92           C  
ANISOU 2316  CG  MET A 295     6196   8182   3069    -55   -436   -217       C  
ATOM   2317  SD  MET A 295      42.314 112.870 255.995  1.00 53.34           S  
ANISOU 2317  SD  MET A 295     7095   9171   4002   -159   -513   -302       S  
ATOM   2318  CE  MET A 295      42.898 112.488 257.661  1.00 52.84           C  
ANISOU 2318  CE  MET A 295     7092   9196   3790   -150   -611   -328       C  
ATOM   2319  N   HIS A 296      44.050 108.154 255.455  1.00 44.67           N  
ANISOU 2319  N   HIS A 296     5840   8277   2857    147   -669    -70       N  
ATOM   2320  CA  HIS A 296      44.462 106.918 256.087  1.00 45.49           C  
ANISOU 2320  CA  HIS A 296     5961   8434   2891    236   -734    -18       C  
ATOM   2321  C   HIS A 296      44.734 107.315 257.530  1.00 46.72           C  
ANISOU 2321  C   HIS A 296     6176   8642   2935    201   -802    -57       C  
ATOM   2322  O   HIS A 296      45.592 108.173 257.785  1.00 47.94           O  
ANISOU 2322  O   HIS A 296     6273   8860   3081    134   -865   -113       O  
ATOM   2323  CB  HIS A 296      45.717 106.364 255.421  1.00 46.11           C  
ANISOU 2323  CB  HIS A 296     5913   8594   3013    287   -798      7       C  
ATOM   2324  CG  HIS A 296      46.074 104.974 255.861  1.00 47.76           C  
ANISOU 2324  CG  HIS A 296     6140   8840   3168    399   -856     70       C  
ATOM   2325  ND1 HIS A 296      47.334 104.632 256.307  1.00 48.91           N  
ANISOU 2325  ND1 HIS A 296     6209   9096   3277    441   -963     78       N  
ATOM   2326  CD2 HIS A 296      45.333 103.841 255.927  1.00 48.14           C  
ANISOU 2326  CD2 HIS A 296     6275   8824   3193    478   -822    133       C  
ATOM   2327  CE1 HIS A 296      47.351 103.350 256.629  1.00 50.22           C  
ANISOU 2327  CE1 HIS A 296     6422   9261   3401    549   -994    143       C  
ATOM   2328  NE2 HIS A 296      46.147 102.848 256.414  1.00 49.08           N  
ANISOU 2328  NE2 HIS A 296     6380   9007   3261    569   -908    177       N  
ATOM   2329  N   GLY A 297      43.981 106.729 258.468  1.00 46.71           N  
ANISOU 2329  N   GLY A 297     6293   8612   2843    238   -789    -28       N  
ATOM   2330  CA  GLY A 297      43.980 107.183 259.853  1.00 47.16           C  
ANISOU 2330  CA  GLY A 297     6434   8704   2781    199   -832    -70       C  
ATOM   2331  C   GLY A 297      43.728 108.679 259.912  1.00 47.22           C  
ANISOU 2331  C   GLY A 297     6455   8680   2807     93   -796   -159       C  
ATOM   2332  O   GLY A 297      42.990 109.221 259.105  1.00 46.26           O  
ANISOU 2332  O   GLY A 297     6329   8477   2769     64   -704   -173       O  
ATOM   2333  N   THR A 298      44.359 109.371 260.846  1.00 48.54           N  
ANISOU 2333  N   THR A 298     6639   8908   2896     35   -872   -220       N  
ATOM   2334  CA  THR A 298      43.974 110.757 261.063  1.00 48.72           C  
ANISOU 2334  CA  THR A 298     6709   8881   2920    -62   -831   -309       C  
ATOM   2335  C   THR A 298      44.958 111.736 260.455  1.00 49.49           C  
ANISOU 2335  C   THR A 298     6699   9011   3094   -147   -880   -364       C  
ATOM   2336  O   THR A 298      44.694 112.935 260.399  1.00 49.35           O  
ANISOU 2336  O   THR A 298     6711   8936   3102   -231   -842   -435       O  
ATOM   2337  CB  THR A 298      43.717 111.070 262.559  1.00 49.41           C  
ANISOU 2337  CB  THR A 298     6924   8986   2862    -87   -857   -358       C  
ATOM   2338  OG1 THR A 298      44.806 110.596 263.340  1.00 50.62           O  
ANISOU 2338  OG1 THR A 298     7053   9254   2925    -74   -989   -348       O  
ATOM   2339  CG2 THR A 298      42.474 110.372 263.045  1.00 49.10           C  
ANISOU 2339  CG2 THR A 298     7000   8894   2763    -24   -771   -311       C  
ATOM   2340  N   ASP A 299      46.061 111.211 259.937  1.00 50.63           N  
ANISOU 2340  N   ASP A 299     6717   9239   3279   -122   -956   -327       N  
ATOM   2341  CA  ASP A 299      47.252 112.031 259.641  1.00 52.74           C  
ANISOU 2341  CA  ASP A 299     6872   9575   3591   -208  -1031   -376       C  
ATOM   2342  C   ASP A 299      47.751 111.992 258.198  1.00 51.69           C  
ANISOU 2342  C   ASP A 299     6600   9450   3590   -206  -1005   -344       C  
ATOM   2343  O   ASP A 299      48.210 113.005 257.663  1.00 52.06           O  
ANISOU 2343  O   ASP A 299     6582   9495   3703   -302  -1005   -389       O  
ATOM   2344  CB  ASP A 299      48.394 111.590 260.552  1.00 54.87           C  
ANISOU 2344  CB  ASP A 299     7099   9978   3771   -196  -1171   -373       C  
ATOM   2345  CG  ASP A 299      48.181 110.164 261.105  1.00 58.83           C  
ANISOU 2345  CG  ASP A 299     7649  10508   4195    -70  -1194   -295       C  
ATOM   2346  OD1 ASP A 299      47.616 109.289 260.338  1.00 58.91           O  
ANISOU 2346  OD1 ASP A 299     7655  10465   4263     17  -1120   -225       O  
ATOM   2347  OD2 ASP A 299      48.559 109.948 262.310  1.00 61.02           O  
ANISOU 2347  OD2 ASP A 299     7977  10858   4350    -63  -1286   -303       O  
ATOM   2348  N   THR A 300      47.686 110.815 257.586  1.00 50.32           N  
ANISOU 2348  N   THR A 300     6385   9285   3449    -99   -983   -266       N  
ATOM   2349  CA  THR A 300      48.256 110.629 256.270  1.00 49.15           C  
ANISOU 2349  CA  THR A 300     6105   9161   3409    -83   -965   -233       C  
ATOM   2350  C   THR A 300      47.202 110.884 255.174  1.00 46.79           C  
ANISOU 2350  C   THR A 300     5836   8743   3198    -87   -839   -220       C  
ATOM   2351  O   THR A 300      46.132 110.296 255.182  1.00 45.67           O  
ANISOU 2351  O   THR A 300     5784   8526   3043    -27   -774   -186       O  
ATOM   2352  CB  THR A 300      49.054 109.264 256.158  1.00 49.81           C  
ANISOU 2352  CB  THR A 300     6107   9336   3483     35  -1027   -165       C  
ATOM   2353  OG1 THR A 300      48.764 108.594 254.915  1.00 50.31           O  
ANISOU 2353  OG1 THR A 300     6130   9356   3631    105   -952   -113       O  
ATOM   2354  CG2 THR A 300      48.770 108.339 257.329  1.00 49.54           C  
ANISOU 2354  CG2 THR A 300     6172   9314   3336    114  -1074   -132       C  
ATOM   2355  N   LEU A 301      47.507 111.784 254.253  1.00 45.51           N  
ANISOU 2355  N   LEU A 301     5600   8569   3123   -165   -809   -246       N  
ATOM   2356  CA  LEU A 301      46.566 112.125 253.200  1.00 43.65           C  
ANISOU 2356  CA  LEU A 301     5390   8227   2968   -175   -701   -232       C  
ATOM   2357  C   LEU A 301      46.999 111.543 251.887  1.00 42.63           C  
ANISOU 2357  C   LEU A 301     5154   8126   2918   -128   -675   -182       C  
ATOM   2358  O   LEU A 301      48.124 111.755 251.465  1.00 43.60           O  
ANISOU 2358  O   LEU A 301     5157   8334   3075   -161   -718   -187       O  
ATOM   2359  CB  LEU A 301      46.504 113.622 253.016  1.00 43.83           C  
ANISOU 2359  CB  LEU A 301     5423   8198   3033   -297   -675   -293       C  
ATOM   2360  CG  LEU A 301      45.561 114.406 253.889  1.00 43.91           C  
ANISOU 2360  CG  LEU A 301     5568   8120   2996   -340   -644   -346       C  
ATOM   2361  CD1 LEU A 301      46.213 114.671 255.255  1.00 43.12           C  
ANISOU 2361  CD1 LEU A 301     5499   8088   2797   -383   -740   -402       C  
ATOM   2362  CD2 LEU A 301      45.185 115.690 253.105  1.00 42.53           C  
ANISOU 2362  CD2 LEU A 301     5402   7852   2904   -427   -577   -377       C  
ATOM   2363  N   ILE A 302      46.113 110.829 251.221  1.00 40.74           N  
ANISOU 2363  N   ILE A 302     4954   7819   2705    -57   -603   -134       N  
ATOM   2364  CA  ILE A 302      46.516 110.156 250.021  1.00 39.86           C  
ANISOU 2364  CA  ILE A 302     4755   7735   2655     -2   -580    -89       C  
ATOM   2365  C   ILE A 302      45.778 110.846 248.924  1.00 38.75           C  
ANISOU 2365  C   ILE A 302     4625   7508   2589    -49   -491    -87       C  
ATOM   2366  O   ILE A 302      44.568 110.687 248.818  1.00 38.36           O  
ANISOU 2366  O   ILE A 302     4665   7367   2542    -26   -430    -70       O  
ATOM   2367  CB  ILE A 302      46.165 108.685 250.088  1.00 39.48           C  
ANISOU 2367  CB  ILE A 302     4747   7680   2575    120   -579    -34       C  
ATOM   2368  CG1 ILE A 302      46.996 108.044 251.185  1.00 40.19           C  
ANISOU 2368  CG1 ILE A 302     4822   7860   2589    170   -676    -30       C  
ATOM   2369  CG2 ILE A 302      46.461 108.025 248.765  1.00 38.73           C  
ANISOU 2369  CG2 ILE A 302     4578   7596   2542    178   -544      5       C  
ATOM   2370  CD1 ILE A 302      46.460 106.781 251.684  1.00 40.03           C  
ANISOU 2370  CD1 ILE A 302     4886   7810   2514    272   -681     17       C  
ATOM   2371  N   VAL A 303      46.521 111.618 248.131  1.00 38.92           N  
ANISOU 2371  N   VAL A 303     4553   7565   2669   -119   -487   -101       N  
ATOM   2372  CA  VAL A 303      45.980 112.541 247.109  1.00 38.34           C  
ANISOU 2372  CA  VAL A 303     4486   7414   2666   -185   -412   -102       C  
ATOM   2373  C   VAL A 303      46.140 112.034 245.664  1.00 37.81           C  
ANISOU 2373  C   VAL A 303     4350   7361   2656   -145   -364    -56       C  
ATOM   2374  O   VAL A 303      47.259 111.797 245.184  1.00 38.36           O  
ANISOU 2374  O   VAL A 303     4307   7525   2741   -138   -389    -48       O  
ATOM   2375  CB  VAL A 303      46.691 113.930 247.214  1.00 39.16           C  
ANISOU 2375  CB  VAL A 303     4546   7537   2796   -313   -437   -151       C  
ATOM   2376  CG1 VAL A 303      46.134 114.920 246.194  1.00 38.67           C  
ANISOU 2376  CG1 VAL A 303     4502   7388   2805   -381   -362   -146       C  
ATOM   2377  CG2 VAL A 303      46.680 114.482 248.685  1.00 39.91           C  
ANISOU 2377  CG2 VAL A 303     4710   7627   2826   -361   -494   -209       C  
ATOM   2378  N   LEU A 304      45.028 111.869 244.959  1.00 36.85           N  
ANISOU 2378  N   LEU A 304     4292   7149   2560   -118   -294    -27       N  
ATOM   2379  CA  LEU A 304      45.077 111.614 243.496  1.00 36.39           C  
ANISOU 2379  CA  LEU A 304     4183   7092   2553    -99   -242     10       C  
ATOM   2380  C   LEU A 304      44.958 112.943 242.750  1.00 36.37           C  
ANISOU 2380  C   LEU A 304     4168   7044   2605   -200   -199      2       C  
ATOM   2381  O   LEU A 304      44.020 113.705 242.985  1.00 36.17           O  
ANISOU 2381  O   LEU A 304     4223   6927   2592   -242   -171    -10       O  
ATOM   2382  CB  LEU A 304      43.973 110.644 243.089  1.00 35.48           C  
ANISOU 2382  CB  LEU A 304     4141   6909   2432    -17   -200     48       C  
ATOM   2383  CG  LEU A 304      43.413 110.621 241.669  1.00 35.48           C  
ANISOU 2383  CG  LEU A 304     4142   6862   2477    -14   -135     82       C  
ATOM   2384  CD1 LEU A 304      44.427 110.019 240.701  1.00 35.11           C  
ANISOU 2384  CD1 LEU A 304     4002   6897   2441     25   -133     98       C  
ATOM   2385  CD2 LEU A 304      42.113 109.819 241.677  1.00 34.04           C  
ANISOU 2385  CD2 LEU A 304     4052   6600   2280     45   -108    109       C  
ATOM   2386  N   THR A 305      45.898 113.239 241.869  1.00 36.79           N  
ANISOU 2386  N   THR A 305     4123   7162   2694   -239   -191     11       N  
ATOM   2387  CA  THR A 305      45.897 114.557 241.267  1.00 36.97           C  
ANISOU 2387  CA  THR A 305     4138   7143   2765   -346   -157      7       C  
ATOM   2388  C   THR A 305      46.483 114.650 239.849  1.00 37.58           C  
ANISOU 2388  C   THR A 305     4131   7265   2882   -367   -113     42       C  
ATOM   2389  O   THR A 305      47.271 113.791 239.439  1.00 37.86           O  
ANISOU 2389  O   THR A 305     4084   7394   2906   -309   -119     57       O  
ATOM   2390  CB  THR A 305      46.629 115.512 242.159  1.00 37.92           C  
ANISOU 2390  CB  THR A 305     4234   7292   2882   -441   -208    -41       C  
ATOM   2391  OG1 THR A 305      46.774 116.747 241.472  1.00 38.24           O  
ANISOU 2391  OG1 THR A 305     4261   7294   2974   -550   -175    -39       O  
ATOM   2392  CG2 THR A 305      47.987 114.982 242.436  1.00 38.78           C  
ANISOU 2392  CG2 THR A 305     4226   7538   2970   -428   -266    -49       C  
ATOM   2393  N   ASN A 306      46.099 115.708 239.125  1.00 38.20           N  
ANISOU 2393  N   ASN A 306     4236   7276   3004   -447    -67     55       N  
ATOM   2394  CA  ASN A 306      46.633 116.002 237.778  1.00 39.24           C  
ANISOU 2394  CA  ASN A 306     4297   7445   3168   -487    -20     91       C  
ATOM   2395  C   ASN A 306      47.728 117.080 237.756  1.00 41.16           C  
ANISOU 2395  C   ASN A 306     4460   7738   3439   -611    -33     77       C  
ATOM   2396  O   ASN A 306      48.142 117.541 236.683  1.00 41.87           O  
ANISOU 2396  O   ASN A 306     4500   7851   3559   -667     11    110       O  
ATOM   2397  CB  ASN A 306      45.502 116.352 236.786  1.00 38.07           C  
ANISOU 2397  CB  ASN A 306     4227   7194   3045   -489     41    132       C  
ATOM   2398  CG  ASN A 306      44.944 117.787 236.960  1.00 37.61           C  
ANISOU 2398  CG  ASN A 306     4239   7029   3024   -585     53    124       C  
ATOM   2399  OD1 ASN A 306      44.868 118.315 238.046  1.00 36.95           O  
ANISOU 2399  OD1 ASN A 306     4193   6908   2936   -621     18     81       O  
ATOM   2400  ND2 ASN A 306      44.519 118.384 235.872  1.00 39.00           N  
ANISOU 2400  ND2 ASN A 306     4438   7149   3231   -620    103    167       N  
ATOM   2401  N   LYS A 307      48.189 117.484 238.941  1.00 42.49           N  
ANISOU 2401  N   LYS A 307     4621   7926   3597   -660    -95     30       N  
ATOM   2402  CA  LYS A 307      49.178 118.571 239.066  1.00 44.25           C  
ANISOU 2402  CA  LYS A 307     4777   8188   3847   -795   -118     10       C  
ATOM   2403  C   LYS A 307      50.472 118.259 238.338  1.00 45.52           C  
ANISOU 2403  C   LYS A 307     4786   8492   4020   -811   -111     33       C  
ATOM   2404  O   LYS A 307      50.789 117.090 238.102  1.00 45.72           O  
ANISOU 2404  O   LYS A 307     4750   8601   4020   -703   -110     49       O  
ATOM   2405  CB  LYS A 307      49.490 118.869 240.532  1.00 44.73           C  
ANISOU 2405  CB  LYS A 307     4854   8260   3881   -835   -197    -51       C  
ATOM   2406  CG  LYS A 307      50.304 120.126 240.733  1.00 45.74           C  
ANISOU 2406  CG  LYS A 307     4942   8397   4038   -991   -225    -79       C  
ATOM   2407  CD  LYS A 307      50.622 120.280 242.177  1.00 48.24           C  
ANISOU 2407  CD  LYS A 307     5277   8736   4316  -1021   -310   -143       C  
ATOM   2408  CE  LYS A 307      52.062 120.691 242.344  1.00 51.91           C  
ANISOU 2408  CE  LYS A 307     5608   9321   4793  -1130   -366   -161       C  
ATOM   2409  NZ  LYS A 307      52.456 120.572 243.758  1.00 54.00           N  
ANISOU 2409  NZ  LYS A 307     5876   9636   5005  -1138   -463   -219       N  
ATOM   2410  N   ASP A 308      51.215 119.312 238.004  1.00 46.93           N  
ANISOU 2410  N   ASP A 308     4904   8692   4235   -945   -104     36       N  
ATOM   2411  CA  ASP A 308      52.479 119.190 237.263  1.00 48.64           C  
ANISOU 2411  CA  ASP A 308     4964   9049   4467   -981    -87     62       C  
ATOM   2412  C   ASP A 308      52.345 118.454 235.906  1.00 47.91           C  
ANISOU 2412  C   ASP A 308     4844   8989   4372   -896     -8    116       C  
ATOM   2413  O   ASP A 308      53.176 117.607 235.577  1.00 47.78           O  
ANISOU 2413  O   ASP A 308     4711   9103   4342   -830     -1    126       O  
ATOM   2414  CB  ASP A 308      53.554 118.510 238.125  1.00 49.59           C  
ANISOU 2414  CB  ASP A 308     4965   9314   4562   -946   -162     31       C  
ATOM   2415  CG  ASP A 308      53.596 119.040 239.548  1.00 52.21           C  
ANISOU 2415  CG  ASP A 308     5340   9618   4879  -1010   -250    -27       C  
ATOM   2416  OD1 ASP A 308      53.957 120.234 239.752  1.00 56.08           O  
ANISOU 2416  OD1 ASP A 308     5827  10083   5397  -1160   -269    -48       O  
ATOM   2417  OD2 ASP A 308      53.283 118.248 240.471  1.00 51.96           O  
ANISOU 2417  OD2 ASP A 308     5351   9590   4802   -911   -301    -53       O  
ATOM   2418  N   LYS A 309      51.303 118.781 235.138  1.00 46.87           N  
ANISOU 2418  N   LYS A 309     4819   8740   4250   -895     51    148       N  
ATOM   2419  CA  LYS A 309      51.057 118.179 233.807  1.00 46.58           C  
ANISOU 2419  CA  LYS A 309     4777   8720   4203   -825    124    198       C  
ATOM   2420  C   LYS A 309      50.789 116.656 233.803  1.00 45.13           C  
ANISOU 2420  C   LYS A 309     4596   8574   3977   -661    121    194       C  
ATOM   2421  O   LYS A 309      50.829 116.017 232.745  1.00 44.31           O  
ANISOU 2421  O   LYS A 309     4470   8509   3856   -599    176    224       O  
ATOM   2422  CB  LYS A 309      52.160 118.508 232.787  1.00 47.80           C  
ANISOU 2422  CB  LYS A 309     4806   8982   4372   -897    176    233       C  
ATOM   2423  CG  LYS A 309      52.744 119.917 232.836  1.00 51.93           C  
ANISOU 2423  CG  LYS A 309     5296   9496   4938  -1072    173    238       C  
ATOM   2424  CD  LYS A 309      51.770 121.014 232.395  1.00 55.22           C  
ANISOU 2424  CD  LYS A 309     5846   9755   5381  -1150    206    267       C  
ATOM   2425  CE  LYS A 309      52.348 122.411 232.743  1.00 58.61           C  
ANISOU 2425  CE  LYS A 309     6261  10156   5854  -1326    185    259       C  
ATOM   2426  NZ  LYS A 309      52.633 122.585 234.229  1.00 59.89           N  
ANISOU 2426  NZ  LYS A 309     6418  10318   6018  -1358     96    189       N  
ATOM   2427  N   CYS A 310      50.498 116.086 234.975  1.00 43.86           N  
ANISOU 2427  N   CYS A 310     4473   8396   3795   -595     59    156       N  
ATOM   2428  CA  CYS A 310      50.119 114.675 235.047  1.00 42.51           C  
ANISOU 2428  CA  CYS A 310     4330   8236   3586   -446     53    155       C  
ATOM   2429  C   CYS A 310      48.634 114.413 234.678  1.00 41.48           C  
ANISOU 2429  C   CYS A 310     4338   7976   3446   -395     84    174       C  
ATOM   2430  O   CYS A 310      47.810 114.081 235.556  1.00 40.22           O  
ANISOU 2430  O   CYS A 310     4264   7746   3270   -349     49    155       O  
ATOM   2431  CB  CYS A 310      50.451 114.118 236.429  1.00 42.84           C  
ANISOU 2431  CB  CYS A 310     4355   8318   3604   -396    -27    116       C  
ATOM   2432  SG  CYS A 310      52.188 114.229 236.869  1.00 41.94           S  
ANISOU 2432  SG  CYS A 310     4064   8374   3497   -438    -76     96       S  
ATOM   2433  N   VAL A 311      48.318 114.541 233.380  1.00 40.86           N  
ANISOU 2433  N   VAL A 311     4276   7876   3374   -403    149    213       N  
ATOM   2434  CA  VAL A 311      46.919 114.503 232.890  1.00 39.88           C  
ANISOU 2434  CA  VAL A 311     4272   7633   3246   -377    176    238       C  
ATOM   2435  C   VAL A 311      46.095 113.272 233.266  1.00 38.78           C  
ANISOU 2435  C   VAL A 311     4203   7455   3075   -260    156    229       C  
ATOM   2436  O   VAL A 311      44.928 113.393 233.618  1.00 38.18           O  
ANISOU 2436  O   VAL A 311     4223   7279   3004   -254    149    232       O  
ATOM   2437  CB  VAL A 311      46.809 114.713 231.353  1.00 39.68           C  
ANISOU 2437  CB  VAL A 311     4247   7609   3221   -398    244    284       C  
ATOM   2438  CG1 VAL A 311      47.403 116.048 230.971  1.00 42.48           C  
ANISOU 2438  CG1 VAL A 311     4556   7974   3609   -528    268    304       C  
ATOM   2439  CG2 VAL A 311      47.510 113.604 230.592  1.00 39.42           C  
ANISOU 2439  CG2 VAL A 311     4148   7677   3152   -315    273    288       C  
ATOM   2440  N   ASN A 312      46.686 112.092 233.148  1.00 39.02           N  
ANISOU 2440  N   ASN A 312     4187   7563   3075   -167    152    221       N  
ATOM   2441  CA  ASN A 312      45.995 110.861 233.495  1.00 38.70           C  
ANISOU 2441  CA  ASN A 312     4216   7483   3005    -60    132    214       C  
ATOM   2442  C   ASN A 312      45.982 110.606 235.001  1.00 38.72           C  
ANISOU 2442  C   ASN A 312     4236   7479   2998    -35     68    185       C  
ATOM   2443  O   ASN A 312      45.330 109.668 235.454  1.00 37.96           O  
ANISOU 2443  O   ASN A 312     4208   7338   2876     42     48    183       O  
ATOM   2444  CB  ASN A 312      46.642 109.669 232.783  1.00 39.60           C  
ANISOU 2444  CB  ASN A 312     4287   7672   3089     38    152    215       C  
ATOM   2445  CG  ASN A 312      46.323 109.613 231.308  1.00 40.96           C  
ANISOU 2445  CG  ASN A 312     4482   7831   3251     37    214    243       C  
ATOM   2446  OD1 ASN A 312      45.689 110.508 230.754  1.00 43.13           O  
ANISOU 2446  OD1 ASN A 312     4795   8049   3542    -40    241    268       O  
ATOM   2447  ND2 ASN A 312      46.749 108.541 230.660  1.00 42.85           N  
ANISOU 2447  ND2 ASN A 312     4703   8119   3458    129    237    237       N  
ATOM   2448  N   GLY A 313      46.730 111.418 235.760  1.00 39.27           N  
ANISOU 2448  N   GLY A 313     4245   7593   3082   -104     35    162       N  
ATOM   2449  CA  GLY A 313      46.742 111.343 237.213  1.00 39.37           C  
ANISOU 2449  CA  GLY A 313     4278   7602   3077    -95    -28    132       C  
ATOM   2450  C   GLY A 313      47.958 110.666 237.845  1.00 40.59           C  
ANISOU 2450  C   GLY A 313     4340   7872   3209    -41    -80    114       C  
ATOM   2451  O   GLY A 313      48.648 109.850 237.214  1.00 41.71           O  
ANISOU 2451  O   GLY A 313     4416   8088   3344     32    -66    125       O  
ATOM   2452  N   LYS A 314      48.229 111.027 239.097  1.00 40.30           N  
ANISOU 2452  N   LYS A 314     4300   7852   3160    -75   -142     85       N  
ATOM   2453  CA  LYS A 314      49.304 110.437 239.884  1.00 40.99           C  
ANISOU 2453  CA  LYS A 314     4306   8047   3222    -25   -207     70       C  
ATOM   2454  C   LYS A 314      48.871 110.492 241.364  1.00 41.17           C  
ANISOU 2454  C   LYS A 314     4405   8030   3207    -30   -270     45       C  
ATOM   2455  O   LYS A 314      48.213 111.442 241.791  1.00 41.31           O  
ANISOU 2455  O   LYS A 314     4492   7973   3231   -113   -267     25       O  
ATOM   2456  CB  LYS A 314      50.626 111.192 239.665  1.00 41.74           C  
ANISOU 2456  CB  LYS A 314     4259   8255   3344   -105   -220     59       C  
ATOM   2457  CG  LYS A 314      50.611 112.625 240.158  1.00 41.15           C  
ANISOU 2457  CG  LYS A 314     4195   8149   3290   -250   -239     32       C  
ATOM   2458  CD  LYS A 314      51.926 113.357 239.974  1.00 41.74           C  
ANISOU 2458  CD  LYS A 314     4128   8338   3395   -344   -256     23       C  
ATOM   2459  CE  LYS A 314      51.846 114.723 240.704  1.00 42.34           C  
ANISOU 2459  CE  LYS A 314     4241   8364   3483   -488   -290    -12       C  
ATOM   2460  NZ  LYS A 314      53.130 115.445 240.895  1.00 42.71           N  
ANISOU 2460  NZ  LYS A 314     4157   8520   3551   -596   -333    -30       N  
ATOM   2461  N   VAL A 315      49.211 109.472 242.137  1.00 41.13           N  
ANISOU 2461  N   VAL A 315     4396   8072   3159     64   -325     46       N  
ATOM   2462  CA  VAL A 315      48.772 109.439 243.515  1.00 41.02           C  
ANISOU 2462  CA  VAL A 315     4462   8024   3098     66   -381     27       C  
ATOM   2463  C   VAL A 315      49.968 109.695 244.431  1.00 42.85           C  
ANISOU 2463  C   VAL A 315     4604   8369   3307     37   -467      1       C  
ATOM   2464  O   VAL A 315      51.029 109.046 244.351  1.00 44.18           O  
ANISOU 2464  O   VAL A 315     4666   8646   3472    101   -504     12       O  
ATOM   2465  CB  VAL A 315      47.918 108.175 243.856  1.00 39.97           C  
ANISOU 2465  CB  VAL A 315     4434   7828   2925    179   -380     53       C  
ATOM   2466  CG1 VAL A 315      48.667 106.926 243.600  1.00 41.01           C  
ANISOU 2466  CG1 VAL A 315     4508   8028   3044    298   -401     77       C  
ATOM   2467  CG2 VAL A 315      47.472 108.209 245.258  1.00 38.48           C  
ANISOU 2467  CG2 VAL A 315     4328   7611   2682    172   -429     37       C  
ATOM   2468  N   VAL A 316      49.778 110.691 245.281  1.00 42.80           N  
ANISOU 2468  N   VAL A 316     4640   8336   3286    -60   -498    -37       N  
ATOM   2469  CA  VAL A 316      50.835 111.282 246.041  1.00 43.18           C  
ANISOU 2469  CA  VAL A 316     4607   8481   3320   -130   -576    -70       C  
ATOM   2470  C   VAL A 316      50.536 110.977 247.497  1.00 43.08           C  
ANISOU 2470  C   VAL A 316     4681   8458   3231   -101   -645    -89       C  
ATOM   2471  O   VAL A 316      49.423 110.571 247.839  1.00 41.22           O  
ANISOU 2471  O   VAL A 316     4570   8128   2964    -53   -616    -79       O  
ATOM   2472  CB  VAL A 316      50.841 112.787 245.745  1.00 43.21           C  
ANISOU 2472  CB  VAL A 316     4602   8448   3367   -281   -550   -103       C  
ATOM   2473  CG1 VAL A 316      50.412 113.611 246.963  1.00 44.33           C  
ANISOU 2473  CG1 VAL A 316     4841   8534   3468   -359   -593   -153       C  
ATOM   2474  CG2 VAL A 316      52.173 113.188 245.302  1.00 44.83           C  
ANISOU 2474  CG2 VAL A 316     4651   8773   3609   -343   -576   -105       C  
ATOM   2475  N   LEU A 317      51.535 111.177 248.349  1.00 44.75           N  
ANISOU 2475  N   LEU A 317     4822   8772   3410   -135   -737   -115       N  
ATOM   2476  CA  LEU A 317      51.405 110.939 249.792  1.00 45.80           C  
ANISOU 2476  CA  LEU A 317     5032   8914   3458   -115   -814   -134       C  
ATOM   2477  C   LEU A 317      51.948 112.127 250.605  1.00 47.15           C  
ANISOU 2477  C   LEU A 317     5186   9123   3607   -249   -882   -195       C  
ATOM   2478  O   LEU A 317      53.086 112.577 250.406  1.00 48.11           O  
ANISOU 2478  O   LEU A 317     5173   9348   3758   -315   -929   -208       O  
ATOM   2479  CB  LEU A 317      52.136 109.648 250.143  1.00 46.52           C  
ANISOU 2479  CB  LEU A 317     5061   9104   3510     13   -881    -96       C  
ATOM   2480  CG  LEU A 317      51.613 108.596 251.114  1.00 47.02           C  
ANISOU 2480  CG  LEU A 317     5233   9141   3493    119   -918    -70       C  
ATOM   2481  CD1 LEU A 317      52.338 107.284 250.825  1.00 46.60           C  
ANISOU 2481  CD1 LEU A 317     5100   9165   3442    260   -949    -18       C  
ATOM   2482  CD2 LEU A 317      51.821 109.039 252.592  1.00 49.82           C  
ANISOU 2482  CD2 LEU A 317     5633   9535   3762     64  -1012   -109       C  
ATOM   2483  N   THR A 318      51.124 112.646 251.507  1.00 47.71           N  
ANISOU 2483  N   THR A 318     5392   9111   3625   -294   -884   -234       N  
ATOM   2484  CA  THR A 318      51.525 113.779 252.325  1.00 49.83           C  
ANISOU 2484  CA  THR A 318     5672   9397   3864   -422   -946   -300       C  
ATOM   2485  C   THR A 318      50.910 113.732 253.699  1.00 50.12           C  
ANISOU 2485  C   THR A 318     5847   9397   3800   -410   -985   -333       C  
ATOM   2486  O   THR A 318      50.149 112.826 253.995  1.00 49.09           O  
ANISOU 2486  O   THR A 318     5800   9227   3626   -306   -959   -297       O  
ATOM   2487  CB  THR A 318      51.195 115.136 251.646  1.00 49.88           C  
ANISOU 2487  CB  THR A 318     5699   9314   3941   -549   -879   -336       C  
ATOM   2488  OG1 THR A 318      51.757 116.212 252.434  1.00 53.44           O  
ANISOU 2488  OG1 THR A 318     6153   9787   4364   -681   -951   -404       O  
ATOM   2489  CG2 THR A 318      49.680 115.328 251.474  1.00 47.41           C  
ANISOU 2489  CG2 THR A 318     5534   8845   3635   -524   -780   -335       C  
ATOM   2490  N   LYS A 319      51.240 114.722 254.527  1.00 52.18           N  
ANISOU 2490  N   LYS A 319     6136   9670   4021   -523  -1045   -401       N  
ATOM   2491  CA  LYS A 319      50.764 114.764 255.924  1.00 53.67           C  
ANISOU 2491  CA  LYS A 319     6458   9836   4097   -522  -1089   -442       C  
ATOM   2492  C   LYS A 319      49.743 115.863 256.218  1.00 53.78           C  
ANISOU 2492  C   LYS A 319     6616   9715   4103   -599  -1023   -504       C  
ATOM   2493  O   LYS A 319      49.727 116.899 255.563  1.00 54.34           O  
ANISOU 2493  O   LYS A 319     6673   9725   4247   -694   -981   -535       O  
ATOM   2494  CB  LYS A 319      51.934 114.810 256.895  1.00 54.66           C  
ANISOU 2494  CB  LYS A 319     6522  10095   4152   -566  -1228   -473       C  
ATOM   2495  CG  LYS A 319      52.654 113.485 256.972  1.00 56.55           C  
ANISOU 2495  CG  LYS A 319     6665  10456   4367   -446  -1295   -405       C  
ATOM   2496  CD  LYS A 319      54.180 113.664 256.997  1.00 61.70           C  
ANISOU 2496  CD  LYS A 319     7145  11264   5035   -502  -1408   -414       C  
ATOM   2497  CE  LYS A 319      54.928 112.301 256.918  1.00 64.46           C  
ANISOU 2497  CE  LYS A 319     7382  11735   5376   -361  -1466   -339       C  
ATOM   2498  NZ  LYS A 319      56.435 112.393 257.112  1.00 64.90           N  
ANISOU 2498  NZ  LYS A 319     7260  11962   5435   -402  -1589   -344       N  
ATOM   2499  N   ARG A 320      48.879 115.604 257.195  1.00 54.26           N  
ANISOU 2499  N   ARG A 320     6815   9727   4073   -552  -1011   -519       N  
ATOM   2500  CA  ARG A 320      47.793 116.507 257.576  1.00 54.38           C  
ANISOU 2500  CA  ARG A 320     6977   9616   4070   -598   -939   -576       C  
ATOM   2501  C   ARG A 320      48.355 117.845 258.010  1.00 55.40           C  
ANISOU 2501  C   ARG A 320     7123   9737   4189   -740   -991   -666       C  
ATOM   2502  O   ARG A 320      47.731 118.900 257.847  1.00 55.46           O  
ANISOU 2502  O   ARG A 320     7211   9629   4232   -805   -926   -716       O  
ATOM   2503  CB  ARG A 320      46.980 115.900 258.727  1.00 54.31           C  
ANISOU 2503  CB  ARG A 320     7100   9591   3945   -523   -932   -576       C  
ATOM   2504  CG  ARG A 320      45.583 116.485 258.814  1.00 55.92           C  
ANISOU 2504  CG  ARG A 320     7439   9658   4152   -521   -818   -605       C  
ATOM   2505  CD  ARG A 320      45.020 116.487 260.228  1.00 59.85           C  
ANISOU 2505  CD  ARG A 320     8078  10146   4515   -506   -825   -650       C  
ATOM   2506  NE  ARG A 320      43.992 115.466 260.454  1.00 61.41           N  
ANISOU 2506  NE  ARG A 320     8341  10319   4672   -396   -758   -588       N  
ATOM   2507  CZ  ARG A 320      42.726 115.724 260.787  1.00 62.11           C  
ANISOU 2507  CZ  ARG A 320     8545  10316   4736   -372   -658   -605       C  
ATOM   2508  NH1 ARG A 320      42.304 116.980 260.914  1.00 61.42           N  
ANISOU 2508  NH1 ARG A 320     8529  10145   4663   -439   -611   -685       N  
ATOM   2509  NH2 ARG A 320      41.880 114.718 261.007  1.00 62.41           N  
ANISOU 2509  NH2 ARG A 320     8631  10347   4737   -281   -604   -542       N  
ATOM   2510  N   SER A 321      49.549 117.766 258.563  1.00 56.42           N  
ANISOU 2510  N   SER A 321     7175   9990   4271   -786  -1113   -685       N  
ATOM   2511  CA  SER A 321      50.210 118.882 259.167  1.00 57.99           C  
ANISOU 2511  CA  SER A 321     7390  10203   4439   -926  -1189   -772       C  
ATOM   2512  C   SER A 321      50.968 119.719 258.156  1.00 58.52           C  
ANISOU 2512  C   SER A 321     7341  10272   4620  -1039  -1191   -780       C  
ATOM   2513  O   SER A 321      51.240 120.877 258.427  1.00 60.12           O  
ANISOU 2513  O   SER A 321     7583  10436   4825  -1171  -1220   -856       O  
ATOM   2514  CB  SER A 321      51.191 118.358 260.193  1.00 59.22           C  
ANISOU 2514  CB  SER A 321     7501  10507   4492   -926  -1330   -780       C  
ATOM   2515  OG  SER A 321      51.972 117.334 259.614  1.00 58.33           O  
ANISOU 2515  OG  SER A 321     7230  10512   4421   -850  -1371   -699       O  
ATOM   2516  N   ALA A 322      51.342 119.134 257.018  1.00 57.32           N  
ANISOU 2516  N   ALA A 322     7051  10169   4559   -990  -1162   -704       N  
ATOM   2517  CA  ALA A 322      52.020 119.868 255.948  1.00 57.03           C  
ANISOU 2517  CA  ALA A 322     6900  10137   4632  -1092  -1148   -699       C  
ATOM   2518  C   ALA A 322      51.409 119.434 254.598  1.00 55.24           C  
ANISOU 2518  C   ALA A 322     6638   9852   4500  -1011  -1030   -624       C  
ATOM   2519  O   ALA A 322      52.054 118.775 253.751  1.00 54.40           O  
ANISOU 2519  O   ALA A 322     6388   9834   4447   -967  -1030   -561       O  
ATOM   2520  CB  ALA A 322      53.526 119.653 256.013  1.00 58.19           C  
ANISOU 2520  CB  ALA A 322     6874  10455   4780  -1143  -1263   -690       C  
ATOM   2521  N   PRO A 323      50.129 119.789 254.419  1.00 54.02           N  
ANISOU 2521  N   PRO A 323     6616   9549   4361   -984   -930   -631       N  
ATOM   2522  CA  PRO A 323      49.310 119.237 253.362  1.00 52.61           C  
ANISOU 2522  CA  PRO A 323     6434   9309   4245   -888   -825   -562       C  
ATOM   2523  C   PRO A 323      49.569 119.803 251.949  1.00 52.66           C  
ANISOU 2523  C   PRO A 323     6356   9287   4366   -949   -768   -530       C  
ATOM   2524  O   PRO A 323      48.904 119.379 250.997  1.00 51.50           O  
ANISOU 2524  O   PRO A 323     6207   9091   4270   -875   -684   -473       O  
ATOM   2525  CB  PRO A 323      47.891 119.534 253.855  1.00 51.83           C  
ANISOU 2525  CB  PRO A 323     6507   9074   4114   -852   -753   -590       C  
ATOM   2526  CG  PRO A 323      48.014 120.733 254.674  1.00 52.01           C  
ANISOU 2526  CG  PRO A 323     6614   9048   4102   -967   -789   -681       C  
ATOM   2527  CD  PRO A 323      49.355 120.685 255.300  1.00 53.97           C  
ANISOU 2527  CD  PRO A 323     6775   9430   4302  -1035   -914   -709       C  
ATOM   2528  N   THR A 324      50.519 120.727 251.795  1.00 54.08           N  
ANISOU 2528  N   THR A 324     6467   9499   4580  -1084   -813   -563       N  
ATOM   2529  CA  THR A 324      50.893 121.148 250.440  1.00 54.24           C  
ANISOU 2529  CA  THR A 324     6393   9514   4701  -1141   -761   -521       C  
ATOM   2530  C   THR A 324      52.162 120.470 249.922  1.00 55.11           C  
ANISOU 2530  C   THR A 324     6317   9789   4835  -1133   -807   -476       C  
ATOM   2531  O   THR A 324      52.517 120.622 248.746  1.00 55.47           O  
ANISOU 2531  O   THR A 324     6270   9851   4955  -1162   -757   -431       O  
ATOM   2532  CB  THR A 324      50.959 122.689 250.249  1.00 55.21           C  
ANISOU 2532  CB  THR A 324     6565   9537   4873  -1299   -746   -569       C  
ATOM   2533  OG1 THR A 324      51.839 123.290 251.209  1.00 55.44           O  
ANISOU 2533  OG1 THR A 324     6583   9621   4860  -1417   -849   -638       O  
ATOM   2534  CG2 THR A 324      49.574 123.288 250.361  1.00 53.75           C  
ANISOU 2534  CG2 THR A 324     6553   9177   4692  -1276   -668   -593       C  
ATOM   2535  N   ASP A 325      52.826 119.716 250.793  1.00 55.95           N  
ANISOU 2535  N   ASP A 325     6367  10018   4873  -1087   -900   -484       N  
ATOM   2536  CA  ASP A 325      54.016 118.965 250.415  1.00 56.92           C  
ANISOU 2536  CA  ASP A 325     6308  10306   5013  -1055   -948   -441       C  
ATOM   2537  C   ASP A 325      53.629 117.688 249.696  1.00 55.08           C  
ANISOU 2537  C   ASP A 325     6047  10089   4792   -892   -887   -370       C  
ATOM   2538  O   ASP A 325      53.208 116.706 250.312  1.00 54.04           O  
ANISOU 2538  O   ASP A 325     5970   9964   4599   -771   -907   -356       O  
ATOM   2539  CB  ASP A 325      54.884 118.643 251.640  1.00 59.10           C  
ANISOU 2539  CB  ASP A 325     6534  10709   5211  -1062  -1079   -474       C  
ATOM   2540  CG  ASP A 325      56.255 118.073 251.257  1.00 62.75           C  
ANISOU 2540  CG  ASP A 325     6787  11353   5702  -1048  -1137   -435       C  
ATOM   2541  OD1 ASP A 325      56.878 118.595 250.298  1.00 67.25           O  
ANISOU 2541  OD1 ASP A 325     7243  11959   6351  -1132  -1103   -417       O  
ATOM   2542  OD2 ASP A 325      56.715 117.105 251.915  1.00 64.74           O  
ANISOU 2542  OD2 ASP A 325     6988  11714   5896   -950  -1215   -418       O  
ATOM   2543  N   TRP A 326      53.777 117.718 248.377  1.00 54.45           N  
ANISOU 2543  N   TRP A 326     5888  10011   4789   -895   -812   -324       N  
ATOM   2544  CA  TRP A 326      53.378 116.600 247.541  1.00 52.98           C  
ANISOU 2544  CA  TRP A 326     5684   9826   4619   -752   -746   -262       C  
ATOM   2545  C   TRP A 326      54.545 116.011 246.793  1.00 53.22           C  
ANISOU 2545  C   TRP A 326     5534  10003   4685   -718   -754   -221       C  
ATOM   2546  O   TRP A 326      54.379 115.496 245.690  1.00 52.77           O  
ANISOU 2546  O   TRP A 326     5444   9941   4666   -649   -678   -175       O  
ATOM   2547  CB  TRP A 326      52.322 117.043 246.548  1.00 52.08           C  
ANISOU 2547  CB  TRP A 326     5657   9574   4556   -762   -635   -241       C  
ATOM   2548  CG  TRP A 326      51.012 117.409 247.184  1.00 51.83           C  
ANISOU 2548  CG  TRP A 326     5802   9399   4494   -757   -610   -270       C  
ATOM   2549  CD1 TRP A 326      50.683 117.323 248.503  1.00 51.08           C  
ANISOU 2549  CD1 TRP A 326     5797   9286   4326   -741   -666   -313       C  
ATOM   2550  CD2 TRP A 326      49.844 117.876 246.508  1.00 51.43           C  
ANISOU 2550  CD2 TRP A 326     5852   9208   4482   -759   -518   -256       C  
ATOM   2551  NE1 TRP A 326      49.400 117.742 248.696  1.00 50.87           N  
ANISOU 2551  NE1 TRP A 326     5917   9118   4292   -735   -608   -329       N  
ATOM   2552  CE2 TRP A 326      48.852 118.078 247.486  1.00 51.00           C  
ANISOU 2552  CE2 TRP A 326     5940   9058   4380   -743   -520   -294       C  
ATOM   2553  CE3 TRP A 326      49.541 118.156 245.170  1.00 51.69           C  
ANISOU 2553  CE3 TRP A 326     5869   9191   4582   -772   -436   -213       C  
ATOM   2554  CZ2 TRP A 326      47.568 118.553 247.171  1.00 49.45           C  
ANISOU 2554  CZ2 TRP A 326     5860   8721   4209   -735   -441   -290       C  
ATOM   2555  CZ3 TRP A 326      48.254 118.620 244.859  1.00 50.63           C  
ANISOU 2555  CZ3 TRP A 326     5855   8912   4468   -766   -366   -207       C  
ATOM   2556  CH2 TRP A 326      47.294 118.816 245.862  1.00 48.32           C  
ANISOU 2556  CH2 TRP A 326     5693   8531   4136   -746   -369   -245       C  
ATOM   2557  N   GLY A 327      55.729 116.095 247.393  1.00 53.96           N  
ANISOU 2557  N   GLY A 327     5507  10231   4763   -766   -848   -241       N  
ATOM   2558  CA  GLY A 327      56.937 115.603 246.762  1.00 53.56           C  
ANISOU 2558  CA  GLY A 327     5266  10337   4748   -737   -861   -205       C  
ATOM   2559  C   GLY A 327      57.028 114.095 246.820  1.00 52.55           C  
ANISOU 2559  C   GLY A 327     5107  10274   4587   -550   -874   -166       C  
ATOM   2560  O   GLY A 327      57.759 113.497 246.041  1.00 52.92           O  
ANISOU 2560  O   GLY A 327     5018  10422   4668   -483   -849   -128       O  
ATOM   2561  N   THR A 328      56.304 113.475 247.747  1.00 51.46           N  
ANISOU 2561  N   THR A 328     5095  10076   4383   -463   -910   -173       N  
ATOM   2562  CA  THR A 328      56.336 112.022 247.858  1.00 50.72           C  
ANISOU 2562  CA  THR A 328     4992  10025   4255   -285   -925   -132       C  
ATOM   2563  C   THR A 328      55.325 111.465 246.921  1.00 48.97           C  
ANISOU 2563  C   THR A 328     4859   9691   4056   -200   -817    -98       C  
ATOM   2564  O   THR A 328      54.158 111.794 247.007  1.00 48.19           O  
ANISOU 2564  O   THR A 328     4907   9456   3947   -225   -770   -110       O  
ATOM   2565  CB  THR A 328      55.940 111.525 249.215  1.00 50.79           C  
ANISOU 2565  CB  THR A 328     5108  10013   4178   -228  -1004   -144       C  
ATOM   2566  OG1 THR A 328      56.381 112.456 250.212  1.00 51.79           O  
ANISOU 2566  OG1 THR A 328     5228  10181   4270   -355  -1093   -196       O  
ATOM   2567  CG2 THR A 328      56.541 110.130 249.423  1.00 51.12           C  
ANISOU 2567  CG2 THR A 328     5080  10151   4190    -64  -1055   -100       C  
ATOM   2568  N   VAL A 329      55.760 110.614 246.015  1.00 48.85           N  
ANISOU 2568  N   VAL A 329     4756   9734   4072    -97   -776    -58       N  
ATOM   2569  CA  VAL A 329      54.862 110.141 245.001  1.00 47.28           C  
ANISOU 2569  CA  VAL A 329     4635   9434   3896    -30   -675    -30       C  
ATOM   2570  C   VAL A 329      54.757 108.659 245.160  1.00 47.04           C  
ANISOU 2570  C   VAL A 329     4634   9409   3831    143   -689      2       C  
ATOM   2571  O   VAL A 329      55.757 107.976 245.137  1.00 48.38           O  
ANISOU 2571  O   VAL A 329     4686   9695   4001    227   -727     19       O  
ATOM   2572  CB  VAL A 329      55.358 110.532 243.600  1.00 47.80           C  
ANISOU 2572  CB  VAL A 329     4592   9542   4028    -72   -595    -14       C  
ATOM   2573  CG1 VAL A 329      54.509 109.843 242.513  1.00 46.17           C  
ANISOU 2573  CG1 VAL A 329     4463   9246   3834     17   -498     17       C  
ATOM   2574  CG2 VAL A 329      55.334 112.067 243.433  1.00 47.19           C  
ANISOU 2574  CG2 VAL A 329     4511   9433   3987   -255   -577    -41       C  
ATOM   2575  N   LEU A 330      53.546 108.160 245.348  1.00 45.93           N  
ANISOU 2575  N   LEU A 330     4651   9141   3660    196   -659     13       N  
ATOM   2576  CA  LEU A 330      53.361 106.744 245.569  1.00 46.15           C  
ANISOU 2576  CA  LEU A 330     4729   9154   3652    352   -674     46       C  
ATOM   2577  C   LEU A 330      53.271 106.008 244.248  1.00 46.23           C  
ANISOU 2577  C   LEU A 330     4722   9143   3699    439   -592     73       C  
ATOM   2578  O   LEU A 330      54.110 105.165 243.955  1.00 47.35           O  
ANISOU 2578  O   LEU A 330     4775   9368   3846    547   -606     91       O  
ATOM   2579  CB  LEU A 330      52.111 106.494 246.395  1.00 45.45           C  
ANISOU 2579  CB  LEU A 330     4814   8943   3512    364   -679     48       C  
ATOM   2580  CG  LEU A 330      51.923 105.021 246.736  1.00 45.29           C  
ANISOU 2580  CG  LEU A 330     4857   8901   3449    516   -702     86       C  
ATOM   2581  CD1 LEU A 330      52.900 104.605 247.826  1.00 46.94           C  
ANISOU 2581  CD1 LEU A 330     5006   9219   3610    571   -812     92       C  
ATOM   2582  CD2 LEU A 330      50.503 104.757 247.159  1.00 43.62           C  
ANISOU 2582  CD2 LEU A 330     4818   8553   3203    519   -671     97       C  
ATOM   2583  N   ILE A 331      52.242 106.324 243.460  1.00 45.61           N  
ANISOU 2583  N   ILE A 331     4731   8954   3644    395   -509     75       N  
ATOM   2584  CA  ILE A 331      52.117 105.836 242.073  1.00 45.24           C  
ANISOU 2584  CA  ILE A 331     4673   8886   3631    450   -426     94       C  
ATOM   2585  C   ILE A 331      52.336 106.945 241.050  1.00 45.25           C  
ANISOU 2585  C   ILE A 331     4602   8909   3682    337   -363     84       C  
ATOM   2586  O   ILE A 331      51.534 107.891 241.015  1.00 44.27           O  
ANISOU 2586  O   ILE A 331     4548   8702   3571    230   -336     74       O  
ATOM   2587  CB  ILE A 331      50.747 105.252 241.832  1.00 43.71           C  
ANISOU 2587  CB  ILE A 331     4636   8551   3423    490   -380    110       C  
ATOM   2588  CG1 ILE A 331      50.660 103.912 242.534  1.00 44.63           C  
ANISOU 2588  CG1 ILE A 331     4816   8648   3494    621   -426    130       C  
ATOM   2589  CG2 ILE A 331      50.522 105.048 240.369  1.00 43.26           C  
ANISOU 2589  CG2 ILE A 331     4576   8466   3397    510   -295    121       C  
ATOM   2590  CD1 ILE A 331      49.295 103.602 242.998  1.00 44.74           C  
ANISOU 2590  CD1 ILE A 331     4988   8531   3479    620   -416    142       C  
ATOM   2591  N   PRO A 332      53.405 106.828 240.208  1.00 46.26           N  
ANISOU 2591  N   PRO A 332     4592   9148   3838    363   -336     90       N  
ATOM   2592  CA  PRO A 332      53.751 107.923 239.281  1.00 46.44           C  
ANISOU 2592  CA  PRO A 332     4535   9206   3904    246   -278     87       C  
ATOM   2593  C   PRO A 332      52.852 107.950 238.049  1.00 45.72           C  
ANISOU 2593  C   PRO A 332     4525   9020   3825    239   -185    103       C  
ATOM   2594  O   PRO A 332      52.103 106.997 237.803  1.00 44.85           O  
ANISOU 2594  O   PRO A 332     4515   8833   3693    336   -164    115       O  
ATOM   2595  CB  PRO A 332      55.224 107.646 238.915  1.00 47.36           C  
ANISOU 2595  CB  PRO A 332     4469   9487   4038    290   -282     91       C  
ATOM   2596  CG  PRO A 332      55.641 106.433 239.703  1.00 47.36           C  
ANISOU 2596  CG  PRO A 332     4456   9534   4005    438   -350     95       C  
ATOM   2597  CD  PRO A 332      54.357 105.709 240.070  1.00 46.92           C  
ANISOU 2597  CD  PRO A 332     4584   9330   3913    504   -353    102       C  
ATOM   2598  N   HIS A 333      52.900 109.057 237.315  1.00 46.49           N  
ANISOU 2598  N   HIS A 333     4588   9119   3956    119   -135    107       N  
ATOM   2599  CA  HIS A 333      52.014 109.274 236.181  1.00 46.44           C  
ANISOU 2599  CA  HIS A 333     4663   9023   3960     94    -55    125       C  
ATOM   2600  C   HIS A 333      52.470 108.385 235.046  1.00 47.54           C  
ANISOU 2600  C   HIS A 333     4753   9221   4091    193      5    140       C  
ATOM   2601  O   HIS A 333      53.668 108.268 234.814  1.00 49.22           O  
ANISOU 2601  O   HIS A 333     4826   9562   4312    215     11    139       O  
ATOM   2602  CB  HIS A 333      52.069 110.747 235.759  1.00 46.42           C  
ANISOU 2602  CB  HIS A 333     4633   9012   3994    -63    -24    130       C  
ATOM   2603  CG  HIS A 333      51.174 111.106 234.592  1.00 46.06           C  
ANISOU 2603  CG  HIS A 333     4667   8877   3956    -97     53    156       C  
ATOM   2604  ND1 HIS A 333      51.668 111.419 233.341  1.00 43.56           N  
ANISOU 2604  ND1 HIS A 333     4284   8614   3651   -133    123    180       N  
ATOM   2605  CD2 HIS A 333      49.827 111.244 234.503  1.00 44.13           C  
ANISOU 2605  CD2 HIS A 333     4560   8498   3708   -106     67    165       C  
ATOM   2606  CE1 HIS A 333      50.670 111.733 232.538  1.00 41.95           C  
ANISOU 2606  CE1 HIS A 333     4179   8313   3448   -161    171    203       C  
ATOM   2607  NE2 HIS A 333      49.542 111.631 233.214  1.00 41.70           N  
ANISOU 2607  NE2 HIS A 333     4267   8168   3411   -143    137    195       N  
ATOM   2608  N   ASP A 334      51.522 107.732 234.377  1.00 47.58           N  
ANISOU 2608  N   ASP A 334     4869   9133   4076    255     47    151       N  
ATOM   2609  CA  ASP A 334      51.790 106.960 233.166  1.00 48.56           C  
ANISOU 2609  CA  ASP A 334     4974   9293   4185    339    113    159       C  
ATOM   2610  C   ASP A 334      50.954 107.524 232.008  1.00 48.03           C  
ANISOU 2610  C   ASP A 334     4979   9151   4118    269    181    179       C  
ATOM   2611  O   ASP A 334      49.754 107.817 232.181  1.00 46.35           O  
ANISOU 2611  O   ASP A 334     4884   8821   3907    227    171    187       O  
ATOM   2612  CB  ASP A 334      51.491 105.460 233.373  1.00 48.39           C  
ANISOU 2612  CB  ASP A 334     5027   9230   4130    492     93    152       C  
ATOM   2613  CG  ASP A 334      52.056 104.566 232.232  1.00 51.02           C  
ANISOU 2613  CG  ASP A 334     5323   9619   4443    599    156    148       C  
ATOM   2614  OD1 ASP A 334      51.959 104.908 231.021  1.00 51.81           O  
ANISOU 2614  OD1 ASP A 334     5423   9725   4539    560    230    157       O  
ATOM   2615  OD2 ASP A 334      52.611 103.495 232.547  1.00 52.97           O  
ANISOU 2615  OD2 ASP A 334     5546   9904   4676    730    133    137       O  
ATOM   2616  N   ASP A 335      51.609 107.694 230.849  1.00 49.16           N  
ANISOU 2616  N   ASP A 335     5047   9373   4260    258    251    190       N  
ATOM   2617  CA  ASP A 335      50.948 108.122 229.593  1.00 49.09           C  
ANISOU 2617  CA  ASP A 335     5101   9311   4239    205    319    213       C  
ATOM   2618  C   ASP A 335      49.773 107.215 229.247  1.00 48.00           C  
ANISOU 2618  C   ASP A 335     5107   9062   4068    281    322    212       C  
ATOM   2619  O   ASP A 335      48.692 107.699 228.939  1.00 47.13           O  
ANISOU 2619  O   ASP A 335     5092   8855   3959    219    329    231       O  
ATOM   2620  CB  ASP A 335      51.928 108.141 228.405  1.00 50.39           C  
ANISOU 2620  CB  ASP A 335     5164   9591   4390    212    398    223       C  
ATOM   2621  CG  ASP A 335      52.879 109.344 228.425  1.00 53.26           C  
ANISOU 2621  CG  ASP A 335     5396  10051   4790     89    413    238       C  
ATOM   2622  OD1 ASP A 335      52.457 110.412 228.961  1.00 53.90           O  
ANISOU 2622  OD1 ASP A 335     5506  10070   4903    -30    379    248       O  
ATOM   2623  OD2 ASP A 335      54.034 109.214 227.887  1.00 54.24           O  
ANISOU 2623  OD2 ASP A 335     5389  10309   4910    110    461    239       O  
ATOM   2624  N   LYS A 336      49.973 105.901 229.301  1.00 48.26           N  
ANISOU 2624  N   LYS A 336     5157   9106   4073    414    315    191       N  
ATOM   2625  CA  LYS A 336      48.924 104.997 228.847  1.00 47.71           C  
ANISOU 2625  CA  LYS A 336     5225   8934   3971    478    321    188       C  
ATOM   2626  C   LYS A 336      48.006 104.493 229.943  1.00 46.11           C  
ANISOU 2626  C   LYS A 336     5119   8628   3771    505    254    184       C  
ATOM   2627  O   LYS A 336      47.144 103.656 229.698  1.00 45.74           O  
ANISOU 2627  O   LYS A 336     5185   8496   3700    555    251    182       O  
ATOM   2628  CB  LYS A 336      49.422 103.867 227.899  1.00 49.18           C  
ANISOU 2628  CB  LYS A 336     5411   9161   4114    597    370    169       C  
ATOM   2629  CG  LYS A 336      50.716 103.136 228.268  1.00 52.41           C  
ANISOU 2629  CG  LYS A 336     5714   9677   4523    709    366    146       C  
ATOM   2630  CD  LYS A 336      51.878 103.485 227.305  1.00 54.56           C  
ANISOU 2630  CD  LYS A 336     5856  10086   4790    707    443    145       C  
ATOM   2631  CE  LYS A 336      53.164 102.766 227.750  1.00 55.97           C  
ANISOU 2631  CE  LYS A 336     5913  10378   4974    827    435    125       C  
ATOM   2632  NZ  LYS A 336      54.364 103.617 227.567  1.00 57.66           N  
ANISOU 2632  NZ  LYS A 336     5950  10744   5215    767    470    135       N  
ATOM   2633  N   VAL A 337      48.146 105.028 231.144  1.00 45.50           N  
ANISOU 2633  N   VAL A 337     5008   8559   3722    462    200    184       N  
ATOM   2634  CA  VAL A 337      47.196 104.679 232.192  1.00 44.13           C  
ANISOU 2634  CA  VAL A 337     4932   8289   3547    474    145    184       C  
ATOM   2635  C   VAL A 337      46.513 105.894 232.808  1.00 43.75           C  
ANISOU 2635  C   VAL A 337     4906   8190   3528    357    125    195       C  
ATOM   2636  O   VAL A 337      47.180 106.800 233.303  1.00 45.00           O  
ANISOU 2636  O   VAL A 337     4984   8406   3709    291    109    189       O  
ATOM   2637  CB  VAL A 337      47.849 103.829 233.307  1.00 44.38           C  
ANISOU 2637  CB  VAL A 337     4937   8357   3568    567     88    170       C  
ATOM   2638  CG1 VAL A 337      46.855 103.581 234.399  1.00 42.69           C  
ANISOU 2638  CG1 VAL A 337     4825   8048   3347    564     37    176       C  
ATOM   2639  CG2 VAL A 337      48.325 102.495 232.769  1.00 44.38           C  
ANISOU 2639  CG2 VAL A 337     4944   8377   3540    702    105    159       C  
ATOM   2640  N   THR A 338      45.183 105.896 232.783  1.00 43.00           N  
ANISOU 2640  N   THR A 338     4920   7987   3431    332    125    209       N  
ATOM   2641  CA  THR A 338      44.357 106.867 233.516  1.00 42.38           C  
ANISOU 2641  CA  THR A 338     4881   7844   3377    246    105    216       C  
ATOM   2642  C   THR A 338      43.941 106.270 234.863  1.00 41.96           C  
ANISOU 2642  C   THR A 338     4883   7751   3310    289     53    207       C  
ATOM   2643  O   THR A 338      43.569 105.091 234.907  1.00 42.08           O  
ANISOU 2643  O   THR A 338     4959   7730   3299    368     43    210       O  
ATOM   2644  CB  THR A 338      43.074 107.251 232.712  1.00 41.84           C  
ANISOU 2644  CB  THR A 338     4893   7687   3318    198    138    242       C  
ATOM   2645  OG1 THR A 338      43.420 108.089 231.593  1.00 42.43           O  
ANISOU 2645  OG1 THR A 338     4921   7795   3405    138    183    257       O  
ATOM   2646  CG2 THR A 338      42.118 108.027 233.581  1.00 41.48           C  
ANISOU 2646  CG2 THR A 338     4897   7567   3296    138    118    247       C  
ATOM   2647  N   ILE A 339      44.027 107.081 235.934  1.00 41.58           N  
ANISOU 2647  N   ILE A 339     4818   7707   3274    233     21    194       N  
ATOM   2648  CA  ILE A 339      43.529 106.770 237.289  1.00 41.17           C  
ANISOU 2648  CA  ILE A 339     4825   7615   3202    253    -24    187       C  
ATOM   2649  C   ILE A 339      42.299 107.654 237.590  1.00 41.66           C  
ANISOU 2649  C   ILE A 339     4956   7590   3283    179     -9    193       C  
ATOM   2650  O   ILE A 339      42.426 108.879 237.719  1.00 41.40           O  
ANISOU 2650  O   ILE A 339     4895   7559   3276     98     -3    182       O  
ATOM   2651  CB  ILE A 339      44.624 107.045 238.378  1.00 41.89           C  
ANISOU 2651  CB  ILE A 339     4846   7788   3283    248    -77    162       C  
ATOM   2652  CG1 ILE A 339      45.940 106.359 238.034  1.00 41.30           C  
ANISOU 2652  CG1 ILE A 339     4678   7816   3199    318    -89    157       C  
ATOM   2653  CG2 ILE A 339      44.186 106.585 239.779  1.00 40.63           C  
ANISOU 2653  CG2 ILE A 339     4755   7596   3088    279   -125    157       C  
ATOM   2654  CD1 ILE A 339      47.125 107.044 238.613  1.00 40.14           C  
ANISOU 2654  CD1 ILE A 339     4424   7768   3059    275   -128    136       C  
ATOM   2655  N   ASP A 340      41.115 107.044 237.699  1.00 42.53           N  
ANISOU 2655  N   ASP A 340     5154   7621   3383    207     -2    212       N  
ATOM   2656  CA  ASP A 340      39.870 107.816 237.807  1.00 43.91           C  
ANISOU 2656  CA  ASP A 340     5385   7718   3581    150     22    223       C  
ATOM   2657  C   ASP A 340      39.552 108.117 239.245  1.00 44.95           C  
ANISOU 2657  C   ASP A 340     5551   7829   3696    136     -3    205       C  
ATOM   2658  O   ASP A 340      39.040 109.204 239.532  1.00 45.35           O  
ANISOU 2658  O   ASP A 340     5618   7843   3771     76     13    196       O  
ATOM   2659  CB  ASP A 340      38.683 107.111 237.151  1.00 43.65           C  
ANISOU 2659  CB  ASP A 340     5419   7618   3550    174     45    254       C  
ATOM   2660  CG  ASP A 340      38.781 107.098 235.632  1.00 47.32           C  
ANISOU 2660  CG  ASP A 340     5861   8091   4027    168     75    270       C  
ATOM   2661  OD1 ASP A 340      39.186 108.130 235.046  1.00 50.29           O  
ANISOU 2661  OD1 ASP A 340     6189   8490   4428    114     95    270       O  
ATOM   2662  OD2 ASP A 340      38.453 106.056 235.002  1.00 51.49           O  
ANISOU 2662  OD2 ASP A 340     6427   8600   4537    214     78    283       O  
ATOM   2663  N   ASP A 341      39.824 107.163 240.144  1.00 45.74           N  
ANISOU 2663  N   ASP A 341     5673   7951   3754    194    -40    201       N  
ATOM   2664  CA  ASP A 341      39.889 107.501 241.544  1.00 47.15           C  
ANISOU 2664  CA  ASP A 341     5872   8138   3905    180    -70    178       C  
ATOM   2665  C   ASP A 341      40.397 106.409 242.467  1.00 47.21           C  
ANISOU 2665  C   ASP A 341     5897   8183   3860    250   -119    180       C  
ATOM   2666  O   ASP A 341      40.432 105.242 242.069  1.00 47.17           O  
ANISOU 2666  O   ASP A 341     5909   8173   3842    318   -123    203       O  
ATOM   2667  CB  ASP A 341      38.586 108.183 242.023  1.00 48.00           C  
ANISOU 2667  CB  ASP A 341     6045   8169   4022    137    -38    179       C  
ATOM   2668  CG  ASP A 341      37.702 107.278 242.854  1.00 51.41           C  
ANISOU 2668  CG  ASP A 341     6554   8564   4416    178    -40    199       C  
ATOM   2669  OD1 ASP A 341      37.784 106.039 242.648  1.00 53.47           O  
ANISOU 2669  OD1 ASP A 341     6832   8827   4656    238    -54    224       O  
ATOM   2670  OD2 ASP A 341      36.932 107.826 243.711  1.00 53.68           O  
ANISOU 2670  OD2 ASP A 341     6887   8816   4693    151    -23    189       O  
ATOM   2671  N   VAL A 342      40.824 106.799 243.674  1.00 47.08           N  
ANISOU 2671  N   VAL A 342     5879   8200   3809    234   -159    154       N  
ATOM   2672  CA  VAL A 342      41.282 105.854 244.681  1.00 47.57           C  
ANISOU 2672  CA  VAL A 342     5963   8298   3812    298   -212    160       C  
ATOM   2673  C   VAL A 342      40.255 105.659 245.744  1.00 46.81           C  
ANISOU 2673  C   VAL A 342     5964   8148   3675    297   -206    169       C  
ATOM   2674  O   VAL A 342      39.524 106.605 246.068  1.00 47.24           O  
ANISOU 2674  O   VAL A 342     6048   8165   3738    236   -174    151       O  
ATOM   2675  CB  VAL A 342      42.507 106.342 245.487  1.00 48.78           C  
ANISOU 2675  CB  VAL A 342     6054   8541   3939    282   -274    126       C  
ATOM   2676  CG1 VAL A 342      43.772 106.053 244.730  1.00 50.47           C  
ANISOU 2676  CG1 VAL A 342     6164   8836   4176    316   -296    126       C  
ATOM   2677  CG2 VAL A 342      42.375 107.835 245.901  1.00 49.91           C  
ANISOU 2677  CG2 VAL A 342     6193   8675   4094    181   -265     84       C  
ATOM   2678  N   ALA A 343      40.233 104.450 246.313  1.00 45.64           N  
ANISOU 2678  N   ALA A 343     5865   7997   3478    367   -234    199       N  
ATOM   2679  CA  ALA A 343      39.593 104.224 247.612  1.00 44.58           C  
ANISOU 2679  CA  ALA A 343     5815   7839   3283    369   -243    208       C  
ATOM   2680  C   ALA A 343      40.606 103.728 248.665  1.00 44.07           C  
ANISOU 2680  C   ALA A 343     5748   7845   3152    417   -320    206       C  
ATOM   2681  O   ALA A 343      41.470 102.909 248.363  1.00 43.52           O  
ANISOU 2681  O   ALA A 343     5642   7814   3081    485   -360    223       O  
ATOM   2682  CB  ALA A 343      38.392 103.276 247.478  1.00 44.41           C  
ANISOU 2682  CB  ALA A 343     5877   7739   3258    394   -203    255       C  
ATOM   2683  N   VAL A 344      40.508 104.248 249.886  1.00 42.99           N  
ANISOU 2683  N   VAL A 344     5651   7726   2958    384   -340    185       N  
ATOM   2684  CA  VAL A 344      41.504 103.915 250.907  1.00 43.06           C  
ANISOU 2684  CA  VAL A 344     5652   7810   2898    421   -423    181       C  
ATOM   2685  C   VAL A 344      40.973 103.192 252.142  1.00 42.54           C  
ANISOU 2685  C   VAL A 344     5692   7726   2745    454   -439    213       C  
ATOM   2686  O   VAL A 344      40.004 103.616 252.758  1.00 42.36           O  
ANISOU 2686  O   VAL A 344     5740   7662   2692    409   -395    206       O  
ATOM   2687  CB  VAL A 344      42.287 105.144 251.352  1.00 43.61           C  
ANISOU 2687  CB  VAL A 344     5663   7948   2959    354   -461    122       C  
ATOM   2688  CG1 VAL A 344      43.136 104.821 252.614  1.00 44.19           C  
ANISOU 2688  CG1 VAL A 344     5745   8100   2945    385   -553    119       C  
ATOM   2689  CG2 VAL A 344      43.154 105.623 250.216  1.00 43.33           C  
ANISOU 2689  CG2 VAL A 344     5511   7954   2999    335   -464    102       C  
ATOM   2690  N   PHE A 345      41.633 102.109 252.507  1.00 42.26           N  
ANISOU 2690  N   PHE A 345     5667   7724   2668    534   -500    251       N  
ATOM   2691  CA  PHE A 345      41.195 101.336 253.628  1.00 42.71           C  
ANISOU 2691  CA  PHE A 345     5829   7762   2639    568   -518    292       C  
ATOM   2692  C   PHE A 345      42.319 101.218 254.635  1.00 44.35           C  
ANISOU 2692  C   PHE A 345     6019   8061   2770    604   -617    288       C  
ATOM   2693  O   PHE A 345      43.422 101.704 254.391  1.00 45.23           O  
ANISOU 2693  O   PHE A 345     6028   8251   2906    601   -670    254       O  
ATOM   2694  CB  PHE A 345      40.662 100.002 253.145  1.00 41.88           C  
ANISOU 2694  CB  PHE A 345     5782   7583   2548    633   -493    357       C  
ATOM   2695  CG  PHE A 345      39.419 100.137 252.300  1.00 41.48           C  
ANISOU 2695  CG  PHE A 345     5756   7446   2560    585   -401    362       C  
ATOM   2696  CD1 PHE A 345      39.514 100.368 250.914  1.00 40.85           C  
ANISOU 2696  CD1 PHE A 345     5604   7350   2568    577   -370    344       C  
ATOM   2697  CD2 PHE A 345      38.149 100.079 252.882  1.00 40.32           C  
ANISOU 2697  CD2 PHE A 345     5699   7241   2380    546   -345    386       C  
ATOM   2698  CE1 PHE A 345      38.380 100.514 250.141  1.00 37.18           C  
ANISOU 2698  CE1 PHE A 345     5158   6812   2156    533   -295    351       C  
ATOM   2699  CE2 PHE A 345      37.001 100.218 252.094  1.00 38.65           C  
ANISOU 2699  CE2 PHE A 345     5496   6960   2230    502   -266    393       C  
ATOM   2700  CZ  PHE A 345      37.124 100.438 250.732  1.00 37.56           C  
ANISOU 2700  CZ  PHE A 345     5287   6806   2177    496   -247    376       C  
ATOM   2701  N   ALA A 346      42.033 100.622 255.786  1.00 45.45           N  
ANISOU 2701  N   ALA A 346     6257   8197   2817    631   -644    325       N  
ATOM   2702  CA  ALA A 346      43.051 100.399 256.816  1.00 47.06           C  
ANISOU 2702  CA  ALA A 346     6456   8488   2936    672   -747    332       C  
ATOM   2703  C   ALA A 346      44.308  99.687 256.286  1.00 48.09           C  
ANISOU 2703  C   ALA A 346     6497   8676   3101    764   -821    354       C  
ATOM   2704  O   ALA A 346      45.420 100.014 256.689  1.00 49.50           O  
ANISOU 2704  O   ALA A 346     6599   8956   3254    773   -906    331       O  
ATOM   2705  CB  ALA A 346      42.459  99.626 257.972  1.00 47.11           C  
ANISOU 2705  CB  ALA A 346     6595   8467   2837    700   -756    387       C  
ATOM   2706  N   LYS A 347      44.129  98.731 255.382  1.00 47.81           N  
ANISOU 2706  N   LYS A 347     6467   8577   3121    831   -788    396       N  
ATOM   2707  CA  LYS A 347      45.211  97.838 255.029  1.00 49.13           C  
ANISOU 2707  CA  LYS A 347     6576   8786   3307    942   -853    427       C  
ATOM   2708  C   LYS A 347      45.650  97.947 253.572  1.00 48.40           C  
ANISOU 2708  C   LYS A 347     6374   8697   3319    959   -817    401       C  
ATOM   2709  O   LYS A 347      46.513  97.171 253.133  1.00 49.19           O  
ANISOU 2709  O   LYS A 347     6421   8827   3443   1060   -855    423       O  
ATOM   2710  CB  LYS A 347      44.804  96.387 255.310  1.00 50.08           C  
ANISOU 2710  CB  LYS A 347     6812   8826   3388   1033   -858    505       C  
ATOM   2711  CG  LYS A 347      45.055  95.865 256.727  1.00 54.39           C  
ANISOU 2711  CG  LYS A 347     7438   9406   3823   1078   -938    552       C  
ATOM   2712  CD  LYS A 347      44.358  94.484 256.897  1.00 58.75           C  
ANISOU 2712  CD  LYS A 347     8129   9847   4345   1144   -919    634       C  
ATOM   2713  CE  LYS A 347      44.030  94.161 258.382  1.00 62.21           C  
ANISOU 2713  CE  LYS A 347     8690  10289   4659   1142   -959    685       C  
ATOM   2714  NZ  LYS A 347      42.886  93.175 258.505  1.00 62.97           N  
ANISOU 2714  NZ  LYS A 347     8934  10259   4734   1145   -899    755       N  
ATOM   2715  N   PHE A 348      45.070  98.872 252.807  1.00 46.48           N  
ANISOU 2715  N   PHE A 348     6100   8424   3137    867   -741    357       N  
ATOM   2716  CA  PHE A 348      45.398  98.939 251.397  1.00 44.86           C  
ANISOU 2716  CA  PHE A 348     5806   8218   3022    879   -700    339       C  
ATOM   2717  C   PHE A 348      44.576 100.008 250.726  1.00 43.73           C  
ANISOU 2717  C   PHE A 348     5652   8031   2931    770   -620    299       C  
ATOM   2718  O   PHE A 348      43.745 100.621 251.398  1.00 43.77           O  
ANISOU 2718  O   PHE A 348     5721   8004   2904    696   -595    287       O  
ATOM   2719  CB  PHE A 348      45.080  97.595 250.777  1.00 44.76           C  
ANISOU 2719  CB  PHE A 348     5858   8123   3028    973   -676    387       C  
ATOM   2720  CG  PHE A 348      43.617  97.328 250.648  1.00 43.81           C  
ANISOU 2720  CG  PHE A 348     5855   7883   2908    927   -604    410       C  
ATOM   2721  CD1 PHE A 348      42.898  96.820 251.713  1.00 44.35           C  
ANISOU 2721  CD1 PHE A 348     6042   7902   2907    927   -613    452       C  
ATOM   2722  CD2 PHE A 348      42.949  97.578 249.441  1.00 42.05           C  
ANISOU 2722  CD2 PHE A 348     5621   7602   2755    883   -527    393       C  
ATOM   2723  CE1 PHE A 348      41.526  96.578 251.578  1.00 44.35           C  
ANISOU 2723  CE1 PHE A 348     6139   7800   2913    878   -543    475       C  
ATOM   2724  CE2 PHE A 348      41.584  97.349 249.310  1.00 40.37           C  
ANISOU 2724  CE2 PHE A 348     5505   7288   2547    836   -466    415       C  
ATOM   2725  CZ  PHE A 348      40.872  96.848 250.364  1.00 41.11           C  
ANISOU 2725  CZ  PHE A 348     5707   7337   2578    832   -472    456       C  
ATOM   2726  N   ALA A 349      44.784 100.227 249.415  1.00 42.65           N  
ANISOU 2726  N   ALA A 349     5440   7893   2871    764   -576    281       N  
ATOM   2727  CA  ALA A 349      43.888 101.082 248.598  1.00 41.40           C  
ANISOU 2727  CA  ALA A 349     5284   7677   2767    674   -495    257       C  
ATOM   2728  C   ALA A 349      43.544 100.431 247.295  1.00 40.97           C  
ANISOU 2728  C   ALA A 349     5236   7564   2766    711   -442    275       C  
ATOM   2729  O   ALA A 349      44.417  99.796 246.737  1.00 42.53           O  
ANISOU 2729  O   ALA A 349     5380   7801   2980    789   -462    281       O  
ATOM   2730  CB  ALA A 349      44.522 102.399 248.301  1.00 40.97           C  
ANISOU 2730  CB  ALA A 349     5125   7692   2749    595   -496    207       C  
ATOM   2731  N   VAL A 350      42.303 100.603 246.808  1.00 39.99           N  
ANISOU 2731  N   VAL A 350     5174   7353   2668    658   -375    281       N  
ATOM   2732  CA  VAL A 350      41.910 100.299 245.413  1.00 39.34           C  
ANISOU 2732  CA  VAL A 350     5089   7220   2640    665   -321    287       C  
ATOM   2733  C   VAL A 350      42.028 101.506 244.490  1.00 39.21           C  
ANISOU 2733  C   VAL A 350     4989   7231   2678    590   -282    253       C  
ATOM   2734  O   VAL A 350      41.455 102.552 244.759  1.00 39.43           O  
ANISOU 2734  O   VAL A 350     5021   7245   2716    507   -259    236       O  
ATOM   2735  CB  VAL A 350      40.417 100.000 245.240  1.00 38.48           C  
ANISOU 2735  CB  VAL A 350     5077   7006   2536    629   -270    314       C  
ATOM   2736  CG1 VAL A 350      40.214  98.932 244.202  1.00 38.38           C  
ANISOU 2736  CG1 VAL A 350     5099   6937   2545    682   -251    335       C  
ATOM   2737  CG2 VAL A 350      39.747  99.664 246.518  1.00 39.14           C  
ANISOU 2737  CG2 VAL A 350     5250   7057   2565    624   -284    340       C  
ATOM   2738  N   LEU A 351      42.702 101.346 243.368  1.00 39.64           N  
ANISOU 2738  N   LEU A 351     4977   7317   2768    622   -268    245       N  
ATOM   2739  CA  LEU A 351      42.669 102.359 242.324  1.00 39.79           C  
ANISOU 2739  CA  LEU A 351     4935   7348   2837    551   -222    225       C  
ATOM   2740  C   LEU A 351      41.792 101.861 241.217  1.00 39.65           C  
ANISOU 2740  C   LEU A 351     4970   7253   2841    557   -172    243       C  
ATOM   2741  O   LEU A 351      41.965 100.741 240.743  1.00 40.29           O  
ANISOU 2741  O   LEU A 351     5078   7316   2913    635   -174    255       O  
ATOM   2742  CB  LEU A 351      44.049 102.604 241.723  1.00 40.09           C  
ANISOU 2742  CB  LEU A 351     4853   7484   2894    572   -232    204       C  
ATOM   2743  CG  LEU A 351      45.033 103.437 242.531  1.00 39.49           C  
ANISOU 2743  CG  LEU A 351     4692   7501   2811    535   -280    179       C  
ATOM   2744  CD1 LEU A 351      45.448 102.696 243.756  1.00 37.66           C  
ANISOU 2744  CD1 LEU A 351     4483   7299   2528    603   -348    189       C  
ATOM   2745  CD2 LEU A 351      46.230 103.702 241.660  1.00 40.01           C  
ANISOU 2745  CD2 LEU A 351     4632   7660   2908    542   -272    165       C  
ATOM   2746  N   SER A 352      40.863 102.704 240.806  1.00 38.93           N  
ANISOU 2746  N   SER A 352     4895   7117   2779    476   -130    243       N  
ATOM   2747  CA  SER A 352      40.016 102.413 239.690  1.00 38.89           C  
ANISOU 2747  CA  SER A 352     4930   7051   2797    467    -87    259       C  
ATOM   2748  C   SER A 352      40.541 103.231 238.500  1.00 38.90           C  
ANISOU 2748  C   SER A 352     4852   7095   2833    430    -56    244       C  
ATOM   2749  O   SER A 352      40.844 104.425 238.634  1.00 39.61           O  
ANISOU 2749  O   SER A 352     4885   7220   2944    366    -51    229       O  
ATOM   2750  CB  SER A 352      38.591 102.870 240.041  1.00 38.84           C  
ANISOU 2750  CB  SER A 352     4985   6973   2801    403    -63    275       C  
ATOM   2751  OG  SER A 352      37.720 101.813 240.438  1.00 40.92           O  
ANISOU 2751  OG  SER A 352     5336   7170   3041    431    -68    303       O  
ATOM   2752  N   GLY A 353      40.637 102.631 237.324  1.00 38.34           N  
ANISOU 2752  N   GLY A 353     4785   7019   2766    465    -33    249       N  
ATOM   2753  CA  GLY A 353      40.984 103.433 236.181  1.00 37.39           C  
ANISOU 2753  CA  GLY A 353     4601   6934   2670    422      3    242       C  
ATOM   2754  C   GLY A 353      40.889 102.720 234.865  1.00 37.61           C  
ANISOU 2754  C   GLY A 353     4654   6946   2691    458     32    246       C  
ATOM   2755  O   GLY A 353      39.981 101.915 234.646  1.00 36.16           O  
ANISOU 2755  O   GLY A 353     4554   6689   2494    476     32    260       O  
ATOM   2756  N   ARG A 354      41.870 103.032 234.001  1.00 38.78           N  
ANISOU 2756  N   ARG A 354     4725   7168   2843    464     58    233       N  
ATOM   2757  CA  ARG A 354      41.878 102.662 232.585  1.00 39.04           C  
ANISOU 2757  CA  ARG A 354     4770   7200   2863    483     97    233       C  
ATOM   2758  C   ARG A 354      43.236 102.354 231.988  1.00 40.58           C  
ANISOU 2758  C   ARG A 354     4888   7487   3045    546    118    212       C  
ATOM   2759  O   ARG A 354      44.219 103.007 232.316  1.00 41.33           O  
ANISOU 2759  O   ARG A 354     4883   7666   3154    530    117    204       O  
ATOM   2760  CB  ARG A 354      41.269 103.784 231.778  1.00 38.20           C  
ANISOU 2760  CB  ARG A 354     4657   7079   2778    390    130    251       C  
ATOM   2761  CG  ARG A 354      39.807 103.789 231.942  1.00 36.73           C  
ANISOU 2761  CG  ARG A 354     4554   6800   2600    350    119    273       C  
ATOM   2762  CD  ARG A 354      39.038 104.270 230.765  1.00 35.28           C  
ANISOU 2762  CD  ARG A 354     4395   6587   2422    297    147    294       C  
ATOM   2763  NE  ARG A 354      37.717 103.796 231.074  1.00 36.09           N  
ANISOU 2763  NE  ARG A 354     4578   6608   2528    288    126    311       N  
ATOM   2764  CZ  ARG A 354      37.089 102.853 230.392  1.00 37.41           C  
ANISOU 2764  CZ  ARG A 354     4813   6730   2670    309    122    316       C  
ATOM   2765  NH1 ARG A 354      37.637 102.342 229.294  1.00 37.11           N  
ANISOU 2765  NH1 ARG A 354     4782   6720   2599    344    140    300       N  
ATOM   2766  NH2 ARG A 354      35.886 102.456 230.791  1.00 36.69           N  
ANISOU 2766  NH2 ARG A 354     4785   6570   2587    290    101    334       N  
ATOM   2767  N   ARG A 355      43.260 101.358 231.099  1.00 41.88           N  
ANISOU 2767  N   ARG A 355     5098   7635   3179    614    140    202       N  
ATOM   2768  CA  ARG A 355      44.368 101.098 230.149  1.00 43.41           C  
ANISOU 2768  CA  ARG A 355     5229   7912   3355    672    182    182       C  
ATOM   2769  C   ARG A 355      43.784 100.383 228.907  1.00 43.58           C  
ANISOU 2769  C   ARG A 355     5340   7879   3339    697    214    174       C  
ATOM   2770  O   ARG A 355      42.835  99.611 229.042  1.00 43.62           O  
ANISOU 2770  O   ARG A 355     5453   7789   3332    711    188    176       O  
ATOM   2771  CB  ARG A 355      45.456 100.252 230.812  1.00 44.23           C  
ANISOU 2771  CB  ARG A 355     5286   8069   3450    784    159    162       C  
ATOM   2772  CG  ARG A 355      46.758 100.118 230.000  1.00 45.69           C  
ANISOU 2772  CG  ARG A 355     5373   8363   3623    849    206    141       C  
ATOM   2773  CD  ARG A 355      47.791  99.189 230.658  1.00 47.70           C  
ANISOU 2773  CD  ARG A 355     5582   8668   3873    978    179    125       C  
ATOM   2774  NE  ARG A 355      47.209  98.048 231.389  1.00 47.13           N  
ANISOU 2774  NE  ARG A 355     5625   8496   3787   1052    130    127       N  
ATOM   2775  CZ  ARG A 355      46.621  97.007 230.797  1.00 46.63           C  
ANISOU 2775  CZ  ARG A 355     5682   8341   3695   1109    143    115       C  
ATOM   2776  NH1 ARG A 355      46.508  96.961 229.462  1.00 45.47           N  
ANISOU 2776  NH1 ARG A 355     5558   8193   3524   1104    201     97       N  
ATOM   2777  NH2 ARG A 355      46.133  96.023 231.538  1.00 45.23           N  
ANISOU 2777  NH2 ARG A 355     5607   8072   3508   1166     97    123       N  
ATOM   2778  N   ASP A 356      44.302 100.670 227.712  1.00 44.03           N  
ANISOU 2778  N   ASP A 356     5356   7997   3376    692    269    166       N  
ATOM   2779  CA  ASP A 356      43.760 100.088 226.445  1.00 45.03           C  
ANISOU 2779  CA  ASP A 356     5572   8080   3458    706    300    155       C  
ATOM   2780  C   ASP A 356      42.248 100.253 226.125  1.00 43.39           C  
ANISOU 2780  C   ASP A 356     5465   7774   3247    625    279    178       C  
ATOM   2781  O   ASP A 356      41.627  99.388 225.478  1.00 43.58           O  
ANISOU 2781  O   ASP A 356     5590   7734   3233    650    276    164       O  
ATOM   2782  CB  ASP A 356      44.181  98.625 226.301  1.00 46.73           C  
ANISOU 2782  CB  ASP A 356     5843   8275   3637    835    302    117       C  
ATOM   2783  CG  ASP A 356      45.506  98.484 225.574  1.00 52.10           C  
ANISOU 2783  CG  ASP A 356     6441   9063   4294    910    362     89       C  
ATOM   2784  OD1 ASP A 356      45.438  98.425 224.303  1.00 57.60           O  
ANISOU 2784  OD1 ASP A 356     7171   9769   4944    906    412     76       O  
ATOM   2785  OD2 ASP A 356      46.590  98.469 226.258  1.00 54.19           O  
ANISOU 2785  OD2 ASP A 356     6603   9406   4581    970    358     83       O  
ATOM   2786  N   GLY A 357      41.678 101.364 226.585  1.00 41.85           N  
ANISOU 2786  N   GLY A 357     5242   7568   3092    530    263    212       N  
ATOM   2787  CA  GLY A 357      40.278 101.667 226.431  1.00 39.21           C  
ANISOU 2787  CA  GLY A 357     4978   7153   2766    456    240    240       C  
ATOM   2788  C   GLY A 357      39.334 100.747 227.153  1.00 37.62           C  
ANISOU 2788  C   GLY A 357     4866   6860   2569    476    194    240       C  
ATOM   2789  O   GLY A 357      38.198 100.633 226.757  1.00 37.29           O  
ANISOU 2789  O   GLY A 357     4892   6754   2521    432    178    257       O  
ATOM   2790  N   LEU A 358      39.789 100.081 228.205  1.00 37.33           N  
ANISOU 2790  N   LEU A 358     4827   6817   2539    540    170    226       N  
ATOM   2791  CA  LEU A 358      38.883  99.293 229.050  1.00 36.17           C  
ANISOU 2791  CA  LEU A 358     4763   6581   2398    548    127    235       C  
ATOM   2792  C   LEU A 358      39.119  99.644 230.478  1.00 35.43           C  
ANISOU 2792  C   LEU A 358     4626   6502   2334    549    102    245       C  
ATOM   2793  O   LEU A 358      40.239  99.990 230.830  1.00 35.44           O  
ANISOU 2793  O   LEU A 358     4545   6579   2341    580    109    232       O  
ATOM   2794  CB  LEU A 358      39.146  97.810 228.884  1.00 36.84           C  
ANISOU 2794  CB  LEU A 358     4926   6625   2447    641    118    208       C  
ATOM   2795  CG  LEU A 358      39.079  97.175 227.500  1.00 38.36           C  
ANISOU 2795  CG  LEU A 358     5182   6799   2596    663    141    183       C  
ATOM   2796  CD1 LEU A 358      39.653  95.776 227.630  1.00 38.49           C  
ANISOU 2796  CD1 LEU A 358     5262   6779   2583    776    134    149       C  
ATOM   2797  CD2 LEU A 358      37.641  97.160 226.912  1.00 38.44           C  
ANISOU 2797  CD2 LEU A 358     5271   6735   2599    579    123    202       C  
ATOM   2798  N   THR A 359      38.077  99.525 231.307  1.00 35.35           N  
ANISOU 2798  N   THR A 359     4668   6424   2338    513     74    268       N  
ATOM   2799  CA  THR A 359      38.213  99.631 232.801  1.00 34.89           C  
ANISOU 2799  CA  THR A 359     4594   6370   2294    522     46    276       C  
ATOM   2800  C   THR A 359      39.219  98.647 233.389  1.00 35.56           C  
ANISOU 2800  C   THR A 359     4683   6473   2355    623     25    259       C  
ATOM   2801  O   THR A 359      39.162  97.443 233.113  1.00 34.98           O  
ANISOU 2801  O   THR A 359     4684   6349   2257    684     16    252       O  
ATOM   2802  CB  THR A 359      36.909  99.323 233.587  1.00 34.05           C  
ANISOU 2802  CB  THR A 359     4560   6182   2194    484     25    304       C  
ATOM   2803  OG1 THR A 359      36.590  97.932 233.458  1.00 35.15           O  
ANISOU 2803  OG1 THR A 359     4793   6254   2308    530      8    305       O  
ATOM   2804  CG2 THR A 359      35.756 100.143 233.124  1.00 33.11           C  
ANISOU 2804  CG2 THR A 359     4442   6037   2102    396     41    326       C  
ATOM   2805  N   ARG A 360      40.109  99.186 234.224  1.00 36.67           N  
ANISOU 2805  N   ARG A 360     4745   6683   2504    637     11    253       N  
ATOM   2806  CA  ARG A 360      41.059  98.413 235.019  1.00 38.12           C  
ANISOU 2806  CA  ARG A 360     4919   6896   2669    731    -20    245       C  
ATOM   2807  C   ARG A 360      41.015  98.782 236.496  1.00 38.51           C  
ANISOU 2807  C   ARG A 360     4958   6956   2719    711    -58    258       C  
ATOM   2808  O   ARG A 360      40.501  99.825 236.874  1.00 38.05           O  
ANISOU 2808  O   ARG A 360     4878   6901   2678    627    -52    264       O  
ATOM   2809  CB  ARG A 360      42.461  98.609 234.482  1.00 38.71           C  
ANISOU 2809  CB  ARG A 360     4893   7072   2744    783     -4    219       C  
ATOM   2810  CG  ARG A 360      42.908  97.478 233.587  1.00 40.58           C  
ANISOU 2810  CG  ARG A 360     5164   7296   2957    880     14    201       C  
ATOM   2811  CD  ARG A 360      42.753  97.737 232.099  1.00 39.68           C  
ANISOU 2811  CD  ARG A 360     5049   7189   2839    849     66    186       C  
ATOM   2812  NE  ARG A 360      42.751  96.429 231.446  1.00 42.17           N  
ANISOU 2812  NE  ARG A 360     5451   7448   3123    938     74    168       N  
ATOM   2813  CZ  ARG A 360      42.895  96.216 230.141  1.00 43.16           C  
ANISOU 2813  CZ  ARG A 360     5591   7582   3227    956    118    144       C  
ATOM   2814  NH1 ARG A 360      43.064  97.210 229.303  1.00 41.78           N  
ANISOU 2814  NH1 ARG A 360     5347   7473   3056    892    159    142       N  
ATOM   2815  NH2 ARG A 360      42.878  94.984 229.665  1.00 47.37           N  
ANISOU 2815  NH2 ARG A 360     6217   8053   3728   1039    121    121       N  
ATOM   2816  N   VAL A 361      41.558  97.904 237.332  1.00 40.15           N  
ANISOU 2816  N   VAL A 361     5188   7166   2901    794    -97    263       N  
ATOM   2817  CA  VAL A 361      41.551  98.088 238.785  1.00 40.39           C  
ANISOU 2817  CA  VAL A 361     5223   7207   2917    785   -139    278       C  
ATOM   2818  C   VAL A 361      42.801  97.495 239.422  1.00 41.48           C  
ANISOU 2818  C   VAL A 361     5321   7408   3033    886   -184    274       C  
ATOM   2819  O   VAL A 361      43.096  96.318 239.217  1.00 41.73           O  
ANISOU 2819  O   VAL A 361     5400   7406   3048    982   -194    280       O  
ATOM   2820  CB  VAL A 361      40.242  97.524 239.445  1.00 40.00           C  
ANISOU 2820  CB  VAL A 361     5291   7056   2851    757   -145    310       C  
ATOM   2821  CG1 VAL A 361      39.706  96.351 238.685  1.00 40.64           C  
ANISOU 2821  CG1 VAL A 361     5464   7051   2927    795   -134    320       C  
ATOM   2822  CG2 VAL A 361      40.460  97.143 240.927  1.00 41.87           C  
ANISOU 2822  CG2 VAL A 361     5558   7298   3050    793   -194    330       C  
ATOM   2823  N   TRP A 362      43.529  98.335 240.168  1.00 42.48           N  
ANISOU 2823  N   TRP A 362     5360   7622   3160    862   -212    264       N  
ATOM   2824  CA  TRP A 362      44.695  97.913 240.964  1.00 44.26           C  
ANISOU 2824  CA  TRP A 362     5534   7921   3362    948   -268    265       C  
ATOM   2825  C   TRP A 362      44.524  98.088 242.478  1.00 44.80           C  
ANISOU 2825  C   TRP A 362     5634   7994   3394    926   -321    281       C  
ATOM   2826  O   TRP A 362      43.705  98.860 242.973  1.00 44.32           O  
ANISOU 2826  O   TRP A 362     5604   7905   3331    833   -311    281       O  
ATOM   2827  CB  TRP A 362      45.955  98.673 240.565  1.00 44.78           C  
ANISOU 2827  CB  TRP A 362     5452   8111   3451    945   -268    237       C  
ATOM   2828  CG  TRP A 362      46.147  98.738 239.122  1.00 46.06           C  
ANISOU 2828  CG  TRP A 362     5574   8286   3643    949   -208    220       C  
ATOM   2829  CD1 TRP A 362      46.893  97.892 238.365  1.00 48.74           C  
ANISOU 2829  CD1 TRP A 362     5886   8651   3981   1055   -193    212       C  
ATOM   2830  CD2 TRP A 362      45.598  99.707 238.225  1.00 44.82           C  
ANISOU 2830  CD2 TRP A 362     5401   8115   3513    847   -153    210       C  
ATOM   2831  NE1 TRP A 362      46.833  98.261 237.041  1.00 48.59           N  
ANISOU 2831  NE1 TRP A 362     5840   8641   3983   1021   -128    195       N  
ATOM   2832  CE2 TRP A 362      46.040  99.373 236.930  1.00 45.94           C  
ANISOU 2832  CE2 TRP A 362     5511   8280   3665    892   -106    197       C  
ATOM   2833  CE3 TRP A 362      44.774 100.822 238.389  1.00 44.40           C  
ANISOU 2833  CE3 TRP A 362     5362   8031   3477    727   -138    211       C  
ATOM   2834  CZ2 TRP A 362      45.681 100.109 235.806  1.00 44.47           C  
ANISOU 2834  CZ2 TRP A 362     5308   8089   3498    816    -49    190       C  
ATOM   2835  CZ3 TRP A 362      44.417 101.560 237.272  1.00 42.42           C  
ANISOU 2835  CZ3 TRP A 362     5093   7772   3254    657    -83    206       C  
ATOM   2836  CH2 TRP A 362      44.860 101.191 235.999  1.00 44.22           C  
ANISOU 2836  CH2 TRP A 362     5292   8025   3485    699    -42    198       C  
ATOM   2837  N   THR A 363      45.372  97.386 243.203  1.00 45.97           N  
ANISOU 2837  N   THR A 363     5769   8185   3511   1019   -379    294       N  
ATOM   2838  CA  THR A 363      45.320  97.346 244.623  1.00 46.11           C  
ANISOU 2838  CA  THR A 363     5826   8211   3482   1018   -437    314       C  
ATOM   2839  C   THR A 363      46.733  97.674 245.118  1.00 47.53           C  
ANISOU 2839  C   THR A 363     5884   8522   3654   1057   -498    300       C  
ATOM   2840  O   THR A 363      47.715  97.307 244.456  1.00 48.05           O  
ANISOU 2840  O   THR A 363     5865   8648   3742   1137   -502    292       O  
ATOM   2841  CB  THR A 363      44.840  95.957 245.041  1.00 46.28           C  
ANISOU 2841  CB  THR A 363     5977   8141   3468   1101   -456    358       C  
ATOM   2842  OG1 THR A 363      44.397  96.005 246.389  1.00 48.41           O  
ANISOU 2842  OG1 THR A 363     6312   8396   3684   1071   -493    383       O  
ATOM   2843  CG2 THR A 363      45.921  94.887 244.886  1.00 46.44           C  
ANISOU 2843  CG2 THR A 363     5972   8190   3482   1245   -494    370       C  
ATOM   2844  N   VAL A 364      46.841  98.400 246.234  1.00 47.90           N  
ANISOU 2844  N   VAL A 364     5914   8618   3667    998   -545    293       N  
ATOM   2845  CA  VAL A 364      48.147  98.770 246.798  1.00 49.63           C  
ANISOU 2845  CA  VAL A 364     6016   8968   3874   1019   -615    279       C  
ATOM   2846  C   VAL A 364      48.186  98.569 248.312  1.00 50.80           C  
ANISOU 2846  C   VAL A 364     6218   9133   3949   1033   -693    301       C  
ATOM   2847  O   VAL A 364      47.336  99.072 249.045  1.00 50.86           O  
ANISOU 2847  O   VAL A 364     6305   9096   3922    952   -687    297       O  
ATOM   2848  CB  VAL A 364      48.629 100.218 246.346  1.00 49.61           C  
ANISOU 2848  CB  VAL A 364     5888   9047   3914    907   -596    232       C  
ATOM   2849  CG1 VAL A 364      47.958 101.337 247.128  1.00 48.77           C  
ANISOU 2849  CG1 VAL A 364     5824   8920   3787    781   -598    209       C  
ATOM   2850  CG2 VAL A 364      50.144 100.362 246.449  1.00 50.88           C  
ANISOU 2850  CG2 VAL A 364     5897   9352   4083    946   -656    221       C  
ATOM   2851  N   ARG A 365      49.181  97.821 248.764  1.00 52.62           N  
ANISOU 2851  N   ARG A 365     6407   9432   4155   1142   -766    324       N  
ATOM   2852  CA  ARG A 365      49.294  97.364 250.160  1.00 53.87           C  
ANISOU 2852  CA  ARG A 365     6628   9606   4235   1183   -849    357       C  
ATOM   2853  C   ARG A 365      50.252  98.217 251.032  1.00 54.74           C  
ANISOU 2853  C   ARG A 365     6633   9851   4313   1138   -933    332       C  
ATOM   2854  O   ARG A 365      51.022  99.007 250.526  1.00 54.57           O  
ANISOU 2854  O   ARG A 365     6476   9921   4337   1093   -935    294       O  
ATOM   2855  CB  ARG A 365      49.801  95.922 250.149  1.00 54.75           C  
ANISOU 2855  CB  ARG A 365     6766   9702   4333   1345   -887    407       C  
ATOM   2856  CG  ARG A 365      48.757  94.859 250.293  1.00 56.11           C  
ANISOU 2856  CG  ARG A 365     7109   9732   4478   1389   -858    454       C  
ATOM   2857  CD  ARG A 365      49.289  93.507 249.806  1.00 59.75           C  
ANISOU 2857  CD  ARG A 365     7587  10160   4955   1548   -872    489       C  
ATOM   2858  NE  ARG A 365      48.872  93.335 248.421  1.00 63.46           N  
ANISOU 2858  NE  ARG A 365     8063  10558   5489   1545   -783    465       N  
ATOM   2859  CZ  ARG A 365      49.683  93.262 247.362  1.00 66.48           C  
ANISOU 2859  CZ  ARG A 365     8339  10993   5926   1608   -758    438       C  
ATOM   2860  NH1 ARG A 365      51.019  93.278 247.496  1.00 66.93           N  
ANISOU 2860  NH1 ARG A 365     8260  11179   5990   1690   -814    433       N  
ATOM   2861  NH2 ARG A 365      49.141  93.142 246.151  1.00 66.47           N  
ANISOU 2861  NH2 ARG A 365     8367  10919   5970   1590   -675    416       N  
ATOM   2862  N   LEU A 366      50.226  98.032 252.346  1.00 56.20           N  
ANISOU 2862  N   LEU A 366     6885  10052   4416   1147  -1007    355       N  
ATOM   2863  CA  LEU A 366      51.272  98.616 253.170  1.00 58.32           C  
ANISOU 2863  CA  LEU A 366     7054  10458   4648   1126  -1105    336       C  
ATOM   2864  C   LEU A 366      52.504  97.730 253.149  1.00 60.49           C  
ANISOU 2864  C   LEU A 366     7233  10822   4927   1269  -1180    371       C  
ATOM   2865  O   LEU A 366      52.403  96.530 252.876  1.00 60.89           O  
ANISOU 2865  O   LEU A 366     7344  10810   4983   1394  -1169    419       O  
ATOM   2866  CB  LEU A 366      50.827  98.800 254.610  1.00 58.37           C  
ANISOU 2866  CB  LEU A 366     7167  10458   4554   1080  -1160    344       C  
ATOM   2867  CG  LEU A 366      49.588  99.614 254.944  1.00 57.55           C  
ANISOU 2867  CG  LEU A 366     7171  10270   4423    954  -1095    313       C  
ATOM   2868  CD1 LEU A 366      49.605  99.905 256.441  1.00 59.15           C  
ANISOU 2868  CD1 LEU A 366     7439  10518   4517    917  -1173    311       C  
ATOM   2869  CD2 LEU A 366      49.503 100.899 254.131  1.00 56.78           C  
ANISOU 2869  CD2 LEU A 366     6995  10180   4400    835  -1033    248       C  
ATOM   2870  N   GLY A 367      53.663  98.332 253.431  1.00 62.36           N  
ANISOU 2870  N   GLY A 367     7321  11207   5166   1248  -1258    347       N  
ATOM   2871  CA  GLY A 367      54.904  97.599 253.572  1.00 64.33           C  
ANISOU 2871  CA  GLY A 367     7461  11566   5416   1382  -1343    380       C  
ATOM   2872  C   GLY A 367      55.015  97.129 255.006  1.00 66.40           C  
ANISOU 2872  C   GLY A 367     7800  11853   5575   1429  -1453    423       C  
ATOM   2873  O   GLY A 367      54.215  97.548 255.862  1.00 65.55           O  
ANISOU 2873  O   GLY A 367     7814  11696   5398   1339  -1459    415       O  
ATOM   2874  N   PRO A 368      55.986  96.224 255.270  1.00 68.57           N  
ANISOU 2874  N   PRO A 368     8010  12205   5838   1579  -1539    471       N  
ATOM   2875  CA  PRO A 368      56.519  95.968 256.598  1.00 70.46           C  
ANISOU 2875  CA  PRO A 368     8260  12526   5984   1622  -1672    508       C  
ATOM   2876  C   PRO A 368      56.668  97.238 257.442  1.00 71.38           C  
ANISOU 2876  C   PRO A 368     8340  12735   6048   1464  -1734    456       C  
ATOM   2877  O   PRO A 368      56.505  97.173 258.655  1.00 72.57           O  
ANISOU 2877  O   PRO A 368     8583  12896   6094   1452  -1813    478       O  
ATOM   2878  CB  PRO A 368      57.899  95.369 256.297  1.00 71.69           C  
ANISOU 2878  CB  PRO A 368     8247  12809   6183   1769  -1742    536       C  
ATOM   2879  CG  PRO A 368      57.809  94.852 254.862  1.00 70.60           C  
ANISOU 2879  CG  PRO A 368     8079  12601   6145   1847  -1629    532       C  
ATOM   2880  CD  PRO A 368      56.454  95.193 254.326  1.00 68.74           C  
ANISOU 2880  CD  PRO A 368     7982  12212   5926   1737  -1506    502       C  
ATOM   2881  N   ASP A 369      56.968  98.378 256.817  1.00 71.68           N  
ANISOU 2881  N   ASP A 369     8253  12832   6150   1341  -1698    388       N  
ATOM   2882  CA  ASP A 369      57.113  99.652 257.550  1.00 72.71           C  
ANISOU 2882  CA  ASP A 369     8353  13037   6236   1179  -1753    330       C  
ATOM   2883  C   ASP A 369      55.801 100.223 258.137  1.00 71.64           C  
ANISOU 2883  C   ASP A 369     8402  12781   6036   1061  -1700    301       C  
ATOM   2884  O   ASP A 369      55.847 101.092 259.026  1.00 72.47           O  
ANISOU 2884  O   ASP A 369     8525  12935   6074    949  -1759    258       O  
ATOM   2885  CB  ASP A 369      57.911 100.720 256.740  1.00 73.17           C  
ANISOU 2885  CB  ASP A 369     8221  13198   6384   1076  -1738    270       C  
ATOM   2886  CG  ASP A 369      57.268 101.097 255.367  1.00 74.36           C  
ANISOU 2886  CG  ASP A 369     8373  13249   6632   1024  -1588    240       C  
ATOM   2887  OD1 ASP A 369      56.083 100.761 255.073  1.00 75.77           O  
ANISOU 2887  OD1 ASP A 369     8703  13276   6810   1035  -1494    252       O  
ATOM   2888  OD2 ASP A 369      57.976 101.759 254.562  1.00 76.20           O  
ANISOU 2888  OD2 ASP A 369     8446  13563   6943    966  -1566    207       O  
ATOM   2889  N   ASN A 370      54.655  99.701 257.659  1.00 70.07           N  
ANISOU 2889  N   ASN A 370     8339  12430   5855   1092  -1590    324       N  
ATOM   2890  CA  ASN A 370      53.292 100.207 257.961  1.00 68.07           C  
ANISOU 2890  CA  ASN A 370     8247  12054   5564    989  -1510    298       C  
ATOM   2891  C   ASN A 370      52.937 101.444 257.128  1.00 66.57           C  
ANISOU 2891  C   ASN A 370     8009  11833   5452    852  -1422    227       C  
ATOM   2892  O   ASN A 370      51.966 102.150 257.420  1.00 65.75           O  
ANISOU 2892  O   ASN A 370     8009  11651   5322    751  -1366    191       O  
ATOM   2893  CB  ASN A 370      53.080 100.473 259.466  1.00 68.76           C  
ANISOU 2893  CB  ASN A 370     8439  12166   5522    940  -1588    294       C  
ATOM   2894  CG  ASN A 370      53.084  99.196 260.306  1.00 69.94           C  
ANISOU 2894  CG  ASN A 370     8684  12306   5583   1071  -1655    377       C  
ATOM   2895  OD1 ASN A 370      52.642  98.124 259.859  1.00 70.16           O  
ANISOU 2895  OD1 ASN A 370     8779  12244   5637   1175  -1604    436       O  
ATOM   2896  ND2 ASN A 370      53.575  99.310 261.540  1.00 70.93           N  
ANISOU 2896  ND2 ASN A 370     8827  12523   5600   1062  -1772    381       N  
ATOM   2897  N   LEU A 371      53.737 101.697 256.095  1.00 65.94           N  
ANISOU 2897  N   LEU A 371     7771  11817   5466    853  -1407    209       N  
ATOM   2898  CA  LEU A 371      53.524 102.813 255.188  1.00 64.88           C  
ANISOU 2898  CA  LEU A 371     7581  11659   5411    731  -1325    152       C  
ATOM   2899  C   LEU A 371      53.326 102.268 253.776  1.00 63.50           C  
ANISOU 2899  C   LEU A 371     7373  11424   5328    798  -1227    175       C  
ATOM   2900  O   LEU A 371      53.920 101.242 253.411  1.00 64.05           O  
ANISOU 2900  O   LEU A 371     7388  11530   5418    931  -1246    219       O  
ATOM   2901  CB  LEU A 371      54.716 103.776 255.233  1.00 66.33           C  
ANISOU 2901  CB  LEU A 371     7600  11983   5618    644  -1396    106       C  
ATOM   2902  CG  LEU A 371      54.730 104.987 256.187  1.00 68.11           C  
ANISOU 2902  CG  LEU A 371     7852  12241   5787    496  -1453     44       C  
ATOM   2903  CD1 LEU A 371      54.744 104.617 257.688  1.00 68.96           C  
ANISOU 2903  CD1 LEU A 371     8051  12382   5768    525  -1558     58       C  
ATOM   2904  CD2 LEU A 371      55.916 105.910 255.839  1.00 69.82           C  
ANISOU 2904  CD2 LEU A 371     7885  12584   6058    401  -1501      2       C  
ATOM   2905  N   PHE A 372      52.503 102.961 252.988  1.00 61.46           N  
ANISOU 2905  N   PHE A 372     7150  11077   5123    710  -1124    145       N  
ATOM   2906  CA  PHE A 372      52.076 102.468 251.676  1.00 59.58           C  
ANISOU 2906  CA  PHE A 372     6914  10764   4959    761  -1025    165       C  
ATOM   2907  C   PHE A 372      53.256 102.197 250.745  1.00 60.19           C  
ANISOU 2907  C   PHE A 372     6826  10942   5101    825  -1030    171       C  
ATOM   2908  O   PHE A 372      54.102 103.053 250.541  1.00 60.55           O  
ANISOU 2908  O   PHE A 372     6737  11088   5180    751  -1053    138       O  
ATOM   2909  CB  PHE A 372      51.059 103.412 251.011  1.00 57.94           C  
ANISOU 2909  CB  PHE A 372     6760  10459   4795    645   -924    130       C  
ATOM   2910  CG  PHE A 372      49.601 103.071 251.294  1.00 55.41           C  
ANISOU 2910  CG  PHE A 372     6611  10001   4442    647   -867    149       C  
ATOM   2911  CD1 PHE A 372      48.967 102.029 250.631  1.00 53.30           C  
ANISOU 2911  CD1 PHE A 372     6409   9648   4195    733   -811    191       C  
ATOM   2912  CD2 PHE A 372      48.850 103.825 252.194  1.00 53.47           C  
ANISOU 2912  CD2 PHE A 372     6457   9712   4146    557   -866    121       C  
ATOM   2913  CE1 PHE A 372      47.624 101.735 250.879  1.00 50.58           C  
ANISOU 2913  CE1 PHE A 372     6209   9184   3824    723   -759    210       C  
ATOM   2914  CE2 PHE A 372      47.516 103.529 252.446  1.00 50.11           C  
ANISOU 2914  CE2 PHE A 372     6175   9173   3694    558   -808    140       C  
ATOM   2915  CZ  PHE A 372      46.906 102.488 251.788  1.00 49.08           C  
ANISOU 2915  CZ  PHE A 372     6096   8964   3586    636   -755    187       C  
ATOM   2916  N   SER A 373      53.274 100.999 250.170  1.00 60.24           N  
ANISOU 2916  N   SER A 373     6849  10916   5125    962  -1004    213       N  
ATOM   2917  CA  SER A 373      54.420 100.479 249.449  1.00 61.32           C  
ANISOU 2917  CA  SER A 373     6841  11151   5309   1062  -1014    225       C  
ATOM   2918  C   SER A 373      54.232 100.423 247.930  1.00 60.93           C  
ANISOU 2918  C   SER A 373     6761  11058   5332   1072   -905    217       C  
ATOM   2919  O   SER A 373      53.633  99.480 247.402  1.00 60.07           O  
ANISOU 2919  O   SER A 373     6745  10850   5228   1160   -853    241       O  
ATOM   2920  CB  SER A 373      54.732  99.087 249.978  1.00 62.06           C  
ANISOU 2920  CB  SER A 373     6975  11246   5361   1230  -1075    278       C  
ATOM   2921  OG  SER A 373      55.847  98.522 249.316  1.00 63.77           O  
ANISOU 2921  OG  SER A 373     7052  11557   5622   1346  -1084    290       O  
ATOM   2922  N   SER A 374      54.784 101.419 247.239  1.00 61.18           N  
ANISOU 2922  N   SER A 374     6663  11167   5417    978   -873    183       N  
ATOM   2923  CA  SER A 374      54.788 101.476 245.785  1.00 61.32           C  
ANISOU 2923  CA  SER A 374     6631  11170   5498    981   -774    175       C  
ATOM   2924  C   SER A 374      54.925 100.106 245.122  1.00 61.60           C  
ANISOU 2924  C   SER A 374     6685  11178   5541   1150   -742    204       C  
ATOM   2925  O   SER A 374      54.228  99.783 244.144  1.00 60.35           O  
ANISOU 2925  O   SER A 374     6601  10925   5405   1167   -656    204       O  
ATOM   2926  CB  SER A 374      55.938 102.375 245.312  1.00 62.44           C  
ANISOU 2926  CB  SER A 374     6581  11456   5687    909   -775    151       C  
ATOM   2927  OG  SER A 374      55.987 103.579 246.063  1.00 64.15           O  
ANISOU 2927  OG  SER A 374     6776  11705   5891    759   -824    122       O  
ATOM   2928  N   ALA A 375      55.825  99.308 245.685  1.00 63.23           N  
ANISOU 2928  N   ALA A 375     6830  11467   5729   1276   -817    228       N  
ATOM   2929  CA  ALA A 375      56.259  98.042 245.096  1.00 64.36           C  
ANISOU 2929  CA  ALA A 375     6961  11608   5884   1452   -797    251       C  
ATOM   2930  C   ALA A 375      55.239  96.913 245.213  1.00 63.67           C  
ANISOU 2930  C   ALA A 375     7068  11360   5764   1540   -780    280       C  
ATOM   2931  O   ALA A 375      55.484  95.794 244.768  1.00 64.37           O  
ANISOU 2931  O   ALA A 375     7178  11420   5858   1690   -764    298       O  
ATOM   2932  CB  ALA A 375      57.586  97.619 245.718  1.00 66.01           C  
ANISOU 2932  CB  ALA A 375     7031  11963   6086   1562   -889    271       C  
ATOM   2933  N   THR A 376      54.100  97.212 245.820  1.00 62.78           N  
ANISOU 2933  N   THR A 376     7097  11142   5616   1447   -783    283       N  
ATOM   2934  CA  THR A 376      53.071  96.203 246.074  1.00 61.99           C  
ANISOU 2934  CA  THR A 376     7182  10892   5480   1507   -773    315       C  
ATOM   2935  C   THR A 376      51.888  96.322 245.104  1.00 60.44           C  
ANISOU 2935  C   THR A 376     7086  10568   5309   1438   -673    300       C  
ATOM   2936  O   THR A 376      50.925  95.565 245.200  1.00 60.07           O  
ANISOU 2936  O   THR A 376     7192  10393   5240   1464   -655    324       O  
ATOM   2937  CB  THR A 376      52.574  96.290 247.526  1.00 61.91           C  
ANISOU 2937  CB  THR A 376     7266  10853   5403   1464   -846    339       C  
ATOM   2938  OG1 THR A 376      52.113  97.627 247.781  1.00 60.68           O  
ANISOU 2938  OG1 THR A 376     7099  10711   5248   1297   -832    304       O  
ATOM   2939  CG2 THR A 376      53.701  95.933 248.490  1.00 62.13           C  
ANISOU 2939  CG2 THR A 376     7214  10995   5396   1555   -956    364       C  
ATOM   2940  N   LEU A 377      51.967  97.279 244.185  1.00 59.58           N  
ANISOU 2940  N   LEU A 377     6892  10501   5246   1345   -611    264       N  
ATOM   2941  CA  LEU A 377      50.961  97.452 243.154  1.00 58.65           C  
ANISOU 2941  CA  LEU A 377     6851  10282   5153   1283   -521    251       C  
ATOM   2942  C   LEU A 377      50.666  96.138 242.414  1.00 59.11           C  
ANISOU 2942  C   LEU A 377     7000  10247   5212   1403   -483    265       C  
ATOM   2943  O   LEU A 377      51.570  95.542 241.813  1.00 60.23           O  
ANISOU 2943  O   LEU A 377     7071  10444   5370   1516   -473    259       O  
ATOM   2944  CB  LEU A 377      51.422  98.513 242.146  1.00 58.29           C  
ANISOU 2944  CB  LEU A 377     6678  10315   5156   1199   -465    217       C  
ATOM   2945  CG  LEU A 377      50.419  98.875 241.040  1.00 57.26           C  
ANISOU 2945  CG  LEU A 377     6614  10094   5049   1121   -377    205       C  
ATOM   2946  CD1 LEU A 377      49.673 100.174 241.362  1.00 54.43           C  
ANISOU 2946  CD1 LEU A 377     6275   9709   4697    963   -368    193       C  
ATOM   2947  CD2 LEU A 377      51.081  98.933 239.631  1.00 59.32           C  
ANISOU 2947  CD2 LEU A 377     6779  10415   5345   1148   -308    186       C  
ATOM   2948  N   LYS A 378      49.401  95.710 242.458  1.00 58.51           N  
ANISOU 2948  N   LYS A 378     7080  10033   5118   1376   -460    281       N  
ATOM   2949  CA  LYS A 378      48.915  94.535 241.725  1.00 58.71           C  
ANISOU 2949  CA  LYS A 378     7217   9948   5143   1461   -422    290       C  
ATOM   2950  C   LYS A 378      47.761  94.944 240.790  1.00 57.53           C  
ANISOU 2950  C   LYS A 378     7133   9712   5012   1356   -349    274       C  
ATOM   2951  O   LYS A 378      46.829  95.614 241.218  1.00 56.89           O  
ANISOU 2951  O   LYS A 378     7099   9590   4927   1243   -345    281       O  
ATOM   2952  CB  LYS A 378      48.485  93.431 242.718  1.00 59.12           C  
ANISOU 2952  CB  LYS A 378     7403   9908   5152   1533   -476    333       C  
ATOM   2953  CG  LYS A 378      48.245  92.040 242.114  1.00 60.29           C  
ANISOU 2953  CG  LYS A 378     7666   9944   5298   1645   -454    345       C  
ATOM   2954  CD  LYS A 378      47.606  91.061 243.118  1.00 62.91           C  
ANISOU 2954  CD  LYS A 378     8151  10165   5587   1684   -501    395       C  
ATOM   2955  CE  LYS A 378      46.924  89.852 242.407  1.00 64.32           C  
ANISOU 2955  CE  LYS A 378     8478  10193   5767   1738   -466    402       C  
ATOM   2956  NZ  LYS A 378      46.677  88.655 243.297  1.00 64.70           N  
ANISOU 2956  NZ  LYS A 378     8666  10139   5777   1817   -517    456       N  
ATOM   2957  N   GLU A 379      47.850  94.585 239.508  1.00 57.93           N  
ANISOU 2957  N   GLU A 379     7184   9745   5083   1395   -291    252       N  
ATOM   2958  CA  GLU A 379      46.747  94.787 238.567  1.00 57.04           C  
ANISOU 2958  CA  GLU A 379     7146   9545   4981   1311   -231    242       C  
ATOM   2959  C   GLU A 379      45.881  93.550 238.609  1.00 57.53           C  
ANISOU 2959  C   GLU A 379     7369   9468   5021   1359   -236    262       C  
ATOM   2960  O   GLU A 379      46.393  92.434 238.541  1.00 58.11           O  
ANISOU 2960  O   GLU A 379     7484   9514   5083   1486   -251    264       O  
ATOM   2961  CB  GLU A 379      47.209  95.059 237.132  1.00 56.74           C  
ANISOU 2961  CB  GLU A 379     7038   9557   4965   1317   -166    208       C  
ATOM   2962  CG  GLU A 379      46.005  95.516 236.279  1.00 57.57           C  
ANISOU 2962  CG  GLU A 379     7211   9586   5077   1206   -115    203       C  
ATOM   2963  CD  GLU A 379      46.244  95.679 234.768  1.00 58.15           C  
ANISOU 2963  CD  GLU A 379     7250   9688   5159   1206    -48    174       C  
ATOM   2964  OE1 GLU A 379      47.045  96.555 234.370  1.00 59.10           O  
ANISOU 2964  OE1 GLU A 379     7242   9917   5295   1177    -22    160       O  
ATOM   2965  OE2 GLU A 379      45.569  94.962 233.982  1.00 56.36           O  
ANISOU 2965  OE2 GLU A 379     7128   9370   4916   1222    -22    166       O  
ATOM   2966  N   LEU A 380      44.571  93.756 238.729  1.00 57.58           N  
ANISOU 2966  N   LEU A 380     7467   9385   5025   1257   -225    277       N  
ATOM   2967  CA  LEU A 380      43.620  92.669 238.951  1.00 58.30           C  
ANISOU 2967  CA  LEU A 380     7712   9342   5096   1273   -235    304       C  
ATOM   2968  C   LEU A 380      43.252  91.975 237.656  1.00 59.48           C  
ANISOU 2968  C   LEU A 380     7933   9416   5250   1296   -193    282       C  
ATOM   2969  O   LEU A 380      42.955  92.635 236.645  1.00 59.65           O  
ANISOU 2969  O   LEU A 380     7919   9456   5289   1227   -147    257       O  
ATOM   2970  CB  LEU A 380      42.365  93.183 239.658  1.00 57.15           C  
ANISOU 2970  CB  LEU A 380     7623   9146   4947   1153   -238    332       C  
ATOM   2971  CG  LEU A 380      42.351  93.060 241.185  1.00 56.95           C  
ANISOU 2971  CG  LEU A 380     7626   9123   4890   1161   -290    368       C  
ATOM   2972  CD1 LEU A 380      43.240  94.088 241.842  1.00 56.60           C  
ANISOU 2972  CD1 LEU A 380     7458   9204   4845   1148   -316    355       C  
ATOM   2973  CD2 LEU A 380      40.937  93.179 241.709  1.00 55.84           C  
ANISOU 2973  CD2 LEU A 380     7574   8903   4741   1060   -278    398       C  
ATOM   2974  N   HIS A 381      43.261  90.645 237.697  1.00 61.08           N  
ANISOU 2974  N   HIS A 381     8245   9528   5434   1391   -211    292       N  
ATOM   2975  CA  HIS A 381      43.115  89.828 236.499  1.00 62.37           C  
ANISOU 2975  CA  HIS A 381     8486   9617   5594   1435   -177    262       C  
ATOM   2976  C   HIS A 381      41.661  89.513 236.197  1.00 61.99           C  
ANISOU 2976  C   HIS A 381     8564   9447   5543   1335   -167    275       C  
ATOM   2977  O   HIS A 381      40.898  89.087 237.061  1.00 61.78           O  
ANISOU 2977  O   HIS A 381     8625   9342   5508   1300   -197    316       O  
ATOM   2978  CB  HIS A 381      43.904  88.534 236.663  1.00 63.96           C  
ANISOU 2978  CB  HIS A 381     8748   9773   5779   1595   -202    262       C  
ATOM   2979  CG  HIS A 381      43.971  87.698 235.421  1.00 66.62           C  
ANISOU 2979  CG  HIS A 381     9161  10043   6109   1662   -164    219       C  
ATOM   2980  ND1 HIS A 381      43.056  86.702 235.144  1.00 67.59           N  
ANISOU 2980  ND1 HIS A 381     9451  10014   6218   1648   -168    222       N  
ATOM   2981  CD2 HIS A 381      44.858  87.692 234.393  1.00 68.94           C  
ANISOU 2981  CD2 HIS A 381     9390  10401   6403   1742   -121    170       C  
ATOM   2982  CE1 HIS A 381      43.367  86.128 233.992  1.00 68.89           C  
ANISOU 2982  CE1 HIS A 381     9658  10146   6372   1717   -132    172       C  
ATOM   2983  NE2 HIS A 381      44.458  86.708 233.518  1.00 69.58           N  
ANISOU 2983  NE2 HIS A 381     9607  10366   6466   1779    -99    140       N  
ATOM   2984  N   PHE A 382      41.280  89.720 234.950  1.00 62.18           N  
ANISOU 2984  N   PHE A 382     8594   9459   5571   1288   -126    241       N  
ATOM   2985  CA  PHE A 382      39.968  89.300 234.510  1.00 62.51           C  
ANISOU 2985  CA  PHE A 382     8753   9388   5609   1201   -122    248       C  
ATOM   2986  C   PHE A 382      40.083  88.393 233.288  1.00 63.83           C  
ANISOU 2986  C   PHE A 382     9006   9489   5757   1260   -101    204       C  
ATOM   2987  O   PHE A 382      41.083  88.457 232.546  1.00 64.59           O  
ANISOU 2987  O   PHE A 382     9042   9652   5845   1343    -70    163       O  
ATOM   2988  CB  PHE A 382      39.120  90.519 234.212  1.00 61.60           C  
ANISOU 2988  CB  PHE A 382     8575   9315   5513   1062   -100    256       C  
ATOM   2989  CG  PHE A 382      38.878  91.394 235.412  1.00 61.55           C  
ANISOU 2989  CG  PHE A 382     8504   9359   5523   1001   -117    293       C  
ATOM   2990  CD1 PHE A 382      37.953  91.023 236.388  1.00 61.08           C  
ANISOU 2990  CD1 PHE A 382     8521   9227   5460    952   -142    337       C  
ATOM   2991  CD2 PHE A 382      39.569  92.596 235.561  1.00 61.06           C  
ANISOU 2991  CD2 PHE A 382     8308   9416   5477    987   -105    283       C  
ATOM   2992  CE1 PHE A 382      37.722  91.836 237.488  1.00 60.48           C  
ANISOU 2992  CE1 PHE A 382     8392   9198   5390    899   -151    365       C  
ATOM   2993  CE2 PHE A 382      39.343  93.416 236.652  1.00 59.45           C  
ANISOU 2993  CE2 PHE A 382     8054   9250   5282    929   -120    309       C  
ATOM   2994  CZ  PHE A 382      38.421  93.035 237.621  1.00 59.83           C  
ANISOU 2994  CZ  PHE A 382     8183   9228   5321    890   -141    348       C  
ATOM   2995  N   ASP A 383      39.060  87.558 233.073  1.00 64.31           N  
ANISOU 2995  N   ASP A 383     9206   9421   5807   1212   -114    211       N  
ATOM   2996  CA  ASP A 383      39.101  86.501 232.028  1.00 65.10           C  
ANISOU 2996  CA  ASP A 383     9423   9432   5882   1269   -103    166       C  
ATOM   2997  C   ASP A 383      38.868  86.937 230.562  1.00 63.77           C  
ANISOU 2997  C   ASP A 383     9239   9293   5699   1217    -65    118       C  
ATOM   2998  O   ASP A 383      39.660  86.572 229.683  1.00 64.40           O  
ANISOU 2998  O   ASP A 383     9327   9387   5753   1310    -34     66       O  
ATOM   2999  CB  ASP A 383      38.225  85.274 232.404  1.00 66.30           C  
ANISOU 2999  CB  ASP A 383     9746   9421   6025   1247   -140    189       C  
ATOM   3000  CG  ASP A 383      36.835  85.658 232.948  1.00 67.26           C  
ANISOU 3000  CG  ASP A 383     9883   9508   6163   1090   -159    241       C  
ATOM   3001  OD1 ASP A 383      36.662  86.792 233.476  1.00 69.53           O  
ANISOU 3001  OD1 ASP A 383    10054   9892   6472   1025   -153    269       O  
ATOM   3002  OD2 ASP A 383      35.921  84.803 232.875  1.00 67.25           O  
ANISOU 3002  OD2 ASP A 383    10013   9384   6156   1033   -180    253       O  
ATOM   3003  N   GLU A 384      37.804  87.694 230.290  1.00 61.48           N  
ANISOU 3003  N   GLU A 384     8927   9013   5420   1075    -65    137       N  
ATOM   3004  CA  GLU A 384      37.496  88.064 228.889  1.00 59.99           C  
ANISOU 3004  CA  GLU A 384     8737   8846   5210   1021    -37     99       C  
ATOM   3005  C   GLU A 384      38.414  89.174 228.386  1.00 58.38           C  
ANISOU 3005  C   GLU A 384     8389   8786   5007   1046      8     81       C  
ATOM   3006  O   GLU A 384      38.875  89.990 229.178  1.00 58.26           O  
ANISOU 3006  O   GLU A 384     8260   8854   5021   1047     10    108       O  
ATOM   3007  CB  GLU A 384      36.027  88.422 228.714  1.00 58.87           C  
ANISOU 3007  CB  GLU A 384     8624   8665   5079    868    -59    129       C  
ATOM   3008  CG  GLU A 384      35.136  87.229 229.009  1.00 61.32           C  
ANISOU 3008  CG  GLU A 384     9082   8832   5384    835    -99    141       C  
ATOM   3009  CD  GLU A 384      33.648  87.582 229.100  1.00 63.72           C  
ANISOU 3009  CD  GLU A 384     9394   9107   5709    681   -124    183       C  
ATOM   3010  OE1 GLU A 384      33.107  88.096 228.099  1.00 66.01           O  
ANISOU 3010  OE1 GLU A 384     9664   9427   5990    607   -119    169       O  
ATOM   3011  OE2 GLU A 384      33.015  87.327 230.159  1.00 63.10           O  
ANISOU 3011  OE2 GLU A 384     9340   8979   5654    637   -147    233       O  
ATOM   3012  N   PRO A 385      38.716  89.189 227.072  1.00 57.34           N  
ANISOU 3012  N   PRO A 385     8266   8682   4839   1064     45     33       N  
ATOM   3013  CA  PRO A 385      39.616  90.233 226.559  1.00 55.67           C  
ANISOU 3013  CA  PRO A 385     7918   8608   4626   1082     93     21       C  
ATOM   3014  C   PRO A 385      38.969  91.619 226.539  1.00 53.11           C  
ANISOU 3014  C   PRO A 385     7503   8348   4329    952     94     61       C  
ATOM   3015  O   PRO A 385      39.683  92.615 226.643  1.00 52.39           O  
ANISOU 3015  O   PRO A 385     7285   8365   4256    952    122     70       O  
ATOM   3016  CB  PRO A 385      39.928  89.764 225.128  1.00 56.32           C  
ANISOU 3016  CB  PRO A 385     8060   8688   4652   1127    134    -38       C  
ATOM   3017  CG  PRO A 385      38.760  88.901 224.741  1.00 56.98           C  
ANISOU 3017  CG  PRO A 385     8301   8638   4710   1069     96    -49       C  
ATOM   3018  CD  PRO A 385      38.279  88.252 226.013  1.00 58.00           C  
ANISOU 3018  CD  PRO A 385     8488   8673   4876   1067     44    -12       C  
ATOM   3019  N   VAL A 386      37.639  91.644 226.398  1.00 51.05           N  
ANISOU 3019  N   VAL A 386     7307   8018   4072    844     64     83       N  
ATOM   3020  CA  VAL A 386      36.807  92.841 226.353  1.00 49.02           C  
ANISOU 3020  CA  VAL A 386     6984   7800   3842    723     59    123       C  
ATOM   3021  C   VAL A 386      35.708  92.686 227.407  1.00 47.83           C  
ANISOU 3021  C   VAL A 386     6869   7578   3728    656     15    168       C  
ATOM   3022  O   VAL A 386      34.792  91.885 227.249  1.00 48.35           O  
ANISOU 3022  O   VAL A 386     7038   7551   3782    616    -16    170       O  
ATOM   3023  CB  VAL A 386      36.207  93.067 224.928  1.00 49.22           C  
ANISOU 3023  CB  VAL A 386     7045   7826   3829    658     68    109       C  
ATOM   3024  CG1 VAL A 386      35.490  91.813 224.409  1.00 52.12           C  
ANISOU 3024  CG1 VAL A 386     7560   8083   4159    651     37     82       C  
ATOM   3025  CG2 VAL A 386      35.243  94.254 224.878  1.00 47.88           C  
ANISOU 3025  CG2 VAL A 386     6814   7686   3690    539     57    157       C  
ATOM   3026  N   PHE A 387      35.809  93.466 228.477  1.00 46.26           N  
ANISOU 3026  N   PHE A 387     6585   7424   3569    640     13    202       N  
ATOM   3027  CA  PHE A 387      34.988  93.324 229.670  1.00 44.74           C  
ANISOU 3027  CA  PHE A 387     6416   7179   3406    596    -19    242       C  
ATOM   3028  C   PHE A 387      34.766  94.695 230.321  1.00 43.93           C  
ANISOU 3028  C   PHE A 387     6206   7142   3343    534     -9    276       C  
ATOM   3029  O   PHE A 387      35.278  95.679 229.836  1.00 44.26           O  
ANISOU 3029  O   PHE A 387     6164   7261   3391    526     17    268       O  
ATOM   3030  CB  PHE A 387      35.732  92.425 230.656  1.00 45.07           C  
ANISOU 3030  CB  PHE A 387     6493   7190   3440    692    -34    239       C  
ATOM   3031  CG  PHE A 387      36.992  93.043 231.222  1.00 43.15           C  
ANISOU 3031  CG  PHE A 387     6145   7044   3207    760    -19    232       C  
ATOM   3032  CD1 PHE A 387      38.212  92.877 230.584  1.00 41.93           C  
ANISOU 3032  CD1 PHE A 387     5955   6944   3032    852      6    193       C  
ATOM   3033  CD2 PHE A 387      36.961  93.772 232.412  1.00 40.80           C  
ANISOU 3033  CD2 PHE A 387     5782   6784   2935    732    -29    263       C  
ATOM   3034  CE1 PHE A 387      39.386  93.450 231.115  1.00 41.53           C  
ANISOU 3034  CE1 PHE A 387     5794   6991   2993    908     16    189       C  
ATOM   3035  CE2 PHE A 387      38.123  94.345 232.939  1.00 39.14           C  
ANISOU 3035  CE2 PHE A 387     5474   6665   2731    784    -24    254       C  
ATOM   3036  CZ  PHE A 387      39.334  94.186 232.292  1.00 39.94           C  
ANISOU 3036  CZ  PHE A 387     5530   6826   2818    869     -4    219       C  
ATOM   3037  N   THR A 388      34.036  94.758 231.434  1.00 43.32           N  
ANISOU 3037  N   THR A 388     6136   7034   3290    493    -27    312       N  
ATOM   3038  CA  THR A 388      33.936  95.984 232.238  1.00 42.22           C  
ANISOU 3038  CA  THR A 388     5907   6952   3184    452    -17    335       C  
ATOM   3039  C   THR A 388      33.983  95.601 233.716  1.00 43.10           C  
ANISOU 3039  C   THR A 388     6038   7041   3295    478    -34    355       C  
ATOM   3040  O   THR A 388      33.283  94.667 234.138  1.00 43.29           O  
ANISOU 3040  O   THR A 388     6146   6991   3311    467    -53    376       O  
ATOM   3041  CB  THR A 388      32.599  96.711 231.995  1.00 41.50           C  
ANISOU 3041  CB  THR A 388     5800   6847   3122    351    -14    367       C  
ATOM   3042  OG1 THR A 388      32.348  96.826 230.591  1.00 41.12           O  
ANISOU 3042  OG1 THR A 388     5759   6801   3062    322     -9    356       O  
ATOM   3043  CG2 THR A 388      32.594  98.086 232.648  1.00 38.92           C  
ANISOU 3043  CG2 THR A 388     5383   6576   2828    318      4    381       C  
ATOM   3044  N   ALA A 389      34.778  96.323 234.508  1.00 43.43           N  
ANISOU 3044  N   ALA A 389     6007   7150   3345    504    -30    351       N  
ATOM   3045  CA  ALA A 389      34.798  96.110 235.958  1.00 44.36           C  
ANISOU 3045  CA  ALA A 389     6141   7260   3455    521    -48    371       C  
ATOM   3046  C   ALA A 389      34.840  97.401 236.758  1.00 44.75           C  
ANISOU 3046  C   ALA A 389     6111   7369   3523    481    -38    375       C  
ATOM   3047  O   ALA A 389      35.545  98.319 236.396  1.00 45.55           O  
ANISOU 3047  O   ALA A 389     6134   7537   3638    479    -25    353       O  
ATOM   3048  CB  ALA A 389      35.944  95.248 236.336  1.00 44.32           C  
ANISOU 3048  CB  ALA A 389     6157   7262   3421    623    -71    357       C  
ATOM   3049  N   HIS A 390      34.067  97.486 237.832  1.00 45.40           N  
ANISOU 3049  N   HIS A 390     6219   7427   3604    445    -40    403       N  
ATOM   3050  CA  HIS A 390      34.310  98.506 238.849  1.00 45.94           C  
ANISOU 3050  CA  HIS A 390     6232   7548   3674    428    -36    398       C  
ATOM   3051  C   HIS A 390      34.229  97.867 240.229  1.00 45.62           C  
ANISOU 3051  C   HIS A 390     6247   7487   3597    453    -56    420       C  
ATOM   3052  O   HIS A 390      33.529  96.877 240.433  1.00 45.71           O  
ANISOU 3052  O   HIS A 390     6339   7434   3595    451    -61    451       O  
ATOM   3053  CB  HIS A 390      33.302  99.679 238.830  1.00 46.22           C  
ANISOU 3053  CB  HIS A 390     6231   7584   3745    347     -4    407       C  
ATOM   3054  CG  HIS A 390      32.904 100.162 237.470  1.00 48.86           C  
ANISOU 3054  CG  HIS A 390     6536   7915   4113    308     15    405       C  
ATOM   3055  ND1 HIS A 390      31.849  99.614 236.763  1.00 51.05           N  
ANISOU 3055  ND1 HIS A 390     6856   8140   4401    275     19    428       N  
ATOM   3056  CD2 HIS A 390      33.357 101.204 236.727  1.00 51.51           C  
ANISOU 3056  CD2 HIS A 390     6805   8293   4472    290     30    387       C  
ATOM   3057  CE1 HIS A 390      31.693 100.278 235.627  1.00 52.95           C  
ANISOU 3057  CE1 HIS A 390     7058   8394   4666    244     31    424       C  
ATOM   3058  NE2 HIS A 390      32.602 101.243 235.577  1.00 53.18           N  
ANISOU 3058  NE2 HIS A 390     7024   8479   4704    254     41    401       N  
ATOM   3059  N   VAL A 391      34.953  98.470 241.165  1.00 45.15           N  
ANISOU 3059  N   VAL A 391     6148   7487   3521    469    -70    406       N  
ATOM   3060  CA  VAL A 391      34.809  98.230 242.587  1.00 44.78           C  
ANISOU 3060  CA  VAL A 391     6144   7436   3433    477    -85    426       C  
ATOM   3061  C   VAL A 391      33.513  98.857 243.038  1.00 44.30           C  
ANISOU 3061  C   VAL A 391     6096   7352   3384    401    -46    443       C  
ATOM   3062  O   VAL A 391      33.203  99.997 242.659  1.00 43.38           O  
ANISOU 3062  O   VAL A 391     5923   7257   3305    353    -18    424       O  
ATOM   3063  CB  VAL A 391      36.016  98.844 243.375  1.00 45.26           C  
ANISOU 3063  CB  VAL A 391     6149   7578   3469    509   -117    398       C  
ATOM   3064  CG1 VAL A 391      36.747  99.878 242.542  1.00 45.15           C  
ANISOU 3064  CG1 VAL A 391     6038   7623   3493    492   -108    358       C  
ATOM   3065  CG2 VAL A 391      35.604  99.454 244.727  1.00 45.33           C  
ANISOU 3065  CG2 VAL A 391     6175   7603   3445    472   -113    401       C  
ATOM   3066  N   VAL A 392      32.743  98.123 243.838  1.00 44.63           N  
ANISOU 3066  N   VAL A 392     6211   7350   3396    392    -42    481       N  
ATOM   3067  CA  VAL A 392      31.517  98.702 244.372  1.00 44.64           C  
ANISOU 3067  CA  VAL A 392     6217   7340   3406    327      3    499       C  
ATOM   3068  C   VAL A 392      31.773  99.349 245.733  1.00 46.17           C  
ANISOU 3068  C   VAL A 392     6410   7579   3556    329      4    486       C  
ATOM   3069  O   VAL A 392      31.861  98.669 246.776  1.00 47.38           O  
ANISOU 3069  O   VAL A 392     6624   7727   3650    353    -12    511       O  
ATOM   3070  CB  VAL A 392      30.362  97.710 244.391  1.00 43.94           C  
ANISOU 3070  CB  VAL A 392     6196   7185   3315    295     20    549       C  
ATOM   3071  CG1 VAL A 392      29.130  98.419 244.789  1.00 43.35           C  
ANISOU 3071  CG1 VAL A 392     6101   7112   3258    232     72    564       C  
ATOM   3072  CG2 VAL A 392      30.146  97.167 243.022  1.00 43.74           C  
ANISOU 3072  CG2 VAL A 392     6174   7118   3329    287     12    551       C  
ATOM   3073  N   CYS A 393      31.921 100.669 245.746  1.00 47.11           N  
ANISOU 3073  N   CYS A 393     6466   7739   3696    304     22    447       N  
ATOM   3074  CA  CYS A 393      32.271 101.308 247.026  1.00 48.78           C  
ANISOU 3074  CA  CYS A 393     6683   7992   3858    305     17    424       C  
ATOM   3075  C   CYS A 393      31.078 101.474 247.929  1.00 48.30           C  
ANISOU 3075  C   CYS A 393     6664   7913   3774    269     67    445       C  
ATOM   3076  O   CYS A 393      31.230 101.487 249.162  1.00 48.87           O  
ANISOU 3076  O   CYS A 393     6778   8011   3781    278     62    442       O  
ATOM   3077  CB  CYS A 393      33.046 102.610 246.851  1.00 48.70           C  
ANISOU 3077  CB  CYS A 393     6603   8029   3870    291      9    369       C  
ATOM   3078  SG  CYS A 393      34.810 102.230 246.727  1.00 55.06           S  
ANISOU 3078  SG  CYS A 393     7373   8894   4654    349    -65    347       S  
ATOM   3079  N   SER A 394      29.895 101.570 247.312  1.00 46.96           N  
ANISOU 3079  N   SER A 394     6481   7706   3654    230    116    468       N  
ATOM   3080  CA  SER A 394      28.653 101.624 248.069  1.00 46.66           C  
ANISOU 3080  CA  SER A 394     6472   7655   3602    197    172    495       C  
ATOM   3081  C   SER A 394      28.342 100.300 248.821  1.00 46.63           C  
ANISOU 3081  C   SER A 394     6548   7629   3541    203    167    549       C  
ATOM   3082  O   SER A 394      27.239 100.130 249.356  1.00 46.65           O  
ANISOU 3082  O   SER A 394     6573   7619   3531    169    219    583       O  
ATOM   3083  CB  SER A 394      27.516 101.975 247.129  1.00 46.22           C  
ANISOU 3083  CB  SER A 394     6370   7572   3620    156    216    512       C  
ATOM   3084  OG  SER A 394      27.165 100.837 246.369  1.00 46.84           O  
ANISOU 3084  OG  SER A 394     6468   7610   3716    147    199    554       O  
ATOM   3085  N   GLN A 395      29.306  99.369 248.828  1.00 45.89           N  
ANISOU 3085  N   GLN A 395     6494   7529   3413    247    108    558       N  
ATOM   3086  CA  GLN A 395      29.160  98.084 249.489  1.00 45.70           C  
ANISOU 3086  CA  GLN A 395     6557   7474   3334    260     94    613       C  
ATOM   3087  C   GLN A 395      30.395  97.757 250.332  1.00 46.52           C  
ANISOU 3087  C   GLN A 395     6699   7609   3366    321     35    605       C  
ATOM   3088  O   GLN A 395      30.489  96.710 250.969  1.00 46.74           O  
ANISOU 3088  O   GLN A 395     6806   7613   3339    345     12    651       O  
ATOM   3089  CB  GLN A 395      28.891  97.007 248.464  1.00 44.98           C  
ANISOU 3089  CB  GLN A 395     6490   7319   3283    256     78    647       C  
ATOM   3090  CG  GLN A 395      27.473  97.017 247.944  1.00 44.10           C  
ANISOU 3090  CG  GLN A 395     6359   7174   3221    186    131    675       C  
ATOM   3091  CD  GLN A 395      27.222  95.993 246.816  1.00 44.01           C  
ANISOU 3091  CD  GLN A 395     6374   7098   3250    172    107    700       C  
ATOM   3092  OE1 GLN A 395      27.891  94.959 246.721  1.00 43.81           O  
ANISOU 3092  OE1 GLN A 395     6413   7033   3199    214     62    713       O  
ATOM   3093  NE2 GLN A 395      26.235  96.280 245.969  1.00 43.47           N  
ANISOU 3093  NE2 GLN A 395     6258   7017   3241    115    136    706       N  
ATOM   3094  N   MET A 396      31.340  98.678 250.337  1.00 46.61           N  
ANISOU 3094  N   MET A 396     6654   7677   3379    343      7    549       N  
ATOM   3095  CA  MET A 396      32.526  98.526 251.120  1.00 47.57           C  
ANISOU 3095  CA  MET A 396     6793   7844   3437    396    -54    536       C  
ATOM   3096  C   MET A 396      32.339  99.403 252.298  1.00 48.22           C  
ANISOU 3096  C   MET A 396     6887   7972   3462    370    -33    512       C  
ATOM   3097  O   MET A 396      32.812 100.540 252.295  1.00 47.94           O  
ANISOU 3097  O   MET A 396     6795   7981   3440    356    -38    454       O  
ATOM   3098  CB  MET A 396      33.721  99.050 250.352  1.00 47.97           C  
ANISOU 3098  CB  MET A 396     6763   7937   3527    427    -99    487       C  
ATOM   3099  CG  MET A 396      33.740  98.610 248.896  1.00 48.90           C  
ANISOU 3099  CG  MET A 396     6848   8014   3717    438    -98    491       C  
ATOM   3100  SD  MET A 396      34.916  97.302 248.626  1.00 49.19           S  
ANISOU 3100  SD  MET A 396     6910   8045   3734    532   -167    511       S  
ATOM   3101  CE  MET A 396      34.910  96.396 250.185  1.00 51.62           C  
ANISOU 3101  CE  MET A 396     7322   8345   3946    566   -199    563       C  
ATOM   3102  N   LYS A 397      31.666  98.877 253.316  1.00 49.00           N  
ANISOU 3102  N   LYS A 397     7066   8059   3494    359     -7    556       N  
ATOM   3103  CA  LYS A 397      31.373  99.663 254.494  1.00 49.70           C  
ANISOU 3103  CA  LYS A 397     7178   8189   3516    334     24    532       C  
ATOM   3104  C   LYS A 397      32.365  99.461 255.649  1.00 50.84           C  
ANISOU 3104  C   LYS A 397     7372   8387   3559    374    -43    529       C  
ATOM   3105  O   LYS A 397      32.235 100.039 256.744  1.00 51.50           O  
ANISOU 3105  O   LYS A 397     7491   8509   3566    357    -27    507       O  
ATOM   3106  CB  LYS A 397      29.950  99.376 254.935  1.00 49.86           C  
ANISOU 3106  CB  LYS A 397     7246   8177   3520    291    105    579       C  
ATOM   3107  CG  LYS A 397      28.935  99.824 253.925  1.00 50.94           C  
ANISOU 3107  CG  LYS A 397     7321   8280   3754    248    169    574       C  
ATOM   3108  CD  LYS A 397      29.075 101.297 253.556  1.00 51.05           C  
ANISOU 3108  CD  LYS A 397     7260   8321   3816    235    187    501       C  
ATOM   3109  CE  LYS A 397      28.145 101.604 252.413  1.00 50.83           C  
ANISOU 3109  CE  LYS A 397     7170   8256   3887    203    236    508       C  
ATOM   3110  NZ  LYS A 397      27.832 103.037 252.444  1.00 53.29           N  
ANISOU 3110  NZ  LYS A 397     7435   8585   4229    185    281    452       N  
ATOM   3111  N   THR A 398      33.369  98.633 255.431  1.00 51.29           N  
ANISOU 3111  N   THR A 398     7434   8447   3609    432   -120    550       N  
ATOM   3112  CA  THR A 398      34.206  98.297 256.563  1.00 52.30           C  
ANISOU 3112  CA  THR A 398     7613   8624   3636    474   -188    562       C  
ATOM   3113  C   THR A 398      35.669  98.655 256.327  1.00 52.51           C  
ANISOU 3113  C   THR A 398     7566   8712   3672    517   -275    516       C  
ATOM   3114  O   THR A 398      36.320  98.181 255.400  1.00 51.72           O  
ANISOU 3114  O   THR A 398     7418   8601   3631    562   -311    522       O  
ATOM   3115  CB  THR A 398      33.915  96.847 257.138  1.00 52.98           C  
ANISOU 3115  CB  THR A 398     7807   8665   3659    507   -200    652       C  
ATOM   3116  OG1 THR A 398      35.109  96.064 257.119  1.00 54.62           O  
ANISOU 3116  OG1 THR A 398     8020   8886   3848    588   -293    673       O  
ATOM   3117  CG2 THR A 398      32.809  96.095 256.354  1.00 51.78           C  
ANISOU 3117  CG2 THR A 398     7680   8424   3572    478   -137    702       C  
ATOM   3118  N   TYR A 399      36.147  99.561 257.170  1.00 53.94           N  
ANISOU 3118  N   TYR A 399     7737   8963   3794    498   -302    466       N  
ATOM   3119  CA  TYR A 399      37.490 100.120 257.069  1.00 54.92           C  
ANISOU 3119  CA  TYR A 399     7782   9159   3924    518   -382    415       C  
ATOM   3120  C   TYR A 399      38.595  99.071 257.257  1.00 56.39           C  
ANISOU 3120  C   TYR A 399     7971   9380   4076    604   -478    458       C  
ATOM   3121  O   TYR A 399      39.618  99.110 256.570  1.00 56.30           O  
ANISOU 3121  O   TYR A 399     7870   9406   4115    639   -530    437       O  
ATOM   3122  CB  TYR A 399      37.649 101.259 258.073  1.00 54.98           C  
ANISOU 3122  CB  TYR A 399     7798   9227   3863    468   -393    353       C  
ATOM   3123  CG  TYR A 399      38.962 101.972 257.935  1.00 55.06           C  
ANISOU 3123  CG  TYR A 399     7719   9313   3888    466   -473    295       C  
ATOM   3124  CD1 TYR A 399      39.287 102.664 256.753  1.00 52.79           C  
ANISOU 3124  CD1 TYR A 399     7329   9023   3707    440   -458    253       C  
ATOM   3125  CD2 TYR A 399      39.893 101.950 258.979  1.00 56.00           C  
ANISOU 3125  CD2 TYR A 399     7852   9513   3912    486   -565    286       C  
ATOM   3126  CE1 TYR A 399      40.513 103.328 256.619  1.00 53.41           C  
ANISOU 3126  CE1 TYR A 399     7316   9176   3801    428   -529    203       C  
ATOM   3127  CE2 TYR A 399      41.119 102.601 258.863  1.00 56.72           C  
ANISOU 3127  CE2 TYR A 399     7849   9682   4018    475   -643    234       C  
ATOM   3128  CZ  TYR A 399      41.422 103.288 257.680  1.00 56.66           C  
ANISOU 3128  CZ  TYR A 399     7736   9669   4122    443   -622    193       C  
ATOM   3129  OH  TYR A 399      42.629 103.929 257.581  1.00 57.94           O  
ANISOU 3129  OH  TYR A 399     7801   9912   4299    422   -696    146       O  
ATOM   3130  N   ASP A 400      38.359  98.138 258.178  1.00 58.10           N  
ANISOU 3130  N   ASP A 400     8289   9581   4204    639   -496    521       N  
ATOM   3131  CA  ASP A 400      39.267  97.038 258.471  1.00 60.03           C  
ANISOU 3131  CA  ASP A 400     8558   9844   4408    730   -584    575       C  
ATOM   3132  C   ASP A 400      39.197  95.869 257.479  1.00 59.62           C  
ANISOU 3132  C   ASP A 400     8515   9713   4425    791   -575    627       C  
ATOM   3133  O   ASP A 400      39.952  94.915 257.614  1.00 60.37           O  
ANISOU 3133  O   ASP A 400     8631   9811   4497    880   -645    672       O  
ATOM   3134  CB  ASP A 400      38.968  96.507 259.881  1.00 62.22           C  
ANISOU 3134  CB  ASP A 400     8957  10128   4556    740   -604    629       C  
ATOM   3135  CG  ASP A 400      40.202  95.849 260.570  1.00 66.60           C  
ANISOU 3135  CG  ASP A 400     9522  10746   5038    829   -725    665       C  
ATOM   3136  OD1 ASP A 400      41.326  95.887 259.984  1.00 68.57           O  
ANISOU 3136  OD1 ASP A 400     9670  11045   5339    882   -792    640       O  
ATOM   3137  OD2 ASP A 400      40.039  95.310 261.715  1.00 70.81           O  
ANISOU 3137  OD2 ASP A 400    10162  11285   5458    846   -751    720       O  
ATOM   3138  N   ALA A 401      38.312  95.937 256.485  1.00 58.95           N  
ANISOU 3138  N   ALA A 401     8418   9557   4424    748   -494    620       N  
ATOM   3139  CA  ALA A 401      38.052  94.794 255.580  1.00 58.78           C  
ANISOU 3139  CA  ALA A 401     8429   9446   4459    792   -478    668       C  
ATOM   3140  C   ALA A 401      39.272  94.203 254.855  1.00 59.14           C  
ANISOU 3140  C   ALA A 401     8417   9507   4546    890   -545    666       C  
ATOM   3141  O   ALA A 401      40.332  94.845 254.734  1.00 59.15           O  
ANISOU 3141  O   ALA A 401     8317   9596   4560    913   -594    619       O  
ATOM   3142  CB  ALA A 401      36.942  95.115 254.579  1.00 57.59           C  
ANISOU 3142  CB  ALA A 401     8260   9231   4391    720   -388    652       C  
ATOM   3143  N   SER A 402      39.106  92.961 254.399  1.00 59.34           N  
ANISOU 3143  N   SER A 402     8510   9446   4591    946   -545    718       N  
ATOM   3144  CA  SER A 402      40.119  92.285 253.589  1.00 59.83           C  
ANISOU 3144  CA  SER A 402     8529   9504   4698   1049   -592    717       C  
ATOM   3145  C   SER A 402      39.491  91.764 252.292  1.00 58.82           C  
ANISOU 3145  C   SER A 402     8421   9279   4650   1039   -534    716       C  
ATOM   3146  O   SER A 402      40.190  91.287 251.404  1.00 58.76           O  
ANISOU 3146  O   SER A 402     8377   9261   4688   1115   -552    702       O  
ATOM   3147  CB  SER A 402      40.805  91.154 254.374  1.00 61.12           C  
ANISOU 3147  CB  SER A 402     8768   9658   4796   1157   -669    780       C  
ATOM   3148  OG  SER A 402      39.850  90.323 255.021  1.00 62.91           O  
ANISOU 3148  OG  SER A 402     9139   9792   4971   1136   -647    851       O  
ATOM   3149  N   LEU A 403      38.167  91.857 252.203  1.00 58.02           N  
ANISOU 3149  N   LEU A 403     8374   9111   4559    945   -464    729       N  
ATOM   3150  CA  LEU A 403      37.447  91.429 251.014  1.00 56.99           C  
ANISOU 3150  CA  LEU A 403     8264   8892   4497    918   -413    728       C  
ATOM   3151  C   LEU A 403      36.972  92.678 250.300  1.00 55.72           C  
ANISOU 3151  C   LEU A 403     8008   8770   4394    830   -357    670       C  
ATOM   3152  O   LEU A 403      36.378  93.589 250.926  1.00 55.91           O  
ANISOU 3152  O   LEU A 403     8015   8831   4398    755   -325    658       O  
ATOM   3153  CB  LEU A 403      36.286  90.484 251.360  1.00 56.95           C  
ANISOU 3153  CB  LEU A 403     8391   8779   4469    876   -381    794       C  
ATOM   3154  CG  LEU A 403      36.753  89.079 251.779  1.00 59.60           C  
ANISOU 3154  CG  LEU A 403     8837   9047   4763    970   -435    856       C  
ATOM   3155  CD1 LEU A 403      35.765  88.358 252.716  1.00 61.09           C  
ANISOU 3155  CD1 LEU A 403     9158   9161   4893    920   -415    935       C  
ATOM   3156  CD2 LEU A 403      37.147  88.185 250.590  1.00 60.48           C  
ANISOU 3156  CD2 LEU A 403     8968   9081   4931   1042   -447    846       C  
ATOM   3157  N   LEU A 404      37.267  92.723 248.999  1.00 54.04           N  
ANISOU 3157  N   LEU A 404     7736   8547   4248    847   -346    633       N  
ATOM   3158  CA  LEU A 404      36.930  93.844 248.147  1.00 51.87           C  
ANISOU 3158  CA  LEU A 404     7372   8305   4032    776   -299    583       C  
ATOM   3159  C   LEU A 404      35.886  93.441 247.101  1.00 51.04           C  
ANISOU 3159  C   LEU A 404     7305   8113   3977    727   -250    592       C  
ATOM   3160  O   LEU A 404      36.043  92.447 246.378  1.00 50.79           O  
ANISOU 3160  O   LEU A 404     7319   8018   3961    776   -262    602       O  
ATOM   3161  CB  LEU A 404      38.205  94.401 247.524  1.00 51.72           C  
ANISOU 3161  CB  LEU A 404     7242   8367   4042    826   -327    532       C  
ATOM   3162  CG  LEU A 404      38.243  94.998 246.113  1.00 51.65           C  
ANISOU 3162  CG  LEU A 404     7154   8370   4103    798   -289    488       C  
ATOM   3163  CD1 LEU A 404      39.170  96.207 246.076  1.00 51.03           C  
ANISOU 3163  CD1 LEU A 404     6955   8397   4038    786   -302    440       C  
ATOM   3164  CD2 LEU A 404      38.681  93.974 245.062  1.00 51.10           C  
ANISOU 3164  CD2 LEU A 404     7105   8255   4056    874   -296    488       C  
ATOM   3165  N   ARG A 405      34.821  94.235 247.037  1.00 49.78           N  
ANISOU 3165  N   ARG A 405     7124   7950   3840    632   -198    587       N  
ATOM   3166  CA  ARG A 405      33.642  93.937 246.254  1.00 48.51           C  
ANISOU 3166  CA  ARG A 405     6996   7717   3719    569   -155    604       C  
ATOM   3167  C   ARG A 405      33.741  94.513 244.827  1.00 47.78           C  
ANISOU 3167  C   ARG A 405     6827   7637   3689    553   -137    559       C  
ATOM   3168  O   ARG A 405      33.972  95.717 244.642  1.00 47.56           O  
ANISOU 3168  O   ARG A 405     6711   7674   3684    528   -122    522       O  
ATOM   3169  CB  ARG A 405      32.426  94.473 247.013  1.00 47.96           C  
ANISOU 3169  CB  ARG A 405     6938   7646   3638    484   -108    627       C  
ATOM   3170  CG  ARG A 405      31.084  94.262 246.340  1.00 48.20           C  
ANISOU 3170  CG  ARG A 405     6987   7616   3712    407    -63    650       C  
ATOM   3171  CD  ARG A 405      30.663  92.781 246.216  1.00 49.55           C  
ANISOU 3171  CD  ARG A 405     7263   7692   3871    409    -77    700       C  
ATOM   3172  NE  ARG A 405      30.589  92.062 247.496  1.00 49.95           N  
ANISOU 3172  NE  ARG A 405     7402   7720   3858    422    -87    752       N  
ATOM   3173  CZ  ARG A 405      29.675  92.272 248.437  1.00 49.03           C  
ANISOU 3173  CZ  ARG A 405     7304   7612   3712    360    -46    789       C  
ATOM   3174  NH1 ARG A 405      28.757  93.205 248.269  1.00 47.58           N  
ANISOU 3174  NH1 ARG A 405     7053   7461   3565    288      7    775       N  
ATOM   3175  NH2 ARG A 405      29.684  91.553 249.554  1.00 49.64           N  
ANISOU 3175  NH2 ARG A 405     7469   7668   3723    375    -57    840       N  
ATOM   3176  N   LEU A 406      33.577  93.641 243.821  1.00 47.56           N  
ANISOU 3176  N   LEU A 406     6842   7544   3684    567   -140    564       N  
ATOM   3177  CA  LEU A 406      33.612  94.021 242.388  1.00 46.25           C  
ANISOU 3177  CA  LEU A 406     6622   7383   3566    552   -124    527       C  
ATOM   3178  C   LEU A 406      32.365  93.580 241.664  1.00 46.02           C  
ANISOU 3178  C   LEU A 406     6641   7280   3563    482   -101    548       C  
ATOM   3179  O   LEU A 406      31.846  92.489 241.924  1.00 46.81           O  
ANISOU 3179  O   LEU A 406     6836   7303   3646    476   -111    584       O  
ATOM   3180  CB  LEU A 406      34.760  93.331 241.661  1.00 46.35           C  
ANISOU 3180  CB  LEU A 406     6640   7394   3576    645   -153    501       C  
ATOM   3181  CG  LEU A 406      36.114  93.257 242.346  1.00 46.73           C  
ANISOU 3181  CG  LEU A 406     6658   7502   3593    739   -191    491       C  
ATOM   3182  CD1 LEU A 406      36.932  92.062 241.854  1.00 45.23           C  
ANISOU 3182  CD1 LEU A 406     6519   7273   3394    845   -218    486       C  
ATOM   3183  CD2 LEU A 406      36.838  94.609 242.197  1.00 45.59           C  
ANISOU 3183  CD2 LEU A 406     6388   7465   3469    727   -183    450       C  
ATOM   3184  N   ARG A 407      31.929  94.429 240.732  1.00 45.21           N  
ANISOU 3184  N   ARG A 407     6473   7202   3501    429    -75    526       N  
ATOM   3185  CA  ARG A 407      30.911  94.139 239.701  1.00 44.57           C  
ANISOU 3185  CA  ARG A 407     6417   7069   3451    366    -63    534       C  
ATOM   3186  C   ARG A 407      31.651  93.908 238.358  1.00 43.99           C  
ANISOU 3186  C   ARG A 407     6336   6995   3383    410    -76    494       C  
ATOM   3187  O   ARG A 407      32.424  94.758 237.923  1.00 43.56           O  
ANISOU 3187  O   ARG A 407     6204   7009   3340    435    -68    461       O  
ATOM   3188  CB  ARG A 407      29.987  95.364 239.580  1.00 44.23           C  
ANISOU 3188  CB  ARG A 407     6296   7064   3444    287    -29    539       C  
ATOM   3189  CG  ARG A 407      28.625  95.169 238.971  1.00 43.98           C  
ANISOU 3189  CG  ARG A 407     6280   6990   3442    205    -17    566       C  
ATOM   3190  CD  ARG A 407      27.810  96.437 239.111  1.00 45.07           C  
ANISOU 3190  CD  ARG A 407     6335   7174   3615    149     18    575       C  
ATOM   3191  NE  ARG A 407      27.780  97.172 237.863  1.00 51.53           N  
ANISOU 3191  NE  ARG A 407     7095   8016   4466    131     20    554       N  
ATOM   3192  CZ  ARG A 407      28.417  98.325 237.625  1.00 54.81           C  
ANISOU 3192  CZ  ARG A 407     7440   8487   4896    151     31    526       C  
ATOM   3193  NH1 ARG A 407      29.127  98.917 238.590  1.00 54.96           N  
ANISOU 3193  NH1 ARG A 407     7434   8546   4902    184     41    510       N  
ATOM   3194  NH2 ARG A 407      28.324  98.899 236.412  1.00 54.37           N  
ANISOU 3194  NH2 ARG A 407     7344   8447   4867    131     32    516       N  
ATOM   3195  N   TYR A 408      31.427  92.757 237.727  1.00 43.61           N  
ANISOU 3195  N   TYR A 408     6375   6870   3326    417    -93    496       N  
ATOM   3196  CA  TYR A 408      32.135  92.365 236.518  1.00 43.55           C  
ANISOU 3196  CA  TYR A 408     6382   6854   3313    469   -101    455       C  
ATOM   3197  C   TYR A 408      31.112  91.968 235.519  1.00 43.96           C  
ANISOU 3197  C   TYR A 408     6481   6846   3374    397   -103    457       C  
ATOM   3198  O   TYR A 408      30.148  91.282 235.877  1.00 44.66           O  
ANISOU 3198  O   TYR A 408     6640   6866   3464    340   -113    492       O  
ATOM   3199  CB  TYR A 408      32.975  91.130 236.770  1.00 44.10           C  
ANISOU 3199  CB  TYR A 408     6536   6871   3350    566   -126    448       C  
ATOM   3200  CG  TYR A 408      33.496  90.460 235.523  1.00 43.87           C  
ANISOU 3200  CG  TYR A 408     6551   6809   3310    620   -130    405       C  
ATOM   3201  CD1 TYR A 408      34.653  90.910 234.922  1.00 45.60           C  
ANISOU 3201  CD1 TYR A 408     6698   7102   3524    693   -117    362       C  
ATOM   3202  CD2 TYR A 408      32.851  89.353 234.957  1.00 44.37           C  
ANISOU 3202  CD2 TYR A 408     6730   6765   3362    596   -145    405       C  
ATOM   3203  CE1 TYR A 408      35.155  90.304 233.760  1.00 45.68           C  
ANISOU 3203  CE1 TYR A 408     6750   7089   3518    749   -111    319       C  
ATOM   3204  CE2 TYR A 408      33.358  88.722 233.816  1.00 43.23           C  
ANISOU 3204  CE2 TYR A 408     6639   6587   3199    651   -147    357       C  
ATOM   3205  CZ  TYR A 408      34.508  89.217 233.230  1.00 43.89           C  
ANISOU 3205  CZ  TYR A 408     6647   6753   3276    731   -126    314       C  
ATOM   3206  OH  TYR A 408      35.067  88.653 232.126  1.00 43.67           O  
ANISOU 3206  OH  TYR A 408     6663   6704   3224    794   -117    264       O  
ATOM   3207  N   SER A 409      31.354  92.341 234.261  1.00 43.89           N  
ANISOU 3207  N   SER A 409     6441   6867   3370    398    -96    421       N  
ATOM   3208  CA  SER A 409      30.372  92.204 233.172  1.00 43.46           C  
ANISOU 3208  CA  SER A 409     6414   6776   3321    320   -102    420       C  
ATOM   3209  C   SER A 409      31.028  92.184 231.793  1.00 43.89           C  
ANISOU 3209  C   SER A 409     6473   6850   3355    358    -99    371       C  
ATOM   3210  O   SER A 409      32.149  92.660 231.588  1.00 43.54           O  
ANISOU 3210  O   SER A 409     6371   6870   3302    427    -79    343       O  
ATOM   3211  CB  SER A 409      29.418  93.387 233.225  1.00 42.61           C  
ANISOU 3211  CB  SER A 409     6219   6719   3251    232    -87    450       C  
ATOM   3212  OG  SER A 409      28.201  93.065 232.632  1.00 42.59           O  
ANISOU 3212  OG  SER A 409     6251   6673   3260    146   -104    469       O  
ATOM   3213  N   SER A 410      30.315  91.625 230.838  1.00 44.68           N  
ANISOU 3213  N   SER A 410     6639   6896   3443    306   -117    362       N  
ATOM   3214  CA  SER A 410      30.640  91.863 229.450  1.00 45.62           C  
ANISOU 3214  CA  SER A 410     6750   7045   3538    314   -110    323       C  
ATOM   3215  C   SER A 410      29.357  91.767 228.634  1.00 46.12           C  
ANISOU 3215  C   SER A 410     6847   7074   3602    209   -137    336       C  
ATOM   3216  O   SER A 410      28.393  91.127 229.043  1.00 46.20           O  
ANISOU 3216  O   SER A 410     6912   7018   3625    145   -164    363       O  
ATOM   3217  CB  SER A 410      31.639  90.828 228.958  1.00 46.50           C  
ANISOU 3217  CB  SER A 410     6946   7116   3606    412   -109    271       C  
ATOM   3218  OG  SER A 410      30.959  89.652 228.551  1.00 47.45           O  
ANISOU 3218  OG  SER A 410     7193   7130   3704    378   -141    261       O  
ATOM   3219  N   MET A 411      29.361  92.386 227.463  1.00 46.73           N  
ANISOU 3219  N   MET A 411     6890   7201   3663    188   -132    318       N  
ATOM   3220  CA  MET A 411      28.238  92.306 226.536  1.00 47.13           C  
ANISOU 3220  CA  MET A 411     6972   7231   3706     94   -166    326       C  
ATOM   3221  C   MET A 411      27.760  90.867 226.244  1.00 47.69           C  
ANISOU 3221  C   MET A 411     7177   7196   3746     66   -206    305       C  
ATOM   3222  O   MET A 411      26.732  90.668 225.617  1.00 48.02           O  
ANISOU 3222  O   MET A 411     7249   7212   3783    -25   -244    315       O  
ATOM   3223  CB  MET A 411      28.618  93.010 225.241  1.00 47.27           C  
ANISOU 3223  CB  MET A 411     6955   7314   3690    100   -154    302       C  
ATOM   3224  CG  MET A 411      28.720  94.512 225.363  1.00 47.19           C  
ANISOU 3224  CG  MET A 411     6820   7396   3716     90   -125    335       C  
ATOM   3225  SD  MET A 411      28.907  95.262 223.732  1.00 49.59           S  
ANISOU 3225  SD  MET A 411     7103   7765   3975     74   -119    321       S  
ATOM   3226  CE  MET A 411      30.584  94.719 223.357  1.00 52.44           C  
ANISOU 3226  CE  MET A 411     7501   8143   4280    191    -74    255       C  
ATOM   3227  N   THR A 412      28.519  89.880 226.705  1.00 48.10           N  
ANISOU 3227  N   THR A 412     7311   7184   3779    145   -200    277       N  
ATOM   3228  CA  THR A 412      28.190  88.458 226.549  1.00 48.49           C  
ANISOU 3228  CA  THR A 412     7506   7116   3803    129   -235    255       C  
ATOM   3229  C   THR A 412      27.763  87.839 227.897  1.00 48.12           C  
ANISOU 3229  C   THR A 412     7493   7000   3790    110   -245    300       C  
ATOM   3230  O   THR A 412      26.782  87.137 227.998  1.00 48.06           O  
ANISOU 3230  O   THR A 412     7554   6916   3789     21   -280    321       O  
ATOM   3231  CB  THR A 412      29.414  87.736 225.979  1.00 48.96           C  
ANISOU 3231  CB  THR A 412     7648   7144   3811    247   -217    187       C  
ATOM   3232  OG1 THR A 412      29.324  87.727 224.557  1.00 48.85           O  
ANISOU 3232  OG1 THR A 412     7672   7140   3748    224   -225    141       O  
ATOM   3233  CG2 THR A 412      29.534  86.310 226.511  1.00 51.07           C  
ANISOU 3233  CG2 THR A 412     8053   7282   4068    287   -236    174       C  
ATOM   3234  N   THR A 413      28.510  88.162 228.930  1.00 47.49           N  
ANISOU 3234  N   THR A 413     7359   6955   3728    187   -215    318       N  
ATOM   3235  CA  THR A 413      28.361  87.595 230.242  1.00 48.14           C  
ANISOU 3235  CA  THR A 413     7480   6983   3830    192   -220    359       C  
ATOM   3236  C   THR A 413      27.450  88.448 231.127  1.00 47.52           C  
ANISOU 3236  C   THR A 413     7303   6958   3795    109   -210    422       C  
ATOM   3237  O   THR A 413      27.817  89.566 231.474  1.00 47.35           O  
ANISOU 3237  O   THR A 413     7170   7031   3792    136   -181    430       O  
ATOM   3238  CB  THR A 413      29.769  87.544 230.868  1.00 48.23           C  
ANISOU 3238  CB  THR A 413     7479   7018   3828    331   -196    342       C  
ATOM   3239  OG1 THR A 413      30.510  86.494 230.239  1.00 50.34           O  
ANISOU 3239  OG1 THR A 413     7856   7212   4057    415   -204    289       O  
ATOM   3240  CG2 THR A 413      29.756  87.369 232.383  1.00 47.54           C  
ANISOU 3240  CG2 THR A 413     7392   6914   3758    345   -195    393       C  
ATOM   3241  N   PRO A 414      26.278  87.918 231.532  1.00 47.69           N  
ANISOU 3241  N   PRO A 414     7366   6919   3833      8   -230    465       N  
ATOM   3242  CA  PRO A 414      25.442  88.651 232.499  1.00 46.96           C  
ANISOU 3242  CA  PRO A 414     7183   6879   3781    -58   -211    525       C  
ATOM   3243  C   PRO A 414      26.237  88.991 233.746  1.00 46.03           C  
ANISOU 3243  C   PRO A 414     7031   6797   3663     25   -180    541       C  
ATOM   3244  O   PRO A 414      27.101  88.220 234.118  1.00 46.72           O  
ANISOU 3244  O   PRO A 414     7195   6834   3722    107   -187    527       O  
ATOM   3245  CB  PRO A 414      24.350  87.639 232.855  1.00 47.82           C  
ANISOU 3245  CB  PRO A 414     7373   6897   3897   -157   -235    566       C  
ATOM   3246  CG  PRO A 414      24.274  86.733 231.665  1.00 48.57           C  
ANISOU 3246  CG  PRO A 414     7574   6914   3966   -182   -277    523       C  
ATOM   3247  CD  PRO A 414      25.700  86.602 231.198  1.00 48.79           C  
ANISOU 3247  CD  PRO A 414     7641   6940   3957    -49   -269    462       C  
ATOM   3248  N   THR A 415      25.938  90.116 234.385  1.00 45.08           N  
ANISOU 3248  N   THR A 415     6799   6759   3569      4   -150    569       N  
ATOM   3249  CA  THR A 415      26.707  90.607 235.559  1.00 45.14           C  
ANISOU 3249  CA  THR A 415     6766   6815   3571     76   -124    578       C  
ATOM   3250  C   THR A 415      27.014  89.599 236.700  1.00 45.92           C  
ANISOU 3250  C   THR A 415     6957   6850   3643    115   -131    605       C  
ATOM   3251  O   THR A 415      26.184  88.736 237.026  1.00 46.59           O  
ANISOU 3251  O   THR A 415     7116   6859   3725     50   -141    644       O  
ATOM   3252  CB  THR A 415      26.040  91.867 236.198  1.00 44.16           C  
ANISOU 3252  CB  THR A 415     6528   6770   3479     29    -90    608       C  
ATOM   3253  OG1 THR A 415      25.529  92.730 235.165  1.00 45.54           O  
ANISOU 3253  OG1 THR A 415     6627   6992   3685    -18    -88    597       O  
ATOM   3254  CG2 THR A 415      27.044  92.616 236.986  1.00 42.19           C  
ANISOU 3254  CG2 THR A 415     6227   6583   3219    106    -69    593       C  
ATOM   3255  N   VAL A 416      28.214  89.705 237.286  1.00 46.12           N  
ANISOU 3255  N   VAL A 416     6975   6904   3644    218   -129    589       N  
ATOM   3256  CA  VAL A 416      28.554  89.014 238.545  1.00 46.77           C  
ANISOU 3256  CA  VAL A 416     7124   6948   3697    262   -135    623       C  
ATOM   3257  C   VAL A 416      29.043  90.070 239.529  1.00 46.90           C  
ANISOU 3257  C   VAL A 416     7051   7061   3709    297   -114    627       C  
ATOM   3258  O   VAL A 416      29.726  91.009 239.132  1.00 46.73           O  
ANISOU 3258  O   VAL A 416     6941   7116   3698    335   -106    588       O  
ATOM   3259  CB  VAL A 416      29.679  87.921 238.391  1.00 47.49           C  
ANISOU 3259  CB  VAL A 416     7313   6975   3758    373   -166    599       C  
ATOM   3260  CG1 VAL A 416      29.944  87.216 239.727  1.00 46.88           C  
ANISOU 3260  CG1 VAL A 416     7308   6856   3648    416   -179    646       C  
ATOM   3261  CG2 VAL A 416      29.356  86.882 237.299  1.00 47.40           C  
ANISOU 3261  CG2 VAL A 416     7403   6861   3745    351   -188    578       C  
ATOM   3262  N   TRP A 417      28.663  89.933 240.800  1.00 47.96           N  
ANISOU 3262  N   TRP A 417     7210   7190   3824    277   -104    675       N  
ATOM   3263  CA  TRP A 417      29.357  90.603 241.921  1.00 48.10           C  
ANISOU 3263  CA  TRP A 417     7180   7280   3814    330    -97    677       C  
ATOM   3264  C   TRP A 417      30.105  89.541 242.659  1.00 50.32           C  
ANISOU 3264  C   TRP A 417     7558   7512   4051    408   -130    700       C  
ATOM   3265  O   TRP A 417      29.553  88.455 242.896  1.00 51.32           O  
ANISOU 3265  O   TRP A 417     7789   7546   4163    380   -139    743       O  
ATOM   3266  CB  TRP A 417      28.402  91.203 242.958  1.00 47.00           C  
ANISOU 3266  CB  TRP A 417     7010   7176   3672    257    -59    717       C  
ATOM   3267  CG  TRP A 417      27.569  92.291 242.464  1.00 43.45           C  
ANISOU 3267  CG  TRP A 417     6465   6776   3267    186    -23    705       C  
ATOM   3268  CD1 TRP A 417      27.681  93.617 242.766  1.00 38.28           C  
ANISOU 3268  CD1 TRP A 417     5717   6204   2624    187      3    682       C  
ATOM   3269  CD2 TRP A 417      26.474  92.161 241.552  1.00 40.23           C  
ANISOU 3269  CD2 TRP A 417     6049   6336   2900    103    -15    716       C  
ATOM   3270  NE1 TRP A 417      26.712  94.319 242.108  1.00 38.32           N  
ANISOU 3270  NE1 TRP A 417     5657   6226   2677    118     31    681       N  
ATOM   3271  CE2 TRP A 417      25.961  93.459 241.346  1.00 38.41           C  
ANISOU 3271  CE2 TRP A 417     5712   6174   2707     66     18    703       C  
ATOM   3272  CE3 TRP A 417      25.873  91.070 240.905  1.00 36.41           C  
ANISOU 3272  CE3 TRP A 417     5640   5769   2425     56    -35    736       C  
ATOM   3273  CZ2 TRP A 417      24.876  93.704 240.516  1.00 36.69           C  
ANISOU 3273  CZ2 TRP A 417     5452   5954   2534    -10     29    714       C  
ATOM   3274  CZ3 TRP A 417      24.806  91.301 240.099  1.00 37.73           C  
ANISOU 3274  CZ3 TRP A 417     5766   5935   2633    -30    -27    743       C  
ATOM   3275  CH2 TRP A 417      24.309  92.615 239.899  1.00 38.56           C  
ANISOU 3275  CH2 TRP A 417     5755   6119   2775    -60      3    734       C  
ATOM   3276  N   TYR A 418      31.334  89.844 243.068  1.00 51.67           N  
ANISOU 3276  N   TYR A 418     7693   7741   4198    503   -151    676       N  
ATOM   3277  CA  TYR A 418      31.978  88.939 244.002  1.00 53.81           C  
ANISOU 3277  CA  TYR A 418     8049   7977   4422    579   -185    710       C  
ATOM   3278  C   TYR A 418      33.056  89.518 244.855  1.00 54.22           C  
ANISOU 3278  C   TYR A 418     8043   8118   4441    654   -206    698       C  
ATOM   3279  O   TYR A 418      33.639  90.517 244.483  1.00 53.86           O  
ANISOU 3279  O   TYR A 418     7891   8157   4414    669   -201    651       O  
ATOM   3280  CB  TYR A 418      32.484  87.677 243.313  1.00 55.00           C  
ANISOU 3280  CB  TYR A 418     8294   8034   4571    651   -217    703       C  
ATOM   3281  CG  TYR A 418      33.204  87.809 241.982  1.00 55.76           C  
ANISOU 3281  CG  TYR A 418     8342   8147   4696    706   -221    639       C  
ATOM   3282  CD1 TYR A 418      33.712  89.027 241.534  1.00 54.96           C  
ANISOU 3282  CD1 TYR A 418     8110   8155   4617    711   -205    592       C  
ATOM   3283  CD2 TYR A 418      33.414  86.659 241.196  1.00 56.51           C  
ANISOU 3283  CD2 TYR A 418     8536   8144   4793    756   -240    626       C  
ATOM   3284  CE1 TYR A 418      34.379  89.092 240.326  1.00 56.66           C  
ANISOU 3284  CE1 TYR A 418     8288   8388   4852    760   -203    539       C  
ATOM   3285  CE2 TYR A 418      34.059  86.713 240.008  1.00 57.73           C  
ANISOU 3285  CE2 TYR A 418     8657   8314   4964    810   -237    567       C  
ATOM   3286  CZ  TYR A 418      34.544  87.924 239.578  1.00 58.27           C  
ANISOU 3286  CZ  TYR A 418     8590   8499   5051    811   -217    526       C  
ATOM   3287  OH  TYR A 418      35.216  87.945 238.399  1.00 61.05           O  
ANISOU 3287  OH  TYR A 418     8912   8872   5414    866   -209    472       O  
ATOM   3288  N   ASP A 419      33.287  88.887 246.007  1.00 55.57           N  
ANISOU 3288  N   ASP A 419     8288   8268   4559    694   -233    746       N  
ATOM   3289  CA  ASP A 419      34.356  89.281 246.923  1.00 56.81           C  
ANISOU 3289  CA  ASP A 419     8403   8508   4674    770   -267    741       C  
ATOM   3290  C   ASP A 419      35.692  88.751 246.413  1.00 57.96           C  
ANISOU 3290  C   ASP A 419     8539   8659   4824    897   -314    715       C  
ATOM   3291  O   ASP A 419      35.726  87.752 245.691  1.00 59.29           O  
ANISOU 3291  O   ASP A 419     8780   8738   5008    938   -322    717       O  
ATOM   3292  CB  ASP A 419      34.075  88.768 248.340  1.00 57.39           C  
ANISOU 3292  CB  ASP A 419     8565   8559   4680    767   -281    808       C  
ATOM   3293  CG  ASP A 419      32.962  89.553 249.049  1.00 57.09           C  
ANISOU 3293  CG  ASP A 419     8509   8555   4628    656   -229    826       C  
ATOM   3294  OD1 ASP A 419      32.818  90.780 248.792  1.00 56.38           O  
ANISOU 3294  OD1 ASP A 419     8315   8540   4567    611   -199    779       O  
ATOM   3295  OD2 ASP A 419      32.241  88.945 249.878  1.00 56.52           O  
ANISOU 3295  OD2 ASP A 419     8528   8433   4513    617   -216    888       O  
ATOM   3296  N   GLU A 420      36.780  89.445 246.734  1.00 58.39           N  
ANISOU 3296  N   GLU A 420     8500   8819   4866    956   -342    685       N  
ATOM   3297  CA  GLU A 420      38.126  88.971 246.398  1.00 59.78           C  
ANISOU 3297  CA  GLU A 420     8650   9020   5045   1086   -387    665       C  
ATOM   3298  C   GLU A 420      39.111  89.404 247.465  1.00 60.47           C  
ANISOU 3298  C   GLU A 420     8679   9209   5089   1143   -437    670       C  
ATOM   3299  O   GLU A 420      39.169  90.596 247.781  1.00 60.28           O  
ANISOU 3299  O   GLU A 420     8562   9278   5063   1084   -428    641       O  
ATOM   3300  CB  GLU A 420      38.591  89.481 245.022  1.00 59.40           C  
ANISOU 3300  CB  GLU A 420     8506   9012   5052   1097   -362    600       C  
ATOM   3301  CG  GLU A 420      40.120  89.322 244.798  1.00 61.20           C  
ANISOU 3301  CG  GLU A 420     8662   9310   5281   1228   -401    572       C  
ATOM   3302  CD  GLU A 420      40.613  89.779 243.421  1.00 62.24           C  
ANISOU 3302  CD  GLU A 420     8701   9487   5461   1241   -368    512       C  
ATOM   3303  OE1 GLU A 420      39.793  89.839 242.464  1.00 61.16           O  
ANISOU 3303  OE1 GLU A 420     8590   9295   5353   1172   -323    494       O  
ATOM   3304  OE2 GLU A 420      41.837  90.059 243.312  1.00 62.56           O  
ANISOU 3304  OE2 GLU A 420     8640   9622   5507   1320   -389    485       O  
ATOM   3305  N   ASP A 421      39.873  88.453 248.016  1.00 61.43           N  
ANISOU 3305  N   ASP A 421     8856   9311   5174   1256   -493    706       N  
ATOM   3306  CA  ASP A 421      40.865  88.779 249.031  1.00 62.21           C  
ANISOU 3306  CA  ASP A 421     8898   9512   5227   1316   -554    715       C  
ATOM   3307  C   ASP A 421      42.007  89.546 248.402  1.00 62.31           C  
ANISOU 3307  C   ASP A 421     8757   9641   5277   1361   -567    654       C  
ATOM   3308  O   ASP A 421      42.701  89.018 247.536  1.00 63.12           O  
ANISOU 3308  O   ASP A 421     8834   9734   5414   1452   -570    634       O  
ATOM   3309  CB  ASP A 421      41.402  87.522 249.719  1.00 63.81           C  
ANISOU 3309  CB  ASP A 421     9200   9663   5384   1436   -616    776       C  
ATOM   3310  CG  ASP A 421      42.225  87.838 250.975  1.00 64.91           C  
ANISOU 3310  CG  ASP A 421     9297   9906   5459   1482   -687    798       C  
ATOM   3311  OD1 ASP A 421      41.636  88.385 251.941  1.00 65.79           O  
ANISOU 3311  OD1 ASP A 421     9433  10045   5519   1396   -683    818       O  
ATOM   3312  OD2 ASP A 421      43.446  87.537 251.002  1.00 64.30           O  
ANISOU 3312  OD2 ASP A 421     9164   9887   5381   1606   -747    796       O  
ATOM   3313  N   VAL A 422      42.177  90.796 248.839  1.00 62.24           N  
ANISOU 3313  N   VAL A 422     8650   9739   5261   1291   -569    623       N  
ATOM   3314  CA  VAL A 422      43.277  91.685 248.428  1.00 62.75           C  
ANISOU 3314  CA  VAL A 422     8558   9928   5355   1310   -585    569       C  
ATOM   3315  C   VAL A 422      44.651  90.976 248.433  1.00 64.83           C  
ANISOU 3315  C   VAL A 422     8774  10243   5614   1459   -648    577       C  
ATOM   3316  O   VAL A 422      45.487  91.201 247.553  1.00 64.99           O  
ANISOU 3316  O   VAL A 422     8686  10326   5680   1505   -640    537       O  
ATOM   3317  CB  VAL A 422      43.334  92.949 249.345  1.00 62.29           C  
ANISOU 3317  CB  VAL A 422     8434   9967   5265   1224   -603    549       C  
ATOM   3318  CG1 VAL A 422      44.619  93.755 249.137  1.00 61.67           C  
ANISOU 3318  CG1 VAL A 422     8200  10023   5210   1246   -638    502       C  
ATOM   3319  CG2 VAL A 422      42.126  93.824 249.122  1.00 60.62           C  
ANISOU 3319  CG2 VAL A 422     8238   9720   5075   1090   -533    527       C  
ATOM   3320  N   LEU A 423      44.876  90.118 249.424  1.00 66.59           N  
ANISOU 3320  N   LEU A 423     9078  10442   5781   1537   -709    633       N  
ATOM   3321  CA  LEU A 423      46.128  89.397 249.504  1.00 68.60           C  
ANISOU 3321  CA  LEU A 423     9292  10741   6031   1690   -773    649       C  
ATOM   3322  C   LEU A 423      46.106  88.124 248.643  1.00 69.32           C  
ANISOU 3322  C   LEU A 423     9468  10717   6153   1795   -751    663       C  
ATOM   3323  O   LEU A 423      46.921  87.973 247.720  1.00 69.57           O  
ANISOU 3323  O   LEU A 423     9417  10785   6230   1880   -740    627       O  
ATOM   3324  CB  LEU A 423      46.453  89.064 250.959  1.00 69.80           C  
ANISOU 3324  CB  LEU A 423     9492  10924   6105   1736   -858    706       C  
ATOM   3325  CG  LEU A 423      47.926  89.284 251.312  1.00 71.90           C  
ANISOU 3325  CG  LEU A 423     9621  11335   6363   1831   -939    697       C  
ATOM   3326  CD1 LEU A 423      48.081  90.674 251.937  1.00 70.71           C  
ANISOU 3326  CD1 LEU A 423     9370  11310   6189   1715   -960    660       C  
ATOM   3327  CD2 LEU A 423      48.502  88.152 252.229  1.00 74.05           C  
ANISOU 3327  CD2 LEU A 423     9967  11591   6578   1973  -1027    771       C  
ATOM   3328  N   SER A 424      45.151  87.235 248.942  1.00 69.47           N  
ANISOU 3328  N   SER A 424     9653  10596   6145   1783   -740    713       N  
ATOM   3329  CA  SER A 424      45.145  85.862 248.430  1.00 69.90           C  
ANISOU 3329  CA  SER A 424     9823  10522   6213   1890   -737    738       C  
ATOM   3330  C   SER A 424      44.928  85.770 246.926  1.00 69.40           C  
ANISOU 3330  C   SER A 424     9748  10406   6213   1882   -668    681       C  
ATOM   3331  O   SER A 424      45.500  84.888 246.277  1.00 70.12           O  
ANISOU 3331  O   SER A 424     9868  10449   6326   2008   -670    672       O  
ATOM   3332  CB  SER A 424      44.123  84.998 249.191  1.00 70.17           C  
ANISOU 3332  CB  SER A 424    10042  10418   6200   1856   -743    810       C  
ATOM   3333  OG  SER A 424      42.842  84.995 248.589  1.00 68.99           O  
ANISOU 3333  OG  SER A 424     9970  10168   6076   1735   -673    799       O  
ATOM   3334  N   GLY A 425      44.110  86.686 246.396  1.00 67.95           N  
ANISOU 3334  N   GLY A 425     9528  10236   6055   1740   -608    644       N  
ATOM   3335  CA  GLY A 425      43.695  86.676 244.992  1.00 67.08           C  
ANISOU 3335  CA  GLY A 425     9419  10073   5994   1706   -542    594       C  
ATOM   3336  C   GLY A 425      42.394  85.940 244.685  1.00 66.66           C  
ANISOU 3336  C   GLY A 425     9524   9862   5941   1637   -508    616       C  
ATOM   3337  O   GLY A 425      41.786  86.180 243.635  1.00 65.93           O  
ANISOU 3337  O   GLY A 425     9430   9737   5882   1565   -455    578       O  
ATOM   3338  N   GLU A 426      41.959  85.061 245.597  1.00 67.19           N  
ANISOU 3338  N   GLU A 426     9725   9835   5969   1651   -540    682       N  
ATOM   3339  CA  GLU A 426      40.787  84.168 245.370  1.00 67.39           C  
ANISOU 3339  CA  GLU A 426     9912   9699   5994   1590   -516    712       C  
ATOM   3340  C   GLU A 426      39.416  84.883 245.296  1.00 65.25           C  
ANISOU 3340  C   GLU A 426     9643   9416   5733   1413   -466    712       C  
ATOM   3341  O   GLU A 426      39.113  85.763 246.108  1.00 64.98           O  
ANISOU 3341  O   GLU A 426     9552   9460   5679   1336   -463    727       O  
ATOM   3342  CB  GLU A 426      40.763  82.982 246.380  1.00 69.21           C  
ANISOU 3342  CB  GLU A 426    10291   9827   6178   1658   -564    790       C  
ATOM   3343  CG  GLU A 426      40.127  83.271 247.772  1.00 70.40           C  
ANISOU 3343  CG  GLU A 426    10478   9996   6275   1572   -580    856       C  
ATOM   3344  CD  GLU A 426      40.735  82.443 248.932  1.00 74.00           C  
ANISOU 3344  CD  GLU A 426    11016  10426   6673   1682   -649    929       C  
ATOM   3345  OE1 GLU A 426      41.987  82.303 249.011  1.00 74.00           O  
ANISOU 3345  OE1 GLU A 426    10956  10490   6670   1824   -699    920       O  
ATOM   3346  OE2 GLU A 426      39.949  81.955 249.788  1.00 74.86           O  
ANISOU 3346  OE2 GLU A 426    11247  10458   6737   1623   -653   1000       O  
ATOM   3347  N   ARG A 427      38.592  84.459 244.343  1.00 63.54           N  
ANISOU 3347  N   ARG A 427     9497   9100   5546   1353   -428    695       N  
ATOM   3348  CA  ARG A 427      37.350  85.146 244.001  1.00 61.18           C  
ANISOU 3348  CA  ARG A 427     9179   8798   5268   1196   -381    686       C  
ATOM   3349  C   ARG A 427      36.105  84.283 244.254  1.00 60.86           C  
ANISOU 3349  C   ARG A 427     9284   8623   5218   1110   -371    740       C  
ATOM   3350  O   ARG A 427      35.797  83.371 243.469  1.00 61.45           O  
ANISOU 3350  O   ARG A 427     9457   8583   5308   1113   -369    731       O  
ATOM   3351  CB  ARG A 427      37.399  85.515 242.514  1.00 60.47           C  
ANISOU 3351  CB  ARG A 427     9028   8725   5223   1182   -346    617       C  
ATOM   3352  CG  ARG A 427      36.988  86.917 242.190  1.00 58.38           C  
ANISOU 3352  CG  ARG A 427     8637   8561   4983   1079   -309    586       C  
ATOM   3353  CD  ARG A 427      37.399  87.272 240.798  1.00 57.08           C  
ANISOU 3353  CD  ARG A 427     8405   8431   4851   1098   -283    522       C  
ATOM   3354  NE  ARG A 427      38.776  87.719 240.771  1.00 59.73           N  
ANISOU 3354  NE  ARG A 427     8633   8875   5188   1199   -295    490       N  
ATOM   3355  CZ  ARG A 427      39.357  88.320 239.742  1.00 61.19           C  
ANISOU 3355  CZ  ARG A 427     8722   9131   5396   1216   -269    436       C  
ATOM   3356  NH1 ARG A 427      38.675  88.565 238.619  1.00 60.84           N  
ANISOU 3356  NH1 ARG A 427     8683   9062   5373   1142   -231    407       N  
ATOM   3357  NH2 ARG A 427      40.634  88.673 239.847  1.00 62.27           N  
ANISOU 3357  NH2 ARG A 427     8756   9372   5533   1306   -282    415       N  
ATOM   3358  N   LYS A 428      35.376  84.568 245.322  1.00 59.28           N  
ANISOU 3358  N   LYS A 428     9097   8436   4989   1027   -364    793       N  
ATOM   3359  CA  LYS A 428      34.082  83.928 245.516  1.00 59.04           C  
ANISOU 3359  CA  LYS A 428     9180   8298   4956    919   -344    845       C  
ATOM   3360  C   LYS A 428      32.977  84.775 244.858  1.00 56.98           C  
ANISOU 3360  C   LYS A 428     8846   8069   4735    781   -294    818       C  
ATOM   3361  O   LYS A 428      32.967  85.999 245.042  1.00 55.67           O  
ANISOU 3361  O   LYS A 428     8558   8016   4576    746   -271    795       O  
ATOM   3362  CB  LYS A 428      33.791  83.745 247.016  1.00 60.25           C  
ANISOU 3362  CB  LYS A 428     9390   8451   5052    898   -354    922       C  
ATOM   3363  CG  LYS A 428      34.832  82.883 247.788  1.00 63.81           C  
ANISOU 3363  CG  LYS A 428     9920   8869   5455   1035   -413    962       C  
ATOM   3364  CD  LYS A 428      34.622  82.847 249.327  1.00 65.57           C  
ANISOU 3364  CD  LYS A 428    10192   9114   5609   1015   -425   1040       C  
ATOM   3365  CE  LYS A 428      35.606  81.833 249.993  1.00 68.52           C  
ANISOU 3365  CE  LYS A 428    10662   9436   5936   1157   -492   1089       C  
ATOM   3366  NZ  LYS A 428      35.250  81.412 251.414  1.00 68.98           N  
ANISOU 3366  NZ  LYS A 428    10822   9471   5918   1133   -506   1183       N  
ATOM   3367  N   VAL A 429      32.075  84.138 244.086  1.00 55.75           N  
ANISOU 3367  N   VAL A 429     8765   7812   4606    704   -280    821       N  
ATOM   3368  CA  VAL A 429      30.801  84.775 243.659  1.00 53.57           C  
ANISOU 3368  CA  VAL A 429     8435   7555   4364    560   -238    819       C  
ATOM   3369  C   VAL A 429      29.919  85.074 244.870  1.00 53.59           C  
ANISOU 3369  C   VAL A 429     8436   7584   4343    473   -210    882       C  
ATOM   3370  O   VAL A 429      29.735  84.216 245.740  1.00 54.34           O  
ANISOU 3370  O   VAL A 429     8637   7609   4400    471   -221    946       O  
ATOM   3371  CB  VAL A 429      29.960  83.920 242.676  1.00 53.39           C  
ANISOU 3371  CB  VAL A 429     8501   7415   4369    486   -239    816       C  
ATOM   3372  CG1 VAL A 429      28.606  84.544 242.446  1.00 51.33           C  
ANISOU 3372  CG1 VAL A 429     8179   7185   4140    338   -202    828       C  
ATOM   3373  CG2 VAL A 429      30.642  83.798 241.370  1.00 52.87           C  
ANISOU 3373  CG2 VAL A 429     8429   7337   4324    553   -254    744       C  
ATOM   3374  N   VAL A 430      29.398  86.299 244.926  1.00 52.32           N  
ANISOU 3374  N   VAL A 430     8155   7523   4201    406   -171    867       N  
ATOM   3375  CA  VAL A 430      28.396  86.682 245.913  1.00 51.68           C  
ANISOU 3375  CA  VAL A 430     8060   7473   4104    314   -131    918       C  
ATOM   3376  C   VAL A 430      27.021  86.564 245.252  1.00 51.03           C  
ANISOU 3376  C   VAL A 430     7975   7350   4067    186   -100    933       C  
ATOM   3377  O   VAL A 430      26.135  85.885 245.761  1.00 51.46           O  
ANISOU 3377  O   VAL A 430     8100   7345   4109    108    -84    995       O  
ATOM   3378  CB  VAL A 430      28.628  88.112 246.451  1.00 50.92           C  
ANISOU 3378  CB  VAL A 430     7840   7507   4001    323   -104    890       C  
ATOM   3379  CG1 VAL A 430      27.545  88.479 247.463  1.00 51.82           C  
ANISOU 3379  CG1 VAL A 430     7945   7652   4094    234    -53    939       C  
ATOM   3380  CG2 VAL A 430      29.982  88.222 247.101  1.00 51.13           C  
ANISOU 3380  CG2 VAL A 430     7864   7580   3982    438   -143    875       C  
ATOM   3381  N   LYS A 431      26.860  87.222 244.110  1.00 49.68           N  
ANISOU 3381  N   LYS A 431     7718   7213   3945    163    -94    881       N  
ATOM   3382  CA  LYS A 431      25.649  87.103 243.325  1.00 49.41           C  
ANISOU 3382  CA  LYS A 431     7673   7145   3954     49    -79    890       C  
ATOM   3383  C   LYS A 431      26.008  87.095 241.869  1.00 49.14           C  
ANISOU 3383  C   LYS A 431     7625   7093   3952     72   -108    829       C  
ATOM   3384  O   LYS A 431      26.752  87.965 241.420  1.00 49.10           O  
ANISOU 3384  O   LYS A 431     7537   7162   3957    134   -107    777       O  
ATOM   3385  CB  LYS A 431      24.705  88.285 243.557  1.00 48.45           C  
ANISOU 3385  CB  LYS A 431     7431   7117   3861    -28    -29    898       C  
ATOM   3386  CG  LYS A 431      23.458  88.175 242.699  1.00 48.74           C  
ANISOU 3386  CG  LYS A 431     7443   7131   3947   -142    -21    911       C  
ATOM   3387  CD  LYS A 431      22.511  89.363 242.802  1.00 49.22           C  
ANISOU 3387  CD  LYS A 431     7373   7284   4044   -205     28    918       C  
ATOM   3388  CE  LYS A 431      21.217  89.096 242.007  1.00 49.08           C  
ANISOU 3388  CE  LYS A 431     7332   7244   4074   -323     27    941       C  
ATOM   3389  NZ  LYS A 431      20.490  87.912 242.572  1.00 52.20           N  
ANISOU 3389  NZ  LYS A 431     7819   7561   4452   -405     30   1006       N  
ATOM   3390  N   ALA A 432      25.469  86.125 241.127  1.00 49.56           N  
ANISOU 3390  N   ALA A 432     7763   7050   4019     15   -131    835       N  
ATOM   3391  CA  ALA A 432      25.481  86.165 239.645  1.00 48.37           C  
ANISOU 3391  CA  ALA A 432     7597   6886   3895      5   -152    778       C  
ATOM   3392  C   ALA A 432      24.068  86.413 239.138  1.00 47.61           C  
ANISOU 3392  C   ALA A 432     7452   6800   3839   -132   -142    799       C  
ATOM   3393  O   ALA A 432      23.101  85.822 239.632  1.00 48.14           O  
ANISOU 3393  O   ALA A 432     7563   6819   3910   -227   -135    855       O  
ATOM   3394  CB  ALA A 432      26.066  84.881 239.046  1.00 48.72           C  
ANISOU 3394  CB  ALA A 432     7780   6812   3920     57   -194    754       C  
ATOM   3395  N   ARG A 433      23.946  87.308 238.170  1.00 46.13           N  
ANISOU 3395  N   ARG A 433     7168   6680   3679   -145   -140    759       N  
ATOM   3396  CA  ARG A 433      22.640  87.646 237.656  1.00 45.55           C  
ANISOU 3396  CA  ARG A 433     7032   6631   3645   -265   -136    780       C  
ATOM   3397  C   ARG A 433      22.137  86.495 236.784  1.00 46.39           C  
ANISOU 3397  C   ARG A 433     7241   6634   3750   -337   -181    775       C  
ATOM   3398  O   ARG A 433      22.900  85.942 236.002  1.00 46.29           O  
ANISOU 3398  O   ARG A 433     7307   6565   3715   -279   -213    724       O  
ATOM   3399  CB  ARG A 433      22.698  88.962 236.890  1.00 44.08           C  
ANISOU 3399  CB  ARG A 433     6720   6544   3486   -250   -125    744       C  
ATOM   3400  CG  ARG A 433      21.347  89.524 236.556  1.00 43.96           C  
ANISOU 3400  CG  ARG A 433     6614   6575   3514   -358   -117    775       C  
ATOM   3401  CD  ARG A 433      21.401  90.234 235.237  1.00 44.17           C  
ANISOU 3401  CD  ARG A 433     6579   6646   3557   -355   -138    734       C  
ATOM   3402  NE  ARG A 433      20.116  90.738 234.740  1.00 44.74           N  
ANISOU 3402  NE  ARG A 433     6564   6763   3671   -454   -143    763       N  
ATOM   3403  CZ  ARG A 433      20.016  91.892 234.075  1.00 45.59           C  
ANISOU 3403  CZ  ARG A 433     6570   6948   3804   -442   -139    750       C  
ATOM   3404  NH1 ARG A 433      21.099  92.627 233.871  1.00 44.35           N  
ANISOU 3404  NH1 ARG A 433     6390   6827   3633   -349   -126    709       N  
ATOM   3405  NH2 ARG A 433      18.854  92.337 233.622  1.00 47.30           N  
ANISOU 3405  NH2 ARG A 433     6705   7207   4061   -522   -149    781       N  
ATOM   3406  N   LYS A 434      20.864  86.120 236.972  1.00 47.65           N  
ANISOU 3406  N   LYS A 434     7402   6770   3933   -465   -181    826       N  
ATOM   3407  CA  LYS A 434      20.120  85.168 236.106  1.00 48.61           C  
ANISOU 3407  CA  LYS A 434     7601   6806   4061   -569   -228    825       C  
ATOM   3408  C   LYS A 434      19.270  85.905 235.034  1.00 47.99           C  
ANISOU 3408  C   LYS A 434     7415   6799   4018   -648   -247    811       C  
ATOM   3409  O   LYS A 434      18.557  86.868 235.346  1.00 47.48           O  
ANISOU 3409  O   LYS A 434     7218   6833   3990   -686   -215    845       O  
ATOM   3410  CB  LYS A 434      19.196  84.286 236.956  1.00 49.97           C  
ANISOU 3410  CB  LYS A 434     7834   6912   4240   -677   -221    896       C  
ATOM   3411  CG  LYS A 434      19.880  83.496 238.093  1.00 53.12           C  
ANISOU 3411  CG  LYS A 434     8348   7235   4601   -613   -206    926       C  
ATOM   3412  CD  LYS A 434      18.865  83.119 239.202  1.00 58.64           C  
ANISOU 3412  CD  LYS A 434     9051   7923   5308   -721   -173   1014       C  
ATOM   3413  CE  LYS A 434      19.542  82.595 240.498  1.00 60.83           C  
ANISOU 3413  CE  LYS A 434     9421   8152   5540   -649   -150   1055       C  
ATOM   3414  NZ  LYS A 434      18.749  82.903 241.739  1.00 61.18           N  
ANISOU 3414  NZ  LYS A 434     9405   8257   5583   -715    -90   1132       N  
ATOM   3415  N   VAL A 435      19.362  85.463 233.776  1.00 47.84           N  
ANISOU 3415  N   VAL A 435     7458   6734   3987   -666   -298    761       N  
ATOM   3416  CA  VAL A 435      18.518  85.989 232.685  1.00 47.51           C  
ANISOU 3416  CA  VAL A 435     7334   6749   3969   -749   -330    752       C  
ATOM   3417  C   VAL A 435      17.660  84.881 232.068  1.00 48.79           C  
ANISOU 3417  C   VAL A 435     7587   6822   4130   -880   -389    756       C  
ATOM   3418  O   VAL A 435      18.187  83.901 231.538  1.00 49.66           O  
ANISOU 3418  O   VAL A 435     7842   6826   4201   -863   -425    710       O  
ATOM   3419  CB  VAL A 435      19.338  86.644 231.551  1.00 46.67           C  
ANISOU 3419  CB  VAL A 435     7205   6688   3840   -665   -345    685       C  
ATOM   3420  CG1 VAL A 435      18.443  87.487 230.658  1.00 45.06           C  
ANISOU 3420  CG1 VAL A 435     6888   6571   3664   -739   -369    694       C  
ATOM   3421  CG2 VAL A 435      20.459  87.488 232.111  1.00 46.47           C  
ANISOU 3421  CG2 VAL A 435     7126   6723   3807   -530   -295    669       C  
ATOM   3422  N   GLY A 436      16.341  85.044 232.130  1.00 49.11           N  
ANISOU 3422  N   GLY A 436     7542   6907   4212  -1010   -398    810       N  
ATOM   3423  CA  GLY A 436      15.423  84.034 231.627  1.00 50.22           C  
ANISOU 3423  CA  GLY A 436     7753   6971   4356  -1156   -457    821       C  
ATOM   3424  C   GLY A 436      15.144  84.242 230.146  1.00 50.74           C  
ANISOU 3424  C   GLY A 436     7803   7064   4411  -1199   -523    774       C  
ATOM   3425  O   GLY A 436      16.039  84.652 229.379  1.00 49.92           O  
ANISOU 3425  O   GLY A 436     7718   6978   4273  -1097   -529    712       O  
ATOM   3426  N   GLY A 437      13.901  83.951 229.744  1.00 51.28           N  
ANISOU 3426  N   GLY A 437     7837   7142   4507  -1353   -572    805       N  
ATOM   3427  CA  GLY A 437      13.474  84.093 228.363  1.00 51.22           C  
ANISOU 3427  CA  GLY A 437     7813   7164   4485  -1415   -646    769       C  
ATOM   3428  C   GLY A 437      14.300  83.234 227.424  1.00 51.77           C  
ANISOU 3428  C   GLY A 437     8061   7121   4486  -1380   -693    683       C  
ATOM   3429  O   GLY A 437      14.352  83.507 226.210  1.00 51.33           O  
ANISOU 3429  O   GLY A 437     8007   7097   4397  -1382   -742    634       O  
ATOM   3430  N   GLY A 438      14.963  82.222 228.001  1.00 51.93           N  
ANISOU 3430  N   GLY A 438     8233   7014   4483  -1341   -674    666       N  
ATOM   3431  CA  GLY A 438      15.785  81.275 227.252  1.00 52.34           C  
ANISOU 3431  CA  GLY A 438     8474   6942   4473  -1294   -709    583       C  
ATOM   3432  C   GLY A 438      17.118  81.785 226.742  1.00 51.32           C  
ANISOU 3432  C   GLY A 438     8362   6840   4298  -1123   -680    515       C  
ATOM   3433  O   GLY A 438      17.736  81.164 225.888  1.00 52.00           O  
ANISOU 3433  O   GLY A 438     8582   6848   4327  -1082   -708    439       O  
ATOM   3434  N   PHE A 439      17.565  82.914 227.275  1.00 50.19           N  
ANISOU 3434  N   PHE A 439     8085   6808   4178  -1024   -619    541       N  
ATOM   3435  CA  PHE A 439      18.859  83.525 226.935  1.00 49.29           C  
ANISOU 3435  CA  PHE A 439     7962   6737   4030   -863   -582    487       C  
ATOM   3436  C   PHE A 439      20.064  82.559 227.106  1.00 49.89           C  
ANISOU 3436  C   PHE A 439     8199   6695   4062   -748   -565    434       C  
ATOM   3437  O   PHE A 439      20.050  81.732 228.027  1.00 50.83           O  
ANISOU 3437  O   PHE A 439     8398   6721   4193   -756   -556    464       O  
ATOM   3438  CB  PHE A 439      19.028  84.779 227.825  1.00 47.76           C  
ANISOU 3438  CB  PHE A 439     7604   6663   3879   -797   -518    538       C  
ATOM   3439  CG  PHE A 439      20.417  85.322 227.869  1.00 45.24           C  
ANISOU 3439  CG  PHE A 439     7275   6380   3535   -637   -471    497       C  
ATOM   3440  CD1 PHE A 439      20.881  86.176 226.870  1.00 45.19           C  
ANISOU 3440  CD1 PHE A 439     7211   6455   3505   -585   -470    458       C  
ATOM   3441  CD2 PHE A 439      21.274  84.971 228.895  1.00 43.76           C  
ANISOU 3441  CD2 PHE A 439     7133   6149   3345   -540   -430    502       C  
ATOM   3442  CE1 PHE A 439      22.195  86.683 226.906  1.00 42.95           C  
ANISOU 3442  CE1 PHE A 439     6908   6210   3199   -444   -423    422       C  
ATOM   3443  CE2 PHE A 439      22.585  85.465 228.933  1.00 42.02           C  
ANISOU 3443  CE2 PHE A 439     6892   5970   3103   -395   -390    465       C  
ATOM   3444  CZ  PHE A 439      23.037  86.329 227.936  1.00 41.42           C  
ANISOU 3444  CZ  PHE A 439     6751   5978   3009   -351   -385    425       C  
ATOM   3445  N   GLU A 440      21.081  82.650 226.232  1.00 49.34           N  
ANISOU 3445  N   GLU A 440     8175   6631   3941   -640   -559    360       N  
ATOM   3446  CA  GLU A 440      22.422  82.097 226.540  1.00 49.51           C  
ANISOU 3446  CA  GLU A 440     8295   6585   3932   -488   -523    316       C  
ATOM   3447  C   GLU A 440      23.632  82.777 225.901  1.00 48.59           C  
ANISOU 3447  C   GLU A 440     8137   6546   3779   -347   -486    259       C  
ATOM   3448  O   GLU A 440      23.645  83.000 224.722  1.00 49.07           O  
ANISOU 3448  O   GLU A 440     8204   6638   3801   -359   -504    211       O  
ATOM   3449  CB  GLU A 440      22.525  80.575 226.361  1.00 51.05           C  
ANISOU 3449  CB  GLU A 440     8694   6608   4094   -498   -557    275       C  
ATOM   3450  CG  GLU A 440      21.369  79.863 225.681  1.00 54.40           C  
ANISOU 3450  CG  GLU A 440     9203   6957   4510   -663   -626    267       C  
ATOM   3451  CD  GLU A 440      21.502  78.316 225.710  1.00 58.24           C  
ANISOU 3451  CD  GLU A 440     9908   7252   4970   -672   -656    232       C  
ATOM   3452  OE1 GLU A 440      22.117  77.750 226.664  1.00 57.69           O  
ANISOU 3452  OE1 GLU A 440     9906   7103   4911   -586   -625    253       O  
ATOM   3453  OE2 GLU A 440      20.979  77.677 224.759  1.00 59.69           O  
ANISOU 3453  OE2 GLU A 440    10197   7362   5119   -767   -714    184       O  
ATOM   3454  N   SER A 441      24.664  83.067 226.700  1.00 48.18           N  
ANISOU 3454  N   SER A 441     8045   6524   3738   -217   -434    267       N  
ATOM   3455  CA  SER A 441      25.908  83.704 226.231  1.00 47.24           C  
ANISOU 3455  CA  SER A 441     7875   6485   3591    -81   -392    219       C  
ATOM   3456  C   SER A 441      26.430  83.161 224.909  1.00 48.20           C  
ANISOU 3456  C   SER A 441     8104   6565   3646    -36   -403    133       C  
ATOM   3457  O   SER A 441      26.888  83.928 224.057  1.00 47.73           O  
ANISOU 3457  O   SER A 441     7979   6598   3558      3   -382    100       O  
ATOM   3458  CB  SER A 441      27.017  83.562 227.273  1.00 46.83           C  
ANISOU 3458  CB  SER A 441     7820   6425   3549     55   -351    227       C  
ATOM   3459  OG  SER A 441      26.687  84.261 228.455  1.00 46.09           O  
ANISOU 3459  OG  SER A 441     7615   6393   3503     28   -333    299       O  
ATOM   3460  N   LYS A 442      26.378  81.838 224.746  1.00 54.05           N  
ANISOU 3460  N   LYS A 442     9466   6775   4295    -17   -175    329       N  
ATOM   3461  CA  LYS A 442      26.995  81.193 223.586  1.00 54.35           C  
ANISOU 3461  CA  LYS A 442     9539   6739   4372     66   -156    279       C  
ATOM   3462  C   LYS A 442      26.291  81.573 222.290  1.00 53.32           C  
ANISOU 3462  C   LYS A 442     9336   6679   4244    -25    -94    219       C  
ATOM   3463  O   LYS A 442      26.812  81.331 221.193  1.00 53.79           O  
ANISOU 3463  O   LYS A 442     9391   6711   4335     40    -68    167       O  
ATOM   3464  CB  LYS A 442      27.105  79.663 223.764  1.00 56.17           C  
ANISOU 3464  CB  LYS A 442     9990   6783   4571     87   -169    297       C  
ATOM   3465  CG  LYS A 442      25.814  78.926 224.193  1.00 57.37           C  
ANISOU 3465  CG  LYS A 442    10295   6864   4638    -86   -151    325       C  
ATOM   3466  CD  LYS A 442      26.021  77.407 224.168  1.00 60.11           C  
ANISOU 3466  CD  LYS A 442    10865   7012   4960    -56   -158    334       C  
ATOM   3467  CE  LYS A 442      24.733  76.624 223.919  1.00 60.21           C  
ANISOU 3467  CE  LYS A 442    11018   6954   4904   -242   -116    326       C  
ATOM   3468  NZ  LYS A 442      24.932  75.648 222.789  1.00 61.69           N  
ANISOU 3468  NZ  LYS A 442    11324   7016   5100   -218    -86    266       N  
ATOM   3469  N   ASN A 443      25.114  82.175 222.420  1.00 51.96           N  
ANISOU 3469  N   ASN A 443     9108   6598   4038   -173    -72    228       N  
ATOM   3470  CA  ASN A 443      24.394  82.693 221.265  1.00 51.20           C  
ANISOU 3470  CA  ASN A 443     8922   6589   3944   -262    -27    181       C  
ATOM   3471  C   ASN A 443      24.933  84.044 220.782  1.00 50.07           C  
ANISOU 3471  C   ASN A 443     8581   6584   3860   -191    -20    159       C  
ATOM   3472  O   ASN A 443      24.567  84.528 219.715  1.00 49.95           O  
ANISOU 3472  O   ASN A 443     8487   6639   3852   -236     11    121       O  
ATOM   3473  CB  ASN A 443      22.915  82.826 221.582  1.00 50.79           C  
ANISOU 3473  CB  ASN A 443     8870   6584   3842   -441     -7    202       C  
ATOM   3474  CG  ASN A 443      22.293  81.528 222.044  1.00 51.86           C  
ANISOU 3474  CG  ASN A 443     9199   6588   3916   -534     -7    225       C  
ATOM   3475  OD1 ASN A 443      22.805  80.433 221.777  1.00 52.47           O  
ANISOU 3475  OD1 ASN A 443     9425   6527   3984   -482    -15    212       O  
ATOM   3476  ND2 ASN A 443      21.158  81.644 222.733  1.00 50.72           N  
ANISOU 3476  ND2 ASN A 443     9056   6482   3733   -675      8    259       N  
ATOM   3477  N   TYR A 444      25.813  84.647 221.561  1.00 49.55           N  
ANISOU 3477  N   TYR A 444     8440   6554   3833    -86    -54    184       N  
ATOM   3478  CA  TYR A 444      26.294  85.959 221.238  1.00 48.72           C  
ANISOU 3478  CA  TYR A 444     8154   6575   3782    -32    -48    169       C  
ATOM   3479  C   TYR A 444      27.819  86.031 221.199  1.00 49.70           C  
ANISOU 3479  C   TYR A 444     8231   6682   3969    136    -73    159       C  
ATOM   3480  O   TYR A 444      28.500  85.240 221.849  1.00 50.94           O  
ANISOU 3480  O   TYR A 444     8481   6744   4129    219   -113    182       O  
ATOM   3481  CB  TYR A 444      25.725  86.925 222.252  1.00 47.55           C  
ANISOU 3481  CB  TYR A 444     7924   6518   3624    -94    -60    206       C  
ATOM   3482  CG  TYR A 444      24.243  86.735 222.449  1.00 47.64           C  
ANISOU 3482  CG  TYR A 444     7984   6539   3580   -253    -32    221       C  
ATOM   3483  CD1 TYR A 444      23.342  87.051 221.439  1.00 47.16           C  
ANISOU 3483  CD1 TYR A 444     7863   6540   3516   -348      6    193       C  
ATOM   3484  CD2 TYR A 444      23.734  86.239 223.644  1.00 49.48           C  
ANISOU 3484  CD2 TYR A 444     8318   6722   3761   -314    -45    265       C  
ATOM   3485  CE1 TYR A 444      21.980  86.882 221.602  1.00 46.40           C  
ANISOU 3485  CE1 TYR A 444     7793   6461   3378   -495     28    208       C  
ATOM   3486  CE2 TYR A 444      22.351  86.069 223.822  1.00 49.20           C  
ANISOU 3486  CE2 TYR A 444     8314   6701   3680   -467    -11    279       C  
ATOM   3487  CZ  TYR A 444      21.492  86.397 222.792  1.00 48.26           C  
ANISOU 3487  CZ  TYR A 444     8118   6648   3569   -555     25    249       C  
ATOM   3488  OH  TYR A 444      20.142  86.241 222.962  1.00 49.57           O  
ANISOU 3488  OH  TYR A 444     8297   6837   3700   -705     55    264       O  
ATOM   3489  N   VAL A 445      28.344  86.974 220.415  1.00 49.53           N  
ANISOU 3489  N   VAL A 445     8065   6754   4000    184    -50    127       N  
ATOM   3490  CA  VAL A 445      29.768  87.278 220.388  1.00 49.84           C  
ANISOU 3490  CA  VAL A 445     8020   6806   4110    332    -68    118       C  
ATOM   3491  C   VAL A 445      29.963  88.775 220.291  1.00 49.33           C  
ANISOU 3491  C   VAL A 445     7776   6879   4088    331    -60    114       C  
ATOM   3492  O   VAL A 445      29.145  89.482 219.680  1.00 47.84           O  
ANISOU 3492  O   VAL A 445     7526   6765   3884    240    -23    100       O  
ATOM   3493  CB  VAL A 445      30.513  86.580 219.221  1.00 50.66           C  
ANISOU 3493  CB  VAL A 445     8157   6847   4243    420    -28     69       C  
ATOM   3494  CG1 VAL A 445      30.554  85.074 219.463  1.00 52.01           C  
ANISOU 3494  CG1 VAL A 445     8514   6864   4384    450    -42     75       C  
ATOM   3495  CG2 VAL A 445      29.891  86.934 217.835  1.00 49.44           C  
ANISOU 3495  CG2 VAL A 445     7970   6747   4069    340     38     22       C  
ATOM   3496  N   CYS A 446      31.049  89.244 220.900  1.00 50.30           N  
ANISOU 3496  N   CYS A 446     7815   7030   4265    431   -101    128       N  
ATOM   3497  CA  CYS A 446      31.416  90.652 220.840  1.00 51.03           C  
ANISOU 3497  CA  CYS A 446     7741   7242   4406    439    -97    122       C  
ATOM   3498  C   CYS A 446      32.873  90.882 220.462  1.00 50.69           C  
ANISOU 3498  C   CYS A 446     7597   7218   4444    569   -101    102       C  
ATOM   3499  O   CYS A 446      33.787  90.440 221.152  1.00 51.88           O  
ANISOU 3499  O   CYS A 446     7759   7328   4627    665   -155    121       O  
ATOM   3500  CB  CYS A 446      31.038  91.410 222.131  1.00 50.93           C  
ANISOU 3500  CB  CYS A 446     7698   7279   4372    387   -142    161       C  
ATOM   3501  SG  CYS A 446      31.986  91.005 223.666  1.00 58.47           S  
ANISOU 3501  SG  CYS A 446     8698   8186   5332    476   -240    205       S  
ATOM   3502  N   ARG A 447      33.074  91.599 219.363  1.00 49.93           N  
ANISOU 3502  N   ARG A 447     7400   7191   4382    568    -43     68       N  
ATOM   3503  CA  ARG A 447      34.408  92.002 218.938  1.00 49.78           C  
ANISOU 3503  CA  ARG A 447     7261   7210   4445    674    -31     47       C  
ATOM   3504  C   ARG A 447      34.525  93.524 218.805  1.00 48.32           C  
ANISOU 3504  C   ARG A 447     6922   7142   4294    637    -17     45       C  
ATOM   3505  O   ARG A 447      33.534  94.224 218.922  1.00 47.41           O  
ANISOU 3505  O   ARG A 447     6800   7072   4141    536    -10     57       O  
ATOM   3506  CB  ARG A 447      34.779  91.306 217.634  1.00 50.93           C  
ANISOU 3506  CB  ARG A 447     7439   7311   4601    726     40      1       C  
ATOM   3507  CG  ARG A 447      33.636  91.135 216.701  1.00 50.55           C  
ANISOU 3507  CG  ARG A 447     7468   7255   4483    621     94    -21       C  
ATOM   3508  CD  ARG A 447      34.065  91.520 215.347  1.00 53.41           C  
ANISOU 3508  CD  ARG A 447     7765   7661   4866    640    171    -64       C  
ATOM   3509  NE  ARG A 447      33.106  91.011 214.386  1.00 57.08           N  
ANISOU 3509  NE  ARG A 447     8337   8094   5258    557    215    -90       N  
ATOM   3510  CZ  ARG A 447      33.134  91.264 213.088  1.00 57.80           C  
ANISOU 3510  CZ  ARG A 447     8411   8218   5333    539    284   -127       C  
ATOM   3511  NH1 ARG A 447      34.075  92.046 212.571  1.00 58.48           N  
ANISOU 3511  NH1 ARG A 447     8373   8370   5475    598    326   -142       N  
ATOM   3512  NH2 ARG A 447      32.212  90.735 212.307  1.00 58.94           N  
ANISOU 3512  NH2 ARG A 447     8664   8329   5401    455    309   -149       N  
ATOM   3513  N   ARG A 448      35.747  94.016 218.579  1.00 48.08           N  
ANISOU 3513  N   ARG A 448     6769   7156   4342    720    -11     31       N  
ATOM   3514  CA  ARG A 448      36.035  95.453 218.456  1.00 46.62           C  
ANISOU 3514  CA  ARG A 448     6439   7074   4199    690      2     29       C  
ATOM   3515  C   ARG A 448      36.682  95.881 217.111  1.00 45.90           C  
ANISOU 3515  C   ARG A 448     6257   7029   4155    719     85     -7       C  
ATOM   3516  O   ARG A 448      37.840  95.597 216.858  1.00 46.72           O  
ANISOU 3516  O   ARG A 448     6301   7129   4323    817     98    -24       O  
ATOM   3517  CB  ARG A 448      36.911  95.899 219.627  1.00 46.68           C  
ANISOU 3517  CB  ARG A 448     6367   7110   4258    738    -77     52       C  
ATOM   3518  CG  ARG A 448      36.183  96.005 220.957  1.00 47.18           C  
ANISOU 3518  CG  ARG A 448     6498   7163   4267    678   -148     88       C  
ATOM   3519  CD  ARG A 448      37.115  96.613 222.024  1.00 48.85           C  
ANISOU 3519  CD  ARG A 448     6623   7415   4524    716   -228    106       C  
ATOM   3520  NE  ARG A 448      36.410  97.484 222.970  1.00 47.91           N  
ANISOU 3520  NE  ARG A 448     6512   7332   4360    626   -261    123       N  
ATOM   3521  CZ  ARG A 448      36.730  98.754 223.244  1.00 48.83           C  
ANISOU 3521  CZ  ARG A 448     6522   7522   4510    593   -272    117       C  
ATOM   3522  NH1 ARG A 448      37.762  99.349 222.641  1.00 49.47           N  
ANISOU 3522  NH1 ARG A 448     6470   7654   4671    636   -255     98       N  
ATOM   3523  NH2 ARG A 448      36.011  99.445 224.133  1.00 48.23           N  
ANISOU 3523  NH2 ARG A 448     6476   7465   4386    514   -294    129       N  
ATOM   3524  N   GLU A 449      35.925  96.560 216.257  1.00 44.15           N  
ANISOU 3524  N   GLU A 449     6025   6851   3899    635    141    -15       N  
ATOM   3525  CA  GLU A 449      36.490  97.248 215.086  1.00 43.24           C  
ANISOU 3525  CA  GLU A 449     5817   6792   3818    644    217    -41       C  
ATOM   3526  C   GLU A 449      37.119  98.620 215.463  1.00 41.29           C  
ANISOU 3526  C   GLU A 449     5423   6628   3636    635    203    -28       C  
ATOM   3527  O   GLU A 449      37.047  99.056 216.603  1.00 40.81           O  
ANISOU 3527  O   GLU A 449     5340   6580   3586    617    134     -3       O  
ATOM   3528  CB  GLU A 449      35.415  97.491 214.017  1.00 43.23           C  
ANISOU 3528  CB  GLU A 449     5868   6807   3750    554    272    -48       C  
ATOM   3529  CG  GLU A 449      34.386  96.399 213.825  1.00 46.14           C  
ANISOU 3529  CG  GLU A 449     6385   7106   4040    513    268    -53       C  
ATOM   3530  CD  GLU A 449      34.826  95.297 212.873  1.00 51.69           C  
ANISOU 3530  CD  GLU A 449     7165   7748   4726    570    323    -94       C  
ATOM   3531  OE1 GLU A 449      35.300  95.586 211.733  1.00 54.16           O  
ANISOU 3531  OE1 GLU A 449     7440   8093   5047    584    397   -123       O  
ATOM   3532  OE2 GLU A 449      34.666  94.122 213.274  1.00 54.00           O  
ANISOU 3532  OE2 GLU A 449     7567   7954   4995    597    297    -99       O  
ATOM   3533  N   LEU A 450      37.718  99.291 214.483  1.00 39.71           N  
ANISOU 3533  N   LEU A 450     5135   6480   3472    640    272    -46       N  
ATOM   3534  CA  LEU A 450      38.301 100.613 214.666  1.00 38.76           C  
ANISOU 3534  CA  LEU A 450     4882   6433   3411    618    272    -36       C  
ATOM   3535  C   LEU A 450      37.926 101.453 213.469  1.00 38.36           C  
ANISOU 3535  C   LEU A 450     4810   6426   3338    554    350    -39       C  
ATOM   3536  O   LEU A 450      38.207 101.079 212.337  1.00 38.82           O  
ANISOU 3536  O   LEU A 450     4883   6481   3385    576    425    -64       O  
ATOM   3537  CB  LEU A 450      39.828 100.534 214.760  1.00 39.71           C  
ANISOU 3537  CB  LEU A 450     4889   6575   3624    710    275    -52       C  
ATOM   3538  CG  LEU A 450      40.539 100.015 216.022  1.00 40.31           C  
ANISOU 3538  CG  LEU A 450     4940   6629   3747    783    181    -40       C  
ATOM   3539  CD1 LEU A 450      42.038  99.971 215.832  1.00 41.40           C  
ANISOU 3539  CD1 LEU A 450     4946   6798   3985    873    199    -58       C  
ATOM   3540  CD2 LEU A 450      40.228 100.871 217.273  1.00 40.97           C  
ANISOU 3540  CD2 LEU A 450     5001   6740   3827    722     94    -12       C  
ATOM   3541  N   ALA A 451      37.282 102.587 213.691  1.00 37.61           N  
ANISOU 3541  N   ALA A 451     4688   6368   3232    475    336    -15       N  
ATOM   3542  CA  ALA A 451      37.012 103.482 212.569  1.00 37.35           C  
ANISOU 3542  CA  ALA A 451     4630   6377   3184    419    405     -9       C  
ATOM   3543  C   ALA A 451      38.096 104.535 212.397  1.00 37.66           C  
ANISOU 3543  C   ALA A 451     4542   6470   3298    423    438    -11       C  
ATOM   3544  O   ALA A 451      38.871 104.841 213.323  1.00 37.89           O  
ANISOU 3544  O   ALA A 451     4491   6513   3392    448    392    -11       O  
ATOM   3545  CB  ALA A 451      35.611 104.114 212.641  1.00 36.49           C  
ANISOU 3545  CB  ALA A 451     4571   6273   3021    333    384     21       C  
ATOM   3546  N   THR A 452      38.135 105.087 211.191  1.00 37.76           N  
ANISOU 3546  N   THR A 452     4539   6511   3296    390    516    -10       N  
ATOM   3547  CA  THR A 452      39.072 106.145 210.875  1.00 38.10           C  
ANISOU 3547  CA  THR A 452     4470   6605   3403    377    562     -8       C  
ATOM   3548  C   THR A 452      38.443 107.524 210.668  1.00 37.53           C  
ANISOU 3548  C   THR A 452     4384   6556   3318    291    570     26       C  
ATOM   3549  O   THR A 452      37.868 107.815 209.632  1.00 37.41           O  
ANISOU 3549  O   THR A 452     4416   6548   3250    250    620     41       O  
ATOM   3550  CB  THR A 452      39.950 105.710 209.730  1.00 38.98           C  
ANISOU 3550  CB  THR A 452     4557   6730   3524    418    656    -36       C  
ATOM   3551  OG1 THR A 452      40.686 104.559 210.183  1.00 39.64           O  
ANISOU 3551  OG1 THR A 452     4628   6787   3645    511    638    -66       O  
ATOM   3552  CG2 THR A 452      40.877 106.826 209.315  1.00 39.43           C  
ANISOU 3552  CG2 THR A 452     4497   6841   3643    391    715    -31       C  
ATOM   3553  N   ALA A 453      38.569 108.348 211.708  1.00 37.26           N  
ANISOU 3553  N   ALA A 453     4294   6532   3333    268    516     38       N  
ATOM   3554  CA  ALA A 453      38.229 109.780 211.704  1.00 36.91           C  
ANISOU 3554  CA  ALA A 453     4220   6502   3300    197    522     66       C  
ATOM   3555  C   ALA A 453      38.906 110.527 210.571  1.00 37.42           C  
ANISOU 3555  C   ALA A 453     4232   6601   3387    170    609     73       C  
ATOM   3556  O   ALA A 453      39.994 110.149 210.147  1.00 38.18           O  
ANISOU 3556  O   ALA A 453     4267   6719   3520    206    657     49       O  
ATOM   3557  CB  ALA A 453      38.654 110.387 212.999  1.00 36.88           C  
ANISOU 3557  CB  ALA A 453     4156   6502   3356    188    459     62       C  
ATOM   3558  N   PRO A 454      38.283 111.617 210.087  1.00 37.13           N  
ANISOU 3558  N   PRO A 454     4213   6564   3329    106    633    108       N  
ATOM   3559  CA  PRO A 454      38.933 112.379 209.025  1.00 37.71           C  
ANISOU 3559  CA  PRO A 454     4245   6664   3417     71    717    120       C  
ATOM   3560  C   PRO A 454      40.371 112.789 209.358  1.00 38.44           C  
ANISOU 3560  C   PRO A 454     4216   6787   3602     74    739     98       C  
ATOM   3561  O   PRO A 454      41.186 112.938 208.443  1.00 39.18           O  
ANISOU 3561  O   PRO A 454     4264   6910   3711     66    824     94       O  
ATOM   3562  CB  PRO A 454      38.048 113.616 208.890  1.00 37.27           C  
ANISOU 3562  CB  PRO A 454     4224   6594   3345      6    711    166       C  
ATOM   3563  CG  PRO A 454      36.763 113.178 209.361  1.00 36.53           C  
ANISOU 3563  CG  PRO A 454     4207   6473   3201     16    648    176       C  
ATOM   3564  CD  PRO A 454      37.012 112.238 210.478  1.00 36.39           C  
ANISOU 3564  CD  PRO A 454     4177   6447   3204     65    589    140       C  
ATOM   3565  N   ASP A 455      40.696 112.988 210.631  1.00 38.35           N  
ANISOU 3565  N   ASP A 455     4151   6772   3647     79    666     85       N  
ATOM   3566  CA  ASP A 455      42.057 113.410 210.962  1.00 39.16           C  
ANISOU 3566  CA  ASP A 455     4129   6909   3840     73    675     66       C  
ATOM   3567  C   ASP A 455      43.025 112.257 211.208  1.00 39.81           C  
ANISOU 3567  C   ASP A 455     4147   7016   3965    154    665     29       C  
ATOM   3568  O   ASP A 455      44.084 112.441 211.788  1.00 40.49           O  
ANISOU 3568  O   ASP A 455     4121   7132   4131    160    640     13       O  
ATOM   3569  CB  ASP A 455      42.075 114.405 212.125  1.00 38.98           C  
ANISOU 3569  CB  ASP A 455     4074   6876   3862     22    605     69       C  
ATOM   3570  CG  ASP A 455      41.899 113.742 213.479  1.00 38.68           C  
ANISOU 3570  CG  ASP A 455     4051   6822   3824     64    500     49       C  
ATOM   3571  OD1 ASP A 455      41.330 112.638 213.538  1.00 39.87           O  
ANISOU 3571  OD1 ASP A 455     4269   6954   3924    121    478     45       O  
ATOM   3572  OD2 ASP A 455      42.308 114.337 214.501  1.00 39.67           O  
ANISOU 3572  OD2 ASP A 455     4128   6950   3993     34    439     39       O  
ATOM   3573  N   GLY A 456      42.665 111.064 210.772  1.00 39.71           N  
ANISOU 3573  N   GLY A 456     4202   6986   3900    216    680     18       N  
ATOM   3574  CA  GLY A 456      43.571 109.953 210.898  1.00 40.46           C  
ANISOU 3574  CA  GLY A 456     4243   7093   4037    304    680    -15       C  
ATOM   3575  C   GLY A 456      43.297 109.100 212.106  1.00 40.15           C  
ANISOU 3575  C   GLY A 456     4240   7023   3994    359    572    -22       C  
ATOM   3576  O   GLY A 456      43.578 107.910 212.057  1.00 40.56           O  
ANISOU 3576  O   GLY A 456     4307   7059   4046    441    572    -42       O  
ATOM   3577  N   THR A 457      42.724 109.679 213.169  1.00 39.51           N  
ANISOU 3577  N   THR A 457     4183   6926   3904    315    487     -7       N  
ATOM   3578  CA  THR A 457      42.520 108.983 214.457  1.00 39.33           C  
ANISOU 3578  CA  THR A 457     4195   6876   3874    356    380    -10       C  
ATOM   3579  C   THR A 457      41.679 107.715 214.363  1.00 38.95           C  
ANISOU 3579  C   THR A 457     4267   6779   3752    406    369    -12       C  
ATOM   3580  O   THR A 457      40.647 107.664 213.662  1.00 38.34           O  
ANISOU 3580  O   THR A 457     4281   6681   3605    375    411     -1       O  
ATOM   3581  CB  THR A 457      41.798 109.895 215.478  1.00 38.65           C  
ANISOU 3581  CB  THR A 457     4143   6775   3767    287    311      5       C  
ATOM   3582  OG1 THR A 457      42.010 111.265 215.134  1.00 38.69           O  
ANISOU 3582  OG1 THR A 457     4092   6804   3805    211    353     13       O  
ATOM   3583  CG2 THR A 457      42.287 109.645 216.893  1.00 38.99           C  
ANISOU 3583  CG2 THR A 457     4158   6817   3838    311    204     -3       C  
ATOM   3584  N   LYS A 458      42.094 106.702 215.116  1.00 39.38           N  
ANISOU 3584  N   LYS A 458     4324   6814   3823    480    306    -22       N  
ATOM   3585  CA  LYS A 458      41.326 105.447 215.185  1.00 39.12           C  
ANISOU 3585  CA  LYS A 458     4414   6726   3724    524    286    -22       C  
ATOM   3586  C   LYS A 458      40.285 105.480 216.313  1.00 38.38           C  
ANISOU 3586  C   LYS A 458     4409   6599   3574    484    204     -3       C  
ATOM   3587  O   LYS A 458      40.656 105.615 217.484  1.00 38.58           O  
ANISOU 3587  O   LYS A 458     4406   6628   3624    490    121      2       O  
ATOM   3588  CB  LYS A 458      42.268 104.246 215.327  1.00 40.09           C  
ANISOU 3588  CB  LYS A 458     4512   6832   3891    632    269    -40       C  
ATOM   3589  CG  LYS A 458      43.336 104.137 214.225  1.00 41.01           C  
ANISOU 3589  CG  LYS A 458     4534   6980   4067    681    364    -65       C  
ATOM   3590  CD  LYS A 458      42.720 103.883 212.864  1.00 40.77           C  
ANISOU 3590  CD  LYS A 458     4585   6933   3971    662    468    -76       C  
ATOM   3591  CE  LYS A 458      43.755 103.360 211.874  1.00 44.30           C  
ANISOU 3591  CE  LYS A 458     4972   7395   4466    735    564   -109       C  
ATOM   3592  NZ  LYS A 458      43.275 103.359 210.445  1.00 47.05           N  
ANISOU 3592  NZ  LYS A 458     5392   7740   4745    699    675   -122       N  
ATOM   3593  N   VAL A 459      38.992 105.389 215.947  1.00 37.61           N  
ANISOU 3593  N   VAL A 459     4416   6475   3401    438    228      9       N  
ATOM   3594  CA  VAL A 459      37.867 105.404 216.904  1.00 36.95           C  
ANISOU 3594  CA  VAL A 459     4417   6362   3260    395    170     27       C  
ATOM   3595  C   VAL A 459      37.361 103.975 217.135  1.00 37.03           C  
ANISOU 3595  C   VAL A 459     4536   6317   3217    434    143     27       C  
ATOM   3596  O   VAL A 459      37.005 103.293 216.180  1.00 37.05           O  
ANISOU 3596  O   VAL A 459     4594   6299   3186    445    193     19       O  
ATOM   3597  CB  VAL A 459      36.694 106.237 216.370  1.00 36.17           C  
ANISOU 3597  CB  VAL A 459     4353   6272   3120    317    212     43       C  
ATOM   3598  CG1 VAL A 459      35.547 106.282 217.404  1.00 35.62           C  
ANISOU 3598  CG1 VAL A 459     4357   6176   3000    275    162     59       C  
ATOM   3599  CG2 VAL A 459      37.149 107.665 215.952  1.00 36.16           C  
ANISOU 3599  CG2 VAL A 459     4259   6314   3168    275    251     47       C  
ATOM   3600  N   PRO A 460      37.349 103.504 218.401  1.00 37.18           N  
ANISOU 3600  N   PRO A 460     4595   6307   3223    453     63     35       N  
ATOM   3601  CA  PRO A 460      36.990 102.107 218.636  1.00 37.42           C  
ANISOU 3601  CA  PRO A 460     4733   6277   3208    493     37     38       C  
ATOM   3602  C   PRO A 460      35.506 101.900 218.522  1.00 36.75           C  
ANISOU 3602  C   PRO A 460     4752   6165   3045    425     56     50       C  
ATOM   3603  O   PRO A 460      34.751 102.766 218.929  1.00 36.16           O  
ANISOU 3603  O   PRO A 460     4674   6113   2952    358     52     63       O  
ATOM   3604  CB  PRO A 460      37.431 101.872 220.093  1.00 37.83           C  
ANISOU 3604  CB  PRO A 460     4794   6313   3266    521    -59     51       C  
ATOM   3605  CG  PRO A 460      38.360 103.007 220.427  1.00 38.03           C  
ANISOU 3605  CG  PRO A 460     4694   6397   3357    515    -82     46       C  
ATOM   3606  CD  PRO A 460      37.837 104.151 219.632  1.00 37.34           C  
ANISOU 3606  CD  PRO A 460     4567   6348   3272    443    -10     41       C  
ATOM   3607  N   ILE A 461      35.091 100.762 217.986  1.00 36.93           N  
ANISOU 3607  N   ILE A 461     4865   6140   3027    442     76     45       N  
ATOM   3608  CA  ILE A 461      33.694 100.367 218.050  1.00 36.48           C  
ANISOU 3608  CA  ILE A 461     4911   6054   2897    375     79     58       C  
ATOM   3609  C   ILE A 461      33.498  99.024 218.772  1.00 36.94           C  
ANISOU 3609  C   ILE A 461     5083   6039   2915    401     34     65       C  
ATOM   3610  O   ILE A 461      34.192  98.047 218.495  1.00 37.63           O  
ANISOU 3610  O   ILE A 461     5203   6080   3014    473     33     52       O  
ATOM   3611  CB  ILE A 461      33.074 100.267 216.655  1.00 36.29           C  
ANISOU 3611  CB  ILE A 461     4910   6037   2843    339    145     47       C  
ATOM   3612  CG1 ILE A 461      33.233 101.572 215.879  1.00 35.93           C  
ANISOU 3612  CG1 ILE A 461     4766   6057   2830    312    190     47       C  
ATOM   3613  CG2 ILE A 461      31.616  99.952 216.764  1.00 35.91           C  
ANISOU 3613  CG2 ILE A 461     4948   5970   2728    262    140     63       C  
ATOM   3614  CD1 ILE A 461      32.931 101.414 214.412  1.00 35.99           C  
ANISOU 3614  CD1 ILE A 461     4797   6072   2806    292    252     36       C  
ATOM   3615  N   SER A 462      32.554  98.981 219.702  1.00 36.65           N  
ANISOU 3615  N   SER A 462     5110   5987   2830    343      3     87       N  
ATOM   3616  CA  SER A 462      32.248  97.745 220.415  1.00 37.12           C  
ANISOU 3616  CA  SER A 462     5290   5973   2841    351    -36    100       C  
ATOM   3617  C   SER A 462      30.919  97.204 219.885  1.00 36.89           C  
ANISOU 3617  C   SER A 462     5347   5918   2750    273      1    102       C  
ATOM   3618  O   SER A 462      29.954  97.969 219.704  1.00 36.28           O  
ANISOU 3618  O   SER A 462     5240   5887   2657    196     28    109       O  
ATOM   3619  CB  SER A 462      32.203  97.967 221.943  1.00 37.18           C  
ANISOU 3619  CB  SER A 462     5320   5977   2830    338    -99    124       C  
ATOM   3620  OG  SER A 462      33.519  97.998 222.488  1.00 37.75           O  
ANISOU 3620  OG  SER A 462     5342   6051   2949    420   -155    125       O  
ATOM   3621  N   LEU A 463      30.861  95.909 219.594  1.00 37.46           N  
ANISOU 3621  N   LEU A 463     5524   5916   2792    293      1     96       N  
ATOM   3622  CA  LEU A 463      29.633  95.368 219.047  1.00 37.36           C  
ANISOU 3622  CA  LEU A 463     5592   5881   2722    209     31     95       C  
ATOM   3623  C   LEU A 463      29.283  93.999 219.497  1.00 38.01           C  
ANISOU 3623  C   LEU A 463     5817   5870   2754    199      9    103       C  
ATOM   3624  O   LEU A 463      30.149  93.171 219.766  1.00 38.71           O  
ANISOU 3624  O   LEU A 463     5959   5892   2855    282    -17    101       O  
ATOM   3625  CB  LEU A 463      29.608  95.370 217.516  1.00 37.33           C  
ANISOU 3625  CB  LEU A 463     5570   5895   2720    203     84     65       C  
ATOM   3626  CG  LEU A 463      30.852  95.300 216.685  1.00 37.73           C  
ANISOU 3626  CG  LEU A 463     5577   5943   2815    295    112     35       C  
ATOM   3627  CD1 LEU A 463      30.656  94.305 215.601  1.00 38.25           C  
ANISOU 3627  CD1 LEU A 463     5737   5956   2842    289    150      5       C  
ATOM   3628  CD2 LEU A 463      31.002  96.664 216.117  1.00 37.13           C  
ANISOU 3628  CD2 LEU A 463     5376   5957   2775    279    142     34       C  
ATOM   3629  N   VAL A 464      27.984  93.758 219.518  1.00 37.86           N  
ANISOU 3629  N   VAL A 464     5856   5845   2682     96     22    115       N  
ATOM   3630  CA  VAL A 464      27.496  92.460 219.842  1.00 39.72           C  
ANISOU 3630  CA  VAL A 464     6236   5991   2865     63     10    123       C  
ATOM   3631  C   VAL A 464      26.383  92.085 218.870  1.00 40.59           C  
ANISOU 3631  C   VAL A 464     6389   6099   2934    -35     45    109       C  
ATOM   3632  O   VAL A 464      25.631  92.950 218.431  1.00 39.65           O  
ANISOU 3632  O   VAL A 464     6188   6061   2818   -101     66    111       O  
ATOM   3633  CB  VAL A 464      27.083  92.415 221.309  1.00 39.38           C  
ANISOU 3633  CB  VAL A 464     6237   5932   2792     28    -24    161       C  
ATOM   3634  CG1 VAL A 464      26.249  93.628 221.630  1.00 40.16           C  
ANISOU 3634  CG1 VAL A 464     6241   6124   2893    -46     -5    173       C  
ATOM   3635  CG2 VAL A 464      26.352  91.149 221.627  1.00 39.57           C  
ANISOU 3635  CG2 VAL A 464     6412   5867   2754    -33    -28    175       C  
ATOM   3636  N   TYR A 465      26.348  90.793 218.525  1.00 42.98           N  
ANISOU 3636  N   TYR A 465     6822   6308   3202    -39     46     94       N  
ATOM   3637  CA  TYR A 465      25.358  90.164 217.639  1.00 45.07           C  
ANISOU 3637  CA  TYR A 465     7158   6549   3416   -138     69     76       C  
ATOM   3638  C   TYR A 465      25.156  88.651 217.937  1.00 47.29           C  
ANISOU 3638  C   TYR A 465     7615   6703   3650   -161     58     76       C  
ATOM   3639  O   TYR A 465      26.075  87.928 218.370  1.00 48.01           O  
ANISOU 3639  O   TYR A 465     7782   6707   3753    -66     40     77       O  
ATOM   3640  CB  TYR A 465      25.726  90.375 216.147  1.00 45.14           C  
ANISOU 3640  CB  TYR A 465     7131   6587   3435   -113    103     34       C  
ATOM   3641  CG  TYR A 465      27.160  89.998 215.808  1.00 46.29           C  
ANISOU 3641  CG  TYR A 465     7291   6681   3616     21    115      5       C  
ATOM   3642  CD1 TYR A 465      28.221  90.917 215.969  1.00 46.43           C  
ANISOU 3642  CD1 TYR A 465     7186   6757   3699    119    116      7       C  
ATOM   3643  CD2 TYR A 465      27.465  88.726 215.366  1.00 45.98           C  
ANISOU 3643  CD2 TYR A 465     7386   6532   3550     51    128    -26       C  
ATOM   3644  CE1 TYR A 465      29.538  90.550 215.680  1.00 46.32           C  
ANISOU 3644  CE1 TYR A 465     7170   6701   3727    243    131    -18       C  
ATOM   3645  CE2 TYR A 465      28.754  88.370 215.083  1.00 47.34           C  
ANISOU 3645  CE2 TYR A 465     7566   6657   3764    182    146    -53       C  
ATOM   3646  CZ  TYR A 465      29.778  89.271 215.233  1.00 47.57           C  
ANISOU 3646  CZ  TYR A 465     7460   6753   3862    278    148    -48       C  
ATOM   3647  OH  TYR A 465      31.046  88.856 214.926  1.00 51.03           O  
ANISOU 3647  OH  TYR A 465     7896   7146   4347    408    170    -76       O  
ATOM   3648  N   ASP A 466      23.937  88.181 217.690  1.00 49.03           N  
ANISOU 3648  N   ASP A 466     7898   6911   3819   -290     66     77       N  
ATOM   3649  CA  ASP A 466      23.646  86.764 217.731  1.00 51.19           C  
ANISOU 3649  CA  ASP A 466     8344   7063   4045   -334     63     71       C  
ATOM   3650  C   ASP A 466      24.569  86.080 216.738  1.00 52.28           C  
ANISOU 3650  C   ASP A 466     8553   7125   4187   -247     80     22       C  
ATOM   3651  O   ASP A 466      24.558  86.420 215.546  1.00 52.13           O  
ANISOU 3651  O   ASP A 466     8488   7154   4166   -258    105    -15       O  
ATOM   3652  CB  ASP A 466      22.184  86.496 217.346  1.00 51.94           C  
ANISOU 3652  CB  ASP A 466     8470   7176   4090   -500     71     71       C  
ATOM   3653  CG  ASP A 466      21.764  85.032 217.587  1.00 54.06           C  
ANISOU 3653  CG  ASP A 466     8925   7310   4304   -568     67     70       C  
ATOM   3654  OD1 ASP A 466      22.147  84.167 216.764  1.00 55.83           O  
ANISOU 3654  OD1 ASP A 466     9258   7447   4508   -545     76     28       O  
ATOM   3655  OD2 ASP A 466      21.057  84.752 218.595  1.00 53.31           O  
ANISOU 3655  OD2 ASP A 466     8874   7196   4185   -647     59    110       O  
ATOM   3656  N   THR A 467      25.350  85.127 217.246  1.00 53.27           N  
ANISOU 3656  N   THR A 467     8792   7132   4317   -159     67     24       N  
ATOM   3657  CA  THR A 467      26.324  84.331 216.478  1.00 54.65           C  
ANISOU 3657  CA  THR A 467     9049   7213   4504    -55     89    -21       C  
ATOM   3658  C   THR A 467      25.856  83.694 215.139  1.00 55.63           C  
ANISOU 3658  C   THR A 467     9265   7295   4579   -126    127    -78       C  
ATOM   3659  O   THR A 467      26.663  83.190 214.355  1.00 56.29           O  
ANISOU 3659  O   THR A 467     9402   7314   4670    -39    160   -126       O  
ATOM   3660  CB  THR A 467      26.949  83.234 217.383  1.00 55.63           C  
ANISOU 3660  CB  THR A 467     9307   7197   4632     30     62      2       C  
ATOM   3661  OG1 THR A 467      28.027  82.613 216.691  1.00 57.19           O  
ANISOU 3661  OG1 THR A 467     9556   7314   4861    158     88    -42       O  
ATOM   3662  CG2 THR A 467      25.934  82.168 217.793  1.00 56.39           C  
ANISOU 3662  CG2 THR A 467     9573   7191   4662    -92     51     20       C  
ATOM   3663  N   SER A 468      24.560  83.727 214.874  1.00 55.95           N  
ANISOU 3663  N   SER A 468     9319   7373   4567   -285    123    -75       N  
ATOM   3664  CA  SER A 468      24.022  83.030 213.732  1.00 56.83           C  
ANISOU 3664  CA  SER A 468     9537   7437   4620   -372    145   -125       C  
ATOM   3665  C   SER A 468      23.493  83.967 212.671  1.00 56.73           C  
ANISOU 3665  C   SER A 468     9410   7553   4591   -443    155   -144       C  
ATOM   3666  O   SER A 468      22.780  83.540 211.776  1.00 57.84           O  
ANISOU 3666  O   SER A 468     9622   7680   4673   -551    158   -178       O  
ATOM   3667  CB  SER A 468      22.889  82.137 214.184  1.00 57.43           C  
ANISOU 3667  CB  SER A 468     9738   7441   4640   -517    124   -107       C  
ATOM   3668  OG  SER A 468      21.759  82.945 214.418  1.00 56.51           O  
ANISOU 3668  OG  SER A 468     9509   7446   4517   -642    105    -72       O  
ATOM   3669  N   ILE A 469      23.801  85.247 212.742  1.00 56.32           N  
ANISOU 3669  N   ILE A 469     9187   7623   4588   -391    155   -122       N  
ATOM   3670  CA  ILE A 469      23.423  86.080 211.608  1.00 56.25           C  
ANISOU 3670  CA  ILE A 469     9089   7722   4561   -444    165   -140       C  
ATOM   3671  C   ILE A 469      24.445  85.890 210.507  1.00 57.21           C  
ANISOU 3671  C   ILE A 469     9248   7811   4677   -351    211   -198       C  
ATOM   3672  O   ILE A 469      25.602  85.532 210.765  1.00 57.32           O  
ANISOU 3672  O   ILE A 469     9291   7758   4732   -218    237   -213       O  
ATOM   3673  CB  ILE A 469      23.233  87.561 211.954  1.00 54.81           C  
ANISOU 3673  CB  ILE A 469     8718   7679   4427   -439    152    -96       C  
ATOM   3674  CG1 ILE A 469      24.463  88.118 212.676  1.00 54.23           C  
ANISOU 3674  CG1 ILE A 469     8563   7615   4425   -292    162    -81       C  
ATOM   3675  CG2 ILE A 469      21.979  87.720 212.777  1.00 54.58           C  
ANISOU 3675  CG2 ILE A 469     8657   7690   4391   -556    118    -50       C  
ATOM   3676  CD1 ILE A 469      24.780  89.546 212.341  1.00 53.16           C  
ANISOU 3676  CD1 ILE A 469     8264   7601   4333   -254    172    -69       C  
ATOM   3677  N   ASP A 470      24.000  86.110 209.281  1.00 58.08           N  
ANISOU 3677  N   ASP A 470     9361   7970   4735   -424    222   -228       N  
ATOM   3678  CA  ASP A 470      24.871  85.995 208.134  1.00 59.54           C  
ANISOU 3678  CA  ASP A 470     9586   8136   4901   -353    277   -285       C  
ATOM   3679  C   ASP A 470      25.692  87.253 208.030  1.00 58.95           C  
ANISOU 3679  C   ASP A 470     9349   8164   4887   -256    301   -268       C  
ATOM   3680  O   ASP A 470      25.138  88.332 207.801  1.00 58.98           O  
ANISOU 3680  O   ASP A 470     9235   8283   4891   -314    280   -235       O  
ATOM   3681  CB  ASP A 470      24.046  85.856 206.867  1.00 60.32           C  
ANISOU 3681  CB  ASP A 470     9749   8260   4908   -479    272   -319       C  
ATOM   3682  CG  ASP A 470      24.892  85.543 205.660  1.00 62.74           C  
ANISOU 3682  CG  ASP A 470    10135   8527   5175   -418    338   -388       C  
ATOM   3683  OD1 ASP A 470      26.151  85.537 205.778  1.00 63.72           O  
ANISOU 3683  OD1 ASP A 470    10239   8617   5354   -270    393   -407       O  
ATOM   3684  OD2 ASP A 470      24.282  85.293 204.592  1.00 64.99           O  
ANISOU 3684  OD2 ASP A 470    10503   8819   5372   -521    334   -423       O  
ATOM   3685  N   LEU A 471      27.004  87.119 208.184  1.00 59.04           N  
ANISOU 3685  N   LEU A 471     9349   8131   4952   -111    345   -288       N  
ATOM   3686  CA  LEU A 471      27.890  88.267 208.099  1.00 58.35           C  
ANISOU 3686  CA  LEU A 471     9108   8135   4928    -20    373   -275       C  
ATOM   3687  C   LEU A 471      28.355  88.581 206.672  1.00 59.08           C  
ANISOU 3687  C   LEU A 471     9199   8265   4985     -6    438   -321       C  
ATOM   3688  O   LEU A 471      28.944  89.636 206.437  1.00 58.83           O  
ANISOU 3688  O   LEU A 471     9039   8320   4994     42    465   -307       O  
ATOM   3689  CB  LEU A 471      29.096  88.091 209.013  1.00 58.47           C  
ANISOU 3689  CB  LEU A 471     9083   8103   5028    127    382   -268       C  
ATOM   3690  CG  LEU A 471      28.963  88.208 210.533  1.00 57.69           C  
ANISOU 3690  CG  LEU A 471     8940   8000   4979    141    320   -212       C  
ATOM   3691  CD1 LEU A 471      30.357  88.289 211.123  1.00 56.30           C  
ANISOU 3691  CD1 LEU A 471     8695   7807   4888    295    330   -209       C  
ATOM   3692  CD2 LEU A 471      28.111  89.411 210.984  1.00 56.94           C  
ANISOU 3692  CD2 LEU A 471     8723   8021   4892     54    279   -160       C  
ATOM   3693  N   LYS A 472      28.088  87.687 205.719  1.00 60.11           N  
ANISOU 3693  N   LYS A 472     9477   8328   5033    -55    466   -376       N  
ATOM   3694  CA  LYS A 472      28.476  87.935 204.319  1.00 60.50           C  
ANISOU 3694  CA  LYS A 472     9547   8410   5029    -53    532   -423       C  
ATOM   3695  C   LYS A 472      27.528  88.896 203.564  1.00 59.39           C  
ANISOU 3695  C   LYS A 472     9351   8386   4828   -176    499   -394       C  
ATOM   3696  O   LYS A 472      27.680  89.112 202.347  1.00 59.76           O  
ANISOU 3696  O   LYS A 472     9431   8464   4810   -197    544   -427       O  
ATOM   3697  CB  LYS A 472      28.675  86.617 203.550  1.00 62.34           C  
ANISOU 3697  CB  LYS A 472     9971   8523   5193    -48    584   -501       C  
ATOM   3698  CG  LYS A 472      30.067  85.969 203.766  1.00 65.02           C  
ANISOU 3698  CG  LYS A 472    10336   8769   5599    120    658   -542       C  
ATOM   3699  CD  LYS A 472      30.249  84.696 202.892  1.00 69.65           C  
ANISOU 3699  CD  LYS A 472    11122   9229   6113    127    723   -628       C  
ATOM   3700  CE  LYS A 472      31.014  83.574 203.624  1.00 71.43           C  
ANISOU 3700  CE  LYS A 472    11427   9310   6402    256    745   -650       C  
ATOM   3701  NZ  LYS A 472      30.244  83.085 204.822  1.00 71.68           N  
ANISOU 3701  NZ  LYS A 472    11499   9287   6449    202    652   -599       N  
ATOM   3702  N   LYS A 473      26.550  89.456 204.278  1.00 57.44           N  
ANISOU 3702  N   LYS A 473     9025   8200   4600   -254    422   -332       N  
ATOM   3703  CA  LYS A 473      25.735  90.553 203.736  1.00 55.99           C  
ANISOU 3703  CA  LYS A 473     8752   8134   4386   -345    384   -290       C  
ATOM   3704  C   LYS A 473      25.373  91.603 204.820  1.00 53.58           C  
ANISOU 3704  C   LYS A 473     8288   7907   4163   -341    336   -218       C  
ATOM   3705  O   LYS A 473      25.454  91.310 206.017  1.00 52.98           O  
ANISOU 3705  O   LYS A 473     8195   7790   4144   -305    316   -200       O  
ATOM   3706  CB  LYS A 473      24.520  90.051 202.921  1.00 56.54           C  
ANISOU 3706  CB  LYS A 473     8928   8205   4350   -492    338   -304       C  
ATOM   3707  CG  LYS A 473      23.770  88.837 203.458  1.00 58.95           C  
ANISOU 3707  CG  LYS A 473     9349   8419   4628   -566    296   -319       C  
ATOM   3708  CD  LYS A 473      22.695  89.202 204.504  1.00 61.84           C  
ANISOU 3708  CD  LYS A 473     9624   8835   5038   -640    223   -253       C  
ATOM   3709  CE  LYS A 473      21.766  87.997 204.816  1.00 64.71           C  
ANISOU 3709  CE  LYS A 473    10113   9118   5356   -750    182   -268       C  
ATOM   3710  NZ  LYS A 473      21.305  87.886 206.257  1.00 64.33           N  
ANISOU 3710  NZ  LYS A 473    10017   9054   5371   -762    150   -221       N  
ATOM   3711  N   PRO A 474      25.023  92.842 204.401  1.00 51.61           N  
ANISOU 3711  N   PRO A 474     7928   7764   3916   -374    320   -176       N  
ATOM   3712  CA  PRO A 474      24.706  93.887 205.372  1.00 49.41           C  
ANISOU 3712  CA  PRO A 474     7505   7553   3715   -366    283   -114       C  
ATOM   3713  C   PRO A 474      23.530  93.539 206.290  1.00 48.36           C  
ANISOU 3713  C   PRO A 474     7375   7413   3589   -446    220    -83       C  
ATOM   3714  O   PRO A 474      22.665  92.764 205.919  1.00 49.26           O  
ANISOU 3714  O   PRO A 474     7578   7501   3638   -542    189    -96       O  
ATOM   3715  CB  PRO A 474      24.369  95.091 204.484  1.00 49.49           C  
ANISOU 3715  CB  PRO A 474     7435   7664   3706   -404    276    -79       C  
ATOM   3716  CG  PRO A 474      24.179  94.529 203.073  1.00 50.35           C  
ANISOU 3716  CG  PRO A 474     7663   7762   3708   -465    287   -118       C  
ATOM   3717  CD  PRO A 474      25.108  93.383 203.031  1.00 51.53           C  
ANISOU 3717  CD  PRO A 474     7926   7811   3844   -401    345   -185       C  
ATOM   3718  N   ASN A 475      23.513  94.098 207.492  1.00 46.41           N  
ANISOU 3718  N   ASN A 475     7032   7186   3416   -412    205    -44       N  
ATOM   3719  CA  ASN A 475      22.503  93.755 208.488  1.00 44.92           C  
ANISOU 3719  CA  ASN A 475     6845   6986   3236   -480    161    -17       C  
ATOM   3720  C   ASN A 475      21.922  94.995 209.116  1.00 43.72           C  
ANISOU 3720  C   ASN A 475     6551   6921   3141   -492    140     38       C  
ATOM   3721  O   ASN A 475      22.569  96.039 209.140  1.00 44.29           O  
ANISOU 3721  O   ASN A 475     6530   7037   3260   -424    160     53       O  
ATOM   3722  CB  ASN A 475      23.114  92.901 209.582  1.00 44.40           C  
ANISOU 3722  CB  ASN A 475     6843   6829   3197   -420    172    -32       C  
ATOM   3723  CG  ASN A 475      23.488  91.535 209.100  1.00 44.55           C  
ANISOU 3723  CG  ASN A 475     7017   6745   3164   -415    190    -84       C  
ATOM   3724  OD1 ASN A 475      22.665  90.635 209.060  1.00 41.88           O  
ANISOU 3724  OD1 ASN A 475     6778   6361   2776   -506    166    -93       O  
ATOM   3725  ND2 ASN A 475      24.749  91.370 208.730  1.00 45.83           N  
ANISOU 3725  ND2 ASN A 475     7203   6869   3341   -308    236   -120       N  
ATOM   3726  N   PRO A 476      20.698  94.907 209.631  1.00 42.73           N  
ANISOU 3726  N   PRO A 476     6406   6817   3012   -581    103     67       N  
ATOM   3727  CA  PRO A 476      20.248  96.100 210.307  1.00 41.69           C  
ANISOU 3727  CA  PRO A 476     6140   6759   2942   -575     95    114       C  
ATOM   3728  C   PRO A 476      21.012  96.326 211.640  1.00 40.74           C  
ANISOU 3728  C   PRO A 476     5993   6608   2879   -491    117    118       C  
ATOM   3729  O   PRO A 476      21.243  95.389 212.389  1.00 41.06           O  
ANISOU 3729  O   PRO A 476     6115   6577   2909   -483    118    103       O  
ATOM   3730  CB  PRO A 476      18.770  95.826 210.513  1.00 41.91           C  
ANISOU 3730  CB  PRO A 476     6156   6815   2954   -690     59    139       C  
ATOM   3731  CG  PRO A 476      18.674  94.327 210.583  1.00 42.51           C  
ANISOU 3731  CG  PRO A 476     6373   6804   2974   -742     53    105       C  
ATOM   3732  CD  PRO A 476      19.710  93.818 209.677  1.00 43.07           C  
ANISOU 3732  CD  PRO A 476     6538   6822   3006   -688     74     60       C  
ATOM   3733  N   THR A 477      21.417  97.564 211.901  1.00 39.82           N  
ANISOU 3733  N   THR A 477     5768   6542   2818   -433    131    139       N  
ATOM   3734  CA  THR A 477      22.295  97.890 213.041  1.00 39.01           C  
ANISOU 3734  CA  THR A 477     5639   6418   2766   -352    146    138       C  
ATOM   3735  C   THR A 477      21.748  99.059 213.869  1.00 37.76           C  
ANISOU 3735  C   THR A 477     5374   6316   2658   -359    146    173       C  
ATOM   3736  O   THR A 477      21.035  99.934 213.347  1.00 37.67           O  
ANISOU 3736  O   THR A 477     5285   6368   2662   -391    143    199       O  
ATOM   3737  CB  THR A 477      23.756  98.211 212.526  1.00 38.73           C  
ANISOU 3737  CB  THR A 477     5588   6374   2754   -257    172    114       C  
ATOM   3738  OG1 THR A 477      24.421  96.986 212.209  1.00 41.45           O  
ANISOU 3738  OG1 THR A 477     6039   6645   3064   -227    181     76       O  
ATOM   3739  CG2 THR A 477      24.592  98.936 213.527  1.00 36.35           C  
ANISOU 3739  CG2 THR A 477     5221   6078   2513   -184    178    121       C  
ATOM   3740  N   MET A 478      22.076  99.060 215.150  1.00 36.25           N  
ANISOU 3740  N   MET A 478     5186   6097   2489   -326    149    174       N  
ATOM   3741  CA  MET A 478      21.883 100.234 215.961  1.00 35.42           C  
ANISOU 3741  CA  MET A 478     4990   6034   2432   -312    159    196       C  
ATOM   3742  C   MET A 478      23.223 100.698 216.518  1.00 35.12           C  
ANISOU 3742  C   MET A 478     4933   5979   2430   -226    163    181       C  
ATOM   3743  O   MET A 478      23.957  99.934 217.174  1.00 35.74           O  
ANISOU 3743  O   MET A 478     5077   6005   2497   -188    150    166       O  
ATOM   3744  CB  MET A 478      20.937  99.942 217.095  1.00 35.94           C  
ANISOU 3744  CB  MET A 478     5074   6093   2488   -367    160    210       C  
ATOM   3745  CG  MET A 478      21.051 100.929 218.237  1.00 36.39           C  
ANISOU 3745  CG  MET A 478     5075   6168   2584   -336    176    219       C  
ATOM   3746  SD  MET A 478      20.148 102.404 217.843  1.00 38.69           S  
ANISOU 3746  SD  MET A 478     5238   6536   2925   -353    198    245       S  
ATOM   3747  CE  MET A 478      18.453 101.845 218.062  1.00 36.18           C  
ANISOU 3747  CE  MET A 478     4918   6242   2588   -453    206    267       C  
ATOM   3748  N   LEU A 479      23.554 101.952 216.239  1.00 34.18           N  
ANISOU 3748  N   LEU A 479     4726   5906   2357   -195    177    189       N  
ATOM   3749  CA  LEU A 479      24.807 102.515 216.687  1.00 34.00           C  
ANISOU 3749  CA  LEU A 479     4670   5876   2373   -125    179    176       C  
ATOM   3750  C   LEU A 479      24.507 103.532 217.797  1.00 33.73           C  
ANISOU 3750  C   LEU A 479     4583   5861   2371   -130    184    188       C  
ATOM   3751  O   LEU A 479      23.789 104.518 217.565  1.00 33.53           O  
ANISOU 3751  O   LEU A 479     4494   5876   2371   -154    202    207       O  
ATOM   3752  CB  LEU A 479      25.535 103.157 215.515  1.00 33.93           C  
ANISOU 3752  CB  LEU A 479     4609   5894   2388    -93    198    172       C  
ATOM   3753  CG  LEU A 479      26.839 103.882 215.847  1.00 33.82           C  
ANISOU 3753  CG  LEU A 479     4541   5884   2425    -31    204    159       C  
ATOM   3754  CD1 LEU A 479      27.958 102.885 216.196  1.00 34.18           C  
ANISOU 3754  CD1 LEU A 479     4633   5886   2468     26    188    132       C  
ATOM   3755  CD2 LEU A 479      27.225 104.702 214.672  1.00 33.78           C  
ANISOU 3755  CD2 LEU A 479     4479   5914   2441    -22    234    165       C  
ATOM   3756  N   TYR A 480      25.037 103.282 218.995  1.00 33.81           N  
ANISOU 3756  N   TYR A 480     4627   5841   2378   -106    166    177       N  
ATOM   3757  CA  TYR A 480      24.707 104.085 220.146  1.00 33.69           C  
ANISOU 3757  CA  TYR A 480     4588   5836   2376   -118    173    181       C  
ATOM   3758  C   TYR A 480      25.913 104.920 220.476  1.00 33.59           C  
ANISOU 3758  C   TYR A 480     4530   5828   2405    -67    162    166       C  
ATOM   3759  O   TYR A 480      27.039 104.427 220.381  1.00 33.77           O  
ANISOU 3759  O   TYR A 480     4567   5832   2434    -20    136    152       O  
ATOM   3760  CB  TYR A 480      24.336 103.167 221.296  1.00 34.00           C  
ANISOU 3760  CB  TYR A 480     4712   5837   2367   -144    158    182       C  
ATOM   3761  CG  TYR A 480      24.043 103.862 222.605  1.00 34.01           C  
ANISOU 3761  CG  TYR A 480     4712   5845   2367   -159    169    181       C  
ATOM   3762  CD1 TYR A 480      25.072 104.202 223.455  1.00 34.10           C  
ANISOU 3762  CD1 TYR A 480     4731   5842   2383   -119    140    166       C  
ATOM   3763  CD2 TYR A 480      22.749 104.175 222.990  1.00 34.06           C  
ANISOU 3763  CD2 TYR A 480     4706   5871   2365   -213    209    192       C  
ATOM   3764  CE1 TYR A 480      24.845 104.818 224.638  1.00 34.21           C  
ANISOU 3764  CE1 TYR A 480     4758   5857   2384   -137    149    159       C  
ATOM   3765  CE2 TYR A 480      22.503 104.809 224.182  1.00 34.18           C  
ANISOU 3765  CE2 TYR A 480     4728   5887   2373   -225    230    185       C  
ATOM   3766  CZ  TYR A 480      23.562 105.128 225.012  1.00 34.25           C  
ANISOU 3766  CZ  TYR A 480     4761   5877   2377   -189    200    167       C  
ATOM   3767  OH  TYR A 480      23.403 105.764 226.235  1.00 34.47           O  
ANISOU 3767  OH  TYR A 480     4810   5901   2385   -204    218    154       O  
ATOM   3768  N   GLY A 481      25.674 106.185 220.842  1.00 33.40           N  
ANISOU 3768  N   GLY A 481     4450   5828   2414    -76    183    168       N  
ATOM   3769  CA  GLY A 481      26.740 107.111 221.267  1.00 33.39           C  
ANISOU 3769  CA  GLY A 481     4406   5830   2452    -44    172    152       C  
ATOM   3770  C   GLY A 481      26.481 107.926 222.529  1.00 33.46           C  
ANISOU 3770  C   GLY A 481     4419   5833   2461    -62    178    142       C  
ATOM   3771  O   GLY A 481      25.342 108.155 222.896  1.00 33.44           O  
ANISOU 3771  O   GLY A 481     4426   5836   2445    -96    211    150       O  
ATOM   3772  N   TYR A 482      27.552 108.355 223.201  1.00 33.63           N  
ANISOU 3772  N   TYR A 482     4433   5849   2498    -41    147    121       N  
ATOM   3773  CA  TYR A 482      27.439 109.363 224.279  1.00 33.77           C  
ANISOU 3773  CA  TYR A 482     4453   5861   2517    -61    155    104       C  
ATOM   3774  C   TYR A 482      27.991 110.697 223.789  1.00 33.68           C  
ANISOU 3774  C   TYR A 482     4368   5862   2569    -54    173     96       C  
ATOM   3775  O   TYR A 482      27.209 111.375 223.199  1.00 33.49           O  
ANISOU 3775  O   TYR A 482     4309   5845   2569    -65    220    110       O  
ATOM   3776  CB  TYR A 482      27.915 108.909 225.641  1.00 34.18           C  
ANISOU 3776  CB  TYR A 482     4575   5892   2521    -63    107     88       C  
ATOM   3777  CG  TYR A 482      27.428 109.784 226.753  1.00 34.39           C  
ANISOU 3777  CG  TYR A 482     4630   5910   2527    -97    131     69       C  
ATOM   3778  CD1 TYR A 482      26.097 109.848 227.086  1.00 34.38           C  
ANISOU 3778  CD1 TYR A 482     4658   5906   2500   -129    189     74       C  
ATOM   3779  CD2 TYR A 482      28.313 110.539 227.503  1.00 34.72           C  
ANISOU 3779  CD2 TYR A 482     4671   5946   2575    -99     97     41       C  
ATOM   3780  CE1 TYR A 482      25.651 110.649 228.133  1.00 34.69           C  
ANISOU 3780  CE1 TYR A 482     4729   5933   2519   -156    223     50       C  
ATOM   3781  CE2 TYR A 482      27.874 111.328 228.558  1.00 35.02           C  
ANISOU 3781  CE2 TYR A 482     4752   5970   2585   -133    123     16       C  
ATOM   3782  CZ  TYR A 482      26.547 111.386 228.852  1.00 35.00           C  
ANISOU 3782  CZ  TYR A 482     4781   5961   2556   -158    191     20       C  
ATOM   3783  OH  TYR A 482      26.140 112.198 229.874  1.00 35.40           O  
ANISOU 3783  OH  TYR A 482     4875   5994   2580   -187    228    -11       O  
ATOM   3784  N   GLY A 483      29.234 111.168 223.899  1.00 33.89           N  
ANISOU 3784  N   GLY A 483     4359   5890   2626    -40    140     78       N  
ATOM   3785  CA  GLY A 483      30.379 110.818 224.682  1.00 34.30           C  
ANISOU 3785  CA  GLY A 483     4425   5938   2668    -26     75     59       C  
ATOM   3786  C   GLY A 483      30.829 112.254 224.992  1.00 34.48           C  
ANISOU 3786  C   GLY A 483     4408   5961   2732    -50     83     37       C  
ATOM   3787  O   GLY A 483      31.432 112.949 224.155  1.00 34.45           O  
ANISOU 3787  O   GLY A 483     4333   5970   2786    -47    100     38       O  
ATOM   3788  N   SER A 484      30.421 112.725 226.179  1.00 34.72           N  
ANISOU 3788  N   SER A 484     4493   5972   2727    -81     82     16       N  
ATOM   3789  CA  SER A 484      30.816 114.008 226.718  1.00 35.05           C  
ANISOU 3789  CA  SER A 484     4523   6001   2792   -112     84    -14       C  
ATOM   3790  C   SER A 484      31.414 113.755 228.056  1.00 35.62           C  
ANISOU 3790  C   SER A 484     4654   6067   2813   -128     15    -40       C  
ATOM   3791  O   SER A 484      31.581 112.601 228.427  1.00 35.74           O  
ANISOU 3791  O   SER A 484     4708   6087   2783   -108    -34    -28       O  
ATOM   3792  CB  SER A 484      29.604 114.870 226.849  1.00 34.92           C  
ANISOU 3792  CB  SER A 484     4530   5961   2777   -133    159    -18       C  
ATOM   3793  OG  SER A 484      29.082 115.049 225.553  1.00 34.48           O  
ANISOU 3793  OG  SER A 484     4418   5915   2767   -114    208     14       O  
ATOM   3794  N   TYR A 485      31.797 114.822 228.754  1.00 36.07           N  
ANISOU 3794  N   TYR A 485     4720   6109   2875   -167      5    -75       N  
ATOM   3795  CA  TYR A 485      32.153 114.756 230.182  1.00 36.73           C  
ANISOU 3795  CA  TYR A 485     4882   6183   2893   -196    -58   -104       C  
ATOM   3796  C   TYR A 485      33.364 113.917 230.618  1.00 37.24           C  
ANISOU 3796  C   TYR A 485     4938   6271   2938   -180   -168    -99       C  
ATOM   3797  O   TYR A 485      33.836 114.074 231.765  1.00 37.94           O  
ANISOU 3797  O   TYR A 485     5083   6356   2977   -212   -234   -124       O  
ATOM   3798  CB  TYR A 485      30.953 114.295 230.992  1.00 36.73           C  
ANISOU 3798  CB  TYR A 485     4982   6162   2810   -207    -19   -104       C  
ATOM   3799  CG  TYR A 485      29.750 115.131 230.788  1.00 36.46           C  
ANISOU 3799  CG  TYR A 485     4955   6106   2794   -220     85   -112       C  
ATOM   3800  CD1 TYR A 485      29.748 116.455 231.179  1.00 36.83           C  
ANISOU 3800  CD1 TYR A 485     5012   6123   2858   -252    118   -151       C  
ATOM   3801  CD2 TYR A 485      28.595 114.607 230.217  1.00 35.97           C  
ANISOU 3801  CD2 TYR A 485     4886   6047   2732   -199    149    -81       C  
ATOM   3802  CE1 TYR A 485      28.639 117.261 231.013  1.00 36.72           C  
ANISOU 3802  CE1 TYR A 485     5003   6082   2867   -252    217   -158       C  
ATOM   3803  CE2 TYR A 485      27.438 115.429 230.047  1.00 35.86           C  
ANISOU 3803  CE2 TYR A 485     4866   6016   2744   -204    244    -86       C  
ATOM   3804  CZ  TYR A 485      27.492 116.762 230.460  1.00 36.26           C  
ANISOU 3804  CZ  TYR A 485     4926   6034   2816   -225    278   -124       C  
ATOM   3805  OH  TYR A 485      26.437 117.612 230.364  1.00 36.32           O  
ANISOU 3805  OH  TYR A 485     4929   6016   2854   -219    369   -130       O  
ATOM   3806  N   GLY A 486      33.854 113.047 229.734  1.00 36.99           N  
ANISOU 3806  N   GLY A 486     4844   6263   2946   -129   -190    -68       N  
ATOM   3807  CA  GLY A 486      34.912 112.106 230.060  1.00 37.51           C  
ANISOU 3807  CA  GLY A 486     4899   6350   3005    -95   -289    -56       C  
ATOM   3808  C   GLY A 486      34.295 110.778 230.422  1.00 37.44           C  
ANISOU 3808  C   GLY A 486     4977   6323   2925    -65   -302    -28       C  
ATOM   3809  O   GLY A 486      34.993 109.795 230.731  1.00 37.91           O  
ANISOU 3809  O   GLY A 486     5049   6386   2969    -25   -383    -10       O  
ATOM   3810  N   ILE A 487      32.971 110.755 230.377  1.00 36.93           N  
ANISOU 3810  N   ILE A 487     4972   6237   2823    -84   -222    -23       N  
ATOM   3811  CA  ILE A 487      32.225 109.534 230.615  1.00 36.84           C  
ANISOU 3811  CA  ILE A 487     5045   6206   2748    -69   -217      4       C  
ATOM   3812  C   ILE A 487      32.354 108.523 229.446  1.00 36.48           C  
ANISOU 3812  C   ILE A 487     4956   6164   2742    -14   -210     34       C  
ATOM   3813  O   ILE A 487      32.392 108.892 228.295  1.00 36.02           O  
ANISOU 3813  O   ILE A 487     4816   6123   2749      0   -163     34       O  
ATOM   3814  CB  ILE A 487      30.758 109.832 231.033  1.00 36.60           C  
ANISOU 3814  CB  ILE A 487     5085   6155   2665   -115   -133     -2       C  
ATOM   3815  CG1 ILE A 487      30.768 110.509 232.415  1.00 37.22           C  
ANISOU 3815  CG1 ILE A 487     5240   6223   2680   -163   -152    -34       C  
ATOM   3816  CG2 ILE A 487      29.907 108.552 231.022  1.00 36.47           C  
ANISOU 3816  CG2 ILE A 487     5139   6122   2596   -108   -113     30       C  
ATOM   3817  CD1 ILE A 487      29.509 111.282 232.795  1.00 37.12           C  
ANISOU 3817  CD1 ILE A 487     5269   6194   2641   -206    -53    -56       C  
ATOM   3818  N   CYS A 488      32.456 107.245 229.797  1.00 36.80           N  
ANISOU 3818  N   CYS A 488     5063   6183   2736     16   -259     57       N  
ATOM   3819  CA  CYS A 488      32.732 106.184 228.856  1.00 36.69           C  
ANISOU 3819  CA  CYS A 488     5027   6161   2752     72   -263     80       C  
ATOM   3820  C   CYS A 488      31.471 105.367 228.802  1.00 36.41           C  
ANISOU 3820  C   CYS A 488     5079   6095   2659     50   -213     99       C  
ATOM   3821  O   CYS A 488      30.906 105.061 229.874  1.00 36.72           O  
ANISOU 3821  O   CYS A 488     5218   6112   2622     15   -224    106       O  
ATOM   3822  CB  CYS A 488      33.850 105.279 229.387  1.00 37.48           C  
ANISOU 3822  CB  CYS A 488     5147   6249   2844    128   -364     94       C  
ATOM   3823  SG  CYS A 488      35.360 106.105 230.000  1.00 38.22           S  
ANISOU 3823  SG  CYS A 488     5158   6381   2982    139   -459     75       S  
ATOM   3824  N   ILE A 489      31.019 105.031 227.581  1.00 35.91           N  
ANISOU 3824  N   ILE A 489     4983   6034   2629     61   -157    107       N  
ATOM   3825  CA  ILE A 489      30.014 103.960 227.430  1.00 35.83           C  
ANISOU 3825  CA  ILE A 489     5054   5991   2569     44   -128    128       C  
ATOM   3826  C   ILE A 489      30.703 102.619 227.414  1.00 36.34           C  
ANISOU 3826  C   ILE A 489     5172   6016   2620     99   -185    145       C  
ATOM   3827  O   ILE A 489      31.411 102.298 226.489  1.00 36.35           O  
ANISOU 3827  O   ILE A 489     5121   6020   2672    153   -190    141       O  
ATOM   3828  CB  ILE A 489      29.089 104.092 226.202  1.00 35.23           C  
ANISOU 3828  CB  ILE A 489     4936   5930   2518     20    -51    130       C  
ATOM   3829  CG1 ILE A 489      28.415 105.471 226.157  1.00 34.82           C  
ANISOU 3829  CG1 ILE A 489     4824   5913   2491    -22      5    118       C  
ATOM   3830  CG2 ILE A 489      28.035 102.928 226.205  1.00 35.31           C  
ANISOU 3830  CG2 ILE A 489     5038   5907   2471    -13    -30    150       C  
ATOM   3831  CD1 ILE A 489      27.680 105.887 227.504  1.00 35.04           C  
ANISOU 3831  CD1 ILE A 489     4913   5934   2466    -71     19    112       C  
ATOM   3832  N   GLU A 490      30.498 101.862 228.490  1.00 38.86           N  
ANISOU 3832  N   GLU A 490     5602   6296   2868     87   -225    164       N  
ATOM   3833  CA  GLU A 490      31.168 100.563 228.755  1.00 40.00           C  
ANISOU 3833  CA  GLU A 490     5819   6389   2990    145   -293    187       C  
ATOM   3834  C   GLU A 490      30.671  99.409 227.910  1.00 41.01           C  
ANISOU 3834  C   GLU A 490     5999   6471   3111    154   -259    199       C  
ATOM   3835  O   GLU A 490      29.498  99.355 227.564  1.00 40.93           O  
ANISOU 3835  O   GLU A 490     6015   6461   3076     90   -194    200       O  
ATOM   3836  CB  GLU A 490      30.987 100.242 230.212  1.00 39.47           C  
ANISOU 3836  CB  GLU A 490     5866   6292   2838    116   -342    208       C  
ATOM   3837  CG  GLU A 490      31.480 101.380 231.030  1.00 38.54           C  
ANISOU 3837  CG  GLU A 490     5707   6217   2719    100   -378    190       C  
ATOM   3838  CD  GLU A 490      32.993 101.486 231.012  1.00 39.19           C  
ANISOU 3838  CD  GLU A 490     5714   6316   2860    174   -467    187       C  
ATOM   3839  OE1 GLU A 490      33.589 100.987 230.029  1.00 40.46           O  
ANISOU 3839  OE1 GLU A 490     5814   6472   3086    240   -467    188       O  
ATOM   3840  OE2 GLU A 490      33.597 102.056 231.977  1.00 39.31           O  
ANISOU 3840  OE2 GLU A 490     5729   6352   2854    166   -535    182       O  
ATOM   3841  N   PRO A 491      31.565  98.482 227.546  1.00 43.10           N  
ANISOU 3841  N   PRO A 491     6278   6698   3402    233   -302    207       N  
ATOM   3842  CA  PRO A 491      31.017  97.264 226.909  1.00 43.79           C  
ANISOU 3842  CA  PRO A 491     6449   6725   3466    232   -272    216       C  
ATOM   3843  C   PRO A 491      30.666  96.294 228.052  1.00 44.76           C  
ANISOU 3843  C   PRO A 491     6720   6780   3507    213   -315    252       C  
ATOM   3844  O   PRO A 491      31.449  95.405 228.388  1.00 45.92           O  
ANISOU 3844  O   PRO A 491     6927   6871   3651    283   -380    272       O  
ATOM   3845  CB  PRO A 491      32.188  96.763 226.051  1.00 44.02           C  
ANISOU 3845  CB  PRO A 491     6428   6736   3561    334   -292    205       C  
ATOM   3846  CG  PRO A 491      33.493  97.271 226.836  1.00 44.84           C  
ANISOU 3846  CG  PRO A 491     6463   6870   3704    399   -375    209       C  
ATOM   3847  CD  PRO A 491      33.016  98.359 227.835  1.00 44.10           C  
ANISOU 3847  CD  PRO A 491     6362   6824   3572    323   -384    210       C  
ATOM   3848  N   GLU A 492      29.534  96.540 228.707  1.00 44.80           N  
ANISOU 3848  N   GLU A 492     6781   6793   3449    120   -280    261       N  
ATOM   3849  CA  GLU A 492      29.080  95.708 229.831  1.00 45.51           C  
ANISOU 3849  CA  GLU A 492     7018   6822   3450     82   -306    296       C  
ATOM   3850  C   GLU A 492      27.790  95.001 229.406  1.00 45.09           C  
ANISOU 3850  C   GLU A 492     7037   6736   3360      2   -236    303       C  
ATOM   3851  O   GLU A 492      27.236  95.281 228.327  1.00 44.42           O  
ANISOU 3851  O   GLU A 492     6880   6684   3314    -26   -176    280       O  
ATOM   3852  CB  GLU A 492      28.892  96.542 231.118  1.00 45.46           C  
ANISOU 3852  CB  GLU A 492     7029   6854   3392     34   -321    301       C  
ATOM   3853  CG  GLU A 492      27.733  97.539 231.059  1.00 45.35           C  
ANISOU 3853  CG  GLU A 492     6962   6897   3371    -54   -231    278       C  
ATOM   3854  CD  GLU A 492      27.892  98.738 231.975  1.00 47.55           C  
ANISOU 3854  CD  GLU A 492     7207   7226   3634    -75   -240    261       C  
ATOM   3855  OE1 GLU A 492      28.600  98.663 233.000  1.00 51.73           O  
ANISOU 3855  OE1 GLU A 492     7798   7740   4119    -53   -315    275       O  
ATOM   3856  OE2 GLU A 492      27.279  99.778 231.686  1.00 47.91           O  
ANISOU 3856  OE2 GLU A 492     7171   7323   3710   -114   -172    235       O  
ATOM   3857  N   PHE A 493      27.319  94.077 230.228  1.00 45.06           N  
ANISOU 3857  N   PHE A 493     7176   6667   3278    -39   -248    337       N  
ATOM   3858  CA  PHE A 493      26.086  93.422 229.888  1.00 44.99           C  
ANISOU 3858  CA  PHE A 493     7232   6629   3234   -128   -183    343       C  
ATOM   3859  C   PHE A 493      24.934  94.372 230.075  1.00 44.36           C  
ANISOU 3859  C   PHE A 493     7090   6622   3143   -224   -107    330       C  
ATOM   3860  O   PHE A 493      24.865  95.086 231.062  1.00 44.31           O  
ANISOU 3860  O   PHE A 493     7082   6649   3104   -244   -106    333       O  
ATOM   3861  CB  PHE A 493      25.824  92.173 230.724  1.00 45.42           C  
ANISOU 3861  CB  PHE A 493     7462   6590   3206   -160   -206    386       C  
ATOM   3862  CG  PHE A 493      24.543  91.510 230.372  1.00 46.00           C  
ANISOU 3862  CG  PHE A 493     7597   6635   3246   -266   -137    392       C  
ATOM   3863  CD1 PHE A 493      24.439  90.741 229.215  1.00 48.96           C  
ANISOU 3863  CD1 PHE A 493     7983   6966   3652   -261   -124    378       C  
ATOM   3864  CD2 PHE A 493      23.419  91.716 231.130  1.00 45.89           C  
ANISOU 3864  CD2 PHE A 493     7618   6645   3174   -375    -80    405       C  
ATOM   3865  CE1 PHE A 493      23.246  90.142 228.871  1.00 48.68           C  
ANISOU 3865  CE1 PHE A 493     8000   6909   3587   -370    -67    381       C  
ATOM   3866  CE2 PHE A 493      22.224  91.129 230.793  1.00 46.96           C  
ANISOU 3866  CE2 PHE A 493     7792   6763   3286   -481    -17    410       C  
ATOM   3867  CZ  PHE A 493      22.134  90.338 229.674  1.00 48.72           C  
ANISOU 3867  CZ  PHE A 493     8031   6942   3539   -482    -15    399       C  
ATOM   3868  N   ASN A 494      24.005  94.349 229.140  1.00 44.35           N  
ANISOU 3868  N   ASN A 494     7042   6643   3165   -282    -45    317       N  
ATOM   3869  CA  ASN A 494      22.790  95.093 229.324  1.00 44.53           C  
ANISOU 3869  CA  ASN A 494     7010   6728   3181   -372     29    310       C  
ATOM   3870  C   ASN A 494      21.592  94.465 228.578  1.00 44.65           C  
ANISOU 3870  C   ASN A 494     7035   6738   3193   -460     83    314       C  
ATOM   3871  O   ASN A 494      21.484  94.564 227.354  1.00 43.35           O  
ANISOU 3871  O   ASN A 494     6794   6597   3078   -453     92    295       O  
ATOM   3872  CB  ASN A 494      23.035  96.564 228.946  1.00 43.81           C  
ANISOU 3872  CB  ASN A 494     6769   6722   3157   -336     45    281       C  
ATOM   3873  CG  ASN A 494      21.779  97.367 228.958  1.00 45.29           C  
ANISOU 3873  CG  ASN A 494     6882   6971   3353   -412    124    274       C  
ATOM   3874  OD1 ASN A 494      21.014  97.329 229.927  1.00 50.40           O  
ANISOU 3874  OD1 ASN A 494     7583   7618   3948   -478    164    285       O  
ATOM   3875  ND2 ASN A 494      21.513  98.064 227.867  1.00 46.81           N  
ANISOU 3875  ND2 ASN A 494     6954   7217   3612   -405    149    257       N  
ATOM   3876  N   SER A 495      20.709  93.816 229.339  1.00 46.04           N  
ANISOU 3876  N   SER A 495     7308   6883   3304   -550    116    338       N  
ATOM   3877  CA  SER A 495      19.507  93.105 228.815  1.00 46.99           C  
ANISOU 3877  CA  SER A 495     7449   6994   3413   -654    164    346       C  
ATOM   3878  C   SER A 495      18.672  93.951 227.865  1.00 46.30           C  
ANISOU 3878  C   SER A 495     7208   6995   3388   -691    211    325       C  
ATOM   3879  O   SER A 495      18.007  93.451 226.958  1.00 46.30           O  
ANISOU 3879  O   SER A 495     7195   6996   3401   -749    223    322       O  
ATOM   3880  CB  SER A 495      18.616  92.611 229.984  1.00 48.25           C  
ANISOU 3880  CB  SER A 495     7709   7128   3496   -755    210    375       C  
ATOM   3881  OG  SER A 495      17.897  93.673 230.639  1.00 49.20           O  
ANISOU 3881  OG  SER A 495     7748   7327   3619   -796    276    369       O  
ATOM   3882  N   ARG A 496      18.733  95.251 228.091  1.00 46.03           N  
ANISOU 3882  N   ARG A 496     7065   7033   3391   -656    232    311       N  
ATOM   3883  CA  ARG A 496      17.953  96.205 227.362  1.00 46.24           C  
ANISOU 3883  CA  ARG A 496     6946   7145   3480   -680    275    298       C  
ATOM   3884  C   ARG A 496      18.125  96.102 225.845  1.00 45.60           C  
ANISOU 3884  C   ARG A 496     6804   7075   3445   -656    246    285       C  
ATOM   3885  O   ARG A 496      17.225  96.449 225.104  1.00 46.44           O  
ANISOU 3885  O   ARG A 496     6820   7239   3588   -705    273    285       O  
ATOM   3886  CB  ARG A 496      18.327  97.595 227.843  1.00 46.06           C  
ANISOU 3886  CB  ARG A 496     6838   7173   3489   -621    290    282       C  
ATOM   3887  CG  ARG A 496      17.132  98.353 228.409  1.00 50.24           C  
ANISOU 3887  CG  ARG A 496     7300   7761   4028   -683    371    283       C  
ATOM   3888  CD  ARG A 496      16.866  98.119 229.927  1.00 52.96           C  
ANISOU 3888  CD  ARG A 496     7746   8079   4297   -728    410    292       C  
ATOM   3889  NE  ARG A 496      17.584  99.065 230.792  1.00 56.38           N  
ANISOU 3889  NE  ARG A 496     8183   8520   4720   -670    405    274       N  
ATOM   3890  CZ  ARG A 496      18.379 100.080 230.399  1.00 58.17           C  
ANISOU 3890  CZ  ARG A 496     8329   8772   5001   -590    375    252       C  
ATOM   3891  NH1 ARG A 496      18.625 100.371 229.111  1.00 58.35           N  
ANISOU 3891  NH1 ARG A 496     8256   8819   5095   -548    348    246       N  
ATOM   3892  NH2 ARG A 496      18.959 100.830 231.328  1.00 59.39           N  
ANISOU 3892  NH2 ARG A 496     8506   8927   5133   -556    371    234       N  
ATOM   3893  N   PHE A 497      19.273  95.625 225.381  1.00 44.74           N  
ANISOU 3893  N   PHE A 497     6746   6916   3337   -582    191    275       N  
ATOM   3894  CA  PHE A 497      19.536  95.540 223.957  1.00 43.15           C  
ANISOU 3894  CA  PHE A 497     6501   6724   3171   -556    170    259       C  
ATOM   3895  C   PHE A 497      19.165  94.182 223.321  1.00 42.82           C  
ANISOU 3895  C   PHE A 497     6556   6621   3092   -614    159    259       C  
ATOM   3896  O   PHE A 497      19.209  94.015 222.077  1.00 41.76           O  
ANISOU 3896  O   PHE A 497     6399   6494   2975   -612    147    243       O  
ATOM   3897  CB  PHE A 497      20.977  96.000 223.640  1.00 43.31           C  
ANISOU 3897  CB  PHE A 497     6490   6738   3226   -439    132    241       C  
ATOM   3898  CG  PHE A 497      22.088  95.076 224.139  1.00 45.40           C  
ANISOU 3898  CG  PHE A 497     6869   6919   3462   -374     86    242       C  
ATOM   3899  CD1 PHE A 497      22.090  93.705 223.863  1.00 48.24           C  
ANISOU 3899  CD1 PHE A 497     7347   7196   3784   -391     70    245       C  
ATOM   3900  CD2 PHE A 497      23.187  95.613 224.828  1.00 47.88           C  
ANISOU 3900  CD2 PHE A 497     7165   7235   3793   -290     53    240       C  
ATOM   3901  CE1 PHE A 497      23.156  92.861 224.315  1.00 50.99           C  
ANISOU 3901  CE1 PHE A 497     7798   7460   4114   -315     24    250       C  
ATOM   3902  CE2 PHE A 497      24.250  94.792 225.290  1.00 49.53           C  
ANISOU 3902  CE2 PHE A 497     7465   7371   3984   -219      0    247       C  
ATOM   3903  CZ  PHE A 497      24.237  93.411 225.023  1.00 51.10           C  
ANISOU 3903  CZ  PHE A 497     7784   7484   4150   -225    -14    254       C  
ATOM   3904  N   LEU A 498      18.769  93.225 224.169  1.00 42.19           N  
ANISOU 3904  N   LEU A 498     6593   6480   2958   -674    165    278       N  
ATOM   3905  CA  LEU A 498      18.399  91.900 223.676  1.00 42.08           C  
ANISOU 3905  CA  LEU A 498     6689   6395   2906   -739    156    278       C  
ATOM   3906  C   LEU A 498      17.248  91.942 222.656  1.00 41.97           C  
ANISOU 3906  C   LEU A 498     6603   6436   2905   -837    175    271       C  
ATOM   3907  O   LEU A 498      17.333  91.281 221.618  1.00 42.63           O  
ANISOU 3907  O   LEU A 498     6730   6486   2980   -851    153    253       O  
ATOM   3908  CB  LEU A 498      18.104  90.919 224.801  1.00 42.27           C  
ANISOU 3908  CB  LEU A 498     6853   6340   2866   -798    163    305       C  
ATOM   3909  CG  LEU A 498      19.305  90.304 225.523  1.00 42.76           C  
ANISOU 3909  CG  LEU A 498     7039   6310   2898   -706    119    316       C  
ATOM   3910  CD1 LEU A 498      18.960  90.025 226.994  1.00 43.42           C  
ANISOU 3910  CD1 LEU A 498     7215   6362   2922   -756    135    352       C  
ATOM   3911  CD2 LEU A 498      19.837  89.043 224.854  1.00 41.98           C  
ANISOU 3911  CD2 LEU A 498     7063   6105   2782   -681     86    306       C  
ATOM   3912  N   PRO A 499      16.197  92.741 222.913  1.00 41.17           N  
ANISOU 3912  N   PRO A 499     6392   6422   2828   -901    215    285       N  
ATOM   3913  CA  PRO A 499      15.208  92.779 221.867  1.00 41.38           C  
ANISOU 3913  CA  PRO A 499     6343   6505   2874   -983    217    282       C  
ATOM   3914  C   PRO A 499      15.768  93.091 220.457  1.00 40.99           C  
ANISOU 3914  C   PRO A 499     6247   6478   2851   -925    180    258       C  
ATOM   3915  O   PRO A 499      15.173  92.627 219.474  1.00 41.89           O  
ANISOU 3915  O   PRO A 499     6364   6601   2953   -997    162    250       O  
ATOM   3916  CB  PRO A 499      14.238  93.865 222.341  1.00 41.34           C  
ANISOU 3916  CB  PRO A 499     6198   6599   2912  -1018    263    300       C  
ATOM   3917  CG  PRO A 499      14.357  93.856 223.784  1.00 40.74           C  
ANISOU 3917  CG  PRO A 499     6178   6493   2808  -1011    299    312       C  
ATOM   3918  CD  PRO A 499      15.801  93.593 224.048  1.00 41.15           C  
ANISOU 3918  CD  PRO A 499     6328   6470   2836   -906    259    301       C  
ATOM   3919  N   TYR A 500      16.881  93.828 220.341  1.00 39.49           N  
ANISOU 3919  N   TYR A 500     6019   6295   2689   -806    168    246       N  
ATOM   3920  CA  TYR A 500      17.428  94.138 219.009  1.00 38.63           C  
ANISOU 3920  CA  TYR A 500     5870   6208   2599   -756    144    225       C  
ATOM   3921  C   TYR A 500      18.257  93.004 218.485  1.00 38.89           C  
ANISOU 3921  C   TYR A 500     6033   6149   2594   -726    120    199       C  
ATOM   3922  O   TYR A 500      18.157  92.633 217.334  1.00 39.13           O  
ANISOU 3922  O   TYR A 500     6084   6176   2607   -752    107    179       O  
ATOM   3923  CB  TYR A 500      18.354  95.346 219.040  1.00 37.96           C  
ANISOU 3923  CB  TYR A 500     5696   6164   2563   -646    146    221       C  
ATOM   3924  CG  TYR A 500      17.708  96.674 219.347  1.00 37.07           C  
ANISOU 3924  CG  TYR A 500     5448   6140   2499   -652    171    241       C  
ATOM   3925  CD1 TYR A 500      16.612  97.129 218.607  1.00 36.86           C  
ANISOU 3925  CD1 TYR A 500     5329   6184   2492   -716    174    256       C  
ATOM   3926  CD2 TYR A 500      18.229  97.504 220.353  1.00 36.35           C  
ANISOU 3926  CD2 TYR A 500     5321   6057   2433   -589    188    244       C  
ATOM   3927  CE1 TYR A 500      16.049  98.356 218.873  1.00 36.58           C  
ANISOU 3927  CE1 TYR A 500     5170   6221   2509   -707    199    275       C  
ATOM   3928  CE2 TYR A 500      17.655  98.725 220.630  1.00 36.06           C  
ANISOU 3928  CE2 TYR A 500     5171   6090   2442   -589    218    257       C  
ATOM   3929  CZ  TYR A 500      16.574  99.142 219.887  1.00 36.18           C  
ANISOU 3929  CZ  TYR A 500     5095   6169   2483   -643    226    273       C  
ATOM   3930  OH  TYR A 500      16.005 100.354 220.154  1.00 36.01           O  
ANISOU 3930  OH  TYR A 500     4960   6208   2513   -632    257    288       O  
ATOM   3931  N   VAL A 501      19.125  92.477 219.332  1.00 38.96           N  
ANISOU 3931  N   VAL A 501     6132   6082   2590   -662    115    198       N  
ATOM   3932  CA  VAL A 501      20.063  91.477 218.888  1.00 39.01           C  
ANISOU 3932  CA  VAL A 501     6253   5995   2573   -606     97    172       C  
ATOM   3933  C   VAL A 501      19.342  90.151 218.666  1.00 40.48           C  
ANISOU 3933  C   VAL A 501     6569   6106   2705   -706     94    167       C  
ATOM   3934  O   VAL A 501      19.707  89.367 217.782  1.00 40.59           O  
ANISOU 3934  O   VAL A 501     6668   6059   2696   -696     85    136       O  
ATOM   3935  CB  VAL A 501      21.198  91.355 219.873  1.00 38.85           C  
ANISOU 3935  CB  VAL A 501     6279   5920   2562   -502     83    179       C  
ATOM   3936  CG1 VAL A 501      22.024  90.178 219.549  1.00 39.50           C  
ANISOU 3936  CG1 VAL A 501     6490   5895   2624   -446     66    159       C  
ATOM   3937  CG2 VAL A 501      22.041  92.603 219.826  1.00 38.08           C  
ANISOU 3937  CG2 VAL A 501     6057   5892   2520   -407     82    174       C  
ATOM   3938  N   ASP A 502      18.281  89.933 219.437  1.00 41.39           N  
ANISOU 3938  N   ASP A 502     6699   6228   2799   -810    106    195       N  
ATOM   3939  CA  ASP A 502      17.435  88.759 219.258  1.00 42.86           C  
ANISOU 3939  CA  ASP A 502     6996   6352   2936   -930    106    193       C  
ATOM   3940  C   ASP A 502      16.731  88.710 217.903  1.00 43.00           C  
ANISOU 3940  C   ASP A 502     6979   6415   2946  -1012     95    170       C  
ATOM   3941  O   ASP A 502      16.239  87.656 217.518  1.00 44.48           O  
ANISOU 3941  O   ASP A 502     7273   6538   3089  -1104     87    157       O  
ATOM   3942  CB  ASP A 502      16.408  88.670 220.386  1.00 43.41           C  
ANISOU 3942  CB  ASP A 502     7066   6436   2990  -1031    131    230       C  
ATOM   3943  CG  ASP A 502      17.005  88.141 221.692  1.00 45.12           C  
ANISOU 3943  CG  ASP A 502     7398   6567   3179   -985    134    253       C  
ATOM   3944  OD1 ASP A 502      18.148  87.615 221.639  1.00 45.12           O  
ANISOU 3944  OD1 ASP A 502     7491   6481   3172   -884    107    240       O  
ATOM   3945  OD2 ASP A 502      16.316  88.230 222.756  1.00 46.55           O  
ANISOU 3945  OD2 ASP A 502     7579   6765   3344  -1052    163    284       O  
ATOM   3946  N   ARG A 503      16.687  89.834 217.186  1.00 42.39           N  
ANISOU 3946  N   ARG A 503     6760   6440   2907   -982     91    167       N  
ATOM   3947  CA  ARG A 503      16.026  89.923 215.848  1.00 42.74           C  
ANISOU 3947  CA  ARG A 503     6761   6539   2939  -1055     71    151       C  
ATOM   3948  C   ARG A 503      17.002  90.106 214.651  1.00 42.43           C  
ANISOU 3948  C   ARG A 503     6733   6495   2895   -968     60    115       C  
ATOM   3949  O   ARG A 503      16.650  90.602 213.561  1.00 41.40           O  
ANISOU 3949  O   ARG A 503     6537   6434   2760   -999     42    108       O  
ATOM   3950  CB  ARG A 503      14.942  91.010 215.840  1.00 42.36           C  
ANISOU 3950  CB  ARG A 503     6545   6618   2931  -1113     71    183       C  
ATOM   3951  CG  ARG A 503      13.820  90.762 216.830  1.00 43.34           C  
ANISOU 3951  CG  ARG A 503     6652   6756   3058  -1219     92    213       C  
ATOM   3952  CD  ARG A 503      12.852  91.927 216.869  1.00 43.37           C  
ANISOU 3952  CD  ARG A 503     6476   6887   3117  -1250    101    244       C  
ATOM   3953  NE  ARG A 503      11.545  91.487 217.308  1.00 44.46           N  
ANISOU 3953  NE  ARG A 503     6592   7049   3252  -1387    115    265       N  
ATOM   3954  CZ  ARG A 503      11.211  91.293 218.573  1.00 45.96           C  
ANISOU 3954  CZ  ARG A 503     6801   7219   3443  -1418    162    284       C  
ATOM   3955  NH1 ARG A 503      12.105  91.521 219.532  1.00 46.51           N  
ANISOU 3955  NH1 ARG A 503     6916   7243   3511  -1319    189    285       N  
ATOM   3956  NH2 ARG A 503       9.984  90.871 218.871  1.00 46.34           N  
ANISOU 3956  NH2 ARG A 503     6821   7295   3489  -1553    180    302       N  
ATOM   3957  N   GLY A 504      18.236  89.692 214.890  1.00 42.95           N  
ANISOU 3957  N   GLY A 504     6882   6477   2959   -860     71     94       N  
ATOM   3958  CA  GLY A 504      19.248  89.658 213.871  1.00 43.88           C  
ANISOU 3958  CA  GLY A 504     7029   6572   3071   -775     76     55       C  
ATOM   3959  C   GLY A 504      19.996  90.961 213.694  1.00 43.83           C  
ANISOU 3959  C   GLY A 504     6890   6645   3117   -671     87     62       C  
ATOM   3960  O   GLY A 504      20.728  91.093 212.710  1.00 44.26           O  
ANISOU 3960  O   GLY A 504     6949   6701   3166   -614     98     33       O  
ATOM   3961  N   MET A 505      19.822  91.915 214.624  1.00 43.19           N  
ANISOU 3961  N   MET A 505     6700   6627   3084   -652     90     99       N  
ATOM   3962  CA  MET A 505      20.505  93.208 214.544  1.00 42.17           C  
ANISOU 3962  CA  MET A 505     6447   6568   3007   -562    101    107       C  
ATOM   3963  C   MET A 505      21.870  93.179 215.173  1.00 41.95           C  
ANISOU 3963  C   MET A 505     6439   6491   3009   -441    110     97       C  
ATOM   3964  O   MET A 505      22.166  92.331 216.012  1.00 42.80           O  
ANISOU 3964  O   MET A 505     6639   6520   3105   -421    103     97       O  
ATOM   3965  CB  MET A 505      19.729  94.272 215.264  1.00 41.81           C  
ANISOU 3965  CB  MET A 505     6281   6604   3001   -593    103    146       C  
ATOM   3966  CG  MET A 505      18.455  94.664 214.583  1.00 42.91           C  
ANISOU 3966  CG  MET A 505     6351   6818   3134   -691     91    164       C  
ATOM   3967  SD  MET A 505      17.915  96.163 215.423  1.00 43.54           S  
ANISOU 3967  SD  MET A 505     6274   6988   3280   -677    108    204       S  
ATOM   3968  CE  MET A 505      18.966  97.350 214.580  1.00 46.00           C  
ANISOU 3968  CE  MET A 505     6506   7341   3629   -575    113    198       C  
ATOM   3969  N   ILE A 506      22.702  94.128 214.767  1.00 41.00           N  
ANISOU 3969  N   ILE A 506     6230   6419   2930   -361    122     91       N  
ATOM   3970  CA  ILE A 506      23.998  94.344 215.392  1.00 39.94           C  
ANISOU 3970  CA  ILE A 506     6077   6261   2838   -248    125     86       C  
ATOM   3971  C   ILE A 506      23.937  95.579 216.302  1.00 38.38           C  
ANISOU 3971  C   ILE A 506     5767   6129   2686   -234    122    115       C  
ATOM   3972  O   ILE A 506      23.676  96.695 215.847  1.00 38.50           O  
ANISOU 3972  O   ILE A 506     5681   6220   2728   -245    133    125       O  
ATOM   3973  CB  ILE A 506      25.076  94.540 214.329  1.00 39.98           C  
ANISOU 3973  CB  ILE A 506     6059   6272   2860   -170    149     55       C  
ATOM   3974  CG1 ILE A 506      25.317  93.228 213.587  1.00 41.14           C  
ANISOU 3974  CG1 ILE A 506     6334   6335   2961   -165    161     18       C  
ATOM   3975  CG2 ILE A 506      26.363  95.083 214.958  1.00 40.39           C  
ANISOU 3975  CG2 ILE A 506     6045   6329   2973    -61    150     55       C  
ATOM   3976  CD1 ILE A 506      26.148  93.382 212.305  1.00 41.63           C  
ANISOU 3976  CD1 ILE A 506     6383   6410   3025   -111    200    -18       C  
ATOM   3977  N   TYR A 507      24.162  95.381 217.584  1.00 36.78           N  
ANISOU 3977  N   TYR A 507     5593   5893   2489   -211    105    129       N  
ATOM   3978  CA  TYR A 507      24.203  96.508 218.491  1.00 36.07           C  
ANISOU 3978  CA  TYR A 507     5414   5856   2436   -196    103    148       C  
ATOM   3979  C   TYR A 507      25.671  96.945 218.676  1.00 35.96           C  
ANISOU 3979  C   TYR A 507     5356   5840   2466    -89     92    136       C  
ATOM   3980  O   TYR A 507      26.571  96.097 218.778  1.00 36.43           O  
ANISOU 3980  O   TYR A 507     5479   5839   2525    -25     74    123       O  
ATOM   3981  CB  TYR A 507      23.551  96.138 219.820  1.00 36.27           C  
ANISOU 3981  CB  TYR A 507     5496   5855   2431   -243     93    171       C  
ATOM   3982  CG  TYR A 507      23.428  97.298 220.758  1.00 37.39           C  
ANISOU 3982  CG  TYR A 507     5558   6049   2599   -241    100    185       C  
ATOM   3983  CD1 TYR A 507      22.296  98.104 220.732  1.00 38.94           C  
ANISOU 3983  CD1 TYR A 507     5682   6307   2806   -306    130    199       C  
ATOM   3984  CD2 TYR A 507      24.434  97.595 221.682  1.00 37.30           C  
ANISOU 3984  CD2 TYR A 507     5546   6024   2604   -172     75    185       C  
ATOM   3985  CE1 TYR A 507      22.163  99.170 221.607  1.00 39.54           C  
ANISOU 3985  CE1 TYR A 507     5694   6422   2905   -301    145    207       C  
ATOM   3986  CE2 TYR A 507      24.315  98.666 222.541  1.00 36.53           C  
ANISOU 3986  CE2 TYR A 507     5387   5969   2522   -177     82    192       C  
ATOM   3987  CZ  TYR A 507      23.179  99.437 222.505  1.00 39.63           C  
ANISOU 3987  CZ  TYR A 507     5719   6415   2923   -240    122    201       C  
ATOM   3988  OH  TYR A 507      23.031 100.510 223.355  1.00 44.74           O  
ANISOU 3988  OH  TYR A 507     6315   7097   3587   -242    139    202       O  
ATOM   3989  N   ALA A 508      25.903  98.259 218.719  1.00 35.43           N  
ANISOU 3989  N   ALA A 508     5179   5839   2445    -72    102    140       N  
ATOM   3990  CA  ALA A 508      27.235  98.816 218.493  1.00 35.36           C  
ANISOU 3990  CA  ALA A 508     5104   5845   2485     12    100    125       C  
ATOM   3991  C   ALA A 508      27.392 100.094 219.278  1.00 34.94           C  
ANISOU 3991  C   ALA A 508     4966   5840   2470     17     95    136       C  
ATOM   3992  O   ALA A 508      26.528 100.968 219.214  1.00 34.55           O  
ANISOU 3992  O   ALA A 508     4866   5835   2426    -34    116    148       O  
ATOM   3993  CB  ALA A 508      27.435  99.098 216.983  1.00 35.29           C  
ANISOU 3993  CB  ALA A 508     5052   5866   2489     19    135    110       C  
ATOM   3994  N   ILE A 509      28.482 100.205 220.025  1.00 35.12           N  
ANISOU 3994  N   ILE A 509     4973   5851   2520     79     63    130       N  
ATOM   3995  CA  ILE A 509      28.778 101.454 220.724  1.00 34.83           C  
ANISOU 3995  CA  ILE A 509     4859   5856   2518     81     56    132       C  
ATOM   3996  C   ILE A 509      29.939 102.220 220.048  1.00 34.79           C  
ANISOU 3996  C   ILE A 509     4758   5885   2575    133     65    117       C  
ATOM   3997  O   ILE A 509      31.061 101.706 219.960  1.00 35.23           O  
ANISOU 3997  O   ILE A 509     4807   5923   2655    199     44    105       O  
ATOM   3998  CB  ILE A 509      29.086 101.256 222.256  1.00 35.14           C  
ANISOU 3998  CB  ILE A 509     4945   5869   2537     93      5    139       C  
ATOM   3999  CG1 ILE A 509      27.958 100.516 222.978  1.00 35.28           C  
ANISOU 3999  CG1 ILE A 509     5063   5852   2489     35      6    156       C  
ATOM   4000  CG2 ILE A 509      29.341 102.597 222.908  1.00 34.90           C  
ANISOU 4000  CG2 ILE A 509     4844   5881   2538     85      1    135       C  
ATOM   4001  CD1 ILE A 509      28.436  99.671 224.154  1.00 35.88           C  
ANISOU 4001  CD1 ILE A 509     5230   5875   2527     61    -50    168       C  
ATOM   4002  N   ALA A 510      29.672 103.437 219.563  1.00 34.37           N  
ANISOU 4002  N   ALA A 510     4627   5879   2551    104     99    120       N  
ATOM   4003  CA  ALA A 510      30.737 104.279 219.019  1.00 34.39           C  
ANISOU 4003  CA  ALA A 510     4540   5914   2612    139    113    109       C  
ATOM   4004  C   ALA A 510      31.461 104.944 220.193  1.00 34.52           C  
ANISOU 4004  C   ALA A 510     4519   5938   2659    153     73    103       C  
ATOM   4005  O   ALA A 510      30.823 105.585 221.005  1.00 34.30           O  
ANISOU 4005  O   ALA A 510     4499   5915   2618    113     68    109       O  
ATOM   4006  CB  ALA A 510      30.149 105.304 218.106  1.00 34.00           C  
ANISOU 4006  CB  ALA A 510     4438   5903   2577    100    159    120       C  
ATOM   4007  N   HIS A 511      32.781 104.768 220.290  1.00 34.98           N  
ANISOU 4007  N   HIS A 511     4536   5998   2757    210     44     90       N  
ATOM   4008  CA  HIS A 511      33.566 105.332 221.418  1.00 35.27           C  
ANISOU 4008  CA  HIS A 511     4536   6045   2819    219     -9     83       C  
ATOM   4009  C   HIS A 511      34.179 106.715 221.108  1.00 35.20           C  
ANISOU 4009  C   HIS A 511     4425   6079   2872    202     13     73       C  
ATOM   4010  O   HIS A 511      35.396 106.917 221.179  1.00 35.69           O  
ANISOU 4010  O   HIS A 511     4415   6160   2985    234    -13     62       O  
ATOM   4011  CB  HIS A 511      34.622 104.335 221.925  1.00 35.98           C  
ANISOU 4011  CB  HIS A 511     4638   6113   2920    288    -71     80       C  
ATOM   4012  CG  HIS A 511      34.037 103.071 222.488  1.00 36.16           C  
ANISOU 4012  CG  HIS A 511     4777   6082   2879    299   -101     94       C  
ATOM   4013  ND1 HIS A 511      33.421 103.019 223.721  1.00 36.16           N  
ANISOU 4013  ND1 HIS A 511     4851   6062   2824    261   -140    106       N  
ATOM   4014  CD2 HIS A 511      33.975 101.810 221.985  1.00 36.43           C  
ANISOU 4014  CD2 HIS A 511     4875   6073   2893    337    -94     97       C  
ATOM   4015  CE1 HIS A 511      32.994 101.785 223.940  1.00 36.40           C  
ANISOU 4015  CE1 HIS A 511     4985   6042   2805    273   -156    120       C  
ATOM   4016  NE2 HIS A 511      33.327 101.030 222.910  1.00 36.58           N  
ANISOU 4016  NE2 HIS A 511     5003   6045   2849    320   -131    114       N  
ATOM   4017  N   VAL A 512      33.323 107.678 220.796  1.00 34.70           N  
ANISOU 4017  N   VAL A 512     4352   6028   2805    149     58     80       N  
ATOM   4018  CA  VAL A 512      33.811 108.949 220.312  1.00 34.68           C  
ANISOU 4018  CA  VAL A 512     4266   6054   2857    129     90     76       C  
ATOM   4019  C   VAL A 512      34.576 109.778 221.328  1.00 35.02           C  
ANISOU 4019  C   VAL A 512     4269   6106   2932    115     46     59       C  
ATOM   4020  O   VAL A 512      34.425 109.631 222.526  1.00 35.16           O  
ANISOU 4020  O   VAL A 512     4334   6107   2917    106     -4     53       O  
ATOM   4021  CB  VAL A 512      32.700 109.773 219.655  1.00 34.18           C  
ANISOU 4021  CB  VAL A 512     4206   5994   2785     85    147     93       C  
ATOM   4022  CG1 VAL A 512      32.155 109.017 218.489  1.00 34.00           C  
ANISOU 4022  CG1 VAL A 512     4211   5974   2735     94    182    108       C  
ATOM   4023  CG2 VAL A 512      31.596 110.106 220.654  1.00 33.92           C  
ANISOU 4023  CG2 VAL A 512     4227   5944   2719     49    139     97       C  
ATOM   4024  N   ARG A 513      35.416 110.654 220.814  1.00 35.25           N  
ANISOU 4024  N   ARG A 513     4212   6159   3020    105     66     52       N  
ATOM   4025  CA  ARG A 513      36.141 111.591 221.630  1.00 35.64           C  
ANISOU 4025  CA  ARG A 513     4218   6218   3105     76     29     34       C  
ATOM   4026  C   ARG A 513      35.115 112.509 222.271  1.00 35.29           C  
ANISOU 4026  C   ARG A 513     4227   6150   3032     23     44     33       C  
ATOM   4027  O   ARG A 513      34.092 112.799 221.663  1.00 34.81           O  
ANISOU 4027  O   ARG A 513     4190   6078   2957      9    101     50       O  
ATOM   4028  CB  ARG A 513      37.147 112.366 220.773  1.00 35.99           C  
ANISOU 4028  CB  ARG A 513     4160   6293   3221     65     64     30       C  
ATOM   4029  CG  ARG A 513      38.433 111.596 220.476  1.00 36.63           C  
ANISOU 4029  CG  ARG A 513     4168   6404   3346    119     41     22       C  
ATOM   4030  CD  ARG A 513      39.353 112.425 219.635  1.00 37.04           C  
ANISOU 4030  CD  ARG A 513     4117   6490   3468     97     89     18       C  
ATOM   4031  NE  ARG A 513      38.974 112.297 218.235  1.00 36.74           N  
ANISOU 4031  NE  ARG A 513     4084   6453   3421    106    175     35       N  
ATOM   4032  CZ  ARG A 513      39.669 112.759 217.191  1.00 37.10           C  
ANISOU 4032  CZ  ARG A 513     4057   6527   3513     96    240     37       C  
ATOM   4033  NH1 ARG A 513      40.796 113.437 217.379  1.00 37.79           N  
ANISOU 4033  NH1 ARG A 513     4046   6644   3669     70    231     24       N  
ATOM   4034  NH2 ARG A 513      39.216 112.545 215.958  1.00 36.85           N  
ANISOU 4034  NH2 ARG A 513     4053   6496   3454    103    313     54       N  
ATOM   4035  N   GLY A 514      35.421 112.974 223.482  1.00 35.66           N  
ANISOU 4035  N   GLY A 514     4288   6188   3071     -4     -8     11       N  
ATOM   4036  CA  GLY A 514      34.445 113.530 224.398  1.00 35.49           C  
ANISOU 4036  CA  GLY A 514     4341   6138   3006    -43     -1      1       C  
ATOM   4037  C   GLY A 514      34.254 112.510 225.505  1.00 35.67           C  
ANISOU 4037  C   GLY A 514     4442   6149   2962    -28    -60     -2       C  
ATOM   4038  O   GLY A 514      34.089 112.872 226.677  1.00 35.96           O  
ANISOU 4038  O   GLY A 514     4534   6170   2959    -60    -90    -22       O  
ATOM   4039  N   GLY A 515      34.278 111.230 225.104  1.00 35.58           N  
ANISOU 4039  N   GLY A 515     4443   6142   2933     20    -74     18       N  
ATOM   4040  CA  GLY A 515      34.363 110.121 226.003  1.00 35.90           C  
ANISOU 4040  CA  GLY A 515     4553   6169   2919     44   -139     22       C  
ATOM   4041  C   GLY A 515      35.757 110.091 226.610  1.00 36.67           C  
ANISOU 4041  C   GLY A 515     4606   6286   3043     62   -226     10       C  
ATOM   4042  O   GLY A 515      36.609 110.932 226.289  1.00 36.93           O  
ANISOU 4042  O   GLY A 515     4548   6344   3139     49   -229     -5       O  
ATOM   4043  N   GLY A 516      36.005 109.114 227.487  1.00 37.15           N  
ANISOU 4043  N   GLY A 516     4727   6333   3056     90   -301     19       N  
ATOM   4044  CA  GLY A 516      37.285 108.949 228.151  1.00 38.03           C  
ANISOU 4044  CA  GLY A 516     4799   6464   3188    114   -402     15       C  
ATOM   4045  C   GLY A 516      37.739 107.527 227.974  1.00 38.39           C  
ANISOU 4045  C   GLY A 516     4855   6499   3235    194   -446     40       C  
ATOM   4046  O   GLY A 516      38.611 107.039 228.708  1.00 39.24           O  
ANISOU 4046  O   GLY A 516     4957   6611   3340    228   -544     49       O  
ATOM   4047  N   GLU A 517      37.148 106.844 226.997  1.00 37.86           N  
ANISOU 4047  N   GLU A 517     4804   6412   3168    224   -376     53       N  
ATOM   4048  CA  GLU A 517      37.460 105.432 226.793  1.00 38.23           C  
ANISOU 4048  CA  GLU A 517     4881   6433   3212    300   -406     75       C  
ATOM   4049  C   GLU A 517      38.971 105.214 226.650  1.00 39.10           C  
ANISOU 4049  C   GLU A 517     4885   6572   3400    369   -467     73       C  
ATOM   4050  O   GLU A 517      39.541 104.420 227.388  1.00 39.89           O  
ANISOU 4050  O   GLU A 517     5012   6656   3487    420   -556     91       O  
ATOM   4051  CB  GLU A 517      36.644 104.853 225.650  1.00 37.59           C  
ANISOU 4051  CB  GLU A 517     4830   6329   3124    312   -318     80       C  
ATOM   4052  CG  GLU A 517      35.154 104.654 225.984  1.00 37.02           C  
ANISOU 4052  CG  GLU A 517     4872   6223   2969    256   -280     91       C  
ATOM   4053  CD  GLU A 517      34.168 105.756 225.504  1.00 36.23           C  
ANISOU 4053  CD  GLU A 517     4751   6144   2871    188   -198     80       C  
ATOM   4054  OE1 GLU A 517      34.562 106.910 225.137  1.00 37.04           O  
ANISOU 4054  OE1 GLU A 517     4767   6281   3027    168   -175     65       O  
ATOM   4055  OE2 GLU A 517      32.950 105.434 225.508  1.00 35.83           O  
ANISOU 4055  OE2 GLU A 517     4775   6071   2768    154   -157     91       O  
ATOM   4056  N   MET A 518      39.625 106.003 225.803  1.00 39.08           N  
ANISOU 4056  N   MET A 518     4758   6614   3477    365   -424     55       N  
ATOM   4057  CA  MET A 518      41.060 105.870 225.529  1.00 39.98           C  
ANISOU 4057  CA  MET A 518     4745   6765   3679    426   -464     51       C  
ATOM   4058  C   MET A 518      42.002 106.674 226.427  1.00 40.74           C  
ANISOU 4058  C   MET A 518     4764   6905   3810    396   -555     41       C  
ATOM   4059  O   MET A 518      43.134 106.991 226.008  1.00 41.40           O  
ANISOU 4059  O   MET A 518     4709   7036   3983    418   -563     31       O  
ATOM   4060  CB  MET A 518      41.384 106.273 224.071  1.00 39.74           C  
ANISOU 4060  CB  MET A 518     4613   6765   3722    434   -362     35       C  
ATOM   4061  CG  MET A 518      40.697 105.489 222.966  1.00 39.21           C  
ANISOU 4061  CG  MET A 518     4601   6665   3632    467   -273     39       C  
ATOM   4062  SD  MET A 518      40.716 103.715 223.235  1.00 39.73           S  
ANISOU 4062  SD  MET A 518     4760   6672   3666    564   -319     58       S  
ATOM   4063  CE  MET A 518      42.479 103.347 223.297  1.00 41.12           C  
ANISOU 4063  CE  MET A 518     4796   6882   3946    664   -381     55       C  
ATOM   4064  N   GLY A 519      41.559 107.039 227.629  1.00 40.75           N  
ANISOU 4064  N   GLY A 519     4850   6894   3740    339   -618     41       N  
ATOM   4065  CA  GLY A 519      42.381 107.894 228.497  1.00 41.52           C  
ANISOU 4065  CA  GLY A 519     4887   7031   3857    292   -706     27       C  
ATOM   4066  C   GLY A 519      41.844 109.304 228.663  1.00 41.00           C  
ANISOU 4066  C   GLY A 519     4835   6970   3772    187   -660     -2       C  
ATOM   4067  O   GLY A 519      41.061 109.779 227.899  1.00 40.12           O  
ANISOU 4067  O   GLY A 519     4738   6845   3662    158   -555    -10       O  
ATOM   4068  N   ARG A 520      42.296 110.000 229.678  1.00 41.66           N  
ANISOU 4068  N   ARG A 520     4917   7072   3840    130   -744    -19       N  
ATOM   4069  CA  ARG A 520      41.766 111.324 229.936  1.00 41.30           C  
ANISOU 4069  CA  ARG A 520     4904   7018   3771     32   -700    -51       C  
ATOM   4070  C   ARG A 520      41.860 112.217 228.710  1.00 40.83           C  
ANISOU 4070  C   ARG A 520     4746   6974   3794      6   -597    -64       C  
ATOM   4071  O   ARG A 520      40.995 113.090 228.533  1.00 40.17           O  
ANISOU 4071  O   ARG A 520     4711   6862   3689    -51   -518    -79       O  
ATOM   4072  CB  ARG A 520      42.489 111.979 231.110  1.00 42.32           C  
ANISOU 4072  CB  ARG A 520     5029   7169   3882    -30   -813    -73       C  
ATOM   4073  CG  ARG A 520      42.005 113.379 231.448  1.00 42.12           C  
ANISOU 4073  CG  ARG A 520     5048   7125   3832   -133   -769   -114       C  
ATOM   4074  CD  ARG A 520      40.764 113.328 232.318  1.00 41.71           C  
ANISOU 4074  CD  ARG A 520     5164   7022   3662   -162   -748   -120       C  
ATOM   4075  NE  ARG A 520      40.362 114.660 232.764  1.00 41.74           N  
ANISOU 4075  NE  ARG A 520     5216   7001   3641   -253   -710   -164       N  
ATOM   4076  CZ  ARG A 520      39.131 115.023 233.130  1.00 41.21           C  
ANISOU 4076  CZ  ARG A 520     5268   6886   3503   -284   -634   -180       C  
ATOM   4077  NH1 ARG A 520      38.128 114.148 233.117  1.00 40.58           N  
ANISOU 4077  NH1 ARG A 520     5268   6783   3367   -240   -588   -154       N  
ATOM   4078  NH2 ARG A 520      38.914 116.287 233.513  1.00 41.42           N  
ANISOU 4078  NH2 ARG A 520     5331   6887   3519   -362   -601   -224       N  
ATOM   4079  N   THR A 521      42.885 112.036 227.877  1.00 41.26           N  
ANISOU 4079  N   THR A 521     4664   7070   3941     47   -593    -58       N  
ATOM   4080  CA  THR A 521      43.055 112.976 226.772  1.00 40.98           C  
ANISOU 4080  CA  THR A 521     4541   7051   3978      9   -496    -69       C  
ATOM   4081  C   THR A 521      42.021 112.782 225.672  1.00 39.90           C  
ANISOU 4081  C   THR A 521     4450   6884   3825     32   -376    -54       C  
ATOM   4082  O   THR A 521      41.752 113.674 224.893  1.00 39.50           O  
ANISOU 4082  O   THR A 521     4376   6829   3802    -11   -291    -59       O  
ATOM   4083  CB  THR A 521      44.458 112.950 226.184  1.00 41.87           C  
ANISOU 4083  CB  THR A 521     4490   7223   4197     34   -513    -70       C  
ATOM   4084  OG1 THR A 521      44.751 111.629 225.724  1.00 42.02           O  
ANISOU 4084  OG1 THR A 521     4480   7250   4234    139   -516    -47       O  
ATOM   4085  CG2 THR A 521      45.478 113.403 227.241  1.00 43.06           C  
ANISOU 4085  CG2 THR A 521     4578   7410   4371    -13   -636    -87       C  
ATOM   4086  N   TRP A 522      41.413 111.611 225.641  1.00 39.50           N  
ANISOU 4086  N   TRP A 522     4474   6810   3724     97   -375    -34       N  
ATOM   4087  CA  TRP A 522      40.371 111.330 224.682  1.00 38.57           C  
ANISOU 4087  CA  TRP A 522     4409   6664   3580    113   -276    -19       C  
ATOM   4088  C   TRP A 522      39.249 112.326 224.916  1.00 37.91           C  
ANISOU 4088  C   TRP A 522     4400   6551   3454     42   -228    -27       C  
ATOM   4089  O   TRP A 522      38.384 112.546 224.054  1.00 37.21           O  
ANISOU 4089  O   TRP A 522     4334   6447   3357     35   -143    -16       O  
ATOM   4090  CB  TRP A 522      39.878 109.906 224.898  1.00 38.41           C  
ANISOU 4090  CB  TRP A 522     4474   6616   3503    179   -300      0       C  
ATOM   4091  CG  TRP A 522      39.093 109.293 223.763  1.00 37.72           C  
ANISOU 4091  CG  TRP A 522     4422   6510   3401    209   -213     14       C  
ATOM   4092  CD1 TRP A 522      37.767 108.951 223.767  1.00 37.01           C  
ANISOU 4092  CD1 TRP A 522     4438   6384   3242    194   -177     26       C  
ATOM   4093  CD2 TRP A 522      39.592 108.901 222.495  1.00 37.81           C  
ANISOU 4093  CD2 TRP A 522     4366   6538   3462    255   -155     17       C  
ATOM   4094  NE1 TRP A 522      37.411 108.371 222.587  1.00 36.66           N  
ANISOU 4094  NE1 TRP A 522     4398   6333   3199    224   -111     36       N  
ATOM   4095  CE2 TRP A 522      38.510 108.339 221.775  1.00 37.13           C  
ANISOU 4095  CE2 TRP A 522     4358   6422   3326    262    -92     29       C  
ATOM   4096  CE3 TRP A 522      40.836 108.986 221.885  1.00 38.48           C  
ANISOU 4096  CE3 TRP A 522     4330   6664   3628    287   -145      8       C  
ATOM   4097  CZ2 TRP A 522      38.650 107.859 220.481  1.00 37.10           C  
ANISOU 4097  CZ2 TRP A 522     4330   6425   3343    299    -24     31       C  
ATOM   4098  CZ3 TRP A 522      40.969 108.514 220.632  1.00 38.46           C  
ANISOU 4098  CZ3 TRP A 522     4300   6665   3647    327    -68      9       C  
ATOM   4099  CH2 TRP A 522      39.893 107.947 219.932  1.00 37.77           C  
ANISOU 4099  CH2 TRP A 522     4306   6545   3501    333     -9     19       C  
ATOM   4100  N   TYR A 523      39.270 112.929 226.100  1.00 38.26           N  
ANISOU 4100  N   TYR A 523     4483   6586   3468     -8   -287    -47       N  
ATOM   4101  CA  TYR A 523      38.251 113.860 226.451  1.00 37.82           C  
ANISOU 4101  CA  TYR A 523     4501   6496   3373    -67   -241    -59       C  
ATOM   4102  C   TYR A 523      38.801 115.290 226.410  1.00 38.19           C  
ANISOU 4102  C   TYR A 523     4490   6548   3474   -135   -228    -84       C  
ATOM   4103  O   TYR A 523      38.290 116.096 225.664  1.00 37.77           O  
ANISOU 4103  O   TYR A 523     4430   6476   3445   -160   -146    -80       O  
ATOM   4104  CB  TYR A 523      37.589 113.431 227.762  1.00 37.89           C  
ANISOU 4104  CB  TYR A 523     4628   6477   3291    -76   -290    -65       C  
ATOM   4105  CG  TYR A 523      36.912 114.526 228.547  1.00 37.90           C  
ANISOU 4105  CG  TYR A 523     4699   6447   3253   -144   -268    -94       C  
ATOM   4106  CD1 TYR A 523      35.839 115.240 228.019  1.00 37.27           C  
ANISOU 4106  CD1 TYR A 523     4643   6338   3178   -163   -169    -93       C  
ATOM   4107  CD2 TYR A 523      37.368 114.853 229.836  1.00 38.66           C  
ANISOU 4107  CD2 TYR A 523     4841   6541   3309   -187   -348   -122       C  
ATOM   4108  CE1 TYR A 523      35.251 116.266 228.767  1.00 37.41           C  
ANISOU 4108  CE1 TYR A 523     4726   6321   3168   -217   -142   -123       C  
ATOM   4109  CE2 TYR A 523      36.790 115.847 230.577  1.00 38.80           C  
ANISOU 4109  CE2 TYR A 523     4932   6524   3286   -249   -321   -156       C  
ATOM   4110  CZ  TYR A 523      35.740 116.562 230.050  1.00 38.18           C  
ANISOU 4110  CZ  TYR A 523     4875   6412   3221   -261   -214   -158       C  
ATOM   4111  OH  TYR A 523      35.183 117.568 230.813  1.00 38.44           O  
ANISOU 4111  OH  TYR A 523     4983   6404   3220   -315   -181   -195       O  
ATOM   4112  N   GLU A 524      39.865 115.599 227.139  1.00 39.07           N  
ANISOU 4112  N   GLU A 524     4558   6682   3606   -166   -311   -106       N  
ATOM   4113  CA  GLU A 524      40.285 116.996 227.285  1.00 39.53           C  
ANISOU 4113  CA  GLU A 524     4583   6733   3703   -247   -304   -135       C  
ATOM   4114  C   GLU A 524      40.877 117.623 226.040  1.00 39.58           C  
ANISOU 4114  C   GLU A 524     4480   6759   3799   -263   -238   -126       C  
ATOM   4115  O   GLU A 524      40.764 118.846 225.840  1.00 39.65           O  
ANISOU 4115  O   GLU A 524     4491   6740   3834   -327   -190   -140       O  
ATOM   4116  CB  GLU A 524      41.327 117.146 228.357  1.00 40.60           C  
ANISOU 4116  CB  GLU A 524     4693   6895   3839   -287   -419   -162       C  
ATOM   4117  CG  GLU A 524      40.956 116.548 229.656  1.00 40.81           C  
ANISOU 4117  CG  GLU A 524     4828   6907   3771   -280   -498   -169       C  
ATOM   4118  CD  GLU A 524      41.843 117.055 230.767  1.00 41.95           C  
ANISOU 4118  CD  GLU A 524     4968   7069   3903   -346   -609   -202       C  
ATOM   4119  OE1 GLU A 524      42.874 117.688 230.486  1.00 42.63           O  
ANISOU 4119  OE1 GLU A 524     4945   7187   4066   -388   -636   -215       O  
ATOM   4120  OE2 GLU A 524      41.504 116.835 231.934  1.00 42.26           O  
ANISOU 4120  OE2 GLU A 524     5116   7089   3851   -363   -671   -215       O  
ATOM   4121  N   VAL A 525      41.572 116.831 225.234  1.00 39.69           N  
ANISOU 4121  N   VAL A 525     4402   6817   3860   -206   -235   -105       N  
ATOM   4122  CA  VAL A 525      42.131 117.371 224.017  1.00 39.81           C  
ANISOU 4122  CA  VAL A 525     4319   6854   3953   -222   -162    -95       C  
ATOM   4123  C   VAL A 525      41.192 117.007 222.900  1.00 38.89           C  
ANISOU 4123  C   VAL A 525     4241   6719   3817   -177    -66    -65       C  
ATOM   4124  O   VAL A 525      40.859 117.852 222.090  1.00 38.64           O  
ANISOU 4124  O   VAL A 525     4208   6669   3805   -212     14    -53       O  
ATOM   4125  CB  VAL A 525      43.597 116.939 223.772  1.00 40.74           C  
ANISOU 4125  CB  VAL A 525     4296   7037   4147   -201   -204    -96       C  
ATOM   4126  CG1 VAL A 525      44.481 117.360 224.959  1.00 41.77           C  
ANISOU 4126  CG1 VAL A 525     4387   7188   4293   -256   -316   -125       C  
ATOM   4127  CG2 VAL A 525      43.729 115.446 223.583  1.00 40.66           C  
ANISOU 4127  CG2 VAL A 525     4274   7050   4127    -98   -227    -78       C  
ATOM   4128  N   GLY A 526      40.685 115.776 222.919  1.00 38.45           N  
ANISOU 4128  N   GLY A 526     4233   6662   3713   -106    -79    -50       N  
ATOM   4129  CA  GLY A 526      39.914 115.226 221.811  1.00 37.73           C  
ANISOU 4129  CA  GLY A 526     4171   6563   3601    -62     -1    -23       C  
ATOM   4130  C   GLY A 526      38.502 115.713 221.552  1.00 36.93           C  
ANISOU 4130  C   GLY A 526     4159   6419   3455    -83     59     -8       C  
ATOM   4131  O   GLY A 526      38.029 115.675 220.424  1.00 36.53           O  
ANISOU 4131  O   GLY A 526     4109   6367   3403    -70    128     16       O  
ATOM   4132  N   GLY A 527      37.816 116.163 222.597  1.00 36.80           N  
ANISOU 4132  N   GLY A 527     4216   6369   3398   -115     32    -22       N  
ATOM   4133  CA  GLY A 527      36.377 116.380 222.514  1.00 36.13           C  
ANISOU 4133  CA  GLY A 527     4213   6246   3269   -118     81     -7       C  
ATOM   4134  C   GLY A 527      35.826 117.277 223.573  1.00 36.23           C  
ANISOU 4134  C   GLY A 527     4287   6220   3258   -164     73    -31       C  
ATOM   4135  O   GLY A 527      35.078 116.853 224.431  1.00 36.06           O  
ANISOU 4135  O   GLY A 527     4341   6181   3179   -156     54    -38       O  
ATOM   4136  N   LYS A 528      36.163 118.549 223.499  1.00 36.58           N  
ANISOU 4136  N   LYS A 528     4307   6244   3346   -215     97    -43       N  
ATOM   4137  CA  LYS A 528      35.655 119.497 224.486  1.00 36.79           C  
ANISOU 4137  CA  LYS A 528     4402   6224   3354   -259     98    -72       C  
ATOM   4138  C   LYS A 528      36.090 120.855 224.002  1.00 37.19           C  
ANISOU 4138  C   LYS A 528     4417   6248   3465   -311    138    -77       C  
ATOM   4139  O   LYS A 528      36.956 120.944 223.120  1.00 37.39           O  
ANISOU 4139  O   LYS A 528     4361   6302   3543   -319    148    -61       O  
ATOM   4140  CB  LYS A 528      36.235 119.119 225.853  1.00 37.33           C  
ANISOU 4140  CB  LYS A 528     4499   6302   3381   -277      9   -109       C  
ATOM   4141  CG  LYS A 528      36.513 120.207 226.846  1.00 38.01           C  
ANISOU 4141  CG  LYS A 528     4624   6353   3463   -345    -15   -154       C  
ATOM   4142  CD  LYS A 528      36.765 119.568 228.175  1.00 38.43           C  
ANISOU 4142  CD  LYS A 528     4733   6420   3450   -352   -103   -181       C  
ATOM   4143  CE  LYS A 528      36.482 120.540 229.266  1.00 38.97           C  
ANISOU 4143  CE  LYS A 528     4888   6439   3479   -413   -105   -228       C  
ATOM   4144  NZ  LYS A 528      36.226 119.747 230.483  1.00 39.18           N  
ANISOU 4144  NZ  LYS A 528     5002   6471   3413   -406   -165   -243       N  
ATOM   4145  N   TYR A 529      35.479 121.906 224.527  1.00 37.37           N  
ANISOU 4145  N   TYR A 529     4503   6212   3483   -345    169    -97       N  
ATOM   4146  CA  TYR A 529      35.843 123.278 224.178  1.00 37.86           C  
ANISOU 4146  CA  TYR A 529     4552   6232   3602   -400    207   -103       C  
ATOM   4147  C   TYR A 529      36.016 123.370 222.689  1.00 37.64           C  
ANISOU 4147  C   TYR A 529     4458   6221   3622   -386    259    -54       C  
ATOM   4148  O   TYR A 529      35.228 122.819 221.949  1.00 37.02           O  
ANISOU 4148  O   TYR A 529     4384   6155   3526   -332    294    -15       O  
ATOM   4149  CB  TYR A 529      37.145 123.674 224.848  1.00 38.72           C  
ANISOU 4149  CB  TYR A 529     4627   6352   3733   -468    142   -145       C  
ATOM   4150  CG  TYR A 529      37.097 124.007 226.314  1.00 39.24           C  
ANISOU 4150  CG  TYR A 529     4773   6386   3752   -510     93   -200       C  
ATOM   4151  CD1 TYR A 529      36.024 124.735 226.867  1.00 39.24           C  
ANISOU 4151  CD1 TYR A 529     4874   6314   3722   -515    144   -221       C  
ATOM   4152  CD2 TYR A 529      38.156 123.663 227.136  1.00 39.89           C  
ANISOU 4152  CD2 TYR A 529     4828   6509   3821   -547     -3   -232       C  
ATOM   4153  CE1 TYR A 529      35.998 125.092 228.231  1.00 39.86           C  
ANISOU 4153  CE1 TYR A 529     5038   6359   3747   -560    107   -279       C  
ATOM   4154  CE2 TYR A 529      38.141 123.993 228.502  1.00 40.50           C  
ANISOU 4154  CE2 TYR A 529     4990   6557   3842   -594    -55   -285       C  
ATOM   4155  CZ  TYR A 529      37.065 124.713 229.046  1.00 40.48           C  
ANISOU 4155  CZ  TYR A 529     5100   6480   3800   -604      4   -311       C  
ATOM   4156  OH  TYR A 529      37.084 125.032 230.397  1.00 41.19           O  
ANISOU 4156  OH  TYR A 529     5284   6541   3826   -655    -41   -368       O  
ATOM   4157  N   LEU A 530      37.058 124.035 222.213  1.00 38.22           N  
ANISOU 4157  N   LEU A 530     4472   6298   3751   -438    265    -54       N  
ATOM   4158  CA  LEU A 530      37.187 124.179 220.757  1.00 38.09           C  
ANISOU 4158  CA  LEU A 530     4407   6296   3772   -429    326     -5       C  
ATOM   4159  C   LEU A 530      37.621 122.910 220.045  1.00 37.77           C  
ANISOU 4159  C   LEU A 530     4300   6330   3722   -380    316     16       C  
ATOM   4160  O   LEU A 530      38.150 122.999 218.979  1.00 37.95           O  
ANISOU 4160  O   LEU A 530     4268   6375   3776   -389    357     43       O  
ATOM   4161  CB  LEU A 530      38.110 125.327 220.368  1.00 38.90           C  
ANISOU 4161  CB  LEU A 530     4469   6374   3935   -507    352     -7       C  
ATOM   4162  CG  LEU A 530      37.696 126.683 220.898  1.00 39.34           C  
ANISOU 4162  CG  LEU A 530     4600   6340   4005   -557    375    -25       C  
ATOM   4163  CD1 LEU A 530      38.720 127.714 220.497  1.00 40.22           C  
ANISOU 4163  CD1 LEU A 530     4672   6432   4179   -644    398    -27       C  
ATOM   4164  CD2 LEU A 530      36.366 127.066 220.421  1.00 38.88           C  
ANISOU 4164  CD2 LEU A 530     4611   6228   3934   -510    434     13       C  
ATOM   4165  N   THR A 531      37.421 121.734 220.606  1.00 37.39           N  
ANISOU 4165  N   THR A 531     4263   6315   3630   -330    266      4       N  
ATOM   4166  CA  THR A 531      37.540 120.556 219.786  1.00 37.05           C  
ANISOU 4166  CA  THR A 531     4181   6322   3573   -274    273     28       C  
ATOM   4167  C   THR A 531      36.335 119.667 220.006  1.00 36.32           C  
ANISOU 4167  C   THR A 531     4158   6224   3418   -219    266     39       C  
ATOM   4168  O   THR A 531      36.452 118.449 219.838  1.00 36.11           O  
ANISOU 4168  O   THR A 531     4120   6233   3366   -172    244     43       O  
ATOM   4169  CB  THR A 531      38.806 119.714 220.075  1.00 37.51           C  
ANISOU 4169  CB  THR A 531     4162   6438   3653   -261    217      5       C  
ATOM   4170  OG1 THR A 531      38.680 119.061 221.358  1.00 37.48           O  
ANISOU 4170  OG1 THR A 531     4198   6434   3608   -241    138    -22       O  
ATOM   4171  CG2 THR A 531      40.076 120.552 220.018  1.00 38.39           C  
ANISOU 4171  CG2 THR A 531     4189   6565   3833   -324    215    -11       C  
ATOM   4172  N   LYS A 532      35.191 120.246 220.389  1.00 36.04           N  
ANISOU 4172  N   LYS A 532     4192   6142   3360   -225    286     44       N  
ATOM   4173  CA  LYS A 532      33.948 119.477 220.560  1.00 35.44           C  
ANISOU 4173  CA  LYS A 532     4174   6063   3230   -181    288     57       C  
ATOM   4174  C   LYS A 532      33.379 118.882 219.255  1.00 35.01           C  
ANISOU 4174  C   LYS A 532     4110   6031   3161   -146    326    102       C  
ATOM   4175  O   LYS A 532      32.662 117.861 219.297  1.00 34.60           O  
ANISOU 4175  O   LYS A 532     4090   5993   3064   -112    313    110       O  
ATOM   4176  CB  LYS A 532      32.883 120.295 221.272  1.00 35.41           C  
ANISOU 4176  CB  LYS A 532     4233   6007   3215   -194    310     49       C  
ATOM   4177  CG  LYS A 532      31.596 119.545 221.606  1.00 34.94           C  
ANISOU 4177  CG  LYS A 532     4224   5948   3105   -158    315     59       C  
ATOM   4178  CD  LYS A 532      31.861 118.228 222.357  1.00 34.84           C  
ANISOU 4178  CD  LYS A 532     4230   5965   3041   -141    258     39       C  
ATOM   4179  CE  LYS A 532      30.572 117.493 222.739  1.00 34.47           C  
ANISOU 4179  CE  LYS A 532     4239   5917   2943   -119    268     48       C  
ATOM   4180  NZ  LYS A 532      30.822 116.355 223.712  1.00 34.53           N  
ANISOU 4180  NZ  LYS A 532     4286   5938   2895   -112    212     27       N  
ATOM   4181  N   ARG A 533      33.713 119.469 218.106  1.00 35.18           N  
ANISOU 4181  N   ARG A 533     4096   6055   3215   -160    370    130       N  
ATOM   4182  CA  ARG A 533      33.176 118.874 216.889  1.00 34.87           C  
ANISOU 4182  CA  ARG A 533     4060   6039   3149   -131    399    171       C  
ATOM   4183  C   ARG A 533      33.662 117.448 216.611  1.00 34.75           C  
ANISOU 4183  C   ARG A 533     4031   6068   3105    -97    377    160       C  
ATOM   4184  O   ARG A 533      33.022 116.736 215.832  1.00 34.47           O  
ANISOU 4184  O   ARG A 533     4019   6047   3030    -74    391    184       O  
ATOM   4185  CB  ARG A 533      33.303 119.758 215.655  1.00 35.13           C  
ANISOU 4185  CB  ARG A 533     4076   6065   3207   -153    453    211       C  
ATOM   4186  CG  ARG A 533      32.898 121.177 215.894  1.00 35.37           C  
ANISOU 4186  CG  ARG A 533     4127   6040   3272   -182    475    223       C  
ATOM   4187  CD  ARG A 533      33.194 122.048 214.747  1.00 35.77           C  
ANISOU 4187  CD  ARG A 533     4166   6077   3347   -208    524    265       C  
ATOM   4188  NE  ARG A 533      31.954 122.237 214.016  1.00 35.58           N  
ANISOU 4188  NE  ARG A 533     4181   6039   3300   -183    541    318       N  
ATOM   4189  CZ  ARG A 533      31.688 121.730 212.806  1.00 35.51           C  
ANISOU 4189  CZ  ARG A 533     4177   6063   3252   -170    555    359       C  
ATOM   4190  NH1 ARG A 533      32.582 120.975 212.195  1.00 35.59           N  
ANISOU 4190  NH1 ARG A 533     4160   6120   3243   -175    566    348       N  
ATOM   4191  NH2 ARG A 533      30.501 121.964 212.247  1.00 35.45           N  
ANISOU 4191  NH2 ARG A 533     4200   6043   3225   -149    556    410       N  
ATOM   4192  N   ASN A 534      34.742 117.006 217.260  1.00 35.05           N  
ANISOU 4192  N   ASN A 534     4033   6124   3160    -92    340    125       N  
ATOM   4193  CA  ASN A 534      35.175 115.635 217.028  1.00 35.04           C  
ANISOU 4193  CA  ASN A 534     4023   6155   3137    -48    321    115       C  
ATOM   4194  C   ASN A 534      34.124 114.674 217.518  1.00 34.57           C  
ANISOU 4194  C   ASN A 534     4033   6084   3019    -22    292    117       C  
ATOM   4195  O   ASN A 534      33.969 113.591 216.962  1.00 34.45           O  
ANISOU 4195  O   ASN A 534     4039   6081   2971     10    295    123       O  
ATOM   4196  CB  ASN A 534      36.499 115.288 217.693  1.00 35.57           C  
ANISOU 4196  CB  ASN A 534     4033   6243   3239    -37    277     82       C  
ATOM   4197  CG  ASN A 534      37.675 115.978 217.076  1.00 36.18           C  
ANISOU 4197  CG  ASN A 534     4024   6344   3377    -63    311     80       C  
ATOM   4198  OD1 ASN A 534      37.689 116.264 215.882  1.00 36.23           O  
ANISOU 4198  OD1 ASN A 534     4017   6359   3389    -72    376    103       O  
ATOM   4199  ND2 ASN A 534      38.695 116.252 217.894  1.00 36.74           N  
ANISOU 4199  ND2 ASN A 534     4038   6429   3494    -80    265     52       N  
ATOM   4200  N   THR A 535      33.393 115.048 218.559  1.00 34.39           N  
ANISOU 4200  N   THR A 535     4051   6034   2982    -38    269    110       N  
ATOM   4201  CA  THR A 535      32.430 114.093 219.105  1.00 34.06           C  
ANISOU 4201  CA  THR A 535     4073   5983   2884    -20    246    111       C  
ATOM   4202  C   THR A 535      31.594 113.672 217.929  1.00 33.76           C  
ANISOU 4202  C   THR A 535     4051   5955   2820    -12    282    143       C  
ATOM   4203  O   THR A 535      31.386 112.473 217.706  1.00 33.65           O  
ANISOU 4203  O   THR A 535     4070   5949   2768     10    269    143       O  
ATOM   4204  CB  THR A 535      31.503 114.675 220.162  1.00 33.94           C  
ANISOU 4204  CB  THR A 535     4102   5940   2853    -43    242    104       C  
ATOM   4205  OG1 THR A 535      32.210 114.830 221.385  1.00 34.28           O  
ANISOU 4205  OG1 THR A 535     4152   5974   2899    -55    197     70       O  
ATOM   4206  CG2 THR A 535      30.425 113.744 220.411  1.00 33.65           C  
ANISOU 4206  CG2 THR A 535     4120   5900   2764    -33    238    113       C  
ATOM   4207  N   PHE A 536      31.174 114.660 217.146  1.00 33.72           N  
ANISOU 4207  N   PHE A 536     4028   5948   2836    -31    323    170       N  
ATOM   4208  CA  PHE A 536      30.202 114.400 216.099  1.00 33.52           C  
ANISOU 4208  CA  PHE A 536     4023   5933   2780    -30    347    206       C  
ATOM   4209  C   PHE A 536      30.838 113.774 214.901  1.00 33.67           C  
ANISOU 4209  C   PHE A 536     4032   5977   2785    -18    364    212       C  
ATOM   4210  O   PHE A 536      30.258 112.942 214.271  1.00 33.57           O  
ANISOU 4210  O   PHE A 536     4053   5975   2727    -13    364    224       O  
ATOM   4211  CB  PHE A 536      29.392 115.660 215.753  1.00 33.53           C  
ANISOU 4211  CB  PHE A 536     4015   5919   2806    -49    376    240       C  
ATOM   4212  CG  PHE A 536      28.958 116.431 216.975  1.00 33.54           C  
ANISOU 4212  CG  PHE A 536     4025   5888   2831    -57    373    224       C  
ATOM   4213  CD1 PHE A 536      28.349 115.790 218.029  1.00 33.38           C  
ANISOU 4213  CD1 PHE A 536     4039   5863   2782    -53    351    203       C  
ATOM   4214  CD2 PHE A 536      29.203 117.792 217.085  1.00 33.81           C  
ANISOU 4214  CD2 PHE A 536     4041   5891   2913    -72    397    227       C  
ATOM   4215  CE1 PHE A 536      27.963 116.514 219.160  1.00 33.50           C  
ANISOU 4215  CE1 PHE A 536     4070   5847   2811    -62    358    184       C  
ATOM   4216  CE2 PHE A 536      28.834 118.501 218.232  1.00 33.92           C  
ANISOU 4216  CE2 PHE A 536     4074   5869   2945    -80    400    204       C  
ATOM   4217  CZ  PHE A 536      28.225 117.863 219.269  1.00 33.77           C  
ANISOU 4217  CZ  PHE A 536     4089   5850   2893    -74    382    181       C  
ATOM   4218  N   MET A 537      32.054 114.152 214.596  1.00 34.01           N  
ANISOU 4218  N   MET A 537     4030   6029   2864    -18    383    200       N  
ATOM   4219  CA  MET A 537      32.683 113.618 213.403  1.00 34.28           C  
ANISOU 4219  CA  MET A 537     4054   6087   2883     -6    416    203       C  
ATOM   4220  C   MET A 537      33.249 112.225 213.575  1.00 34.40           C  
ANISOU 4220  C   MET A 537     4081   6109   2879     34    397    171       C  
ATOM   4221  O   MET A 537      33.222 111.437 212.616  1.00 34.53           O  
ANISOU 4221  O   MET A 537     4127   6136   2857     48    421    172       O  
ATOM   4222  CB  MET A 537      33.669 114.609 212.837  1.00 34.71           C  
ANISOU 4222  CB  MET A 537     4053   6152   2984    -26    459    209       C  
ATOM   4223  CG  MET A 537      32.881 115.826 212.547  1.00 34.63           C  
ANISOU 4223  CG  MET A 537     4054   6122   2980    -60    477    249       C  
ATOM   4224  SD  MET A 537      33.687 116.942 211.456  1.00 41.47           S  
ANISOU 4224  SD  MET A 537     4886   6993   3878    -95    540    276       S  
ATOM   4225  CE  MET A 537      33.188 116.231 209.851  1.00 40.90           C  
ANISOU 4225  CE  MET A 537     4864   6949   3729    -89    573    309       C  
ATOM   4226  N   ASP A 538      33.727 111.922 214.782  1.00 34.44           N  
ANISOU 4226  N   ASP A 538     4074   6104   2906     53    352    143       N  
ATOM   4227  CA  ASP A 538      34.131 110.593 215.100  1.00 34.60           C  
ANISOU 4227  CA  ASP A 538     4116   6120   2908     98    323    119       C  
ATOM   4228  C   ASP A 538      32.929 109.647 214.930  1.00 34.26           C  
ANISOU 4228  C   ASP A 538     4158   6060   2799     97    313    130       C  
ATOM   4229  O   ASP A 538      33.051 108.588 214.348  1.00 34.45           O  
ANISOU 4229  O   ASP A 538     4217   6080   2793    123    322    120       O  
ATOM   4230  CB  ASP A 538      34.671 110.541 216.527  1.00 34.74           C  
ANISOU 4230  CB  ASP A 538     4118   6129   2952    111    263     98       C  
ATOM   4231  CG  ASP A 538      36.084 111.200 216.686  1.00 35.29           C  
ANISOU 4231  CG  ASP A 538     4095   6222   3092    114    261     81       C  
ATOM   4232  OD1 ASP A 538      36.694 111.750 215.694  1.00 36.14           O  
ANISOU 4232  OD1 ASP A 538     4145   6353   3233    104    316     86       O  
ATOM   4233  OD2 ASP A 538      36.574 111.166 217.851  1.00 35.52           O  
ANISOU 4233  OD2 ASP A 538     4110   6248   3140    122    200     64       O  
ATOM   4234  N   PHE A 539      31.765 110.053 215.412  1.00 33.86           N  
ANISOU 4234  N   PHE A 539     4137   5999   2728     63    298    148       N  
ATOM   4235  CA  PHE A 539      30.542 109.258 215.326  1.00 33.62           C  
ANISOU 4235  CA  PHE A 539     4173   5958   2641     49    287    161       C  
ATOM   4236  C   PHE A 539      30.194 108.929 213.880  1.00 33.70           C  
ANISOU 4236  C   PHE A 539     4206   5983   2617     39    319    176       C  
ATOM   4237  O   PHE A 539      29.977 107.770 213.500  1.00 33.83           O  
ANISOU 4237  O   PHE A 539     4278   5989   2588     46    314    166       O  
ATOM   4238  CB  PHE A 539      29.371 109.998 216.018  1.00 33.30           C  
ANISOU 4238  CB  PHE A 539     4138   5913   2601     14    280    180       C  
ATOM   4239  CG  PHE A 539      28.193 109.118 216.309  1.00 33.16           C  
ANISOU 4239  CG  PHE A 539     4179   5886   2535     -4    263    187       C  
ATOM   4240  CD1 PHE A 539      28.213 108.237 217.387  1.00 33.21           C  
ANISOU 4240  CD1 PHE A 539     4234   5869   2518      4    231    169       C  
ATOM   4241  CD2 PHE A 539      27.078 109.140 215.491  1.00 33.09           C  
ANISOU 4241  CD2 PHE A 539     4179   5893   2502    -34    275    216       C  
ATOM   4242  CE1 PHE A 539      27.141 107.393 217.641  1.00 33.18           C  
ANISOU 4242  CE1 PHE A 539     4286   5854   2468    -23    221    177       C  
ATOM   4243  CE2 PHE A 539      25.996 108.289 215.723  1.00 33.08           C  
ANISOU 4243  CE2 PHE A 539     4223   5887   2458    -62    259    222       C  
ATOM   4244  CZ  PHE A 539      26.024 107.418 216.807  1.00 33.12           C  
ANISOU 4244  CZ  PHE A 539     4276   5865   2441    -59    237    202       C  
ATOM   4245  N   ILE A 540      30.168 109.977 213.079  1.00 33.73           N  
ANISOU 4245  N   ILE A 540     4172   6006   2637     19    352    200       N  
ATOM   4246  CA  ILE A 540      29.902 109.918 211.663  1.00 33.92           C  
ANISOU 4246  CA  ILE A 540     4215   6048   2623      3    381    220       C  
ATOM   4247  C   ILE A 540      30.905 108.988 210.980  1.00 34.33           C  
ANISOU 4247  C   ILE A 540     4286   6102   2657     34    409    189       C  
ATOM   4248  O   ILE A 540      30.536 108.197 210.122  1.00 34.53           O  
ANISOU 4248  O   ILE A 540     4368   6127   2623     25    418    187       O  
ATOM   4249  CB  ILE A 540      29.902 111.388 211.099  1.00 33.97           C  
ANISOU 4249  CB  ILE A 540     4178   6070   2661    -19    411    256       C  
ATOM   4250  CG1 ILE A 540      28.497 111.986 211.294  1.00 33.72           C  
ANISOU 4250  CG1 ILE A 540     4151   6037   2626    -45    387    294       C  
ATOM   4251  CG2 ILE A 540      30.337 111.444 209.648  1.00 34.39           C  
ANISOU 4251  CG2 ILE A 540     4241   6143   2683    -28    455    269       C  
ATOM   4252  CD1 ILE A 540      28.418 113.480 211.367  1.00 33.75           C  
ANISOU 4252  CD1 ILE A 540     4112   6033   2679    -55    403    324       C  
ATOM   4253  N   ALA A 541      32.172 109.079 211.392  1.00 34.57           N  
ANISOU 4253  N   ALA A 541     4265   6131   2737     69    422    163       N  
ATOM   4254  CA  ALA A 541      33.220 108.175 210.925  1.00 35.08           C  
ANISOU 4254  CA  ALA A 541     4333   6195   2801    113    451    130       C  
ATOM   4255  C   ALA A 541      32.934 106.686 211.240  1.00 35.15           C  
ANISOU 4255  C   ALA A 541     4416   6169   2769    142    421    106       C  
ATOM   4256  O   ALA A 541      33.083 105.826 210.366  1.00 35.54           O  
ANISOU 4256  O   ALA A 541     4516   6210   2779    158    453     87       O  
ATOM   4257  CB  ALA A 541      34.544 108.603 211.459  1.00 35.39           C  
ANISOU 4257  CB  ALA A 541     4288   6245   2915    144    459    111       C  
ATOM   4258  N   CYS A 542      32.484 106.393 212.464  1.00 34.83           N  
ANISOU 4258  N   CYS A 542     4394   6107   2734    144    364    106       N  
ATOM   4259  CA  CYS A 542      32.159 105.027 212.870  1.00 34.94           C  
ANISOU 4259  CA  CYS A 542     4487   6080   2708    164    333     90       C  
ATOM   4260  C   CYS A 542      31.076 104.478 212.016  1.00 34.90           C  
ANISOU 4260  C   CYS A 542     4559   6068   2633    121    342     98       C  
ATOM   4261  O   CYS A 542      31.030 103.288 211.717  1.00 35.24           O  
ANISOU 4261  O   CYS A 542     4677   6078   2636    135    343     77       O  
ATOM   4262  CB  CYS A 542      31.646 105.002 214.281  1.00 34.61           C  
ANISOU 4262  CB  CYS A 542     4460   6020   2671    153    277     98       C  
ATOM   4263  SG  CYS A 542      32.891 105.480 215.438  1.00 34.80           S  
ANISOU 4263  SG  CYS A 542     4410   6048   2764    198    245     86       S  
ATOM   4264  N   ALA A 543      30.183 105.356 211.608  1.00 34.57           N  
ANISOU 4264  N   ALA A 543     4501   6057   2579     67    346    130       N  
ATOM   4265  CA  ALA A 543      29.044 104.892 210.890  1.00 34.60           C  
ANISOU 4265  CA  ALA A 543     4567   6062   2517     18    339    143       C  
ATOM   4266  C   ALA A 543      29.409 104.671 209.443  1.00 35.07           C  
ANISOU 4266  C   ALA A 543     4657   6132   2535     16    383    133       C  
ATOM   4267  O   ALA A 543      28.852 103.803 208.801  1.00 35.35           O  
ANISOU 4267  O   ALA A 543     4770   6154   2507    -12    378    123       O  
ATOM   4268  CB  ALA A 543      27.923 105.849 211.042  1.00 34.22           C  
ANISOU 4268  CB  ALA A 543     4485   6041   2474    -31    319    184       C  
ATOM   4269  N   GLU A 544      30.353 105.432 208.920  1.00 35.24           N  
ANISOU 4269  N   GLU A 544     4624   6177   2589     39    428    132       N  
ATOM   4270  CA  GLU A 544      30.754 105.228 207.524  1.00 35.80           C  
ANISOU 4270  CA  GLU A 544     4730   6260   2612     35    482    120       C  
ATOM   4271  C   GLU A 544      31.506 103.898 207.409  1.00 36.34           C  
ANISOU 4271  C   GLU A 544     4854   6289   2665     86    508     68       C  
ATOM   4272  O   GLU A 544      31.339 103.178 206.410  1.00 36.84           O  
ANISOU 4272  O   GLU A 544     4998   6340   2658     71    535     48       O  
ATOM   4273  CB  GLU A 544      31.666 106.357 207.065  1.00 35.96           C  
ANISOU 4273  CB  GLU A 544     4676   6313   2675     46    535    132       C  
ATOM   4274  CG  GLU A 544      31.082 107.742 207.114  1.00 35.58           C  
ANISOU 4274  CG  GLU A 544     4578   6292   2649      5    518    184       C  
ATOM   4275  CD  GLU A 544      30.999 108.330 205.733  1.00 37.16           C  
ANISOU 4275  CD  GLU A 544     4799   6520   2801    -31    559    212       C  
ATOM   4276  OE1 GLU A 544      30.426 107.631 204.856  1.00 38.69           O  
ANISOU 4276  OE1 GLU A 544     5073   6715   2912    -58    557    209       O  
ATOM   4277  OE2 GLU A 544      31.513 109.471 205.513  1.00 37.94           O  
ANISOU 4277  OE2 GLU A 544     4841   6635   2937    -38    593    237       O  
ATOM   4278  N   HIS A 545      32.317 103.602 208.450  1.00 36.32           N  
ANISOU 4278  N   HIS A 545     4811   6264   2727    146    496     47       N  
ATOM   4279  CA  HIS A 545      33.089 102.342 208.597  1.00 36.90           C  
ANISOU 4279  CA  HIS A 545     4926   6290   2804    213    510      3       C  
ATOM   4280  C   HIS A 545      32.147 101.185 208.627  1.00 36.96           C  
ANISOU 4280  C   HIS A 545     5048   6249   2745    188    476     -8       C  
ATOM   4281  O   HIS A 545      32.409 100.152 208.021  1.00 37.59           O  
ANISOU 4281  O   HIS A 545     5207   6289   2788    213    508    -45       O  
ATOM   4282  CB  HIS A 545      33.940 102.294 209.893  1.00 36.87           C  
ANISOU 4282  CB  HIS A 545     4856   6272   2881    277    476     -4       C  
ATOM   4283  CG  HIS A 545      34.669 100.985 210.117  1.00 38.63           C  
ANISOU 4283  CG  HIS A 545     5122   6440   3115    356    480    -41       C  
ATOM   4284  ND1 HIS A 545      35.981 100.778 209.727  1.00 41.06           N  
ANISOU 4284  ND1 HIS A 545     5378   6751   3471    432    534    -72       N  
ATOM   4285  CD2 HIS A 545      34.270  99.825 210.700  1.00 37.97           C  
ANISOU 4285  CD2 HIS A 545     5130   6294   3004    374    437    -50       C  
ATOM   4286  CE1 HIS A 545      36.343  99.544 210.038  1.00 39.59           C  
ANISOU 4286  CE1 HIS A 545     5249   6503   3289    500    524    -98       C  
ATOM   4287  NE2 HIS A 545      35.323  98.944 210.624  1.00 38.51           N  
ANISOU 4287  NE2 HIS A 545     5206   6323   3104    464    464    -85       N  
ATOM   4288  N   LEU A 546      31.049 101.335 209.344  1.00 36.38           N  
ANISOU 4288  N   LEU A 546     4988   6177   2659    135    417     22       N  
ATOM   4289  CA  LEU A 546      30.120 100.238 209.375  1.00 36.52           C  
ANISOU 4289  CA  LEU A 546     5112   6150   2615     98    386     14       C  
ATOM   4290  C   LEU A 546      29.567  99.965 207.970  1.00 36.92           C  
ANISOU 4290  C   LEU A 546     5233   6209   2585     43    412      5       C  
ATOM   4291  O   LEU A 546      29.425  98.804 207.572  1.00 37.47           O  
ANISOU 4291  O   LEU A 546     5407   6228   2601     37    419    -28       O  
ATOM   4292  CB  LEU A 546      29.051 100.444 210.452  1.00 35.95           C  
ANISOU 4292  CB  LEU A 546     5031   6080   2547     49    326     48       C  
ATOM   4293  CG  LEU A 546      29.600 100.042 211.829  1.00 35.90           C  
ANISOU 4293  CG  LEU A 546     5020   6035   2586    103    295     42       C  
ATOM   4294  CD1 LEU A 546      28.821 100.600 213.003  1.00 35.34           C  
ANISOU 4294  CD1 LEU A 546     4917   5980   2532     65    252     74       C  
ATOM   4295  CD2 LEU A 546      29.643  98.549 211.898  1.00 36.47           C  
ANISOU 4295  CD2 LEU A 546     5203   6034   2621    122    288     15       C  
ATOM   4296  N   ILE A 547      29.343 101.028 207.199  1.00 36.76           N  
ANISOU 4296  N   ILE A 547     5164   6247   2554      6    429     32       N  
ATOM   4297  CA  ILE A 547      28.743 100.895 205.861  1.00 37.18           C  
ANISOU 4297  CA  ILE A 547     5286   6319   2523    -54    441     32       C  
ATOM   4298  C   ILE A 547      29.702 100.348 204.814  1.00 37.98           C  
ANISOU 4298  C   ILE A 547     5445   6400   2587    -18    515    -15       C  
ATOM   4299  O   ILE A 547      29.356  99.432 204.087  1.00 38.57           O  
ANISOU 4299  O   ILE A 547     5628   6444   2583    -49    521    -46       O  
ATOM   4300  CB  ILE A 547      28.042 102.203 205.396  1.00 36.85           C  
ANISOU 4300  CB  ILE A 547     5183   6343   2476   -109    423     87       C  
ATOM   4301  CG1 ILE A 547      26.759 102.415 206.229  1.00 36.32           C  
ANISOU 4301  CG1 ILE A 547     5089   6288   2424   -158    352    126       C  
ATOM   4302  CG2 ILE A 547      27.727 102.167 203.919  1.00 37.46           C  
ANISOU 4302  CG2 ILE A 547     5327   6443   2462   -160    440     89       C  
ATOM   4303  CD1 ILE A 547      26.413 103.867 206.527  1.00 35.81           C  
ANISOU 4303  CD1 ILE A 547     4923   6271   2412   -165    337    179       C  
ATOM   4304  N   SER A 548      30.904 100.898 204.765  1.00 38.09           N  
ANISOU 4304  N   SER A 548     5385   6430   2656     45    573    -24       N  
ATOM   4305  CA  SER A 548      31.906 100.458 203.789  1.00 38.95           C  
ANISOU 4305  CA  SER A 548     5533   6526   2740     87    659    -71       C  
ATOM   4306  C   SER A 548      32.595  99.109 204.121  1.00 39.54           C  
ANISOU 4306  C   SER A 548     5666   6529   2830    163    684   -128       C  
ATOM   4307  O   SER A 548      33.144  98.452 203.234  1.00 40.42           O  
ANISOU 4307  O   SER A 548     5845   6613   2899    190    755   -176       O  
ATOM   4308  CB  SER A 548      32.957 101.551 203.595  1.00 38.98           C  
ANISOU 4308  CB  SER A 548     5427   6579   2806    122    720    -59       C  
ATOM   4309  OG  SER A 548      33.696 101.714 204.784  1.00 38.67           O  
ANISOU 4309  OG  SER A 548     5291   6532   2869    187    703    -59       O  
ATOM   4310  N   SER A 549      32.580  98.689 205.376  1.00 39.18           N  
ANISOU 4310  N   SER A 549     5601   6446   2840    199    629   -124       N  
ATOM   4311  CA  SER A 549      33.081  97.358 205.668  1.00 39.83           C  
ANISOU 4311  CA  SER A 549     5756   6449   2929    268    642   -170       C  
ATOM   4312  C   SER A 549      31.991  96.347 205.317  1.00 40.09           C  
ANISOU 4312  C   SER A 549     5935   6428   2868    200    612   -187       C  
ATOM   4313  O   SER A 549      32.195  95.149 205.409  1.00 40.73           O  
ANISOU 4313  O   SER A 549     6111   6430   2935    240    621   -226       O  
ATOM   4314  CB  SER A 549      33.496  97.223 207.138  1.00 39.51           C  
ANISOU 4314  CB  SER A 549     5654   6383   2974    331    588   -155       C  
ATOM   4315  OG  SER A 549      32.372  97.038 207.971  1.00 38.92           O  
ANISOU 4315  OG  SER A 549     5620   6290   2876    271    509   -125       O  
ATOM   4316  N   GLY A 550      30.818  96.850 204.946  1.00 39.65           N  
ANISOU 4316  N   GLY A 550     5895   6416   2754     97    570   -153       N  
ATOM   4317  CA  GLY A 550      29.669  96.023 204.587  1.00 39.92           C  
ANISOU 4317  CA  GLY A 550     6053   6415   2700     12    531   -163       C  
ATOM   4318  C   GLY A 550      28.796  95.490 205.719  1.00 39.53           C  
ANISOU 4318  C   GLY A 550     6029   6328   2662    -24    455   -141       C  
ATOM   4319  O   GLY A 550      27.883  94.713 205.461  1.00 39.87           O  
ANISOU 4319  O   GLY A 550     6176   6338   2637    -99    424   -152       O  
ATOM   4320  N   LEU A 551      29.028  95.900 206.966  1.00 38.90           N  
ANISOU 4320  N   LEU A 551     5862   6256   2662     20    425   -111       N  
ATOM   4321  CA  LEU A 551      28.170  95.437 208.063  1.00 38.59           C  
ANISOU 4321  CA  LEU A 551     5852   6185   2627    -21    360    -88       C  
ATOM   4322  C   LEU A 551      26.727  95.896 207.935  1.00 38.21           C  
ANISOU 4322  C   LEU A 551     5790   6188   2538   -135    313    -50       C  
ATOM   4323  O   LEU A 551      25.813  95.199 208.352  1.00 38.33           O  
ANISOU 4323  O   LEU A 551     5869   6171   2522   -199    273    -45       O  
ATOM   4324  CB  LEU A 551      28.706  95.870 209.427  1.00 38.06           C  
ANISOU 4324  CB  LEU A 551     5698   6121   2643     43    337    -63       C  
ATOM   4325  CG  LEU A 551      30.023  95.355 209.991  1.00 38.46           C  
ANISOU 4325  CG  LEU A 551     5745   6119   2750    158    355    -87       C  
ATOM   4326  CD1 LEU A 551      29.907  95.392 211.496  1.00 41.04           C  
ANISOU 4326  CD1 LEU A 551     6045   6432   3117    172    298    -55       C  
ATOM   4327  CD2 LEU A 551      30.375  93.940 209.546  1.00 42.55           C  
ANISOU 4327  CD2 LEU A 551     6392   6543   3232    196    383   -134       C  
ATOM   4328  N   THR A 552      26.533  97.070 207.360  1.00 37.84           N  
ANISOU 4328  N   THR A 552     5659   6221   2496   -159    317    -21       N  
ATOM   4329  CA  THR A 552      25.243  97.732 207.319  1.00 37.48           C  
ANISOU 4329  CA  THR A 552     5569   6236   2435   -247    270     24       C  
ATOM   4330  C   THR A 552      25.204  98.655 206.103  1.00 37.55           C  
ANISOU 4330  C   THR A 552     5542   6311   2416   -270    286     42       C  
ATOM   4331  O   THR A 552      26.228  98.906 205.452  1.00 37.77           O  
ANISOU 4331  O   THR A 552     5566   6341   2444   -216    340     21       O  
ATOM   4332  CB  THR A 552      25.069  98.545 208.612  1.00 36.71           C  
ANISOU 4332  CB  THR A 552     5370   6166   2414   -228    247     63       C  
ATOM   4333  OG1 THR A 552      24.791  97.632 209.662  1.00 37.20           O  
ANISOU 4333  OG1 THR A 552     5485   6171   2479   -235    223     56       O  
ATOM   4334  CG2 THR A 552      23.944  99.519 208.558  1.00 36.36           C  
ANISOU 4334  CG2 THR A 552     5249   6190   2376   -291    214    113       C  
ATOM   4335  N   THR A 553      24.004  99.126 205.799  1.00 37.49           N  
ANISOU 4335  N   THR A 553     5507   6355   2382   -350    238     82       N  
ATOM   4336  CA  THR A 553      23.756 100.165 204.822  1.00 37.53           C  
ANISOU 4336  CA  THR A 553     5466   6428   2367   -375    234    118       C  
ATOM   4337  C   THR A 553      22.886 101.175 205.581  1.00 36.93           C  
ANISOU 4337  C   THR A 553     5279   6401   2354   -393    192    177       C  
ATOM   4338  O   THR A 553      22.212 100.818 206.524  1.00 36.73           O  
ANISOU 4338  O   THR A 553     5240   6363   2354   -416    162    183       O  
ATOM   4339  CB  THR A 553      23.005  99.600 203.577  1.00 38.33           C  
ANISOU 4339  CB  THR A 553     5659   6541   2364   -462    203    111       C  
ATOM   4340  OG1 THR A 553      21.680  99.207 203.948  1.00 38.42           O  
ANISOU 4340  OG1 THR A 553     5671   6564   2364   -544    135    132       O  
ATOM   4341  CG2 THR A 553      23.722  98.391 203.028  1.00 39.02           C  
ANISOU 4341  CG2 THR A 553     5876   6562   2388   -449    247     43       C  
ATOM   4342  N   PRO A 554      22.889 102.437 205.171  1.00 36.75           N  
ANISOU 4342  N   PRO A 554     5179   6429   2354   -381    195    220       N  
ATOM   4343  CA  PRO A 554      22.037 103.361 205.922  1.00 36.29           C  
ANISOU 4343  CA  PRO A 554     5020   6409   2360   -390    161    271       C  
ATOM   4344  C   PRO A 554      20.546 102.977 205.971  1.00 36.59           C  
ANISOU 4344  C   PRO A 554     5054   6472   2375   -470     97    296       C  
ATOM   4345  O   PRO A 554      19.921 103.194 206.989  1.00 36.27           O  
ANISOU 4345  O   PRO A 554     4951   6438   2390   -473     83    314       O  
ATOM   4346  CB  PRO A 554      22.214 104.697 205.187  1.00 36.29           C  
ANISOU 4346  CB  PRO A 554     4962   6452   2373   -373    170    316       C  
ATOM   4347  CG  PRO A 554      23.462 104.528 204.360  1.00 36.56           C  
ANISOU 4347  CG  PRO A 554     5054   6469   2369   -340    227    282       C  
ATOM   4348  CD  PRO A 554      23.530 103.072 204.007  1.00 37.05           C  
ANISOU 4348  CD  PRO A 554     5225   6493   2359   -367    229    228       C  
ATOM   4349  N   ALA A 555      19.947 102.421 204.927  1.00 37.27           N  
ANISOU 4349  N   ALA A 555     5203   6577   2383   -540     58    297       N  
ATOM   4350  CA  ALA A 555      18.530 102.039 205.088  1.00 37.63           C  
ANISOU 4350  CA  ALA A 555     5228   6651   2418   -622     -6    320       C  
ATOM   4351  C   ALA A 555      18.280 101.018 206.244  1.00 37.50           C  
ANISOU 4351  C   ALA A 555     5240   6587   2420   -642      0    287       C  
ATOM   4352  O   ALA A 555      17.139 100.801 206.679  1.00 37.72           O  
ANISOU 4352  O   ALA A 555     5230   6639   2462   -706    -39    308       O  
ATOM   4353  CB  ALA A 555      17.921 101.553 203.795  1.00 38.51           C  
ANISOU 4353  CB  ALA A 555     5406   6791   2436   -705    -59    323       C  
ATOM   4354  N   GLN A 556      19.346 100.412 206.743  1.00 37.23           N  
ANISOU 4354  N   GLN A 556     5270   6487   2389   -588     48    240       N  
ATOM   4355  CA  GLN A 556      19.242  99.413 207.800  1.00 37.20           C  
ANISOU 4355  CA  GLN A 556     5313   6427   2393   -602     54    212       C  
ATOM   4356  C   GLN A 556      19.909  99.884 209.094  1.00 36.49           C  
ANISOU 4356  C   GLN A 556     5171   6315   2378   -522     90    213       C  
ATOM   4357  O   GLN A 556      20.071  99.118 210.055  1.00 36.44           O  
ANISOU 4357  O   GLN A 556     5212   6256   2379   -515    100    191       O  
ATOM   4358  CB  GLN A 556      19.948  98.148 207.346  1.00 37.67           C  
ANISOU 4358  CB  GLN A 556     5510   6415   2389   -601     72    155       C  
ATOM   4359  CG  GLN A 556      19.467  97.552 206.024  1.00 38.50           C  
ANISOU 4359  CG  GLN A 556     5698   6527   2404   -681     42    139       C  
ATOM   4360  CD  GLN A 556      20.302  96.353 205.694  1.00 38.99           C  
ANISOU 4360  CD  GLN A 556     5900   6504   2412   -662     77     76       C  
ATOM   4361  OE1 GLN A 556      20.069  95.250 206.194  1.00 39.33           O  
ANISOU 4361  OE1 GLN A 556     6026   6482   2437   -697     70     49       O  
ATOM   4362  NE2 GLN A 556      21.333  96.572 204.909  1.00 39.09           N  
ANISOU 4362  NE2 GLN A 556     5940   6509   2403   -600    122     51       N  
ATOM   4363  N   LEU A 557      20.323 101.147 209.113  1.00 36.02           N  
ANISOU 4363  N   LEU A 557     5023   6292   2370   -465    109    238       N  
ATOM   4364  CA  LEU A 557      21.085 101.672 210.214  1.00 35.44           C  
ANISOU 4364  CA  LEU A 557     4905   6200   2360   -393    140    233       C  
ATOM   4365  C   LEU A 557      20.279 102.691 211.012  1.00 35.11           C  
ANISOU 4365  C   LEU A 557     4763   6199   2378   -399    134    273       C  
ATOM   4366  O   LEU A 557      19.616 103.562 210.448  1.00 35.18           O  
ANISOU 4366  O   LEU A 557     4704   6260   2402   -416    119    311       O  
ATOM   4367  CB  LEU A 557      22.345 102.311 209.690  1.00 35.25           C  
ANISOU 4367  CB  LEU A 557     4865   6177   2353   -322    174    223       C  
ATOM   4368  CG  LEU A 557      23.213 103.000 210.716  1.00 34.75           C  
ANISOU 4368  CG  LEU A 557     4745   6101   2357   -253    200    219       C  
ATOM   4369  CD1 LEU A 557      23.887 102.004 211.614  1.00 34.78           C  
ANISOU 4369  CD1 LEU A 557     4809   6045   2360   -219    203    183       C  
ATOM   4370  CD2 LEU A 557      24.222 103.807 209.975  1.00 34.70           C  
ANISOU 4370  CD2 LEU A 557     4705   6111   2369   -206    232    218       C  
ATOM   4371  N   SER A 558      20.367 102.562 212.334  1.00 34.84           N  
ANISOU 4371  N   SER A 558     4726   6138   2375   -380    147    263       N  
ATOM   4372  CA  SER A 558      19.771 103.487 213.266  1.00 34.58           C  
ANISOU 4372  CA  SER A 558     4611   6131   2397   -376    158    289       C  
ATOM   4373  C   SER A 558      20.796 103.928 214.302  1.00 34.16           C  
ANISOU 4373  C   SER A 558     4551   6047   2381   -309    183    270       C  
ATOM   4374  O   SER A 558      21.852 103.303 214.454  1.00 34.13           O  
ANISOU 4374  O   SER A 558     4606   6001   2361   -272    185    239       O  
ATOM   4375  CB  SER A 558      18.587 102.803 213.969  1.00 34.89           C  
ANISOU 4375  CB  SER A 558     4661   6172   2424   -444    149    296       C  
ATOM   4376  OG  SER A 558      18.991 101.635 214.681  1.00 35.76           O  
ANISOU 4376  OG  SER A 558     4867   6222   2499   -451    151    266       O  
ATOM   4377  N   CYS A 559      20.478 104.992 215.033  1.00 33.93           N  
ANISOU 4377  N   CYS A 559     4452   6039   2403   -293    201    286       N  
ATOM   4378  CA  CYS A 559      21.340 105.463 216.107  1.00 33.63           C  
ANISOU 4378  CA  CYS A 559     4410   5974   2395   -244    219    267       C  
ATOM   4379  C   CYS A 559      20.534 105.903 217.273  1.00 33.65           C  
ANISOU 4379  C   CYS A 559     4382   5982   2419   -261    238    275       C  
ATOM   4380  O   CYS A 559      19.387 106.258 217.136  1.00 33.83           O  
ANISOU 4380  O   CYS A 559     4356   6039   2460   -294    247    300       O  
ATOM   4381  CB  CYS A 559      22.209 106.632 215.660  1.00 33.39           C  
ANISOU 4381  CB  CYS A 559     4326   5955   2407   -194    232    270       C  
ATOM   4382  SG  CYS A 559      21.333 108.130 215.125  1.00 33.41           S  
ANISOU 4382  SG  CYS A 559     4234   6000   2459   -198    246    314       S  
ATOM   4383  N   GLU A 560      21.156 105.878 218.437  1.00 33.54           N  
ANISOU 4383  N   GLU A 560     4401   5937   2406   -236    245    252       N  
ATOM   4384  CA  GLU A 560      20.522 106.300 219.666  1.00 33.63           C  
ANISOU 4384  CA  GLU A 560     4401   5948   2429   -251    272    251       C  
ATOM   4385  C   GLU A 560      21.529 107.025 220.586  1.00 33.46           C  
ANISOU 4385  C   GLU A 560     4384   5904   2426   -206    277    228       C  
ATOM   4386  O   GLU A 560      22.737 106.636 220.687  1.00 33.38           O  
ANISOU 4386  O   GLU A 560     4413   5868   2403   -173    248    209       O  
ATOM   4387  CB  GLU A 560      19.914 105.089 220.352  1.00 33.95           C  
ANISOU 4387  CB  GLU A 560     4513   5969   2418   -301    270    248       C  
ATOM   4388  CG  GLU A 560      19.231 105.406 221.677  1.00 37.41           C  
ANISOU 4388  CG  GLU A 560     4952   6407   2855   -324    309    246       C  
ATOM   4389  CD  GLU A 560      18.848 104.165 222.492  1.00 42.70           C  
ANISOU 4389  CD  GLU A 560     5711   7047   3465   -375    309    243       C  
ATOM   4390  OE1 GLU A 560      19.249 103.016 222.103  1.00 43.28           O  
ANISOU 4390  OE1 GLU A 560     5856   7089   3499   -384    273    241       O  
ATOM   4391  OE2 GLU A 560      18.148 104.372 223.532  1.00 44.63           O  
ANISOU 4391  OE2 GLU A 560     5959   7296   3701   -404    352    242       O  
ATOM   4392  N   GLY A 561      21.008 108.089 221.220  1.00 33.51           N  
ANISOU 4392  N   GLY A 561     4346   5920   2465   -205    313    229       N  
ATOM   4393  CA  GLY A 561      21.702 108.896 222.236  1.00 33.49           C  
ANISOU 4393  CA  GLY A 561     4352   5896   2475   -179    323    203       C  
ATOM   4394  C   GLY A 561      20.732 109.408 223.295  1.00 33.79           C  
ANISOU 4394  C   GLY A 561     4388   5934   2515   -200    373    197       C  
ATOM   4395  O   GLY A 561      19.549 109.466 223.074  1.00 33.98           O  
ANISOU 4395  O   GLY A 561     4372   5983   2555   -224    406    217       O  
ATOM   4396  N   ARG A 562      21.252 109.779 224.457  1.00 33.92           N  
ANISOU 4396  N   ARG A 562     4448   5926   2515   -194    379    168       N  
ATOM   4397  CA  ARG A 562      20.453 110.313 225.540  1.00 34.31           C  
ANISOU 4397  CA  ARG A 562     4508   5970   2557   -212    436    153       C  
ATOM   4398  C   ARG A 562      21.267 111.432 226.198  1.00 34.37           C  
ANISOU 4398  C   ARG A 562     4525   5952   2581   -188    440    120       C  
ATOM   4399  O   ARG A 562      22.484 111.331 226.314  1.00 34.24           O  
ANISOU 4399  O   ARG A 562     4538   5921   2551   -173    386    105       O  
ATOM   4400  CB  ARG A 562      20.114 109.205 226.566  1.00 34.65           C  
ANISOU 4400  CB  ARG A 562     4639   6001   2526   -254    439    147       C  
ATOM   4401  CG  ARG A 562      18.695 108.529 226.406  1.00 36.22           C  
ANISOU 4401  CG  ARG A 562     4819   6226   2716   -301    481    172       C  
ATOM   4402  CD  ARG A 562      18.144 107.698 227.659  1.00 39.54           C  
ANISOU 4402  CD  ARG A 562     5327   6632   3063   -355    513    165       C  
ATOM   4403  NE  ARG A 562      18.741 108.195 228.914  1.00 43.40           N  
ANISOU 4403  NE  ARG A 562     5886   7092   3512   -346    523    132       N  
ATOM   4404  CZ  ARG A 562      18.124 108.920 229.850  1.00 44.61           C  
ANISOU 4404  CZ  ARG A 562     6046   7245   3658   -359    597    109       C  
ATOM   4405  NH1 ARG A 562      16.817 109.230 229.750  1.00 44.76           N  
ANISOU 4405  NH1 ARG A 562     5997   7294   3716   -377    677    118       N  
ATOM   4406  NH2 ARG A 562      18.834 109.323 230.908  1.00 44.71           N  
ANISOU 4406  NH2 ARG A 562     6136   7228   3624   -354    590     76       N  
ATOM   4407  N   SER A 563      20.577 112.484 226.642  1.00 34.67           N  
ANISOU 4407  N   SER A 563     4538   5985   2650   -184    504    107       N  
ATOM   4408  CA  SER A 563      21.164 113.595 227.363  1.00 34.89           C  
ANISOU 4408  CA  SER A 563     4587   5981   2688   -172    518     70       C  
ATOM   4409  C   SER A 563      22.188 114.266 226.476  1.00 34.55           C  
ANISOU 4409  C   SER A 563     4499   5931   2697   -143    477     75       C  
ATOM   4410  O   SER A 563      21.857 114.682 225.372  1.00 34.35           O  
ANISOU 4410  O   SER A 563     4404   5920   2728   -122    489    105       O  
ATOM   4411  CB  SER A 563      21.760 113.123 228.677  1.00 35.19           C  
ANISOU 4411  CB  SER A 563     4726   5998   2648   -198    493     36       C  
ATOM   4412  OG  SER A 563      22.028 114.217 229.544  1.00 35.60           O  
ANISOU 4412  OG  SER A 563     4810   6019   2698   -199    521     -6       O  
ATOM   4413  N   ALA A 564      23.432 114.367 226.922  1.00 34.57           N  
ANISOU 4413  N   ALA A 564     4539   5916   2680   -145    428     47       N  
ATOM   4414  CA  ALA A 564      24.478 114.826 226.009  1.00 34.30           C  
ANISOU 4414  CA  ALA A 564     4456   5884   2694   -125    390     55       C  
ATOM   4415  C   ALA A 564      24.565 114.006 224.717  1.00 33.88           C  
ANISOU 4415  C   ALA A 564     4359   5860   2652   -110    363     94       C  
ATOM   4416  O   ALA A 564      24.849 114.556 223.682  1.00 33.71           O  
ANISOU 4416  O   ALA A 564     4283   5845   2679    -95    365    113       O  
ATOM   4417  CB  ALA A 564      25.800 114.893 226.695  1.00 34.50           C  
ANISOU 4417  CB  ALA A 564     4516   5895   2698   -135    334     22       C  
ATOM   4418  N   GLY A 565      24.284 112.704 224.777  1.00 33.79           N  
ANISOU 4418  N   GLY A 565     4382   5864   2592   -119    341    105       N  
ATOM   4419  CA  GLY A 565      24.153 111.857 223.575  1.00 33.49           C  
ANISOU 4419  CA  GLY A 565     4319   5851   2557   -112    324    138       C  
ATOM   4420  C   GLY A 565      23.032 112.291 222.645  1.00 33.42           C  
ANISOU 4420  C   GLY A 565     4252   5863   2584   -113    363    171       C  
ATOM   4421  O   GLY A 565      23.081 112.040 221.427  1.00 33.23           O  
ANISOU 4421  O   GLY A 565     4196   5859   2573   -106    349    197       O  
ATOM   4422  N   GLY A 566      22.002 112.915 223.225  1.00 33.68           N  
ANISOU 4422  N   GLY A 566     4273   5892   2632   -122    413    170       N  
ATOM   4423  CA  GLY A 566      20.951 113.568 222.452  1.00 33.78           C  
ANISOU 4423  CA  GLY A 566     4218   5922   2693   -112    449    203       C  
ATOM   4424  C   GLY A 566      21.581 114.682 221.625  1.00 33.69           C  
ANISOU 4424  C   GLY A 566     4164   5899   2736    -83    446    215       C  
ATOM   4425  O   GLY A 566      21.242 114.868 220.415  1.00 33.64           O  
ANISOU 4425  O   GLY A 566     4110   5914   2757    -73    439    256       O  
ATOM   4426  N   LEU A 567      22.524 115.402 222.250  1.00 33.74           N  
ANISOU 4426  N   LEU A 567     4194   5873   2753    -77    447    182       N  
ATOM   4427  CA  LEU A 567      23.275 116.445 221.553  1.00 33.73           C  
ANISOU 4427  CA  LEU A 567     4162   5855   2801    -60    446    190       C  
ATOM   4428  C   LEU A 567      23.984 115.780 220.404  1.00 33.43           C  
ANISOU 4428  C   LEU A 567     4109   5844   2751    -60    406    212       C  
ATOM   4429  O   LEU A 567      23.962 116.280 219.268  1.00 33.43           O  
ANISOU 4429  O   LEU A 567     4071   5852   2780    -50    411    248       O  
ATOM   4430  CB  LEU A 567      24.305 117.105 222.486  1.00 33.92           C  
ANISOU 4430  CB  LEU A 567     4218   5841   2827    -69    442    144       C  
ATOM   4431  CG  LEU A 567      25.456 117.951 221.924  1.00 33.96           C  
ANISOU 4431  CG  LEU A 567     4201   5830   2873    -69    430    143       C  
ATOM   4432  CD1 LEU A 567      24.948 119.185 221.128  1.00 34.17           C  
ANISOU 4432  CD1 LEU A 567     4191   5831   2959    -53    471    177       C  
ATOM   4433  CD2 LEU A 567      26.430 118.346 223.031  1.00 34.24           C  
ANISOU 4433  CD2 LEU A 567     4272   5837   2900    -91    411     91       C  
ATOM   4434  N   LEU A 568      24.602 114.634 220.687  1.00 33.27           N  
ANISOU 4434  N   LEU A 568     4122   5835   2684    -68    369    193       N  
ATOM   4435  CA  LEU A 568      25.355 113.983 219.669  1.00 33.10           C  
ANISOU 4435  CA  LEU A 568     4091   5833   2651    -62    341    205       C  
ATOM   4436  C   LEU A 568      24.375 113.644 218.545  1.00 33.04           C  
ANISOU 4436  C   LEU A 568     4064   5853   2635    -66    348    246       C  
ATOM   4437  O   LEU A 568      24.639 113.988 217.388  1.00 33.04           O  
ANISOU 4437  O   LEU A 568     4038   5865   2651    -60    350    272       O  
ATOM   4438  CB  LEU A 568      26.102 112.790 220.236  1.00 33.06           C  
ANISOU 4438  CB  LEU A 568     4129   5829   2603    -60    302    178       C  
ATOM   4439  CG  LEU A 568      26.892 111.852 219.332  1.00 33.00           C  
ANISOU 4439  CG  LEU A 568     4122   5836   2579    -45    278    181       C  
ATOM   4440  CD1 LEU A 568      27.817 110.964 220.151  1.00 33.13           C  
ANISOU 4440  CD1 LEU A 568     4176   5840   2572    -30    236    152       C  
ATOM   4441  CD2 LEU A 568      25.915 111.020 218.519  1.00 32.91           C  
ANISOU 4441  CD2 LEU A 568     4128   5841   2534    -57    281    207       C  
ATOM   4442  N   VAL A 569      23.229 113.047 218.879  1.00 33.08           N  
ANISOU 4442  N   VAL A 569     4082   5869   2616    -82    351    255       N  
ATOM   4443  CA  VAL A 569      22.253 112.680 217.824  1.00 33.14           C  
ANISOU 4443  CA  VAL A 569     4067   5909   2615    -95    346    295       C  
ATOM   4444  C   VAL A 569      21.823 113.897 216.929  1.00 33.32           C  
ANISOU 4444  C   VAL A 569     4034   5939   2686    -79    362    336       C  
ATOM   4445  O   VAL A 569      21.852 113.847 215.674  1.00 33.37           O  
ANISOU 4445  O   VAL A 569     4029   5967   2682    -82    345    368       O  
ATOM   4446  CB  VAL A 569      20.998 111.920 218.381  1.00 33.30           C  
ANISOU 4446  CB  VAL A 569     4097   5944   2610   -124    350    299       C  
ATOM   4447  CG1 VAL A 569      20.029 111.588 217.259  1.00 33.48           C  
ANISOU 4447  CG1 VAL A 569     4088   6005   2627   -145    334    340       C  
ATOM   4448  CG2 VAL A 569      21.393 110.635 219.043  1.00 33.21           C  
ANISOU 4448  CG2 VAL A 569     4154   5921   2545   -143    330    269       C  
ATOM   4449  N   GLY A 570      21.451 114.980 217.609  1.00 33.50           N  
ANISOU 4449  N   GLY A 570     4033   5939   2757    -62    395    335       N  
ATOM   4450  CA  GLY A 570      20.917 116.166 216.962  1.00 33.80           C  
ANISOU 4450  CA  GLY A 570     4023   5972   2847    -39    412    377       C  
ATOM   4451  C   GLY A 570      21.915 116.830 216.044  1.00 33.78           C  
ANISOU 4451  C   GLY A 570     4021   5955   2857    -30    407    393       C  
ATOM   4452  O   GLY A 570      21.539 117.286 214.943  1.00 34.01           O  
ANISOU 4452  O   GLY A 570     4026   5998   2900    -22    399    444       O  
ATOM   4453  N   ALA A 571      23.179 116.891 216.478  1.00 33.59           N  
ANISOU 4453  N   ALA A 571     4024   5909   2830    -35    410    353       N  
ATOM   4454  CA  ALA A 571      24.217 117.429 215.616  1.00 33.64           C  
ANISOU 4454  CA  ALA A 571     4026   5908   2849    -35    412    365       C  
ATOM   4455  C   ALA A 571      24.348 116.498 214.406  1.00 33.56           C  
ANISOU 4455  C   ALA A 571     4023   5938   2789    -46    388    388       C  
ATOM   4456  O   ALA A 571      24.311 116.934 213.263  1.00 33.78           O  
ANISOU 4456  O   ALA A 571     4043   5974   2816    -48    390    430       O  
ATOM   4457  CB  ALA A 571      25.513 117.577 216.360  1.00 33.57           C  
ANISOU 4457  CB  ALA A 571     4031   5876   2849    -43    415    317       C  
ATOM   4458  N   VAL A 572      24.427 115.203 214.660  1.00 33.33           N  
ANISOU 4458  N   VAL A 572     4020   5929   2715    -56    367    360       N  
ATOM   4459  CA  VAL A 572      24.740 114.237 213.620  1.00 33.32           C  
ANISOU 4459  CA  VAL A 572     4041   5956   2663    -66    350    366       C  
ATOM   4460  C   VAL A 572      23.633 114.117 212.577  1.00 33.54           C  
ANISOU 4460  C   VAL A 572     4065   6013   2664    -81    333    415       C  
ATOM   4461  O   VAL A 572      23.917 113.933 211.384  1.00 33.72           O  
ANISOU 4461  O   VAL A 572     4104   6054   2652    -91    329    434       O  
ATOM   4462  CB  VAL A 572      25.016 112.892 214.254  1.00 33.13           C  
ANISOU 4462  CB  VAL A 572     4055   5933   2600    -70    331    325       C  
ATOM   4463  CG1 VAL A 572      24.829 111.790 213.254  1.00 33.22           C  
ANISOU 4463  CG1 VAL A 572     4100   5967   2554    -85    314    332       C  
ATOM   4464  CG2 VAL A 572      26.413 112.879 214.878  1.00 33.07           C  
ANISOU 4464  CG2 VAL A 572     4049   5907   2611    -52    335    284       C  
ATOM   4465  N   LEU A 573      22.372 114.211 213.031  1.00 33.62           N  
ANISOU 4465  N   LEU A 573     4053   6031   2690    -85    323    433       N  
ATOM   4466  CA  LEU A 573      21.244 114.377 212.103  1.00 33.98           C  
ANISOU 4466  CA  LEU A 573     4075   6108   2728    -96    299    488       C  
ATOM   4467  C   LEU A 573      21.268 115.709 211.368  1.00 34.31           C  
ANISOU 4467  C   LEU A 573     4090   6138   2806    -74    308    538       C  
ATOM   4468  O   LEU A 573      20.758 115.796 210.241  1.00 34.68           O  
ANISOU 4468  O   LEU A 573     4134   6213   2830    -85    280    588       O  
ATOM   4469  CB  LEU A 573      19.885 114.157 212.762  1.00 34.14           C  
ANISOU 4469  CB  LEU A 573     4060   6144   2765   -104    289    498       C  
ATOM   4470  CG  LEU A 573      19.557 112.781 213.393  1.00 33.98           C  
ANISOU 4470  CG  LEU A 573     4071   6138   2704   -138    277    462       C  
ATOM   4471  CD1 LEU A 573      18.114 112.784 213.982  1.00 34.31           C  
ANISOU 4471  CD1 LEU A 573     4061   6201   2774   -150    279    480       C  
ATOM   4472  CD2 LEU A 573      19.761 111.544 212.491  1.00 34.01           C  
ANISOU 4472  CD2 LEU A 573     4126   6161   2635   -175    243    456       C  
ATOM   4473  N   ASN A 574      21.846 116.754 211.957  1.00 34.26           N  
ANISOU 4473  N   ASN A 574     4073   6091   2854    -50    344    527       N  
ATOM   4474  CA  ASN A 574      21.991 117.999 211.194  1.00 34.65           C  
ANISOU 4474  CA  ASN A 574     4112   6118   2934    -34    356    576       C  
ATOM   4475  C   ASN A 574      22.982 117.832 210.048  1.00 34.72           C  
ANISOU 4475  C   ASN A 574     4155   6139   2896    -55    358    586       C  
ATOM   4476  O   ASN A 574      22.765 118.400 208.956  1.00 35.16           O  
ANISOU 4476  O   ASN A 574     4218   6201   2941    -57    348    644       O  
ATOM   4477  CB  ASN A 574      22.417 119.173 212.062  1.00 34.69           C  
ANISOU 4477  CB  ASN A 574     4107   6066   3007    -11    396    558       C  
ATOM   4478  CG  ASN A 574      21.257 119.907 212.621  1.00 35.01           C  
ANISOU 4478  CG  ASN A 574     4113   6087   3103     22    405    580       C  
ATOM   4479  OD1 ASN A 574      20.197 119.935 211.995  1.00 35.38           O  
ANISOU 4479  OD1 ASN A 574     4130   6160   3153     34    378    634       O  
ATOM   4480  ND2 ASN A 574      21.419 120.481 213.822  1.00 34.98           N  
ANISOU 4480  ND2 ASN A 574     4110   6037   3143     36    442    538       N  
ATOM   4481  N   MET A 575      24.043 117.044 210.276  1.00 34.38           N  
ANISOU 4481  N   MET A 575     4137   6101   2826    -68    371    532       N  
ATOM   4482  CA  MET A 575      25.138 116.957 209.300  1.00 34.54           C  
ANISOU 4482  CA  MET A 575     4183   6129   2812    -84    392    532       C  
ATOM   4483  C   MET A 575      25.002 115.856 208.290  1.00 34.66           C  
ANISOU 4483  C   MET A 575     4236   6184   2748   -104    372    536       C  
ATOM   4484  O   MET A 575      25.130 116.094 207.114  1.00 35.07           O  
ANISOU 4484  O   MET A 575     4312   6250   2761   -120    378    573       O  
ATOM   4485  CB  MET A 575      26.473 116.835 210.003  1.00 34.32           C  
ANISOU 4485  CB  MET A 575     4148   6083   2808    -81    422    475       C  
ATOM   4486  CG  MET A 575      26.581 117.727 211.229  1.00 34.21           C  
ANISOU 4486  CG  MET A 575     4107   6029   2862    -69    433    455       C  
ATOM   4487  SD  MET A 575      28.003 117.236 212.215  1.00 34.00           S  
ANISOU 4487  SD  MET A 575     4070   5997   2852    -70    441    384       S  
ATOM   4488  CE  MET A 575      28.233 118.699 213.257  1.00 34.15           C  
ANISOU 4488  CE  MET A 575     4069   5964   2944    -74    458    372       C  
ATOM   4489  N   ARG A 576      24.746 114.645 208.763  1.00 34.38           N  
ANISOU 4489  N   ARG A 576     4216   6163   2684   -109    350    498       N  
ATOM   4490  CA  ARG A 576      24.712 113.449 207.916  1.00 34.53           C  
ANISOU 4490  CA  ARG A 576     4286   6210   2625   -131    334    486       C  
ATOM   4491  C   ARG A 576      23.441 112.659 208.142  1.00 34.51           C  
ANISOU 4491  C   ARG A 576     4289   6226   2596   -151    286    492       C  
ATOM   4492  O   ARG A 576      23.472 111.461 208.394  1.00 34.39           O  
ANISOU 4492  O   ARG A 576     4310   6211   2545   -163    276    452       O  
ATOM   4493  CB  ARG A 576      25.933 112.553 208.184  1.00 34.37           C  
ANISOU 4493  CB  ARG A 576     4290   6179   2592   -119    363    425       C  
ATOM   4494  CG  ARG A 576      27.276 113.083 207.657  1.00 34.60           C  
ANISOU 4494  CG  ARG A 576     4310   6203   2634   -109    416    416       C  
ATOM   4495  CD  ARG A 576      27.203 113.509 206.187  1.00 35.13           C  
ANISOU 4495  CD  ARG A 576     4408   6290   2651   -134    432    462       C  
ATOM   4496  NE  ARG A 576      26.820 112.422 205.303  1.00 35.41           N  
ANISOU 4496  NE  ARG A 576     4507   6348   2599   -156    415    455       N  
ATOM   4497  CZ  ARG A 576      27.636 111.455 204.878  1.00 35.62           C  
ANISOU 4497  CZ  ARG A 576     4575   6376   2583   -152    449    408       C  
ATOM   4498  NH1 ARG A 576      28.909 111.412 205.265  1.00 35.59           N  
ANISOU 4498  NH1 ARG A 576     4543   6359   2621   -121    499    367       N  
ATOM   4499  NH2 ARG A 576      27.172 110.529 204.046  1.00 35.96           N  
ANISOU 4499  NH2 ARG A 576     4690   6433   2542   -178    432    401       N  
ATOM   4500  N   PRO A 577      22.302 113.333 208.030  1.00 34.73           N  
ANISOU 4500  N   PRO A 577     4281   6268   2646   -156    257    544       N  
ATOM   4501  CA  PRO A 577      21.016 112.677 208.250  1.00 34.83           C  
ANISOU 4501  CA  PRO A 577     4282   6308   2646   -181    212    554       C  
ATOM   4502  C   PRO A 577      20.809 111.481 207.330  1.00 35.13           C  
ANISOU 4502  C   PRO A 577     4379   6372   2596   -227    179    545       C  
ATOM   4503  O   PRO A 577      20.045 110.591 207.672  1.00 35.16           O  
ANISOU 4503  O   PRO A 577     4389   6389   2582   -258    150    531       O  
ATOM   4504  CB  PRO A 577      20.025 113.757 207.874  1.00 35.26           C  
ANISOU 4504  CB  PRO A 577     4283   6378   2737   -171    187    622       C  
ATOM   4505  CG  PRO A 577      20.797 114.694 206.928  1.00 35.51           C  
ANISOU 4505  CG  PRO A 577     4333   6398   2761   -157    206    656       C  
ATOM   4506  CD  PRO A 577      22.153 114.717 207.538  1.00 35.05           C  
ANISOU 4506  CD  PRO A 577     4291   6302   2722   -139    263    601       C  
ATOM   4507  N   ASP A 578      21.474 111.495 206.164  1.00 35.42           N  
ANISOU 4507  N   ASP A 578     4465   6416   2578   -236    188    553       N  
ATOM   4508  CA  ASP A 578      21.437 110.426 205.124  1.00 35.84           C  
ANISOU 4508  CA  ASP A 578     4594   6489   2535   -281    166    539       C  
ATOM   4509  C   ASP A 578      21.976 109.071 205.587  1.00 35.61           C  
ANISOU 4509  C   ASP A 578     4620   6434   2476   -287    184    469       C  
ATOM   4510  O   ASP A 578      21.726 108.064 204.959  1.00 35.98           O  
ANISOU 4510  O   ASP A 578     4733   6488   2450   -328    162    450       O  
ATOM   4511  CB  ASP A 578      22.317 110.836 203.959  1.00 36.21           C  
ANISOU 4511  CB  ASP A 578     4685   6537   2534   -280    198    551       C  
ATOM   4512  CG  ASP A 578      23.739 111.124 204.400  1.00 35.85           C  
ANISOU 4512  CG  ASP A 578     4632   6458   2530   -237    270    512       C  
ATOM   4513  OD1 ASP A 578      23.960 112.236 204.906  1.00 35.63           O  
ANISOU 4513  OD1 ASP A 578     4547   6416   2574   -208    290    535       O  
ATOM   4514  OD2 ASP A 578      24.622 110.255 204.273  1.00 35.86           O  
ANISOU 4514  OD2 ASP A 578     4680   6446   2498   -232    307    458       O  
ATOM   4515  N   LEU A 579      22.743 109.077 206.674  1.00 35.09           N  
ANISOU 4515  N   LEU A 579     4533   6335   2466   -244    222    431       N  
ATOM   4516  CA  LEU A 579      23.349 107.892 207.183  1.00 34.94           C  
ANISOU 4516  CA  LEU A 579     4563   6284   2429   -236    238    372       C  
ATOM   4517  C   LEU A 579      22.370 107.039 207.982  1.00 34.86           C  
ANISOU 4517  C   LEU A 579     4563   6268   2415   -267    201    361       C  
ATOM   4518  O   LEU A 579      22.632 105.846 208.233  1.00 34.92           O  
ANISOU 4518  O   LEU A 579     4633   6245   2389   -274    202    318       O  
ATOM   4519  CB  LEU A 579      24.555 108.269 208.029  1.00 34.55           C  
ANISOU 4519  CB  LEU A 579     4482   6206   2440   -180    281    342       C  
ATOM   4520  CG  LEU A 579      25.836 108.752 207.293  1.00 34.74           C  
ANISOU 4520  CG  LEU A 579     4505   6230   2467   -153    333    334       C  
ATOM   4521  CD1 LEU A 579      26.966 108.824 208.266  1.00 34.47           C  
ANISOU 4521  CD1 LEU A 579     4436   6170   2491   -105    361    297       C  
ATOM   4522  CD2 LEU A 579      26.259 107.851 206.122  1.00 35.26           C  
ANISOU 4522  CD2 LEU A 579     4647   6298   2454   -166    354    309       C  
ATOM   4523  N   PHE A 580      21.226 107.619 208.345  1.00 34.85           N  
ANISOU 4523  N   PHE A 580     4502   6293   2446   -287    171    402       N  
ATOM   4524  CA  PHE A 580      20.260 106.910 209.163  1.00 34.85           C  
ANISOU 4524  CA  PHE A 580     4500   6293   2450   -322    146    395       C  
ATOM   4525  C   PHE A 580      18.879 106.784 208.557  1.00 35.37           C  
ANISOU 4525  C   PHE A 580     4544   6404   2491   -384     94    434       C  
ATOM   4526  O   PHE A 580      18.437 107.624 207.736  1.00 35.68           O  
ANISOU 4526  O   PHE A 580     4541   6480   2534   -386     70    483       O  
ATOM   4527  CB  PHE A 580      20.230 107.576 210.522  1.00 34.43           C  
ANISOU 4527  CB  PHE A 580     4387   6225   2469   -287    170    394       C  
ATOM   4528  CG  PHE A 580      21.594 107.692 211.096  1.00 34.04           C  
ANISOU 4528  CG  PHE A 580     4356   6137   2442   -234    207    357       C  
ATOM   4529  CD1 PHE A 580      22.202 106.592 211.674  1.00 33.96           C  
ANISOU 4529  CD1 PHE A 580     4406   6090   2407   -227    211    313       C  
ATOM   4530  CD2 PHE A 580      22.331 108.856 210.934  1.00 33.89           C  
ANISOU 4530  CD2 PHE A 580     4295   6118   2464   -193    233    369       C  
ATOM   4531  CE1 PHE A 580      23.492 106.672 212.131  1.00 33.74           C  
ANISOU 4531  CE1 PHE A 580     4385   6033   2402   -176    235    282       C  
ATOM   4532  CE2 PHE A 580      23.633 108.942 211.387  1.00 33.66           C  
ANISOU 4532  CE2 PHE A 580     4273   6060   2457   -153    261    335       C  
ATOM   4533  CZ  PHE A 580      24.222 107.852 211.986  1.00 33.60           C  
ANISOU 4533  CZ  PHE A 580     4313   6023   2429   -141    259    292       C  
ATOM   4534  N   HIS A 581      18.192 105.722 208.961  1.00 35.57           N  
ANISOU 4534  N   HIS A 581     4598   6424   2491   -436     73    416       N  
ATOM   4535  CA  HIS A 581      16.824 105.511 208.537  1.00 36.15           C  
ANISOU 4535  CA  HIS A 581     4640   6547   2550   -504     20    450       C  
ATOM   4536  C   HIS A 581      15.863 105.830 209.675  1.00 36.12           C  
ANISOU 4536  C   HIS A 581     4550   6559   2614   -509     28    468       C  
ATOM   4537  O   HIS A 581      14.703 106.187 209.453  1.00 36.61           O  
ANISOU 4537  O   HIS A 581     4535   6672   2701   -541     -7    511       O  
ATOM   4538  CB  HIS A 581      16.643 104.078 208.069  1.00 36.60           C  
ANISOU 4538  CB  HIS A 581     4792   6589   2527   -576     -8    417       C  
ATOM   4539  CG  HIS A 581      15.334 103.839 207.397  1.00 37.36           C  
ANISOU 4539  CG  HIS A 581     4860   6740   2596   -659    -74    451       C  
ATOM   4540  ND1 HIS A 581      15.033 104.350 206.147  1.00 37.87           N  
ANISOU 4540  ND1 HIS A 581     4910   6851   2627   -677   -122    490       N  
ATOM   4541  CD2 HIS A 581      14.238 103.161 207.807  1.00 37.81           C  
ANISOU 4541  CD2 HIS A 581     4896   6815   2655   -734   -103    454       C  
ATOM   4542  CE1 HIS A 581      13.810 103.988 205.815  1.00 38.60           C  
ANISOU 4542  CE1 HIS A 581     4971   6993   2704   -757   -187    516       C  
ATOM   4543  NE2 HIS A 581      13.304 103.267 206.805  1.00 38.58           N  
ANISOU 4543  NE2 HIS A 581     4958   6975   2726   -795   -173    493       N  
ATOM   4544  N   VAL A 582      16.385 105.709 210.888  1.00 35.62           N  
ANISOU 4544  N   VAL A 582     4502   6453   2579   -476     75    435       N  
ATOM   4545  CA  VAL A 582      15.645 105.927 212.121  1.00 35.60           C  
ANISOU 4545  CA  VAL A 582     4439   6456   2630   -479    100    440       C  
ATOM   4546  C   VAL A 582      16.585 106.263 213.314  1.00 35.00           C  
ANISOU 4546  C   VAL A 582     4382   6331   2584   -418    152    408       C  
ATOM   4547  O   VAL A 582      17.759 105.897 213.338  1.00 34.66           O  
ANISOU 4547  O   VAL A 582     4408   6247   2514   -388    162    375       O  
ATOM   4548  CB  VAL A 582      14.713 104.745 212.454  1.00 36.06           C  
ANISOU 4548  CB  VAL A 582     4522   6522   2658   -563     83    431       C  
ATOM   4549  CG1 VAL A 582      15.488 103.460 212.690  1.00 35.93           C  
ANISOU 4549  CG1 VAL A 582     4629   6444   2579   -582     89    383       C  
ATOM   4550  CG2 VAL A 582      13.811 105.100 213.648  1.00 36.20           C  
ANISOU 4550  CG2 VAL A 582     4463   6556   2734   -570    119    443       C  
ATOM   4551  N   ALA A 583      16.038 106.955 214.304  1.00 34.98           N  
ANISOU 4551  N   ALA A 583     4316   6337   2638   -401    185    417       N  
ATOM   4552  CA  ALA A 583      16.842 107.680 215.259  1.00 34.53           C  
ANISOU 4552  CA  ALA A 583     4260   6245   2615   -342    228    396       C  
ATOM   4553  C   ALA A 583      16.082 107.932 216.570  1.00 34.69           C  
ANISOU 4553  C   ALA A 583     4244   6266   2669   -348    270    391       C  
ATOM   4554  O   ALA A 583      14.914 108.351 216.516  1.00 35.13           O  
ANISOU 4554  O   ALA A 583     4220   6362   2765   -364    278    421       O  
ATOM   4555  CB  ALA A 583      17.281 109.004 214.619  1.00 34.39           C  
ANISOU 4555  CB  ALA A 583     4192   6234   2640   -287    231    419       C  
ATOM   4556  N   LEU A 584      16.740 107.677 217.717  1.00 34.43           N  
ANISOU 4556  N   LEU A 584     4270   6191   2621   -334    297    355       N  
ATOM   4557  CA  LEU A 584      16.187 107.957 219.071  1.00 34.61           C  
ANISOU 4557  CA  LEU A 584     4280   6208   2664   -339    348    343       C  
ATOM   4558  C   LEU A 584      17.029 108.965 219.807  1.00 34.32           C  
ANISOU 4558  C   LEU A 584     4248   6139   2653   -281    376    320       C  
ATOM   4559  O   LEU A 584      18.235 108.848 219.838  1.00 33.96           O  
ANISOU 4559  O   LEU A 584     4255   6062   2586   -255    356    298       O  
ATOM   4560  CB  LEU A 584      16.136 106.702 219.931  1.00 34.76           C  
ANISOU 4560  CB  LEU A 584     4382   6201   2623   -388    352    321       C  
ATOM   4561  CG  LEU A 584      15.289 105.486 219.517  1.00 35.18           C  
ANISOU 4561  CG  LEU A 584     4456   6272   2640   -465    330    334       C  
ATOM   4562  CD1 LEU A 584      15.496 104.329 220.514  1.00 35.32           C  
ANISOU 4562  CD1 LEU A 584     4580   6244   2597   -504    339    312       C  
ATOM   4563  CD2 LEU A 584      13.817 105.815 219.369  1.00 35.75           C  
ANISOU 4563  CD2 LEU A 584     4427   6402   2755   -505    351    365       C  
ATOM   4564  N   ALA A 585      16.393 109.960 220.400  1.00 34.57           N  
ANISOU 4564  N   ALA A 585     4223   6177   2734   -262    425    323       N  
ATOM   4565  CA  ALA A 585      17.077 110.984 221.195  1.00 34.43           C  
ANISOU 4565  CA  ALA A 585     4217   6124   2740   -217    457    296       C  
ATOM   4566  C   ALA A 585      16.308 111.214 222.532  1.00 34.87           C  
ANISOU 4566  C   ALA A 585     4275   6174   2799   -229    523    276       C  
ATOM   4567  O   ALA A 585      15.381 112.009 222.594  1.00 35.29           O  
ANISOU 4567  O   ALA A 585     4256   6244   2907   -213    570    290       O  
ATOM   4568  CB  ALA A 585      17.146 112.245 220.409  1.00 34.41           C  
ANISOU 4568  CB  ALA A 585     4148   6125   2800   -170    459    319       C  
ATOM   4569  N   GLY A 586      16.646 110.500 223.590  1.00 34.89           N  
ANISOU 4569  N   GLY A 586     4362   6154   2743   -256    531    246       N  
ATOM   4570  CA  GLY A 586      15.995 110.763 224.853  1.00 35.39           C  
ANISOU 4570  CA  GLY A 586     4439   6209   2798   -271    601    224       C  
ATOM   4571  C   GLY A 586      16.578 111.985 225.515  1.00 35.40           C  
ANISOU 4571  C   GLY A 586     4455   6176   2822   -227    631    191       C  
ATOM   4572  O   GLY A 586      17.764 112.246 225.381  1.00 35.01           O  
ANISOU 4572  O   GLY A 586     4438   6099   2764   -203    587    177       O  
ATOM   4573  N   VAL A 587      15.734 112.729 226.240  1.00 35.97           N  
ANISOU 4573  N   VAL A 587     4499   6246   2922   -219    711    177       N  
ATOM   4574  CA  VAL A 587      16.140 113.915 227.018  1.00 36.18           C  
ANISOU 4574  CA  VAL A 587     4551   6230   2964   -184    754    138       C  
ATOM   4575  C   VAL A 587      17.340 114.665 226.411  1.00 35.69           C  
ANISOU 4575  C   VAL A 587     4492   6140   2930   -147    701    134       C  
ATOM   4576  O   VAL A 587      18.321 114.846 227.089  1.00 35.62           O  
ANISOU 4576  O   VAL A 587     4553   6097   2883   -150    682     98       O  
ATOM   4577  CB  VAL A 587      16.476 113.528 228.473  1.00 36.47           C  
ANISOU 4577  CB  VAL A 587     4699   6240   2917   -220    778     93       C  
ATOM   4578  CG1 VAL A 587      15.174 113.329 229.307  1.00 37.23           C  
ANISOU 4578  CG1 VAL A 587     4791   6355   3001   -250    873     86       C  
ATOM   4579  CG2 VAL A 587      17.399 112.296 228.500  1.00 36.04           C  
ANISOU 4579  CG2 VAL A 587     4722   6182   2788   -251    695     98       C  
ATOM   4580  N   PRO A 588      17.244 115.108 225.136  1.00 35.47           N  
ANISOU 4580  N   PRO A 588     4385   6127   2965   -116    676    174       N  
ATOM   4581  CA  PRO A 588      18.374 115.581 224.345  1.00 35.02           C  
ANISOU 4581  CA  PRO A 588     4326   6052   2928    -92    623    180       C  
ATOM   4582  C   PRO A 588      18.785 117.042 224.501  1.00 35.23           C  
ANISOU 4582  C   PRO A 588     4348   6032   3005    -57    652    161       C  
ATOM   4583  O   PRO A 588      17.987 117.938 224.273  1.00 35.63           O  
ANISOU 4583  O   PRO A 588     4347   6073   3119    -23    700    178       O  
ATOM   4584  CB  PRO A 588      17.890 115.359 222.908  1.00 34.86           C  
ANISOU 4584  CB  PRO A 588     4232   6071   2941    -84    591    236       C  
ATOM   4585  CG  PRO A 588      16.443 115.520 222.966  1.00 35.40           C  
ANISOU 4585  CG  PRO A 588     4235   6165   3048    -79    640    258       C  
ATOM   4586  CD  PRO A 588      15.998 115.157 224.352  1.00 35.76           C  
ANISOU 4586  CD  PRO A 588     4326   6204   3056   -105    696    219       C  
ATOM   4587  N   PHE A 589      20.062 117.245 224.810  1.00 35.02           N  
ANISOU 4587  N   PHE A 589     4374   5975   2955    -65    618    130       N  
ATOM   4588  CA  PHE A 589      20.620 118.555 225.040  1.00 35.27           C  
ANISOU 4588  CA  PHE A 589     4418   5956   3025    -47    639    105       C  
ATOM   4589  C   PHE A 589      20.751 119.138 223.697  1.00 35.10           C  
ANISOU 4589  C   PHE A 589     4336   5936   3064    -21    622    151       C  
ATOM   4590  O   PHE A 589      21.671 118.783 222.975  1.00 34.69           O  
ANISOU 4590  O   PHE A 589     4279   5900   3001    -31    569    164       O  
ATOM   4591  CB  PHE A 589      22.015 118.454 225.691  1.00 35.15           C  
ANISOU 4591  CB  PHE A 589     4468   5921   2966    -76    592     62       C  
ATOM   4592  CG  PHE A 589      22.691 119.799 225.944  1.00 35.49           C  
ANISOU 4592  CG  PHE A 589     4529   5909   3046    -73    607     31       C  
ATOM   4593  CD1 PHE A 589      21.960 120.960 226.118  1.00 36.01           C  
ANISOU 4593  CD1 PHE A 589     4589   5930   3162    -48    677     23       C  
ATOM   4594  CD2 PHE A 589      24.063 119.891 226.050  1.00 35.40           C  
ANISOU 4594  CD2 PHE A 589     4541   5889   3022    -98    552      8       C  
ATOM   4595  CE1 PHE A 589      22.588 122.176 226.368  1.00 36.41           C  
ANISOU 4595  CE1 PHE A 589     4669   5920   3244    -52    692     -8       C  
ATOM   4596  CE2 PHE A 589      24.692 121.135 226.287  1.00 35.81           C  
ANISOU 4596  CE2 PHE A 589     4611   5888   3108   -109    564    -23       C  
ATOM   4597  CZ  PHE A 589      23.948 122.260 226.450  1.00 36.30           C  
ANISOU 4597  CZ  PHE A 589     4681   5898   3214    -89    634    -32       C  
ATOM   4598  N   VAL A 590      19.842 120.021 223.305  1.00 35.50           N  
ANISOU 4598  N   VAL A 590     4338   5971   3178     17    668    178       N  
ATOM   4599  CA  VAL A 590      19.867 120.460 221.874  1.00 35.40           C  
ANISOU 4599  CA  VAL A 590     4270   5966   3213     41    642    237       C  
ATOM   4600  C   VAL A 590      19.748 121.956 221.577  1.00 35.90           C  
ANISOU 4600  C   VAL A 590     4319   5972   3351     81    679    253       C  
ATOM   4601  O   VAL A 590      20.020 122.349 220.465  1.00 35.85           O  
ANISOU 4601  O   VAL A 590     4287   5964   3371     92    653    299       O  
ATOM   4602  CB  VAL A 590      18.844 119.698 221.010  1.00 35.34           C  
ANISOU 4602  CB  VAL A 590     4201   6019   3207     47    623    291       C  
ATOM   4603  CG1 VAL A 590      19.307 118.311 220.765  1.00 34.79           C  
ANISOU 4603  CG1 VAL A 590     4153   5996   3070      7    569    289       C  
ATOM   4604  CG2 VAL A 590      17.462 119.694 221.644  1.00 35.86           C  
ANISOU 4604  CG2 VAL A 590     4231   6098   3297     64    677    291       C  
ATOM   4605  N   ASP A 591      19.353 122.774 222.545  1.00 36.47           N  
ANISOU 4605  N   ASP A 591     4415   5991   3450    101    742    215       N  
ATOM   4606  CA  ASP A 591      19.165 124.205 222.343  1.00 37.09           C  
ANISOU 4606  CA  ASP A 591     4490   6000   3602    144    785    227       C  
ATOM   4607  C   ASP A 591      20.390 124.884 222.936  1.00 37.15           C  
ANISOU 4607  C   ASP A 591     4573   5946   3597    110    786    173       C  
ATOM   4608  O   ASP A 591      20.278 125.662 223.891  1.00 37.73           O  
ANISOU 4608  O   ASP A 591     4695   5957   3685    118    842    123       O  
ATOM   4609  CB  ASP A 591      17.877 124.629 223.056  1.00 37.82           C  
ANISOU 4609  CB  ASP A 591     4563   6072   3736    191    862    215       C  
ATOM   4610  CG  ASP A 591      17.450 126.096 222.789  1.00 38.64           C  
ANISOU 4610  CG  ASP A 591     4656   6098   3929    255    912    236       C  
ATOM   4611  OD1 ASP A 591      17.805 126.713 221.746  1.00 38.67           O  
ANISOU 4611  OD1 ASP A 591     4646   6076   3970    272    880    288       O  
ATOM   4612  OD2 ASP A 591      16.707 126.636 223.669  1.00 40.94           O  
ANISOU 4612  OD2 ASP A 591     4956   6347   4251    292    992    200       O  
ATOM   4613  N   VAL A 592      21.563 124.580 222.373  1.00 36.65           N  
ANISOU 4613  N   VAL A 592     4517   5901   3508     71    727    180       N  
ATOM   4614  CA  VAL A 592      22.854 124.825 223.048  1.00 36.65           C  
ANISOU 4614  CA  VAL A 592     4576   5869   3480     20    708    123       C  
ATOM   4615  C   VAL A 592      23.196 126.288 223.250  1.00 37.32           C  
ANISOU 4615  C   VAL A 592     4701   5863   3615     20    747    101       C  
ATOM   4616  O   VAL A 592      23.496 126.714 224.371  1.00 37.73           O  
ANISOU 4616  O   VAL A 592     4816   5869   3650     -6    769     36       O  
ATOM   4617  CB  VAL A 592      24.015 124.137 222.316  1.00 36.08           C  
ANISOU 4617  CB  VAL A 592     4484   5844   3380    -16    641    139       C  
ATOM   4618  CG1 VAL A 592      25.184 123.864 223.229  1.00 36.04           C  
ANISOU 4618  CG1 VAL A 592     4523   5839   3332    -67    606     79       C  
ATOM   4619  CG2 VAL A 592      23.535 122.846 221.810  1.00 35.54           C  
ANISOU 4619  CG2 VAL A 592     4378   5850   3275     -6    611    173       C  
ATOM   4620  N   MET A 593      23.170 127.055 222.175  1.00 37.51           N  
ANISOU 4620  N   MET A 593     4699   5858   3697     43    753    156       N  
ATOM   4621  CA  MET A 593      23.418 128.477 222.299  1.00 38.26           C  
ANISOU 4621  CA  MET A 593     4838   5853   3844     44    793    142       C  
ATOM   4622  C   MET A 593      22.528 129.172 223.364  1.00 38.99           C  
ANISOU 4622  C   MET A 593     4976   5879   3960     81    866     96       C  
ATOM   4623  O   MET A 593      23.020 129.902 224.236  1.00 39.53           O  
ANISOU 4623  O   MET A 593     5117   5876   4025     49    893     32       O  
ATOM   4624  CB  MET A 593      23.266 129.142 220.936  1.00 38.46           C  
ANISOU 4624  CB  MET A 593     4831   5855   3925     74    793    223       C  
ATOM   4625  CG  MET A 593      24.221 128.606 219.918  1.00 37.92           C  
ANISOU 4625  CG  MET A 593     4733   5843   3832     32    737    260       C  
ATOM   4626  SD  MET A 593      25.875 129.161 220.334  1.00 38.13           S  
ANISOU 4626  SD  MET A 593     4806   5828   3854    -53    725    204       S  
ATOM   4627  CE  MET A 593      25.837 130.813 219.660  1.00 39.04           C  
ANISOU 4627  CE  MET A 593     4957   5832   4044    -42    770    247       C  
ATOM   4628  N   THR A 594      21.223 128.924 223.283  1.00 39.11           N  
ANISOU 4628  N   THR A 594     4945   5916   3996    146    900    127       N  
ATOM   4629  CA  THR A 594      20.239 129.657 224.085  1.00 39.96           C  
ANISOU 4629  CA  THR A 594     5079   5960   4144    199    985     95       C  
ATOM   4630  C   THR A 594      20.363 129.340 225.566  1.00 40.10           C  
ANISOU 4630  C   THR A 594     5164   5974   4097    160   1016      4       C  
ATOM   4631  O   THR A 594      20.322 130.239 226.405  1.00 40.90           O  
ANISOU 4631  O   THR A 594     5338   5990   4210    164   1077    -55       O  
ATOM   4632  CB  THR A 594      18.778 129.426 223.567  1.00 40.16           C  
ANISOU 4632  CB  THR A 594     5017   6024   4218    279   1011    156       C  
ATOM   4633  OG1 THR A 594      18.654 129.999 222.261  1.00 40.32           O  
ANISOU 4633  OG1 THR A 594     4994   6027   4299    319    984    240       O  
ATOM   4634  CG2 THR A 594      17.702 130.056 224.531  1.00 41.15           C  
ANISOU 4634  CG2 THR A 594     5157   6093   4385    340   1113    114       C  
ATOM   4635  N   THR A 595      20.532 128.057 225.863  1.00 39.39           N  
ANISOU 4635  N   THR A 595     5061   5972   3935    121    971     -6       N  
ATOM   4636  CA  THR A 595      20.693 127.596 227.210  1.00 39.50           C  
ANISOU 4636  CA  THR A 595     5144   5993   3873     79    986    -81       C  
ATOM   4637  C   THR A 595      22.040 128.008 227.712  1.00 39.60           C  
ANISOU 4637  C   THR A 595     5234   5964   3849     11    946   -135       C  
ATOM   4638  O   THR A 595      22.146 128.614 228.759  1.00 40.30           O  
ANISOU 4638  O   THR A 595     5407   5991   3913    -11    988   -205       O  
ATOM   4639  CB  THR A 595      20.544 126.107 227.269  1.00 38.78           C  
ANISOU 4639  CB  THR A 595     5019   6000   3717     57    942    -65       C  
ATOM   4640  OG1 THR A 595      19.213 125.794 226.838  1.00 38.85           O  
ANISOU 4640  OG1 THR A 595     4952   6046   3765    113    982    -17       O  
ATOM   4641  CG2 THR A 595      20.813 125.546 228.716  1.00 38.94           C  
ANISOU 4641  CG2 THR A 595     5126   6028   3643      6    947   -138       C  
ATOM   4642  N   MET A 596      23.070 127.745 226.940  1.00 39.03           N  
ANISOU 4642  N   MET A 596     5131   5923   3775    -25    868   -105       N  
ATOM   4643  CA  MET A 596      24.391 127.989 227.431  1.00 39.16           C  
ANISOU 4643  CA  MET A 596     5203   5917   3759    -97    820   -154       C  
ATOM   4644  C   MET A 596      24.751 129.452 227.689  1.00 40.04           C  
ANISOU 4644  C   MET A 596     5379   5922   3912   -116    859   -193       C  
ATOM   4645  O   MET A 596      25.712 129.720 228.421  1.00 40.40           O  
ANISOU 4645  O   MET A 596     5486   5942   3920   -185    826   -253       O  
ATOM   4646  CB  MET A 596      25.413 127.268 226.562  1.00 38.43           C  
ANISOU 4646  CB  MET A 596     5051   5892   3658   -128    734   -114       C  
ATOM   4647  CG  MET A 596      25.469 125.755 226.865  1.00 37.78           C  
ANISOU 4647  CG  MET A 596     4951   5899   3505   -137    682   -112       C  
ATOM   4648  SD  MET A 596      25.706 125.250 228.625  1.00 38.15           S  
ANISOU 4648  SD  MET A 596     5093   5949   3453   -184    665   -193       S  
ATOM   4649  CE  MET A 596      27.050 126.297 229.212  1.00 38.86           C  
ANISOU 4649  CE  MET A 596     5243   5979   3543   -256    628   -254       C  
ATOM   4650  N   CYS A 597      23.983 130.397 227.148  1.00 40.50           N  
ANISOU 4650  N   CYS A 597     5428   5914   4047    -57    925   -163       N  
ATOM   4651  CA  CYS A 597      24.311 131.807 227.361  1.00 41.43           C  
ANISOU 4651  CA  CYS A 597     5618   5916   4208    -75    965   -199       C  
ATOM   4652  C   CYS A 597      23.749 132.306 228.675  1.00 42.31           C  
ANISOU 4652  C   CYS A 597     5823   5959   4292    -68   1040   -280       C  
ATOM   4653  O   CYS A 597      24.204 133.313 229.221  1.00 43.16           O  
ANISOU 4653  O   CYS A 597     6020   5973   4405   -107   1065   -339       O  
ATOM   4654  CB  CYS A 597      23.780 132.679 226.233  1.00 41.73           C  
ANISOU 4654  CB  CYS A 597     5620   5896   4339    -11   1004   -128       C  
ATOM   4655  SG  CYS A 597      22.095 133.171 226.489  1.00 42.45           S  
ANISOU 4655  SG  CYS A 597     5709   5934   4485    100   1108   -121       S  
ATOM   4656  N   ASP A 598      22.753 131.584 229.162  1.00 42.17           N  
ANISOU 4656  N   ASP A 598     5788   5990   4244    -23   1079   -285       N  
ATOM   4657  CA  ASP A 598      21.852 132.019 230.245  1.00 43.08           C  
ANISOU 4657  CA  ASP A 598     5974   6048   4346     10   1179   -349       C  
ATOM   4658  C   ASP A 598      22.193 131.362 231.586  1.00 43.17           C  
ANISOU 4658  C   ASP A 598     6068   6093   4243    -57   1165   -427       C  
ATOM   4659  O   ASP A 598      21.988 130.175 231.758  1.00 42.53           O  
ANISOU 4659  O   ASP A 598     5950   6105   4106    -63   1134   -410       O  
ATOM   4660  CB  ASP A 598      20.422 131.626 229.832  1.00 42.98           C  
ANISOU 4660  CB  ASP A 598     5873   6077   4381    105   1239   -294       C  
ATOM   4661  CG  ASP A 598      19.378 131.929 230.879  1.00 43.94           C  
ANISOU 4661  CG  ASP A 598     6044   6156   4495    149   1355   -353       C  
ATOM   4662  OD1 ASP A 598      19.715 132.135 232.047  1.00 44.52           O  
ANISOU 4662  OD1 ASP A 598     6229   6189   4498     98   1384   -441       O  
ATOM   4663  OD2 ASP A 598      18.184 131.949 230.534  1.00 44.21           O  
ANISOU 4663  OD2 ASP A 598     6002   6201   4594    234   1419   -313       O  
ATOM   4664  N   PRO A 599      22.660 132.138 232.565  1.00 44.08           N  
ANISOU 4664  N   PRO A 599     6303   6127   4319   -109   1190   -513       N  
ATOM   4665  CA  PRO A 599      23.079 131.582 233.864  1.00 44.32           C  
ANISOU 4665  CA  PRO A 599     6428   6186   4228   -182   1164   -587       C  
ATOM   4666  C   PRO A 599      21.949 130.962 234.718  1.00 44.59           C  
ANISOU 4666  C   PRO A 599     6487   6252   4205   -146   1247   -612       C  
ATOM   4667  O   PRO A 599      22.218 130.198 235.655  1.00 44.61           O  
ANISOU 4667  O   PRO A 599     6551   6300   4097   -203   1215   -650       O  
ATOM   4668  CB  PRO A 599      23.638 132.794 234.574  1.00 45.47           C  
ANISOU 4668  CB  PRO A 599     6698   6218   4360   -235   1190   -671       C  
ATOM   4669  CG  PRO A 599      22.788 133.925 234.032  1.00 46.11           C  
ANISOU 4669  CG  PRO A 599     6769   6199   4550   -150   1296   -657       C  
ATOM   4670  CD  PRO A 599      22.699 133.608 232.563  1.00 45.11           C  
ANISOU 4670  CD  PRO A 599     6501   6127   4512    -98   1251   -548       C  
ATOM   4671  N   SER A 600      20.700 131.283 234.407  1.00 44.91           N  
ANISOU 4671  N   SER A 600     6476   6268   4319    -55   1353   -587       N  
ATOM   4672  CA  SER A 600      19.611 130.822 235.214  1.00 45.36           C  
ANISOU 4672  CA  SER A 600     6551   6350   4333    -24   1448   -615       C  
ATOM   4673  C   SER A 600      19.184 129.377 234.924  1.00 44.40           C  
ANISOU 4673  C   SER A 600     6337   6352   4182    -19   1408   -552       C  
ATOM   4674  O   SER A 600      18.542 128.748 235.795  1.00 44.73           O  
ANISOU 4674  O   SER A 600     6415   6429   4153    -28   1467   -581       O  
ATOM   4675  CB  SER A 600      18.444 131.738 235.045  1.00 46.25           C  
ANISOU 4675  CB  SER A 600     6637   6392   4544     74   1580   -616       C  
ATOM   4676  OG  SER A 600      17.808 131.433 233.836  1.00 45.59           O  
ANISOU 4676  OG  SER A 600     6405   6361   4557    147   1566   -519       O  
ATOM   4677  N   ILE A 601      19.514 128.833 233.745  1.00 43.32           N  
ANISOU 4677  N   ILE A 601     6092   6276   4092     -9   1317   -470       N  
ATOM   4678  CA  ILE A 601      19.126 127.448 233.484  1.00 42.50           C  
ANISOU 4678  CA  ILE A 601     5914   6280   3956    -11   1279   -416       C  
ATOM   4679  C   ILE A 601      19.976 126.440 234.291  1.00 42.16           C  
ANISOU 4679  C   ILE A 601     5947   6286   3786    -95   1198   -444       C  
ATOM   4680  O   ILE A 601      21.189 126.548 234.336  1.00 41.96           O  
ANISOU 4680  O   ILE A 601     5963   6250   3730   -148   1108   -462       O  
ATOM   4681  CB  ILE A 601      19.068 127.140 231.998  1.00 41.61           C  
ANISOU 4681  CB  ILE A 601     5671   6215   3924     28   1218   -323       C  
ATOM   4682  CG1 ILE A 601      18.201 128.197 231.288  1.00 42.15           C  
ANISOU 4682  CG1 ILE A 601     5675   6228   4113    115   1293   -291       C  
ATOM   4683  CG2 ILE A 601      18.501 125.727 231.785  1.00 40.95           C  
ANISOU 4683  CG2 ILE A 601     5520   6233   3807     25   1193   -275       C  
ATOM   4684  CD1 ILE A 601      18.409 128.336 229.741  1.00 41.50           C  
ANISOU 4684  CD1 ILE A 601     5493   6162   4113    148   1225   -204       C  
ATOM   4685  N   PRO A 602      19.325 125.484 234.981  1.00 42.24           N  
ANISOU 4685  N   PRO A 602     5977   6349   3724   -109   1231   -450       N  
ATOM   4686  CA  PRO A 602      20.056 124.720 236.020  1.00 42.30           C  
ANISOU 4686  CA  PRO A 602     6091   6381   3600   -186   1171   -488       C  
ATOM   4687  C   PRO A 602      21.508 124.213 235.815  1.00 41.63           C  
ANISOU 4687  C   PRO A 602     6019   6325   3474   -240   1021   -474       C  
ATOM   4688  O   PRO A 602      22.252 124.230 236.811  1.00 42.13           O  
ANISOU 4688  O   PRO A 602     6192   6372   3444   -301    978   -528       O  
ATOM   4689  CB  PRO A 602      19.080 123.613 236.423  1.00 42.30           C  
ANISOU 4689  CB  PRO A 602     6081   6443   3548   -187   1220   -468       C  
ATOM   4690  CG  PRO A 602      17.753 124.224 236.205  1.00 42.85           C  
ANISOU 4690  CG  PRO A 602     6086   6492   3703   -119   1353   -464       C  
ATOM   4691  CD  PRO A 602      17.865 125.320 235.151  1.00 42.71           C  
ANISOU 4691  CD  PRO A 602     5992   6426   3810    -60   1350   -441       C  
ATOM   4692  N   LEU A 603      21.962 123.797 234.638  1.00 40.69           N  
ANISOU 4692  N   LEU A 603     5797   6247   3415   -222    942   -409       N  
ATOM   4693  CA  LEU A 603      23.390 123.343 234.605  1.00 40.29           C  
ANISOU 4693  CA  LEU A 603     5762   6222   3323   -271    810   -406       C  
ATOM   4694  C   LEU A 603      24.400 124.205 233.803  1.00 40.12           C  
ANISOU 4694  C   LEU A 603     5695   6171   3377   -277    755   -400       C  
ATOM   4695  O   LEU A 603      25.535 123.811 233.581  1.00 39.79           O  
ANISOU 4695  O   LEU A 603     5635   6159   3323   -309    652   -388       O  
ATOM   4696  CB  LEU A 603      23.483 121.903 234.101  1.00 39.44           C  
ANISOU 4696  CB  LEU A 603     5599   6193   3195   -266    740   -345       C  
ATOM   4697  CG  LEU A 603      23.003 120.769 234.978  1.00 39.59           C  
ANISOU 4697  CG  LEU A 603     5681   6248   3114   -288    746   -346       C  
ATOM   4698  CD1 LEU A 603      23.031 119.465 234.202  1.00 38.75           C  
ANISOU 4698  CD1 LEU A 603     5507   6204   3012   -274    685   -280       C  
ATOM   4699  CD2 LEU A 603      23.921 120.704 236.071  1.00 40.14           C  
ANISOU 4699  CD2 LEU A 603     5859   6304   3087   -345    681   -393       C  
ATOM   4700  N   THR A 604      23.973 125.363 233.344  1.00 40.43           N  
ANISOU 4700  N   THR A 604     5713   6149   3498   -243    827   -405       N  
ATOM   4701  CA  THR A 604      24.770 126.206 232.459  1.00 40.31           C  
ANISOU 4701  CA  THR A 604     5653   6102   3563   -247    792   -389       C  
ATOM   4702  C   THR A 604      26.166 126.608 233.018  1.00 40.75           C  
ANISOU 4702  C   THR A 604     5768   6134   3580   -325    712   -440       C  
ATOM   4703  O   THR A 604      27.194 126.371 232.378  1.00 40.32           O  
ANISOU 4703  O   THR A 604     5656   6115   3550   -349    626   -411       O  
ATOM   4704  CB  THR A 604      23.927 127.433 232.002  1.00 40.78           C  
ANISOU 4704  CB  THR A 604     5699   6085   3712   -193    893   -385       C  
ATOM   4705  OG1 THR A 604      22.717 126.966 231.386  1.00 40.40           O  
ANISOU 4705  OG1 THR A 604     5572   6074   3705   -123    946   -329       O  
ATOM   4706  CG2 THR A 604      24.680 128.300 231.049  1.00 40.74           C  
ANISOU 4706  CG2 THR A 604     5654   6039   3785   -200    863   -361       C  
ATOM   4707  N   THR A 605      26.220 127.203 234.207  1.00 41.69           N  
ANISOU 4707  N   THR A 605     6002   6198   3640   -369    738   -516       N  
ATOM   4708  CA  THR A 605      27.509 127.727 234.707  1.00 42.28           C  
ANISOU 4708  CA  THR A 605     6132   6247   3685   -451    659   -567       C  
ATOM   4709  C   THR A 605      28.557 126.637 234.978  1.00 41.96           C  
ANISOU 4709  C   THR A 605     6074   6288   3580   -496    529   -554       C  
ATOM   4710  O   THR A 605      29.737 126.853 234.730  1.00 42.06           O  
ANISOU 4710  O   THR A 605     6053   6311   3616   -543    444   -556       O  
ATOM   4711  CB  THR A 605      27.370 128.677 235.925  1.00 43.51           C  
ANISOU 4711  CB  THR A 605     6430   6319   3785   -496    713   -659       C  
ATOM   4712  OG1 THR A 605      26.864 127.943 237.034  1.00 43.80           O  
ANISOU 4712  OG1 THR A 605     6550   6383   3710   -505    729   -690       O  
ATOM   4713  CG2 THR A 605      26.449 129.879 235.612  1.00 44.00           C  
ANISOU 4713  CG2 THR A 605     6508   6284   3926   -444    842   -673       C  
ATOM   4714  N   GLY A 606      28.139 125.472 235.475  1.00 41.67           N  
ANISOU 4714  N   GLY A 606     6057   6308   3467   -480    514   -539       N  
ATOM   4715  CA  GLY A 606      29.052 124.340 235.542  1.00 41.31           C  
ANISOU 4715  CA  GLY A 606     5982   6338   3378   -501    392   -511       C  
ATOM   4716  C   GLY A 606      29.726 124.147 234.191  1.00 40.54           C  
ANISOU 4716  C   GLY A 606     5751   6279   3374   -475    343   -452       C  
ATOM   4717  O   GLY A 606      30.963 124.173 234.102  1.00 40.73           O  
ANISOU 4717  O   GLY A 606     5739   6324   3410   -516    250   -456       O  
ATOM   4718  N   GLU A 607      28.901 123.994 233.146  1.00 39.80           N  
ANISOU 4718  N   GLU A 607     5583   6193   3346   -411    410   -399       N  
ATOM   4719  CA  GLU A 607      29.335 123.668 231.765  1.00 39.03           C  
ANISOU 4719  CA  GLU A 607     5366   6137   3326   -380    380   -336       C  
ATOM   4720  C   GLU A 607      29.886 124.795 230.889  1.00 39.15           C  
ANISOU 4720  C   GLU A 607     5329   6115   3433   -393    393   -329       C  
ATOM   4721  O   GLU A 607      30.146 124.573 229.707  1.00 38.59           O  
ANISOU 4721  O   GLU A 607     5167   6075   3420   -367    383   -277       O  
ATOM   4722  CB  GLU A 607      28.203 122.967 230.998  1.00 38.27           C  
ANISOU 4722  CB  GLU A 607     5221   6071   3251   -313    435   -279       C  
ATOM   4723  CG  GLU A 607      27.934 121.611 231.608  1.00 38.06           C  
ANISOU 4723  CG  GLU A 607     5226   6092   3142   -308    402   -271       C  
ATOM   4724  CD  GLU A 607      26.814 120.830 230.995  1.00 37.45           C  
ANISOU 4724  CD  GLU A 607     5109   6046   3074   -258    450   -221       C  
ATOM   4725  OE1 GLU A 607      26.196 121.261 230.004  1.00 37.14           O  
ANISOU 4725  OE1 GLU A 607     5006   6000   3106   -222    504   -187       O  
ATOM   4726  OE2 GLU A 607      26.547 119.754 231.550  1.00 37.38           O  
ANISOU 4726  OE2 GLU A 607     5139   6067   2995   -261    430   -216       O  
ATOM   4727  N   TRP A 608      30.059 125.994 231.438  1.00 39.96           N  
ANISOU 4727  N   TRP A 608     5495   6146   3543   -437    420   -383       N  
ATOM   4728  CA  TRP A 608      30.926 126.942 230.782  1.00 40.25           C  
ANISOU 4728  CA  TRP A 608     5491   6151   3652   -475    406   -381       C  
ATOM   4729  C   TRP A 608      32.353 126.354 230.689  1.00 40.24           C  
ANISOU 4729  C   TRP A 608     5427   6216   3647   -521    295   -376       C  
ATOM   4730  O   TRP A 608      33.147 126.748 229.843  1.00 40.26           O  
ANISOU 4730  O   TRP A 608     5356   6224   3716   -543    278   -354       O  
ATOM   4731  CB  TRP A 608      30.915 128.306 231.471  1.00 41.26           C  
ANISOU 4731  CB  TRP A 608     5711   6182   3783   -524    450   -446       C  
ATOM   4732  CG  TRP A 608      29.660 129.070 231.270  1.00 41.38           C  
ANISOU 4732  CG  TRP A 608     5762   6124   3837   -468    565   -442       C  
ATOM   4733  CD1 TRP A 608      28.705 128.842 230.325  1.00 40.73           C  
ANISOU 4733  CD1 TRP A 608     5616   6054   3803   -388    623   -378       C  
ATOM   4734  CD2 TRP A 608      29.222 130.218 232.008  1.00 42.35           C  
ANISOU 4734  CD2 TRP A 608     5990   6145   3955   -485    637   -505       C  
ATOM   4735  NE1 TRP A 608      27.699 129.769 230.429  1.00 41.23           N  
ANISOU 4735  NE1 TRP A 608     5729   6036   3902   -347    722   -391       N  
ATOM   4736  CE2 TRP A 608      27.993 130.620 231.463  1.00 42.23           C  
ANISOU 4736  CE2 TRP A 608     5962   6087   3997   -402    738   -471       C  
ATOM   4737  CE3 TRP A 608      29.750 130.949 233.076  1.00 43.40           C  
ANISOU 4737  CE3 TRP A 608     6230   6217   4042   -563    624   -588       C  
ATOM   4738  CZ2 TRP A 608      27.295 131.724 231.947  1.00 43.13           C  
ANISOU 4738  CZ2 TRP A 608     6163   6096   4131   -385    833   -518       C  
ATOM   4739  CZ3 TRP A 608      29.062 132.040 233.543  1.00 44.27           C  
ANISOU 4739  CZ3 TRP A 608     6436   6220   4163   -554    720   -638       C  
ATOM   4740  CH2 TRP A 608      27.849 132.420 232.983  1.00 44.14           C  
ANISOU 4740  CH2 TRP A 608     6401   6158   4210   -461    827   -603       C  
ATOM   4741  N   GLU A 609      32.688 125.407 231.553  1.00 40.31           N  
ANISOU 4741  N   GLU A 609     5463   6275   3579   -533    220   -394       N  
ATOM   4742  CA  GLU A 609      33.974 124.701 231.430  1.00 40.34           C  
ANISOU 4742  CA  GLU A 609     5393   6349   3586   -556    112   -380       C  
ATOM   4743  C   GLU A 609      33.830 123.321 230.796  1.00 39.47           C  
ANISOU 4743  C   GLU A 609     5217   6309   3473   -488     91   -322       C  
ATOM   4744  O   GLU A 609      34.592 122.431 231.073  1.00 39.56           O  
ANISOU 4744  O   GLU A 609     5199   6374   3457   -488      4   -316       O  
ATOM   4745  CB  GLU A 609      34.675 124.599 232.785  1.00 41.22           C  
ANISOU 4745  CB  GLU A 609     5573   6468   3620   -619     20   -435       C  
ATOM   4746  CG  GLU A 609      35.323 125.861 233.228  1.00 42.21           C  
ANISOU 4746  CG  GLU A 609     5736   6542   3762   -706      5   -491       C  
ATOM   4747  CD  GLU A 609      36.133 125.643 234.493  1.00 43.15           C  
ANISOU 4747  CD  GLU A 609     5912   6685   3800   -773   -109   -539       C  
ATOM   4748  OE1 GLU A 609      36.195 124.477 234.949  1.00 42.98           O  
ANISOU 4748  OE1 GLU A 609     5895   6719   3715   -742   -175   -519       O  
ATOM   4749  OE2 GLU A 609      36.707 126.624 235.041  1.00 44.15           O  
ANISOU 4749  OE2 GLU A 609     6083   6770   3922   -860   -137   -595       O  
ATOM   4750  N   GLU A 610      32.830 123.149 229.961  1.00 38.74           N  
ANISOU 4750  N   GLU A 610     5103   6211   3407   -430    170   -280       N  
ATOM   4751  CA  GLU A 610      32.677 121.911 229.221  1.00 37.98           C  
ANISOU 4751  CA  GLU A 610     4947   6172   3311   -372    156   -228       C  
ATOM   4752  C   GLU A 610      32.586 122.263 227.725  1.00 37.50           C  
ANISOU 4752  C   GLU A 610     4804   6114   3331   -344    209   -181       C  
ATOM   4753  O   GLU A 610      33.517 122.002 226.991  1.00 37.43           O  
ANISOU 4753  O   GLU A 610     4718   6144   3362   -346    175   -160       O  
ATOM   4754  CB  GLU A 610      31.473 121.092 229.728  1.00 37.62           C  
ANISOU 4754  CB  GLU A 610     4966   6131   3199   -334    188   -219       C  
ATOM   4755  CG  GLU A 610      31.141 119.839 228.947  1.00 36.89           C  
ANISOU 4755  CG  GLU A 610     4826   6086   3103   -281    183   -167       C  
ATOM   4756  CD  GLU A 610      32.149 118.696 229.131  1.00 36.93           C  
ANISOU 4756  CD  GLU A 610     4810   6141   3082   -274     88   -159       C  
ATOM   4757  OE1 GLU A 610      32.975 118.782 230.060  1.00 37.57           O  
ANISOU 4757  OE1 GLU A 610     4920   6223   3132   -310     17   -192       O  
ATOM   4758  OE2 GLU A 610      32.094 117.694 228.363  1.00 36.42           O  
ANISOU 4758  OE2 GLU A 610     4703   6110   3024   -230     81   -119       O  
ATOM   4759  N   TRP A 611      31.500 122.873 227.274  1.00 37.28           N  
ANISOU 4759  N   TRP A 611     4793   6046   3328   -320    293   -163       N  
ATOM   4760  CA  TRP A 611      31.389 123.205 225.869  1.00 36.94           C  
ANISOU 4760  CA  TRP A 611     4683   6003   3349   -295    335   -113       C  
ATOM   4761  C   TRP A 611      32.144 124.489 225.633  1.00 37.52           C  
ANISOU 4761  C   TRP A 611     4745   6032   3480   -345    347   -128       C  
ATOM   4762  O   TRP A 611      32.792 124.628 224.618  1.00 37.47           O  
ANISOU 4762  O   TRP A 611     4673   6044   3520   -353    347    -96       O  
ATOM   4763  CB  TRP A 611      29.917 123.387 225.472  1.00 36.62           C  
ANISOU 4763  CB  TRP A 611     4660   5938   3317   -247    409    -82       C  
ATOM   4764  CG  TRP A 611      29.042 122.595 226.327  1.00 36.46           C  
ANISOU 4764  CG  TRP A 611     4688   5932   3235   -226    413    -96       C  
ATOM   4765  CD1 TRP A 611      28.266 123.056 227.336  1.00 36.87           C  
ANISOU 4765  CD1 TRP A 611     4810   5940   3259   -229    457   -133       C  
ATOM   4766  CD2 TRP A 611      28.901 121.174 226.320  1.00 35.98           C  
ANISOU 4766  CD2 TRP A 611     4616   5928   3125   -204    376    -76       C  
ATOM   4767  NE1 TRP A 611      27.629 122.018 227.952  1.00 36.66           N  
ANISOU 4767  NE1 TRP A 611     4814   5946   3170   -215    452   -135       N  
ATOM   4768  CE2 TRP A 611      27.997 120.846 227.341  1.00 36.10           C  
ANISOU 4768  CE2 TRP A 611     4698   5935   3086   -200    400    -99       C  
ATOM   4769  CE3 TRP A 611      29.460 120.144 225.554  1.00 35.53           C  
ANISOU 4769  CE3 TRP A 611     4508   5926   3066   -188    331    -44       C  
ATOM   4770  CZ2 TRP A 611      27.629 119.527 227.624  1.00 35.80           C  
ANISOU 4770  CZ2 TRP A 611     4676   5937   2988   -187    376    -86       C  
ATOM   4771  CZ3 TRP A 611      29.076 118.825 225.822  1.00 35.22           C  
ANISOU 4771  CZ3 TRP A 611     4488   5921   2971   -168    306    -34       C  
ATOM   4772  CH2 TRP A 611      28.174 118.537 226.852  1.00 35.35           C  
ANISOU 4772  CH2 TRP A 611     4572   5925   2933   -171    326    -53       C  
ATOM   4773  N   GLY A 612      32.067 125.389 226.613  1.00 38.17           N  
ANISOU 4773  N   GLY A 612     4899   6053   3552   -384    359   -179       N  
ATOM   4774  CA  GLY A 612      32.492 126.770 226.509  1.00 38.86           C  
ANISOU 4774  CA  GLY A 612     5002   6072   3690   -434    386   -198       C  
ATOM   4775  C   GLY A 612      31.328 127.642 226.969  1.00 39.17           C  
ANISOU 4775  C   GLY A 612     5124   6029   3730   -413    463   -218       C  
ATOM   4776  O   GLY A 612      30.313 127.105 227.409  1.00 38.88           O  
ANISOU 4776  O   GLY A 612     5119   6001   3652   -365    489   -219       O  
ATOM   4777  N   ASN A 613      31.487 128.972 226.851  1.00 39.85           N  
ANISOU 4777  N   ASN A 613     5244   6033   3865   -447    503   -233       N  
ATOM   4778  CA  ASN A 613      30.496 130.000 227.208  1.00 40.37           C  
ANISOU 4778  CA  ASN A 613     5389   6002   3949   -424    584   -254       C  
ATOM   4779  C   ASN A 613      30.191 130.948 226.030  1.00 40.51           C  
ANISOU 4779  C   ASN A 613     5386   5960   4048   -397    643   -198       C  
ATOM   4780  O   ASN A 613      31.045 131.735 225.634  1.00 41.00           O  
ANISOU 4780  O   ASN A 613     5445   5983   4151   -455    637   -197       O  
ATOM   4781  CB  ASN A 613      31.067 130.822 228.333  1.00 41.35           C  
ANISOU 4781  CB  ASN A 613     5602   6061   4050   -500    573   -335       C  
ATOM   4782  CG  ASN A 613      30.142 131.903 228.803  1.00 42.06           C  
ANISOU 4782  CG  ASN A 613     5786   6041   4156   -477    662   -369       C  
ATOM   4783  OD1 ASN A 613      29.023 132.070 228.315  1.00 41.87           O  
ANISOU 4783  OD1 ASN A 613     5753   5989   4166   -396    733   -329       O  
ATOM   4784  ND2 ASN A 613      30.602 132.639 229.789  1.00 43.01           N  
ANISOU 4784  ND2 ASN A 613     5998   6096   4248   -548    657   -446       N  
ATOM   4785  N   PRO A 614      28.971 130.903 225.477  1.00 40.20           N  
ANISOU 4785  N   PRO A 614     5331   5911   4030   -313    698   -148       N  
ATOM   4786  CA  PRO A 614      28.801 131.654 224.247  1.00 40.33           C  
ANISOU 4786  CA  PRO A 614     5321   5885   4116   -288    734    -81       C  
ATOM   4787  C   PRO A 614      28.601 133.133 224.453  1.00 41.33           C  
ANISOU 4787  C   PRO A 614     5527   5883   4294   -296    794   -102       C  
ATOM   4788  O   PRO A 614      28.408 133.859 223.491  1.00 41.60           O  
ANISOU 4788  O   PRO A 614     5554   5866   4386   -272    826    -43       O  
ATOM   4789  CB  PRO A 614      27.578 131.013 223.597  1.00 39.73           C  
ANISOU 4789  CB  PRO A 614     5196   5853   4044   -197    756    -18       C  
ATOM   4790  CG  PRO A 614      26.803 130.462 224.713  1.00 39.65           C  
ANISOU 4790  CG  PRO A 614     5217   5860   3988   -169    772    -65       C  
ATOM   4791  CD  PRO A 614      27.804 130.054 225.772  1.00 39.71           C  
ANISOU 4791  CD  PRO A 614     5260   5893   3934   -243    719   -138       C  
ATOM   4792  N   ASN A 615      28.683 133.600 225.685  1.00 41.99           N  
ANISOU 4792  N   ASN A 615     5694   5908   4352   -331    809   -184       N  
ATOM   4793  CA  ASN A 615      28.759 135.038 225.935  1.00 43.10           C  
ANISOU 4793  CA  ASN A 615     5922   5916   4537   -359    861   -217       C  
ATOM   4794  C   ASN A 615      30.141 135.609 225.577  1.00 43.53           C  
ANISOU 4794  C   ASN A 615     5976   5948   4614   -464    821   -223       C  
ATOM   4795  O   ASN A 615      30.395 136.810 225.729  1.00 44.52           O  
ANISOU 4795  O   ASN A 615     6178   5960   4777   -508    855   -250       O  
ATOM   4796  CB  ASN A 615      28.447 135.311 227.409  1.00 43.76           C  
ANISOU 4796  CB  ASN A 615     6107   5946   4575   -374    891   -313       C  
ATOM   4797  CG  ASN A 615      27.006 134.989 227.767  1.00 43.63           C  
ANISOU 4797  CG  ASN A 615     6096   5932   4550   -272    956   -311       C  
ATOM   4798  OD1 ASN A 615      26.067 135.645 227.273  1.00 43.99           O  
ANISOU 4798  OD1 ASN A 615     6144   5910   4660   -191   1026   -271       O  
ATOM   4799  ND2 ASN A 615      26.815 133.980 228.629  1.00 43.22           N  
ANISOU 4799  ND2 ASN A 615     6045   5956   4419   -274    933   -349       N  
ATOM   4800  N   GLU A 616      31.038 134.742 225.119  1.00 42.87           N  
ANISOU 4800  N   GLU A 616     5806   5971   4513   -505    752   -198       N  
ATOM   4801  CA  GLU A 616      32.415 135.117 224.848  1.00 43.31           C  
ANISOU 4801  CA  GLU A 616     5839   6029   4589   -609    711   -207       C  
ATOM   4802  C   GLU A 616      32.798 134.966 223.375  1.00 42.92           C  
ANISOU 4802  C   GLU A 616     5704   6023   4580   -604    711   -120       C  
ATOM   4803  O   GLU A 616      32.457 133.945 222.737  1.00 42.00           O  
ANISOU 4803  O   GLU A 616     5514   5997   4445   -542    696    -68       O  
ATOM   4804  CB  GLU A 616      33.326 134.222 225.658  1.00 43.11           C  
ANISOU 4804  CB  GLU A 616     5778   6096   4506   -669    626   -261       C  
ATOM   4805  CG  GLU A 616      32.960 134.107 227.102  1.00 43.41           C  
ANISOU 4805  CG  GLU A 616     5899   6115   4480   -673    615   -341       C  
ATOM   4806  CD  GLU A 616      34.084 133.570 227.964  1.00 43.64           C  
ANISOU 4806  CD  GLU A 616     5914   6211   4459   -758    519   -398       C  
ATOM   4807  OE1 GLU A 616      35.003 132.922 227.444  1.00 43.31           O  
ANISOU 4807  OE1 GLU A 616     5771   6256   4427   -785    458   -368       O  
ATOM   4808  OE2 GLU A 616      34.051 133.792 229.193  1.00 44.27           O  
ANISOU 4808  OE2 GLU A 616     6083   6254   4483   -796    504   -473       O  
ATOM   4809  N   TYR A 617      33.543 135.934 222.831  1.00 43.68           N  
ANISOU 4809  N   TYR A 617     5812   6057   4726   -677    729   -105       N  
ATOM   4810  CA  TYR A 617      34.039 135.781 221.465  1.00 43.44           C  
ANISOU 4810  CA  TYR A 617     5706   6073   4725   -687    733    -26       C  
ATOM   4811  C   TYR A 617      34.744 134.432 221.221  1.00 42.63           C  
ANISOU 4811  C   TYR A 617     5494   6116   4589   -692    674    -19       C  
ATOM   4812  O   TYR A 617      34.620 133.842 220.177  1.00 42.05           O  
ANISOU 4812  O   TYR A 617     5361   6104   4514   -649    682     46       O  
ATOM   4813  CB  TYR A 617      35.005 136.885 221.107  1.00 44.47           C  
ANISOU 4813  CB  TYR A 617     5859   6133   4906   -792    752    -25       C  
ATOM   4814  CG  TYR A 617      34.503 138.284 221.272  1.00 45.46           C  
ANISOU 4814  CG  TYR A 617     6100   6101   5070   -799    812    -30       C  
ATOM   4815  CD1 TYR A 617      33.535 138.807 220.421  1.00 45.52           C  
ANISOU 4815  CD1 TYR A 617     6147   6039   5110   -717    869     46       C  
ATOM   4816  CD2 TYR A 617      35.038 139.115 222.259  1.00 46.46           C  
ANISOU 4816  CD2 TYR A 617     6303   6145   5205   -891    807   -112       C  
ATOM   4817  CE1 TYR A 617      33.088 140.114 220.573  1.00 46.55           C  
ANISOU 4817  CE1 TYR A 617     6390   6015   5284   -715    925     43       C  
ATOM   4818  CE2 TYR A 617      34.614 140.418 222.409  1.00 47.49           C  
ANISOU 4818  CE2 TYR A 617     6551   6118   5374   -898    866   -122       C  
ATOM   4819  CZ  TYR A 617      33.646 140.920 221.559  1.00 47.54           C  
ANISOU 4819  CZ  TYR A 617     6594   6050   5417   -807    928    -43       C  
ATOM   4820  OH  TYR A 617      33.214 142.222 221.718  1.00 48.66           O  
ANISOU 4820  OH  TYR A 617     6859   6027   5604   -804    989    -51       O  
ATOM   4821  N   LYS A 618      35.487 133.950 222.194  1.00 42.71           N  
ANISOU 4821  N   LYS A 618     5481   6175   4570   -744    612    -87       N  
ATOM   4822  CA  LYS A 618      36.268 132.740 222.028  1.00 42.16           C  
ANISOU 4822  CA  LYS A 618     5308   6232   4479   -748    554    -84       C  
ATOM   4823  C   LYS A 618      35.406 131.570 221.652  1.00 41.07           C  
ANISOU 4823  C   LYS A 618     5140   6164   4302   -644    552    -44       C  
ATOM   4824  O   LYS A 618      35.896 130.674 221.011  1.00 40.62           O  
ANISOU 4824  O   LYS A 618     5001   6195   4238   -631    530    -16       O  
ATOM   4825  CB  LYS A 618      37.049 132.431 223.321  1.00 42.53           C  
ANISOU 4825  CB  LYS A 618     5351   6313   4496   -809    476   -164       C  
ATOM   4826  CG  LYS A 618      37.835 131.090 223.413  1.00 42.09           C  
ANISOU 4826  CG  LYS A 618     5192   6383   4415   -800    402   -168       C  
ATOM   4827  CD  LYS A 618      38.673 131.023 224.761  1.00 42.77           C  
ANISOU 4827  CD  LYS A 618     5286   6490   4476   -873    314   -245       C  
ATOM   4828  CE  LYS A 618      39.355 129.667 225.085  1.00 42.46           C  
ANISOU 4828  CE  LYS A 618     5159   6566   4408   -851    227   -252       C  
ATOM   4829  NZ  LYS A 618      40.539 129.435 224.230  1.00 42.74           N  
ANISOU 4829  NZ  LYS A 618     5066   6672   4503   -884    214   -224       N  
ATOM   4830  N   PHE A 619      34.121 131.600 222.011  1.00 40.76           N  
ANISOU 4830  N   PHE A 619     5164   6082   4239   -573    580    -43       N  
ATOM   4831  CA  PHE A 619      33.237 130.405 221.959  1.00 39.81           C  
ANISOU 4831  CA  PHE A 619     5021   6030   4074   -486    569    -20       C  
ATOM   4832  C   PHE A 619      31.918 130.527 221.199  1.00 39.46           C  
ANISOU 4832  C   PHE A 619     4994   5960   4040   -404    622     42       C  
ATOM   4833  O   PHE A 619      31.351 129.510 220.784  1.00 38.72           O  
ANISOU 4833  O   PHE A 619     4862   5934   3917   -346    610     76       O  
ATOM   4834  CB  PHE A 619      32.871 129.977 223.370  1.00 39.75           C  
ANISOU 4834  CB  PHE A 619     5063   6027   4015   -477    538    -85       C  
ATOM   4835  CG  PHE A 619      33.931 129.219 224.075  1.00 39.78           C  
ANISOU 4835  CG  PHE A 619     5032   6099   3984   -524    461   -130       C  
ATOM   4836  CD1 PHE A 619      34.304 127.956 223.647  1.00 39.15           C  
ANISOU 4836  CD1 PHE A 619     4875   6115   3883   -496    418   -104       C  
ATOM   4837  CD2 PHE A 619      34.549 129.768 225.204  1.00 40.56           C  
ANISOU 4837  CD2 PHE A 619     5180   6162   4070   -597    426   -200       C  
ATOM   4838  CE1 PHE A 619      35.273 127.261 224.339  1.00 39.30           C  
ANISOU 4838  CE1 PHE A 619     4862   6193   3877   -529    341   -142       C  
ATOM   4839  CE2 PHE A 619      35.530 129.082 225.899  1.00 40.73           C  
ANISOU 4839  CE2 PHE A 619     5167   6248   4059   -639    341   -237       C  
ATOM   4840  CZ  PHE A 619      35.894 127.838 225.478  1.00 40.11           C  
ANISOU 4840  CZ  PHE A 619     5007   6265   3968   -601    297   -206       C  
ATOM   4841  N   PHE A 620      31.412 131.755 221.060  1.00 40.09           N  
ANISOU 4841  N   PHE A 620     5131   5938   4162   -398    675     57       N  
ATOM   4842  CA  PHE A 620      30.223 132.044 220.208  1.00 39.99           C  
ANISOU 4842  CA  PHE A 620     5127   5894   4173   -319    720    128       C  
ATOM   4843  C   PHE A 620      30.161 131.222 218.904  1.00 39.35           C  
ANISOU 4843  C   PHE A 620     4978   5897   4078   -288    705    202       C  
ATOM   4844  O   PHE A 620      29.386 130.283 218.831  1.00 38.71           O  
ANISOU 4844  O   PHE A 620     4869   5876   3964   -231    690    219       O  
ATOM   4845  CB  PHE A 620      30.081 133.550 219.898  1.00 40.93           C  
ANISOU 4845  CB  PHE A 620     5309   5890   4352   -329    773    150       C  
ATOM   4846  CG  PHE A 620      28.812 133.899 219.215  1.00 41.01           C  
ANISOU 4846  CG  PHE A 620     5330   5861   4390   -239    811    220       C  
ATOM   4847  CD1 PHE A 620      27.625 133.999 219.943  1.00 41.11           C  
ANISOU 4847  CD1 PHE A 620     5372   5839   4410   -166    839    199       C  
ATOM   4848  CD2 PHE A 620      28.781 134.090 217.845  1.00 41.06           C  
ANISOU 4848  CD2 PHE A 620     5314   5873   4414   -225    816    309       C  
ATOM   4849  CE1 PHE A 620      26.389 134.309 219.291  1.00 41.31           C  
ANISOU 4849  CE1 PHE A 620     5390   5834   4471    -74    869    270       C  
ATOM   4850  CE2 PHE A 620      27.579 134.402 217.172  1.00 41.24           C  
ANISOU 4850  CE2 PHE A 620     5343   5865   4463   -138    837    382       C  
ATOM   4851  CZ  PHE A 620      26.372 134.517 217.902  1.00 41.38           C  
ANISOU 4851  CZ  PHE A 620     5376   5848   4499    -59    860    363       C  
ATOM   4852  N   ASP A 621      30.994 131.548 217.916  1.00 39.61           N  
ANISOU 4852  N   ASP A 621     4988   5932   4129   -334    711    242       N  
ATOM   4853  CA  ASP A 621      30.923 130.903 216.587  1.00 39.19           C  
ANISOU 4853  CA  ASP A 621     4888   5947   4056   -309    707    314       C  
ATOM   4854  C   ASP A 621      31.020 129.384 216.571  1.00 38.34           C  
ANISOU 4854  C   ASP A 621     4723   5950   3895   -288    665    301       C  
ATOM   4855  O   ASP A 621      30.257 128.684 215.868  1.00 37.88           O  
ANISOU 4855  O   ASP A 621     4646   5938   3807   -236    658    347       O  
ATOM   4856  CB  ASP A 621      31.943 131.476 215.595  1.00 39.72           C  
ANISOU 4856  CB  ASP A 621     4945   6003   4144   -374    730    351       C  
ATOM   4857  CG  ASP A 621      31.824 130.844 214.201  1.00 39.41           C  
ANISOU 4857  CG  ASP A 621     4872   6029   4072   -350    734    423       C  
ATOM   4858  OD1 ASP A 621      32.386 129.728 213.995  1.00 39.19           O  
ANISOU 4858  OD1 ASP A 621     4789   6094   4008   -357    711    407       O  
ATOM   4859  OD2 ASP A 621      31.170 131.439 213.298  1.00 39.74           O  
ANISOU 4859  OD2 ASP A 621     4949   6030   4121   -322    757    497       O  
ATOM   4860  N   TYR A 622      31.981 128.884 217.320  1.00 38.25           N  
ANISOU 4860  N   TYR A 622     4684   5977   3872   -332    634    239       N  
ATOM   4861  CA  TYR A 622      32.239 127.451 217.342  1.00 37.58           C  
ANISOU 4861  CA  TYR A 622     4550   5988   3742   -313    593    224       C  
ATOM   4862  C   TYR A 622      31.009 126.660 217.764  1.00 36.99           C  
ANISOU 4862  C   TYR A 622     4490   5934   3628   -247    577    224       C  
ATOM   4863  O   TYR A 622      30.576 125.775 217.045  1.00 36.51           O  
ANISOU 4863  O   TYR A 622     4407   5929   3536   -211    569    260       O  
ATOM   4864  CB  TYR A 622      33.393 127.129 218.281  1.00 37.74           C  
ANISOU 4864  CB  TYR A 622     4542   6036   3762   -362    552    158       C  
ATOM   4865  CG  TYR A 622      33.900 125.754 218.106  1.00 37.27           C  
ANISOU 4865  CG  TYR A 622     4426   6066   3668   -343    514    151       C  
ATOM   4866  CD1 TYR A 622      33.374 124.708 218.823  1.00 36.73           C  
ANISOU 4866  CD1 TYR A 622     4370   6032   3555   -300    476    128       C  
ATOM   4867  CD2 TYR A 622      34.935 125.499 217.227  1.00 37.46           C  
ANISOU 4867  CD2 TYR A 622     4389   6137   3707   -368    523    167       C  
ATOM   4868  CE1 TYR A 622      33.862 123.429 218.661  1.00 36.39           C  
ANISOU 4868  CE1 TYR A 622     4284   6060   3483   -279    442    122       C  
ATOM   4869  CE2 TYR A 622      35.433 124.217 217.061  1.00 37.14           C  
ANISOU 4869  CE2 TYR A 622     4298   6172   3641   -342    494    158       C  
ATOM   4870  CZ  TYR A 622      34.888 123.193 217.778  1.00 36.60           C  
ANISOU 4870  CZ  TYR A 622     4249   6129   3529   -295    451    136       C  
ATOM   4871  OH  TYR A 622      35.364 121.927 217.602  1.00 36.37           O  
ANISOU 4871  OH  TYR A 622     4180   6162   3476   -265    424    129       O  
ATOM   4872  N   MET A 623      30.460 126.993 218.930  1.00 37.11           N  
ANISOU 4872  N   MET A 623     4549   5906   3645   -238    578    182       N  
ATOM   4873  CA  MET A 623      29.273 126.353 219.425  1.00 36.70           C  
ANISOU 4873  CA  MET A 623     4512   5870   3562   -184    576    179       C  
ATOM   4874  C   MET A 623      28.118 126.511 218.458  1.00 36.62           C  
ANISOU 4874  C   MET A 623     4495   5855   3565   -131    603    248       C  
ATOM   4875  O   MET A 623      27.343 125.593 218.226  1.00 36.17           O  
ANISOU 4875  O   MET A 623     4417   5849   3476    -94    589    270       O  
ATOM   4876  CB  MET A 623      28.927 126.955 220.769  1.00 37.09           C  
ANISOU 4876  CB  MET A 623     4617   5859   3614   -190    591    122       C  
ATOM   4877  CG  MET A 623      29.931 126.577 221.847  1.00 37.17           C  
ANISOU 4877  CG  MET A 623     4640   5889   3594   -241    546     54       C  
ATOM   4878  SD  MET A 623      29.310 126.919 223.492  1.00 37.57           S  
ANISOU 4878  SD  MET A 623     4770   5887   3616   -243    562    -16       S  
ATOM   4879  CE  MET A 623      30.475 128.166 223.874  1.00 38.42           C  
ANISOU 4879  CE  MET A 623     4912   5928   3759   -322    557    -61       C  
ATOM   4880  N   ASN A 624      28.012 127.680 217.869  1.00 37.17           N  
ANISOU 4880  N   ASN A 624     4581   5860   3680   -130    637    286       N  
ATOM   4881  CA  ASN A 624      27.003 127.887 216.880  1.00 37.24           C  
ANISOU 4881  CA  ASN A 624     4581   5865   3703    -80    651    360       C  
ATOM   4882  C   ASN A 624      27.024 126.837 215.736  1.00 36.75           C  
ANISOU 4882  C   ASN A 624     4478   5888   3596    -74    621    407       C  
ATOM   4883  O   ASN A 624      25.997 126.432 215.250  1.00 36.60           O  
ANISOU 4883  O   ASN A 624     4444   5898   3564    -31    610    450       O  
ATOM   4884  CB  ASN A 624      27.094 129.309 216.368  1.00 38.01           C  
ANISOU 4884  CB  ASN A 624     4713   5875   3855    -85    687    398       C  
ATOM   4885  CG  ASN A 624      25.914 129.675 215.548  1.00 38.29           C  
ANISOU 4885  CG  ASN A 624     4744   5892   3911    -22    697    475       C  
ATOM   4886  OD1 ASN A 624      24.778 129.625 216.006  1.00 38.33           O  
ANISOU 4886  OD1 ASN A 624     4742   5890   3931     36    704    476       O  
ATOM   4887  ND2 ASN A 624      26.157 129.982 214.293  1.00 38.54           N  
ANISOU 4887  ND2 ASN A 624     4777   5923   3942    -31    694    545       N  
ATOM   4888  N   SER A 625      28.202 126.386 215.341  1.00 36.58           N  
ANISOU 4888  N   SER A 625     4440   5907   3553   -119    608    395       N  
ATOM   4889  CA  SER A 625      28.374 125.515 214.189  1.00 36.29           C  
ANISOU 4889  CA  SER A 625     4378   5938   3473   -119    592    434       C  
ATOM   4890  C   SER A 625      27.907 124.093 214.426  1.00 35.66           C  
ANISOU 4890  C   SER A 625     4280   5926   3343    -95    557    415       C  
ATOM   4891  O   SER A 625      27.789 123.293 213.467  1.00 35.45           O  
ANISOU 4891  O   SER A 625     4243   5953   3274    -89    543    446       O  
ATOM   4892  CB  SER A 625      29.829 125.481 213.763  1.00 36.45           C  
ANISOU 4892  CB  SER A 625     4379   5977   3492   -172    601    419       C  
ATOM   4893  OG  SER A 625      30.654 124.838 214.721  1.00 36.21           O  
ANISOU 4893  OG  SER A 625     4327   5975   3456   -192    578    351       O  
ATOM   4894  N   TYR A 626      27.676 123.746 215.688  1.00 35.43           N  
ANISOU 4894  N   TYR A 626     4256   5893   3311    -87    544    361       N  
ATOM   4895  CA  TYR A 626      27.131 122.450 215.976  1.00 34.92           C  
ANISOU 4895  CA  TYR A 626     4186   5883   3201    -67    515    347       C  
ATOM   4896  C   TYR A 626      25.835 122.453 216.788  1.00 34.90           C  
ANISOU 4896  C   TYR A 626     4193   5866   3203    -36    521    341       C  
ATOM   4897  O   TYR A 626      25.219 121.386 216.933  1.00 34.57           O  
ANISOU 4897  O   TYR A 626     4145   5867   3122    -25    501    339       O  
ATOM   4898  CB  TYR A 626      28.175 121.584 216.634  1.00 34.67           C  
ANISOU 4898  CB  TYR A 626     4150   5880   3143    -89    489    292       C  
ATOM   4899  CG  TYR A 626      28.661 122.034 218.009  1.00 34.86           C  
ANISOU 4899  CG  TYR A 626     4193   5868   3184   -109    484    234       C  
ATOM   4900  CD1 TYR A 626      28.028 121.589 219.173  1.00 34.72           C  
ANISOU 4900  CD1 TYR A 626     4203   5848   3141    -98    473    199       C  
ATOM   4901  CD2 TYR A 626      29.795 122.826 218.150  1.00 35.26           C  
ANISOU 4901  CD2 TYR A 626     4237   5892   3269   -148    489    211       C  
ATOM   4902  CE1 TYR A 626      28.469 121.948 220.421  1.00 34.98           C  
ANISOU 4902  CE1 TYR A 626     4265   5850   3175   -121    466    145       C  
ATOM   4903  CE2 TYR A 626      30.237 123.178 219.392  1.00 35.52           C  
ANISOU 4903  CE2 TYR A 626     4291   5896   3309   -174    475    156       C  
ATOM   4904  CZ  TYR A 626      29.552 122.734 220.535  1.00 35.38           C  
ANISOU 4904  CZ  TYR A 626     4310   5874   3256   -158    462    122       C  
ATOM   4905  OH  TYR A 626      29.968 123.070 221.789  1.00 35.72           O  
ANISOU 4905  OH  TYR A 626     4389   5890   3293   -188    446     66       O  
ATOM   4906  N   SER A 627      25.424 123.616 217.314  1.00 35.35           N  
ANISOU 4906  N   SER A 627     4265   5859   3307    -23    555    337       N  
ATOM   4907  CA  SER A 627      24.193 123.712 218.106  1.00 35.49           C  
ANISOU 4907  CA  SER A 627     4286   5861   3336     11    577    328       C  
ATOM   4908  C   SER A 627      23.042 123.102 217.299  1.00 35.38           C  
ANISOU 4908  C   SER A 627     4235   5896   3312     42    562    385       C  
ATOM   4909  O   SER A 627      22.776 123.565 216.189  1.00 35.63           O  
ANISOU 4909  O   SER A 627     4248   5926   3363     58    557    446       O  
ATOM   4910  CB  SER A 627      23.890 125.157 218.462  1.00 36.14           C  
ANISOU 4910  CB  SER A 627     4391   5861   3480     31    623    327       C  
ATOM   4911  OG  SER A 627      22.907 125.223 219.472  1.00 36.36           O  
ANISOU 4911  OG  SER A 627     4427   5871   3517     60    656    299       O  
ATOM   4912  N   PRO A 628      22.402 122.018 217.818  1.00 35.08           N  
ANISOU 4912  N   PRO A 628     4188   5905   3236     42    549    366       N  
ATOM   4913  CA  PRO A 628      21.447 121.375 216.920  1.00 35.04           C  
ANISOU 4913  CA  PRO A 628     4144   5952   3217     55    524    420       C  
ATOM   4914  C   PRO A 628      20.301 122.258 216.502  1.00 35.63           C  
ANISOU 4914  C   PRO A 628     4180   6009   3348    101    542    474       C  
ATOM   4915  O   PRO A 628      20.158 122.494 215.306  1.00 35.82           O  
ANISOU 4915  O   PRO A 628     4186   6046   3377    110    517    535       O  
ATOM   4916  CB  PRO A 628      21.024 120.127 217.689  1.00 34.72           C  
ANISOU 4916  CB  PRO A 628     4108   5954   3131     38    514    385       C  
ATOM   4917  CG  PRO A 628      22.294 119.733 218.277  1.00 34.38           C  
ANISOU 4917  CG  PRO A 628     4108   5901   3053      9    502    333       C  
ATOM   4918  CD  PRO A 628      22.817 121.063 218.850  1.00 34.72           C  
ANISOU 4918  CD  PRO A 628     4171   5880   3143     15    537    308       C  
ATOM   4919  N   ILE A 629      19.531 122.783 217.444  1.00 36.02           N  
ANISOU 4919  N   ILE A 629     4220   6026   3440    131    587    453       N  
ATOM   4920  CA  ILE A 629      18.432 123.656 217.044  1.00 36.72           C  
ANISOU 4920  CA  ILE A 629     4263   6094   3595    187    605    508       C  
ATOM   4921  C   ILE A 629      18.853 124.721 215.984  1.00 37.08           C  
ANISOU 4921  C   ILE A 629     4320   6095   3675    206    594    564       C  
ATOM   4922  O   ILE A 629      18.082 125.042 215.074  1.00 37.56           O  
ANISOU 4922  O   ILE A 629     4340   6167   3764    242    571    636       O  
ATOM   4923  CB  ILE A 629      17.736 124.287 218.259  1.00 37.24           C  
ANISOU 4923  CB  ILE A 629     4326   6114   3711    225    673    468       C  
ATOM   4924  CG1 ILE A 629      16.894 123.219 218.929  1.00 37.12           C  
ANISOU 4924  CG1 ILE A 629     4279   6159   3668    212    682    445       C  
ATOM   4925  CG2 ILE A 629      16.820 125.402 217.841  1.00 38.11           C  
ANISOU 4925  CG2 ILE A 629     4394   6183   3904    296    698    522       C  
ATOM   4926  CD1 ILE A 629      15.919 123.754 219.986  1.00 37.82           C  
ANISOU 4926  CD1 ILE A 629     4347   6217   3806    254    759    416       C  
ATOM   4927  N   ASP A 630      20.083 125.221 216.093  1.00 36.94           N  
ANISOU 4927  N   ASP A 630     4355   6028   3650    176    606    534       N  
ATOM   4928  CA  ASP A 630      20.522 126.356 215.312  1.00 37.40           C  
ANISOU 4928  CA  ASP A 630     4438   6029   3745    187    612    580       C  
ATOM   4929  C   ASP A 630      20.953 125.938 213.941  1.00 37.21           C  
ANISOU 4929  C   ASP A 630     4411   6052   3677    160    565    636       C  
ATOM   4930  O   ASP A 630      21.143 126.741 213.047  1.00 37.68           O  
ANISOU 4930  O   ASP A 630     4487   6075   3753    167    562    693       O  
ATOM   4931  CB  ASP A 630      21.642 127.052 216.052  1.00 37.44           C  
ANISOU 4931  CB  ASP A 630     4498   5965   3762    154    647    521       C  
ATOM   4932  CG  ASP A 630      21.138 127.716 217.356  1.00 37.87           C  
ANISOU 4932  CG  ASP A 630     4574   5956   3861    184    702    467       C  
ATOM   4933  OD1 ASP A 630      20.271 128.643 217.263  1.00 41.45           O  
ANISOU 4933  OD1 ASP A 630     5018   6352   4378    245    734    503       O  
ATOM   4934  OD2 ASP A 630      21.583 127.308 218.475  1.00 40.85           O  
ANISOU 4934  OD2 ASP A 630     4977   6335   4207    151    715    391       O  
ATOM   4935  N   ASN A 631      21.068 124.642 213.768  1.00 36.61           N  
ANISOU 4935  N   ASN A 631     4321   6053   3537    128    530    620       N  
ATOM   4936  CA  ASN A 631      21.511 124.102 212.514  1.00 36.46           C  
ANISOU 4936  CA  ASN A 631     4308   6081   3463     99    492    660       C  
ATOM   4937  C   ASN A 631      20.513 123.249 211.785  1.00 36.48           C  
ANISOU 4937  C   ASN A 631     4277   6154   3430    106    444    705       C  
ATOM   4938  O   ASN A 631      20.862 122.654 210.772  1.00 36.37           O  
ANISOU 4938  O   ASN A 631     4279   6183   3357     75    412    729       O  
ATOM   4939  CB  ASN A 631      22.853 123.424 212.680  1.00 35.90           C  
ANISOU 4939  CB  ASN A 631     4265   6029   3347     48    496    604       C  
ATOM   4940  CG  ASN A 631      23.925 124.407 212.857  1.00 36.12           C  
ANISOU 4940  CG  ASN A 631     4320   5996   3407     29    530    586       C  
ATOM   4941  OD1 ASN A 631      24.528 124.815 211.900  1.00 36.38           O  
ANISOU 4941  OD1 ASN A 631     4369   6021   3432      9    535    624       O  
ATOM   4942  ND2 ASN A 631      24.113 124.874 214.055  1.00 36.14           N  
ANISOU 4942  ND2 ASN A 631     4334   5952   3447     30    558    533       N  
ATOM   4943  N   VAL A 632      19.273 123.232 212.269  1.00 36.74           N  
ANISOU 4943  N   VAL A 632     4263   6197   3498    142    440    715       N  
ATOM   4944  CA  VAL A 632      18.142 122.649 211.533  1.00 37.02           C  
ANISOU 4944  CA  VAL A 632     4253   6297   3517    149    388    769       C  
ATOM   4945  C   VAL A 632      17.913 123.345 210.191  1.00 37.68           C  
ANISOU 4945  C   VAL A 632     4339   6377   3601    167    350    859       C  
ATOM   4946  O   VAL A 632      17.818 124.577 210.128  1.00 38.26           O  
ANISOU 4946  O   VAL A 632     4415   6387   3735    211    371    896       O  
ATOM   4947  CB  VAL A 632      16.847 122.670 212.356  1.00 37.37           C  
ANISOU 4947  CB  VAL A 632     4231   6351   3617    189    401    766       C  
ATOM   4948  CG1 VAL A 632      15.655 122.622 211.463  1.00 38.04           C  
ANISOU 4948  CG1 VAL A 632     4254   6485   3714    210    346    844       C  
ATOM   4949  CG2 VAL A 632      16.792 121.488 213.246  1.00 36.80           C  
ANISOU 4949  CG2 VAL A 632     4158   6319   3507    151    411    701       C  
ATOM   4950  N   ARG A 633      17.823 122.583 209.107  1.00 37.70           N  
ANISOU 4950  N   ARG A 633     4349   6441   3533    132    293    894       N  
ATOM   4951  CA  ARG A 633      17.633 123.254 207.823  1.00 38.42           C  
ANISOU 4951  CA  ARG A 633     4456   6530   3613    145    253    983       C  
ATOM   4952  C   ARG A 633      16.745 122.522 206.787  1.00 38.85           C  
ANISOU 4952  C   ARG A 633     4487   6662   3610    125    170   1039       C  
ATOM   4953  O   ARG A 633      16.362 121.378 206.965  1.00 38.52           O  
ANISOU 4953  O   ARG A 633     4425   6681   3532     90    145   1005       O  
ATOM   4954  CB  ARG A 633      19.001 123.653 207.295  1.00 38.27           C  
ANISOU 4954  CB  ARG A 633     4511   6472   3557    113    285    978       C  
ATOM   4955  CG  ARG A 633      19.688 122.601 206.421  1.00 37.95           C  
ANISOU 4955  CG  ARG A 633     4517   6488   3413     51    264    965       C  
ATOM   4956  CD  ARG A 633      21.157 122.865 206.319  1.00 37.69           C  
ANISOU 4956  CD  ARG A 633     4537   6420   3362     20    320    931       C  
ATOM   4957  NE  ARG A 633      21.829 121.947 207.218  1.00 36.89           N  
ANISOU 4957  NE  ARG A 633     4431   6334   3251     -2    348    841       N  
ATOM   4958  CZ  ARG A 633      23.012 122.163 207.769  1.00 39.37           C  
ANISOU 4958  CZ  ARG A 633     4760   6614   3584    -17    399    788       C  
ATOM   4959  NH1 ARG A 633      23.676 123.274 207.504  1.00 42.11           N  
ANISOU 4959  NH1 ARG A 633     5129   6908   3961    -21    434    813       N  
ATOM   4960  NH2 ARG A 633      23.532 121.269 208.603  1.00 41.67           N  
ANISOU 4960  NH2 ARG A 633     5044   6923   3866    -30    410    713       N  
ATOM   4961  N   ALA A 634      16.388 123.186 205.712  1.00 39.67           N  
ANISOU 4961  N   ALA A 634     4600   6765   3706    142    123   1128       N  
ATOM   4962  CA  ALA A 634      15.555 122.529 204.714  1.00 40.20           C  
ANISOU 4962  CA  ALA A 634     4650   6909   3714    117     34   1183       C  
ATOM   4963  C   ALA A 634      16.234 121.318 204.058  1.00 39.73           C  
ANISOU 4963  C   ALA A 634     4658   6901   3537     37     18   1144       C  
ATOM   4964  O   ALA A 634      17.003 121.500 203.113  1.00 39.91           O  
ANISOU 4964  O   ALA A 634     4756   6914   3492     10     20   1169       O  
ATOM   4965  CB  ALA A 634      15.173 123.521 203.664  1.00 41.25           C  
ANISOU 4965  CB  ALA A 634     4796   7026   3851    150    -17   1289       C  
ATOM   4966  N   GLN A 635      15.953 120.101 204.542  1.00 39.24           N  
ANISOU 4966  N   GLN A 635     4574   6888   3449      0      8   1084       N  
ATOM   4967  CA  GLN A 635      16.540 118.854 203.998  1.00 38.87           C  
ANISOU 4967  CA  GLN A 635     4594   6881   3294    -70     -3   1040       C  
ATOM   4968  C   GLN A 635      15.819 117.643 204.557  1.00 38.62           C  
ANISOU 4968  C   GLN A 635     4524   6898   3253   -104    -29    994       C  
ATOM   4969  O   GLN A 635      15.146 117.755 205.604  1.00 38.51           O  
ANISOU 4969  O   GLN A 635     4436   6880   3318    -74    -13    979       O  
ATOM   4970  CB  GLN A 635      18.007 118.742 204.400  1.00 38.09           C  
ANISOU 4970  CB  GLN A 635     4554   6738   3181    -80     78    970       C  
ATOM   4971  CG  GLN A 635      18.286 118.214 205.852  1.00 37.26           C  
ANISOU 4971  CG  GLN A 635     4422   6614   3122    -72    129    885       C  
ATOM   4972  CD  GLN A 635      19.718 118.514 206.301  1.00 36.72           C  
ANISOU 4972  CD  GLN A 635     4392   6494   3065    -67    201    833       C  
ATOM   4973  OE1 GLN A 635      20.556 118.895 205.489  1.00 36.90           O  
ANISOU 4973  OE1 GLN A 635     4463   6505   3054    -79    220    851       O  
ATOM   4974  NE2 GLN A 635      19.995 118.379 207.583  1.00 36.16           N  
ANISOU 4974  NE2 GLN A 635     4299   6397   3041    -52    240    772       N  
ATOM   4975  N   ASP A 636      15.985 116.476 203.933  1.00 38.58           N  
ANISOU 4975  N   ASP A 636     4576   6932   3151   -168    -60    967       N  
ATOM   4976  CA  ASP A 636      15.482 115.245 204.573  1.00 38.29           C  
ANISOU 4976  CA  ASP A 636     4520   6926   3102   -209    -71    913       C  
ATOM   4977  C   ASP A 636      16.145 114.860 205.914  1.00 37.38           C  
ANISOU 4977  C   ASP A 636     4409   6771   3025   -195      4    832       C  
ATOM   4978  O   ASP A 636      17.353 114.881 206.022  1.00 36.88           O  
ANISOU 4978  O   ASP A 636     4400   6668   2943   -186     56    792       O  
ATOM   4979  CB  ASP A 636      15.556 114.089 203.597  1.00 38.54           C  
ANISOU 4979  CB  ASP A 636     4627   6997   3019   -282   -118    898       C  
ATOM   4980  CG  ASP A 636      14.807 114.391 202.297  1.00 39.56           C  
ANISOU 4980  CG  ASP A 636     4758   7175   3099   -306   -207    978       C  
ATOM   4981  OD1 ASP A 636      14.077 115.420 202.276  1.00 40.09           O  
ANISOU 4981  OD1 ASP A 636     4749   7248   3235   -260   -239   1049       O  
ATOM   4982  OD2 ASP A 636      14.946 113.617 201.309  1.00 39.93           O  
ANISOU 4982  OD2 ASP A 636     4885   7249   3037   -369   -246    971       O  
ATOM   4983  N   TYR A 637      15.346 114.539 206.937  1.00 37.29           N  
ANISOU 4983  N   TYR A 637     4335   6769   3065   -194      9    812       N  
ATOM   4984  CA  TYR A 637      15.813 113.858 208.169  1.00 36.58           C  
ANISOU 4984  CA  TYR A 637     4262   6650   2985   -199     64    736       C  
ATOM   4985  C   TYR A 637      15.124 112.463 208.289  1.00 36.69           C  
ANISOU 4985  C   TYR A 637     4285   6703   2953   -265     29    710       C  
ATOM   4986  O   TYR A 637      14.112 112.226 207.631  1.00 37.36           O  
ANISOU 4986  O   TYR A 637     4334   6839   3022   -302    -33    751       O  
ATOM   4987  CB  TYR A 637      15.459 114.712 209.372  1.00 36.48           C  
ANISOU 4987  CB  TYR A 637     4182   6610   3068   -147    111    732       C  
ATOM   4988  CG  TYR A 637      16.173 116.061 209.497  1.00 36.37           C  
ANISOU 4988  CG  TYR A 637     4169   6543   3106    -87    155    745       C  
ATOM   4989  CD1 TYR A 637      15.670 117.188 208.871  1.00 37.00           C  
ANISOU 4989  CD1 TYR A 637     4207   6620   3230    -47    134    815       C  
ATOM   4990  CD2 TYR A 637      17.333 116.220 210.297  1.00 35.74           C  
ANISOU 4990  CD2 TYR A 637     4132   6412   3035    -71    213    688       C  
ATOM   4991  CE1 TYR A 637      16.298 118.427 208.993  1.00 36.99           C  
ANISOU 4991  CE1 TYR A 637     4217   6561   3278      1    176    827       C  
ATOM   4992  CE2 TYR A 637      17.965 117.477 210.445  1.00 35.74           C  
ANISOU 4992  CE2 TYR A 637     4134   6361   3086    -28    251    697       C  
ATOM   4993  CZ  TYR A 637      17.431 118.575 209.786  1.00 36.37           C  
ANISOU 4993  CZ  TYR A 637     4180   6432   3206      6    236    766       C  
ATOM   4994  OH  TYR A 637      18.003 119.840 209.868  1.00 36.49           O  
ANISOU 4994  OH  TYR A 637     4206   6388   3272     44    274    780       O  
ATOM   4995  N   PRO A 638      15.622 111.531 209.141  1.00 36.15           N  
ANISOU 4995  N   PRO A 638     4264   6609   2864   -285     64    645       N  
ATOM   4996  CA  PRO A 638      14.897 110.249 209.181  1.00 36.41           C  
ANISOU 4996  CA  PRO A 638     4312   6670   2852   -354     31    627       C  
ATOM   4997  C   PRO A 638      13.808 110.203 210.248  1.00 36.61           C  
ANISOU 4997  C   PRO A 638     4260   6714   2937   -364     46    629       C  
ATOM   4998  O   PRO A 638      13.629 111.160 210.978  1.00 36.55           O  
ANISOU 4998  O   PRO A 638     4190   6694   3004   -311     86    639       O  
ATOM   4999  CB  PRO A 638      15.997 109.255 209.570  1.00 35.84           C  
ANISOU 4999  CB  PRO A 638     4338   6553   2728   -365     63    560       C  
ATOM   5000  CG  PRO A 638      16.946 110.041 210.393  1.00 35.26           C  
ANISOU 5000  CG  PRO A 638     4260   6435   2703   -300    121    538       C  
ATOM   5001  CD  PRO A 638      16.710 111.528 210.131  1.00 35.45           C  
ANISOU 5001  CD  PRO A 638     4214   6467   2789   -252    126    589       C  
ATOM   5002  N   HIS A 639      13.088 109.094 210.339  1.00 36.94           N  
ANISOU 5002  N   HIS A 639     4308   6782   2946   -436     19    616       N  
ATOM   5003  CA  HIS A 639      12.155 108.885 211.431  1.00 37.17           C  
ANISOU 5003  CA  HIS A 639     4274   6825   3023   -456     48    609       C  
ATOM   5004  C   HIS A 639      12.854 109.137 212.775  1.00 36.52           C  
ANISOU 5004  C   HIS A 639     4219   6688   2969   -409    125    565       C  
ATOM   5005  O   HIS A 639      13.917 108.563 213.046  1.00 35.96           O  
ANISOU 5005  O   HIS A 639     4242   6570   2851   -407    142    521       O  
ATOM   5006  CB  HIS A 639      11.570 107.466 211.354  1.00 37.56           C  
ANISOU 5006  CB  HIS A 639     4360   6894   3015   -554     15    591       C  
ATOM   5007  CG  HIS A 639      10.818 107.219 210.088  1.00 38.33           C  
ANISOU 5007  CG  HIS A 639     4431   7050   3081   -612    -69    632       C  
ATOM   5008  ND1 HIS A 639       9.570 107.757 209.846  1.00 39.14           N  
ANISOU 5008  ND1 HIS A 639     4408   7220   3243   -622   -107    687       N  
ATOM   5009  CD2 HIS A 639      11.165 106.552 208.961  1.00 38.50           C  
ANISOU 5009  CD2 HIS A 639     4537   7074   3018   -659   -124    626       C  
ATOM   5010  CE1 HIS A 639       9.175 107.416 208.636  1.00 39.78           C  
ANISOU 5010  CE1 HIS A 639     4497   7346   3274   -678   -192    716       C  
ATOM   5011  NE2 HIS A 639      10.119 106.678 208.080  1.00 39.41           N  
ANISOU 5011  NE2 HIS A 639     4582   7258   3133   -705   -202    677       N  
ATOM   5012  N   LEU A 640      12.264 110.000 213.603  1.00 36.70           N  
ANISOU 5012  N   LEU A 640     4160   6715   3068   -369    171    577       N  
ATOM   5013  CA  LEU A 640      12.863 110.323 214.887  1.00 36.22           C  
ANISOU 5013  CA  LEU A 640     4129   6605   3028   -329    241    535       C  
ATOM   5014  C   LEU A 640      11.862 110.337 216.015  1.00 36.65           C  
ANISOU 5014  C   LEU A 640     4124   6674   3126   -342    295    528       C  
ATOM   5015  O   LEU A 640      10.821 110.968 215.926  1.00 37.29           O  
ANISOU 5015  O   LEU A 640     4100   6794   3272   -327    302    565       O  
ATOM   5016  CB  LEU A 640      13.529 111.697 214.813  1.00 35.96           C  
ANISOU 5016  CB  LEU A 640     4080   6541   3043   -249    264    545       C  
ATOM   5017  CG  LEU A 640      14.042 112.322 216.105  1.00 35.65           C  
ANISOU 5017  CG  LEU A 640     4059   6451   3034   -206    333    505       C  
ATOM   5018  CD1 LEU A 640      15.300 111.623 216.524  1.00 35.01           C  
ANISOU 5018  CD1 LEU A 640     4080   6329   2892   -218    335    456       C  
ATOM   5019  CD2 LEU A 640      14.309 113.774 215.885  1.00 35.70           C  
ANISOU 5019  CD2 LEU A 640     4030   6433   3101   -138    351    527       C  
ATOM   5020  N   MET A 641      12.195 109.665 217.102  1.00 36.38           N  
ANISOU 5020  N   MET A 641     4159   6608   3057   -367    335    483       N  
ATOM   5021  CA  MET A 641      11.420 109.791 218.345  1.00 36.79           C  
ANISOU 5021  CA  MET A 641     4172   6663   3142   -374    406    468       C  
ATOM   5022  C   MET A 641      12.230 110.510 219.391  1.00 36.38           C  
ANISOU 5022  C   MET A 641     4168   6557   3099   -319    464    430       C  
ATOM   5023  O   MET A 641      13.356 110.106 219.668  1.00 35.81           O  
ANISOU 5023  O   MET A 641     4192   6441   2972   -317    452    398       O  
ATOM   5024  CB  MET A 641      10.995 108.429 218.884  1.00 37.03           C  
ANISOU 5024  CB  MET A 641     4250   6701   3118   -460    413    450       C  
ATOM   5025  CG  MET A 641      10.123 108.515 220.123  1.00 38.13           C  
ANISOU 5025  CG  MET A 641     4351   6852   3287   -478    495    438       C  
ATOM   5026  SD  MET A 641       9.405 106.917 220.528  1.00 43.21           S  
ANISOU 5026  SD  MET A 641     5036   7512   3871   -597    498    432       S  
ATOM   5027  CE  MET A 641       9.298 107.096 222.298  1.00 43.32           C  
ANISOU 5027  CE  MET A 641     5088   7494   3876   -594    607    395       C  
ATOM   5028  N   ILE A 642      11.664 111.577 219.949  1.00 36.78           N  
ANISOU 5028  N   ILE A 642     4150   6609   3217   -272    524    433       N  
ATOM   5029  CA  ILE A 642      12.265 112.281 221.074  1.00 36.60           C  
ANISOU 5029  CA  ILE A 642     4174   6533   3198   -230    586    391       C  
ATOM   5030  C   ILE A 642      11.464 111.985 222.344  1.00 37.15           C  
ANISOU 5030  C   ILE A 642     4243   6610   3264   -262    665    366       C  
ATOM   5031  O   ILE A 642      10.251 112.058 222.306  1.00 37.87           O  
ANISOU 5031  O   ILE A 642     4239   6747   3404   -273    697    390       O  
ATOM   5032  CB  ILE A 642      12.212 113.779 220.845  1.00 36.79           C  
ANISOU 5032  CB  ILE A 642     4137   6541   3302   -153    611    406       C  
ATOM   5033  CG1 ILE A 642      12.793 114.122 219.474  1.00 36.45           C  
ANISOU 5033  CG1 ILE A 642     4083   6499   3266   -128    539    444       C  
ATOM   5034  CG2 ILE A 642      12.882 114.527 222.029  1.00 36.68           C  
ANISOU 5034  CG2 ILE A 642     4186   6465   3285   -118    674    355       C  
ATOM   5035  CD1 ILE A 642      12.158 115.294 218.820  1.00 36.97           C  
ANISOU 5035  CD1 ILE A 642     4057   6574   3416    -68    541    491       C  
ATOM   5036  N   GLN A 643      12.144 111.683 223.449  1.00 36.92           N  
ANISOU 5036  N   GLN A 643     4315   6538   3174   -277    695    320       N  
ATOM   5037  CA  GLN A 643      11.523 111.373 224.752  1.00 37.48           C  
ANISOU 5037  CA  GLN A 643     4413   6608   3220   -313    776    292       C  
ATOM   5038  C   GLN A 643      11.969 112.452 225.705  1.00 37.55           C  
ANISOU 5038  C   GLN A 643     4459   6570   3239   -261    837    251       C  
ATOM   5039  O   GLN A 643      13.162 112.585 225.931  1.00 37.01           O  
ANISOU 5039  O   GLN A 643     4475   6456   3130   -245    803    225       O  
ATOM   5040  CB  GLN A 643      12.018 110.012 225.272  1.00 37.24           C  
ANISOU 5040  CB  GLN A 643     4498   6560   3093   -381    749    275       C  
ATOM   5041  CG  GLN A 643      11.389 109.505 226.572  1.00 39.64           C  
ANISOU 5041  CG  GLN A 643     4848   6863   3352   -434    828    253       C  
ATOM   5042  CD  GLN A 643      12.113 109.977 227.888  1.00 44.79           C  
ANISOU 5042  CD  GLN A 643     5602   7462   3954   -413    874    205       C  
ATOM   5043  OE1 GLN A 643      13.255 109.563 228.173  1.00 48.07           O  
ANISOU 5043  OE1 GLN A 643     6124   7837   4304   -414    819    188       O  
ATOM   5044  NE2 GLN A 643      11.432 110.819 228.692  1.00 42.19           N  
ANISOU 5044  NE2 GLN A 643     5240   7135   3656   -394    973    182       N  
ATOM   5045  N   ALA A 644      11.035 113.203 226.284  1.00 38.32           N  
ANISOU 5045  N   ALA A 644     4494   6675   3390   -237    929    242       N  
ATOM   5046  CA  ALA A 644      11.378 114.253 227.259  1.00 38.56           C  
ANISOU 5046  CA  ALA A 644     4571   6653   3425   -192    999    195       C  
ATOM   5047  C   ALA A 644      10.627 114.057 228.565  1.00 39.37           C  
ANISOU 5047  C   ALA A 644     4703   6760   3497   -226   1105    160       C  
ATOM   5048  O   ALA A 644       9.673 113.295 228.610  1.00 39.86           O  
ANISOU 5048  O   ALA A 644     4716   6870   3558   -275   1135    181       O  
ATOM   5049  CB  ALA A 644      11.114 115.641 226.693  1.00 38.82           C  
ANISOU 5049  CB  ALA A 644     4516   6672   3559   -110   1020    209       C  
ATOM   5050  N   GLY A 645      11.058 114.737 229.628  1.00 39.62           N  
ANISOU 5050  N   GLY A 645     4817   6740   3497   -207   1165    107       N  
ATOM   5051  CA  GLY A 645      10.377 114.678 230.926  1.00 40.52           C  
ANISOU 5051  CA  GLY A 645     4972   6852   3573   -237   1280     68       C  
ATOM   5052  C   GLY A 645      10.145 116.079 231.474  1.00 41.20           C  
ANISOU 5052  C   GLY A 645     5047   6896   3711   -170   1376     26       C  
ATOM   5053  O   GLY A 645      11.082 116.875 231.574  1.00 40.87           O  
ANISOU 5053  O   GLY A 645     5069   6798   3663   -134   1349     -4       O  
ATOM   5054  N   LEU A 646       8.902 116.387 231.849  1.00 42.25           N  
ANISOU 5054  N   LEU A 646     5099   7054   3899   -154   1493     21       N  
ATOM   5055  CA  LEU A 646       8.568 117.743 232.316  1.00 43.06           C  
ANISOU 5055  CA  LEU A 646     5184   7112   4065    -79   1597    -20       C  
ATOM   5056  C   LEU A 646       9.422 118.310 233.455  1.00 43.20           C  
ANISOU 5056  C   LEU A 646     5360   7055   3999    -84   1636    -94       C  
ATOM   5057  O   LEU A 646       9.800 119.472 233.413  1.00 43.31           O  
ANISOU 5057  O   LEU A 646     5389   7010   4059    -22   1649   -121       O  
ATOM   5058  CB  LEU A 646       7.087 117.883 232.659  1.00 44.34           C  
ANISOU 5058  CB  LEU A 646     5235   7316   4295    -62   1730    -19       C  
ATOM   5059  CG  LEU A 646       6.614 119.332 232.838  1.00 45.27           C  
ANISOU 5059  CG  LEU A 646     5301   7387   4511     39   1833    -49       C  
ATOM   5060  CD1 LEU A 646       6.719 120.110 231.551  1.00 44.88           C  
ANISOU 5060  CD1 LEU A 646     5152   7327   4574    121   1753      2       C  
ATOM   5061  CD2 LEU A 646       5.179 119.373 233.363  1.00 46.70           C  
ANISOU 5061  CD2 LEU A 646     5378   7613   4752     52   1981    -57       C  
ATOM   5062  N   HIS A 647       9.715 117.529 234.477  1.00 43.30           N  
ANISOU 5062  N   HIS A 647     5496   7067   3890   -159   1652   -126       N  
ATOM   5063  CA  HIS A 647      10.457 118.120 235.595  1.00 43.63           C  
ANISOU 5063  CA  HIS A 647     5688   7040   3847   -167   1687   -198       C  
ATOM   5064  C   HIS A 647      11.984 117.865 235.572  1.00 42.65           C  
ANISOU 5064  C   HIS A 647     5678   6884   3643   -198   1550   -205       C  
ATOM   5065  O   HIS A 647      12.628 117.760 236.625  1.00 42.90           O  
ANISOU 5065  O   HIS A 647     5854   6882   3563   -243   1550   -253       O  
ATOM   5066  CB  HIS A 647       9.798 117.745 236.924  1.00 44.71           C  
ANISOU 5066  CB  HIS A 647     5905   7185   3898   -220   1813   -242       C  
ATOM   5067  CG  HIS A 647       8.335 118.051 236.954  1.00 45.80           C  
ANISOU 5067  CG  HIS A 647     5918   7358   4126   -186   1956   -239       C  
ATOM   5068  ND1 HIS A 647       7.846 119.301 237.272  1.00 46.76           N  
ANISOU 5068  ND1 HIS A 647     6012   7437   4318   -111   2074   -285       N  
ATOM   5069  CD2 HIS A 647       7.257 117.291 236.635  1.00 46.15           C  
ANISOU 5069  CD2 HIS A 647     5845   7476   4214   -212   1996   -192       C  
ATOM   5070  CE1 HIS A 647       6.526 119.287 237.180  1.00 47.69           C  
ANISOU 5070  CE1 HIS A 647     5995   7604   4521    -86   2184   -267       C  
ATOM   5071  NE2 HIS A 647       6.144 118.080 236.797  1.00 47.34           N  
ANISOU 5071  NE2 HIS A 647     5891   7635   4462   -151   2137   -210       N  
ATOM   5072  N   ASP A 648      12.542 117.815 234.356  1.00 41.66           N  
ANISOU 5072  N   ASP A 648     5483   6770   3577   -172   1436   -157       N  
ATOM   5073  CA  ASP A 648      13.921 117.406 234.098  1.00 40.73           C  
ANISOU 5073  CA  ASP A 648     5435   6637   3402   -197   1302   -150       C  
ATOM   5074  C   ASP A 648      14.890 118.526 234.485  1.00 40.81           C  
ANISOU 5074  C   ASP A 648     5521   6580   3405   -175   1288   -202       C  
ATOM   5075  O   ASP A 648      15.047 119.518 233.767  1.00 40.67           O  
ANISOU 5075  O   ASP A 648     5443   6533   3476   -120   1281   -197       O  
ATOM   5076  CB  ASP A 648      14.038 116.979 232.616  1.00 39.82           C  
ANISOU 5076  CB  ASP A 648     5212   6561   3357   -177   1208    -82       C  
ATOM   5077  CG  ASP A 648      15.419 116.422 232.232  1.00 38.90           C  
ANISOU 5077  CG  ASP A 648     5151   6438   3192   -198   1076    -70       C  
ATOM   5078  OD1 ASP A 648      16.412 116.798 232.860  1.00 38.91           O  
ANISOU 5078  OD1 ASP A 648     5243   6397   3142   -207   1045   -111       O  
ATOM   5079  OD2 ASP A 648      15.503 115.632 231.252  1.00 38.26           O  
ANISOU 5079  OD2 ASP A 648     5015   6394   3128   -204   1004    -20       O  
ATOM   5080  N   PRO A 649      15.554 118.374 235.639  1.00 41.13           N  
ANISOU 5080  N   PRO A 649     5702   6593   3334   -224   1279   -252       N  
ATOM   5081  CA  PRO A 649      16.377 119.490 236.129  1.00 41.44           C  
ANISOU 5081  CA  PRO A 649     5819   6567   3361   -216   1274   -311       C  
ATOM   5082  C   PRO A 649      17.719 119.569 235.426  1.00 40.59           C  
ANISOU 5082  C   PRO A 649     5705   6449   3268   -215   1139   -293       C  
ATOM   5083  O   PRO A 649      18.559 120.374 235.805  1.00 40.82           O  
ANISOU 5083  O   PRO A 649     5799   6429   3281   -224   1113   -339       O  
ATOM   5084  CB  PRO A 649      16.586 119.153 237.600  1.00 42.18           C  
ANISOU 5084  CB  PRO A 649     6066   6644   3316   -279   1300   -364       C  
ATOM   5085  CG  PRO A 649      16.516 117.662 237.647  1.00 41.80           C  
ANISOU 5085  CG  PRO A 649     6032   6651   3200   -324   1248   -318       C  
ATOM   5086  CD  PRO A 649      15.651 117.184 236.500  1.00 41.29           C  
ANISOU 5086  CD  PRO A 649     5820   6636   3231   -293   1261   -253       C  
ATOM   5087  N   ARG A 650      17.910 118.733 234.417  1.00 39.71           N  
ANISOU 5087  N   ARG A 650     5517   6385   3187   -210   1058   -231       N  
ATOM   5088  CA  ARG A 650      19.182 118.582 233.733  1.00 38.94           C  
ANISOU 5088  CA  ARG A 650     5408   6289   3098   -212    935   -210       C  
ATOM   5089  C   ARG A 650      19.097 119.091 232.275  1.00 38.38           C  
ANISOU 5089  C   ARG A 650     5214   6225   3143   -160    919   -164       C  
ATOM   5090  O   ARG A 650      19.806 120.033 231.883  1.00 38.30           O  
ANISOU 5090  O   ARG A 650     5193   6179   3181   -143    894   -175       O  
ATOM   5091  CB  ARG A 650      19.624 117.117 233.805  1.00 38.50           C  
ANISOU 5091  CB  ARG A 650     5386   6275   2967   -250    851   -180       C  
ATOM   5092  CG  ARG A 650      20.146 116.704 235.200  1.00 39.06           C  
ANISOU 5092  CG  ARG A 650     5596   6330   2914   -302    828   -221       C  
ATOM   5093  CD  ARG A 650      20.445 115.203 235.275  1.00 38.75           C  
ANISOU 5093  CD  ARG A 650     5595   6324   2805   -331    752   -182       C  
ATOM   5094  NE  ARG A 650      20.729 114.709 236.624  1.00 39.42           N  
ANISOU 5094  NE  ARG A 650     5818   6396   2765   -381    736   -209       N  
ATOM   5095  CZ  ARG A 650      21.664 113.811 236.852  1.00 39.30           C  
ANISOU 5095  CZ  ARG A 650     5860   6386   2685   -398    627   -190       C  
ATOM   5096  NH1 ARG A 650      22.375 113.362 235.832  1.00 38.55           N  
ANISOU 5096  NH1 ARG A 650     5692   6308   2646   -368    539   -152       N  
ATOM   5097  NH2 ARG A 650      21.915 113.370 238.059  1.00 40.00           N  
ANISOU 5097  NH2 ARG A 650     6079   6462   2656   -442    604   -207       N  
ATOM   5098  N   VAL A 651      18.231 118.469 231.481  1.00 38.08           N  
ANISOU 5098  N   VAL A 651     5089   6234   3145   -143    932   -111       N  
ATOM   5099  CA  VAL A 651      17.924 118.973 230.199  1.00 37.77           C  
ANISOU 5099  CA  VAL A 651     4942   6203   3205    -95    927    -66       C  
ATOM   5100  C   VAL A 651      16.478 119.450 230.335  1.00 38.47           C  
ANISOU 5100  C   VAL A 651     4974   6295   3349    -61   1036    -62       C  
ATOM   5101  O   VAL A 651      15.590 118.641 230.541  1.00 38.66           O  
ANISOU 5101  O   VAL A 651     4974   6363   3353    -80   1071    -46       O  
ATOM   5102  CB  VAL A 651      18.092 117.857 229.129  1.00 36.99           C  
ANISOU 5102  CB  VAL A 651     4790   6160   3106   -105    846     -8       C  
ATOM   5103  CG1 VAL A 651      17.689 118.348 227.749  1.00 36.77           C  
ANISOU 5103  CG1 VAL A 651     4655   6146   3171    -60    838     44       C  
ATOM   5104  CG2 VAL A 651      19.509 117.387 229.089  1.00 36.47           C  
ANISOU 5104  CG2 VAL A 651     4776   6090   2992   -129    751    -16       C  
ATOM   5105  N   ALA A 652      16.244 120.764 230.238  1.00 38.96           N  
ANISOU 5105  N   ALA A 652     5012   6307   3484    -11   1093    -77       N  
ATOM   5106  CA  ALA A 652      14.897 121.358 230.265  1.00 39.76           C  
ANISOU 5106  CA  ALA A 652     5042   6405   3660     41   1197    -70       C  
ATOM   5107  C   ALA A 652      13.948 120.848 229.206  1.00 39.61           C  
ANISOU 5107  C   ALA A 652     4895   6451   3704     64   1183      2       C  
ATOM   5108  O   ALA A 652      14.269 120.771 228.032  1.00 39.01           O  
ANISOU 5108  O   ALA A 652     4764   6395   3664     77   1104     54       O  
ATOM   5109  CB  ALA A 652      14.980 122.833 230.184  1.00 40.28           C  
ANISOU 5109  CB  ALA A 652     5111   6396   3798     97   1242    -91       C  
ATOM   5110  N   TYR A 653      12.749 120.515 229.648  1.00 40.27           N  
ANISOU 5110  N   TYR A 653     4931   6571   3799     66   1263      3       N  
ATOM   5111  CA  TYR A 653      11.686 120.039 228.762  1.00 40.37           C  
ANISOU 5111  CA  TYR A 653     4813   6652   3876     81   1256     67       C  
ATOM   5112  C   TYR A 653      11.518 120.873 227.463  1.00 40.35           C  
ANISOU 5112  C   TYR A 653     4711   6642   3978    151   1215    125       C  
ATOM   5113  O   TYR A 653      11.105 120.344 226.439  1.00 40.10           O  
ANISOU 5113  O   TYR A 653     4592   6670   3976    148   1154    187       O  
ATOM   5114  CB  TYR A 653      10.353 119.992 229.558  1.00 41.46           C  
ANISOU 5114  CB  TYR A 653     4900   6815   4037     87   1379     50       C  
ATOM   5115  CG  TYR A 653       9.668 121.339 229.627  1.00 42.44           C  
ANISOU 5115  CG  TYR A 653     4965   6895   4265    178   1472     39       C  
ATOM   5116  CD1 TYR A 653       8.944 121.824 228.520  1.00 42.74           C  
ANISOU 5116  CD1 TYR A 653     4865   6956   4419    246   1452    105       C  
ATOM   5117  CD2 TYR A 653       9.770 122.132 230.762  1.00 43.15           C  
ANISOU 5117  CD2 TYR A 653     5143   6916   4335    197   1573    -34       C  
ATOM   5118  CE1 TYR A 653       8.346 123.050 228.555  1.00 43.72           C  
ANISOU 5118  CE1 TYR A 653     4936   7031   4643    339   1532    100       C  
ATOM   5119  CE2 TYR A 653       9.154 123.348 230.823  1.00 44.14           C  
ANISOU 5119  CE2 TYR A 653     5222   6990   4558    285   1663    -47       C  
ATOM   5120  CZ  TYR A 653       8.448 123.806 229.709  1.00 44.41           C  
ANISOU 5120  CZ  TYR A 653     5114   7045   4716    360   1642     23       C  
ATOM   5121  OH  TYR A 653       7.852 125.027 229.722  1.00 45.48           O  
ANISOU 5121  OH  TYR A 653     5202   7122   4955    459   1726     17       O  
ATOM   5122  N   TRP A 654      11.798 122.175 227.517  1.00 40.71           N  
ANISOU 5122  N   TRP A 654     4778   6614   4077    211   1250    105       N  
ATOM   5123  CA  TRP A 654      11.484 123.027 226.377  1.00 40.93           C  
ANISOU 5123  CA  TRP A 654     4717   6628   4207    283   1224    165       C  
ATOM   5124  C   TRP A 654      12.453 122.775 225.241  1.00 39.96           C  
ANISOU 5124  C   TRP A 654     4605   6516   4062    259   1105    210       C  
ATOM   5125  O   TRP A 654      12.100 122.918 224.046  1.00 39.96           O  
ANISOU 5125  O   TRP A 654     4522   6544   4119    292   1052    280       O  
ATOM   5126  CB  TRP A 654      11.417 124.516 226.726  1.00 41.76           C  
ANISOU 5126  CB  TRP A 654     4845   6640   4383    358   1301    136       C  
ATOM   5127  CG  TRP A 654      12.624 125.108 227.401  1.00 41.54           C  
ANISOU 5127  CG  TRP A 654     4954   6530   4301    332   1306     70       C  
ATOM   5128  CD1 TRP A 654      13.763 125.557 226.804  1.00 40.97           C  
ANISOU 5128  CD1 TRP A 654     4930   6414   4222    320   1232     80       C  
ATOM   5129  CD2 TRP A 654      12.789 125.348 228.815  1.00 42.05           C  
ANISOU 5129  CD2 TRP A 654     5122   6545   4310    309   1390    -18       C  
ATOM   5130  NE1 TRP A 654      14.631 126.051 227.758  1.00 41.08           N  
ANISOU 5130  NE1 TRP A 654     5064   6359   4186    288   1259      5       N  
ATOM   5131  CE2 TRP A 654      14.063 125.929 228.994  1.00 41.73           C  
ANISOU 5131  CE2 TRP A 654     5188   6436   4233    281   1351    -57       C  
ATOM   5132  CE3 TRP A 654      11.998 125.089 229.940  1.00 42.79           C  
ANISOU 5132  CE3 TRP A 654     5233   6652   4376    302   1495    -67       C  
ATOM   5133  CZ2 TRP A 654      14.560 126.257 230.236  1.00 42.14           C  
ANISOU 5133  CZ2 TRP A 654     5362   6431   4218    245   1401   -142       C  
ATOM   5134  CZ3 TRP A 654      12.486 125.432 231.181  1.00 43.20           C  
ANISOU 5134  CZ3 TRP A 654     5415   6644   4356    270   1554   -153       C  
ATOM   5135  CH2 TRP A 654      13.758 126.014 231.320  1.00 42.88           C  
ANISOU 5135  CH2 TRP A 654     5481   6534   4276    242   1502   -190       C  
ATOM   5136  N   GLU A 655      13.656 122.341 225.606  1.00 39.22           N  
ANISOU 5136  N   GLU A 655     4611   6407   3882    201   1061    170       N  
ATOM   5137  CA  GLU A 655      14.673 122.044 224.599  1.00 38.35           C  
ANISOU 5137  CA  GLU A 655     4515   6309   3748    176    959    204       C  
ATOM   5138  C   GLU A 655      14.227 121.068 223.524  1.00 37.98           C  
ANISOU 5138  C   GLU A 655     4393   6341   3697    158    891    268       C  
ATOM   5139  O   GLU A 655      14.219 121.429 222.355  1.00 37.93           O  
ANISOU 5139  O   GLU A 655     4336   6341   3733    186    844    325       O  
ATOM   5140  CB  GLU A 655      16.024 121.660 225.220  1.00 37.75           C  
ANISOU 5140  CB  GLU A 655     4545   6211   3587    119    922    152       C  
ATOM   5141  CG  GLU A 655      16.624 122.768 226.099  1.00 38.17           C  
ANISOU 5141  CG  GLU A 655     4677   6181   3644    128    970     91       C  
ATOM   5142  CD  GLU A 655      18.142 122.756 226.082  1.00 43.25           C  
ANISOU 5142  CD  GLU A 655     5389   6802   4241     85    902     67       C  
ATOM   5143  OE1 GLU A 655      18.714 122.330 225.027  1.00 44.31           O  
ANISOU 5143  OE1 GLU A 655     5492   6970   4376     74    829    111       O  
ATOM   5144  OE2 GLU A 655      18.755 123.151 227.123  1.00 44.28           O  
ANISOU 5144  OE2 GLU A 655     5605   6885   4334     59    922      3       O  
ATOM   5145  N   PRO A 656      13.850 119.842 223.883  1.00 37.81           N  
ANISOU 5145  N   PRO A 656     4370   6375   3620    107    885    261       N  
ATOM   5146  CA  PRO A 656      13.478 119.028 222.763  1.00 37.54           C  
ANISOU 5146  CA  PRO A 656     4273   6407   3584     87    816    319       C  
ATOM   5147  C   PRO A 656      12.185 119.515 222.175  1.00 38.31           C  
ANISOU 5147  C   PRO A 656     4254   6535   3768    135    836    372       C  
ATOM   5148  O   PRO A 656      11.931 119.300 220.989  1.00 38.25           O  
ANISOU 5148  O   PRO A 656     4188   6569   3777    136    768    432       O  
ATOM   5149  CB  PRO A 656      13.251 117.665 223.383  1.00 37.37           C  
ANISOU 5149  CB  PRO A 656     4281   6429   3490     20    816    297       C  
ATOM   5150  CG  PRO A 656      13.048 117.917 224.752  1.00 37.81           C  
ANISOU 5150  CG  PRO A 656     4381   6454   3532     19    901    243       C  
ATOM   5151  CD  PRO A 656      13.960 119.028 225.080  1.00 37.75           C  
ANISOU 5151  CD  PRO A 656     4433   6374   3535     55    916    208       C  
ATOM   5152  N   ALA A 657      11.375 120.190 222.992  1.00 39.14           N  
ANISOU 5152  N   ALA A 657     4324   6618   3928    177    927    351       N  
ATOM   5153  CA  ALA A 657      10.085 120.691 222.527  1.00 40.06           C  
ANISOU 5153  CA  ALA A 657     4315   6766   4142    234    952    402       C  
ATOM   5154  C   ALA A 657      10.217 121.611 221.285  1.00 40.18           C  
ANISOU 5154  C   ALA A 657     4288   6758   4219    296    893    466       C  
ATOM   5155  O   ALA A 657       9.430 121.517 220.328  1.00 40.59           O  
ANISOU 5155  O   ALA A 657     4241   6864   4317    314    842    534       O  
ATOM   5156  CB  ALA A 657       9.399 121.396 223.654  1.00 40.98           C  
ANISOU 5156  CB  ALA A 657     4416   6847   4308    280   1072    358       C  
ATOM   5157  N   LYS A 658      11.221 122.491 221.326  1.00 39.90           N  
ANISOU 5157  N   LYS A 658     4334   6643   4182    321    897    444       N  
ATOM   5158  CA  LYS A 658      11.511 123.443 220.248  1.00 40.03           C  
ANISOU 5158  CA  LYS A 658     4339   6622   4249    372    851    501       C  
ATOM   5159  C   LYS A 658      12.082 122.727 219.019  1.00 39.31           C  
ANISOU 5159  C   LYS A 658     4255   6579   4101    324    745    549       C  
ATOM   5160  O   LYS A 658      11.850 123.085 217.866  1.00 39.58           O  
ANISOU 5160  O   LYS A 658     4245   6627   4168    353    688    621       O  
ATOM   5161  CB  LYS A 658      12.560 124.456 220.728  1.00 39.91           C  
ANISOU 5161  CB  LYS A 658     4424   6506   4234    389    889    455       C  
ATOM   5162  CG  LYS A 658      12.240 125.283 221.987  1.00 40.65           C  
ANISOU 5162  CG  LYS A 658     4545   6530   4368    432    999    393       C  
ATOM   5163  CD  LYS A 658      13.334 126.331 222.090  1.00 40.58           C  
ANISOU 5163  CD  LYS A 658     4633   6422   4362    439   1008    365       C  
ATOM   5164  CE  LYS A 658      13.205 127.237 223.264  1.00 41.33           C  
ANISOU 5164  CE  LYS A 658     4783   6433   4488    474   1111    296       C  
ATOM   5165  NZ  LYS A 658      14.100 128.396 222.985  1.00 41.46           N  
ANISOU 5165  NZ  LYS A 658     4873   6351   4530    489   1106    293       N  
ATOM   5166  N   TRP A 659      12.872 121.709 219.291  1.00 38.45           N  
ANISOU 5166  N   TRP A 659     4212   6493   3904    251    720    508       N  
ATOM   5167  CA  TRP A 659      13.700 121.102 218.271  1.00 37.75           C  
ANISOU 5167  CA  TRP A 659     4157   6431   3754    207    637    534       C  
ATOM   5168  C   TRP A 659      12.741 120.300 217.459  1.00 37.98           C  
ANISOU 5168  C   TRP A 659     4110   6543   3780    187    582    587       C  
ATOM   5169  O   TRP A 659      12.786 120.368 216.242  1.00 38.03           O  
ANISOU 5169  O   TRP A 659     4098   6570   3781    189    516    645       O  
ATOM   5170  CB  TRP A 659      14.818 120.276 218.949  1.00 36.92           C  
ANISOU 5170  CB  TRP A 659     4143   6319   3565    146    634    468       C  
ATOM   5171  CG  TRP A 659      15.659 119.405 218.083  1.00 36.24           C  
ANISOU 5171  CG  TRP A 659     4094   6265   3412     99    563    480       C  
ATOM   5172  CD1 TRP A 659      16.332 119.751 216.925  1.00 36.08           C  
ANISOU 5172  CD1 TRP A 659     4085   6238   3387    104    517    519       C  
ATOM   5173  CD2 TRP A 659      15.969 118.038 218.331  1.00 35.73           C  
ANISOU 5173  CD2 TRP A 659     4067   6236   3272     42    536    450       C  
ATOM   5174  NE1 TRP A 659      17.002 118.654 216.427  1.00 35.52           N  
ANISOU 5174  NE1 TRP A 659     4051   6201   3243     55    470    511       N  
ATOM   5175  CE2 TRP A 659      16.802 117.593 217.277  1.00 35.29           C  
ANISOU 5175  CE2 TRP A 659     4040   6196   3174     20    478    469       C  
ATOM   5176  CE3 TRP A 659      15.599 117.131 219.325  1.00 35.69           C  
ANISOU 5176  CE3 TRP A 659     4080   6250   3231      7    560    412       C  
ATOM   5177  CZ2 TRP A 659      17.269 116.270 217.202  1.00 34.83           C  
ANISOU 5177  CZ2 TRP A 659     4027   6165   3043    -29    443    447       C  
ATOM   5178  CZ3 TRP A 659      16.060 115.834 219.245  1.00 35.22           C  
ANISOU 5178  CZ3 TRP A 659     4069   6215   3098    -45    519    396       C  
ATOM   5179  CH2 TRP A 659      16.897 115.414 218.200  1.00 34.80           C  
ANISOU 5179  CH2 TRP A 659     4042   6171   3009    -58    461    412       C  
ATOM   5180  N   ALA A 660      11.808 119.627 218.135  1.00 38.29           N  
ANISOU 5180  N   ALA A 660     4101   6625   3822    166    613    570       N  
ATOM   5181  CA  ALA A 660      10.746 118.890 217.456  1.00 38.72           C  
ANISOU 5181  CA  ALA A 660     4068   6760   3882    140    563    620       C  
ATOM   5182  C   ALA A 660       9.846 119.779 216.587  1.00 39.63           C  
ANISOU 5182  C   ALA A 660     4082   6892   4083    205    535    696       C  
ATOM   5183  O   ALA A 660       9.531 119.406 215.454  1.00 39.80           O  
ANISOU 5183  O   ALA A 660     4066   6967   4089    183    450    754       O  
ATOM   5184  CB  ALA A 660       9.945 118.065 218.409  1.00 38.98           C  
ANISOU 5184  CB  ALA A 660     4070   6834   3908     99    611    586       C  
ATOM   5185  N   SER A 661       9.487 120.955 217.081  1.00 40.27           N  
ANISOU 5185  N   SER A 661     4129   6923   4250    285    600    697       N  
ATOM   5186  CA  SER A 661       8.652 121.874 216.323  1.00 41.27           C  
ANISOU 5186  CA  SER A 661     4160   7053   4467    362    575    773       C  
ATOM   5187  C   SER A 661       9.396 122.494 215.138  1.00 41.08           C  
ANISOU 5187  C   SER A 661     4187   6995   4427    382    504    828       C  
ATOM   5188  O   SER A 661       8.804 122.755 214.077  1.00 41.74           O  
ANISOU 5188  O   SER A 661     4206   7113   4542    410    432    909       O  
ATOM   5189  CB  SER A 661       8.106 122.969 217.243  1.00 42.10           C  
ANISOU 5189  CB  SER A 661     4227   7100   4671    450    676    753       C  
ATOM   5190  OG  SER A 661       7.402 123.970 216.528  1.00 43.14           O  
ANISOU 5190  OG  SER A 661     4276   7219   4898    540    652    829       O  
ATOM   5191  N   LYS A 662      10.695 122.716 215.321  1.00 40.27           N  
ANISOU 5191  N   LYS A 662     4198   6829   4274    362    523    785       N  
ATOM   5192  CA  LYS A 662      11.534 123.298 214.286  1.00 40.09           C  
ANISOU 5192  CA  LYS A 662     4234   6769   4230    370    472    828       C  
ATOM   5193  C   LYS A 662      11.859 122.302 213.183  1.00 39.62           C  
ANISOU 5193  C   LYS A 662     4196   6777   4083    300    383    858       C  
ATOM   5194  O   LYS A 662      11.939 122.687 212.002  1.00 39.94           O  
ANISOU 5194  O   LYS A 662     4241   6821   4114    312    321    927       O  
ATOM   5195  CB  LYS A 662      12.831 123.819 214.872  1.00 39.48           C  
ANISOU 5195  CB  LYS A 662     4261   6608   4131    362    524    769       C  
ATOM   5196  CG  LYS A 662      13.240 125.076 214.210  1.00 39.91           C  
ANISOU 5196  CG  LYS A 662     4346   6591   4226    411    519    817       C  
ATOM   5197  CD  LYS A 662      14.711 125.294 214.224  1.00 39.22           C  
ANISOU 5197  CD  LYS A 662     4361   6451   4091    369    532    779       C  
ATOM   5198  CE  LYS A 662      15.021 126.692 213.756  1.00 39.83           C  
ANISOU 5198  CE  LYS A 662     4473   6441   4221    417    545    823       C  
ATOM   5199  NZ  LYS A 662      16.442 127.044 214.077  1.00 39.31           N  
ANISOU 5199  NZ  LYS A 662     4499   6314   4125    374    577    770       N  
ATOM   5200  N   LEU A 663      12.050 121.034 213.562  1.00 38.96           N  
ANISOU 5200  N   LEU A 663     4134   6740   3930    229    378    807       N  
ATOM   5201  CA  LEU A 663      12.305 119.992 212.584  1.00 38.61           C  
ANISOU 5201  CA  LEU A 663     4117   6754   3799    161    301    825       C  
ATOM   5202  C   LEU A 663      11.085 119.923 211.678  1.00 39.51           C  
ANISOU 5202  C   LEU A 663     4139   6934   3937    168    229    903       C  
ATOM   5203  O   LEU A 663      11.190 119.994 210.460  1.00 39.74           O  
ANISOU 5203  O   LEU A 663     4185   6985   3931    158    158    960       O  
ATOM   5204  CB  LEU A 663      12.555 118.653 213.263  1.00 37.94           C  
ANISOU 5204  CB  LEU A 663     4068   6698   3648     91    313    758       C  
ATOM   5205  CG  LEU A 663      13.956 118.367 213.840  1.00 37.02           C  
ANISOU 5205  CG  LEU A 663     4053   6535   3479     66    349    690       C  
ATOM   5206  CD1 LEU A 663      13.932 117.288 214.966  1.00 36.62           C  
ANISOU 5206  CD1 LEU A 663     4026   6497   3391     21    380    624       C  
ATOM   5207  CD2 LEU A 663      15.006 117.986 212.790  1.00 36.57           C  
ANISOU 5207  CD2 LEU A 663     4065   6481   3349     33    302    698       C  
ATOM   5208  N   ARG A 664       9.907 119.838 212.275  1.00 40.13           N  
ANISOU 5208  N   ARG A 664     4120   7049   4080    186    249    907       N  
ATOM   5209  CA  ARG A 664       8.711 119.688 211.482  1.00 41.09           C  
ANISOU 5209  CA  ARG A 664     4139   7245   4230    186    174    979       C  
ATOM   5210  C   ARG A 664       8.487 120.899 210.613  1.00 41.89           C  
ANISOU 5210  C   ARG A 664     4209   7322   4386    263    132   1062       C  
ATOM   5211  O   ARG A 664       7.907 120.803 209.510  1.00 42.59           O  
ANISOU 5211  O   ARG A 664     4254   7467   4463    253     35   1137       O  
ATOM   5212  CB  ARG A 664       7.512 119.469 212.375  1.00 41.74           C  
ANISOU 5212  CB  ARG A 664     4107   7368   4385    195    217    965       C  
ATOM   5213  CG  ARG A 664       7.543 118.143 212.999  1.00 41.18           C  
ANISOU 5213  CG  ARG A 664     4063   7334   4251    105    237    903       C  
ATOM   5214  CD  ARG A 664       6.164 117.693 213.352  1.00 42.09           C  
ANISOU 5214  CD  ARG A 664     4049   7523   4422     85    241    916       C  
ATOM   5215  NE  ARG A 664       6.202 116.628 214.347  1.00 41.62           N  
ANISOU 5215  NE  ARG A 664     4025   7474   4317     11    298    846       N  
ATOM   5216  CZ  ARG A 664       6.315 116.839 215.644  1.00 41.44           C  
ANISOU 5216  CZ  ARG A 664     4020   7408   4318     34    405    788       C  
ATOM   5217  NH1 ARG A 664       6.390 118.071 216.158  1.00 41.68           N  
ANISOU 5217  NH1 ARG A 664     4037   7379   4422    129    474    783       N  
ATOM   5218  NH2 ARG A 664       6.340 115.791 216.420  1.00 41.10           N  
ANISOU 5218  NH2 ARG A 664     4018   7378   4221    -42    442    735       N  
ATOM   5219  N   GLU A 665       8.961 122.035 211.111  1.00 41.87           N  
ANISOU 5219  N   GLU A 665     4238   7231   4439    336    201   1051       N  
ATOM   5220  CA  GLU A 665       8.761 123.283 210.424  1.00 42.71           C  
ANISOU 5220  CA  GLU A 665     4326   7295   4608    418    174   1130       C  
ATOM   5221  C   GLU A 665       9.598 123.380 209.152  1.00 42.49           C  
ANISOU 5221  C   GLU A 665     4389   7258   4498    386    103   1178       C  
ATOM   5222  O   GLU A 665       9.109 123.876 208.140  1.00 43.38           O  
ANISOU 5222  O   GLU A 665     4472   7387   4625    419     27   1269       O  
ATOM   5223  CB  GLU A 665       9.071 124.438 211.346  1.00 42.80           C  
ANISOU 5223  CB  GLU A 665     4361   7204   4697    495    274   1097       C  
ATOM   5224  CG  GLU A 665       8.367 125.683 210.934  1.00 44.05           C  
ANISOU 5224  CG  GLU A 665     4460   7321   4956    600    261   1179       C  
ATOM   5225  CD  GLU A 665       9.047 126.925 211.454  1.00 50.41           C  
ANISOU 5225  CD  GLU A 665     5340   8002   5811    662    343   1156       C  
ATOM   5226  OE1 GLU A 665       9.706 126.852 212.535  1.00 52.88           O  
ANISOU 5226  OE1 GLU A 665     5713   8269   6109    638    430   1063       O  
ATOM   5227  OE2 GLU A 665       8.923 127.982 210.781  1.00 53.04           O  
ANISOU 5227  OE2 GLU A 665     5679   8279   6195    733    316   1232       O  
ATOM   5228  N   LEU A 666      10.844 122.896 209.210  1.00 41.40           N  
ANISOU 5228  N   LEU A 666     4360   7098   4274    323    128   1119       N  
ATOM   5229  CA  LEU A 666      11.779 123.075 208.105  1.00 41.22           C  
ANISOU 5229  CA  LEU A 666     4430   7056   4175    295     87   1153       C  
ATOM   5230  C   LEU A 666      12.000 121.814 207.290  1.00 40.85           C  
ANISOU 5230  C   LEU A 666     4421   7084   4015    206     21   1148       C  
ATOM   5231  O   LEU A 666      12.209 121.888 206.079  1.00 41.20           O  
ANISOU 5231  O   LEU A 666     4510   7145   3998    185    -42   1206       O  
ATOM   5232  CB  LEU A 666      13.116 123.650 208.581  1.00 40.51           C  
ANISOU 5232  CB  LEU A 666     4434   6880   4080    296    165   1101       C  
ATOM   5233  CG  LEU A 666      13.140 125.064 209.179  1.00 40.97           C  
ANISOU 5233  CG  LEU A 666     4491   6841   4236    377    229   1109       C  
ATOM   5234  CD1 LEU A 666      14.451 125.371 209.928  1.00 40.20           C  
ANISOU 5234  CD1 LEU A 666     4477   6670   4127    355    307   1032       C  
ATOM   5235  CD2 LEU A 666      12.881 126.135 208.167  1.00 41.96           C  
ANISOU 5235  CD2 LEU A 666     4621   6930   4392    430    185   1210       C  
ATOM   5236  N   LYS A 667      11.926 120.659 207.932  1.00 40.25           N  
ANISOU 5236  N   LYS A 667     4336   7050   3907    151     37   1080       N  
ATOM   5237  CA  LYS A 667      12.215 119.411 207.253  1.00 39.90           C  
ANISOU 5237  CA  LYS A 667     4343   7062   3755     66    -15   1062       C  
ATOM   5238  C   LYS A 667      11.419 119.250 205.916  1.00 40.84           C  
ANISOU 5238  C   LYS A 667     4436   7248   3833     42   -124   1145       C  
ATOM   5239  O   LYS A 667      10.249 119.605 205.842  1.00 41.74           O  
ANISOU 5239  O   LYS A 667     4451   7398   4013     77   -169   1202       O  
ATOM   5240  CB  LYS A 667      11.995 118.239 208.206  1.00 39.37           C  
ANISOU 5240  CB  LYS A 667     4258   7025   3674     17     13    987       C  
ATOM   5241  CG  LYS A 667      10.585 117.779 208.371  1.00 40.07           C  
ANISOU 5241  CG  LYS A 667     4242   7181   3801      3    -26   1011       C  
ATOM   5242  CD  LYS A 667      10.493 116.704 209.435  1.00 39.53           C  
ANISOU 5242  CD  LYS A 667     4174   7127   3720    -47     19    935       C  
ATOM   5243  CE  LYS A 667       9.193 115.904 209.302  1.00 40.27           C  
ANISOU 5243  CE  LYS A 667     4179   7302   3819    -99    -36    957       C  
ATOM   5244  NZ  LYS A 667       8.894 115.363 207.899  1.00 40.82           N  
ANISOU 5244  NZ  LYS A 667     4262   7432   3815   -159   -147   1007       N  
ATOM   5245  N   THR A 668      12.058 118.736 204.867  1.00 40.73           N  
ANISOU 5245  N   THR A 668     4513   7253   3711    -15   -166   1151       N  
ATOM   5246  CA  THR A 668      11.436 118.630 203.551  1.00 41.68           C  
ANISOU 5246  CA  THR A 668     4633   7432   3774    -45   -273   1228       C  
ATOM   5247  C   THR A 668      11.006 117.200 203.306  1.00 41.70           C  
ANISOU 5247  C   THR A 668     4640   7505   3700   -135   -327   1194       C  
ATOM   5248  O   THR A 668      10.235 116.944 202.398  1.00 42.60           O  
ANISOU 5248  O   THR A 668     4733   7681   3772   -172   -426   1250       O  
ATOM   5249  CB  THR A 668      12.388 119.030 202.414  1.00 41.78           C  
ANISOU 5249  CB  THR A 668     4757   7418   3701    -58   -285   1262       C  
ATOM   5250  OG1 THR A 668      13.575 118.249 202.520  1.00 40.84           O  
ANISOU 5250  OG1 THR A 668     4732   7279   3506   -108   -225   1180       O  
ATOM   5251  CG2 THR A 668      12.758 120.474 202.509  1.00 41.97           C  
ANISOU 5251  CG2 THR A 668     4783   7368   3794     21   -241   1307       C  
ATOM   5252  N   ASP A 669      11.508 116.261 204.098  1.00 40.80           N  
ANISOU 5252  N   ASP A 669     4560   7378   3563   -174   -267   1105       N  
ATOM   5253  CA  ASP A 669      11.022 114.878 204.051  1.00 40.86           C  
ANISOU 5253  CA  ASP A 669     4572   7441   3512   -261   -309   1067       C  
ATOM   5254  C   ASP A 669       9.642 114.728 204.727  1.00 41.43           C  
ANISOU 5254  C   ASP A 669     4511   7563   3667   -262   -333   1083       C  
ATOM   5255  O   ASP A 669       9.071 115.673 205.321  1.00 41.75           O  
ANISOU 5255  O   ASP A 669     4452   7593   3817   -188   -308   1117       O  
ATOM   5256  CB  ASP A 669      11.993 113.998 204.804  1.00 39.79           C  
ANISOU 5256  CB  ASP A 669     4515   7265   3340   -289   -232    972       C  
ATOM   5257  CG  ASP A 669      12.023 114.346 206.283  1.00 40.99           C  
ANISOU 5257  CG  ASP A 669     4611   7377   3587   -238   -148    932       C  
ATOM   5258  OD1 ASP A 669      12.478 115.464 206.602  1.00 43.69           O  
ANISOU 5258  OD1 ASP A 669     4944   7670   3988   -166    -99    945       O  
ATOM   5259  OD2 ASP A 669      11.543 113.545 207.126  1.00 45.48           O  
ANISOU 5259  OD2 ASP A 669     5150   7961   4170   -272   -130    890       O  
ATOM   5260  N   SER A 670       9.124 113.511 204.689  1.00 41.62           N  
ANISOU 5260  N   SER A 670     4534   7636   3643   -349   -373   1054       N  
ATOM   5261  CA  SER A 670       7.879 113.255 205.370  1.00 42.18           C  
ANISOU 5261  CA  SER A 670     4480   7758   3791   -365   -385   1062       C  
ATOM   5262  C   SER A 670       7.985 112.053 206.262  1.00 41.60           C  
ANISOU 5262  C   SER A 670     4439   7675   3691   -432   -333    981       C  
ATOM   5263  O   SER A 670       7.076 111.252 206.304  1.00 42.45           O  
ANISOU 5263  O   SER A 670     4495   7837   3795   -505   -375    980       O  
ATOM   5264  CB  SER A 670       6.747 113.054 204.378  1.00 43.48           C  
ANISOU 5264  CB  SER A 670     4573   8008   3938   -417   -509   1130       C  
ATOM   5265  OG  SER A 670       7.090 111.979 203.530  1.00 45.12           O  
ANISOU 5265  OG  SER A 670     4892   8233   4017   -516   -565   1102       O  
ATOM   5266  N   ASN A 671       9.077 111.932 207.004  1.00 40.52           N  
ANISOU 5266  N   ASN A 671     4387   7468   3540   -408   -245    916       N  
ATOM   5267  CA  ASN A 671       9.160 110.870 208.012  1.00 40.02           C  
ANISOU 5267  CA  ASN A 671     4356   7388   3462   -458   -192    845       C  
ATOM   5268  C   ASN A 671       8.626 111.383 209.343  1.00 40.00           C  
ANISOU 5268  C   ASN A 671     4259   7376   3562   -410   -116    836       C  
ATOM   5269  O   ASN A 671       8.385 112.574 209.496  1.00 40.24           O  
ANISOU 5269  O   ASN A 671     4214   7401   3673   -329    -96    874       O  
ATOM   5270  CB  ASN A 671      10.585 110.332 208.086  1.00 39.04           C  
ANISOU 5270  CB  ASN A 671     4373   7199   3262   -462   -148    782       C  
ATOM   5271  CG  ASN A 671      11.102 109.882 206.696  1.00 39.22           C  
ANISOU 5271  CG  ASN A 671     4491   7230   3180   -505   -211    790       C  
ATOM   5272  OD1 ASN A 671      10.460 109.079 206.003  1.00 41.55           O  
ANISOU 5272  OD1 ASN A 671     4797   7571   3419   -586   -281    799       O  
ATOM   5273  ND2 ASN A 671      12.244 110.423 206.281  1.00 38.73           N  
ANISOU 5273  ND2 ASN A 671     4498   7126   3092   -457   -183    785       N  
ATOM   5274  N   GLU A 672       8.390 110.508 210.303  1.00 39.83           N  
ANISOU 5274  N   GLU A 672     4244   7353   3537   -460    -72    787       N  
ATOM   5275  CA  GLU A 672       7.804 111.015 211.516  1.00 39.98           C  
ANISOU 5275  CA  GLU A 672     4175   7369   3647   -419      4    780       C  
ATOM   5276  C   GLU A 672       8.856 111.404 212.496  1.00 39.06           C  
ANISOU 5276  C   GLU A 672     4131   7175   3533   -361     92    729       C  
ATOM   5277  O   GLU A 672       9.862 110.708 212.711  1.00 38.30           O  
ANISOU 5277  O   GLU A 672     4150   7035   3367   -386    107    679       O  
ATOM   5278  CB  GLU A 672       6.718 110.109 212.137  1.00 40.61           C  
ANISOU 5278  CB  GLU A 672     4191   7496   3741   -499     16    768       C  
ATOM   5279  CG  GLU A 672       7.151 108.707 212.621  1.00 40.49           C  
ANISOU 5279  CG  GLU A 672     4290   7453   3643   -586     34    707       C  
ATOM   5280  CD  GLU A 672       5.977 107.672 212.607  1.00 46.56           C  
ANISOU 5280  CD  GLU A 672     5002   8283   4405   -699      2    715       C  
ATOM   5281  OE1 GLU A 672       4.917 107.923 211.952  1.00 49.41           O  
ANISOU 5281  OE1 GLU A 672     5241   8719   4811   -719    -60    768       O  
ATOM   5282  OE2 GLU A 672       6.121 106.589 213.238  1.00 46.87           O  
ANISOU 5282  OE2 GLU A 672     5120   8294   4392   -770     34    669       O  
ATOM   5283  N   VAL A 673       8.598 112.583 213.038  1.00 39.25           N  
ANISOU 5283  N   VAL A 673     4083   7185   3646   -280    143    745       N  
ATOM   5284  CA  VAL A 673       9.215 113.083 214.234  1.00 38.70           C  
ANISOU 5284  CA  VAL A 673     4051   7053   3601   -230    235    697       C  
ATOM   5285  C   VAL A 673       8.209 113.053 215.402  1.00 39.26           C  
ANISOU 5285  C   VAL A 673     4043   7143   3731   -234    308    681       C  
ATOM   5286  O   VAL A 673       7.431 113.984 215.568  1.00 39.96           O  
ANISOU 5286  O   VAL A 673     4027   7246   3909   -174    337    711       O  
ATOM   5287  CB  VAL A 673       9.642 114.490 213.949  1.00 38.67           C  
ANISOU 5287  CB  VAL A 673     4033   7009   3649   -138    247    724       C  
ATOM   5288  CG1 VAL A 673      10.146 115.170 215.188  1.00 38.31           C  
ANISOU 5288  CG1 VAL A 673     4017   6900   3639    -86    340    676       C  
ATOM   5289  CG2 VAL A 673      10.699 114.441 212.928  1.00 38.14           C  
ANISOU 5289  CG2 VAL A 673     4053   6922   3517   -144    193    733       C  
ATOM   5290  N   LEU A 674       8.196 111.983 216.190  1.00 39.07           N  
ANISOU 5290  N   LEU A 674     4068   7119   3658   -303    340    636       N  
ATOM   5291  CA  LEU A 674       7.313 111.921 217.393  1.00 39.64           C  
ANISOU 5291  CA  LEU A 674     4080   7206   3775   -315    425    615       C  
ATOM   5292  C   LEU A 674       8.004 112.450 218.646  1.00 39.17           C  
ANISOU 5292  C   LEU A 674     4089   7080   3716   -267    517    562       C  
ATOM   5293  O   LEU A 674       9.196 112.279 218.812  1.00 38.33           O  
ANISOU 5293  O   LEU A 674     4097   6919   3548   -263    510    528       O  
ATOM   5294  CB  LEU A 674       6.770 110.494 217.631  1.00 39.92           C  
ANISOU 5294  CB  LEU A 674     4131   7278   3758   -426    416    601       C  
ATOM   5295  CG  LEU A 674       6.342 109.742 216.343  1.00 40.28           C  
ANISOU 5295  CG  LEU A 674     4150   7380   3773   -496    310    641       C  
ATOM   5296  CD1 LEU A 674       5.833 108.332 216.571  1.00 40.63           C  
ANISOU 5296  CD1 LEU A 674     4222   7450   3765   -615    302    624       C  
ATOM   5297  CD2 LEU A 674       5.315 110.539 215.572  1.00 41.21           C  
ANISOU 5297  CD2 LEU A 674     4116   7565   3978   -461    268    705       C  
ATOM   5298  N   LEU A 675       7.279 113.117 219.525  1.00 39.81           N  
ANISOU 5298  N   LEU A 675     4099   7163   3865   -228    604    554       N  
ATOM   5299  CA  LEU A 675       7.889 113.589 220.772  1.00 39.50           C  
ANISOU 5299  CA  LEU A 675     4137   7059   3814   -193    692    497       C  
ATOM   5300  C   LEU A 675       7.101 113.149 221.982  1.00 40.13           C  
ANISOU 5300  C   LEU A 675     4199   7156   3893   -234    785    467       C  
ATOM   5301  O   LEU A 675       6.055 113.701 222.226  1.00 41.06           O  
ANISOU 5301  O   LEU A 675     4204   7306   4092   -203    845    481       O  
ATOM   5302  CB  LEU A 675       7.976 115.105 220.762  1.00 39.72           C  
ANISOU 5302  CB  LEU A 675     4123   7047   3920    -90    728    505       C  
ATOM   5303  CG  LEU A 675       7.918 115.865 222.085  1.00 40.06           C  
ANISOU 5303  CG  LEU A 675     4186   7042   3992    -45    843    455       C  
ATOM   5304  CD1 LEU A 675       9.211 115.724 222.916  1.00 39.23           C  
ANISOU 5304  CD1 LEU A 675     4233   6871   3802    -61    860    394       C  
ATOM   5305  CD2 LEU A 675       7.671 117.297 221.730  1.00 40.56           C  
ANISOU 5305  CD2 LEU A 675     4180   7079   4153     56    863    482       C  
ATOM   5306  N   LYS A 676       7.615 112.177 222.740  1.00 39.72           N  
ANISOU 5306  N   LYS A 676     4260   7080   3751   -301    801    426       N  
ATOM   5307  CA  LYS A 676       6.981 111.702 223.992  1.00 40.33           C  
ANISOU 5307  CA  LYS A 676     4350   7165   3807   -350    896    395       C  
ATOM   5308  C   LYS A 676       7.362 112.483 225.267  1.00 40.40           C  
ANISOU 5308  C   LYS A 676     4424   7117   3808   -303    995    342       C  
ATOM   5309  O   LYS A 676       8.474 112.381 225.768  1.00 39.71           O  
ANISOU 5309  O   LYS A 676     4466   6973   3648   -303    982    306       O  
ATOM   5310  CB  LYS A 676       7.200 110.197 224.201  1.00 40.08           C  
ANISOU 5310  CB  LYS A 676     4413   7135   3679   -453    865    385       C  
ATOM   5311  CG  LYS A 676       6.219 109.612 225.205  1.00 43.20           C  
ANISOU 5311  CG  LYS A 676     4791   7559   4064   -523    957    372       C  
ATOM   5312  CD  LYS A 676       6.585 108.196 225.691  1.00 49.24           C  
ANISOU 5312  CD  LYS A 676     5688   8301   4722   -621    941    357       C  
ATOM   5313  CE  LYS A 676       5.847 107.860 227.011  1.00 52.14           C  
ANISOU 5313  CE  LYS A 676     6071   8675   5063   -679   1058    334       C  
ATOM   5314  NZ  LYS A 676       6.155 108.877 228.107  1.00 54.67           N  
ANISOU 5314  NZ  LYS A 676     6433   8956   5384   -610   1152    291       N  
ATOM   5315  N   MET A 677       6.405 113.247 225.780  1.00 41.35           N  
ANISOU 5315  N   MET A 677     4451   7255   4004   -263   1092    337       N  
ATOM   5316  CA  MET A 677       6.556 114.022 226.995  1.00 42.84           C  
ANISOU 5316  CA  MET A 677     4695   7393   4188   -222   1200    284       C  
ATOM   5317  C   MET A 677       5.819 113.367 228.187  1.00 44.67           C  
ANISOU 5317  C   MET A 677     4948   7647   4379   -290   1307    254       C  
ATOM   5318  O   MET A 677       4.589 113.472 228.282  1.00 45.82           O  
ANISOU 5318  O   MET A 677     4967   7846   4597   -291   1381    270       O  
ATOM   5319  CB  MET A 677       5.972 115.403 226.715  1.00 43.82           C  
ANISOU 5319  CB  MET A 677     4704   7513   4431   -119   1248    297       C  
ATOM   5320  CG  MET A 677       6.098 116.369 227.819  1.00 45.20           C  
ANISOU 5320  CG  MET A 677     4932   7628   4614    -65   1360    239       C  
ATOM   5321  SD  MET A 677       7.830 116.822 227.908  1.00 49.03           S  
ANISOU 5321  SD  MET A 677     5581   8024   5026    -45   1294    202       S  
ATOM   5322  CE  MET A 677       7.907 118.276 226.864  1.00 46.59           C  
ANISOU 5322  CE  MET A 677     5189   7681   4831     67   1262    238       C  
ATOM   5323  N   ASP A 678       6.548 112.691 229.087  1.00 45.88           N  
ANISOU 5323  N   ASP A 678     5254   7761   4418   -347   1316    216       N  
ATOM   5324  CA  ASP A 678       5.957 112.242 230.360  1.00 48.18           C  
ANISOU 5324  CA  ASP A 678     5591   8059   4657   -406   1432    183       C  
ATOM   5325  C   ASP A 678       5.948 113.422 231.298  1.00 48.89           C  
ANISOU 5325  C   ASP A 678     5706   8105   4765   -340   1544    131       C  
ATOM   5326  O   ASP A 678       6.994 113.836 231.783  1.00 48.55           O  
ANISOU 5326  O   ASP A 678     5787   7998   4662   -315   1526     92       O  
ATOM   5327  CB  ASP A 678       6.671 111.034 231.027  1.00 48.68           C  
ANISOU 5327  CB  ASP A 678     5819   8094   4584   -495   1400    168       C  
ATOM   5328  CG  ASP A 678       5.938 110.536 232.394  1.00 53.50           C  
ANISOU 5328  CG  ASP A 678     6484   8713   5130   -569   1532    140       C  
ATOM   5329  OD1 ASP A 678       4.733 110.845 232.655  1.00 55.25           O  
ANISOU 5329  OD1 ASP A 678     6591   8982   5419   -571   1645    140       O  
ATOM   5330  OD2 ASP A 678       6.562 109.804 233.213  1.00 55.74           O  
ANISOU 5330  OD2 ASP A 678     6926   8959   5295   -628   1525    121       O  
ATOM   5331  N   LEU A 679       4.758 113.965 231.533  1.00 50.49           N  
ANISOU 5331  N   LEU A 679     5786   8345   5054   -310   1657    130       N  
ATOM   5332  CA  LEU A 679       4.577 115.113 232.406  1.00 51.76           C  
ANISOU 5332  CA  LEU A 679     5961   8462   5242   -241   1783     76       C  
ATOM   5333  C   LEU A 679       4.701 114.709 233.876  1.00 52.74           C  
ANISOU 5333  C   LEU A 679     6232   8560   5247   -306   1883     19       C  
ATOM   5334  O   LEU A 679       4.430 115.513 234.755  1.00 54.00           O  
ANISOU 5334  O   LEU A 679     6418   8688   5412   -267   2008    -33       O  
ATOM   5335  CB  LEU A 679       3.203 115.766 232.169  1.00 52.98           C  
ANISOU 5335  CB  LEU A 679     5926   8667   5536   -181   1879     95       C  
ATOM   5336  CG  LEU A 679       2.501 115.749 230.799  1.00 53.22           C  
ANISOU 5336  CG  LEU A 679     5769   8765   5685   -152   1798    169       C  
ATOM   5337  CD1 LEU A 679       0.993 115.568 230.954  1.00 52.90           C  
ANISOU 5337  CD1 LEU A 679     5561   8807   5733   -167   1901    189       C  
ATOM   5338  CD2 LEU A 679       2.808 116.985 229.967  1.00 52.99           C  
ANISOU 5338  CD2 LEU A 679     5686   8697   5751    -33   1746    189       C  
ATOM   5339  N   GLU A 680       5.111 113.474 234.146  1.00 53.09           N  
ANISOU 5339  N   GLU A 680     6381   8611   5180   -404   1829     29       N  
ATOM   5340  CA  GLU A 680       5.164 112.974 235.520  1.00 54.93           C  
ANISOU 5340  CA  GLU A 680     6758   8823   5290   -476   1918    -13       C  
ATOM   5341  C   GLU A 680       6.585 112.789 236.051  1.00 54.01           C  
ANISOU 5341  C   GLU A 680     6838   8638   5046   -494   1835    -42       C  
ATOM   5342  O   GLU A 680       6.805 112.783 237.265  1.00 54.79           O  
ANISOU 5342  O   GLU A 680     7074   8702   5041   -528   1906    -89       O  
ATOM   5343  CB  GLU A 680       4.423 111.644 235.630  1.00 56.17           C  
ANISOU 5343  CB  GLU A 680     6898   9037   5408   -586   1938     22       C  
ATOM   5344  CG  GLU A 680       2.956 111.638 235.134  1.00 59.94           C  
ANISOU 5344  CG  GLU A 680     7170   9596   6009   -590   2013     56       C  
ATOM   5345  CD  GLU A 680       1.971 112.242 236.123  1.00 64.44           C  
ANISOU 5345  CD  GLU A 680     7693  10183   6608   -576   2205     14       C  
ATOM   5346  OE1 GLU A 680       2.033 113.476 236.375  1.00 65.69           O  
ANISOU 5346  OE1 GLU A 680     7838  10305   6818   -478   2270    -28       O  
ATOM   5347  OE2 GLU A 680       1.120 111.476 236.636  1.00 66.13           O  
ANISOU 5347  OE2 GLU A 680     7884  10445   6798   -666   2296     22       O  
ATOM   5348  N   SER A 681       7.532 112.662 235.122  1.00 52.75           N  
ANISOU 5348  N   SER A 681     6685   8462   4896   -470   1686    -14       N  
ATOM   5349  CA  SER A 681       8.936 112.332 235.395  1.00 51.50           C  
ANISOU 5349  CA  SER A 681     6684   8251   4633   -486   1581    -28       C  
ATOM   5350  C   SER A 681       9.953 113.424 235.077  1.00 50.47           C  
ANISOU 5350  C   SER A 681     6571   8071   4534   -407   1519    -54       C  
ATOM   5351  O   SER A 681       9.610 114.465 234.520  1.00 49.77           O  
ANISOU 5351  O   SER A 681     6376   7981   4552   -335   1549    -55       O  
ATOM   5352  CB  SER A 681       9.322 111.094 234.588  1.00 50.81           C  
ANISOU 5352  CB  SER A 681     6602   8182   4520   -533   1456     25       C  
ATOM   5353  OG  SER A 681       9.238 111.337 233.197  1.00 50.31           O  
ANISOU 5353  OG  SER A 681     6406   8147   4563   -486   1384     63       O  
ATOM   5354  N   GLY A 682      11.212 113.149 235.419  1.00 50.21           N  
ANISOU 5354  N   GLY A 682     6670   7996   4410   -424   1428    -69       N  
ATOM   5355  CA  GLY A 682      12.314 114.078 235.175  1.00 50.75           C  
ANISOU 5355  CA  GLY A 682     6766   8019   4498   -367   1360    -94       C  
ATOM   5356  C   GLY A 682      13.285 113.680 234.057  1.00 50.48           C  
ANISOU 5356  C   GLY A 682     6707   7987   4486   -352   1215    -54       C  
ATOM   5357  O   GLY A 682      12.893 113.433 232.897  1.00 49.69           O  
ANISOU 5357  O   GLY A 682     6495   7924   4462   -335   1179     -6       O  
ATOM   5358  N   HIS A 683      14.565 113.623 234.421  1.00 50.68           N  
ANISOU 5358  N   HIS A 683     6839   7976   4443   -358   1132    -75       N  
ATOM   5359  CA  HIS A 683      15.625 113.286 233.499  1.00 50.15           C  
ANISOU 5359  CA  HIS A 683     6758   7906   4391   -341   1005    -46       C  
ATOM   5360  C   HIS A 683      15.765 111.798 233.316  1.00 51.15           C  
ANISOU 5360  C   HIS A 683     6922   8053   4460   -387    939     -8       C  
ATOM   5361  O   HIS A 683      15.815 111.284 232.188  1.00 51.33           O  
ANISOU 5361  O   HIS A 683     6877   8099   4528   -377    879     33       O  
ATOM   5362  CB  HIS A 683      16.962 113.811 233.998  1.00 49.15           C  
ANISOU 5362  CB  HIS A 683     6719   7736   4221   -331    941    -84       C  
ATOM   5363  CG  HIS A 683      18.068 113.610 233.015  1.00 47.97           C  
ANISOU 5363  CG  HIS A 683     6537   7587   4102   -306    824    -58       C  
ATOM   5364  ND1 HIS A 683      18.244 114.433 231.921  1.00 46.15           N  
ANISOU 5364  ND1 HIS A 683     6209   7358   3969   -257    808    -45       N  
ATOM   5365  CD2 HIS A 683      19.006 112.639 232.916  1.00 46.24           C  
ANISOU 5365  CD2 HIS A 683     6367   7369   3832   -321    724    -40       C  
ATOM   5366  CE1 HIS A 683      19.268 113.997 231.214  1.00 45.85           C  
ANISOU 5366  CE1 HIS A 683     6162   7324   3934   -248    710    -24       C  
ATOM   5367  NE2 HIS A 683      19.751 112.912 231.798  1.00 46.11           N  
ANISOU 5367  NE2 HIS A 683     6280   7358   3883   -282    657    -22       N  
ATOM   5368  N   PHE A 684      15.878 111.110 234.438  1.00 52.85           N  
ANISOU 5368  N   PHE A 684     7258   8253   4569   -438    947    -21       N  
ATOM   5369  CA  PHE A 684      16.303 109.736 234.430  1.00 54.04           C  
ANISOU 5369  CA  PHE A 684     7480   8401   4652   -476    870     11       C  
ATOM   5370  C   PHE A 684      15.147 108.871 234.265  1.00 55.67           C  
ANISOU 5370  C   PHE A 684     7656   8638   4858   -525    924     43       C  
ATOM   5371  O   PHE A 684      15.264 107.736 233.823  1.00 56.40           O  
ANISOU 5371  O   PHE A 684     7769   8731   4927   -552    865     79       O  
ATOM   5372  CB  PHE A 684      16.946 109.376 235.737  1.00 53.77           C  
ANISOU 5372  CB  PHE A 684     7599   8332   4497   -510    848    -11       C  
ATOM   5373  CG  PHE A 684      18.356 109.721 235.779  1.00 54.07           C  
ANISOU 5373  CG  PHE A 684     7678   8344   4522   -474    745    -28       C  
ATOM   5374  CD1 PHE A 684      19.244 109.089 234.915  1.00 53.65           C  
ANISOU 5374  CD1 PHE A 684     7599   8290   4494   -446    636      3       C  
ATOM   5375  CD2 PHE A 684      18.809 110.710 236.639  1.00 53.95           C  
ANISOU 5375  CD2 PHE A 684     7718   8305   4474   -469    760    -77       C  
ATOM   5376  CE1 PHE A 684      20.578 109.402 234.929  1.00 54.70           C  
ANISOU 5376  CE1 PHE A 684     7753   8406   4625   -413    542    -11       C  
ATOM   5377  CE2 PHE A 684      20.132 111.029 236.674  1.00 55.13           C  
ANISOU 5377  CE2 PHE A 684     7895   8436   4615   -445    659    -92       C  
ATOM   5378  CZ  PHE A 684      21.034 110.369 235.814  1.00 56.04           C  
ANISOU 5378  CZ  PHE A 684     7973   8558   4763   -416    549    -57       C  
ATOM   5379  N   SER A 685      14.010 109.404 234.652  1.00 57.96           N  
ANISOU 5379  N   SER A 685     7898   8951   5175   -538   1043     28       N  
ATOM   5380  CA  SER A 685      12.859 108.568 234.815  1.00 59.43           C  
ANISOU 5380  CA  SER A 685     8068   9166   5345   -603   1112     53       C  
ATOM   5381  C   SER A 685      12.552 107.905 233.468  1.00 59.66           C  
ANISOU 5381  C   SER A 685     7998   9228   5441   -608   1052    101       C  
ATOM   5382  O   SER A 685      13.138 106.875 233.138  1.00 59.52           O  
ANISOU 5382  O   SER A 685     8041   9193   5380   -631    965    126       O  
ATOM   5383  CB  SER A 685      11.701 109.373 235.409  1.00 59.90           C  
ANISOU 5383  CB  SER A 685     8071   9250   5438   -606   1257     26       C  
ATOM   5384  OG  SER A 685      12.225 110.461 236.178  1.00 59.36           O  
ANISOU 5384  OG  SER A 685     8061   9145   5347   -566   1290    -27       O  
ATOM   5385  N   ALA A 686      11.710 108.525 232.657  1.00 60.50           N  
ANISOU 5385  N   ALA A 686     7957   9379   5653   -581   1092    113       N  
ATOM   5386  CA  ALA A 686      10.710 107.733 231.960  1.00 61.53           C  
ANISOU 5386  CA  ALA A 686     8004   9555   5820   -633   1099    153       C  
ATOM   5387  C   ALA A 686       9.861 107.249 233.178  1.00 62.68           C  
ANISOU 5387  C   ALA A 686     8206   9707   5901   -709   1209    143       C  
ATOM   5388  O   ALA A 686       8.732 107.729 233.368  1.00 64.26           O  
ANISOU 5388  O   ALA A 686     8308   9949   6157   -716   1315    138       O  
ATOM   5389  CB  ALA A 686      11.340 106.561 231.130  1.00 60.42           C  
ANISOU 5389  CB  ALA A 686     7908   9401   5647   -660    982    185       C  
ATOM   5390  N   SER A 687      10.418 106.365 234.019  1.00 62.40           N  
ANISOU 5390  N   SER A 687     8329   9630   5750   -760   1188    140       N  
ATOM   5391  CA  SER A 687       9.984 106.225 235.431  1.00 63.03           C  
ANISOU 5391  CA  SER A 687     8506   9697   5744   -816   1293    118       C  
ATOM   5392  C   SER A 687      10.846 105.330 236.361  1.00 62.61           C  
ANISOU 5392  C   SER A 687     8650   9587   5552   -860   1243    119       C  
ATOM   5393  O   SER A 687      11.925 104.818 235.996  1.00 61.65           O  
ANISOU 5393  O   SER A 687     8596   9429   5401   -837   1121    134       O  
ATOM   5394  CB  SER A 687       8.489 105.874 235.539  1.00 64.18           C  
ANISOU 5394  CB  SER A 687     8566   9897   5923   -888   1407    134       C  
ATOM   5395  OG  SER A 687       8.137 104.820 234.655  1.00 64.98           O  
ANISOU 5395  OG  SER A 687     8625  10020   6046   -944   1347    179       O  
ATOM   5396  N   ASP A 688      10.329 105.162 237.572  1.00 63.37           N  
ANISOU 5396  N   ASP A 688     8835   9678   5565   -921   1345    105       N  
ATOM   5397  CA  ASP A 688      10.944 104.408 238.660  1.00 63.43           C  
ANISOU 5397  CA  ASP A 688     9039   9634   5429   -969   1320    109       C  
ATOM   5398  C   ASP A 688      10.119 103.158 238.959  1.00 63.82           C  
ANISOU 5398  C   ASP A 688     9141   9686   5423  -1077   1371    148       C  
ATOM   5399  O   ASP A 688      10.003 102.768 240.107  1.00 64.77           O  
ANISOU 5399  O   ASP A 688     9399   9782   5429  -1139   1428    147       O  
ATOM   5400  CB  ASP A 688      10.976 105.331 239.857  1.00 64.26           C  
ANISOU 5400  CB  ASP A 688     9215   9729   5473   -959   1408     58       C  
ATOM   5401  CG  ASP A 688      10.006 106.518 239.690  1.00 65.80           C  
ANISOU 5401  CG  ASP A 688     9258   9970   5772   -923   1535     22       C  
ATOM   5402  OD1 ASP A 688       9.679 106.867 238.525  1.00 64.70           O  
ANISOU 5402  OD1 ASP A 688     8955   9867   5761   -877   1513     36       O  
ATOM   5403  OD2 ASP A 688       9.567 107.116 240.704  1.00 68.24           O  
ANISOU 5403  OD2 ASP A 688     9613  10279   6036   -937   1657    -20       O  
ATOM   5404  N   ARG A 689       9.608 102.515 237.897  1.00 63.19           N  
ANISOU 5404  N   ARG A 689     8961   9631   5417  -1104   1341    184       N  
ATOM   5405  CA  ARG A 689       8.628 101.435 237.957  1.00 63.46           C  
ANISOU 5405  CA  ARG A 689     9005   9679   5429  -1215   1397    219       C  
ATOM   5406  C   ARG A 689       8.923 100.212 237.045  1.00 62.20           C  
ANISOU 5406  C   ARG A 689     8872   9488   5272  -1248   1284    263       C  
ATOM   5407  O   ARG A 689      10.061  99.826 236.817  1.00 60.99           O  
ANISOU 5407  O   ARG A 689     8810   9280   5082  -1201   1165    272       O  
ATOM   5408  CB  ARG A 689       7.258 102.014 237.569  1.00 64.16           C  
ANISOU 5408  CB  ARG A 689     8902   9848   5628  -1234   1513    212       C  
ATOM   5409  CG  ARG A 689       6.173 101.931 238.611  1.00 67.51           C  
ANISOU 5409  CG  ARG A 689     9341  10301   6011  -1321   1675    204       C  
ATOM   5410  CD  ARG A 689       4.801 101.630 237.994  1.00 72.39           C  
ANISOU 5410  CD  ARG A 689     9789  10990   6725  -1391   1746    228       C  
ATOM   5411  NE  ARG A 689       4.376 100.233 238.200  1.00 79.12           N  
ANISOU 5411  NE  ARG A 689    10729  11826   7509  -1523   1755    268       N  
ATOM   5412  CZ  ARG A 689       3.193  99.697 237.825  1.00 82.30           C  
ANISOU 5412  CZ  ARG A 689    11016  12283   7969  -1620   1815    293       C  
ATOM   5413  NH1 ARG A 689       2.275 100.434 237.195  1.00 83.02           N  
ANISOU 5413  NH1 ARG A 689    10887  12460   8195  -1593   1868    286       N  
ATOM   5414  NH2 ARG A 689       2.913  98.408 238.082  1.00 82.25           N  
ANISOU 5414  NH2 ARG A 689    11116  12247   7889  -1747   1821    329       N  
ATOM   5415  N   TYR A 690       7.824  99.577 236.620  1.00 61.98           N  
ANISOU 5415  N   TYR A 690     8769   9498   5284  -1337   1334    288       N  
ATOM   5416  CA  TYR A 690       7.712  98.654 235.497  1.00 59.79           C  
ANISOU 5416  CA  TYR A 690     8457   9214   5045  -1375   1252    321       C  
ATOM   5417  C   TYR A 690       7.356  99.517 234.313  1.00 59.03           C  
ANISOU 5417  C   TYR A 690     8159   9187   5083  -1314   1232    310       C  
ATOM   5418  O   TYR A 690       7.302  99.059 233.184  1.00 58.33           O  
ANISOU 5418  O   TYR A 690     8012   9107   5043  -1325   1156    329       O  
ATOM   5419  CB  TYR A 690       6.494  97.748 235.710  1.00 60.65           C  
ANISOU 5419  CB  TYR A 690     8561   9344   5140  -1515   1335    348       C  
ATOM   5420  CG  TYR A 690       6.714  96.526 236.565  1.00 59.17           C  
ANISOU 5420  CG  TYR A 690     8580   9079   4825  -1604   1337    376       C  
ATOM   5421  CD1 TYR A 690       6.783  96.619 237.951  1.00 56.60           C  
ANISOU 5421  CD1 TYR A 690     8383   8728   4396  -1627   1417    370       C  
ATOM   5422  CD2 TYR A 690       6.835  95.266 235.982  1.00 57.21           C  
ANISOU 5422  CD2 TYR A 690     8408   8776   4553  -1666   1259    409       C  
ATOM   5423  CE1 TYR A 690       6.982  95.499 238.715  1.00 56.12           C  
ANISOU 5423  CE1 TYR A 690     8518   8591   4213  -1708   1413    403       C  
ATOM   5424  CE2 TYR A 690       7.038  94.141 236.750  1.00 55.79           C  
ANISOU 5424  CE2 TYR A 690     8426   8515   4258  -1744   1258    440       C  
ATOM   5425  CZ  TYR A 690       7.112  94.266 238.108  1.00 55.89           C  
ANISOU 5425  CZ  TYR A 690     8560   8505   4171  -1763   1332    440       C  
ATOM   5426  OH  TYR A 690       7.323  93.141 238.860  1.00 58.14           O  
ANISOU 5426  OH  TYR A 690     9051   8704   4337  -1839   1325    478       O  
ATOM   5427  N   LYS A 691       7.047 100.775 234.581  1.00 59.05           N  
ANISOU 5427  N   LYS A 691     8058   9238   5142  -1253   1306    281       N  
ATOM   5428  CA  LYS A 691       6.668 101.690 233.525  1.00 58.81           C  
ANISOU 5428  CA  LYS A 691     7837   9270   5239  -1189   1292    277       C  
ATOM   5429  C   LYS A 691       7.886 102.223 232.767  1.00 57.52           C  
ANISOU 5429  C   LYS A 691     7679   9077   5100  -1079   1175    267       C  
ATOM   5430  O   LYS A 691       7.802 102.602 231.587  1.00 57.11           O  
ANISOU 5430  O   LYS A 691     7505   9061   5135  -1037   1120    277       O  
ATOM   5431  CB  LYS A 691       5.736 102.783 234.063  1.00 59.62           C  
ANISOU 5431  CB  LYS A 691     7819   9431   5404  -1167   1427    253       C  
ATOM   5432  CG  LYS A 691       4.296 102.266 234.371  1.00 62.25           C  
ANISOU 5432  CG  LYS A 691     8074   9821   5757  -1279   1540    271       C  
ATOM   5433  CD  LYS A 691       3.635 101.547 233.139  1.00 63.75           C  
ANISOU 5433  CD  LYS A 691     8148  10056   6016  -1342   1473    310       C  
ATOM   5434  CE  LYS A 691       2.772 100.333 233.526  1.00 64.44           C  
ANISOU 5434  CE  LYS A 691     8272  10155   6059  -1494   1530    336       C  
ATOM   5435  NZ  LYS A 691       1.350 100.726 233.671  1.00 66.33           N  
ANISOU 5435  NZ  LYS A 691     8332  10485   6387  -1539   1654    339       N  
ATOM   5436  N   TYR A 692       9.027 102.215 233.438  1.00 57.10           N  
ANISOU 5436  N   TYR A 692     7770   8960   4965  -1039   1135    250       N  
ATOM   5437  CA  TYR A 692      10.288 102.458 232.779  1.00 55.93           C  
ANISOU 5437  CA  TYR A 692     7646   8778   4827   -952   1020    244       C  
ATOM   5438  C   TYR A 692      10.358 101.520 231.605  1.00 55.58           C  
ANISOU 5438  C   TYR A 692     7586   8729   4802   -979    931    274       C  
ATOM   5439  O   TYR A 692      10.550 101.944 230.467  1.00 55.49           O  
ANISOU 5439  O   TYR A 692     7478   8742   4864   -927    874    277       O  
ATOM   5440  CB  TYR A 692      11.439 102.162 233.730  1.00 55.97           C  
ANISOU 5440  CB  TYR A 692     7825   8714   4727   -934    977    232       C  
ATOM   5441  CG  TYR A 692      12.811 102.345 233.133  1.00 56.53           C  
ANISOU 5441  CG  TYR A 692     7918   8751   4808   -847    860    226       C  
ATOM   5442  CD1 TYR A 692      13.426 101.313 232.425  1.00 58.18           C  
ANISOU 5442  CD1 TYR A 692     8180   8924   5001   -849    764    250       C  
ATOM   5443  CD2 TYR A 692      13.505 103.550 233.276  1.00 56.90           C  
ANISOU 5443  CD2 TYR A 692     7936   8801   4884   -766    850    194       C  
ATOM   5444  CE1 TYR A 692      14.691 101.474 231.874  1.00 58.22           C  
ANISOU 5444  CE1 TYR A 692     8197   8903   5022   -767    666    242       C  
ATOM   5445  CE2 TYR A 692      14.770 103.718 232.732  1.00 56.85           C  
ANISOU 5445  CE2 TYR A 692     7940   8768   4891   -694    747    189       C  
ATOM   5446  CZ  TYR A 692      15.356 102.676 232.035  1.00 57.90           C  
ANISOU 5446  CZ  TYR A 692     8116   8873   5011   -693    659    213       C  
ATOM   5447  OH  TYR A 692      16.609 102.823 231.489  1.00 58.35           O  
ANISOU 5447  OH  TYR A 692     8175   8908   5087   -620    568    207       O  
ATOM   5448  N   LEU A 693      10.182 100.238 231.885  1.00 56.16           N  
ANISOU 5448  N   LEU A 693     7766   8767   4806  -1064    924    295       N  
ATOM   5449  CA  LEU A 693      10.263  99.214 230.851  1.00 56.30           C  
ANISOU 5449  CA  LEU A 693     7797   8765   4828  -1099    844    318       C  
ATOM   5450  C   LEU A 693       9.224  99.390 229.732  1.00 56.46           C  
ANISOU 5450  C   LEU A 693     7654   8858   4939  -1134    851    331       C  
ATOM   5451  O   LEU A 693       9.505  99.107 228.577  1.00 55.68           O  
ANISOU 5451  O   LEU A 693     7528   8758   4869  -1119    770    338       O  
ATOM   5452  CB  LEU A 693      10.188  97.814 231.469  1.00 56.74           C  
ANISOU 5452  CB  LEU A 693     8009   8758   4790  -1192    845    340       C  
ATOM   5453  CG  LEU A 693      11.373  97.301 232.309  1.00 56.56           C  
ANISOU 5453  CG  LEU A 693     8170   8649   4671  -1157    796    341       C  
ATOM   5454  CD1 LEU A 693      11.141  95.818 232.670  1.00 57.18           C  
ANISOU 5454  CD1 LEU A 693     8396   8662   4669  -1256    792    372       C  
ATOM   5455  CD2 LEU A 693      12.771  97.496 231.675  1.00 54.37           C  
ANISOU 5455  CD2 LEU A 693     7911   8337   4409  -1045    686    329       C  
ATOM   5456  N   ARG A 694       8.040  99.870 230.098  1.00 57.44           N  
ANISOU 5456  N   ARG A 694     7671   9047   5108  -1178    948    333       N  
ATOM   5457  CA  ARG A 694       6.969 100.148 229.162  1.00 57.96           C  
ANISOU 5457  CA  ARG A 694     7563   9191   5267  -1207    957    348       C  
ATOM   5458  C   ARG A 694       7.396 101.244 228.201  1.00 56.97           C  
ANISOU 5458  C   ARG A 694     7329   9096   5220  -1098    901    342       C  
ATOM   5459  O   ARG A 694       7.197 101.126 226.992  1.00 56.55           O  
ANISOU 5459  O   ARG A 694     7200   9074   5212  -1103    833    360       O  
ATOM   5460  CB  ARG A 694       5.758 100.639 229.934  1.00 59.31           C  
ANISOU 5460  CB  ARG A 694     7634   9423   5476  -1249   1085    347       C  
ATOM   5461  CG  ARG A 694       4.443 100.116 229.432  1.00 62.42           C  
ANISOU 5461  CG  ARG A 694     7910   9884   5922  -1354   1109    374       C  
ATOM   5462  CD  ARG A 694       3.959  99.045 230.360  1.00 66.45           C  
ANISOU 5462  CD  ARG A 694     8524  10369   6356  -1479   1178    382       C  
ATOM   5463  NE  ARG A 694       2.992  98.164 229.717  1.00 70.72           N  
ANISOU 5463  NE  ARG A 694     8999  10949   6924  -1602   1162    409       N  
ATOM   5464  CZ  ARG A 694       2.388  97.152 230.332  1.00 72.43           C  
ANISOU 5464  CZ  ARG A 694     9284  11151   7087  -1734   1220    422       C  
ATOM   5465  NH1 ARG A 694       2.637  96.889 231.617  1.00 73.89           N  
ANISOU 5465  NH1 ARG A 694     9610  11282   7183  -1758   1300    415       N  
ATOM   5466  NH2 ARG A 694       1.530  96.407 229.661  1.00 72.28           N  
ANISOU 5466  NH2 ARG A 694     9195  11169   7098  -1850   1197    445       N  
ATOM   5467  N   GLU A 695       7.967 102.309 228.772  1.00 56.47           N  
ANISOU 5467  N   GLU A 695     7269   9020   5166  -1005    933    318       N  
ATOM   5468  CA  GLU A 695       8.519 103.461 228.041  1.00 55.39           C  
ANISOU 5468  CA  GLU A 695     7053   8898   5097   -897    889    311       C  
ATOM   5469  C   GLU A 695       9.595 103.053 227.067  1.00 52.99           C  
ANISOU 5469  C   GLU A 695     6806   8556   4771   -863    775    315       C  
ATOM   5470  O   GLU A 695       9.647 103.523 225.938  1.00 52.27           O  
ANISOU 5470  O   GLU A 695     6628   8495   4738   -822    722    327       O  
ATOM   5471  CB  GLU A 695       9.142 104.447 229.036  1.00 56.17           C  
ANISOU 5471  CB  GLU A 695     7196   8966   5181   -823    940    277       C  
ATOM   5472  CG  GLU A 695       8.259 105.646 229.434  1.00 59.99           C  
ANISOU 5472  CG  GLU A 695     7559   9495   5740   -787   1042    265       C  
ATOM   5473  CD  GLU A 695       8.677 106.931 228.727  1.00 63.15           C  
ANISOU 5473  CD  GLU A 695     7874   9901   6219   -682   1011    260       C  
ATOM   5474  OE1 GLU A 695       9.108 106.854 227.541  1.00 63.11           O  
ANISOU 5474  OE1 GLU A 695     7837   9901   6240   -657    917    282       O  
ATOM   5475  OE2 GLU A 695       8.570 108.013 229.366  1.00 65.46           O  
ANISOU 5475  OE2 GLU A 695     8140  10189   6544   -627   1086    234       O  
ATOM   5476  N   ASN A 696      10.458 102.164 227.535  1.00 51.55           N  
ANISOU 5476  N   ASN A 696     6775   8307   4503   -879    740    306       N  
ATOM   5477  CA  ASN A 696      11.618 101.738 226.786  1.00 49.60           C  
ANISOU 5477  CA  ASN A 696     6597   8016   4231   -837    643    304       C  
ATOM   5478  C   ASN A 696      11.227 100.888 225.609  1.00 48.43           C  
ANISOU 5478  C   ASN A 696     6430   7881   4091   -892    588    324       C  
ATOM   5479  O   ASN A 696      11.948 100.792 224.637  1.00 47.61           O  
ANISOU 5479  O   ASN A 696     6335   7763   3993   -851    518    323       O  
ATOM   5480  CB  ASN A 696      12.534 100.957 227.712  1.00 49.93           C  
ANISOU 5480  CB  ASN A 696     6805   7983   4185   -838    624    294       C  
ATOM   5481  CG  ASN A 696      13.747 100.435 227.009  1.00 51.03           C  
ANISOU 5481  CG  ASN A 696     7013   8073   4303   -789    532    291       C  
ATOM   5482  OD1 ASN A 696      13.835  99.249 226.697  1.00 54.26           O  
ANISOU 5482  OD1 ASN A 696     7504   8441   4670   -833    494    301       O  
ATOM   5483  ND2 ASN A 696      14.681 101.317 226.721  1.00 52.87           N  
ANISOU 5483  ND2 ASN A 696     7211   8307   4568   -699    500    275       N  
ATOM   5484  N   ALA A 697      10.058 100.278 225.728  1.00 48.45           N  
ANISOU 5484  N   ALA A 697     6404   7912   4092   -991    627    341       N  
ATOM   5485  CA  ALA A 697       9.552  99.299 224.788  1.00 47.85           C  
ANISOU 5485  CA  ALA A 697     6328   7844   4009  -1072    579    357       C  
ATOM   5486  C   ALA A 697       9.056  99.961 223.486  1.00 47.57           C  
ANISOU 5486  C   ALA A 697     6145   7880   4048  -1055    539    372       C  
ATOM   5487  O   ALA A 697       9.281  99.457 222.371  1.00 46.55           O  
ANISOU 5487  O   ALA A 697     6034   7744   3907  -1070    465    376       O  
ATOM   5488  CB  ALA A 697       8.454  98.502 225.448  1.00 48.14           C  
ANISOU 5488  CB  ALA A 697     6378   7890   4022  -1193    638    371       C  
ATOM   5489  N   ILE A 698       8.396 101.104 223.646  1.00 47.55           N  
ANISOU 5489  N   ILE A 698     6005   7941   4119  -1019    589    380       N  
ATOM   5490  CA  ILE A 698       7.904 101.891 222.523  1.00 47.51           C  
ANISOU 5490  CA  ILE A 698     5857   8005   4191   -989    551    402       C  
ATOM   5491  C   ILE A 698       9.070 102.409 221.671  1.00 46.43           C  
ANISOU 5491  C   ILE A 698     5748   7842   4053   -895    484    395       C  
ATOM   5492  O   ILE A 698       9.068 102.348 220.451  1.00 46.03           O  
ANISOU 5492  O   ILE A 698     5665   7815   4011   -899    415    410       O  
ATOM   5493  CB  ILE A 698       7.000 103.010 223.053  1.00 47.80           C  
ANISOU 5493  CB  ILE A 698     5751   8103   4310   -957    630    412       C  
ATOM   5494  CG1 ILE A 698       5.527 102.620 222.869  1.00 49.91           C  
ANISOU 5494  CG1 ILE A 698     5901   8442   4619  -1054    651    439       C  
ATOM   5495  CG2 ILE A 698       7.267 104.288 222.348  1.00 47.17           C  
ANISOU 5495  CG2 ILE A 698     5580   8047   4297   -853    604    422       C  
ATOM   5496  CD1 ILE A 698       4.988 101.551 223.869  1.00 52.44           C  
ANISOU 5496  CD1 ILE A 698     6291   8748   4888  -1167    716    431       C  
ATOM   5497  N   GLN A 699      10.087 102.894 222.358  1.00 46.07           N  
ANISOU 5497  N   GLN A 699     5768   7748   3990   -818    506    371       N  
ATOM   5498  CA  GLN A 699      11.327 103.265 221.743  1.00 44.81           C  
ANISOU 5498  CA  GLN A 699     5649   7554   3822   -738    452    360       C  
ATOM   5499  C   GLN A 699      11.874 102.186 220.822  1.00 43.69           C  
ANISOU 5499  C   GLN A 699     5592   7381   3626   -769    380    357       C  
ATOM   5500  O   GLN A 699      12.273 102.486 219.688  1.00 43.39           O  
ANISOU 5500  O   GLN A 699     5529   7356   3601   -734    330    364       O  
ATOM   5501  CB  GLN A 699      12.326 103.646 222.835  1.00 44.76           C  
ANISOU 5501  CB  GLN A 699     5720   7495   3792   -677    484    331       C  
ATOM   5502  CG  GLN A 699      12.499 105.165 222.899  1.00 47.74           C  
ANISOU 5502  CG  GLN A 699     6013   7892   4234   -594    512    328       C  
ATOM   5503  CD  GLN A 699      12.415 105.718 224.278  1.00 50.36           C  
ANISOU 5503  CD  GLN A 699     6361   8209   4565   -577    587    306       C  
ATOM   5504  OE1 GLN A 699      13.180 105.326 225.152  1.00 53.03           O  
ANISOU 5504  OE1 GLN A 699     6808   8497   4842   -575    589    283       O  
ATOM   5505  NE2 GLN A 699      11.486 106.647 224.493  1.00 51.47           N  
ANISOU 5505  NE2 GLN A 699     6396   8389   4769   -563    649    313       N  
ATOM   5506  N   GLN A 700      11.884 100.937 221.291  1.00 42.76           N  
ANISOU 5506  N   GLN A 700     5583   7218   3447   -835    380    347       N  
ATOM   5507  CA  GLN A 700      12.468  99.854 220.502  1.00 41.66           C  
ANISOU 5507  CA  GLN A 700     5543   7032   3253   -858    319    338       C  
ATOM   5508  C   GLN A 700      11.470  99.507 219.419  1.00 41.66           C  
ANISOU 5508  C   GLN A 700     5483   7083   3263   -938    284    357       C  
ATOM   5509  O   GLN A 700      11.828  99.228 218.273  1.00 40.97           O  
ANISOU 5509  O   GLN A 700     5420   6991   3157   -936    228    353       O  
ATOM   5510  CB  GLN A 700      12.849  98.656 221.373  1.00 41.41           C  
ANISOU 5510  CB  GLN A 700     5658   6923   3153   -895    328    324       C  
ATOM   5511  CG  GLN A 700      13.895  99.000 222.444  1.00 42.63           C  
ANISOU 5511  CG  GLN A 700     5874   7030   3291   -815    347    309       C  
ATOM   5512  CD  GLN A 700      14.550  97.784 223.099  1.00 43.88           C  
ANISOU 5512  CD  GLN A 700     6191   7101   3379   -828    331    300       C  
ATOM   5513  OE1 GLN A 700      13.993  97.164 224.001  1.00 45.74           O  
ANISOU 5513  OE1 GLN A 700     6489   7314   3577   -896    365    310       O  
ATOM   5514  NE2 GLN A 700      15.753  97.462 222.662  1.00 43.96           N  
ANISOU 5514  NE2 GLN A 700     6268   7061   3373   -760    283    285       N  
ATOM   5515  N   ALA A 701      10.200  99.593 219.789  1.00 41.99           N  
ANISOU 5515  N   ALA A 701     5439   7179   3337  -1008    319    377       N  
ATOM   5516  CA  ALA A 701       9.121  99.322 218.864  1.00 42.07           C  
ANISOU 5516  CA  ALA A 701     5371   7250   3365  -1093    282    399       C  
ATOM   5517  C   ALA A 701       9.239 100.260 217.694  1.00 41.35           C  
ANISOU 5517  C   ALA A 701     5189   7210   3314  -1032    232    416       C  
ATOM   5518  O   ALA A 701       9.237  99.811 216.559  1.00 42.15           O  
ANISOU 5518  O   ALA A 701     5312   7318   3384  -1069    166    418       O  
ATOM   5519  CB  ALA A 701       7.786  99.485 219.534  1.00 42.85           C  
ANISOU 5519  CB  ALA A 701     5362   7410   3510  -1160    337    420       C  
ATOM   5520  N   PHE A 702       9.380 101.551 217.980  1.00 40.29           N  
ANISOU 5520  N   PHE A 702     4967   7101   3239   -941    264    426       N  
ATOM   5521  CA  PHE A 702       9.433 102.592 216.955  1.00 39.17           C  
ANISOU 5521  CA  PHE A 702     4736   7005   3143   -878    223    450       C  
ATOM   5522  C   PHE A 702      10.539 102.313 215.948  1.00 38.24           C  
ANISOU 5522  C   PHE A 702     4711   6849   2970   -847    166    435       C  
ATOM   5523  O   PHE A 702      10.319 102.392 214.748  1.00 38.36           O  
ANISOU 5523  O   PHE A 702     4696   6901   2979   -864    107    455       O  
ATOM   5524  CB  PHE A 702       9.604 103.958 217.621  1.00 38.39           C  
ANISOU 5524  CB  PHE A 702     4563   6914   3111   -780    279    455       C  
ATOM   5525  CG  PHE A 702       9.860 105.097 216.662  1.00 37.97           C  
ANISOU 5525  CG  PHE A 702     4440   6888   3100   -704    244    481       C  
ATOM   5526  CD1 PHE A 702       8.849 105.603 215.857  1.00 38.62           C  
ANISOU 5526  CD1 PHE A 702     4399   7042   3234   -716    206    526       C  
ATOM   5527  CD2 PHE A 702      11.111 105.702 216.600  1.00 37.18           C  
ANISOU 5527  CD2 PHE A 702     4393   6741   2991   -620    247    464       C  
ATOM   5528  CE1 PHE A 702       9.096 106.679 214.997  1.00 38.47           C  
ANISOU 5528  CE1 PHE A 702     4326   7039   3250   -643    173    557       C  
ATOM   5529  CE2 PHE A 702      11.351 106.784 215.725  1.00 37.01           C  
ANISOU 5529  CE2 PHE A 702     4315   6740   3009   -555    220    492       C  
ATOM   5530  CZ  PHE A 702      10.346 107.256 214.936  1.00 37.65           C  
ANISOU 5530  CZ  PHE A 702     4289   6884   3133   -566    184    539       C  
ATOM   5531  N   VAL A 703      11.700 101.927 216.457  1.00 37.48           N  
ANISOU 5531  N   VAL A 703     4728   6679   2832   -806    186    400       N  
ATOM   5532  CA  VAL A 703      12.868 101.625 215.642  1.00 37.03           C  
ANISOU 5532  CA  VAL A 703     4761   6579   2729   -768    149    379       C  
ATOM   5533  C   VAL A 703      12.607 100.387 214.809  1.00 38.09           C  
ANISOU 5533  C   VAL A 703     4973   6701   2800   -853    101    370       C  
ATOM   5534  O   VAL A 703      12.558 100.465 213.586  1.00 38.57           O  
ANISOU 5534  O   VAL A 703     5023   6790   2843   -866     53    379       O  
ATOM   5535  CB  VAL A 703      14.098 101.333 216.519  1.00 36.48           C  
ANISOU 5535  CB  VAL A 703     4791   6435   2635   -710    178    345       C  
ATOM   5536  CG1 VAL A 703      15.170 100.660 215.718  1.00 36.29           C  
ANISOU 5536  CG1 VAL A 703     4867   6363   2560   -686    146    319       C  
ATOM   5537  CG2 VAL A 703      14.621 102.590 217.220  1.00 36.12           C  
ANISOU 5537  CG2 VAL A 703     4688   6393   2641   -622    217    346       C  
ATOM   5538  N   LEU A 704      12.444  99.245 215.477  1.00 39.02           N  
ANISOU 5538  N   LEU A 704     5177   6770   2878   -916    114    351       N  
ATOM   5539  CA  LEU A 704      12.166  97.980 214.817  1.00 40.23           C  
ANISOU 5539  CA  LEU A 704     5420   6896   2968  -1008     75    336       C  
ATOM   5540  C   LEU A 704      11.044  98.099 213.769  1.00 42.06           C  
ANISOU 5540  C   LEU A 704     5569   7207   3207  -1089     22    363       C  
ATOM   5541  O   LEU A 704      11.124  97.494 212.681  1.00 41.97           O  
ANISOU 5541  O   LEU A 704     5621   7185   3140  -1133    -29    350       O  
ATOM   5542  CB  LEU A 704      11.779  96.927 215.850  1.00 40.64           C  
ANISOU 5542  CB  LEU A 704     5550   6898   2994  -1081    104    327       C  
ATOM   5543  CG  LEU A 704      12.866  96.420 216.787  1.00 38.96           C  
ANISOU 5543  CG  LEU A 704     5458   6593   2751  -1022    135    302       C  
ATOM   5544  CD1 LEU A 704      12.205  95.674 217.874  1.00 39.15           C  
ANISOU 5544  CD1 LEU A 704     5528   6589   2758  -1102    169    308       C  
ATOM   5545  CD2 LEU A 704      13.823  95.534 216.049  1.00 38.60           C  
ANISOU 5545  CD2 LEU A 704     5543   6473   2650  -1001    104    269       C  
ATOM   5546  N   LYS A 705      10.007  98.869 214.102  1.00 43.23           N  
ANISOU 5546  N   LYS A 705     5574   7431   3421  -1106     34    400       N  
ATOM   5547  CA  LYS A 705       9.027  99.200 213.119  1.00 45.43           C  
ANISOU 5547  CA  LYS A 705     5750   7793   3719  -1159    -24    434       C  
ATOM   5548  C   LYS A 705       9.765  99.779 211.936  1.00 45.92           C  
ANISOU 5548  C   LYS A 705     5826   7862   3760  -1093    -69    437       C  
ATOM   5549  O   LYS A 705       9.743  99.198 210.839  1.00 47.11           O  
ANISOU 5549  O   LYS A 705     6037   8015   3849  -1150   -129    429       O  
ATOM   5550  CB  LYS A 705       7.975 100.199 213.601  1.00 46.06           C  
ANISOU 5550  CB  LYS A 705     5657   7954   3890  -1148      0    476       C  
ATOM   5551  CG  LYS A 705       6.968 100.533 212.452  1.00 48.50           C  
ANISOU 5551  CG  LYS A 705     5852   8354   4221  -1199    -80    519       C  
ATOM   5552  CD  LYS A 705       5.910 101.584 212.790  1.00 51.42           C  
ANISOU 5552  CD  LYS A 705     6035   8809   4695  -1173    -63    566       C  
ATOM   5553  CE  LYS A 705       5.244 102.118 211.504  1.00 52.79           C  
ANISOU 5553  CE  LYS A 705     6107   9065   4887  -1185   -158    616       C  
ATOM   5554  NZ  LYS A 705       4.308 103.283 211.726  1.00 53.16           N  
ANISOU 5554  NZ  LYS A 705     5964   9188   5045  -1132   -147    668       N  
ATOM   5555  N   HIS A 706      10.435 100.905 212.128  1.00 45.69           N  
ANISOU 5555  N   HIS A 706     5753   7834   3775   -981    -37    447       N  
ATOM   5556  CA  HIS A 706      11.048 101.546 210.957  1.00 46.49           C  
ANISOU 5556  CA  HIS A 706     5858   7949   3858   -927    -76    459       C  
ATOM   5557  C   HIS A 706      12.085 100.724 210.196  1.00 46.75           C  
ANISOU 5557  C   HIS A 706     6036   7922   3804   -929    -91    417       C  
ATOM   5558  O   HIS A 706      12.147 100.800 208.958  1.00 47.18           O  
ANISOU 5558  O   HIS A 706     6111   8001   3815   -944   -141    426       O  
ATOM   5559  CB  HIS A 706      11.489 102.959 211.263  1.00 45.59           C  
ANISOU 5559  CB  HIS A 706     5665   7847   3812   -817    -40    481       C  
ATOM   5560  CG  HIS A 706      10.332 103.850 211.546  1.00 46.96           C  
ANISOU 5560  CG  HIS A 706     5687   8088   4066   -814    -40    528       C  
ATOM   5561  ND1 HIS A 706       9.306 104.025 210.643  1.00 50.05           N  
ANISOU 5561  ND1 HIS A 706     5995   8552   4468   -863   -108    573       N  
ATOM   5562  CD2 HIS A 706       9.992 104.555 212.646  1.00 47.67           C  
ANISOU 5562  CD2 HIS A 706     5697   8185   4232   -770     20    537       C  
ATOM   5563  CE1 HIS A 706       8.396 104.824 211.168  1.00 51.00           C  
ANISOU 5563  CE1 HIS A 706     5978   8722   4676   -