CNRS Nantes University US2B US2B
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***  mcGAS4DNA2  ***

elNémo ID: 23042218125668734

Job options:

ID        	=	 23042218125668734
JOBID     	=	 mcGAS4DNA2
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER mcGAS4DNA2

HEADER    TRANSFERASE                             15-FEB-17   5N6I              
TITLE     CRYSTAL STRUCTURE OF MOUSE CGAS IN COMPLEX WITH 39 BP DNA             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIC GMP-AMP SYNTHASE;                                   
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 SYNONYM: M-CGAS,2'3'-CGAMP SYNTHASE,MAB-21 DOMAIN-CONTAINING PROTEIN 
COMPND   5 1;                                                                   
COMPND   6 EC: 2.7.7.86;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 OTHER_DETAILS: DNA-BINDING AND CATALYTIC DOMAIN, MAB21;              
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: DNA (37-MER);                                              
COMPND  11 CHAIN: G, I, K, M;                                                   
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 OTHER_DETAILS: NUCLEOTIDS 1 AND 39 WERE NOT VISIBLE IN THE ELECTRON  
COMPND  14 DENSITY.;                                                            
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: DNA (36-MER);                                              
COMPND  17 CHAIN: H, J, L, N;                                                   
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 OTHER_DETAILS: NUCLEOTIDS 1, 2 AND 39 WERE NOT VISIBLE IN THE        
COMPND  20 ELECTRON DENSITY.                                                    
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: MB21D1;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  11 ORGANISM_TAXID: 32630;                                               
SOURCE  12 MOL_ID: 3;                                                           
SOURCE  13 SYNTHETIC: YES;                                                      
SOURCE  14 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  15 ORGANISM_TAXID: 32630                                                
KEYWDS    NUCLEOTIDYLTRANSFERASE, CYCLIC GMP-AMP SYNTHASE, CGAS, DNA-BINDING,   
KEYWDS   2 ACTIVATOR DNA, PATTERN RECOGNITION RECEPTOR, INNATE IMMUNE RESPONSE, 
KEYWDS   3 VIRAL DNA RECOGNITION, TRANSFERASE                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.ANDREEVA,D.KOSTREWA,K.-P.HOPFNER                                    
REVDAT   5   16-OCT-19 5N6I    1       REMARK                                   
REVDAT   4   24-JAN-18 5N6I    1       SOURCE                                   
REVDAT   3   04-OCT-17 5N6I    1       JRNL                                     
REVDAT   2   27-SEP-17 5N6I    1       JRNL                                     
REVDAT   1   13-SEP-17 5N6I    0                                                
JRNL        AUTH   L.ANDREEVA,B.HILLER,D.KOSTREWA,C.LASSIG,                     
JRNL        AUTH 2 C.C.DE OLIVEIRA MANN,D.JAN DREXLER,A.MAISER,M.GAIDT,         
JRNL        AUTH 3 H.LEONHARDT,V.HORNUNG,K.P.HOPFNER                            
JRNL        TITL   CGAS SENSES LONG AND HMGB/TFAM-BOUND U-TURN DNA BY FORMING   
JRNL        TITL 2 PROTEIN-DNA LADDERS.                                         
JRNL        REF    NATURE                        V. 549   394 2017              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   28902841                                                     
JRNL        DOI    10.1038/NATURE23890                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 66.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 26998                          
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) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1402                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE SET COUNT          : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 17712                                   
REMARK   3   NUCLEIC ACID ATOMS       : 4365                                    
REMARK   3   HETEROGEN ATOMS          : 6                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 191.4                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.75000                                              
REMARK   3    B22 (A**2) : -3.02000                                             
REMARK   3    B33 (A**2) : 0.89000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.58000                                              
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): 0.971         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.787         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 141.768       
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.935                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 23255 ; 0.010 ; 0.018       
REMARK   3   BOND LENGTHS OTHERS               (A): 19761 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 31850 ; 1.443 ; 1.789       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 46164 ; 1.136 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  3260 ; 7.823 ; 5.498       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   858 ;35.261 ;24.056       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3600 ;18.642 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   120 ;15.261 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3451 ; 0.163 ; 0.218       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 22047 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  4728 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  8562 ; 4.018 ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  8561 ; 4.016 ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10692 ; 6.797 ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2): 10693 ; 6.797 ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 14692 ; 3.773 ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2): 14691 ; 3.773 ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2): 21158 ; 6.535 ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):112217 ;13.563 ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):112218 ;13.563 ;  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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 27                                
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A   149    505       B   149    505   24886  0.01  0.05     
REMARK   3    2     A   149    505       C   149    505   24906  0.01  0.05     
REMARK   3    3     A   149    505       D   149    505   24922  0.01  0.05     
REMARK   3    4     A   149    505       E   149    505   24870  0.01  0.05     
REMARK   3    5     A   149    505       F   149    505   24948  0.01  0.05     
REMARK   3    6     B   149    505       C   149    505   24884  0.01  0.05     
REMARK   3    7     B   149    505       D   149    505   24898  0.01  0.05     
REMARK   3    8     B   149    505       E   149    505   24854  0.01  0.05     
REMARK   3    9     B   149    505       F   149    505   24904  0.01  0.05     
REMARK   3   10     C   149    505       D   149    505   24896  0.01  0.05     
REMARK   3   11     C   149    505       E   149    505   24860  0.01  0.05     
REMARK   3   12     C   149    505       F   149    505   24908  0.01  0.05     
REMARK   3   13     D   149    505       E   149    505   24862  0.01  0.05     
REMARK   3   14     D   149    505       F   149    505   24922  0.01  0.05     
REMARK   3   15     E   149    505       F   149    505   24878  0.01  0.05     
REMARK   3   16     G     2     36       I     2     36    6154  0.07  0.05     
REMARK   3   17     G    20     35       K    20     35    2806  0.05  0.05     
REMARK   3   18     G    20     35       M    20     35    2794  0.05  0.05     
REMARK   3   19     H     3     38       J     3     38    6346  0.07  0.05     
REMARK   3   20     H     4     19       L     4     19    2782  0.03  0.05     
REMARK   3   21     H     4     19       N     4     19    2794  0.03  0.05     
REMARK   3   22     I    20     35       K    20     35    2814  0.04  0.05     
REMARK   3   23     I    20     35       M    20     35    2802  0.04  0.05     
REMARK   3   24     J     4     19       L     4     19    2778  0.03  0.05     
REMARK   3   25     J     4     19       N     4     19    2794  0.03  0.05     
REMARK   3   26     K    20     36       M    20     36    3038  0.01  0.05     
REMARK   3   27     L     4     20       N     4     20    2946  0.02  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   149        A   601                          
REMARK   3    RESIDUE RANGE :   B   149        B   601                          
REMARK   3    ORIGIN FOR THE GROUP (A):  50.3600  54.5290  75.1370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3995 T22:   0.3429                                     
REMARK   3      T33:   0.2392 T12:   0.0035                                     
REMARK   3      T13:   0.1979 T23:  -0.0512                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3446 L22:   4.0604                                     
REMARK   3      L33:   1.6270 L12:  -1.4749                                     
REMARK   3      L13:  -0.0364 L23:   1.1296                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3269 S12:  -0.4505 S13:   0.7326                       
REMARK   3      S21:  -0.3819 S22:   0.0001 S23:  -0.3660                       
REMARK   3      S31:  -0.6562 S32:  -0.1382 S33:  -0.3270                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   149        C   601                          
REMARK   3    RESIDUE RANGE :   D   149        D   601                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.3990  44.4110  41.5500              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2232 T22:   0.2932                                     
REMARK   3      T33:   0.0790 T12:   0.0971                                     
REMARK   3      T13:   0.0238 T23:   0.1024                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6882 L22:   3.5826                                     
REMARK   3      L33:   2.1542 L12:  -1.3209                                     
REMARK   3      L13:  -0.5591 L23:   0.9473                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0072 S12:   0.1130 S13:  -0.1657                       
REMARK   3      S21:  -0.4450 S22:  -0.1326 S23:  -0.0539                       
REMARK   3      S31:   0.3777 S32:   0.3430 S33:   0.1397                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   149        E   601                          
REMARK   3    RESIDUE RANGE :   F   149        F   601                          
REMARK   3    ORIGIN FOR THE GROUP (A): -52.9800  42.0260  15.9220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2292 T22:   0.2525                                     
REMARK   3      T33:   0.2002 T12:  -0.1801                                     
REMARK   3      T13:  -0.1516 T23:   0.0625                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8907 L22:   2.5886                                     
REMARK   3      L33:   3.6975 L12:  -0.3408                                     
REMARK   3      L13:  -0.9500 L23:   0.4117                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1537 S12:   0.1879 S13:  -0.1246                       
REMARK   3      S21:  -0.4531 S22:   0.1344 S23:   0.4757                       
REMARK   3      S31:  -0.1735 S32:  -0.2066 S33:   0.0193                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G     2        G    38                          
REMARK   3    RESIDUE RANGE :   H     3        H    38                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.6470  58.6470  45.4230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7995 T22:   0.7871                                     
REMARK   3      T33:   0.6888 T12:   0.0740                                     
REMARK   3      T13:   0.1661 T23:   0.1704                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.6713 L22:   0.3514                                     
REMARK   3      L33:   1.0061 L12:  -1.2628                                     
REMARK   3      L13:   2.5451 L23:  -0.4363                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3283 S12:   0.7348 S13:   0.9629                       
REMARK   3      S21:  -0.3017 S22:  -0.3557 S23:  -0.2167                       
REMARK   3      S31:   0.1167 S32:   0.2902 S33:   0.0274                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   I     2        I    37                          
REMARK   3    RESIDUE RANGE :   J     3        J    38                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.4040  40.3870  72.2550              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1642 T22:   1.0166                                     
REMARK   3      T33:   0.9589 T12:   0.0702                                     
REMARK   3      T13:   0.1266 T23:  -0.0472                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  13.1249 L22:   3.1123                                     
REMARK   3      L33:   7.3840 L12:   5.1838                                     
REMARK   3      L13:   8.8744 L23:   3.7359                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.9379 S12:  -0.6764 S13:   0.6588                       
REMARK   3      S21:   0.8851 S22:  -0.7416 S23:   0.6456                       
REMARK   3      S31:   1.3466 S32:  -0.0982 S33:  -0.1963                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   K    20        K    36                          
REMARK   3    RESIDUE RANGE :   L     4        L    20                          
REMARK   3    ORIGIN FOR THE GROUP (A): -56.0600  60.1380   7.5860              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1136 T22:   0.7196                                     
REMARK   3      T33:   0.6614 T12:  -0.1247                                     
REMARK   3      T13:  -0.1718 T23:   0.2105                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.4640 L22:   0.6104                                     
REMARK   3      L33:   2.3696 L12:   0.5587                                     
REMARK   3      L13:   1.2769 L23:   0.8083                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2197 S12:   0.4322 S13:   1.4004                       
REMARK   3      S21:  -0.6127 S22:  -0.1157 S23:   0.3418                       
REMARK   3      S31:  -0.7719 S32:  -0.3822 S33:  -0.1040                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   M    20        M    36                          
REMARK   3    RESIDUE RANGE :   N     4        N    20                          
REMARK   3    ORIGIN FOR THE GROUP (A): -60.3730  23.0340  18.6740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1861 T22:   0.8123                                     
REMARK   3      T33:   0.8708 T12:   0.0269                                     
REMARK   3      T13:  -0.3381 T23:   0.0691                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9202 L22:   0.8670                                     
REMARK   3      L33:  10.7326 L12:   0.7786                                     
REMARK   3      L13:   2.2183 L23:   1.7926                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4848 S12:   0.1427 S13:  -0.2870                       
REMARK   3      S21:  -0.1939 S22:  -0.3846 S23:   0.3352                       
REMARK   3      S31:   1.8112 S32:  -0.5059 S33:  -0.1002                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5N6I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200003547.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-MAY-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99988                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE, STARANISO                  
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41980                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 5.070                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 9.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
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: 4LEY                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.68                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS PH 8, 0.2M AMMONIUM CITRATE    
REMARK 280  PH 7, 27,5% W/V PEG3350, VAPOR DIFFUSION, HANGING DROP,             
REMARK 280  TEMPERATURE 293.15K                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       84.26500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       61.47000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       84.26500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       61.47000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRADECAMERIC             
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 29470 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 126200 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -127.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,         
REMARK 350                    AND CHAINS: K, L, M, N                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   138                                                      
REMARK 465     ALA A   139                                                      
REMARK 465     MET A   140                                                      
REMARK 465     ARG A   141                                                      
REMARK 465     GLY A   142                                                      
REMARK 465     SER A   143                                                      
REMARK 465     ARG A   144                                                      
REMARK 465     LYS A   145                                                      
REMARK 465     GLU A   146                                                      
REMARK 465     PRO A   147                                                      
REMARK 465     ASP A   148                                                      
REMARK 465     LYS A   506                                                      
REMARK 465     LEU A   507                                                      
REMARK 465     GLY B   138                                                      
REMARK 465     ALA B   139                                                      
REMARK 465     MET B   140                                                      
REMARK 465     ARG B   141                                                      
REMARK 465     GLY B   142                                                      
REMARK 465     SER B   143                                                      
REMARK 465     ARG B   144                                                      
REMARK 465     LYS B   145                                                      
REMARK 465     GLU B   146                                                      
REMARK 465     PRO B   147                                                      
REMARK 465     ASP B   148                                                      
REMARK 465     LYS B   506                                                      
REMARK 465     LEU B   507                                                      
REMARK 465     GLY C   138                                                      
REMARK 465     ALA C   139                                                      
REMARK 465     MET C   140                                                      
REMARK 465     ARG C   141                                                      
REMARK 465     GLY C   142                                                      
REMARK 465     SER C   143                                                      
REMARK 465     ARG C   144                                                      
REMARK 465     LYS C   145                                                      
REMARK 465     GLU C   146                                                      
REMARK 465     PRO C   147                                                      
REMARK 465     ASP C   148                                                      
REMARK 465     LYS C   506                                                      
REMARK 465     LEU C   507                                                      
REMARK 465     GLY D   138                                                      
REMARK 465     ALA D   139                                                      
REMARK 465     MET D   140                                                      
REMARK 465     ARG D   141                                                      
REMARK 465     GLY D   142                                                      
REMARK 465     SER D   143                                                      
REMARK 465     ARG D   144                                                      
REMARK 465     LYS D   145                                                      
REMARK 465     GLU D   146                                                      
REMARK 465     PRO D   147                                                      
REMARK 465     ASP D   148                                                      
REMARK 465     LYS D   506                                                      
REMARK 465     LEU D   507                                                      
REMARK 465     GLY E   138                                                      
REMARK 465     ALA E   139                                                      
REMARK 465     MET E   140                                                      
REMARK 465     ARG E   141                                                      
REMARK 465     GLY E   142                                                      
REMARK 465     SER E   143                                                      
REMARK 465     ARG E   144                                                      
REMARK 465     LYS E   145                                                      
REMARK 465     GLU E   146                                                      
REMARK 465     PRO E   147                                                      
REMARK 465     ASP E   148                                                      
REMARK 465     LYS E   506                                                      
REMARK 465     LEU E   507                                                      
REMARK 465     GLY F   138                                                      
REMARK 465     ALA F   139                                                      
REMARK 465     MET F   140                                                      
REMARK 465     ARG F   141                                                      
REMARK 465     GLY F   142                                                      
REMARK 465     SER F   143                                                      
REMARK 465     ARG F   144                                                      
REMARK 465     LYS F   145                                                      
REMARK 465     GLU F   146                                                      
REMARK 465     PRO F   147                                                      
REMARK 465     ASP F   148                                                      
REMARK 465     LYS F   506                                                      
REMARK 465     LEU F   507                                                      
REMARK 465      DA G     1                                                      
REMARK 465      DT G    39                                                      
REMARK 465      DA H     1                                                      
REMARK 465      DG H     2                                                      
REMARK 465      DT H    39                                                      
REMARK 465      DA I     1                                                      
REMARK 465      DC I    38                                                      
REMARK 465      DT I    39                                                      
REMARK 465      DA J     1                                                      
REMARK 465      DG J     2                                                      
REMARK 465      DT J    39                                                      
REMARK 465      DA K     1                                                      
REMARK 465      DG K     2                                                      
REMARK 465      DA K     3                                                      
REMARK 465      DT K     4                                                      
REMARK 465      DC K     5                                                      
REMARK 465      DT K     6                                                      
REMARK 465      DA K     7                                                      
REMARK 465      DC K     8                                                      
REMARK 465      DT K     9                                                      
REMARK 465      DA K    10                                                      
REMARK 465      DG K    11                                                      
REMARK 465      DT K    12                                                      
REMARK 465      DG K    13                                                      
REMARK 465      DA K    14                                                      
REMARK 465      DT K    15                                                      
REMARK 465      DC K    16                                                      
REMARK 465      DT K    17                                                      
REMARK 465      DA K    18                                                      
REMARK 465      DT K    19                                                      
REMARK 465      DT K    37                                                      
REMARK 465      DC K    38                                                      
REMARK 465      DT K    39                                                      
REMARK 465      DA L     1                                                      
REMARK 465      DG L     2                                                      
REMARK 465      DA L     3                                                      
REMARK 465      DA L    21                                                      
REMARK 465      DT L    22                                                      
REMARK 465      DA L    23                                                      
REMARK 465      DG L    24                                                      
REMARK 465      DA L    25                                                      
REMARK 465      DT L    26                                                      
REMARK 465      DC L    27                                                      
REMARK 465      DA L    28                                                      
REMARK 465      DC L    29                                                      
REMARK 465      DT L    30                                                      
REMARK 465      DA L    31                                                      
REMARK 465      DG L    32                                                      
REMARK 465      DT L    33                                                      
REMARK 465      DA L    34                                                      
REMARK 465      DG L    35                                                      
REMARK 465      DA L    36                                                      
REMARK 465      DT L    37                                                      
REMARK 465      DC L    38                                                      
REMARK 465      DT L    39                                                      
REMARK 465      DA M     1                                                      
REMARK 465      DG M     2                                                      
REMARK 465      DA M     3                                                      
REMARK 465      DT M     4                                                      
REMARK 465      DC M     5                                                      
REMARK 465      DT M     6                                                      
REMARK 465      DA M     7                                                      
REMARK 465      DC M     8                                                      
REMARK 465      DT M     9                                                      
REMARK 465      DA M    10                                                      
REMARK 465      DG M    11                                                      
REMARK 465      DT M    12                                                      
REMARK 465      DG M    13                                                      
REMARK 465      DA M    14                                                      
REMARK 465      DT M    15                                                      
REMARK 465      DC M    16                                                      
REMARK 465      DT M    17                                                      
REMARK 465      DA M    18                                                      
REMARK 465      DT M    19                                                      
REMARK 465      DT M    37                                                      
REMARK 465      DC M    38                                                      
REMARK 465      DT M    39                                                      
REMARK 465      DA N     1                                                      
REMARK 465      DG N     2                                                      
REMARK 465      DA N     3                                                      
REMARK 465      DA N    21                                                      
REMARK 465      DT N    22                                                      
REMARK 465      DA N    23                                                      
REMARK 465      DG N    24                                                      
REMARK 465      DA N    25                                                      
REMARK 465      DT N    26                                                      
REMARK 465      DC N    27                                                      
REMARK 465      DA N    28                                                      
REMARK 465      DC N    29                                                      
REMARK 465      DT N    30                                                      
REMARK 465      DA N    31                                                      
REMARK 465      DG N    32                                                      
REMARK 465      DT N    33                                                      
REMARK 465      DA N    34                                                      
REMARK 465      DG N    35                                                      
REMARK 465      DA N    36                                                      
REMARK 465      DT N    37                                                      
REMARK 465      DC N    38                                                      
REMARK 465      DT N    39                                                      
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   NZ   LYS B   372     OP1   DG I    11              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE1  GLN A   413     O    GLU D   287     3545     1.27            
REMARK 500   O    GLU A   287     OE1  GLN D   413     3545     1.79            
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    PRO A 301   C   -  N   -  CD  ANGL. DEV. = -17.9 DEGREES          
REMARK 500    PRO B 301   C   -  N   -  CD  ANGL. DEV. = -17.2 DEGREES          
REMARK 500    PRO C 301   C   -  N   -  CD  ANGL. DEV. = -18.0 DEGREES          
REMARK 500    PRO D 301   C   -  N   -  CD  ANGL. DEV. = -17.9 DEGREES          
REMARK 500    PRO E 301   C   -  N   -  CD  ANGL. DEV. = -17.9 DEGREES          
REMARK 500    PRO F 301   C   -  N   -  CD  ANGL. DEV. = -17.4 DEGREES          
REMARK 500     DG G  13   O5' -  C5' -  C4' ANGL. DEV. =  -4.9 DEGREES          
REMARK 500     DT G  37   O4' -  C1' -  N1  ANGL. DEV. =   2.3 DEGREES          
REMARK 500     DG I   2   O4' -  C1' -  N9  ANGL. DEV. =   1.8 DEGREES          
REMARK 500     DG I  13   O5' -  C5' -  C4' ANGL. DEV. =  -5.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A 184     -102.25    -57.45                                   
REMARK 500    GLU A 186       80.80    -54.41                                   
REMARK 500    SER A 207      -66.40     59.94                                   
REMARK 500    TYR A 228       97.03    -68.76                                   
REMARK 500    TYR A 229     -123.48     65.05                                   
REMARK 500    ILE A 242       94.11    -64.80                                   
REMARK 500    ARG A 244     -108.47   -154.49                                   
REMARK 500    ASN A 246      124.59     65.45                                   
REMARK 500    GLU A 253       52.49   -117.32                                   
REMARK 500    PRO A 301      -72.36     35.09                                   
REMARK 500    PHE A 504        3.14    -68.57                                   
REMARK 500    LYS B 184     -101.21    -57.83                                   
REMARK 500    GLU B 186       80.97    -54.63                                   
REMARK 500    SER B 207      -66.38     59.72                                   
REMARK 500    TYR B 228       96.59    -68.23                                   
REMARK 500    TYR B 229     -123.30     64.76                                   
REMARK 500    ILE B 242       94.08    -64.06                                   
REMARK 500    ARG B 244     -109.13   -154.41                                   
REMARK 500    ASN B 246      124.46     66.80                                   
REMARK 500    GLU B 253       52.84   -117.19                                   
REMARK 500    PRO B 301      -72.80     35.61                                   
REMARK 500    PHE B 504        4.56    -68.97                                   
REMARK 500    LYS C 184     -100.81    -57.35                                   
REMARK 500    GLU C 186       81.10    -54.51                                   
REMARK 500    SER C 207      -65.78     59.59                                   
REMARK 500    TYR C 228       96.50    -68.63                                   
REMARK 500    TYR C 229     -123.42     65.08                                   
REMARK 500    ILE C 242       94.57    -63.61                                   
REMARK 500    ARG C 244     -108.41   -154.12                                   
REMARK 500    ASN C 246      124.48     65.28                                   
REMARK 500    GLU C 253       52.54   -117.69                                   
REMARK 500    PRO C 301      -72.41     35.16                                   
REMARK 500    PHE C 504        3.48    -68.65                                   
REMARK 500    LYS D 184     -102.99    -57.37                                   
REMARK 500    GLU D 186       80.79    -54.66                                   
REMARK 500    SER D 207      -65.66     59.34                                   
REMARK 500    TYR D 228       95.96    -68.39                                   
REMARK 500    TYR D 229     -122.91     64.50                                   
REMARK 500    ILE D 242       93.97    -64.75                                   
REMARK 500    ARG D 244     -109.06   -154.27                                   
REMARK 500    ASN D 246      124.41     65.50                                   
REMARK 500    GLU D 253       52.41   -117.66                                   
REMARK 500    PRO D 301      -72.45     35.03                                   
REMARK 500    PHE D 504        4.04    -68.76                                   
REMARK 500    LYS E 184     -101.79    -57.24                                   
REMARK 500    GLU E 186       80.94    -54.36                                   
REMARK 500    SER E 207      -66.41     60.35                                   
REMARK 500    TYR E 228       96.55    -68.25                                   
REMARK 500    TYR E 229     -123.13     64.76                                   
REMARK 500    ILE E 242       94.05    -65.28                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      66 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 ASN A  300     PRO A  301                 -138.59                    
REMARK 500 ASN B  300     PRO B  301                 -138.95                    
REMARK 500 ASN C  300     PRO C  301                 -138.44                    
REMARK 500 ASN D  300     PRO D  301                 -138.63                    
REMARK 500 ASN E  300     PRO E  301                 -138.64                    
REMARK 500 ASN F  300     PRO F  301                 -138.50                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 601  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 378   NE2                                                    
REMARK 620 2 CYS A 384   SG  118.4                                              
REMARK 620 3 CYS A 385   SG   90.2 139.6                                        
REMARK 620 4 CYS A 392   SG   89.8 110.9  95.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 601  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 378   NE2                                                    
REMARK 620 2 CYS B 384   SG  121.2                                              
REMARK 620 3 CYS B 385   SG   90.3 139.7                                        
REMARK 620 4 CYS B 392   SG   89.0 109.8  93.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 601  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 378   NE2                                                    
REMARK 620 2 CYS C 384   SG  118.7                                              
REMARK 620 3 CYS C 385   SG   87.9 142.7                                        
REMARK 620 4 CYS C 392   SG   86.9 111.9  94.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 601  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 378   NE2                                                    
REMARK 620 2 CYS D 384   SG  115.6                                              
REMARK 620 3 CYS D 385   SG   86.8 144.3                                        
REMARK 620 4 CYS D 392   SG   86.1 113.1  94.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E 601  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E 378   NE2                                                    
REMARK 620 2 CYS E 384   SG  118.8                                              
REMARK 620 3 CYS E 385   SG   87.9 139.2                                        
REMARK 620 4 CYS E 392   SG   89.1 113.0  96.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F 601  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F 378   NE2                                                    
REMARK 620 2 CYS F 384   SG  115.3                                              
REMARK 620 3 CYS F 385   SG   87.6 142.2                                        
REMARK 620 4 CYS F 392   SG   86.4 112.8  97.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN E 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN F 601                  
DBREF  5N6I A  139   507  UNP    Q8C6L5   CGAS_MOUSE     139    507             
DBREF  5N6I B  139   507  UNP    Q8C6L5   CGAS_MOUSE     139    507             
DBREF  5N6I C  139   507  UNP    Q8C6L5   CGAS_MOUSE     139    507             
DBREF  5N6I D  139   507  UNP    Q8C6L5   CGAS_MOUSE     139    507             
DBREF  5N6I E  139   507  UNP    Q8C6L5   CGAS_MOUSE     139    507             
DBREF  5N6I F  139   507  UNP    Q8C6L5   CGAS_MOUSE     139    507             
DBREF  5N6I G    1    39  PDB    5N6I     5N6I             1     39             
DBREF  5N6I H    1    39  PDB    5N6I     5N6I             1     39             
DBREF  5N6I I    1    39  PDB    5N6I     5N6I             1     39             
DBREF  5N6I J    1    39  PDB    5N6I     5N6I             1     39             
DBREF  5N6I K    1    39  PDB    5N6I     5N6I             1     39             
DBREF  5N6I L    1    39  PDB    5N6I     5N6I             1     39             
DBREF  5N6I M    1    39  PDB    5N6I     5N6I             1     39             
DBREF  5N6I N    1    39  PDB    5N6I     5N6I             1     39             
SEQADV 5N6I GLY A  138  UNP  Q8C6L5              EXPRESSION TAG                 
SEQADV 5N6I MET A  140  UNP  Q8C6L5    PRO   140 CONFLICT                       
SEQADV 5N6I GLY B  138  UNP  Q8C6L5              EXPRESSION TAG                 
SEQADV 5N6I MET B  140  UNP  Q8C6L5    PRO   140 CONFLICT                       
SEQADV 5N6I GLY C  138  UNP  Q8C6L5              EXPRESSION TAG                 
SEQADV 5N6I MET C  140  UNP  Q8C6L5    PRO   140 CONFLICT                       
SEQADV 5N6I GLY D  138  UNP  Q8C6L5              EXPRESSION TAG                 
SEQADV 5N6I MET D  140  UNP  Q8C6L5    PRO   140 CONFLICT                       
SEQADV 5N6I GLY E  138  UNP  Q8C6L5              EXPRESSION TAG                 
SEQADV 5N6I MET E  140  UNP  Q8C6L5    PRO   140 CONFLICT                       
SEQADV 5N6I GLY F  138  UNP  Q8C6L5              EXPRESSION TAG                 
SEQADV 5N6I MET F  140  UNP  Q8C6L5    PRO   140 CONFLICT                       
SEQRES   1 A  370  GLY ALA MET ARG GLY SER ARG LYS GLU PRO ASP LYS LEU          
SEQRES   2 A  370  LYS LYS VAL LEU ASP LYS LEU ARG LEU LYS ARG LYS ASP          
SEQRES   3 A  370  ILE SER GLU ALA ALA GLU THR VAL ASN LYS VAL VAL GLU          
SEQRES   4 A  370  ARG LEU LEU ARG ARG MET GLN LYS ARG GLU SER GLU PHE          
SEQRES   5 A  370  LYS GLY VAL GLU GLN LEU ASN THR GLY SER TYR TYR GLU          
SEQRES   6 A  370  HIS VAL LYS ILE SER ALA PRO ASN GLU PHE ASP VAL MET          
SEQRES   7 A  370  PHE LYS LEU GLU VAL PRO ARG ILE GLU LEU GLN GLU TYR          
SEQRES   8 A  370  TYR GLU THR GLY ALA PHE TYR LEU VAL LYS PHE LYS ARG          
SEQRES   9 A  370  ILE PRO ARG GLY ASN PRO LEU SER HIS PHE LEU GLU GLY          
SEQRES  10 A  370  GLU VAL LEU SER ALA THR LYS MET LEU SER LYS PHE ARG          
SEQRES  11 A  370  LYS ILE ILE LYS GLU GLU VAL LYS GLU ILE LYS ASP ILE          
SEQRES  12 A  370  ASP VAL SER VAL GLU LYS GLU LYS PRO GLY SER PRO ALA          
SEQRES  13 A  370  VAL THR LEU LEU ILE ARG ASN PRO GLU GLU ILE SER VAL          
SEQRES  14 A  370  ASP ILE ILE LEU ALA LEU GLU SER LYS GLY SER TRP PRO          
SEQRES  15 A  370  ILE SER THR LYS GLU GLY LEU PRO ILE GLN GLY TRP LEU          
SEQRES  16 A  370  GLY THR LYS VAL ARG THR ASN LEU ARG ARG GLU PRO PHE          
SEQRES  17 A  370  TYR LEU VAL PRO LYS ASN ALA LYS ASP GLY ASN SER PHE          
SEQRES  18 A  370  GLN GLY GLU THR TRP ARG LEU SER PHE SER HIS THR GLU          
SEQRES  19 A  370  LYS TYR ILE LEU ASN ASN HIS GLY ILE GLU LYS THR CYS          
SEQRES  20 A  370  CYS GLU SER SER GLY ALA LYS CYS CYS ARG LYS GLU CYS          
SEQRES  21 A  370  LEU LYS LEU MET LYS TYR LEU LEU GLU GLN LEU LYS LYS          
SEQRES  22 A  370  GLU PHE GLN GLU LEU ASP ALA PHE CYS SER TYR HIS VAL          
SEQRES  23 A  370  LYS THR ALA ILE PHE HIS MET TRP THR GLN ASP PRO GLN          
SEQRES  24 A  370  ASP SER GLN TRP ASP PRO ARG ASN LEU SER SER CYS PHE          
SEQRES  25 A  370  ASP LYS LEU LEU ALA PHE PHE LEU GLU CYS LEU ARG THR          
SEQRES  26 A  370  GLU LYS LEU ASP HIS TYR PHE ILE PRO LYS PHE ASN LEU          
SEQRES  27 A  370  PHE SER GLN GLU LEU ILE ASP ARG LYS SER LYS GLU PHE          
SEQRES  28 A  370  LEU SER LYS LYS ILE GLU TYR GLU ARG ASN ASN GLY PHE          
SEQRES  29 A  370  PRO ILE PHE ASP LYS LEU                                      
SEQRES   1 B  370  GLY ALA MET ARG GLY SER ARG LYS GLU PRO ASP LYS LEU          
SEQRES   2 B  370  LYS LYS VAL LEU ASP LYS LEU ARG LEU LYS ARG LYS ASP          
SEQRES   3 B  370  ILE SER GLU ALA ALA GLU THR VAL ASN LYS VAL VAL GLU          
SEQRES   4 B  370  ARG LEU LEU ARG ARG MET GLN LYS ARG GLU SER GLU PHE          
SEQRES   5 B  370  LYS GLY VAL GLU GLN LEU ASN THR GLY SER TYR TYR GLU          
SEQRES   6 B  370  HIS VAL LYS ILE SER ALA PRO ASN GLU PHE ASP VAL MET          
SEQRES   7 B  370  PHE LYS LEU GLU VAL PRO ARG ILE GLU LEU GLN GLU TYR          
SEQRES   8 B  370  TYR GLU THR GLY ALA PHE TYR LEU VAL LYS PHE LYS ARG          
SEQRES   9 B  370  ILE PRO ARG GLY ASN PRO LEU SER HIS PHE LEU GLU GLY          
SEQRES  10 B  370  GLU VAL LEU SER ALA THR LYS MET LEU SER LYS PHE ARG          
SEQRES  11 B  370  LYS ILE ILE LYS GLU GLU VAL LYS GLU ILE LYS ASP ILE          
SEQRES  12 B  370  ASP VAL SER VAL GLU LYS GLU LYS PRO GLY SER PRO ALA          
SEQRES  13 B  370  VAL THR LEU LEU ILE ARG ASN PRO GLU GLU ILE SER VAL          
SEQRES  14 B  370  ASP ILE ILE LEU ALA LEU GLU SER LYS GLY SER TRP PRO          
SEQRES  15 B  370  ILE SER THR LYS GLU GLY LEU PRO ILE GLN GLY TRP LEU          
SEQRES  16 B  370  GLY THR LYS VAL ARG THR ASN LEU ARG ARG GLU PRO PHE          
SEQRES  17 B  370  TYR LEU VAL PRO LYS ASN ALA LYS ASP GLY ASN SER PHE          
SEQRES  18 B  370  GLN GLY GLU THR TRP ARG LEU SER PHE SER HIS THR GLU          
SEQRES  19 B  370  LYS TYR ILE LEU ASN ASN HIS GLY ILE GLU LYS THR CYS          
SEQRES  20 B  370  CYS GLU SER SER GLY ALA LYS CYS CYS ARG LYS GLU CYS          
SEQRES  21 B  370  LEU LYS LEU MET LYS TYR LEU LEU GLU GLN LEU LYS LYS          
SEQRES  22 B  370  GLU PHE GLN GLU LEU ASP ALA PHE CYS SER TYR HIS VAL          
SEQRES  23 B  370  LYS THR ALA ILE PHE HIS MET TRP THR GLN ASP PRO GLN          
SEQRES  24 B  370  ASP SER GLN TRP ASP PRO ARG ASN LEU SER SER CYS PHE          
SEQRES  25 B  370  ASP LYS LEU LEU ALA PHE PHE LEU GLU CYS LEU ARG THR          
SEQRES  26 B  370  GLU LYS LEU ASP HIS TYR PHE ILE PRO LYS PHE ASN LEU          
SEQRES  27 B  370  PHE SER GLN GLU LEU ILE ASP ARG LYS SER LYS GLU PHE          
SEQRES  28 B  370  LEU SER LYS LYS ILE GLU TYR GLU ARG ASN ASN GLY PHE          
SEQRES  29 B  370  PRO ILE PHE ASP LYS LEU                                      
SEQRES   1 C  370  GLY ALA MET ARG GLY SER ARG LYS GLU PRO ASP LYS LEU          
SEQRES   2 C  370  LYS LYS VAL LEU ASP LYS LEU ARG LEU LYS ARG LYS ASP          
SEQRES   3 C  370  ILE SER GLU ALA ALA GLU THR VAL ASN LYS VAL VAL GLU          
SEQRES   4 C  370  ARG LEU LEU ARG ARG MET GLN LYS ARG GLU SER GLU PHE          
SEQRES   5 C  370  LYS GLY VAL GLU GLN LEU ASN THR GLY SER TYR TYR GLU          
SEQRES   6 C  370  HIS VAL LYS ILE SER ALA PRO ASN GLU PHE ASP VAL MET          
SEQRES   7 C  370  PHE LYS LEU GLU VAL PRO ARG ILE GLU LEU GLN GLU TYR          
SEQRES   8 C  370  TYR GLU THR GLY ALA PHE TYR LEU VAL LYS PHE LYS ARG          
SEQRES   9 C  370  ILE PRO ARG GLY ASN PRO LEU SER HIS PHE LEU GLU GLY          
SEQRES  10 C  370  GLU VAL LEU SER ALA THR LYS MET LEU SER LYS PHE ARG          
SEQRES  11 C  370  LYS ILE ILE LYS GLU GLU VAL LYS GLU ILE LYS ASP ILE          
SEQRES  12 C  370  ASP VAL SER VAL GLU LYS GLU LYS PRO GLY SER PRO ALA          
SEQRES  13 C  370  VAL THR LEU LEU ILE ARG ASN PRO GLU GLU ILE SER VAL          
SEQRES  14 C  370  ASP ILE ILE LEU ALA LEU GLU SER LYS GLY SER TRP PRO          
SEQRES  15 C  370  ILE SER THR LYS GLU GLY LEU PRO ILE GLN GLY TRP LEU          
SEQRES  16 C  370  GLY THR LYS VAL ARG THR ASN LEU ARG ARG GLU PRO PHE          
SEQRES  17 C  370  TYR LEU VAL PRO LYS ASN ALA LYS ASP GLY ASN SER PHE          
SEQRES  18 C  370  GLN GLY GLU THR TRP ARG LEU SER PHE SER HIS THR GLU          
SEQRES  19 C  370  LYS TYR ILE LEU ASN ASN HIS GLY ILE GLU LYS THR CYS          
SEQRES  20 C  370  CYS GLU SER SER GLY ALA LYS CYS CYS ARG LYS GLU CYS          
SEQRES  21 C  370  LEU LYS LEU MET LYS TYR LEU LEU GLU GLN LEU LYS LYS          
SEQRES  22 C  370  GLU PHE GLN GLU LEU ASP ALA PHE CYS SER TYR HIS VAL          
SEQRES  23 C  370  LYS THR ALA ILE PHE HIS MET TRP THR GLN ASP PRO GLN          
SEQRES  24 C  370  ASP SER GLN TRP ASP PRO ARG ASN LEU SER SER CYS PHE          
SEQRES  25 C  370  ASP LYS LEU LEU ALA PHE PHE LEU GLU CYS LEU ARG THR          
SEQRES  26 C  370  GLU LYS LEU ASP HIS TYR PHE ILE PRO LYS PHE ASN LEU          
SEQRES  27 C  370  PHE SER GLN GLU LEU ILE ASP ARG LYS SER LYS GLU PHE          
SEQRES  28 C  370  LEU SER LYS LYS ILE GLU TYR GLU ARG ASN ASN GLY PHE          
SEQRES  29 C  370  PRO ILE PHE ASP LYS LEU                                      
SEQRES   1 D  370  GLY ALA MET ARG GLY SER ARG LYS GLU PRO ASP LYS LEU          
SEQRES   2 D  370  LYS LYS VAL LEU ASP LYS LEU ARG LEU LYS ARG LYS ASP          
SEQRES   3 D  370  ILE SER GLU ALA ALA GLU THR VAL ASN LYS VAL VAL GLU          
SEQRES   4 D  370  ARG LEU LEU ARG ARG MET GLN LYS ARG GLU SER GLU PHE          
SEQRES   5 D  370  LYS GLY VAL GLU GLN LEU ASN THR GLY SER TYR TYR GLU          
SEQRES   6 D  370  HIS VAL LYS ILE SER ALA PRO ASN GLU PHE ASP VAL MET          
SEQRES   7 D  370  PHE LYS LEU GLU VAL PRO ARG ILE GLU LEU GLN GLU TYR          
SEQRES   8 D  370  TYR GLU THR GLY ALA PHE TYR LEU VAL LYS PHE LYS ARG          
SEQRES   9 D  370  ILE PRO ARG GLY ASN PRO LEU SER HIS PHE LEU GLU GLY          
SEQRES  10 D  370  GLU VAL LEU SER ALA THR LYS MET LEU SER LYS PHE ARG          
SEQRES  11 D  370  LYS ILE ILE LYS GLU GLU VAL LYS GLU ILE LYS ASP ILE          
SEQRES  12 D  370  ASP VAL SER VAL GLU LYS GLU LYS PRO GLY SER PRO ALA          
SEQRES  13 D  370  VAL THR LEU LEU ILE ARG ASN PRO GLU GLU ILE SER VAL          
SEQRES  14 D  370  ASP ILE ILE LEU ALA LEU GLU SER LYS GLY SER TRP PRO          
SEQRES  15 D  370  ILE SER THR LYS GLU GLY LEU PRO ILE GLN GLY TRP LEU          
SEQRES  16 D  370  GLY THR LYS VAL ARG THR ASN LEU ARG ARG GLU PRO PHE          
SEQRES  17 D  370  TYR LEU VAL PRO LYS ASN ALA LYS ASP GLY ASN SER PHE          
SEQRES  18 D  370  GLN GLY GLU THR TRP ARG LEU SER PHE SER HIS THR GLU          
SEQRES  19 D  370  LYS TYR ILE LEU ASN ASN HIS GLY ILE GLU LYS THR CYS          
SEQRES  20 D  370  CYS GLU SER SER GLY ALA LYS CYS CYS ARG LYS GLU CYS          
SEQRES  21 D  370  LEU LYS LEU MET LYS TYR LEU LEU GLU GLN LEU LYS LYS          
SEQRES  22 D  370  GLU PHE GLN GLU LEU ASP ALA PHE CYS SER TYR HIS VAL          
SEQRES  23 D  370  LYS THR ALA ILE PHE HIS MET TRP THR GLN ASP PRO GLN          
SEQRES  24 D  370  ASP SER GLN TRP ASP PRO ARG ASN LEU SER SER CYS PHE          
SEQRES  25 D  370  ASP LYS LEU LEU ALA PHE PHE LEU GLU CYS LEU ARG THR          
SEQRES  26 D  370  GLU LYS LEU ASP HIS TYR PHE ILE PRO LYS PHE ASN LEU          
SEQRES  27 D  370  PHE SER GLN GLU LEU ILE ASP ARG LYS SER LYS GLU PHE          
SEQRES  28 D  370  LEU SER LYS LYS ILE GLU TYR GLU ARG ASN ASN GLY PHE          
SEQRES  29 D  370  PRO ILE PHE ASP LYS LEU                                      
SEQRES   1 E  370  GLY ALA MET ARG GLY SER ARG LYS GLU PRO ASP LYS LEU          
SEQRES   2 E  370  LYS LYS VAL LEU ASP LYS LEU ARG LEU LYS ARG LYS ASP          
SEQRES   3 E  370  ILE SER GLU ALA ALA GLU THR VAL ASN LYS VAL VAL GLU          
SEQRES   4 E  370  ARG LEU LEU ARG ARG MET GLN LYS ARG GLU SER GLU PHE          
SEQRES   5 E  370  LYS GLY VAL GLU GLN LEU ASN THR GLY SER TYR TYR GLU          
SEQRES   6 E  370  HIS VAL LYS ILE SER ALA PRO ASN GLU PHE ASP VAL MET          
SEQRES   7 E  370  PHE LYS LEU GLU VAL PRO ARG ILE GLU LEU GLN GLU TYR          
SEQRES   8 E  370  TYR GLU THR GLY ALA PHE TYR LEU VAL LYS PHE LYS ARG          
SEQRES   9 E  370  ILE PRO ARG GLY ASN PRO LEU SER HIS PHE LEU GLU GLY          
SEQRES  10 E  370  GLU VAL LEU SER ALA THR LYS MET LEU SER LYS PHE ARG          
SEQRES  11 E  370  LYS ILE ILE LYS GLU GLU VAL LYS GLU ILE LYS ASP ILE          
SEQRES  12 E  370  ASP VAL SER VAL GLU LYS GLU LYS PRO GLY SER PRO ALA          
SEQRES  13 E  370  VAL THR LEU LEU ILE ARG ASN PRO GLU GLU ILE SER VAL          
SEQRES  14 E  370  ASP ILE ILE LEU ALA LEU GLU SER LYS GLY SER TRP PRO          
SEQRES  15 E  370  ILE SER THR LYS GLU GLY LEU PRO ILE GLN GLY TRP LEU          
SEQRES  16 E  370  GLY THR LYS VAL ARG THR ASN LEU ARG ARG GLU PRO PHE          
SEQRES  17 E  370  TYR LEU VAL PRO LYS ASN ALA LYS ASP GLY ASN SER PHE          
SEQRES  18 E  370  GLN GLY GLU THR TRP ARG LEU SER PHE SER HIS THR GLU          
SEQRES  19 E  370  LYS TYR ILE LEU ASN ASN HIS GLY ILE GLU LYS THR CYS          
SEQRES  20 E  370  CYS GLU SER SER GLY ALA LYS CYS CYS ARG LYS GLU CYS          
SEQRES  21 E  370  LEU LYS LEU MET LYS TYR LEU LEU GLU GLN LEU LYS LYS          
SEQRES  22 E  370  GLU PHE GLN GLU LEU ASP ALA PHE CYS SER TYR HIS VAL          
SEQRES  23 E  370  LYS THR ALA ILE PHE HIS MET TRP THR GLN ASP PRO GLN          
SEQRES  24 E  370  ASP SER GLN TRP ASP PRO ARG ASN LEU SER SER CYS PHE          
SEQRES  25 E  370  ASP LYS LEU LEU ALA PHE PHE LEU GLU CYS LEU ARG THR          
SEQRES  26 E  370  GLU LYS LEU ASP HIS TYR PHE ILE PRO LYS PHE ASN LEU          
SEQRES  27 E  370  PHE SER GLN GLU LEU ILE ASP ARG LYS SER LYS GLU PHE          
SEQRES  28 E  370  LEU SER LYS LYS ILE GLU TYR GLU ARG ASN ASN GLY PHE          
SEQRES  29 E  370  PRO ILE PHE ASP LYS LEU                                      
SEQRES   1 F  370  GLY ALA MET ARG GLY SER ARG LYS GLU PRO ASP LYS LEU          
SEQRES   2 F  370  LYS LYS VAL LEU ASP LYS LEU ARG LEU LYS ARG LYS ASP          
SEQRES   3 F  370  ILE SER GLU ALA ALA GLU THR VAL ASN LYS VAL VAL GLU          
SEQRES   4 F  370  ARG LEU LEU ARG ARG MET GLN LYS ARG GLU SER GLU PHE          
SEQRES   5 F  370  LYS GLY VAL GLU GLN LEU ASN THR GLY SER TYR TYR GLU          
SEQRES   6 F  370  HIS VAL LYS ILE SER ALA PRO ASN GLU PHE ASP VAL MET          
SEQRES   7 F  370  PHE LYS LEU GLU VAL PRO ARG ILE GLU LEU GLN GLU TYR          
SEQRES   8 F  370  TYR GLU THR GLY ALA PHE TYR LEU VAL LYS PHE LYS ARG          
SEQRES   9 F  370  ILE PRO ARG GLY ASN PRO LEU SER HIS PHE LEU GLU GLY          
SEQRES  10 F  370  GLU VAL LEU SER ALA THR LYS MET LEU SER LYS PHE ARG          
SEQRES  11 F  370  LYS ILE ILE LYS GLU GLU VAL LYS GLU ILE LYS ASP ILE          
SEQRES  12 F  370  ASP VAL SER VAL GLU LYS GLU LYS PRO GLY SER PRO ALA          
SEQRES  13 F  370  VAL THR LEU LEU ILE ARG ASN PRO GLU GLU ILE SER VAL          
SEQRES  14 F  370  ASP ILE ILE LEU ALA LEU GLU SER LYS GLY SER TRP PRO          
SEQRES  15 F  370  ILE SER THR LYS GLU GLY LEU PRO ILE GLN GLY TRP LEU          
SEQRES  16 F  370  GLY THR LYS VAL ARG THR ASN LEU ARG ARG GLU PRO PHE          
SEQRES  17 F  370  TYR LEU VAL PRO LYS ASN ALA LYS ASP GLY ASN SER PHE          
SEQRES  18 F  370  GLN GLY GLU THR TRP ARG LEU SER PHE SER HIS THR GLU          
SEQRES  19 F  370  LYS TYR ILE LEU ASN ASN HIS GLY ILE GLU LYS THR CYS          
SEQRES  20 F  370  CYS GLU SER SER GLY ALA LYS CYS CYS ARG LYS GLU CYS          
SEQRES  21 F  370  LEU LYS LEU MET LYS TYR LEU LEU GLU GLN LEU LYS LYS          
SEQRES  22 F  370  GLU PHE GLN GLU LEU ASP ALA PHE CYS SER TYR HIS VAL          
SEQRES  23 F  370  LYS THR ALA ILE PHE HIS MET TRP THR GLN ASP PRO GLN          
SEQRES  24 F  370  ASP SER GLN TRP ASP PRO ARG ASN LEU SER SER CYS PHE          
SEQRES  25 F  370  ASP LYS LEU LEU ALA PHE PHE LEU GLU CYS LEU ARG THR          
SEQRES  26 F  370  GLU LYS LEU ASP HIS TYR PHE ILE PRO LYS PHE ASN LEU          
SEQRES  27 F  370  PHE SER GLN GLU LEU ILE ASP ARG LYS SER LYS GLU PHE          
SEQRES  28 F  370  LEU SER LYS LYS ILE GLU TYR GLU ARG ASN ASN GLY PHE          
SEQRES  29 F  370  PRO ILE PHE ASP LYS LEU                                      
SEQRES   1 G   39   DA  DG  DA  DT  DC  DT  DA  DC  DT  DA  DG  DT  DG          
SEQRES   2 G   39   DA  DT  DC  DT  DA  DT  DG  DA  DC  DT  DG  DA  DT          
SEQRES   3 G   39   DC  DT  DG  DT  DA  DC  DA  DT  DG  DA  DT  DC  DT          
SEQRES   1 H   39   DA  DG  DA  DT  DC  DA  DT  DG  DT  DA  DC  DA  DG          
SEQRES   2 H   39   DA  DT  DC  DA  DG  DT  DC  DA  DT  DA  DG  DA  DT          
SEQRES   3 H   39   DC  DA  DC  DT  DA  DG  DT  DA  DG  DA  DT  DC  DT          
SEQRES   1 I   39   DA  DG  DA  DT  DC  DT  DA  DC  DT  DA  DG  DT  DG          
SEQRES   2 I   39   DA  DT  DC  DT  DA  DT  DG  DA  DC  DT  DG  DA  DT          
SEQRES   3 I   39   DC  DT  DG  DT  DA  DC  DA  DT  DG  DA  DT  DC  DT          
SEQRES   1 J   39   DA  DG  DA  DT  DC  DA  DT  DG  DT  DA  DC  DA  DG          
SEQRES   2 J   39   DA  DT  DC  DA  DG  DT  DC  DA  DT  DA  DG  DA  DT          
SEQRES   3 J   39   DC  DA  DC  DT  DA  DG  DT  DA  DG  DA  DT  DC  DT          
SEQRES   1 K   39   DA  DG  DA  DT  DC  DT  DA  DC  DT  DA  DG  DT  DG          
SEQRES   2 K   39   DA  DT  DC  DT  DA  DT  DG  DA  DC  DT  DG  DA  DT          
SEQRES   3 K   39   DC  DT  DG  DT  DA  DC  DA  DT  DG  DA  DT  DC  DT          
SEQRES   1 L   39   DA  DG  DA  DT  DC  DA  DT  DG  DT  DA  DC  DA  DG          
SEQRES   2 L   39   DA  DT  DC  DA  DG  DT  DC  DA  DT  DA  DG  DA  DT          
SEQRES   3 L   39   DC  DA  DC  DT  DA  DG  DT  DA  DG  DA  DT  DC  DT          
SEQRES   1 M   39   DA  DG  DA  DT  DC  DT  DA  DC  DT  DA  DG  DT  DG          
SEQRES   2 M   39   DA  DT  DC  DT  DA  DT  DG  DA  DC  DT  DG  DA  DT          
SEQRES   3 M   39   DC  DT  DG  DT  DA  DC  DA  DT  DG  DA  DT  DC  DT          
SEQRES   1 N   39   DA  DG  DA  DT  DC  DA  DT  DG  DT  DA  DC  DA  DG          
SEQRES   2 N   39   DA  DT  DC  DA  DG  DT  DC  DA  DT  DA  DG  DA  DT          
SEQRES   3 N   39   DC  DA  DC  DT  DA  DG  DT  DA  DG  DA  DT  DC  DT          
HET     ZN  A 601       1                                                       
HET     ZN  B 601       1                                                       
HET     ZN  C 601       1                                                       
HET     ZN  D 601       1                                                       
HET     ZN  E 601       1                                                       
HET     ZN  F 601       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL  15   ZN    6(ZN 2+)                                                     
HELIX    1 AA1 LYS A  149  ARG A  158  1                                  10    
HELIX    2 AA2 LYS A  160  LYS A  184  1                                  25    
HELIX    3 AA3 LEU A  248  LEU A  252  5                                   5    
HELIX    4 AA4 SER A  258  GLU A  276  1                                  19    
HELIX    5 AA5 PRO A  319  LYS A  323  5                                   5    
HELIX    6 AA6 GLY A  333  ARG A  341  1                                   9    
HELIX    7 AA7 PHE A  367  ASN A  377  1                                  11    
HELIX    8 AA8 CYS A  393  PHE A  412  1                                  20    
HELIX    9 AA9 GLN A  413  ASP A  416  5                                   4    
HELIX   10 AB1 CYS A  419  ASP A  434  1                                  16    
HELIX   11 AB2 GLN A  436  ARG A  443  5                                   8    
HELIX   12 AB3 ASN A  444  GLU A  463  1                                  20    
HELIX   13 AB4 ASP A  482  ASN A  498  1                                  17    
HELIX   14 AB5 PHE A  501  ASP A  505  5                                   5    
HELIX   15 AB6 LEU B  150  ARG B  158  1                                   9    
HELIX   16 AB7 LYS B  160  LYS B  184  1                                  25    
HELIX   17 AB8 LEU B  248  LEU B  252  5                                   5    
HELIX   18 AB9 SER B  258  GLU B  276  1                                  19    
HELIX   19 AC1 PRO B  319  LYS B  323  5                                   5    
HELIX   20 AC2 GLY B  333  ARG B  341  1                                   9    
HELIX   21 AC3 PHE B  367  ASN B  377  1                                  11    
HELIX   22 AC4 CYS B  393  PHE B  412  1                                  20    
HELIX   23 AC5 GLN B  413  ASP B  416  5                                   4    
HELIX   24 AC6 CYS B  419  ASP B  434  1                                  16    
HELIX   25 AC7 GLN B  436  ARG B  443  5                                   8    
HELIX   26 AC8 ASN B  444  GLU B  463  1                                  20    
HELIX   27 AC9 ASP B  482  ASN B  498  1                                  17    
HELIX   28 AD1 PHE B  501  ASP B  505  5                                   5    
HELIX   29 AD2 LEU C  150  ARG C  158  1                                   9    
HELIX   30 AD3 LYS C  160  LYS C  184  1                                  25    
HELIX   31 AD4 LEU C  248  LEU C  252  5                                   5    
HELIX   32 AD5 SER C  258  GLU C  276  1                                  19    
HELIX   33 AD6 PRO C  319  LYS C  323  5                                   5    
HELIX   34 AD7 GLY C  333  ARG C  342  1                                  10    
HELIX   35 AD8 PHE C  367  ASN C  377  1                                  11    
HELIX   36 AD9 CYS C  393  PHE C  412  1                                  20    
HELIX   37 AE1 GLN C  413  ASP C  416  5                                   4    
HELIX   38 AE2 CYS C  419  ASP C  434  1                                  16    
HELIX   39 AE3 GLN C  436  ARG C  443  5                                   8    
HELIX   40 AE4 ASN C  444  GLU C  463  1                                  20    
HELIX   41 AE5 ASP C  482  ASN C  498  1                                  17    
HELIX   42 AE6 PHE C  501  ASP C  505  5                                   5    
HELIX   43 AE7 LEU D  150  ARG D  158  1                                   9    
HELIX   44 AE8 LYS D  160  LYS D  184  1                                  25    
HELIX   45 AE9 LEU D  248  LEU D  252  5                                   5    
HELIX   46 AF1 SER D  258  GLU D  276  1                                  19    
HELIX   47 AF2 PRO D  319  LYS D  323  5                                   5    
HELIX   48 AF3 GLY D  333  ARG D  341  1                                   9    
HELIX   49 AF4 PHE D  367  ASN D  377  1                                  11    
HELIX   50 AF5 CYS D  393  PHE D  412  1                                  20    
HELIX   51 AF6 GLN D  413  ASP D  416  5                                   4    
HELIX   52 AF7 CYS D  419  ASP D  434  1                                  16    
HELIX   53 AF8 GLN D  436  ARG D  443  5                                   8    
HELIX   54 AF9 ASN D  444  GLU D  463  1                                  20    
HELIX   55 AG1 ASP D  482  ASN D  498  1                                  17    
HELIX   56 AG2 PHE D  501  ASP D  505  5                                   5    
HELIX   57 AG3 LEU E  150  ARG E  158  1                                   9    
HELIX   58 AG4 LYS E  160  LYS E  184  1                                  25    
HELIX   59 AG5 LEU E  248  LEU E  252  5                                   5    
HELIX   60 AG6 SER E  258  GLU E  276  1                                  19    
HELIX   61 AG7 PRO E  319  LYS E  323  5                                   5    
HELIX   62 AG8 GLY E  333  ARG E  341  1                                   9    
HELIX   63 AG9 PHE E  367  ASN E  377  1                                  11    
HELIX   64 AH1 CYS E  393  PHE E  412  1                                  20    
HELIX   65 AH2 GLN E  413  ASP E  416  5                                   4    
HELIX   66 AH3 CYS E  419  ASP E  434  1                                  16    
HELIX   67 AH4 GLN E  436  ARG E  443  5                                   8    
HELIX   68 AH5 ASN E  444  GLU E  463  1                                  20    
HELIX   69 AH6 ASP E  482  ASN E  498  1                                  17    
HELIX   70 AH7 PHE E  501  ASP E  505  5                                   5    
HELIX   71 AH8 LEU F  150  ARG F  158  1                                   9    
HELIX   72 AH9 LYS F  160  LYS F  184  1                                  25    
HELIX   73 AI1 LEU F  248  LEU F  252  5                                   5    
HELIX   74 AI2 SER F  258  GLU F  276  1                                  19    
HELIX   75 AI3 PRO F  319  LYS F  323  5                                   5    
HELIX   76 AI4 GLY F  333  ARG F  341  1                                   9    
HELIX   77 AI5 PHE F  367  ASN F  377  1                                  11    
HELIX   78 AI6 CYS F  393  PHE F  412  1                                  20    
HELIX   79 AI7 GLN F  413  ASP F  416  5                                   4    
HELIX   80 AI8 CYS F  419  ASP F  434  1                                  16    
HELIX   81 AI9 GLN F  436  ARG F  443  5                                   8    
HELIX   82 AJ1 ASN F  444  GLU F  463  1                                  20    
HELIX   83 AJ2 ASP F  482  ASN F  498  1                                  17    
HELIX   84 AJ3 PHE F  501  ASP F  505  5                                   5    
SHEET    1 AA1 7 GLU A 193  THR A 197  0                                        
SHEET    2 AA1 7 GLU A 211  GLU A 219 -1  O  MET A 215   N  LEU A 195           
SHEET    3 AA1 7 GLU A 303  SER A 314  1  O  ILE A 309   N  PHE A 216           
SHEET    4 AA1 7 PHE A 345  PRO A 349 -1  O  PHE A 345   N  SER A 314           
SHEET    5 AA1 7 THR A 362  SER A 366 -1  O  ARG A 364   N  VAL A 348           
SHEET    6 AA1 7 PHE A 234  PHE A 239 -1  N  TYR A 235   O  TRP A 363           
SHEET    7 AA1 7 ILE A 223  GLU A 227 -1  N  GLU A 224   O  LYS A 238           
SHEET    1 AA2 5 GLU A 193  THR A 197  0                                        
SHEET    2 AA2 5 GLU A 211  GLU A 219 -1  O  MET A 215   N  LEU A 195           
SHEET    3 AA2 5 GLU A 303  SER A 314  1  O  ILE A 309   N  PHE A 216           
SHEET    4 AA2 5 ALA A 293  ARG A 299 -1  N  ILE A 298   O  ILE A 304           
SHEET    5 AA2 5 VAL A 282  VAL A 284 -1  N  SER A 283   O  LEU A 297           
SHEET    1 AA3 7 GLU B 193  THR B 197  0                                        
SHEET    2 AA3 7 GLU B 211  GLU B 219 -1  O  MET B 215   N  LEU B 195           
SHEET    3 AA3 7 GLU B 303  SER B 314  1  O  ILE B 309   N  PHE B 216           
SHEET    4 AA3 7 PHE B 345  PRO B 349 -1  O  PHE B 345   N  SER B 314           
SHEET    5 AA3 7 THR B 362  SER B 366 -1  O  ARG B 364   N  VAL B 348           
SHEET    6 AA3 7 PHE B 234  PHE B 239 -1  N  TYR B 235   O  TRP B 363           
SHEET    7 AA3 7 ILE B 223  GLU B 227 -1  N  GLU B 224   O  LYS B 238           
SHEET    1 AA4 5 GLU B 193  THR B 197  0                                        
SHEET    2 AA4 5 GLU B 211  GLU B 219 -1  O  MET B 215   N  LEU B 195           
SHEET    3 AA4 5 GLU B 303  SER B 314  1  O  ILE B 309   N  PHE B 216           
SHEET    4 AA4 5 ALA B 293  ARG B 299 -1  N  ILE B 298   O  ILE B 304           
SHEET    5 AA4 5 VAL B 282  VAL B 284 -1  N  SER B 283   O  LEU B 297           
SHEET    1 AA5 7 GLU C 193  THR C 197  0                                        
SHEET    2 AA5 7 GLU C 211  GLU C 219 -1  O  MET C 215   N  LEU C 195           
SHEET    3 AA5 7 GLU C 303  SER C 314  1  O  ILE C 309   N  PHE C 216           
SHEET    4 AA5 7 PHE C 345  PRO C 349 -1  O  PHE C 345   N  SER C 314           
SHEET    5 AA5 7 THR C 362  SER C 366 -1  O  ARG C 364   N  VAL C 348           
SHEET    6 AA5 7 PHE C 234  PHE C 239 -1  N  TYR C 235   O  TRP C 363           
SHEET    7 AA5 7 ILE C 223  GLU C 227 -1  N  GLU C 224   O  LYS C 238           
SHEET    1 AA6 5 GLU C 193  THR C 197  0                                        
SHEET    2 AA6 5 GLU C 211  GLU C 219 -1  O  MET C 215   N  LEU C 195           
SHEET    3 AA6 5 GLU C 303  SER C 314  1  O  ILE C 309   N  PHE C 216           
SHEET    4 AA6 5 ALA C 293  ARG C 299 -1  N  ILE C 298   O  ILE C 304           
SHEET    5 AA6 5 VAL C 282  VAL C 284 -1  N  SER C 283   O  LEU C 297           
SHEET    1 AA7 7 GLU D 193  THR D 197  0                                        
SHEET    2 AA7 7 GLU D 211  GLU D 219 -1  O  MET D 215   N  LEU D 195           
SHEET    3 AA7 7 GLU D 303  SER D 314  1  O  ILE D 309   N  PHE D 216           
SHEET    4 AA7 7 PHE D 345  PRO D 349 -1  O  PHE D 345   N  SER D 314           
SHEET    5 AA7 7 THR D 362  SER D 366 -1  O  ARG D 364   N  VAL D 348           
SHEET    6 AA7 7 PHE D 234  PHE D 239 -1  N  TYR D 235   O  TRP D 363           
SHEET    7 AA7 7 ILE D 223  GLU D 227 -1  N  GLU D 224   O  LYS D 238           
SHEET    1 AA8 5 GLU D 193  THR D 197  0                                        
SHEET    2 AA8 5 GLU D 211  GLU D 219 -1  O  MET D 215   N  LEU D 195           
SHEET    3 AA8 5 GLU D 303  SER D 314  1  O  ILE D 309   N  PHE D 216           
SHEET    4 AA8 5 ALA D 293  ARG D 299 -1  N  ILE D 298   O  ILE D 304           
SHEET    5 AA8 5 VAL D 282  VAL D 284 -1  N  SER D 283   O  LEU D 297           
SHEET    1 AA9 7 GLU E 193  THR E 197  0                                        
SHEET    2 AA9 7 GLU E 211  GLU E 219 -1  O  MET E 215   N  LEU E 195           
SHEET    3 AA9 7 GLU E 303  SER E 314  1  O  ILE E 309   N  PHE E 216           
SHEET    4 AA9 7 PHE E 345  PRO E 349 -1  O  PHE E 345   N  SER E 314           
SHEET    5 AA9 7 THR E 362  SER E 366 -1  O  ARG E 364   N  VAL E 348           
SHEET    6 AA9 7 PHE E 234  PHE E 239 -1  N  TYR E 235   O  TRP E 363           
SHEET    7 AA9 7 ILE E 223  GLU E 227 -1  N  GLU E 224   O  LYS E 238           
SHEET    1 AB1 5 GLU E 193  THR E 197  0                                        
SHEET    2 AB1 5 GLU E 211  GLU E 219 -1  O  MET E 215   N  LEU E 195           
SHEET    3 AB1 5 GLU E 303  SER E 314  1  O  ILE E 309   N  PHE E 216           
SHEET    4 AB1 5 ALA E 293  ARG E 299 -1  N  ILE E 298   O  ILE E 304           
SHEET    5 AB1 5 VAL E 282  VAL E 284 -1  N  SER E 283   O  LEU E 297           
SHEET    1 AB2 7 GLU F 193  THR F 197  0                                        
SHEET    2 AB2 7 GLU F 211  GLU F 219 -1  O  MET F 215   N  LEU F 195           
SHEET    3 AB2 7 GLU F 303  SER F 314  1  O  ILE F 309   N  PHE F 216           
SHEET    4 AB2 7 PHE F 345  PRO F 349 -1  O  PHE F 345   N  SER F 314           
SHEET    5 AB2 7 THR F 362  SER F 366 -1  O  ARG F 364   N  VAL F 348           
SHEET    6 AB2 7 PHE F 234  PHE F 239 -1  N  TYR F 235   O  TRP F 363           
SHEET    7 AB2 7 ILE F 223  GLU F 227 -1  N  GLU F 224   O  LYS F 238           
SHEET    1 AB3 5 GLU F 193  THR F 197  0                                        
SHEET    2 AB3 5 GLU F 211  GLU F 219 -1  O  MET F 215   N  LEU F 195           
SHEET    3 AB3 5 GLU F 303  SER F 314  1  O  ILE F 309   N  PHE F 216           
SHEET    4 AB3 5 ALA F 293  ARG F 299 -1  N  ILE F 298   O  ILE F 304           
SHEET    5 AB3 5 VAL F 282  VAL F 284 -1  N  SER F 283   O  LEU F 297           
LINK         NE2 HIS A 378                ZN    ZN A 601     1555   1555  2.03  
LINK         SG  CYS A 384                ZN    ZN A 601     1555   1555  2.36  
LINK         SG  CYS A 385                ZN    ZN A 601     1555   1555  2.27  
LINK         SG  CYS A 392                ZN    ZN A 601     1555   1555  2.32  
LINK         NE2 HIS B 378                ZN    ZN B 601     1555   1555  1.99  
LINK         SG  CYS B 384                ZN    ZN B 601     1555   1555  2.32  
LINK         SG  CYS B 385                ZN    ZN B 601     1555   1555  2.32  
LINK         SG  CYS B 392                ZN    ZN B 601     1555   1555  2.37  
LINK         NE2 HIS C 378                ZN    ZN C 601     1555   1555  2.09  
LINK         SG  CYS C 384                ZN    ZN C 601     1555   1555  2.30  
LINK         SG  CYS C 385                ZN    ZN C 601     1555   1555  2.31  
LINK         SG  CYS C 392                ZN    ZN C 601     1555   1555  2.36  
LINK         NE2 HIS D 378                ZN    ZN D 601     1555   1555  2.16  
LINK         SG  CYS D 384                ZN    ZN D 601     1555   1555  2.30  
LINK         SG  CYS D 385                ZN    ZN D 601     1555   1555  2.28  
LINK         SG  CYS D 392                ZN    ZN D 601     1555   1555  2.33  
LINK         NE2 HIS E 378                ZN    ZN E 601     1555   1555  2.07  
LINK         SG  CYS E 384                ZN    ZN E 601     1555   1555  2.32  
LINK         SG  CYS E 385                ZN    ZN E 601     1555   1555  2.31  
LINK         SG  CYS E 392                ZN    ZN E 601     1555   1555  2.28  
LINK         NE2 HIS F 378                ZN    ZN F 601     1555   1555  2.14  
LINK         SG  CYS F 384                ZN    ZN F 601     1555   1555  2.33  
LINK         SG  CYS F 385                ZN    ZN F 601     1555   1555  2.30  
LINK         SG  CYS F 392                ZN    ZN F 601     1555   1555  2.30  
SITE     1 AC1  4 HIS A 378  CYS A 384  CYS A 385  CYS A 392                    
SITE     1 AC2  4 HIS B 378  CYS B 384  CYS B 385  CYS B 392                    
SITE     1 AC3  4 HIS C 378  CYS C 384  CYS C 385  CYS C 392                    
SITE     1 AC4  4 HIS D 378  CYS D 384  CYS D 385  CYS D 392                    
SITE     1 AC5  4 HIS E 378  CYS E 384  CYS E 385  CYS E 392                    
SITE     1 AC6  4 HIS F 378  CYS F 384  CYS F 385  CYS F 392                    
CRYST1  168.530  122.940  179.980  90.00  96.37  90.00 C 1 2 1      24          
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      0.005934  0.000000  0.000663        0.00000                         
SCALE2      0.000000  0.008134  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005591        0.00000                         
ATOM      1  N   LYS A 149      85.379  42.524  69.567  1.00181.77           N  
ANISOU    1  N   LYS A 149    16809  21403  30849  -2404   3979  -4837       N  
ATOM      2  CA  LYS A 149      85.244  41.119  70.074  1.00178.37           C  
ANISOU    2  CA  LYS A 149    16377  21246  30147  -2177   3386  -4839       C  
ATOM      3  C   LYS A 149      83.847  40.599  69.669  1.00172.50           C  
ANISOU    3  C   LYS A 149    16223  20662  28655  -2017   3308  -4393       C  
ATOM      4  O   LYS A 149      83.643  39.985  68.599  1.00171.40           O  
ANISOU    4  O   LYS A 149    16307  20526  28290  -1923   3576  -4185       O  
ATOM      5  CB  LYS A 149      85.488  41.062  71.605  1.00176.75           C  
ANISOU    5  CB  LYS A 149    15888  21181  30087  -2143   2721  -5132       C  
ATOM      6  CG  LYS A 149      86.755  41.798  72.023  1.00180.98           C  
ANISOU    6  CG  LYS A 149    15853  21536  31376  -2317   2797  -5596       C  
ATOM      7  CD  LYS A 149      86.922  42.197  73.457  1.00180.46           C  
ANISOU    7  CD  LYS A 149    15549  21555  31461  -2320   2246  -5904       C  
ATOM      8  CE  LYS A 149      88.041  43.236  73.521  1.00184.22           C  
ANISOU    8  CE  LYS A 149    15513  21763  32717  -2552   2524  -6324       C  
ATOM      9  NZ  LYS A 149      89.327  42.784  72.895  1.00188.25           N  
ANISOU    9  NZ  LYS A 149    15550  22141  33833  -2596   2780  -6581       N  
ATOM     10  N   LEU A 150      82.866  40.917  70.513  1.00169.01           N  
ANISOU   10  N   LEU A 150    16029  20345  27839  -1988   2960  -4262       N  
ATOM     11  CA  LEU A 150      81.470  40.642  70.231  1.00167.63           C  
ANISOU   11  CA  LEU A 150    16383  20299  27007  -1867   2896  -3863       C  
ATOM     12  C   LEU A 150      80.859  41.592  69.218  1.00168.01           C  
ANISOU   12  C   LEU A 150    16779  20181  26876  -1950   3462  -3608       C  
ATOM     13  O   LEU A 150      79.915  41.228  68.522  1.00165.69           O  
ANISOU   13  O   LEU A 150    16897  19954  26103  -1831   3542  -3291       O  
ATOM     14  CB  LEU A 150      80.662  40.762  71.509  1.00168.28           C  
ANISOU   14  CB  LEU A 150    16584  20562  26791  -1818   2379  -3827       C  
ATOM     15  CG  LEU A 150      80.873  39.604  72.470  1.00169.44           C  
ANISOU   15  CG  LEU A 150    16564  20925  26889  -1663   1764  -3936       C  
ATOM     16  CD1 LEU A 150      80.563  40.042  73.888  1.00170.69           C  
ANISOU   16  CD1 LEU A 150    16685  21215  26951  -1659   1320  -4046       C  
ATOM     17  CD2 LEU A 150      80.013  38.414  72.045  1.00166.50           C  
ANISOU   17  CD2 LEU A 150    16524  20697  26040  -1483   1607  -3614       C  
ATOM     18  N   LYS A 151      81.385  42.805  69.131  1.00173.16           N  
ANISOU   18  N   LYS A 151    17268  20604  27919  -2143   3844  -3749       N  
ATOM     19  CA  LYS A 151      80.957  43.820  68.190  1.00178.94           C  
ANISOU   19  CA  LYS A 151    18302  21130  28555  -2231   4419  -3520       C  
ATOM     20  C   LYS A 151      81.099  43.321  66.740  1.00178.18           C  
ANISOU   20  C   LYS A 151    18393  20973  28332  -2152   4883  -3327       C  
ATOM     21  O   LYS A 151      80.273  43.614  65.868  1.00177.78           O  
ANISOU   21  O   LYS A 151    18787  20881  27878  -2087   5183  -3007       O  
ATOM     22  CB  LYS A 151      81.782  45.096  68.424  1.00191.46           C  
ANISOU   22  CB  LYS A 151    19568  22444  30735  -2470   4739  -3771       C  
ATOM     23  CG  LYS A 151      81.849  45.560  69.900  1.00197.82           C  
ANISOU   23  CG  LYS A 151    20114  23309  31738  -2539   4253  -4057       C  
ATOM     24  CD  LYS A 151      83.166  45.190  70.622  1.00206.84           C  
ANISOU   24  CD  LYS A 151    20664  24462  33464  -2595   3985  -4510       C  
ATOM     25  CE  LYS A 151      82.936  44.568  72.002  1.00206.90           C  
ANISOU   25  CE  LYS A 151    20576  24752  33282  -2460   3230  -4666       C  
ATOM     26  NZ  LYS A 151      84.173  44.099  72.701  1.00210.72           N  
ANISOU   26  NZ  LYS A 151    20512  25272  34279  -2462   2899  -5099       N  
ATOM     27  N   LYS A 152      82.169  42.585  66.498  1.00180.03           N  
ANISOU   27  N   LYS A 152    18281  21205  28915  -2143   4931  -3544       N  
ATOM     28  CA  LYS A 152      82.426  42.013  65.191  1.00185.08           C  
ANISOU   28  CA  LYS A 152    19052  21811  29460  -2050   5345  -3419       C  
ATOM     29  C   LYS A 152      81.403  40.923  64.871  1.00180.49           C  
ANISOU   29  C   LYS A 152    18865  21458  28255  -1809   5032  -3165       C  
ATOM     30  O   LYS A 152      80.947  40.787  63.726  1.00177.71           O  
ANISOU   30  O   LYS A 152    18876  21090  27553  -1700   5365  -2924       O  
ATOM     31  CB  LYS A 152      83.866  41.501  65.143  1.00194.20           C  
ANISOU   31  CB  LYS A 152    19679  22909  31199  -2102   5437  -3763       C  
ATOM     32  CG  LYS A 152      84.881  42.651  65.235  1.00206.15           C  
ANISOU   32  CG  LYS A 152    20804  24148  33375  -2358   5860  -4004       C  
ATOM     33  CD  LYS A 152      86.011  42.490  66.255  1.00213.06           C  
ANISOU   33  CD  LYS A 152    21048  25018  34887  -2452   5523  -4461       C  
ATOM     34  CE  LYS A 152      86.381  43.875  66.827  1.00217.39           C  
ANISOU   34  CE  LYS A 152    21347  25335  35914  -2702   5691  -4651       C  
ATOM     35  NZ  LYS A 152      87.639  43.936  67.628  1.00221.97           N  
ANISOU   35  NZ  LYS A 152    21264  25844  37229  -2824   5492  -5142       N  
ATOM     36  N   VAL A 153      81.033  40.166  65.900  1.00182.20           N  
ANISOU   36  N   VAL A 153    19011  21880  28336  -1721   4389  -3223       N  
ATOM     37  CA  VAL A 153      79.985  39.149  65.744  1.00183.84           C  
ANISOU   37  CA  VAL A 153    19567  22286  27995  -1513   4049  -2987       C  
ATOM     38  C   VAL A 153      78.664  39.822  65.387  1.00178.77           C  
ANISOU   38  C   VAL A 153    19419  21644  26859  -1481   4170  -2659       C  
ATOM     39  O   VAL A 153      77.955  39.383  64.491  1.00175.01           O  
ANISOU   39  O   VAL A 153    19300  21217  25978  -1332   4266  -2435       O  
ATOM     40  CB  VAL A 153      79.748  38.282  66.998  1.00186.33           C  
ANISOU   40  CB  VAL A 153    19743  22804  28248  -1433   3354  -3066       C  
ATOM     41  CG1 VAL A 153      78.911  37.050  66.623  1.00181.40           C  
ANISOU   41  CG1 VAL A 153    19406  22335  27182  -1225   3085  -2855       C  
ATOM     42  CG2 VAL A 153      81.075  37.845  67.613  1.00195.54           C  
ANISOU   42  CG2 VAL A 153    20384  23961  29949  -1471   3164  -3425       C  
ATOM     43  N   LEU A 154      78.348  40.906  66.084  1.00177.26           N  
ANISOU   43  N   LEU A 154    19238  21393  26718  -1611   4156  -2655       N  
ATOM     44  CA  LEU A 154      77.137  41.669  65.809  1.00175.77           C  
ANISOU   44  CA  LEU A 154    19487  21182  26115  -1586   4276  -2368       C  
ATOM     45  C   LEU A 154      77.150  42.263  64.406  1.00177.60           C  
ANISOU   45  C   LEU A 154    19993  21232  26255  -1576   4900  -2190       C  
ATOM     46  O   LEU A 154      76.105  42.381  63.770  1.00177.10           O  
ANISOU   46  O   LEU A 154    20363  21196  25730  -1451   4974  -1914       O  
ATOM     47  CB  LEU A 154      76.943  42.789  66.827  1.00177.74           C  
ANISOU   47  CB  LEU A 154    19652  21373  26506  -1733   4176  -2445       C  
ATOM     48  CG  LEU A 154      76.507  42.381  68.251  1.00177.14           C  
ANISOU   48  CG  LEU A 154    19463  21510  26329  -1702   3549  -2532       C  
ATOM     49  CD1 LEU A 154      76.153  43.614  69.075  1.00179.69           C  
ANISOU   49  CD1 LEU A 154    19790  21770  26714  -1822   3520  -2584       C  
ATOM     50  CD2 LEU A 154      75.342  41.411  68.239  1.00175.09           C  
ANISOU   50  CD2 LEU A 154    19512  21466  25548  -1515   3203  -2286       C  
ATOM     51  N   ASP A 155      78.339  42.627  63.922  1.00182.21           N  
ANISOU   51  N   ASP A 155    20321  21629  27282  -1697   5353  -2349       N  
ATOM     52  CA  ASP A 155      78.492  43.063  62.541  1.00187.92           C  
ANISOU   52  CA  ASP A 155    21296  22183  27920  -1670   5989  -2175       C  
ATOM     53  C   ASP A 155      78.175  41.933  61.568  1.00187.30           C  
ANISOU   53  C   ASP A 155    21474  22252  27438  -1436   5975  -2046       C  
ATOM     54  O   ASP A 155      77.505  42.144  60.554  1.00190.86           O  
ANISOU   54  O   ASP A 155    22366  22677  27472  -1302   6252  -1785       O  
ATOM     55  CB  ASP A 155      79.906  43.585  62.255  1.00196.15           C  
ANISOU   55  CB  ASP A 155    21962  22995  29569  -1856   6497  -2388       C  
ATOM     56  CG  ASP A 155      80.210  44.877  62.963  1.00203.67           C  
ANISOU   56  CG  ASP A 155    22707  23737  30940  -2093   6630  -2502       C  
ATOM     57  OD1 ASP A 155      79.287  45.683  63.141  1.00210.84           O  
ANISOU   57  OD1 ASP A 155    23916  24598  31592  -2099   6607  -2310       O  
ATOM     58  OD2 ASP A 155      81.380  45.099  63.323  1.00210.19           O  
ANISOU   58  OD2 ASP A 155    23053  24432  32374  -2269   6760  -2801       O  
ATOM     59  N   LYS A 156      78.656  40.734  61.876  1.00186.75           N  
ANISOU   59  N   LYS A 156    21132  22330  27492  -1370   5635  -2239       N  
ATOM     60  CA  LYS A 156      78.365  39.553  61.049  1.00187.12           C  
ANISOU   60  CA  LYS A 156    21385  22516  27193  -1142   5550  -2163       C  
ATOM     61  C   LYS A 156      76.857  39.227  61.038  1.00177.30           C  
ANISOU   61  C   LYS A 156    20571  21427  25365   -972   5182  -1912       C  
ATOM     62  O   LYS A 156      76.329  38.754  60.047  1.00174.66           O  
ANISOU   62  O   LYS A 156    20569  21147  24643   -781   5269  -1767       O  
ATOM     63  CB  LYS A 156      79.176  38.344  61.561  1.00195.04           C  
ANISOU   63  CB  LYS A 156    21975  23627  28503  -1113   5196  -2438       C  
ATOM     64  CG  LYS A 156      79.019  37.067  60.715  1.00198.13           C  
ANISOU   64  CG  LYS A 156    22524  24136  28620   -882   5110  -2413       C  
ATOM     65  CD  LYS A 156      80.054  35.964  61.008  1.00199.78           C  
ANISOU   65  CD  LYS A 156    22301  24392  29212   -852   4894  -2704       C  
ATOM     66  CE  LYS A 156      79.544  34.845  61.939  1.00195.82           C  
ANISOU   66  CE  LYS A 156    21730  24058  28612   -755   4184  -2729       C  
ATOM     67  NZ  LYS A 156      80.448  33.665  61.878  1.00197.69           N  
ANISOU   67  NZ  LYS A 156    21650  24324  29138   -661   4030  -2968       N  
ATOM     68  N   LEU A 157      76.183  39.461  62.159  1.00171.62           N  
ANISOU   68  N   LEU A 157    19825  20781  24598  -1036   4762  -1882       N  
ATOM     69  CA  LEU A 157      74.782  39.100  62.299  1.00170.32           C  
ANISOU   69  CA  LEU A 157    19992  20766  23954   -896   4384  -1674       C  
ATOM     70  C   LEU A 157      73.832  40.133  61.694  1.00167.80           C  
ANISOU   70  C   LEU A 157    20101  20368  23286   -855   4653  -1415       C  
ATOM     71  O   LEU A 157      72.638  39.867  61.510  1.00169.28           O  
ANISOU   71  O   LEU A 157    20604  20662  23052   -707   4419  -1234       O  
ATOM     72  CB  LEU A 157      74.424  38.846  63.756  1.00173.43           C  
ANISOU   72  CB  LEU A 157    20190  21288  24416   -961   3834  -1738       C  
ATOM     73  CG  LEU A 157      75.191  37.729  64.480  1.00180.11           C  
ANISOU   73  CG  LEU A 157    20656  22230  25545   -959   3462  -1959       C  
ATOM     74  CD1 LEU A 157      74.456  37.385  65.768  1.00181.87           C  
ANISOU   74  CD1 LEU A 157    20844  22609  25647   -957   2908  -1918       C  
ATOM     75  CD2 LEU A 157      75.388  36.448  63.672  1.00183.90           C  
ANISOU   75  CD2 LEU A 157    21163  22764  25946   -791   3413  -1983       C  
ATOM     76  N   ARG A 158      74.375  41.297  61.374  1.00168.69           N  
ANISOU   76  N   ARG A 158    20212  20280  23601   -982   5145  -1405       N  
ATOM     77  CA  ARG A 158      73.578  42.408  60.863  1.00169.98           C  
ANISOU   77  CA  ARG A 158    20766  20329  23488   -953   5425  -1159       C  
ATOM     78  C   ARG A 158      72.946  42.069  59.520  1.00163.01           C  
ANISOU   78  C   ARG A 158    20331  19482  22121   -707   5598   -948       C  
ATOM     79  O   ARG A 158      73.585  41.502  58.655  1.00158.88           O  
ANISOU   79  O   ARG A 158    19812  18957  21597   -621   5841   -998       O  
ATOM     80  CB  ARG A 158      74.433  43.677  60.731  1.00182.15           C  
ANISOU   80  CB  ARG A 158    22194  21605  25409  -1147   5967  -1193       C  
ATOM     81  CG  ARG A 158      73.898  44.709  59.740  1.00194.28           C  
ANISOU   81  CG  ARG A 158    24180  22969  26666  -1074   6430   -910       C  
ATOM     82  CD  ARG A 158      74.687  45.995  59.706  1.00206.25           C  
ANISOU   82  CD  ARG A 158    25576  24187  28600  -1286   6958   -927       C  
ATOM     83  NE  ARG A 158      75.131  46.394  61.033  1.00211.06           N  
ANISOU   83  NE  ARG A 158    25756  24755  29682  -1517   6723  -1174       N  
ATOM     84  CZ  ARG A 158      76.396  46.559  61.419  1.00218.37           C  
ANISOU   84  CZ  ARG A 158    26225  25554  31192  -1725   6901  -1439       C  
ATOM     85  NH1 ARG A 158      77.429  46.399  60.590  1.00219.10           N  
ANISOU   85  NH1 ARG A 158    26191  25528  31527  -1760   7374  -1493       N  
ATOM     86  NH2 ARG A 158      76.633  46.947  62.671  1.00224.28           N  
ANISOU   86  NH2 ARG A 158    26627  26287  32302  -1899   6608  -1669       N  
ATOM     87  N   LEU A 159      71.684  42.418  59.352  1.00158.47           N  
ANISOU   87  N   LEU A 159    20128  18948  21133   -580   5459   -732       N  
ATOM     88  CA  LEU A 159      71.036  42.258  58.056  1.00163.16           C  
ANISOU   88  CA  LEU A 159    21179  19566  21248   -326   5619   -537       C  
ATOM     89  C   LEU A 159      71.451  43.349  57.096  1.00173.47           C  
ANISOU   89  C   LEU A 159    22733  20650  22527   -323   6265   -382       C  
ATOM     90  O   LEU A 159      71.876  44.425  57.517  1.00177.82           O  
ANISOU   90  O   LEU A 159    23163  21010  23389   -521   6539   -374       O  
ATOM     91  CB  LEU A 159      69.519  42.210  58.213  1.00160.94           C  
ANISOU   91  CB  LEU A 159    21185  19407  20556   -175   5210   -379       C  
ATOM     92  CG  LEU A 159      68.935  41.120  59.105  1.00162.06           C  
ANISOU   92  CG  LEU A 159    21133  19759  20684   -162   4592   -481       C  
ATOM     93  CD1 LEU A 159      67.440  40.985  58.834  1.00163.91           C  
ANISOU   93  CD1 LEU A 159    21704  20097  20475     38   4290   -315       C  
ATOM     94  CD2 LEU A 159      69.613  39.777  58.911  1.00163.04           C  
ANISOU   94  CD2 LEU A 159    21047  19982  20915   -112   4451   -657       C  
ATOM     95  N   LYS A 160      71.332  43.037  55.813  1.00183.61           N  
ANISOU   95  N   LYS A 160    24364  21957  23440    -90   6501   -265       N  
ATOM     96  CA  LYS A 160      71.796  43.921  54.731  1.00190.04           C  
ANISOU   96  CA  LYS A 160    25464  22572  24171    -45   7169    -90       C  
ATOM     97  C   LYS A 160      70.594  44.479  53.997  1.00184.16           C  
ANISOU   97  C   LYS A 160    25276  21817  22878    199   7180    195       C  
ATOM     98  O   LYS A 160      69.700  43.718  53.634  1.00181.97           O  
ANISOU   98  O   LYS A 160    25224  21730  22183    440   6802    217       O  
ATOM     99  CB  LYS A 160      72.670  43.143  53.741  1.00197.61           C  
ANISOU   99  CB  LYS A 160    26422  23571  25087     69   7484   -178       C  
ATOM    100  CG  LYS A 160      73.842  42.367  54.353  1.00198.99           C  
ANISOU  100  CG  LYS A 160    26044  23784  25777   -115   7420   -489       C  
ATOM    101  CD  LYS A 160      74.964  43.283  54.832  1.00202.34           C  
ANISOU  101  CD  LYS A 160    26114  23976  26789   -418   7849   -572       C  
ATOM    102  CE  LYS A 160      75.895  42.615  55.837  1.00200.64           C  
ANISOU  102  CE  LYS A 160    25297  23813  27122   -617   7587   -906       C  
ATOM    103  NZ  LYS A 160      76.470  43.622  56.792  1.00201.96           N  
ANISOU  103  NZ  LYS A 160    25116  23788  27830   -920   7706  -1002       N  
ATOM    104  N   ARG A 161      70.569  45.801  53.809  1.00178.46           N  
ANISOU  104  N   ARG A 161    24758  20862  22187    138   7590    400       N  
ATOM    105  CA  ARG A 161      69.345  46.496  53.433  1.00177.47           C  
ANISOU  105  CA  ARG A 161    25102  20705  21622    337   7511    660       C  
ATOM    106  C   ARG A 161      68.834  46.136  52.041  1.00177.20           C  
ANISOU  106  C   ARG A 161    25586  20762  20979    707   7610    829       C  
ATOM    107  O   ARG A 161      67.663  46.355  51.714  1.00178.31           O  
ANISOU  107  O   ARG A 161    26103  20956  20690    939   7370    992       O  
ATOM    108  CB  ARG A 161      69.449  48.020  53.667  1.00182.65           C  
ANISOU  108  CB  ARG A 161    25829  21059  22507    175   7899    830       C  
ATOM    109  CG  ARG A 161      69.936  48.942  52.546  1.00193.35           C  
ANISOU  109  CG  ARG A 161    27544  22155  23765    243   8620   1090       C  
ATOM    110  CD  ARG A 161      70.172  50.359  53.115  1.00199.46           C  
ANISOU  110  CD  ARG A 161    28228  22603  24953     -4   8933   1181       C  
ATOM    111  NE  ARG A 161      71.013  51.245  52.276  1.00206.40           N  
ANISOU  111  NE  ARG A 161    29285  23169  25968    -56   9713   1384       N  
ATOM    112  CZ  ARG A 161      71.263  52.552  52.503  1.00205.51           C  
ANISOU  112  CZ  ARG A 161    29172  22709  26202   -244  10103   1513       C  
ATOM    113  NH1 ARG A 161      70.757  53.194  53.561  1.00202.91           N  
ANISOU  113  NH1 ARG A 161    28673  22301  26122   -396   9786   1440       N  
ATOM    114  NH2 ARG A 161      72.035  53.242  51.663  1.00206.61           N  
ANISOU  114  NH2 ARG A 161    29483  22563  26455   -282  10839   1715       N  
ATOM    115  N   LYS A 162      69.732  45.614  51.215  1.00180.72           N  
ANISOU  115  N   LYS A 162    26047  21224  21394    772   7971    777       N  
ATOM    116  CA  LYS A 162      69.355  45.148  49.878  1.00190.22           C  
ANISOU  116  CA  LYS A 162    27729  22544  22002   1144   8056    889       C  
ATOM    117  C   LYS A 162      68.560  43.861  49.993  1.00184.14           C  
ANISOU  117  C   LYS A 162    26919  22059  20984   1323   7381    706       C  
ATOM    118  O   LYS A 162      67.442  43.750  49.451  1.00178.87           O  
ANISOU  118  O   LYS A 162    26641  21499  19821   1617   7092    810       O  
ATOM    119  CB  LYS A 162      70.633  44.958  49.043  1.00203.39           C  
ANISOU  119  CB  LYS A 162    29377  24146  23753   1141   8670    857       C  
ATOM    120  CG  LYS A 162      70.393  44.695  47.542  1.00215.72           C  
ANISOU  120  CG  LYS A 162    31498  25797  24668   1540   8908   1004       C  
ATOM    121  CD  LYS A 162      70.596  45.869  46.500  1.00226.72           C  
ANISOU  121  CD  LYS A 162    33395  26967  25781   1670   9629   1361       C  
ATOM    122  CE  LYS A 162      69.287  46.445  45.897  1.00231.27           C  
ANISOU  122  CE  LYS A 162    34581  27552  25738   2006   9451   1642       C  
ATOM    123  NZ  LYS A 162      68.533  45.527  45.020  1.00237.53           N  
ANISOU  123  NZ  LYS A 162    35739  28613  25895   2424   9086   1586       N  
ATOM    124  N   ASP A 163      69.143  42.897  50.708  1.00183.82           N  
ANISOU  124  N   ASP A 163    26399  22127  21317   1148   7127    429       N  
ATOM    125  CA  ASP A 163      68.481  41.617  51.007  1.00182.12           C  
ANISOU  125  CA  ASP A 163    26060  22147  20990   1258   6478    238       C  
ATOM    126  C   ASP A 163      67.122  41.893  51.627  1.00174.45           C  
ANISOU  126  C   ASP A 163    25183  21227  19871   1293   5986    329       C  
ATOM    127  O   ASP A 163      66.098  41.320  51.216  1.00173.67           O  
ANISOU  127  O   ASP A 163    25316  21275  19393   1547   5591    328       O  
ATOM    128  CB  ASP A 163      69.262  40.793  52.066  1.00184.73           C  
ANISOU  128  CB  ASP A 163    25804  22531  21851    995   6244    -32       C  
ATOM    129  CG  ASP A 163      70.500  40.099  51.497  1.00192.95           C  
ANISOU  129  CG  ASP A 163    26679  23583  23049   1001   6565   -206       C  
ATOM    130  OD1 ASP A 163      70.363  39.167  50.670  1.00194.51           O  
ANISOU  130  OD1 ASP A 163    27048  23915  22939   1253   6457   -292       O  
ATOM    131  OD2 ASP A 163      71.619  40.462  51.917  1.00200.47           O  
ANISOU  131  OD2 ASP A 163    27298  24407  24464    753   6906   -284       O  
ATOM    132  N   ILE A 164      67.134  42.765  52.635  1.00169.62           N  
ANISOU  132  N   ILE A 164    24365  20492  19587   1036   6009    383       N  
ATOM    133  CA  ILE A 164      65.920  43.177  53.347  1.00167.67           C  
ANISOU  133  CA  ILE A 164    24169  20276  19262   1034   5602    466       C  
ATOM    134  C   ILE A 164      64.885  43.733  52.378  1.00164.97           C  
ANISOU  134  C   ILE A 164    24366  19918  18396   1346   5628    689       C  
ATOM    135  O   ILE A 164      63.714  43.350  52.423  1.00161.67           O  
ANISOU  135  O   ILE A 164    24063  19636  17729   1515   5156    686       O  
ATOM    136  CB  ILE A 164      66.237  44.210  54.428  1.00169.77           C  
ANISOU  136  CB  ILE A 164    24180  20381  19943    730   5738    490       C  
ATOM    137  CG1 ILE A 164      67.075  43.554  55.537  1.00169.91           C  
ANISOU  137  CG1 ILE A 164    23651  20458  20449    455   5562    240       C  
ATOM    138  CG2 ILE A 164      64.959  44.806  55.020  1.00168.47           C  
ANISOU  138  CG2 ILE A 164    24129  20229  19651    763   5404    599       C  
ATOM    139  CD1 ILE A 164      67.940  44.532  56.310  1.00172.62           C  
ANISOU  139  CD1 ILE A 164    23714  20608  21264    156   5868    201       C  
ATOM    140  N   SER A 165      65.327  44.637  51.509  1.00166.93           N  
ANISOU  140  N   SER A 165    24938  19991  18494   1426   6184    884       N  
ATOM    141  CA  SER A 165      64.435  45.285  50.559  1.00171.81           C  
ANISOU  141  CA  SER A 165    26107  20569  18604   1742   6254   1125       C  
ATOM    142  C   SER A 165      63.742  44.291  49.621  1.00171.99           C  
ANISOU  142  C   SER A 165    26413  20806  18127   2108   5924   1062       C  
ATOM    143  O   SER A 165      62.509  44.303  49.494  1.00169.31           O  
ANISOU  143  O   SER A 165    26294  20551  17484   2326   5520   1110       O  
ATOM    144  CB  SER A 165      65.194  46.333  49.784  1.00180.20           C  
ANISOU  144  CB  SER A 165    27457  21392  19617   1755   6961   1355       C  
ATOM    145  OG  SER A 165      64.294  47.046  48.973  1.00189.16           O  
ANISOU  145  OG  SER A 165    29134  22469  20267   2064   7004   1611       O  
ATOM    146  N   GLU A 166      64.525  43.426  48.986  1.00176.06           N  
ANISOU  146  N   GLU A 166    26901  21408  18584   2179   6078    928       N  
ATOM    147  CA  GLU A 166      63.964  42.446  48.053  1.00181.82           C  
ANISOU  147  CA  GLU A 166    27892  22335  18854   2534   5776    826       C  
ATOM    148  C   GLU A 166      63.027  41.444  48.740  1.00173.93           C  
ANISOU  148  C   GLU A 166    26633  21516  17934   2535   5050    617       C  
ATOM    149  O   GLU A 166      61.854  41.260  48.319  1.00176.18           O  
ANISOU  149  O   GLU A 166    27179  21902  17858   2812   4654    625       O  
ATOM    150  CB  GLU A 166      65.087  41.689  47.347  1.00191.82           C  
ANISOU  150  CB  GLU A 166    29121  23652  20107   2580   6098    687       C  
ATOM    151  CG  GLU A 166      65.896  42.571  46.404  1.00202.59           C  
ANISOU  151  CG  GLU A 166    30830  24860  21285   2659   6841    909       C  
ATOM    152  CD  GLU A 166      67.255  41.995  46.021  1.00209.50           C  
ANISOU  152  CD  GLU A 166    31518  25741  22339   2581   7270    764       C  
ATOM    153  OE1 GLU A 166      67.707  40.999  46.640  1.00208.29           O  
ANISOU  153  OE1 GLU A 166    30908  25684  22547   2413   7008    487       O  
ATOM    154  OE2 GLU A 166      67.888  42.584  45.102  1.00218.73           O  
ANISOU  154  OE2 GLU A 166    33003  26804  23299   2689   7900    941       O  
ATOM    155  N   ALA A 167      63.548  40.810  49.792  1.00165.63           N  
ANISOU  155  N   ALA A 167    25069  20494  17368   2231   4883    434       N  
ATOM    156  CA  ALA A 167      62.779  39.838  50.559  1.00161.25           C  
ANISOU  156  CA  ALA A 167    24227  20082  16957   2186   4251    258       C  
ATOM    157  C   ALA A 167      61.444  40.441  51.008  1.00159.99           C  
ANISOU  157  C   ALA A 167    24173  19926  16690   2231   3918    380       C  
ATOM    158  O   ALA A 167      60.379  39.866  50.779  1.00159.02           O  
ANISOU  158  O   ALA A 167    24145  19921  16353   2435   3463    311       O  
ATOM    159  CB  ALA A 167      63.581  39.370  51.757  1.00156.38           C  
ANISOU  159  CB  ALA A 167    23073  19457  16884   1832   4192    112       C  
ATOM    160  N   ALA A 168      61.515  41.616  51.628  1.00159.40           N  
ANISOU  160  N   ALA A 168    24068  19709  16786   2045   4155    544       N  
ATOM    161  CA  ALA A 168      60.310  42.331  52.045  1.00159.01           C  
ANISOU  161  CA  ALA A 168    24124  19642  16648   2091   3902    666       C  
ATOM    162  C   ALA A 168      59.337  42.623  50.890  1.00156.29           C  
ANISOU  162  C   ALA A 168    24284  19322  15775   2490   3812    782       C  
ATOM    163  O   ALA A 168      58.125  42.483  51.065  1.00148.34           O  
ANISOU  163  O   ALA A 168    23304  18400  14659   2617   3365    757       O  
ATOM    164  CB  ALA A 168      60.686  43.635  52.722  1.00163.74           C  
ANISOU  164  CB  ALA A 168    24660  20055  17497   1857   4249    817       C  
ATOM    165  N   GLU A 169      59.863  43.042  49.733  1.00161.32           N  
ANISOU  165  N   GLU A 169    25317  19885  16091   2693   4240    909       N  
ATOM    166  CA  GLU A 169      59.020  43.268  48.563  1.00168.39           C  
ANISOU  166  CA  GLU A 169    26730  20818  16434   3116   4151   1014       C  
ATOM    167  C   GLU A 169      58.164  42.032  48.273  1.00165.96           C  
ANISOU  167  C   GLU A 169    26386  20721  15948   3336   3557    782       C  
ATOM    168  O   GLU A 169      56.908  42.070  48.383  1.00169.94           O  
ANISOU  168  O   GLU A 169    26948  21285  16336   3488   3110    766       O  
ATOM    169  CB  GLU A 169      59.845  43.685  47.328  1.00178.58           C  
ANISOU  169  CB  GLU A 169    28448  22024  17379   3314   4719   1168       C  
ATOM    170  CG  GLU A 169      59.096  44.512  46.275  1.00187.15           C  
ANISOU  170  CG  GLU A 169    30139  23060  17910   3713   4793   1401       C  
ATOM    171  CD  GLU A 169      59.548  44.224  44.822  1.00196.52           C  
ANISOU  171  CD  GLU A 169    31785  24306  18576   4065   5081   1437       C  
ATOM    172  OE1 GLU A 169      59.839  43.045  44.491  1.00197.87           O  
ANISOU  172  OE1 GLU A 169    31842  24648  18690   4138   4912   1190       O  
ATOM    173  OE2 GLU A 169      59.597  45.180  44.027  1.00203.80           O  
ANISOU  173  OE2 GLU A 169    33191  25101  19143   4278   5477   1716       O  
ATOM    174  N   THR A 170      58.842  40.938  47.925  1.00164.21           N  
ANISOU  174  N   THR A 170    26045  20599  15746   3348   3550    585       N  
ATOM    175  CA  THR A 170      58.159  39.691  47.579  1.00165.12           C  
ANISOU  175  CA  THR A 170    26117  20889  15730   3554   3015    335       C  
ATOM    176  C   THR A 170      57.170  39.250  48.688  1.00159.87           C  
ANISOU  176  C   THR A 170    25069  20279  15394   3387   2460    225       C  
ATOM    177  O   THR A 170      55.979  39.029  48.445  1.00157.38           O  
ANISOU  177  O   THR A 170    24855  20040  14901   3608   2014    158       O  
ATOM    178  CB  THR A 170      59.191  38.556  47.408  1.00167.01           C  
ANISOU  178  CB  THR A 170    26142  21193  16118   3479   3100    119       C  
ATOM    179  OG1 THR A 170      60.361  39.056  46.744  1.00172.87           O  
ANISOU  179  OG1 THR A 170    27096  21856  16729   3496   3728    236       O  
ATOM    180  CG2 THR A 170      58.584  37.396  46.616  1.00169.64           C  
ANISOU  180  CG2 THR A 170    26587  21681  16187   3796   2649   -129       C  
ATOM    181  N   VAL A 171      57.692  39.160  49.905  1.00156.13           N  
ANISOU  181  N   VAL A 171    24155  19762  15402   3000   2511    211       N  
ATOM    182  CA  VAL A 171      56.920  38.734  51.063  1.00153.44           C  
ANISOU  182  CA  VAL A 171    23434  19471  15396   2805   2069    132       C  
ATOM    183  C   VAL A 171      55.627  39.535  51.229  1.00144.49           C  
ANISOU  183  C   VAL A 171    22440  18326  14133   2918   1848    249       C  
ATOM    184  O   VAL A 171      54.552  38.937  51.305  1.00135.90           O  
ANISOU  184  O   VAL A 171    21266  17325  13042   3027   1371    131       O  
ATOM    185  CB  VAL A 171      57.739  38.696  52.364  1.00157.08           C  
ANISOU  185  CB  VAL A 171    23455  19885  16342   2395   2204    129       C  
ATOM    186  CG1 VAL A 171      56.855  38.324  53.557  1.00154.45           C  
ANISOU  186  CG1 VAL A 171    22778  19610  16296   2222   1772     83       C  
ATOM    187  CG2 VAL A 171      58.890  37.715  52.209  1.00160.02           C  
ANISOU  187  CG2 VAL A 171    23646  20282  16872   2315   2320    -29       C  
ATOM    188  N   ASN A 172      55.736  40.862  51.245  1.00143.05           N  
ANISOU  188  N   ASN A 172    22465  18021  13864   2900   2195    469       N  
ATOM    189  CA  ASN A 172      54.569  41.729  51.335  1.00146.85           C  
ANISOU  189  CA  ASN A 172    23109  18473  14214   3033   2024    588       C  
ATOM    190  C   ASN A 172      53.549  41.469  50.218  1.00145.98           C  
ANISOU  190  C   ASN A 172    23340  18446  13680   3460   1691    529       C  
ATOM    191  O   ASN A 172      52.325  41.515  50.450  1.00143.89           O  
ANISOU  191  O   ASN A 172    23027  18226  13416   3564   1291    489       O  
ATOM    192  CB  ASN A 172      54.992  43.201  51.276  1.00154.04           C  
ANISOU  192  CB  ASN A 172    24265  19204  15058   2997   2507    839       C  
ATOM    193  CG  ASN A 172      55.553  43.720  52.627  1.00153.42           C  
ANISOU  193  CG  ASN A 172    23816  19035  15439   2586   2704    878       C  
ATOM    194  OD1 ASN A 172      54.930  43.602  53.705  1.00150.53           O  
ANISOU  194  OD1 ASN A 172    23135  18725  15334   2416   2408    814       O  
ATOM    195  ND2 ASN A 172      56.734  44.331  52.564  1.00153.91           N  
ANISOU  195  ND2 ASN A 172    23922  18954  15600   2435   3217    980       N  
ATOM    196  N   LYS A 173      54.043  41.242  49.002  1.00149.02           N  
ANISOU  196  N   LYS A 173    24071  18850  13697   3722   1861    517       N  
ATOM    197  CA  LYS A 173      53.131  40.927  47.901  1.00153.31           C  
ANISOU  197  CA  LYS A 173    24950  19490  13809   4159   1513    424       C  
ATOM    198  C   LYS A 173      52.292  39.680  48.176  1.00146.95           C  
ANISOU  198  C   LYS A 173    23826  18820  13188   4175    908    138       C  
ATOM    199  O   LYS A 173      51.054  39.727  48.179  1.00149.67           O  
ANISOU  199  O   LYS A 173    24173  19206  13489   4341    487     77       O  
ATOM    200  CB  LYS A 173      53.904  40.765  46.578  1.00162.37           C  
ANISOU  200  CB  LYS A 173    26514  20660  14517   4438   1809    431       C  
ATOM    201  CG  LYS A 173      54.450  42.053  45.989  1.00168.02           C  
ANISOU  201  CG  LYS A 173    27671  21233  14932   4545   2374    740       C  
ATOM    202  CD  LYS A 173      54.620  41.974  44.457  1.00172.96           C  
ANISOU  202  CD  LYS A 173    28850  21919  14946   4993   2511    760       C  
ATOM    203  CE  LYS A 173      54.538  43.354  43.803  1.00176.74           C  
ANISOU  203  CE  LYS A 173    29860  22257  15034   5225   2885   1100       C  
ATOM    204  NZ  LYS A 173      54.046  43.354  42.393  1.00181.88           N  
ANISOU  204  NZ  LYS A 173    31095  23000  15010   5773   2764   1115       N  
ATOM    205  N   VAL A 174      52.977  38.578  48.429  1.00140.34           N  
ANISOU  205  N   VAL A 174    22696  18032  12593   3995    876    -37       N  
ATOM    206  CA  VAL A 174      52.319  37.298  48.745  1.00140.41           C  
ANISOU  206  CA  VAL A 174    22367  18133  12850   3966    343   -304       C  
ATOM    207  C   VAL A 174      51.325  37.430  49.916  1.00138.15           C  
ANISOU  207  C   VAL A 174    21728  17836  12925   3756     44   -283       C  
ATOM    208  O   VAL A 174      50.157  37.020  49.810  1.00135.40           O  
ANISOU  208  O   VAL A 174    21310  17542  12594   3911   -422   -426       O  
ATOM    209  CB  VAL A 174      53.393  36.285  49.195  1.00139.62           C  
ANISOU  209  CB  VAL A 174    21938  18037  13072   3699    451   -427       C  
ATOM    210  CG1 VAL A 174      52.754  34.979  49.662  1.00139.76           C  
ANISOU  210  CG1 VAL A 174    21578  18107  13416   3623    -64   -668       C  
ATOM    211  CG2 VAL A 174      54.417  36.040  48.082  1.00141.57           C  
ANISOU  211  CG2 VAL A 174    22480  18303  13005   3892    759   -482       C  
ATOM    212  N   VAL A 175      51.798  37.990  51.030  1.00138.29           N  
ANISOU  212  N   VAL A 175    21514  17787  13241   3409    315   -122       N  
ATOM    213  CA  VAL A 175      50.954  38.193  52.205  1.00140.27           C  
ANISOU  213  CA  VAL A 175    21444  18037  13813   3201    102    -84       C  
ATOM    214  C   VAL A 175      49.677  38.992  51.865  1.00151.27           C  
ANISOU  214  C   VAL A 175    23048  19430  14997   3459   -108    -33       C  
ATOM    215  O   VAL A 175      48.577  38.640  52.296  1.00148.41           O  
ANISOU  215  O   VAL A 175    22456  19113  14817   3460   -500   -134       O  
ATOM    216  CB  VAL A 175      51.731  38.885  53.317  1.00137.21           C  
ANISOU  216  CB  VAL A 175    20866  17580  13686   2847    470     82       C  
ATOM    217  CG1 VAL A 175      50.802  39.360  54.461  1.00137.02           C  
ANISOU  217  CG1 VAL A 175    20594  17560  13906   2683    306    144       C  
ATOM    218  CG2 VAL A 175      52.845  37.963  53.806  1.00134.35           C  
ANISOU  218  CG2 VAL A 175    20220  17230  13597   2592    575     -2       C  
ATOM    219  N   GLU A 176      49.837  40.065  51.095  1.00165.51           N  
ANISOU  219  N   GLU A 176    25282  21170  16433   3679    162    128       N  
ATOM    220  CA  GLU A 176      48.693  40.876  50.712  1.00173.71           C  
ANISOU  220  CA  GLU A 176    26556  22195  17251   3958    -30    187       C  
ATOM    221  C   GLU A 176      47.673  40.058  49.902  1.00172.52           C  
ANISOU  221  C   GLU A 176    26463  22147  16939   4292   -559    -48       C  
ATOM    222  O   GLU A 176      46.479  40.097  50.187  1.00171.19           O  
ANISOU  222  O   GLU A 176    26144  22007  16894   4364   -930   -126       O  
ATOM    223  CB  GLU A 176      49.162  42.154  49.999  1.00189.95           C  
ANISOU  223  CB  GLU A 176    29095  24137  18938   4140    392    432       C  
ATOM    224  CG  GLU A 176      48.257  43.373  50.208  1.00203.40           C  
ANISOU  224  CG  GLU A 176    30934  25758  20587   4251    356    586       C  
ATOM    225  CD  GLU A 176      47.004  43.348  49.352  1.00216.27           C  
ANISOU  225  CD  GLU A 176    32797  27453  21923   4685    -94    486       C  
ATOM    226  OE1 GLU A 176      45.962  43.885  49.800  1.00214.30           O  
ANISOU  226  OE1 GLU A 176    32447  27185  21790   4730   -324    495       O  
ATOM    227  OE2 GLU A 176      47.053  42.793  48.224  1.00230.64           O  
ANISOU  227  OE2 GLU A 176    34896  29344  23391   4996   -230    381       O  
ATOM    228  N   ARG A 177      48.161  39.294  48.930  1.00173.50           N  
ANISOU  228  N   ARG A 177    26774  22326  16820   4485   -595   -184       N  
ATOM    229  CA  ARG A 177      47.283  38.423  48.154  1.00176.99           C  
ANISOU  229  CA  ARG A 177    27250  22865  17133   4799  -1118   -458       C  
ATOM    230  C   ARG A 177      46.502  37.422  49.031  1.00167.94           C  
ANISOU  230  C   ARG A 177    25567  21754  16488   4583  -1553   -669       C  
ATOM    231  O   ARG A 177      45.296  37.242  48.878  1.00169.49           O  
ANISOU  231  O   ARG A 177    25680  21985  16732   4764  -2001   -825       O  
ATOM    232  CB  ARG A 177      48.053  37.638  47.063  1.00184.87           C  
ANISOU  232  CB  ARG A 177    28493  23922  17827   5009  -1072   -607       C  
ATOM    233  CG  ARG A 177      48.179  38.377  45.737  1.00194.52           C  
ANISOU  233  CG  ARG A 177    30331  25157  18419   5446   -905   -504       C  
ATOM    234  CD  ARG A 177      48.642  37.518  44.565  1.00199.64           C  
ANISOU  234  CD  ARG A 177    31235  25900  18717   5740   -975   -714       C  
ATOM    235  NE  ARG A 177      47.727  36.426  44.219  1.00203.68           N  
ANISOU  235  NE  ARG A 177    31585  26505  19299   5938  -1606  -1081       N  
ATOM    236  CZ  ARG A 177      47.860  35.640  43.133  1.00208.80           C  
ANISOU  236  CZ  ARG A 177    32458  27248  19627   6265  -1800  -1336       C  
ATOM    237  NH1 ARG A 177      48.859  35.800  42.250  1.00211.51           N  
ANISOU  237  NH1 ARG A 177    33218  27624  19519   6450  -1397  -1256       N  
ATOM    238  NH2 ARG A 177      46.975  34.658  42.911  1.00209.55           N  
ANISOU  238  NH2 ARG A 177    32351  27403  19864   6416  -2404  -1696       N  
ATOM    239  N   LEU A 178      47.204  36.785  49.948  1.00160.80           N  
ANISOU  239  N   LEU A 178    24299  20831  15965   4200  -1409   -666       N  
ATOM    240  CA  LEU A 178      46.566  35.829  50.834  1.00161.21           C  
ANISOU  240  CA  LEU A 178    23857  20895  16499   3971  -1752   -819       C  
ATOM    241  C   LEU A 178      45.519  36.435  51.752  1.00155.10           C  
ANISOU  241  C   LEU A 178    22851  20108  15969   3850  -1876   -732       C  
ATOM    242  O   LEU A 178      44.430  35.893  51.895  1.00152.30           O  
ANISOU  242  O   LEU A 178    22252  19775  15841   3894  -2288   -901       O  
ATOM    243  CB  LEU A 178      47.612  35.112  51.657  1.00166.66           C  
ANISOU  243  CB  LEU A 178    24249  21560  17512   3602  -1539   -792       C  
ATOM    244  CG  LEU A 178      48.337  34.093  50.759  1.00171.29           C  
ANISOU  244  CG  LEU A 178    24943  22167  17973   3742  -1588   -988       C  
ATOM    245  CD1 LEU A 178      49.648  33.695  51.368  1.00173.29           C  
ANISOU  245  CD1 LEU A 178    25021  22387  18435   3436  -1260   -918       C  
ATOM    246  CD2 LEU A 178      47.467  32.865  50.548  1.00169.62           C  
ANISOU  246  CD2 LEU A 178    24497  21968  17980   3835  -2118  -1281       C  
ATOM    247  N   LEU A 179      45.843  37.565  52.372  1.00152.96           N  
ANISOU  247  N   LEU A 179    22646  19796  15675   3699  -1513   -484       N  
ATOM    248  CA  LEU A 179      44.893  38.292  53.228  1.00155.27           C  
ANISOU  248  CA  LEU A 179    22757  20078  16160   3606  -1582   -396       C  
ATOM    249  C   LEU A 179      43.637  38.659  52.430  1.00158.43           C  
ANISOU  249  C   LEU A 179    23335  20497  16362   3988  -1939   -501       C  
ATOM    250  O   LEU A 179      42.507  38.368  52.839  1.00153.15           O  
ANISOU  250  O   LEU A 179    22373  19855  15963   3982  -2281   -625       O  
ATOM    251  CB  LEU A 179      45.579  39.561  53.732  1.00156.33           C  
ANISOU  251  CB  LEU A 179    23040  20146  16210   3460  -1112   -135       C  
ATOM    252  CG  LEU A 179      44.827  40.485  54.702  1.00158.33           C  
ANISOU  252  CG  LEU A 179    23133  20378  16645   3341  -1084    -24       C  
ATOM    253  CD1 LEU A 179      44.635  39.819  56.056  1.00155.28           C  
ANISOU  253  CD1 LEU A 179    22253  20041  16705   2985  -1159    -61       C  
ATOM    254  CD2 LEU A 179      45.549  41.809  54.878  1.00158.98           C  
ANISOU  254  CD2 LEU A 179    23458  20365  16581   3280   -632    203       C  
ATOM    255  N   ARG A 180      43.855  39.289  51.287  1.00167.04           N  
ANISOU  255  N   ARG A 180    24909  21572  16984   4328  -1853   -449       N  
ATOM    256  CA  ARG A 180      42.770  39.727  50.417  1.00177.55           C  
ANISOU  256  CA  ARG A 180    26486  22922  18052   4749  -2188   -535       C  
ATOM    257  C   ARG A 180      41.844  38.565  50.028  1.00174.42           C  
ANISOU  257  C   ARG A 180    25863  22597  17812   4905  -2754   -868       C  
ATOM    258  O   ARG A 180      40.628  38.678  50.112  1.00182.41           O  
ANISOU  258  O   ARG A 180    26716  23622  18968   5035  -3113   -988       O  
ATOM    259  CB  ARG A 180      43.420  40.327  49.175  1.00190.85           C  
ANISOU  259  CB  ARG A 180    28759  24585  19167   5084  -1967   -421       C  
ATOM    260  CG  ARG A 180      42.578  41.213  48.282  1.00204.62           C  
ANISOU  260  CG  ARG A 180    30905  26319  20523   5540  -2157   -388       C  
ATOM    261  CD  ARG A 180      43.271  42.576  48.052  1.00213.26           C  
ANISOU  261  CD  ARG A 180    32441  27298  21289   5602  -1647    -47       C  
ATOM    262  NE  ARG A 180      43.387  42.995  46.645  1.00223.82           N  
ANISOU  262  NE  ARG A 180    34382  28634  22025   6074  -1621     19       N  
ATOM    263  CZ  ARG A 180      43.793  44.195  46.246  1.00227.71           C  
ANISOU  263  CZ  ARG A 180    35322  29007  22187   6217  -1232    319       C  
ATOM    264  NH1 ARG A 180      44.124  45.156  47.115  1.00226.28           N  
ANISOU  264  NH1 ARG A 180    35055  28687  22232   5929   -844    563       N  
ATOM    265  NH2 ARG A 180      43.851  44.464  44.940  1.00231.88           N  
ANISOU  265  NH2 ARG A 180    36413  29548  22141   6672  -1231    379       N  
ATOM    266  N   ARG A 181      42.430  37.453  49.601  1.00169.20           N  
ANISOU  266  N   ARG A 181    25169  21968  17149   4892  -2830  -1034       N  
ATOM    267  CA  ARG A 181      41.657  36.242  49.330  1.00169.36           C  
ANISOU  267  CA  ARG A 181    24918  22026  17402   4984  -3350  -1372       C  
ATOM    268  C   ARG A 181      40.885  35.791  50.584  1.00160.14           C  
ANISOU  268  C   ARG A 181    23173  20830  16839   4644  -3515  -1418       C  
ATOM    269  O   ARG A 181      39.737  35.388  50.514  1.00156.55           O  
ANISOU  269  O   ARG A 181    22483  20383  16614   4756  -3950  -1639       O  
ATOM    270  CB  ARG A 181      42.597  35.129  48.898  1.00173.27           C  
ANISOU  270  CB  ARG A 181    25426  22535  17872   4942  -3320  -1513       C  
ATOM    271  CG  ARG A 181      41.969  33.732  48.814  1.00177.36           C  
ANISOU  271  CG  ARG A 181    25587  23053  18748   4941  -3813  -1862       C  
ATOM    272  CD  ARG A 181      41.046  33.526  47.624  1.00185.95           C  
ANISOU  272  CD  ARG A 181    26864  24191  19596   5411  -4322  -2169       C  
ATOM    273  NE  ARG A 181      41.023  32.096  47.297  1.00188.27           N  
ANISOU  273  NE  ARG A 181    26932  24470  20132   5418  -4667  -2508       N  
ATOM    274  CZ  ARG A 181      40.198  31.174  47.800  1.00187.13           C  
ANISOU  274  CZ  ARG A 181    26297  24262  20542   5259  -5042  -2733       C  
ATOM    275  NH1 ARG A 181      39.255  31.498  48.668  1.00186.51           N  
ANISOU  275  NH1 ARG A 181    25877  24146  20840   5083  -5132  -2666       N  
ATOM    276  NH2 ARG A 181      40.301  29.922  47.423  1.00186.62           N  
ANISOU  276  NH2 ARG A 181    26074  24158  20672   5280  -5320  -3034       N  
ATOM    277  N   MET A 182      41.532  35.894  51.733  1.00156.56           N  
ANISOU  277  N   MET A 182    22500  20346  16638   4237  -3149  -1207       N  
ATOM    278  CA  MET A 182      40.919  35.490  52.978  1.00159.28           C  
ANISOU  278  CA  MET A 182    22336  20673  17509   3907  -3229  -1206       C  
ATOM    279  C   MET A 182      39.702  36.343  53.300  1.00161.32           C  
ANISOU  279  C   MET A 182    22502  20939  17853   3999  -3369  -1184       C  
ATOM    280  O   MET A 182      38.815  35.915  54.057  1.00165.10           O  
ANISOU  280  O   MET A 182    22553  21411  18764   3834  -3561  -1266       O  
ATOM    281  CB  MET A 182      41.912  35.541  54.139  1.00158.39           C  
ANISOU  281  CB  MET A 182    22062  20541  17575   3492  -2801   -973       C  
ATOM    282  CG  MET A 182      41.566  34.606  55.300  1.00156.90           C  
ANISOU  282  CG  MET A 182    21360  20335  17918   3147  -2898  -1002       C  
ATOM    283  SD  MET A 182      41.708  32.866  54.891  1.00166.98           S  
ANISOU  283  SD  MET A 182    22425  21564  19453   3123  -3214  -1259       S  
ATOM    284  CE  MET A 182      43.436  32.735  54.419  1.00167.41           C  
ANISOU  284  CE  MET A 182    22792  21619  19194   3106  -2875  -1179       C  
ATOM    285  N   GLN A 183      39.652  37.544  52.714  1.00162.65           N  
ANISOU  285  N   GLN A 183    23068  21111  17619   4270  -3261  -1071       N  
ATOM    286  CA  GLN A 183      38.483  38.418  52.826  1.00168.04           C  
ANISOU  286  CA  GLN A 183    23719  21794  18334   4437  -3429  -1072       C  
ATOM    287  C   GLN A 183      37.513  38.207  51.680  1.00180.42           C  
ANISOU  287  C   GLN A 183    25411  23387  19753   4876  -3935  -1340       C  
ATOM    288  O   GLN A 183      36.297  38.092  51.883  1.00171.22           O  
ANISOU  288  O   GLN A 183    23942  22228  18883   4940  -4283  -1512       O  
ATOM    289  CB  GLN A 183      38.873  39.903  52.702  1.00166.28           C  
ANISOU  289  CB  GLN A 183    23901  21532  17743   4554  -3080   -810       C  
ATOM    290  CG  GLN A 183      40.040  40.407  53.518  1.00160.77           C  
ANISOU  290  CG  GLN A 183    23239  20795  17050   4218  -2545   -543       C  
ATOM    291  CD  GLN A 183      39.796  40.287  54.982  1.00158.74           C  
ANISOU  291  CD  GLN A 183    22518  20553  17243   3829  -2443   -493       C  
ATOM    292  OE1 GLN A 183      38.665  40.022  55.436  1.00159.18           O  
ANISOU  292  OE1 GLN A 183    22234  20638  17608   3810  -2722   -620       O  
ATOM    293  NE2 GLN A 183      40.861  40.486  55.749  1.00160.67           N  
ANISOU  293  NE2 GLN A 183    22737  20777  17532   3519  -2036   -312       N  
ATOM    294  N   LYS A 184      38.062  38.187  50.467  1.00205.18           N  
ANISOU  294  N   LYS A 184    28997  26540  22419   5192  -3970  -1383       N  
ATOM    295  CA  LYS A 184      37.290  38.111  49.211  1.00226.30           C  
ANISOU  295  CA  LYS A 184    31913  29255  24814   5687  -4442  -1629       C  
ATOM    296  C   LYS A 184      36.403  36.848  49.222  1.00235.63           C  
ANISOU  296  C   LYS A 184    32639  30452  26436   5671  -4959  -2001       C  
ATOM    297  O   LYS A 184      35.388  36.836  49.922  1.00232.05           O  
ANISOU  297  O   LYS A 184    31770  29980  26418   5552  -5152  -2083       O  
ATOM    298  CB  LYS A 184      38.260  38.231  47.991  1.00234.64           C  
ANISOU  298  CB  LYS A 184    33556  30339  25256   5988  -4293  -1576       C  
ATOM    299  CG  LYS A 184      37.717  38.053  46.566  1.00238.66           C  
ANISOU  299  CG  LYS A 184    34411  30914  25356   6539  -4752  -1832       C  
ATOM    300  CD  LYS A 184      38.858  37.871  45.560  1.00239.48           C  
ANISOU  300  CD  LYS A 184    35007  31057  24927   6732  -4528  -1787       C  
ATOM    301  CE  LYS A 184      38.472  36.977  44.394  1.00243.55           C  
ANISOU  301  CE  LYS A 184    35654  31657  25224   7134  -5042  -2170       C  
ATOM    302  NZ  LYS A 184      37.354  37.519  43.566  1.00248.56           N  
ANISOU  302  NZ  LYS A 184    36535  32337  25569   7648  -5508  -2316       N  
ATOM    303  N   ARG A 185      36.805  35.785  48.511  1.00244.25           N  
ANISOU  303  N   ARG A 185    33781  31564  27456   5764  -5153  -2225       N  
ATOM    304  CA  ARG A 185      35.884  34.678  48.204  1.00248.19           C  
ANISOU  304  CA  ARG A 185    33935  32058  28305   5865  -5720  -2631       C  
ATOM    305  C   ARG A 185      35.160  34.279  49.481  1.00245.68           C  
ANISOU  305  C   ARG A 185    32986  31677  28683   5465  -5757  -2644       C  
ATOM    306  O   ARG A 185      35.809  34.046  50.514  1.00245.80           O  
ANISOU  306  O   ARG A 185    32782  31654  28955   5033  -5378  -2431       O  
ATOM    307  CB  ARG A 185      36.600  33.485  47.602  1.00249.56           C  
ANISOU  307  CB  ARG A 185    34154  32234  28431   5882  -5822  -2839       C  
ATOM    308  CG  ARG A 185      37.103  33.696  46.192  1.00251.84           C  
ANISOU  308  CG  ARG A 185    35040  32604  28042   6348  -5887  -2918       C  
ATOM    309  CD  ARG A 185      37.387  32.355  45.539  1.00255.48           C  
ANISOU  309  CD  ARG A 185    35439  33067  28562   6430  -6176  -3265       C  
ATOM    310  NE  ARG A 185      38.510  32.429  44.610  1.00256.45           N  
ANISOU  310  NE  ARG A 185    36096  33260  28082   6657  -5930  -3204       N  
ATOM    311  CZ  ARG A 185      39.015  31.377  43.969  1.00258.91           C  
ANISOU  311  CZ  ARG A 185    36451  33588  28333   6751  -6078  -3470       C  
ATOM    312  NH1 ARG A 185      38.492  30.155  44.123  1.00259.25           N  
ANISOU  312  NH1 ARG A 185    36044  33563  28896   6643  -6497  -3823       N  
ATOM    313  NH2 ARG A 185      40.049  31.546  43.153  1.00261.25           N  
ANISOU  313  NH2 ARG A 185    37243  33957  28060   6958  -5793  -3388       N  
ATOM    314  N   GLU A 186      33.819  34.244  49.409  1.00238.51           N  
ANISOU  314  N   GLU A 186    31797  30759  28066   5623  -6200  -2889       N  
ATOM    315  CA  GLU A 186      32.985  34.295  50.607  1.00222.21           C  
ANISOU  315  CA  GLU A 186    29202  28647  26578   5306  -6165  -2840       C  
ATOM    316  C   GLU A 186      33.354  33.222  51.604  1.00211.73           C  
ANISOU  316  C   GLU A 186    27435  27248  25763   4822  -5986  -2797       C  
ATOM    317  O   GLU A 186      32.733  32.148  51.696  1.00212.63           O  
ANISOU  317  O   GLU A 186    27127  27288  26372   4726  -6305  -3061       O  
ATOM    318  CB  GLU A 186      31.472  34.335  50.304  1.00223.60           C  
ANISOU  318  CB  GLU A 186    29105  28817  27036   5564  -6693  -3156       C  
ATOM    319  CG  GLU A 186      30.918  35.756  50.185  1.00223.36           C  
ANISOU  319  CG  GLU A 186    29312  28834  26719   5835  -6672  -3027       C  
ATOM    320  CD  GLU A 186      31.440  36.700  51.265  1.00218.00           C  
ANISOU  320  CD  GLU A 186    28676  28155  25999   5527  -6092  -2611       C  
ATOM    321  OE1 GLU A 186      31.658  36.257  52.413  1.00213.70           O  
ANISOU  321  OE1 GLU A 186    27756  27579  25860   5073  -5808  -2482       O  
ATOM    322  OE2 GLU A 186      31.661  37.889  50.957  1.00219.88           O  
ANISOU  322  OE2 GLU A 186    29339  28416  25786   5748  -5918  -2411       O  
ATOM    323  N   SER A 187      34.412  33.555  52.337  1.00198.03           N  
ANISOU  323  N   SER A 187    25822  25523  23896   4530  -5465  -2453       N  
ATOM    324  CA  SER A 187      35.053  32.665  53.275  1.00184.71           C  
ANISOU  324  CA  SER A 187    23837  23779  22564   4093  -5219  -2339       C  
ATOM    325  C   SER A 187      34.294  32.791  54.575  1.00184.04           C  
ANISOU  325  C   SER A 187    23291  23670  22963   3777  -5097  -2220       C  
ATOM    326  O   SER A 187      33.327  33.548  54.678  1.00185.80           O  
ANISOU  326  O   SER A 187    23429  23921  23242   3905  -5201  -2249       O  
ATOM    327  CB  SER A 187      36.520  33.087  53.446  1.00173.17           C  
ANISOU  327  CB  SER A 187    22728  22351  20715   3962  -4733  -2040       C  
ATOM    328  OG  SER A 187      36.626  34.472  53.735  1.00169.71           O  
ANISOU  328  OG  SER A 187    22530  21964  19985   3999  -4428  -1787       O  
ATOM    329  N   GLU A 188      34.798  32.067  55.591  1.00181.60           N  
ANISOU  329  N   GLU A 188    22706  23312  22981   3370  -4847  -2068       N  
ATOM    330  CA  GLU A 188      34.370  32.221  56.978  1.00180.90           C  
ANISOU  330  CA  GLU A 188    22248  23220  23266   3030  -4599  -1873       C  
ATOM    331  C   GLU A 188      35.487  32.856  57.830  1.00169.47           C  
ANISOU  331  C   GLU A 188    20990  21831  21567   2793  -4085  -1519       C  
ATOM    332  O   GLU A 188      35.289  33.191  58.966  1.00164.18           O  
ANISOU  332  O   GLU A 188    20112  21190  21079   2548  -3833  -1332       O  
ATOM    333  CB  GLU A 188      33.849  30.890  57.568  1.00187.69           C  
ANISOU  333  CB  GLU A 188    22595  23966  24751   2760  -4743  -1979       C  
ATOM    334  CG  GLU A 188      34.655  29.645  57.245  1.00190.27           C  
ANISOU  334  CG  GLU A 188    22924  24199  25171   2671  -4825  -2060       C  
ATOM    335  CD  GLU A 188      34.112  28.807  56.078  1.00195.67           C  
ANISOU  335  CD  GLU A 188    23545  24797  26002   2932  -5341  -2464       C  
ATOM    336  OE1 GLU A 188      34.692  28.885  54.975  1.00196.90           O  
ANISOU  336  OE1 GLU A 188    24089  24994  25729   3224  -5476  -2598       O  
ATOM    337  OE2 GLU A 188      33.122  28.052  56.278  1.00197.82           O  
ANISOU  337  OE2 GLU A 188    23375  24956  26829   2844  -5601  -2654       O  
ATOM    338  N   PHE A 189      36.645  33.071  57.223  1.00161.99           N  
ANISOU  338  N   PHE A 189    20451  20906  20190   2894  -3939  -1450       N  
ATOM    339  CA  PHE A 189      37.741  33.771  57.798  1.00156.40           C  
ANISOU  339  CA  PHE A 189    19962  20245  19217   2732  -3495  -1168       C  
ATOM    340  C   PHE A 189      37.726  35.216  57.270  1.00153.80           C  
ANISOU  340  C   PHE A 189    20020  19967  18450   2997  -3385  -1092       C  
ATOM    341  O   PHE A 189      38.702  35.973  57.402  1.00155.33           O  
ANISOU  341  O   PHE A 189    20493  20179  18342   2948  -3034   -892       O  
ATOM    342  CB  PHE A 189      39.050  33.095  57.412  1.00155.34           C  
ANISOU  342  CB  PHE A 189    20013  20083  18923   2680  -3388  -1152       C  
ATOM    343  CG  PHE A 189      39.116  31.644  57.796  1.00154.55           C  
ANISOU  343  CG  PHE A 189    19575  19904  19240   2461  -3523  -1235       C  
ATOM    344  CD1 PHE A 189      39.608  31.255  59.046  1.00150.72           C  
ANISOU  344  CD1 PHE A 189    18858  19406  19002   2098  -3265  -1028       C  
ATOM    345  CD2 PHE A 189      38.682  30.651  56.911  1.00157.86           C  
ANISOU  345  CD2 PHE A 189    19913  20252  19812   2629  -3923  -1526       C  
ATOM    346  CE1 PHE A 189      39.675  29.928  59.385  1.00149.77           C  
ANISOU  346  CE1 PHE A 189    18452  19189  19265   1910  -3383  -1078       C  
ATOM    347  CE2 PHE A 189      38.751  29.318  57.256  1.00155.62           C  
ANISOU  347  CE2 PHE A 189    19319  19861  19946   2425  -4043  -1601       C  
ATOM    348  CZ  PHE A 189      39.253  28.953  58.491  1.00151.07           C  
ANISOU  348  CZ  PHE A 189    18531  19259  19610   2064  -3764  -1361       C  
ATOM    349  N   LYS A 190      36.606  35.624  56.693  1.00151.61           N  
ANISOU  349  N   LYS A 190    19747  19696  18162   3278  -3685  -1253       N  
ATOM    350  CA  LYS A 190      36.420  36.985  56.309  1.00151.78           C  
ANISOU  350  CA  LYS A 190    20093  19744  17831   3527  -3602  -1168       C  
ATOM    351  C   LYS A 190      36.311  37.845  57.571  1.00142.62           C  
ANISOU  351  C   LYS A 190    18780  18607  16799   3283  -3269   -951       C  
ATOM    352  O   LYS A 190      35.660  37.478  58.558  1.00136.28           O  
ANISOU  352  O   LYS A 190    17557  17819  16402   3051  -3275   -957       O  
ATOM    353  CB  LYS A 190      35.142  37.073  55.488  1.00163.50           C  
ANISOU  353  CB  LYS A 190    21548  21228  19346   3884  -4061  -1421       C  
ATOM    354  CG  LYS A 190      34.840  38.426  54.870  1.00174.36           C  
ANISOU  354  CG  LYS A 190    23302  22614  20332   4231  -4064  -1362       C  
ATOM    355  CD  LYS A 190      33.530  38.331  54.108  1.00188.97           C  
ANISOU  355  CD  LYS A 190    25060  24468  22271   4585  -4586  -1653       C  
ATOM    356  CE  LYS A 190      33.296  39.520  53.199  1.00201.28           C  
ANISOU  356  CE  LYS A 190    27081  26028  23367   5021  -4671  -1618       C  
ATOM    357  NZ  LYS A 190      34.065  39.396  51.929  1.00208.30           N  
ANISOU  357  NZ  LYS A 190    28474  26924  23745   5318  -4730  -1641       N  
ATOM    358  N   GLY A 191      36.973  38.995  57.547  1.00141.34           N  
ANISOU  358  N   GLY A 191    18965  18443  16293   3334  -2958   -758       N  
ATOM    359  CA  GLY A 191      37.049  39.844  58.719  1.00138.92           C  
ANISOU  359  CA  GLY A 191    18555  18154  16072   3107  -2623   -567       C  
ATOM    360  C   GLY A 191      38.356  39.640  59.469  1.00133.40           C  
ANISOU  360  C   GLY A 191    17864  17462  15358   2781  -2252   -389       C  
ATOM    361  O   GLY A 191      38.617  40.295  60.475  1.00130.92           O  
ANISOU  361  O   GLY A 191    17483  17169  15090   2577  -1959   -239       O  
ATOM    362  N   VAL A 192      39.183  38.734  58.965  1.00132.32           N  
ANISOU  362  N   VAL A 192    17807  17309  15158   2748  -2281   -427       N  
ATOM    363  CA  VAL A 192      40.485  38.502  59.552  1.00134.92           C  
ANISOU  363  CA  VAL A 192    18153  17640  15470   2475  -1963   -284       C  
ATOM    364  C   VAL A 192      41.353  39.765  59.352  1.00137.83           C  
ANISOU  364  C   VAL A 192    18894  17972  15503   2532  -1620   -125       C  
ATOM    365  O   VAL A 192      41.194  40.480  58.372  1.00141.03           O  
ANISOU  365  O   VAL A 192    19630  18334  15620   2827  -1656   -133       O  
ATOM    366  CB  VAL A 192      41.150  37.245  58.961  1.00138.17           C  
ANISOU  366  CB  VAL A 192    18567  18031  15900   2462  -2090   -385       C  
ATOM    367  CG1 VAL A 192      41.873  37.543  57.663  1.00141.46           C  
ANISOU  367  CG1 VAL A 192    19420  18415  15913   2726  -2046   -411       C  
ATOM    368  CG2 VAL A 192      42.076  36.614  59.956  1.00136.64           C  
ANISOU  368  CG2 VAL A 192    18174  17847  15894   2118  -1877   -277       C  
ATOM    369  N   GLU A 193      42.230  40.050  60.303  1.00142.34           N  
ANISOU  369  N   GLU A 193    19403  18550  16127   2257  -1294     17       N  
ATOM    370  CA  GLU A 193      43.191  41.123  60.148  1.00145.24           C  
ANISOU  370  CA  GLU A 193    20079  18856  16248   2266   -950    150       C  
ATOM    371  C   GLU A 193      44.617  40.694  60.354  1.00141.72           C  
ANISOU  371  C   GLU A 193    19648  18398  15800   2058   -711    206       C  
ATOM    372  O   GLU A 193      44.889  39.621  60.879  1.00136.51           O  
ANISOU  372  O   GLU A 193    18733  17787  15347   1867   -789    167       O  
ATOM    373  CB  GLU A 193      42.819  42.318  61.000  1.00151.38           C  
ANISOU  373  CB  GLU A 193    20820  19627  17071   2198   -773    242       C  
ATOM    374  CG  GLU A 193      41.519  42.959  60.542  1.00162.12           C  
ANISOU  374  CG  GLU A 193    22250  20971  18377   2474   -984    188       C  
ATOM    375  CD  GLU A 193      41.004  43.962  61.570  1.00173.55           C  
ANISOU  375  CD  GLU A 193    23569  22427  19946   2381   -843    244       C  
ATOM    376  OE1 GLU A 193      41.814  44.850  61.910  1.00182.70           O  
ANISOU  376  OE1 GLU A 193    24879  23521  21016   2283   -527    355       O  
ATOM    377  OE2 GLU A 193      39.822  43.882  62.046  1.00182.35           O  
ANISOU  377  OE2 GLU A 193    24422  23604  21257   2403  -1034    166       O  
ATOM    378  N   GLN A 194      45.536  41.523  59.916  1.00143.99           N  
ANISOU  378  N   GLN A 194    20231  18606  15870   2100   -415    298       N  
ATOM    379  CA  GLN A 194      46.958  41.183  59.868  1.00147.46           C  
ANISOU  379  CA  GLN A 194    20717  19017  16291   1950   -175    329       C  
ATOM    380  C   GLN A 194      47.712  41.766  61.067  1.00146.57           C  
ANISOU  380  C   GLN A 194    20459  18896  16332   1661    112    416       C  
ATOM    381  O   GLN A 194      47.354  42.849  61.558  1.00151.08           O  
ANISOU  381  O   GLN A 194    21060  19437  16904   1647    232    479       O  
ATOM    382  CB  GLN A 194      47.536  41.765  58.590  1.00150.95           C  
ANISOU  382  CB  GLN A 194    21579  19364  16411   2181      7    375       C  
ATOM    383  CG  GLN A 194      48.986  41.392  58.311  1.00152.75           C  
ANISOU  383  CG  GLN A 194    21872  19556  16609   2071    266    386       C  
ATOM    384  CD  GLN A 194      49.488  41.930  57.003  1.00159.16           C  
ANISOU  384  CD  GLN A 194    23108  20278  17086   2315    476    444       C  
ATOM    385  OE1 GLN A 194      48.723  42.449  56.206  1.00169.53           O  
ANISOU  385  OE1 GLN A 194    24695  21564  18154   2602    375    471       O  
ATOM    386  NE2 GLN A 194      50.786  41.834  56.779  1.00160.11           N  
ANISOU  386  NE2 GLN A 194    23292  20350  17192   2213    781    469       N  
ATOM    387  N   LEU A 195      48.742  41.061  61.513  1.00143.95           N  
ANISOU  387  N   LEU A 195    19972  18588  16132   1452    203    401       N  
ATOM    388  CA  LEU A 195      49.536  41.532  62.639  1.00142.76           C  
ANISOU  388  CA  LEU A 195    19673  18439  16128   1193    438    449       C  
ATOM    389  C   LEU A 195      50.931  40.905  62.504  1.00136.83           C  
ANISOU  389  C   LEU A 195    18891  17665  15431   1071    580    420       C  
ATOM    390  O   LEU A 195      51.108  39.729  62.772  1.00129.41           O  
ANISOU  390  O   LEU A 195    17753  16790  14625    985    409    366       O  
ATOM    391  CB  LEU A 195      48.854  41.122  63.930  1.00147.59           C  
ANISOU  391  CB  LEU A 195    19962  19168  16946   1027    271    444       C  
ATOM    392  CG  LEU A 195      49.227  41.936  65.171  1.00153.26           C  
ANISOU  392  CG  LEU A 195    20561  19910  17759    828    467    481       C  
ATOM    393  CD1 LEU A 195      48.537  41.333  66.392  1.00157.30           C  
ANISOU  393  CD1 LEU A 195    20771  20560  18435    689    297    486       C  
ATOM    394  CD2 LEU A 195      50.731  42.059  65.391  1.00152.18           C  
ANISOU  394  CD2 LEU A 195    20423  19723  17673    669    704    471       C  
ATOM    395  N   ASN A 196      51.893  41.697  62.089  1.00135.93           N  
ANISOU  395  N   ASN A 196    18964  17446  15238   1067    897    455       N  
ATOM    396  CA  ASN A 196      53.252  41.207  61.922  1.00134.20           C  
ANISOU  396  CA  ASN A 196    18702  17194  15091    959   1065    413       C  
ATOM    397  C   ASN A 196      53.954  41.043  63.248  1.00132.44           C  
ANISOU  397  C   ASN A 196    18177  17022  15122    685   1101    382       C  
ATOM    398  O   ASN A 196      54.023  41.990  64.031  1.00134.47           O  
ANISOU  398  O   ASN A 196    18386  17258  15447    571   1239    406       O  
ATOM    399  CB  ASN A 196      54.017  42.142  61.013  1.00134.68           C  
ANISOU  399  CB  ASN A 196    19055  17111  15006   1045   1426    467       C  
ATOM    400  CG  ASN A 196      53.299  42.370  59.715  1.00134.80           C  
ANISOU  400  CG  ASN A 196    19414  17084  14717   1351   1385    515       C  
ATOM    401  OD1 ASN A 196      52.811  41.415  59.094  1.00133.91           O  
ANISOU  401  OD1 ASN A 196    19331  17045  14504   1508   1121    446       O  
ATOM    402  ND2 ASN A 196      53.178  43.631  59.320  1.00137.75           N  
ANISOU  402  ND2 ASN A 196    20053  17335  14949   1453   1619    626       N  
ATOM    403  N   THR A 197      54.495  39.848  63.500  1.00131.06           N  
ANISOU  403  N   THR A 197    17804  16908  15083    594    966    317       N  
ATOM    404  CA  THR A 197      55.203  39.536  64.756  1.00133.50           C  
ANISOU  404  CA  THR A 197    17830  17277  15616    363    952    284       C  
ATOM    405  C   THR A 197      56.587  38.915  64.497  1.00142.64           C  
ANISOU  405  C   THR A 197    18908  18394  16893    294   1058    202       C  
ATOM    406  O   THR A 197      56.925  38.605  63.371  1.00143.40           O  
ANISOU  406  O   THR A 197    19155  18430  16898    422   1133    170       O  
ATOM    407  CB  THR A 197      54.376  38.519  65.561  1.00128.97           C  
ANISOU  407  CB  THR A 197    17042  16825  15135    315    626    303       C  
ATOM    408  OG1 THR A 197      54.293  37.280  64.840  1.00129.90           O  
ANISOU  408  OG1 THR A 197    17150  16939  15268    408    433    262       O  
ATOM    409  CG2 THR A 197      52.973  39.026  65.785  1.00124.73           C  
ANISOU  409  CG2 THR A 197    16545  16332  14512    387    520    366       C  
ATOM    410  N   GLY A 198      57.355  38.727  65.553  1.00149.13           N  
ANISOU  410  N   GLY A 198    19493  19258  17912    111   1050    157       N  
ATOM    411  CA  GLY A 198      58.595  37.959  65.484  1.00150.79           C  
ANISOU  411  CA  GLY A 198    19562  19446  18283     45   1079     63       C  
ATOM    412  C   GLY A 198      59.853  38.796  65.217  1.00155.05           C  
ANISOU  412  C   GLY A 198    20119  19877  18914    -26   1427    -10       C  
ATOM    413  O   GLY A 198      59.773  40.017  65.104  1.00157.04           O  
ANISOU  413  O   GLY A 198    20504  20052  19110    -33   1658     24       O  
ATOM    414  N   SER A 199      60.981  38.122  65.041  1.00155.41           N  
ANISOU  414  N   SER A 199    20030  19897  19121    -68   1472   -113       N  
ATOM    415  CA  SER A 199      62.289  38.793  65.042  1.00156.16           C  
ANISOU  415  CA  SER A 199    20039  19893  19399   -179   1781   -212       C  
ATOM    416  C   SER A 199      62.410  39.863  63.959  1.00149.26           C  
ANISOU  416  C   SER A 199    19430  18876  18405   -106   2168   -164       C  
ATOM    417  O   SER A 199      62.990  40.927  64.192  1.00145.37           O  
ANISOU  417  O   SER A 199    18910  18279  18043   -219   2438   -191       O  
ATOM    418  CB  SER A 199      63.413  37.771  64.889  1.00164.92           C  
ANISOU  418  CB  SER A 199    20956  20999  20705   -204   1753   -341       C  
ATOM    419  OG  SER A 199      63.405  36.855  65.975  1.00169.30           O  
ANISOU  419  OG  SER A 199    21271  21665  21389   -273   1409   -369       O  
ATOM    420  N   TYR A 200      61.880  39.581  62.770  1.00143.23           N  
ANISOU  420  N   TYR A 200    18928  18096  17397     88   2195    -95       N  
ATOM    421  CA  TYR A 200      62.012  40.555  61.696  1.00141.22           C  
ANISOU  421  CA  TYR A 200    18966  17704  16987    187   2574    -20       C  
ATOM    422  C   TYR A 200      61.311  41.855  62.027  1.00140.97           C  
ANISOU  422  C   TYR A 200    19072  17609  16880    168   2670     89       C  
ATOM    423  O   TYR A 200      61.858  42.923  61.742  1.00149.75           O  
ANISOU  423  O   TYR A 200    20284  18564  18050    120   3039    123       O  
ATOM    424  CB  TYR A 200      61.540  40.055  60.325  1.00141.34           C  
ANISOU  424  CB  TYR A 200    19278  17727  16696    442   2571     28       C  
ATOM    425  CG  TYR A 200      61.539  41.183  59.299  1.00142.26           C  
ANISOU  425  CG  TYR A 200    19748  17705  16599    568   2960    151       C  
ATOM    426  CD1 TYR A 200      62.690  41.516  58.591  1.00143.12           C  
ANISOU  426  CD1 TYR A 200    19922  17690  16766    550   3396    139       C  
ATOM    427  CD2 TYR A 200      60.395  41.973  59.086  1.00141.01           C  
ANISOU  427  CD2 TYR A 200    19852  17523  16199    702   2912    291       C  
ATOM    428  CE1 TYR A 200      62.700  42.580  57.677  1.00142.95           C  
ANISOU  428  CE1 TYR A 200    20245  17520  16547    663   3790    289       C  
ATOM    429  CE2 TYR A 200      60.401  43.033  58.179  1.00141.60           C  
ANISOU  429  CE2 TYR A 200    20273  17452  16075    829   3268    430       C  
ATOM    430  CZ  TYR A 200      61.564  43.339  57.477  1.00141.78           C  
ANISOU  430  CZ  TYR A 200    20380  17345  16143    807   3720    442       C  
ATOM    431  OH  TYR A 200      61.592  44.392  56.585  1.00138.35           O  
ANISOU  431  OH  TYR A 200    20307  16746  15512    932   4109    613       O  
ATOM    432  N   TYR A 201      60.134  41.782  62.641  1.00136.06           N  
ANISOU  432  N   TYR A 201    18442  17092  16163    200   2359    139       N  
ATOM    433  CA  TYR A 201      59.362  42.985  62.946  1.00138.20           C  
ANISOU  433  CA  TYR A 201    18843  17308  16356    208   2423    231       C  
ATOM    434  C   TYR A 201      59.738  43.619  64.279  1.00141.60           C  
ANISOU  434  C   TYR A 201    19027  17736  17035    -11   2441    156       C  
ATOM    435  O   TYR A 201      59.196  44.668  64.632  1.00148.65           O  
ANISOU  435  O   TYR A 201    20000  18573  17905    -20   2507    203       O  
ATOM    436  CB  TYR A 201      57.902  42.634  62.935  1.00135.86           C  
ANISOU  436  CB  TYR A 201    18640  17125  15854    359   2097    300       C  
ATOM    437  CG  TYR A 201      57.516  42.208  61.569  1.00136.66           C  
ANISOU  437  CG  TYR A 201    19013  17212  15699    602   2080    348       C  
ATOM    438  CD1 TYR A 201      57.237  43.155  60.594  1.00138.88           C  
ANISOU  438  CD1 TYR A 201    19639  17371  15757    776   2308    458       C  
ATOM    439  CD2 TYR A 201      57.482  40.862  61.220  1.00134.30           C  
ANISOU  439  CD2 TYR A 201    18641  17010  15374    672   1841    278       C  
ATOM    440  CE1 TYR A 201      56.892  42.781  59.309  1.00136.18           C  
ANISOU  440  CE1 TYR A 201    19579  17029  15131   1034   2280    493       C  
ATOM    441  CE2 TYR A 201      57.139  40.471  59.934  1.00135.51           C  
ANISOU  441  CE2 TYR A 201    19053  17156  15275    917   1807    287       C  
ATOM    442  CZ  TYR A 201      56.847  41.453  58.986  1.00134.08           C  
ANISOU  442  CZ  TYR A 201    19230  16878  14837   1104   2026    393       C  
ATOM    443  OH  TYR A 201      56.501  41.129  57.713  1.00132.67           O  
ANISOU  443  OH  TYR A 201    19340  16704  14362   1378   1984    399       O  
ATOM    444  N   GLU A 202      60.673  42.995  64.986  1.00140.33           N  
ANISOU  444  N   GLU A 202    18577  17633  17108   -167   2373     27       N  
ATOM    445  CA  GLU A 202      61.191  43.536  66.226  1.00141.04           C  
ANISOU  445  CA  GLU A 202    18425  17730  17434   -359   2373    -82       C  
ATOM    446  C   GLU A 202      62.592  44.065  65.999  1.00136.33           C  
ANISOU  446  C   GLU A 202    17731  16969  17096   -484   2709   -193       C  
ATOM    447  O   GLU A 202      63.178  44.687  66.884  1.00132.47           O  
ANISOU  447  O   GLU A 202    17045  16441  16843   -642   2757   -320       O  
ATOM    448  CB  GLU A 202      61.171  42.441  67.271  1.00145.97           C  
ANISOU  448  CB  GLU A 202    18790  18544  18126   -424   2014   -148       C  
ATOM    449  CG  GLU A 202      59.738  42.048  67.631  1.00152.10           C  
ANISOU  449  CG  GLU A 202    19631  19463  18695   -332   1724    -35       C  
ATOM    450  CD  GLU A 202      59.578  40.660  68.216  1.00157.76           C  
ANISOU  450  CD  GLU A 202    20171  20337  19432   -342   1392    -33       C  
ATOM    451  OE1 GLU A 202      60.475  39.813  68.006  1.00165.94           O  
ANISOU  451  OE1 GLU A 202    21090  21366  20594   -366   1362   -102       O  
ATOM    452  OE2 GLU A 202      58.526  40.413  68.869  1.00158.24           O  
ANISOU  452  OE2 GLU A 202    20210  20518  19395   -322   1174     43       O  
ATOM    453  N   HIS A 203      63.116  43.841  64.795  1.00137.22           N  
ANISOU  453  N   HIS A 203    17981  16984  17171   -405   2949   -157       N  
ATOM    454  CA  HIS A 203      64.469  44.223  64.402  1.00143.75           C  
ANISOU  454  CA  HIS A 203    18712  17646  18258   -513   3317   -251       C  
ATOM    455  C   HIS A 203      65.503  43.460  65.216  1.00141.20           C  
ANISOU  455  C   HIS A 203    18008  17404  18236   -658   3161   -453       C  
ATOM    456  O   HIS A 203      66.525  44.013  65.619  1.00147.10           O  
ANISOU  456  O   HIS A 203    18538  18043  19308   -819   3345   -601       O  
ATOM    457  CB  HIS A 203      64.657  45.743  64.488  1.00151.03           C  
ANISOU  457  CB  HIS A 203    19702  18360  19321   -610   3649   -236       C  
ATOM    458  CG  HIS A 203      63.436  46.567  64.164  1.00152.42           C  
ANISOU  458  CG  HIS A 203    20203  18484  19223   -476   3674    -53       C  
ATOM    459  ND1 HIS A 203      63.015  46.814  62.872  1.00157.80           N  
ANISOU  459  ND1 HIS A 203    21251  19068  19635   -287   3891    131       N  
ATOM    460  CD2 HIS A 203      62.594  47.253  64.975  1.00150.11           C  
ANISOU  460  CD2 HIS A 203    19921  18216  18896   -494   3518    -40       C  
ATOM    461  CE1 HIS A 203      61.942  47.584  62.904  1.00158.38           C  
ANISOU  461  CE1 HIS A 203    21541  19108  19529   -188   3840    253       C  
ATOM    462  NE2 HIS A 203      61.668  47.866  64.165  1.00154.43           N  
ANISOU  462  NE2 HIS A 203    20821  18677  19178   -317   3625    148       N  
ATOM    463  N   VAL A 204      65.228  42.179  65.463  1.00134.26           N  
ANISOU  463  N   VAL A 204    17040  16703  17268   -592   2806   -465       N  
ATOM    464  CA  VAL A 204      66.194  41.317  66.120  1.00131.75           C  
ANISOU  464  CA  VAL A 204    16390  16458  17209   -686   2633   -637       C  
ATOM    465  C   VAL A 204      66.482  40.084  65.269  1.00129.24           C  
ANISOU  465  C   VAL A 204    16089  16176  16840   -569   2584   -642       C  
ATOM    466  O   VAL A 204      67.037  39.072  65.722  1.00128.78           O  
ANISOU  466  O   VAL A 204    15793  16198  16937   -592   2355   -752       O  
ATOM    467  CB  VAL A 204      65.759  40.932  67.529  1.00131.95           C  
ANISOU  467  CB  VAL A 204    16237  16653  17244   -740   2224   -671       C  
ATOM    468  CG1 VAL A 204      65.403  42.208  68.296  1.00136.03           C  
ANISOU  468  CG1 VAL A 204    16768  17137  17779   -830   2286   -683       C  
ATOM    469  CG2 VAL A 204      64.622  39.916  67.499  1.00127.49           C  
ANISOU  469  CG2 VAL A 204    15791  16233  16413   -608   1902   -526       C  
ATOM    470  N   LYS A 205      66.058  40.147  64.003  1.00130.09           N  
ANISOU  470  N   LYS A 205    16496  16224  16706   -419   2784   -524       N  
ATOM    471  CA  LYS A 205      66.402  39.081  63.058  1.00133.40           C  
ANISOU  471  CA  LYS A 205    16954  16662  17068   -290   2789   -559       C  
ATOM    472  C   LYS A 205      67.888  39.169  62.794  1.00131.28           C  
ANISOU  472  C   LYS A 205    16485  16286  17107   -386   3107   -715       C  
ATOM    473  O   LYS A 205      68.464  40.256  62.729  1.00127.91           O  
ANISOU  473  O   LYS A 205    16044  15719  16837   -496   3466   -732       O  
ATOM    474  CB  LYS A 205      65.576  39.205  61.773  1.00142.33           C  
ANISOU  474  CB  LYS A 205    18478  17766  17831    -80   2917   -412       C  
ATOM    475  CG  LYS A 205      65.673  38.010  60.819  1.00148.85           C  
ANISOU  475  CG  LYS A 205    19378  18642  18534     92   2838   -461       C  
ATOM    476  CD  LYS A 205      64.939  36.781  61.341  1.00151.72           C  
ANISOU  476  CD  LYS A 205    19635  19142  18869    141   2339   -479       C  
ATOM    477  CE  LYS A 205      65.422  35.512  60.680  1.00157.25           C  
ANISOU  477  CE  LYS A 205    20280  19865  19602    253   2249   -601       C  
ATOM    478  NZ  LYS A 205      66.772  35.066  61.112  1.00158.80           N  
ANISOU  478  NZ  LYS A 205    20150  20034  20149    129   2311   -765       N  
ATOM    479  N   ILE A 206      68.496  38.001  62.626  1.00133.51           N  
ANISOU  479  N   ILE A 206    16602  16622  17504   -343   2977   -835       N  
ATOM    480  CA  ILE A 206      69.970  37.853  62.604  1.00141.90           C  
ANISOU  480  CA  ILE A 206    17372  17610  18932   -441   3190  -1031       C  
ATOM    481  C   ILE A 206      70.380  37.189  61.298  1.00145.49           C  
ANISOU  481  C   ILE A 206    17947  18038  19294   -287   3406  -1064       C  
ATOM    482  O   ILE A 206      69.564  36.481  60.686  1.00147.32           O  
ANISOU  482  O   ILE A 206    18409  18346  19220   -104   3227   -984       O  
ATOM    483  CB  ILE A 206      70.383  36.924  63.782  1.00141.03           C  
ANISOU  483  CB  ILE A 206    16905  17604  19076   -514   2765  -1176       C  
ATOM    484  CG1 ILE A 206      69.497  35.657  63.861  1.00140.71           C  
ANISOU  484  CG1 ILE A 206    16944  17693  18824   -374   2331  -1099       C  
ATOM    485  CG2 ILE A 206      70.241  37.649  65.089  1.00138.75           C  
ANISOU  485  CG2 ILE A 206    16470  17344  18905   -666   2605  -1190       C  
ATOM    486  CD1 ILE A 206      70.094  34.486  64.577  1.00140.49           C  
ANISOU  486  CD1 ILE A 206    16614  17728  19037   -386   1991  -1230       C  
ATOM    487  N   SER A 207      71.642  37.405  60.884  1.00148.84           N  
ANISOU  487  N   SER A 207    18201  18353  19995   -355   3787  -1202       N  
ATOM    488  CA  SER A 207      72.122  36.834  59.622  1.00155.00           C  
ANISOU  488  CA  SER A 207    19094  19112  20685   -202   4054  -1248       C  
ATOM    489  C   SER A 207      71.393  37.237  58.326  1.00158.81           C  
ANISOU  489  C   SER A 207    20054  19569  20715    -10   4331  -1060       C  
ATOM    490  O   SER A 207      71.987  37.900  57.453  1.00174.35           O  
ANISOU  490  O   SER A 207    22151  21420  22672      2   4855  -1027       O  
ATOM    491  CB  SER A 207      72.199  35.302  59.745  1.00155.15           C  
ANISOU  491  CB  SER A 207    18954  19246  20749    -97   3648  -1380       C  
ATOM    492  OG  SER A 207      72.589  34.913  61.055  1.00154.97           O  
ANISOU  492  OG  SER A 207    18558  19265  21055   -237   3295  -1500       O  
ATOM    493  N   ALA A 208      70.125  36.825  58.195  1.00151.67           N  
ANISOU  493  N   ALA A 208    19409  18772  19447    147   3984   -940       N  
ATOM    494  CA  ALA A 208      69.355  37.042  56.979  1.00153.26           C  
ANISOU  494  CA  ALA A 208    20063  18975  19190    377   4140   -791       C  
ATOM    495  C   ALA A 208      67.862  37.212  57.257  1.00148.88           C  
ANISOU  495  C   ALA A 208    19734  18494  18338    458   3782   -633       C  
ATOM    496  O   ALA A 208      67.358  36.715  58.268  1.00150.09           O  
ANISOU  496  O   ALA A 208    19692  18731  18603    378   3347   -660       O  
ATOM    497  CB  ALA A 208      69.558  35.874  56.032  1.00158.21           C  
ANISOU  497  CB  ALA A 208    20764  19674  19674    587   4092   -911       C  
ATOM    498  N   PRO A 209      67.169  37.928  56.359  1.00145.91           N  
ANISOU  498  N   PRO A 209    19769  18082  17586    625   3979   -465       N  
ATOM    499  CA  PRO A 209      65.713  38.024  56.425  1.00143.18           C  
ANISOU  499  CA  PRO A 209    19653  17809  16940    750   3639   -338       C  
ATOM    500  C   PRO A 209      65.008  36.888  55.709  1.00148.15           C  
ANISOU  500  C   PRO A 209    20436  18555  17299    997   3309   -401       C  
ATOM    501  O   PRO A 209      64.363  37.093  54.685  1.00156.85           O  
ANISOU  501  O   PRO A 209    21912  19668  18014   1239   3363   -320       O  
ATOM    502  CB  PRO A 209      65.468  39.366  55.723  1.00141.76           C  
ANISOU  502  CB  PRO A 209    19840  17510  16510    831   4039   -142       C  
ATOM    503  CG  PRO A 209      66.518  39.411  54.657  1.00144.05           C  
ANISOU  503  CG  PRO A 209    20251  17724  16756    908   4527   -167       C  
ATOM    504  CD  PRO A 209      67.718  38.780  55.272  1.00145.66           C  
ANISOU  504  CD  PRO A 209    20012  17927  17404    705   4555   -370       C  
ATOM    505  N   ASN A 210      65.118  35.692  56.250  1.00148.31           N  
ANISOU  505  N   ASN A 210    20171  18652  17526    947   2952   -550       N  
ATOM    506  CA  ASN A 210      64.580  34.469  55.636  1.00153.54           C  
ANISOU  506  CA  ASN A 210    20912  19400  18027   1157   2619   -658       C  
ATOM    507  C   ASN A 210      63.437  33.855  56.445  1.00157.17           C  
ANISOU  507  C   ASN A 210    21249  19931  18537   1129   2090   -641       C  
ATOM    508  O   ASN A 210      62.962  32.775  56.106  1.00166.90           O  
ANISOU  508  O   ASN A 210    22482  21211  19722   1265   1768   -745       O  
ATOM    509  CB  ASN A 210      65.735  33.470  55.518  1.00154.10           C  
ANISOU  509  CB  ASN A 210    20739  19468  18345   1133   2664   -858       C  
ATOM    510  CG  ASN A 210      66.396  33.171  56.860  1.00154.71           C  
ANISOU  510  CG  ASN A 210    20380  19531  18869    870   2522   -919       C  
ATOM    511  OD1 ASN A 210      66.265  33.928  57.835  1.00154.85           O  
ANISOU  511  OD1 ASN A 210    20284  19534  19017    684   2516   -818       O  
ATOM    512  ND2 ASN A 210      67.112  32.064  56.916  1.00162.12           N  
ANISOU  512  ND2 ASN A 210    21082  20477  20036    873   2394  -1096       N  
ATOM    513  N   GLU A 211      63.019  34.543  57.500  1.00156.75           N  
ANISOU  513  N   GLU A 211    21085  19876  18596    951   2021   -520       N  
ATOM    514  CA  GLU A 211      61.918  34.043  58.350  1.00158.39           C  
ANISOU  514  CA  GLU A 211    21167  20151  18861    907   1571   -481       C  
ATOM    515  C   GLU A 211      60.975  35.188  58.718  1.00149.61           C  
ANISOU  515  C   GLU A 211    20196  19042  17604    881   1593   -316       C  
ATOM    516  O   GLU A 211      61.401  36.219  59.247  1.00145.42           O  
ANISOU  516  O   GLU A 211    19629  18465  17158    734   1845   -244       O  
ATOM    517  CB  GLU A 211      62.448  33.448  59.668  1.00168.73           C  
ANISOU  517  CB  GLU A 211    22090  21480  20538    681   1388   -524       C  
ATOM    518  CG  GLU A 211      63.148  32.090  59.588  1.00180.58           C  
ANISOU  518  CG  GLU A 211    23391  22977  22243    700   1224   -682       C  
ATOM    519  CD  GLU A 211      63.861  31.659  60.889  1.00188.51           C  
ANISOU  519  CD  GLU A 211    24036  23988  23600    492   1090   -712       C  
ATOM    520  OE1 GLU A 211      64.552  30.608  60.872  1.00192.47           O  
ANISOU  520  OE1 GLU A 211    24360  24468  24300    507    973   -841       O  
ATOM    521  OE2 GLU A 211      63.773  32.370  61.930  1.00194.48           O  
ANISOU  521  OE2 GLU A 211    24690  24769  24432    331   1096   -619       O  
ATOM    522  N   PHE A 212      59.699  34.994  58.441  1.00143.02           N  
ANISOU  522  N   PHE A 212    19502  18254  16582   1028   1317   -277       N  
ATOM    523  CA  PHE A 212      58.697  36.026  58.695  1.00136.59           C  
ANISOU  523  CA  PHE A 212    18828  17444  15623   1043   1310   -137       C  
ATOM    524  C   PHE A 212      57.484  35.452  59.408  1.00135.04           C  
ANISOU  524  C   PHE A 212    18482  17322  15502   1020    893   -121       C  
ATOM    525  O   PHE A 212      57.014  34.365  59.076  1.00134.74           O  
ANISOU  525  O   PHE A 212    18400  17314  15478   1121    598   -210       O  
ATOM    526  CB  PHE A 212      58.322  36.692  57.385  1.00134.57           C  
ANISOU  526  CB  PHE A 212    18974  17151  15003   1302   1481    -88       C  
ATOM    527  CG  PHE A 212      59.470  37.405  56.753  1.00135.47           C  
ANISOU  527  CG  PHE A 212    19247  17175  15049   1305   1960    -58       C  
ATOM    528  CD1 PHE A 212      59.715  38.734  57.047  1.00134.59           C  
ANISOU  528  CD1 PHE A 212    19212  16971  14953   1201   2285     72       C  
ATOM    529  CD2 PHE A 212      60.351  36.736  55.928  1.00140.41           C  
ANISOU  529  CD2 PHE A 212    19916  17794  15639   1396   2104   -171       C  
ATOM    530  CE1 PHE A 212      60.792  39.406  56.485  1.00135.97           C  
ANISOU  530  CE1 PHE A 212    19510  17033  15117   1181   2763    108       C  
ATOM    531  CE2 PHE A 212      61.429  37.389  55.367  1.00143.77           C  
ANISOU  531  CE2 PHE A 212    20464  18130  16031   1385   2589   -138       C  
ATOM    532  CZ  PHE A 212      61.659  38.732  55.643  1.00140.48           C  
ANISOU  532  CZ  PHE A 212    20122  17606  15647   1269   2930      9       C  
ATOM    533  N   ASP A 213      56.991  36.146  60.418  1.00133.99           N  
ANISOU  533  N   ASP A 213    18251  17212  15445    882    873    -19       N  
ATOM    534  CA  ASP A 213      55.837  35.676  61.198  1.00136.87           C  
ANISOU  534  CA  ASP A 213    18454  17648  15900    839    531     13       C  
ATOM    535  C   ASP A 213      54.650  36.642  61.032  1.00133.46           C  
ANISOU  535  C   ASP A 213    18203  17225  15281    953    512     99       C  
ATOM    536  O   ASP A 213      54.730  37.810  61.420  1.00139.16           O  
ANISOU  536  O   ASP A 213    18989  17921  15965    888    730    181       O  
ATOM    537  CB  ASP A 213      56.222  35.450  62.669  1.00144.14           C  
ANISOU  537  CB  ASP A 213    19067  18615  17083    588    480     45       C  
ATOM    538  CG  ASP A 213      57.033  34.154  62.886  1.00153.42           C  
ANISOU  538  CG  ASP A 213    20032  19789  18470    516    349    -39       C  
ATOM    539  OD1 ASP A 213      57.450  33.891  64.034  1.00161.94           O  
ANISOU  539  OD1 ASP A 213    20880  20904  19743    340    294    -12       O  
ATOM    540  OD2 ASP A 213      57.237  33.358  61.950  1.00159.82           O  
ANISOU  540  OD2 ASP A 213    20907  20563  19254    647    280   -138       O  
ATOM    541  N   VAL A 214      53.560  36.167  60.430  1.00127.26           N  
ANISOU  541  N   VAL A 214    17493  16463  14397   1134    241     60       N  
ATOM    542  CA  VAL A 214      52.401  37.007  60.252  1.00128.41           C  
ANISOU  542  CA  VAL A 214    17787  16617  14386   1265    182    121       C  
ATOM    543  C   VAL A 214      51.150  36.393  60.819  1.00123.75           C  
ANISOU  543  C   VAL A 214    16986  16088  13944   1246   -161    104       C  
ATOM    544  O   VAL A 214      50.762  35.296  60.416  1.00115.50           O  
ANISOU  544  O   VAL A 214    15863  15048  12973   1323   -431      1       O  
ATOM    545  CB  VAL A 214      52.132  37.456  58.827  1.00136.17           C  
ANISOU  545  CB  VAL A 214    19133  17556  15047   1563    226     99       C  
ATOM    546  CG1 VAL A 214      50.941  38.422  58.810  1.00137.66           C  
ANISOU  546  CG1 VAL A 214    19450  17745  15107   1691    156    171       C  
ATOM    547  CG2 VAL A 214      53.364  38.149  58.273  1.00139.60           C  
ANISOU  547  CG2 VAL A 214    19786  17913  15341   1572    634    147       C  
ATOM    548  N   MET A 215      50.506  37.124  61.726  1.00127.99           N  
ANISOU  548  N   MET A 215    17430  16661  14539   1150   -139    193       N  
ATOM    549  CA  MET A 215      49.251  36.658  62.343  1.00136.21           C  
ANISOU  549  CA  MET A 215    18252  17759  15739   1119   -415    192       C  
ATOM    550  C   MET A 215      48.033  37.119  61.575  1.00133.73           C  
ANISOU  550  C   MET A 215    18088  17438  15283   1361   -573    153       C  
ATOM    551  O   MET A 215      47.818  38.308  61.339  1.00134.73           O  
ANISOU  551  O   MET A 215    18417  17541  15230   1467   -427    208       O  
ATOM    552  CB  MET A 215      49.120  37.127  63.776  1.00150.56           C  
ANISOU  552  CB  MET A 215    19872  19640  17694    903   -317    294       C  
ATOM    553  CG  MET A 215      49.818  36.206  64.747  1.00163.13           C  
ANISOU  553  CG  MET A 215    21217  21269  19496    680   -337    320       C  
ATOM    554  SD  MET A 215      49.825  36.752  66.462  1.00182.39           S  
ANISOU  554  SD  MET A 215    23460  23805  22032    451   -212    431       S  
ATOM    555  CE  MET A 215      48.071  36.899  66.833  1.00175.18           C  
ANISOU  555  CE  MET A 215    22435  22952  21171    503   -373    467       C  
ATOM    556  N   PHE A 216      47.216  36.161  61.188  1.00133.13           N  
ANISOU  556  N   PHE A 216    17902  17368  15312   1456   -891     47       N  
ATOM    557  CA  PHE A 216      45.857  36.437  60.687  1.00136.16           C  
ANISOU  557  CA  PHE A 216    18324  17758  15649   1666  -1124    -19       C  
ATOM    558  C   PHE A 216      44.923  36.213  61.857  1.00134.48           C  
ANISOU  558  C   PHE A 216    17773  17596  15725   1492  -1229     21       C  
ATOM    559  O   PHE A 216      44.530  35.086  62.125  1.00135.18           O  
ANISOU  559  O   PHE A 216    17608  17680  16071   1406  -1438    -34       O  
ATOM    560  CB  PHE A 216      45.531  35.474  59.551  1.00141.03           C  
ANISOU  560  CB  PHE A 216    18995  18345  16243   1877  -1428   -199       C  
ATOM    561  CG  PHE A 216      46.114  35.869  58.224  1.00146.28           C  
ANISOU  561  CG  PHE A 216    20053  18980  16546   2138  -1346   -248       C  
ATOM    562  CD1 PHE A 216      47.359  36.509  58.119  1.00148.02           C  
ANISOU  562  CD1 PHE A 216    20487  19175  16577   2088   -976   -138       C  
ATOM    563  CD2 PHE A 216      45.430  35.578  57.057  1.00150.31           C  
ANISOU  563  CD2 PHE A 216    20719  19485  16906   2446  -1636   -413       C  
ATOM    564  CE1 PHE A 216      47.869  36.870  56.888  1.00150.35           C  
ANISOU  564  CE1 PHE A 216    21154  19439  16533   2332   -859   -161       C  
ATOM    565  CE2 PHE A 216      45.957  35.911  55.819  1.00152.26           C  
ANISOU  565  CE2 PHE A 216    21360  19717  16773   2713  -1550   -448       C  
ATOM    566  CZ  PHE A 216      47.183  36.551  55.739  1.00152.85           C  
ANISOU  566  CZ  PHE A 216    21654  19765  16655   2650  -1140   -307       C  
ATOM    567  N   LYS A 217      44.597  37.291  62.557  1.00135.05           N  
ANISOU  567  N   LYS A 217    17844  17706  15762   1439  -1063    120       N  
ATOM    568  CA  LYS A 217      43.762  37.224  63.757  1.00134.90           C  
ANISOU  568  CA  LYS A 217    17521  17753  15982   1273  -1094    174       C  
ATOM    569  C   LYS A 217      42.301  37.475  63.410  1.00128.38           C  
ANISOU  569  C   LYS A 217    16631  16931  15215   1453  -1316     87       C  
ATOM    570  O   LYS A 217      41.999  38.304  62.570  1.00128.29           O  
ANISOU  570  O   LYS A 217    16861  16888  14992   1692  -1345     43       O  
ATOM    571  CB  LYS A 217      44.201  38.314  64.744  1.00140.27           C  
ANISOU  571  CB  LYS A 217    18230  18479  16588   1132   -793    297       C  
ATOM    572  CG  LYS A 217      43.911  39.753  64.314  1.00144.67           C  
ANISOU  572  CG  LYS A 217    19032  19002  16933   1309   -674    305       C  
ATOM    573  CD  LYS A 217      44.942  40.728  64.865  1.00151.43           C  
ANISOU  573  CD  LYS A 217    20011  19843  17681   1186   -346    392       C  
ATOM    574  CE  LYS A 217      44.845  42.103  64.213  1.00161.25           C  
ANISOU  574  CE  LYS A 217    21552  20998  18716   1377   -209    410       C  
ATOM    575  NZ  LYS A 217      43.720  42.920  64.757  1.00167.79           N  
ANISOU  575  NZ  LYS A 217    22299  21857  19595   1431   -237    409       N  
ATOM    576  N   LEU A 218      41.403  36.770  64.072  1.00127.04           N  
ANISOU  576  N   LEU A 218    16132  16793  15345   1343  -1462     69       N  
ATOM    577  CA  LEU A 218      39.974  36.912  63.810  1.00135.33           C  
ANISOU  577  CA  LEU A 218    17048  17843  16526   1496  -1686    -38       C  
ATOM    578  C   LEU A 218      39.222  37.042  65.089  1.00138.45           C  
ANISOU  578  C   LEU A 218    17140  18311  17152   1314  -1585     42       C  
ATOM    579  O   LEU A 218      39.275  36.146  65.913  1.00140.89           O  
ANISOU  579  O   LEU A 218    17200  18638  17693   1091  -1555    113       O  
ATOM    580  CB  LEU A 218      39.503  35.689  63.044  1.00142.33           C  
ANISOU  580  CB  LEU A 218    17802  18665  17609   1582  -2025   -203       C  
ATOM    581  CG  LEU A 218      38.076  35.712  62.528  1.00153.88           C  
ANISOU  581  CG  LEU A 218    19124  20111  19230   1781  -2327   -376       C  
ATOM    582  CD1 LEU A 218      37.828  36.912  61.617  1.00160.35           C  
ANISOU  582  CD1 LEU A 218    20270  20933  19721   2098  -2373   -434       C  
ATOM    583  CD2 LEU A 218      37.826  34.407  61.787  1.00157.44           C  
ANISOU  583  CD2 LEU A 218    19443  20481  19893   1841  -2662   -563       C  
ATOM    584  N   GLU A 219      38.543  38.159  65.287  1.00143.26           N  
ANISOU  584  N   GLU A 219    17779  18958  17692   1413  -1515     42       N  
ATOM    585  CA  GLU A 219      37.818  38.386  66.554  1.00147.08           C  
ANISOU  585  CA  GLU A 219    17982  19530  18371   1252  -1378    112       C  
ATOM    586  C   GLU A 219      36.634  37.415  66.692  1.00147.80           C  
ANISOU  586  C   GLU A 219    17700  19609  18845   1213  -1590     30       C  
ATOM    587  O   GLU A 219      35.912  37.231  65.767  1.00145.86           O  
ANISOU  587  O   GLU A 219    17427  19303  18689   1409  -1867   -133       O  
ATOM    588  CB  GLU A 219      37.300  39.818  66.615  1.00153.12           C  
ANISOU  588  CB  GLU A 219    18862  20322  18994   1403  -1279     94       C  
ATOM    589  CG  GLU A 219      37.010  40.306  68.022  1.00159.03           C  
ANISOU  589  CG  GLU A 219    19421  21178  19823   1227  -1031    186       C  
ATOM    590  CD  GLU A 219      35.553  40.198  68.479  1.00168.62           C  
ANISOU  590  CD  GLU A 219    20295  22441  21330   1239  -1112    119       C  
ATOM    591  OE1 GLU A 219      34.641  40.391  67.630  1.00185.81           O  
ANISOU  591  OE1 GLU A 219    22446  24563  23588   1467  -1350    -28       O  
ATOM    592  OE2 GLU A 219      35.318  39.952  69.698  1.00164.55           O  
ANISOU  592  OE2 GLU A 219    19538  22023  20958   1034   -928    210       O  
ATOM    593  N   VAL A 220      36.610  36.690  67.779  1.00153.56           N  
ANISOU  593  N   VAL A 220    18170  20383  19793    959  -1463    147       N  
ATOM    594  CA  VAL A 220      35.594  35.679  67.970  1.00167.98           C  
ANISOU  594  CA  VAL A 220    19627  22169  22029    879  -1616     97       C  
ATOM    595  C   VAL A 220      34.868  35.965  69.293  1.00168.08           C  
ANISOU  595  C   VAL A 220    19377  22286  22199    721  -1377    210       C  
ATOM    596  O   VAL A 220      35.315  35.555  70.406  1.00175.51           O  
ANISOU  596  O   VAL A 220    20235  23288  23160    490  -1147    399       O  
ATOM    597  CB  VAL A 220      36.106  34.241  67.877  1.00182.84           C  
ANISOU  597  CB  VAL A 220    21409  23957  24101    734  -1722    129       C  
ATOM    598  CG1 VAL A 220      34.958  33.262  68.128  1.00192.24           C  
ANISOU  598  CG1 VAL A 220    22188  25076  25775    636  -1853     80       C  
ATOM    599  CG2 VAL A 220      36.699  33.998  66.490  1.00184.85           C  
ANISOU  599  CG2 VAL A 220    21916  24120  24196    928  -1967    -24       C  
ATOM    600  N   PRO A 221      33.746  36.687  69.138  1.00169.44           N  
ANISOU  600  N   PRO A 221    19433  22482  22464    872  -1438     86       N  
ATOM    601  CA  PRO A 221      32.949  37.136  70.302  1.00172.41           C  
ANISOU  601  CA  PRO A 221    19567  22969  22972    768  -1200    156       C  
ATOM    602  C   PRO A 221      32.318  36.008  71.147  1.00173.67           C  
ANISOU  602  C   PRO A 221    19332  23122  23531    536  -1115    251       C  
ATOM    603  O   PRO A 221      32.120  34.888  70.662  1.00163.02           O  
ANISOU  603  O   PRO A 221    17819  21647  22472    490  -1320    200       O  
ATOM    604  CB  PRO A 221      31.849  37.960  69.632  1.00174.97           C  
ANISOU  604  CB  PRO A 221    19833  23277  23370   1024  -1377    -47       C  
ATOM    605  CG  PRO A 221      31.589  37.239  68.355  1.00173.32           C  
ANISOU  605  CG  PRO A 221    19605  22933  23312   1176  -1762   -227       C  
ATOM    606  CD  PRO A 221      32.906  36.695  67.908  1.00171.35           C  
ANISOU  606  CD  PRO A 221    19638  22633  22834   1126  -1789   -151       C  
ATOM    607  N   ARG A 222      31.900  36.401  72.340  1.00181.50           N  
ANISOU  607  N   ARG A 222    20173  24240  24546    419   -818    367       N  
ATOM    608  CA  ARG A 222      31.049  35.588  73.218  1.00188.56           C  
ANISOU  608  CA  ARG A 222    20677  25143  25823    225   -669    465       C  
ATOM    609  C   ARG A 222      31.568  34.193  73.500  1.00186.20           C  
ANISOU  609  C   ARG A 222    20299  24753  25693      9   -657    635       C  
ATOM    610  O   ARG A 222      30.835  33.202  73.342  1.00192.02           O  
ANISOU  610  O   ARG A 222    20723  25361  26874    -74   -762    604       O  
ATOM    611  CB  ARG A 222      29.645  35.464  72.610  1.00198.47           C  
ANISOU  611  CB  ARG A 222    21591  26311  27504    336   -879    247       C  
ATOM    612  CG  ARG A 222      28.995  36.755  72.129  1.00202.75           C  
ANISOU  612  CG  ARG A 222    22185  26906  27942    597   -973     44       C  
ATOM    613  CD  ARG A 222      28.353  36.553  70.758  1.00209.51           C  
ANISOU  613  CD  ARG A 222    22961  27621  29020    818  -1406   -226       C  
ATOM    614  NE  ARG A 222      27.033  37.152  70.649  1.00218.24           N  
ANISOU  614  NE  ARG A 222    23792  28743  30384    975  -1487   -421       N  
ATOM    615  CZ  ARG A 222      26.094  36.805  69.758  1.00223.40           C  
ANISOU  615  CZ  ARG A 222    24201  29285  31394   1129  -1843   -675       C  
ATOM    616  NH1 ARG A 222      26.302  35.847  68.851  1.00221.29           N  
ANISOU  616  NH1 ARG A 222    23938  28878  31264   1154  -2166   -781       N  
ATOM    617  NH2 ARG A 222      24.912  37.426  69.776  1.00227.93           N  
ANISOU  617  NH2 ARG A 222    24508  29887  32207   1272  -1894   -851       N  
ATOM    618  N   ILE A 223      32.814  34.109  73.917  1.00177.52           N  
ANISOU  618  N   ILE A 223    19469  23703  24276    -77   -539    803       N  
ATOM    619  CA  ILE A 223      33.418  32.789  74.224  1.00173.87           C  
ANISOU  619  CA  ILE A 223    18964  23147  23950   -268   -532    981       C  
ATOM    620  C   ILE A 223      33.717  32.574  75.696  1.00171.84           C  
ANISOU  620  C   ILE A 223    18689  23013  23588   -461   -190   1266       C  
ATOM    621  O   ILE A 223      33.843  33.526  76.449  1.00168.66           O  
ANISOU  621  O   ILE A 223    18402  22792  22889   -438     32   1316       O  
ATOM    622  CB  ILE A 223      34.725  32.598  73.442  1.00167.30           C  
ANISOU  622  CB  ILE A 223    18445  22247  22872   -206   -718    945       C  
ATOM    623  CG1 ILE A 223      35.614  33.853  73.570  1.00158.67           C  
ANISOU  623  CG1 ILE A 223    17690  21298  21299   -110   -597    940       C  
ATOM    624  CG2 ILE A 223      34.400  32.337  71.987  1.00170.72           C  
ANISOU  624  CG2 ILE A 223    18863  22527  23475    -39  -1077    693       C  
ATOM    625  CD1 ILE A 223      37.040  33.635  73.236  1.00155.48           C  
ANISOU  625  CD1 ILE A 223    17563  20859  20652   -116   -656    975       C  
ATOM    626  N   GLU A 224      33.781  31.302  76.072  1.00171.05           N  
ANISOU  626  N   GLU A 224    18443  22802  23745   -635   -161   1444       N  
ATOM    627  CA  GLU A 224      34.190  30.906  77.421  1.00169.46           C  
ANISOU  627  CA  GLU A 224    18269  22696  23421   -804    135   1750       C  
ATOM    628  C   GLU A 224      35.310  29.859  77.316  1.00157.88           C  
ANISOU  628  C   GLU A 224    16942  21104  21939   -886     13   1883       C  
ATOM    629  O   GLU A 224      35.207  28.884  76.561  1.00152.13           O  
ANISOU  629  O   GLU A 224    16091  20161  21551   -916   -207   1824       O  
ATOM    630  CB  GLU A 224      33.004  30.317  78.184  1.00181.75           C  
ANISOU  630  CB  GLU A 224    19475  24224  25357   -950    361   1899       C  
ATOM    631  CG  GLU A 224      31.730  31.174  78.125  1.00190.69           C  
ANISOU  631  CG  GLU A 224    20381  25436  26635   -865    441   1725       C  
ATOM    632  CD  GLU A 224      30.665  30.738  79.104  1.00201.01           C  
ANISOU  632  CD  GLU A 224    21359  26760  28254  -1019    763   1902       C  
ATOM    633  OE1 GLU A 224      30.569  29.528  79.391  1.00212.81           O  
ANISOU  633  OE1 GLU A 224    22694  28098  30064  -1193    826   2099       O  
ATOM    634  OE2 GLU A 224      29.897  31.606  79.576  1.00203.72           O  
ANISOU  634  OE2 GLU A 224    21593  27261  28550   -965    968   1844       O  
ATOM    635  N   LEU A 225      36.394  30.086  78.044  1.00154.94           N  
ANISOU  635  N   LEU A 225    16824  20864  21181   -906    135   2033       N  
ATOM    636  CA  LEU A 225      37.513  29.165  78.020  1.00157.86           C  
ANISOU  636  CA  LEU A 225    17329  21130  21519   -966     23   2155       C  
ATOM    637  C   LEU A 225      37.483  28.196  79.167  1.00162.03           C  
ANISOU  637  C   LEU A 225    17773  21638  22151  -1129    220   2485       C  
ATOM    638  O   LEU A 225      37.312  28.578  80.311  1.00164.74           O  
ANISOU  638  O   LEU A 225    18144  22163  22285  -1167    495   2660       O  
ATOM    639  CB  LEU A 225      38.826  29.908  78.072  1.00159.57           C  
ANISOU  639  CB  LEU A 225    17864  21478  21284   -882      0   2106       C  
ATOM    640  CG  LEU A 225      39.026  30.944  76.991  1.00163.51           C  
ANISOU  640  CG  LEU A 225    18505  21993  21627   -718   -148   1821       C  
ATOM    641  CD1 LEU A 225      40.504  31.339  77.032  1.00161.22           C  
ANISOU  641  CD1 LEU A 225    18497  21770  20988   -679   -170   1804       C  
ATOM    642  CD2 LEU A 225      38.594  30.431  75.613  1.00166.33           C  
ANISOU  642  CD2 LEU A 225    18761  22147  22289   -648   -424   1628       C  
ATOM    643  N   GLN A 226      37.655  26.930  78.862  1.00164.53           N  
ANISOU  643  N   GLN A 226    18000  21727  22784  -1215     82   2573       N  
ATOM    644  CA  GLN A 226      37.860  25.928  79.932  1.00164.94           C  
ANISOU  644  CA  GLN A 226    18035  21729  22905  -1356    253   2927       C  
ATOM    645  C   GLN A 226      39.305  25.505  79.938  1.00159.44           C  
ANISOU  645  C   GLN A 226    17585  21005  21990  -1326    103   2990       C  
ATOM    646  O   GLN A 226      39.770  24.864  79.017  1.00155.30           O  
ANISOU  646  O   GLN A 226    17058  20285  21661  -1306   -156   2866       O  
ATOM    647  CB  GLN A 226      36.938  24.720  79.777  1.00171.81           C  
ANISOU  647  CB  GLN A 226    18596  22330  24352  -1496    252   3030       C  
ATOM    648  CG  GLN A 226      36.648  24.033  81.096  1.00182.43           C  
ANISOU  648  CG  GLN A 226    19882  23670  25763  -1643    573   3432       C  
ATOM    649  CD  GLN A 226      35.147  23.628  81.290  1.00191.58           C  
ANISOU  649  CD  GLN A 226    20668  24703  27418  -1779    780   3509       C  
ATOM    650  OE1 GLN A 226      34.563  24.005  82.296  1.00200.38           O  
ANISOU  650  OE1 GLN A 226    21739  25985  28410  -1824   1128   3697       O  
ATOM    651  NE2 GLN A 226      34.536  22.877  80.340  1.00191.35           N  
ANISOU  651  NE2 GLN A 226    20362  24385  27953  -1838    572   3346       N  
ATOM    652  N   GLU A 227      40.026  25.915  80.954  1.00159.81           N  
ANISOU  652  N   GLU A 227    17841  21256  21624  -1305    252   3150       N  
ATOM    653  CA  GLU A 227      41.477  25.652  81.043  1.00159.89           C  
ANISOU  653  CA  GLU A 227    18082  21271  21396  -1256    104   3184       C  
ATOM    654  C   GLU A 227      41.761  24.164  80.908  1.00159.27           C  
ANISOU  654  C   GLU A 227    17935  20923  21657  -1337    -26   3353       C  
ATOM    655  O   GLU A 227      41.227  23.367  81.643  1.00156.31           O  
ANISOU  655  O   GLU A 227    17458  20460  21471  -1443    130   3642       O  
ATOM    656  CB  GLU A 227      42.032  26.168  82.385  1.00164.55           C  
ANISOU  656  CB  GLU A 227    18868  22120  21531  -1227    295   3367       C  
ATOM    657  CG  GLU A 227      43.552  26.096  82.561  1.00163.60           C  
ANISOU  657  CG  GLU A 227    18975  22046  21138  -1156    134   3359       C  
ATOM    658  CD  GLU A 227      44.065  26.709  83.883  1.00167.26           C  
ANISOU  658  CD  GLU A 227    19628  22786  21134  -1100    287   3487       C  
ATOM    659  OE1 GLU A 227      43.317  27.480  84.573  1.00167.33           O  
ANISOU  659  OE1 GLU A 227    19629  22994  20955  -1092    524   3517       O  
ATOM    660  OE2 GLU A 227      45.249  26.475  84.207  1.00174.33           O  
ANISOU  660  OE2 GLU A 227    20681  23711  21843  -1045    153   3520       O  
ATOM    661  N   TYR A 228      42.575  23.811  79.928  1.00161.51           N  
ANISOU  661  N   TYR A 228    18272  21063  22030  -1281   -301   3167       N  
ATOM    662  CA  TYR A 228      42.963  22.425  79.705  1.00166.11           C  
ANISOU  662  CA  TYR A 228    18802  21374  22939  -1335   -461   3282       C  
ATOM    663  C   TYR A 228      43.859  21.983  80.864  1.00170.48           C  
ANISOU  663  C   TYR A 228    19524  21988  23260  -1340   -391   3583       C  
ATOM    664  O   TYR A 228      45.069  22.259  80.886  1.00159.76           O  
ANISOU  664  O   TYR A 228    18354  20727  21620  -1246   -511   3504       O  
ATOM    665  CB  TYR A 228      43.673  22.209  78.378  1.00164.84           C  
ANISOU  665  CB  TYR A 228    18671  21068  22890  -1250   -764   2983       C  
ATOM    666  CG  TYR A 228      43.808  20.758  77.937  1.00166.31           C  
ANISOU  666  CG  TYR A 228    18744  20932  23512  -1302   -951   3033       C  
ATOM    667  CD1 TYR A 228      42.691  19.933  77.815  1.00167.88           C  
ANISOU  667  CD1 TYR A 228    18694  20902  24189  -1416   -935   3108       C  
ATOM    668  CD2 TYR A 228      45.059  20.220  77.600  1.00166.75           C  
ANISOU  668  CD2 TYR A 228    18924  20895  23538  -1235  -1149   2976       C  
ATOM    669  CE1 TYR A 228      42.820  18.620  77.404  1.00169.99           C  
ANISOU  669  CE1 TYR A 228    18852  20849  24885  -1465  -1114   3133       C  
ATOM    670  CE2 TYR A 228      45.187  18.914  77.155  1.00169.24           C  
ANISOU  670  CE2 TYR A 228    19134  20902  24264  -1269  -1332   2992       C  
ATOM    671  CZ  TYR A 228      44.065  18.116  77.059  1.00171.04           C  
ANISOU  671  CZ  TYR A 228    19128  20897  24962  -1384  -1319   3070       C  
ATOM    672  OH  TYR A 228      44.199  16.821  76.632  1.00173.13           O  
ANISOU  672  OH  TYR A 228    19284  20833  25665  -1420  -1506   3073       O  
ATOM    673  N   TYR A 229      43.218  21.319  81.828  1.00188.36           N  
ANISOU  673  N   TYR A 229    21717  24195  25653  -1443   -187   3928       N  
ATOM    674  CA  TYR A 229      43.856  20.909  83.070  1.00205.02           C  
ANISOU  674  CA  TYR A 229    24002  26379  27513  -1431    -84   4267       C  
ATOM    675  C   TYR A 229      44.281  22.118  83.917  1.00214.01           C  
ANISOU  675  C   TYR A 229    25346  27887  28080  -1332     46   4251       C  
ATOM    676  O   TYR A 229      43.468  22.978  84.270  1.00221.72           O  
ANISOU  676  O   TYR A 229    26283  29053  28907  -1344    266   4225       O  
ATOM    677  CB  TYR A 229      45.085  19.997  82.814  1.00205.48           C  
ANISOU  677  CB  TYR A 229    24163  26257  27651  -1378   -353   4289       C  
ATOM    678  CG  TYR A 229      44.856  18.688  82.154  1.00209.05           C  
ANISOU  678  CG  TYR A 229    24449  26333  28647  -1460   -498   4333       C  
ATOM    679  CD1 TYR A 229      45.176  18.475  80.826  1.00208.64           C  
ANISOU  679  CD1 TYR A 229    24316  26113  28845  -1424   -771   4000       C  
ATOM    680  CD2 TYR A 229      44.450  17.632  82.903  1.00214.35           C  
ANISOU  680  CD2 TYR A 229    25072  26811  29557  -1556   -366   4715       C  
ATOM    681  CE1 TYR A 229      44.997  17.230  80.221  1.00213.20           C  
ANISOU  681  CE1 TYR A 229    24738  26331  29936  -1487   -928   4010       C  
ATOM    682  CE2 TYR A 229      44.329  16.339  82.363  1.00217.02           C  
ANISOU  682  CE2 TYR A 229    25260  26761  30433  -1632   -510   4768       C  
ATOM    683  CZ  TYR A 229      44.599  16.153  81.022  1.00215.96           C  
ANISOU  683  CZ  TYR A 229    25025  26465  30563  -1597   -803   4396       C  
ATOM    684  OH  TYR A 229      44.442  14.901  80.494  1.00220.32           O  
ANISOU  684  OH  TYR A 229    25421  26633  31656  -1666   -953   4416       O  
ATOM    685  N   GLU A 230      45.564  22.198  84.258  1.00213.12           N  
ANISOU  685  N   GLU A 230    25439  27873  27662  -1227    -98   4242       N  
ATOM    686  CA  GLU A 230      46.088  23.315  85.020  1.00209.88           C  
ANISOU  686  CA  GLU A 230    25214  27791  26737  -1124    -25   4177       C  
ATOM    687  C   GLU A 230      47.388  23.737  84.384  1.00193.98           C  
ANISOU  687  C   GLU A 230    23297  25807  24598  -1026   -285   3880       C  
ATOM    688  O   GLU A 230      48.310  24.220  85.041  1.00191.10           O  
ANISOU  688  O   GLU A 230    23096  25633  23878   -929   -335   3849       O  
ATOM    689  CB  GLU A 230      46.254  22.939  86.497  1.00222.07           C  
ANISOU  689  CB  GLU A 230    26920  29465  27990  -1087    119   4546       C  
ATOM    690  CG  GLU A 230      44.941  22.549  87.174  1.00230.58           C  
ANISOU  690  CG  GLU A 230    27903  30518  29186  -1190    444   4867       C  
ATOM    691  CD  GLU A 230      44.801  23.070  88.587  1.00235.98           C  
ANISOU  691  CD  GLU A 230    28768  31508  29386  -1117    694   5080       C  
ATOM    692  OE1 GLU A 230      43.717  23.607  88.896  1.00239.06           O  
ANISOU  692  OE1 GLU A 230    29067  32020  29745  -1168    981   5110       O  
ATOM    693  OE2 GLU A 230      45.768  22.956  89.371  1.00241.48           O  
ANISOU  693  OE2 GLU A 230    29691  32328  29732   -994    595   5196       O  
ATOM    694  N   THR A 231      47.415  23.618  83.066  1.00182.07           N  
ANISOU  694  N   THR A 231    21676  24115  23387  -1046   -443   3634       N  
ATOM    695  CA  THR A 231      48.575  24.004  82.263  1.00171.84           C  
ANISOU  695  CA  THR A 231    20447  22817  22028   -964   -654   3335       C  
ATOM    696  C   THR A 231      48.725  25.509  82.229  1.00158.12           C  
ANISOU  696  C   THR A 231    18786  21318  19971   -907   -571   3090       C  
ATOM    697  O   THR A 231      49.814  26.033  82.063  1.00147.83           O  
ANISOU  697  O   THR A 231    17575  20089  18504   -837   -675   2898       O  
ATOM    698  CB  THR A 231      48.421  23.452  80.839  1.00178.13           C  
ANISOU  698  CB  THR A 231    21113  23355  23211   -988   -814   3148       C  
ATOM    699  OG1 THR A 231      47.175  23.911  80.293  1.00182.41           O  
ANISOU  699  OG1 THR A 231    21534  23889  23884  -1035   -705   3054       O  
ATOM    700  CG2 THR A 231      48.422  21.921  80.864  1.00183.64           C  
ANISOU  700  CG2 THR A 231    21732  23782  24259  -1038   -926   3362       C  
ATOM    701  N   GLY A 232      47.606  26.216  82.327  1.00156.81           N  
ANISOU  701  N   GLY A 232    18566  21253  19760   -941   -379   3080       N  
ATOM    702  CA  GLY A 232      47.586  27.666  82.228  1.00152.80           C  
ANISOU  702  CA  GLY A 232    18121  20939  18997   -889   -289   2845       C  
ATOM    703  C   GLY A 232      47.701  28.150  80.815  1.00146.01           C  
ANISOU  703  C   GLY A 232    17234  19970  18272   -858   -393   2549       C  
ATOM    704  O   GLY A 232      47.236  29.252  80.520  1.00140.00           O  
ANISOU  704  O   GLY A 232    16486  19303  17403   -827   -296   2384       O  
ATOM    705  N   ALA A 233      48.338  27.356  79.951  1.00144.77           N  
ANISOU  705  N   ALA A 233    17056  19618  18330   -850   -585   2480       N  
ATOM    706  CA  ALA A 233      48.622  27.753  78.588  1.00142.48           C  
ANISOU  706  CA  ALA A 233    16780  19232  18122   -796   -684   2203       C  
ATOM    707  C   ALA A 233      47.570  27.302  77.597  1.00138.09           C  
ANISOU  707  C   ALA A 233    16099  18508  17861   -807   -742   2151       C  
ATOM    708  O   ALA A 233      47.338  27.941  76.550  1.00142.15           O  
ANISOU  708  O   ALA A 233    16637  18996  18376   -740   -770   1931       O  
ATOM    709  CB  ALA A 233      49.973  27.199  78.147  1.00146.53           C  
ANISOU  709  CB  ALA A 233    17343  19644  18688   -758   -855   2115       C  
ATOM    710  N   PHE A 234      46.899  26.205  77.974  1.00133.98           N  
ANISOU  710  N   PHE A 234    15443  17867  17593   -888   -756   2360       N  
ATOM    711  CA  PHE A 234      46.000  25.505  77.079  1.00138.35           C  
ANISOU  711  CA  PHE A 234    15840  18218  18508   -909   -861   2303       C  
ATOM    712  C   PHE A 234      44.560  25.577  77.533  1.00138.89           C  
ANISOU  712  C   PHE A 234    15749  18310  18712   -982   -710   2424       C  
ATOM    713  O   PHE A 234      44.222  25.439  78.720  1.00142.35           O  
ANISOU  713  O   PHE A 234    16159  18835  19092  -1059   -530   2678       O  
ATOM    714  CB  PHE A 234      46.450  24.067  76.961  1.00144.04           C  
ANISOU  714  CB  PHE A 234    16499  18715  19516   -949  -1024   2405       C  
ATOM    715  CG  PHE A 234      47.812  23.877  76.335  1.00147.13           C  
ANISOU  715  CG  PHE A 234    17006  19051  19845   -867  -1189   2247       C  
ATOM    716  CD1 PHE A 234      48.065  24.297  75.029  1.00147.33           C  
ANISOU  716  CD1 PHE A 234    17082  19039  19856   -768  -1295   1949       C  
ATOM    717  CD2 PHE A 234      48.824  23.217  77.032  1.00156.56           C  
ANISOU  717  CD2 PHE A 234    18255  20221  21010   -877  -1241   2399       C  
ATOM    718  CE1 PHE A 234      49.300  24.085  74.443  1.00150.17           C  
ANISOU  718  CE1 PHE A 234    17531  19345  20180   -695  -1411   1804       C  
ATOM    719  CE2 PHE A 234      50.070  23.009  76.436  1.00160.30           C  
ANISOU  719  CE2 PHE A 234    18799  20636  21469   -800  -1390   2234       C  
ATOM    720  CZ  PHE A 234      50.304  23.443  75.138  1.00155.67           C  
ANISOU  720  CZ  PHE A 234    18249  20018  20880   -716  -1459   1935       C  
ATOM    721  N   TYR A 235      43.670  25.758  76.542  1.00134.10           N  
ANISOU  721  N   TYR A 235    15030  17620  18302   -945   -788   2231       N  
ATOM    722  CA  TYR A 235      42.261  25.968  76.812  1.00133.20           C  
ANISOU  722  CA  TYR A 235    14732  17529  18347   -997   -658   2279       C  
ATOM    723  C   TYR A 235      41.402  25.247  75.804  1.00136.27           C  
ANISOU  723  C   TYR A 235    14914  17692  19167   -999   -842   2137       C  
ATOM    724  O   TYR A 235      41.841  24.918  74.701  1.00132.08           O  
ANISOU  724  O   TYR A 235    14427  17031  18724   -916  -1078   1932       O  
ATOM    725  CB  TYR A 235      41.952  27.449  76.791  1.00130.10           C  
ANISOU  725  CB  TYR A 235    14425  17346  17658   -908   -539   2136       C  
ATOM    726  CG  TYR A 235      42.638  28.142  77.919  1.00126.25           C  
ANISOU  726  CG  TYR A 235    14102  17078  16787   -916   -350   2264       C  
ATOM    727  CD1 TYR A 235      41.977  28.374  79.118  1.00128.77           C  
ANISOU  727  CD1 TYR A 235    14359  17544  17021   -981   -108   2459       C  
ATOM    728  CD2 TYR A 235      43.973  28.520  77.807  1.00122.04           C  
ANISOU  728  CD2 TYR A 235    13776  16604  15988   -855   -415   2181       C  
ATOM    729  CE1 TYR A 235      42.604  28.985  80.173  1.00132.25           C  
ANISOU  729  CE1 TYR A 235    14959  18196  17092   -968     40   2552       C  
ATOM    730  CE2 TYR A 235      44.620  29.133  78.840  1.00123.44           C  
ANISOU  730  CE2 TYR A 235    14087  16976  15840   -854   -280   2263       C  
ATOM    731  CZ  TYR A 235      43.927  29.382  80.034  1.00131.06           C  
ANISOU  731  CZ  TYR A 235    15006  18098  16691   -902    -63   2442       C  
ATOM    732  OH  TYR A 235      44.553  30.009  81.085  1.00140.41           O  
ANISOU  732  OH  TYR A 235    16333  19491  17526   -879     52   2495       O  
ATOM    733  N   LEU A 236      40.159  24.980  76.198  1.00145.17           N  
ANISOU  733  N   LEU A 236    15802  18772  20581  -1092   -731   2235       N  
ATOM    734  CA  LEU A 236      39.137  24.524  75.282  1.00151.84           C  
ANISOU  734  CA  LEU A 236    16409  19431  21852  -1085   -903   2051       C  
ATOM    735  C   LEU A 236      38.202  25.683  75.071  1.00147.75           C  
ANISOU  735  C   LEU A 236    15832  19062  21241  -1000   -838   1888       C  
ATOM    736  O   LEU A 236      37.972  26.433  76.003  1.00154.00           O  
ANISOU  736  O   LEU A 236    16653  20048  21809  -1029   -580   2023       O  
ATOM    737  CB  LEU A 236      38.446  23.252  75.720  1.00161.59           C  
ANISOU  737  CB  LEU A 236    17372  20441  23580  -1255   -863   2240       C  
ATOM    738  CG  LEU A 236      39.016  22.004  74.979  1.00170.97           C  
ANISOU  738  CG  LEU A 236    18537  21352  25070  -1264  -1136   2170       C  
ATOM    739  CD1 LEU A 236      40.519  21.776  75.241  1.00175.08           C  
ANISOU  739  CD1 LEU A 236    19327  21907  25287  -1234  -1165   2282       C  
ATOM    740  CD2 LEU A 236      38.276  20.716  75.284  1.00176.21           C  
ANISOU  740  CD2 LEU A 236    18911  21737  26303  -1435  -1117   2329       C  
ATOM    741  N   VAL A 237      37.774  25.896  73.830  1.00141.69           N  
ANISOU  741  N   VAL A 237    15021  18220  20592   -865  -1084   1585       N  
ATOM    742  CA  VAL A 237      36.989  27.086  73.480  1.00144.02           C  
ANISOU  742  CA  VAL A 237    15304  18653  20765   -736  -1069   1403       C  
ATOM    743  C   VAL A 237      35.526  26.763  73.296  1.00153.16           C  
ANISOU  743  C   VAL A 237    16107  19701  22386   -769  -1124   1308       C  
ATOM    744  O   VAL A 237      35.186  26.023  72.385  1.00156.97           O  
ANISOU  744  O   VAL A 237    16446  19987  23206   -732  -1399   1121       O  
ATOM    745  CB  VAL A 237      37.502  27.688  72.170  1.00140.09           C  
ANISOU  745  CB  VAL A 237    15035  18161  20030   -519  -1313   1122       C  
ATOM    746  CG1 VAL A 237      36.687  28.908  71.772  1.00142.11           C  
ANISOU  746  CG1 VAL A 237    15298  18535  20162   -362  -1318    947       C  
ATOM    747  CG2 VAL A 237      38.970  28.041  72.295  1.00133.73           C  
ANISOU  747  CG2 VAL A 237    14551  17449  18809   -493  -1243   1192       C  
ATOM    748  N   LYS A 238      34.677  27.363  74.139  1.00157.86           N  
ANISOU  748  N   LYS A 238    16556  20428  22994   -823   -869   1407       N  
ATOM    749  CA  LYS A 238      33.235  27.171  74.051  1.00160.87           C  
ANISOU  749  CA  LYS A 238    16563  20723  23837   -858   -882   1309       C  
ATOM    750  C   LYS A 238      32.569  28.487  73.697  1.00160.12           C  
ANISOU  750  C   LYS A 238    16480  20785  23572   -676   -901   1098       C  
ATOM    751  O   LYS A 238      33.174  29.556  73.837  1.00154.56           O  
ANISOU  751  O   LYS A 238    16063  20265  22396   -571   -808   1104       O  
ATOM    752  CB  LYS A 238      32.654  26.695  75.383  1.00166.24           C  
ANISOU  752  CB  LYS A 238    17010  21410  24743  -1079   -526   1612       C  
ATOM    753  CG  LYS A 238      32.745  25.195  75.641  1.00171.20           C  
ANISOU  753  CG  LYS A 238    17474  21791  25780  -1272   -524   1802       C  
ATOM    754  CD  LYS A 238      31.792  24.675  76.698  1.00175.97           C  
ANISOU  754  CD  LYS A 238    17763  22342  26752  -1478   -190   2054       C  
ATOM    755  CE  LYS A 238      32.100  23.198  76.936  1.00175.27           C  
ANISOU  755  CE  LYS A 238    17586  21984  27023  -1659   -191   2276       C  
ATOM    756  NZ  LYS A 238      31.142  22.457  77.788  1.00176.09           N  
ANISOU  756  NZ  LYS A 238    17352  21949  27603  -1877    116   2525       N  
ATOM    757  N   PHE A 239      31.342  28.384  73.176  1.00166.64           N  
ANISOU  757  N   PHE A 239    16987  21513  24814   -630  -1050    891       N  
ATOM    758  CA  PHE A 239      30.558  29.549  72.830  1.00176.45           C  
ANISOU  758  CA  PHE A 239    18193  22878  25972   -445  -1095    682       C  
ATOM    759  C   PHE A 239      29.416  29.715  73.794  1.00185.41           C  
ANISOU  759  C   PHE A 239    18985  24076  27385   -563   -803    774       C  
ATOM    760  O   PHE A 239      28.775  28.732  74.175  1.00186.75           O  
ANISOU  760  O   PHE A 239    18814  24102  28040   -747   -719    861       O  
ATOM    761  CB  PHE A 239      29.973  29.419  71.427  1.00185.55           C  
ANISOU  761  CB  PHE A 239    19237  23890  27372   -250  -1529    326       C  
ATOM    762  CG  PHE A 239      30.903  29.867  70.352  1.00188.51           C  
ANISOU  762  CG  PHE A 239    20011  24286  27328    -27  -1788    174       C  
ATOM    763  CD1 PHE A 239      31.038  31.226  70.079  1.00189.22           C  
ANISOU  763  CD1 PHE A 239    20364  24534  26994    180  -1772     96       C  
ATOM    764  CD2 PHE A 239      31.698  28.942  69.643  1.00188.66           C  
ANISOU  764  CD2 PHE A 239    20155  24158  27367    -25  -2016    124       C  
ATOM    765  CE1 PHE A 239      31.898  31.655  69.086  1.00188.39           C  
ANISOU  765  CE1 PHE A 239    20638  24437  26504    382  -1966    -16       C  
ATOM    766  CE2 PHE A 239      32.575  29.371  68.692  1.00187.16           C  
ANISOU  766  CE2 PHE A 239    20336  23999  26774    177  -2201      1       C  
ATOM    767  CZ  PHE A 239      32.668  30.719  68.393  1.00188.95           C  
ANISOU  767  CZ  PHE A 239    20823  24378  26588    379  -2170    -62       C  
ATOM    768  N   LYS A 240      29.153  30.964  74.175  1.00194.73           N  
ANISOU  768  N   LYS A 240    20250  25459  28280   -455   -634    750       N  
ATOM    769  CA  LYS A 240      27.853  31.318  74.700  1.00205.37           C  
ANISOU  769  CA  LYS A 240    21242  26862  29927   -478   -450    706       C  
ATOM    770  C   LYS A 240      26.887  31.177  73.530  1.00208.67           C  
ANISOU  770  C   LYS A 240    21391  27127  30767   -328   -835    362       C  
ATOM    771  O   LYS A 240      26.039  30.279  73.529  1.00209.33           O  
ANISOU  771  O   LYS A 240    21067  27049  31420   -454   -870    316       O  
ATOM    772  CB  LYS A 240      27.827  32.746  75.257  1.00207.70           C  
ANISOU  772  CB  LYS A 240    21707  27398  29811   -358   -228    710       C  
ATOM    773  CG  LYS A 240      28.715  32.985  76.464  1.00209.26           C  
ANISOU  773  CG  LYS A 240    22157  27769  29581   -480    133   1005       C  
ATOM    774  CD  LYS A 240      28.555  34.398  76.997  1.00211.72           C  
ANISOU  774  CD  LYS A 240    22590  28300  29553   -355    335    957       C  
ATOM    775  CE  LYS A 240      29.716  34.789  77.911  1.00211.02           C  
ANISOU  775  CE  LYS A 240    22848  28379  28947   -411    573   1168       C  
ATOM    776  NZ  LYS A 240      29.633  36.243  78.234  1.00210.12           N  
ANISOU  776  NZ  LYS A 240    22879  28447  28509   -259    703   1059       N  
ATOM    777  N   ARG A 241      27.074  32.013  72.505  1.00210.61           N  
ANISOU  777  N   ARG A 241    21877  27407  30736    -55  -1137    122       N  
ATOM    778  CA  ARG A 241      26.032  32.251  71.499  1.00217.42           C  
ANISOU  778  CA  ARG A 241    22515  28190  31902    159  -1490   -224       C  
ATOM    779  C   ARG A 241      26.433  31.793  70.084  1.00223.12           C  
ANISOU  779  C   ARG A 241    23401  28766  32607    335  -1968   -454       C  
ATOM    780  O   ARG A 241      27.261  32.420  69.427  1.00224.02           O  
ANISOU  780  O   ARG A 241    23937  28938  32240    527  -2104   -494       O  
ATOM    781  CB  ARG A 241      25.679  33.745  71.482  1.00216.86           C  
ANISOU  781  CB  ARG A 241    22574  28288  31534    387  -1447   -332       C  
ATOM    782  CG  ARG A 241      25.494  34.403  72.866  1.00216.86           C  
ANISOU  782  CG  ARG A 241    22517  28472  31408    258   -965   -120       C  
ATOM    783  CD  ARG A 241      24.047  34.651  73.292  1.00221.15           C  
ANISOU  783  CD  ARG A 241    22594  29042  32391    259   -845   -241       C  
ATOM    784  NE  ARG A 241      23.457  33.494  73.982  1.00222.75           N  
ANISOU  784  NE  ARG A 241    22371  29150  33114    -20   -636   -113       N  
ATOM    785  CZ  ARG A 241      22.672  32.553  73.440  1.00228.85           C  
ANISOU  785  CZ  ARG A 241    22746  29722  34486    -73   -865   -281       C  
ATOM    786  NH1 ARG A 241      22.341  32.556  72.144  1.00232.88           N  
ANISOU  786  NH1 ARG A 241    23216  30113  35154    154  -1364   -616       N  
ATOM    787  NH2 ARG A 241      22.213  31.575  74.215  1.00233.26           N  
ANISOU  787  NH2 ARG A 241    22941  30186  35498   -354   -591   -110       N  
ATOM    788  N   ILE A 242      25.867  30.668  69.643  1.00230.34           N  
ANISOU  788  N   ILE A 242    23980  29481  34054    264  -2203   -602       N  
ATOM    789  CA  ILE A 242      25.819  30.305  68.212  1.00231.86           C  
ANISOU  789  CA  ILE A 242    24222  29539  34332    490  -2722   -930       C  
ATOM    790  C   ILE A 242      24.937  31.351  67.463  1.00234.72           C  
ANISOU  790  C   ILE A 242    24555  29973  34655    819  -2993  -1233       C  
ATOM    791  O   ILE A 242      23.719  31.178  67.444  1.00247.77           O  
ANISOU  791  O   ILE A 242    25758  31557  36824    828  -3109  -1432       O  
ATOM    792  CB  ILE A 242      25.312  28.822  68.028  1.00233.15           C  
ANISOU  792  CB  ILE A 242    23968  29453  35163    316  -2903  -1042       C  
ATOM    793  CG1 ILE A 242      25.381  28.362  66.565  1.00232.05           C  
ANISOU  793  CG1 ILE A 242    23909  29180  35078    555  -3454  -1397       C  
ATOM    794  CG2 ILE A 242      23.897  28.581  68.587  1.00235.91           C  
ANISOU  794  CG2 ILE A 242    23732  29730  36172    179  -2796  -1117       C  
ATOM    795  CD1 ILE A 242      24.994  26.903  66.364  1.00234.33           C  
ANISOU  795  CD1 ILE A 242    23810  29201  36020    384  -3647  -1528       C  
ATOM    796  N   PRO A 243      25.529  32.440  66.857  1.00226.34           N  
ANISOU  796  N   PRO A 243    23958  29035  33005   1094  -3089  -1266       N  
ATOM    797  CA  PRO A 243      24.746  33.636  66.429  1.00225.18           C  
ANISOU  797  CA  PRO A 243    23827  28976  32752   1395  -3241  -1464       C  
ATOM    798  C   PRO A 243      23.498  33.364  65.587  1.00233.76           C  
ANISOU  798  C   PRO A 243    24548  29955  34312   1596  -3689  -1849       C  
ATOM    799  O   PRO A 243      22.405  33.858  65.923  1.00243.21           O  
ANISOU  799  O   PRO A 243    25412  31189  35808   1645  -3658  -1961       O  
ATOM    800  CB  PRO A 243      25.744  34.467  65.599  1.00219.24           C  
ANISOU  800  CB  PRO A 243    23667  28291  31340   1661  -3360  -1452       C  
ATOM    801  CG  PRO A 243      26.870  33.564  65.297  1.00220.05           C  
ANISOU  801  CG  PRO A 243    23996  28322  31290   1546  -3391  -1356       C  
ATOM    802  CD  PRO A 243      26.933  32.583  66.441  1.00223.00           C  
ANISOU  802  CD  PRO A 243    24058  28648  32020   1154  -3084  -1140       C  
ATOM    803  N   ARG A 244      23.664  32.614  64.502  1.00230.35           N  
ANISOU  803  N   ARG A 244    24176  29398  33946   1728  -4112  -2070       N  
ATOM    804  CA  ARG A 244      22.525  32.072  63.781  1.00233.82           C  
ANISOU  804  CA  ARG A 244    24204  29709  34927   1868  -4560  -2457       C  
ATOM    805  C   ARG A 244      22.977  30.796  63.032  1.00228.69           C  
ANISOU  805  C   ARG A 244    23562  28891  34437   1834  -4871  -2601       C  
ATOM    806  O   ARG A 244      23.213  29.771  63.684  1.00218.54           O  
ANISOU  806  O   ARG A 244    22057  27491  33485   1495  -4661  -2445       O  
ATOM    807  CB  ARG A 244      21.844  33.166  62.927  1.00235.58           C  
ANISOU  807  CB  ARG A 244    24539  30009  34963   2300  -4909  -2728       C  
ATOM    808  CG  ARG A 244      20.351  32.931  62.701  1.00234.78           C  
ANISOU  808  CG  ARG A 244    23861  29820  35525   2395  -5230  -3092       C  
ATOM    809  CD  ARG A 244      19.599  34.225  62.431  1.00233.93           C  
ANISOU  809  CD  ARG A 244    23789  29822  35269   2737  -5373  -3242       C  
ATOM    810  NE  ARG A 244      18.379  34.005  61.652  1.00239.07           N  
ANISOU  810  NE  ARG A 244    24040  30384  36410   2987  -5903  -3695       N  
ATOM    811  CZ  ARG A 244      17.594  34.972  61.169  1.00242.69           C  
ANISOU  811  CZ  ARG A 244    24488  30904  36817   3356  -6183  -3920       C  
ATOM    812  NH1 ARG A 244      17.861  36.265  61.379  1.00241.24           N  
ANISOU  812  NH1 ARG A 244    24674  30858  36125   3518  -5970  -3728       N  
ATOM    813  NH2 ARG A 244      16.506  34.652  60.465  1.00247.72           N  
ANISOU  813  NH2 ARG A 244    24727  31453  37943   3577  -6701  -4359       N  
ATOM    814  N   GLY A 245      23.091  30.833  61.700  1.00230.64           N  
ANISOU  814  N   GLY A 245    24063  29117  34450   2185  -5359  -2892       N  
ATOM    815  CA  GLY A 245      23.804  29.793  60.957  1.00231.13           C  
ANISOU  815  CA  GLY A 245    24278  29059  34482   2191  -5611  -3001       C  
ATOM    816  C   GLY A 245      25.264  29.785  61.355  1.00232.57           C  
ANISOU  816  C   GLY A 245    24900  29303  34161   2025  -5240  -2634       C  
ATOM    817  O   GLY A 245      25.848  28.708  61.476  1.00236.50           O  
ANISOU  817  O   GLY A 245    25350  29679  34829   1812  -5201  -2569       O  
ATOM    818  N   ASN A 246      25.830  30.986  61.552  1.00237.44           N  
ANISOU  818  N   ASN A 246    25924  30094  34196   2128  -4983  -2412       N  
ATOM    819  CA  ASN A 246      27.168  31.215  62.138  1.00239.13           C  
ANISOU  819  CA  ASN A 246    26519  30390  33947   1952  -4564  -2044       C  
ATOM    820  C   ASN A 246      28.318  30.682  61.278  1.00227.60           C  
ANISOU  820  C   ASN A 246    25443  28888  32144   2045  -4715  -2074       C  
ATOM    821  O   ASN A 246      28.368  29.485  60.970  1.00235.71           O  
ANISOU  821  O   ASN A 246    26294  29770  33494   1961  -4921  -2214       O  
ATOM    822  CB  ASN A 246      27.282  30.620  63.554  1.00247.07           C  
ANISOU  822  CB  ASN A 246    27231  31367  35277   1518  -4134  -1748       C  
ATOM    823  CG  ASN A 246      28.634  30.907  64.228  1.00242.85           C  
ANISOU  823  CG  ASN A 246    27068  30931  34273   1352  -3727  -1389       C  
ATOM    824  OD1 ASN A 246      29.323  31.889  63.919  1.00232.68           O  
ANISOU  824  OD1 ASN A 246    26206  29759  32440   1525  -3653  -1318       O  
ATOM    825  ND2 ASN A 246      29.001  30.048  65.183  1.00241.54           N  
ANISOU  825  ND2 ASN A 246    26727  30705  34341   1015  -3459  -1159       N  
ATOM    826  N   PRO A 247      29.277  31.559  60.935  1.00205.92           N  
ANISOU  826  N   PRO A 247    23212  26257  28768   2204  -4582  -1937       N  
ATOM    827  CA  PRO A 247      30.457  31.095  60.212  1.00200.22           C  
ANISOU  827  CA  PRO A 247    22855  25508  27708   2271  -4646  -1936       C  
ATOM    828  C   PRO A 247      31.177  29.823  60.760  1.00195.68           C  
ANISOU  828  C   PRO A 247    22131  24825  27391   1944  -4507  -1811       C  
ATOM    829  O   PRO A 247      31.716  29.051  59.940  1.00197.99           O  
ANISOU  829  O   PRO A 247    22554  25037  27634   2036  -4736  -1966       O  
ATOM    830  CB  PRO A 247      31.403  32.301  60.310  1.00197.07           C  
ANISOU  830  CB  PRO A 247    22931  25246  26700   2344  -4324  -1688       C  
ATOM    831  CG  PRO A 247      30.510  33.484  60.413  1.00196.48           C  
ANISOU  831  CG  PRO A 247    22836  25252  26566   2514  -4323  -1712       C  
ATOM    832  CD  PRO A 247      29.230  33.034  61.037  1.00199.67           C  
ANISOU  832  CD  PRO A 247    22685  25605  27575   2373  -4412  -1824       C  
ATOM    833  N   LEU A 248      31.252  29.730  62.084  1.00185.50           N  
ANISOU  833  N   LEU A 248    20633  23549  26297   1607  -4129  -1528       N  
ATOM    834  CA  LEU A 248      32.150  28.864  62.800  1.00177.95           C  
ANISOU  834  CA  LEU A 248    19649  22531  25432   1309  -3894  -1303       C  
ATOM    835  C   LEU A 248      31.483  27.602  63.286  1.00176.66           C  
ANISOU  835  C   LEU A 248    19009  22190  25921   1068  -3964  -1339       C  
ATOM    836  O   LEU A 248      32.090  26.816  64.022  1.00171.10           O  
ANISOU  836  O   LEU A 248    18235  21412  25363    802  -3758  -1122       O  
ATOM    837  CB  LEU A 248      32.712  29.661  63.982  1.00174.04           C  
ANISOU  837  CB  LEU A 248    19277  22178  24669   1121  -3423   -952       C  
ATOM    838  CG  LEU A 248      33.035  31.131  63.688  1.00173.45           C  
ANISOU  838  CG  LEU A 248    19584  22262  24056   1339  -3314   -916       C  
ATOM    839  CD1 LEU A 248      33.533  31.808  64.973  1.00173.75           C  
ANISOU  839  CD1 LEU A 248    19679  22422  23913   1124  -2865   -602       C  
ATOM    840  CD2 LEU A 248      34.093  31.245  62.592  1.00171.95           C  
ANISOU  840  CD2 LEU A 248    19829  22072  23429   1550  -3432   -992       C  
ATOM    841  N   SER A 249      30.246  27.388  62.846  1.00182.12           N  
ANISOU  841  N   SER A 249    19373  22798  27026   1170  -4268  -1618       N  
ATOM    842  CA  SER A 249      29.452  26.195  63.217  1.00187.52           C  
ANISOU  842  CA  SER A 249    19549  23274  28424    947  -4357  -1695       C  
ATOM    843  C   SER A 249      30.059  24.938  62.679  1.00188.87           C  
ANISOU  843  C   SER A 249    19730  23258  28773    905  -4573  -1808       C  
ATOM    844  O   SER A 249      29.966  23.888  63.319  1.00188.16           O  
ANISOU  844  O   SER A 249    19337  22987  29169    624  -4474  -1698       O  
ATOM    845  CB  SER A 249      28.032  26.304  62.682  1.00193.56           C  
ANISOU  845  CB  SER A 249    19965  23987  29591   1112  -4695  -2040       C  
ATOM    846  OG  SER A 249      27.372  27.425  63.219  1.00196.11           O  
ANISOU  846  OG  SER A 249    20227  24467  29817   1149  -4498  -1952       O  
ATOM    847  N   HIS A 250      30.658  25.083  61.493  1.00192.06           N  
ANISOU  847  N   HIS A 250    20493  23702  28779   1199  -4858  -2026       N  
ATOM    848  CA  HIS A 250      31.293  23.996  60.750  1.00197.65           C  
ANISOU  848  CA  HIS A 250    21274  24254  29568   1241  -5115  -2205       C  
ATOM    849  C   HIS A 250      32.609  23.612  61.449  1.00195.47           C  
ANISOU  849  C   HIS A 250    21196  23972  29098   1012  -4768  -1864       C  
ATOM    850  O   HIS A 250      33.226  22.594  61.116  1.00199.02           O  
ANISOU  850  O   HIS A 250    21664  24272  29682    974  -4897  -1940       O  
ATOM    851  CB  HIS A 250      31.622  24.415  59.296  1.00200.57           C  
ANISOU  851  CB  HIS A 250    22034  24714  29457   1656  -5465  -2512       C  
ATOM    852  CG  HIS A 250      30.587  25.279  58.638  1.00203.93           C  
ANISOU  852  CG  HIS A 250    22447  25237  29799   1959  -5739  -2764       C  
ATOM    853  ND1 HIS A 250      30.640  26.658  58.675  1.00199.54           N  
ANISOU  853  ND1 HIS A 250    22186  24888  28742   2118  -5562  -2620       N  
ATOM    854  CD2 HIS A 250      29.496  24.960  57.899  1.00208.61           C  
ANISOU  854  CD2 HIS A 250    22771  25739  30748   2151  -6201  -3165       C  
ATOM    855  CE1 HIS A 250      29.611  27.148  58.005  1.00204.53           C  
ANISOU  855  CE1 HIS A 250    22739  25553  29419   2400  -5898  -2903       C  
ATOM    856  NE2 HIS A 250      28.904  26.139  57.522  1.00208.89           N  
ANISOU  856  NE2 HIS A 250    22947  25937  30484   2431  -6299  -3245       N  
ATOM    857  N   PHE A 251      33.058  24.481  62.357  1.00188.09           N  
ANISOU  857  N   PHE A 251    20428  23210  27828    895  -4356  -1519       N  
ATOM    858  CA  PHE A 251      34.300  24.288  63.061  1.00183.30           C  
ANISOU  858  CA  PHE A 251    20020  22630  26995    707  -4036  -1205       C  
ATOM    859  C   PHE A 251      34.052  23.835  64.488  1.00186.89           C  
ANISOU  859  C   PHE A 251    20175  23022  27811    358  -3718   -885       C  
ATOM    860  O   PHE A 251      35.031  23.721  65.263  1.00204.15           O  
ANISOU  860  O   PHE A 251    22509  25245  29811    194  -3435   -590       O  
ATOM    861  CB  PHE A 251      35.162  25.542  63.028  1.00175.90           C  
ANISOU  861  CB  PHE A 251    19517  21921  25396    835  -3811  -1062       C  
ATOM    862  CG  PHE A 251      35.502  26.003  61.657  1.00171.69           C  
ANISOU  862  CG  PHE A 251    19325  21449  24460   1178  -4060  -1320       C  
ATOM    863  CD1 PHE A 251      35.946  25.110  60.689  1.00174.57           C  
ANISOU  863  CD1 PHE A 251    19769  21695  24863   1304  -4345  -1555       C  
ATOM    864  CD2 PHE A 251      35.390  27.338  61.330  1.00168.58           C  
ANISOU  864  CD2 PHE A 251    19192  21225  23633   1388  -3999  -1322       C  
ATOM    865  CE1 PHE A 251      36.259  25.548  59.407  1.00177.17           C  
ANISOU  865  CE1 PHE A 251    20446  22097  24772   1646  -4554  -1786       C  
ATOM    866  CE2 PHE A 251      35.708  27.784  60.065  1.00170.61           C  
ANISOU  866  CE2 PHE A 251    19802  21536  23486   1720  -4200  -1525       C  
ATOM    867  CZ  PHE A 251      36.151  26.883  59.103  1.00174.52           C  
ANISOU  867  CZ  PHE A 251    20387  21933  23988   1851  -4470  -1753       C  
ATOM    868  N   LEU A 252      32.801  23.456  64.761  1.00182.82           N  
ANISOU  868  N   LEU A 252    19239  22389  27832    258  -3790   -963       N  
ATOM    869  CA  LEU A 252      32.407  22.982  66.084  1.00181.40           C  
ANISOU  869  CA  LEU A 252    18751  22134  28037    -65  -3472   -659       C  
ATOM    870  C   LEU A 252      32.417  21.460  66.184  1.00186.52           C  
ANISOU  870  C   LEU A 252    19138  22485  29245   -258  -3571   -653       C  
ATOM    871  O   LEU A 252      31.971  20.783  65.295  1.00198.76           O  
ANISOU  871  O   LEU A 252    20515  23852  31151   -166  -3936   -978       O  
ATOM    872  CB  LEU A 252      31.036  23.525  66.507  1.00180.62           C  
ANISOU  872  CB  LEU A 252    18322  22084  28220    -98  -3391   -692       C  
ATOM    873  CG  LEU A 252      30.994  25.005  66.881  1.00175.68           C  
ANISOU  873  CG  LEU A 252    17904  21738  27107      6  -3160   -583       C  
ATOM    874  CD1 LEU A 252      29.567  25.557  66.861  1.00179.18           C  
ANISOU  874  CD1 LEU A 252    18024  22214  27840     76  -3222   -757       C  
ATOM    875  CD2 LEU A 252      31.646  25.257  68.240  1.00171.12           C  
ANISOU  875  CD2 LEU A 252    17445  21285  26285   -214  -2690   -161       C  
ATOM    876  N   GLU A 253      32.918  20.945  67.303  1.00182.94           N  
ANISOU  876  N   GLU A 253    18663  21979  28867   -517  -3246   -278       N  
ATOM    877  CA  GLU A 253      32.811  19.534  67.653  1.00182.59           C  
ANISOU  877  CA  GLU A 253    18341  21628  29406   -741  -3257   -186       C  
ATOM    878  C   GLU A 253      31.996  19.432  68.937  1.00179.16           C  
ANISOU  878  C   GLU A 253    17598  21160  29312  -1009  -2884    129       C  
ATOM    879  O   GLU A 253      32.451  18.861  69.927  1.00173.21           O  
ANISOU  879  O   GLU A 253    16856  20333  28621  -1220  -2601    495       O  
ATOM    880  CB  GLU A 253      34.210  18.892  67.810  1.00183.47           C  
ANISOU  880  CB  GLU A 253    18727  21677  29305   -790  -3210     -2       C  
ATOM    881  CG  GLU A 253      34.720  18.114  66.596  1.00187.50           C  
ANISOU  881  CG  GLU A 253    19312  22010  29916   -635  -3615   -336       C  
ATOM    882  CD  GLU A 253      34.148  16.684  66.480  1.00194.34           C  
ANISOU  882  CD  GLU A 253    19800  22495  31544   -785  -3804   -443       C  
ATOM    883  OE1 GLU A 253      32.915  16.534  66.383  1.00200.71           O  
ANISOU  883  OE1 GLU A 253    20240  23183  32838   -836  -3901   -603       O  
ATOM    884  OE2 GLU A 253      34.913  15.686  66.517  1.00194.37           O  
ANISOU  884  OE2 GLU A 253    19849  22297  31706   -860  -3851   -369       O  
ATOM    885  N   GLY A 254      30.831  20.051  68.916  1.00183.62           N  
ANISOU  885  N   GLY A 254    17916  21799  30050   -974  -2876     -7       N  
ATOM    886  CA  GLY A 254      29.959  20.098  70.089  1.00192.66           C  
ANISOU  886  CA  GLY A 254    18759  22946  31496  -1203  -2492    263       C  
ATOM    887  C   GLY A 254      29.631  21.526  70.452  1.00200.43           C  
ANISOU  887  C   GLY A 254    19853  24254  32046  -1095  -2289    301       C  
ATOM    888  O   GLY A 254      29.047  22.228  69.634  1.00211.29           O  
ANISOU  888  O   GLY A 254    21190  25714  33377   -881  -2539    -27       O  
ATOM    889  N   GLU A 255      30.041  21.919  71.670  1.00202.78           N  
ANISOU  889  N   GLU A 255    20304  24722  32021  -1227  -1855    694       N  
ATOM    890  CA  GLU A 255      30.042  23.280  72.138  1.00206.08           C  
ANISOU  890  CA  GLU A 255    20912  25457  31930  -1128  -1630    770       C  
ATOM    891  C   GLU A 255      31.446  23.860  72.000  1.00202.49           C  
ANISOU  891  C   GLU A 255    20958  25182  30797   -997  -1646    839       C  
ATOM    892  O   GLU A 255      31.647  25.042  72.290  1.00202.10           O  
ANISOU  892  O   GLU A 255    21124  25385  30276   -895  -1491    879       O  
ATOM    893  CB  GLU A 255      29.637  23.322  73.605  1.00209.39           C  
ANISOU  893  CB  GLU A 255    21188  25956  32415  -1348  -1139   1143       C  
ATOM    894  CG  GLU A 255      28.162  23.028  73.854  1.00217.09           C  
ANISOU  894  CG  GLU A 255    21653  26805  34026  -1474  -1030   1085       C  
ATOM    895  CD  GLU A 255      27.559  23.876  74.977  1.00219.79           C  
ANISOU  895  CD  GLU A 255    21916  27378  34216  -1536   -585   1289       C  
ATOM    896  OE1 GLU A 255      28.014  25.018  75.201  1.00211.94           O  
ANISOU  896  OE1 GLU A 255    21229  26663  32633  -1394   -489   1311       O  
ATOM    897  OE2 GLU A 255      26.602  23.409  75.647  1.00229.51           O  
ANISOU  897  OE2 GLU A 255    22762  28503  35936  -1727   -314   1419       O  
ATOM    898  N   VAL A 256      32.346  22.999  71.507  1.00198.89           N  
ANISOU  898  N   VAL A 256    20644  24569  30354   -999  -1845    821       N  
ATOM    899  CA  VAL A 256      33.780  23.225  71.507  1.00195.47           C  
ANISOU  899  CA  VAL A 256    20627  24248  29393   -933  -1826    929       C  
ATOM    900  C   VAL A 256      34.290  23.539  70.115  1.00186.02           C  
ANISOU  900  C   VAL A 256    19660  23061  27957   -680  -2184    593       C  
ATOM    901  O   VAL A 256      34.194  22.718  69.227  1.00192.66           O  
ANISOU  901  O   VAL A 256    20399  23700  29101   -628  -2495    368       O  
ATOM    902  CB  VAL A 256      34.529  21.947  71.952  1.00202.12           C  
ANISOU  902  CB  VAL A 256    21474  24893  30429  -1105  -1787   1158       C  
ATOM    903  CG1 VAL A 256      35.965  22.298  72.361  1.00202.12           C  
ANISOU  903  CG1 VAL A 256    21865  25055  29877  -1072  -1665   1344       C  
ATOM    904  CG2 VAL A 256      33.755  21.201  73.047  1.00204.53           C  
ANISOU  904  CG2 VAL A 256    21462  25062  31186  -1359  -1511   1449       C  
ATOM    905  N   LEU A 257      34.901  24.703  69.936  1.00168.06           N  
ANISOU  905  N   LEU A 257    17712  21014  25129   -521  -2128    566       N  
ATOM    906  CA  LEU A 257      35.537  25.063  68.656  1.00152.79           C  
ANISOU  906  CA  LEU A 257    16059  19103  22889   -275  -2403    299       C  
ATOM    907  C   LEU A 257      36.771  24.226  68.358  1.00142.59           C  
ANISOU  907  C   LEU A 257    14945  17704  21525   -293  -2494    326       C  
ATOM    908  O   LEU A 257      37.714  24.217  69.149  1.00136.50           O  
ANISOU  908  O   LEU A 257    14327  17001  20535   -405  -2270    577       O  
ATOM    909  CB  LEU A 257      35.921  26.546  68.691  1.00149.31           C  
ANISOU  909  CB  LEU A 257    15921  18911  21899   -134  -2248    319       C  
ATOM    910  CG  LEU A 257      36.457  27.206  67.428  1.00148.88           C  
ANISOU  910  CG  LEU A 257    16186  18910  21472    136  -2454     81       C  
ATOM    911  CD1 LEU A 257      35.434  27.184  66.311  1.00154.86           C  
ANISOU  911  CD1 LEU A 257    16817  19589  22432    341  -2797   -242       C  
ATOM    912  CD2 LEU A 257      36.835  28.644  67.738  1.00147.87           C  
ANISOU  912  CD2 LEU A 257    16321  18993  20866    214  -2221    173       C  
ATOM    913  N   SER A 258      36.749  23.524  67.226  1.00140.90           N  
ANISOU  913  N   SER A 258    14703  17326  21504   -170  -2835     48       N  
ATOM    914  CA  SER A 258      37.849  22.631  66.841  1.00140.12           C  
ANISOU  914  CA  SER A 258    14741  17101  21395   -169  -2950     26       C  
ATOM    915  C   SER A 258      38.956  23.387  66.125  1.00140.12           C  
ANISOU  915  C   SER A 258    15138  17252  20845     30  -2961    -67       C  
ATOM    916  O   SER A 258      38.726  23.970  65.088  1.00136.18           O  
ANISOU  916  O   SER A 258    14778  16814  20150    262  -3139   -318       O  
ATOM    917  CB  SER A 258      37.369  21.490  65.928  1.00140.48           C  
ANISOU  917  CB  SER A 258    14578  16892  21904   -117  -3316   -259       C  
ATOM    918  OG  SER A 258      38.468  20.747  65.420  1.00135.94           O  
ANISOU  918  OG  SER A 258    14168  16214  21268    -69  -3442   -328       O  
ATOM    919  N   ALA A 259      40.171  23.296  66.667  1.00144.83           N  
ANISOU  919  N   ALA A 259    15912  17893  21223    -56  -2775    133       N  
ATOM    920  CA  ALA A 259      41.324  24.010  66.149  1.00143.91           C  
ANISOU  920  CA  ALA A 259    16144  17911  20622     91  -2715     82       C  
ATOM    921  C   ALA A 259      41.815  23.350  64.862  1.00146.94           C  
ANISOU  921  C   ALA A 259    16635  18175  21019    267  -2992   -197       C  
ATOM    922  O   ALA A 259      42.291  23.997  63.936  1.00150.39           O  
ANISOU  922  O   ALA A 259    17340  18705  21095    476  -3029   -359       O  
ATOM    923  CB  ALA A 259      42.427  24.032  67.197  1.00141.45           C  
ANISOU  923  CB  ALA A 259    15929  17669  20144    -65  -2453    361       C  
ATOM    924  N   THR A 260      41.692  22.045  64.805  1.00147.93           N  
ANISOU  924  N   THR A 260    16553  18083  21567    187  -3174   -252       N  
ATOM    925  CA  THR A 260      42.218  21.271  63.665  1.00152.29           C  
ANISOU  925  CA  THR A 260    17189  18506  22166    347  -3440   -529       C  
ATOM    926  C   THR A 260      41.347  21.398  62.449  1.00155.48           C  
ANISOU  926  C   THR A 260    17590  18891  22592    581  -3744   -878       C  
ATOM    927  O   THR A 260      41.907  21.469  61.350  1.00171.38           O  
ANISOU  927  O   THR A 260    19842  20936  24337    810  -3881  -1110       O  
ATOM    928  CB  THR A 260      42.522  19.812  63.998  1.00156.42           C  
ANISOU  928  CB  THR A 260    17514  18783  23134    196  -3540   -483       C  
ATOM    929  OG1 THR A 260      43.363  19.783  65.143  1.00160.80           O  
ANISOU  929  OG1 THR A 260    18106  19379  23610     13  -3267   -149       O  
ATOM    930  CG2 THR A 260      43.289  19.142  62.842  1.00157.56           C  
ANISOU  930  CG2 THR A 260    17793  18826  23245    381  -3774   -776       C  
ATOM    931  N   LYS A 261      40.028  21.491  62.598  1.00149.23           N  
ANISOU  931  N   LYS A 261    16553  18066  22080    550  -3845   -927       N  
ATOM    932  CA  LYS A 261      39.116  21.717  61.480  1.00151.64           C  
ANISOU  932  CA  LYS A 261    16846  18372  22398    797  -4165  -1274       C  
ATOM    933  C   LYS A 261      39.350  23.102  60.856  1.00144.87           C  
ANISOU  933  C   LYS A 261    16351  17750  20940   1044  -4088  -1319       C  
ATOM    934  O   LYS A 261      39.500  23.269  59.636  1.00144.35           O  
ANISOU  934  O   LYS A 261    16516  17720  20608   1330  -4303  -1587       O  
ATOM    935  CB  LYS A 261      37.675  21.621  61.966  1.00160.39           C  
ANISOU  935  CB  LYS A 261    17576  19404  23961    681  -4236  -1281       C  
ATOM    936  CG  LYS A 261      37.279  20.217  62.389  1.00173.65           C  
ANISOU  936  CG  LYS A 261    18877  20803  26295    462  -4345  -1280       C  
ATOM    937  CD  LYS A 261      35.803  20.112  62.761  1.00185.45           C  
ANISOU  937  CD  LYS A 261    19965  22205  28289    354  -4413  -1324       C  
ATOM    938  CE  LYS A 261      35.387  18.661  62.967  1.00194.78           C  
ANISOU  938  CE  LYS A 261    20771  23062  30174    160  -4557  -1376       C  
ATOM    939  NZ  LYS A 261      33.907  18.456  62.982  1.00200.33           N  
ANISOU  939  NZ  LYS A 261    21045  23635  31434    103  -4713  -1543       N  
ATOM    940  N   MET A 262      39.332  24.091  61.732  1.00140.98           N  
ANISOU  940  N   MET A 262    15907  17410  20248    934  -3776  -1051       N  
ATOM    941  CA  MET A 262      39.580  25.472  61.351  1.00142.17           C  
ANISOU  941  CA  MET A 262    16389  17759  19870   1122  -3639  -1031       C  
ATOM    942  C   MET A 262      40.913  25.585  60.621  1.00139.24           C  
ANISOU  942  C   MET A 262    16380  17434  19091   1262  -3575  -1074       C  
ATOM    943  O   MET A 262      41.004  26.152  59.535  1.00135.53           O  
ANISOU  943  O   MET A 262    16189  17033  18271   1541  -3676  -1248       O  
ATOM    944  CB  MET A 262      39.568  26.342  62.599  1.00144.19           C  
ANISOU  944  CB  MET A 262    16615  18142  20027    930  -3281   -718       C  
ATOM    945  CG  MET A 262      39.063  27.732  62.362  1.00148.98           C  
ANISOU  945  CG  MET A 262    17389  18900  20317   1101  -3216   -734       C  
ATOM    946  SD  MET A 262      38.386  28.444  63.850  1.00157.55           S  
ANISOU  946  SD  MET A 262    18261  20084  21516    876  -2917   -468       S  
ATOM    947  CE  MET A 262      38.019  30.107  63.293  1.00156.61           C  
ANISOU  947  CE  MET A 262    18416  20114  20973   1141  -2876   -533       C  
ATOM    948  N   LEU A 263      41.934  24.984  61.213  1.00140.47           N  
ANISOU  948  N   LEU A 263    16520  17542  19310   1075  -3409   -917       N  
ATOM    949  CA  LEU A 263      43.281  25.000  60.638  1.00144.38           C  
ANISOU  949  CA  LEU A 263    17305  18069  19483   1173  -3312   -950       C  
ATOM    950  C   LEU A 263      43.317  24.308  59.291  1.00145.06           C  
ANISOU  950  C   LEU A 263    17486  18071  19559   1419  -3623  -1281       C  
ATOM    951  O   LEU A 263      44.020  24.742  58.385  1.00144.94           O  
ANISOU  951  O   LEU A 263    17789  18132  19148   1632  -3578  -1385       O  
ATOM    952  CB  LEU A 263      44.318  24.393  61.583  1.00149.85           C  
ANISOU  952  CB  LEU A 263    17915  18713  20306    931  -3116   -739       C  
ATOM    953  CG  LEU A 263      45.790  24.636  61.192  1.00150.66           C  
ANISOU  953  CG  LEU A 263    18293  18877  20074   1001  -2936   -737       C  
ATOM    954  CD1 LEU A 263      46.223  26.083  61.408  1.00145.82           C  
ANISOU  954  CD1 LEU A 263    17913  18437  19051   1020  -2627   -589       C  
ATOM    955  CD2 LEU A 263      46.731  23.707  61.944  1.00149.70           C  
ANISOU  955  CD2 LEU A 263    18040  18663  20176    806  -2865   -609       C  
ATOM    956  N   SER A 264      42.540  23.246  59.135  1.00147.86           N  
ANISOU  956  N   SER A 264    17568  18262  20349   1400  -3935  -1458       N  
ATOM    957  CA  SER A 264      42.463  22.505  57.859  1.00155.09           C  
ANISOU  957  CA  SER A 264    18543  19087  21298   1647  -4286  -1825       C  
ATOM    958  C   SER A 264      41.810  23.292  56.744  1.00156.62           C  
ANISOU  958  C   SER A 264    18959  19394  21156   1982  -4478  -2056       C  
ATOM    959  O   SER A 264      42.297  23.276  55.610  1.00159.65           O  
ANISOU  959  O   SER A 264    19624  19817  21216   2255  -4589  -2273       O  
ATOM    960  CB  SER A 264      41.771  21.151  58.039  1.00161.96           C  
ANISOU  960  CB  SER A 264    19028  19721  22786   1522  -4579  -1969       C  
ATOM    961  OG  SER A 264      42.587  20.292  58.821  1.00168.91           O  
ANISOU  961  OG  SER A 264    19782  20474  23919   1280  -4435  -1787       O  
ATOM    962  N   LYS A 265      40.714  23.982  57.043  1.00157.89           N  
ANISOU  962  N   LYS A 265    19005  19609  21377   1983  -4517  -2013       N  
ATOM    963  CA  LYS A 265      40.052  24.823  56.037  1.00162.25           C  
ANISOU  963  CA  LYS A 265    19779  20271  21595   2323  -4709  -2209       C  
ATOM    964  C   LYS A 265      40.951  26.002  55.653  1.00155.37           C  
ANISOU  964  C   LYS A 265    19366  19571  20096   2479  -4408  -2060       C  
ATOM    965  O   LYS A 265      41.098  26.330  54.473  1.00162.24           O  
ANISOU  965  O   LYS A 265    20566  20508  20570   2810  -4533  -2243       O  
ATOM    966  CB  LYS A 265      38.686  25.316  56.527  1.00170.86           C  
ANISOU  966  CB  LYS A 265    20613  21374  22930   2280  -4804  -2189       C  
ATOM    967  CG  LYS A 265      37.772  25.884  55.442  1.00179.30           C  
ANISOU  967  CG  LYS A 265    21819  22510  23795   2653  -5138  -2468       C  
ATOM    968  CD  LYS A 265      37.229  24.796  54.504  1.00187.42           C  
ANISOU  968  CD  LYS A 265    22700  23410  25097   2839  -5635  -2889       C  
ATOM    969  CE  LYS A 265      36.208  25.323  53.504  1.00189.38           C  
ANISOU  969  CE  LYS A 265    23045  23726  25184   3221  -6021  -3187       C  
ATOM    970  NZ  LYS A 265      34.915  25.701  54.138  1.00188.14           N  
ANISOU  970  NZ  LYS A 265    22532  23553  25398   3128  -6104  -3172       N  
ATOM    971  N   PHE A 266      41.543  26.626  56.659  1.00141.89           N  
ANISOU  971  N   PHE A 266    17677  17925  18310   2242  -4009  -1730       N  
ATOM    972  CA  PHE A 266      42.515  27.698  56.493  1.00135.59           C  
ANISOU  972  CA  PHE A 266    17255  17250  17010   2314  -3665  -1558       C  
ATOM    973  C   PHE A 266      43.622  27.262  55.508  1.00134.92           C  
ANISOU  973  C   PHE A 266    17445  17160  16657   2483  -3652  -1696       C  
ATOM    974  O   PHE A 266      43.936  27.947  54.522  1.00134.66           O  
ANISOU  974  O   PHE A 266    17789  17209  16165   2761  -3598  -1757       O  
ATOM    975  CB  PHE A 266      43.117  27.994  57.873  1.00129.07           C  
ANISOU  975  CB  PHE A 266    16302  16448  16290   1973  -3292  -1234       C  
ATOM    976  CG  PHE A 266      43.818  29.320  57.995  1.00126.71           C  
ANISOU  976  CG  PHE A 266    16300  16264  15579   1993  -2928  -1036       C  
ATOM    977  CD1 PHE A 266      43.115  30.501  57.830  1.00125.93           C  
ANISOU  977  CD1 PHE A 266    16346  16240  15260   2139  -2895   -995       C  
ATOM    978  CD2 PHE A 266      45.165  29.394  58.368  1.00126.13           C  
ANISOU  978  CD2 PHE A 266    16327  16206  15390   1848  -2614   -887       C  
ATOM    979  CE1 PHE A 266      43.742  31.748  57.980  1.00125.09           C  
ANISOU  979  CE1 PHE A 266    16501  16206  14819   2143  -2548   -808       C  
ATOM    980  CE2 PHE A 266      45.801  30.632  58.493  1.00124.73           C  
ANISOU  980  CE2 PHE A 266    16394  16108  14887   1850  -2274   -721       C  
ATOM    981  CZ  PHE A 266      45.091  31.812  58.288  1.00124.02           C  
ANISOU  981  CZ  PHE A 266    16465  16076  14579   1995  -2235   -677       C  
ATOM    982  N   ARG A 267      44.183  26.094  55.793  1.00133.00           N  
ANISOU  982  N   ARG A 267    17007  16810  16715   2319  -3695  -1741       N  
ATOM    983  CA  ARG A 267      45.239  25.525  54.988  1.00137.35           C  
ANISOU  983  CA  ARG A 267    17750  17341  17093   2448  -3681  -1886       C  
ATOM    984  C   ARG A 267      44.795  25.282  53.556  1.00137.04           C  
ANISOU  984  C   ARG A 267    17912  17312  16845   2825  -4015  -2229       C  
ATOM    985  O   ARG A 267      45.511  25.608  52.610  1.00129.64           O  
ANISOU  985  O   ARG A 267    17333  16453  15471   3064  -3906  -2305       O  
ATOM    986  CB  ARG A 267      45.757  24.253  55.658  1.00145.00           C  
ANISOU  986  CB  ARG A 267    18422  18167  18503   2198  -3714  -1877       C  
ATOM    987  CG  ARG A 267      47.183  23.842  55.280  1.00147.77           C  
ANISOU  987  CG  ARG A 267    18933  18510  18703   2227  -3542  -1915       C  
ATOM    988  CD  ARG A 267      47.632  22.649  56.098  1.00147.81           C  
ANISOU  988  CD  ARG A 267    18627  18361  19171   1972  -3580  -1867       C  
ATOM    989  NE  ARG A 267      48.731  21.967  55.431  1.00152.18           N  
ANISOU  989  NE  ARG A 267    19292  18873  19655   2080  -3565  -2035       N  
ATOM    990  CZ  ARG A 267      50.011  22.333  55.481  1.00155.61           C  
ANISOU  990  CZ  ARG A 267    19885  19377  19861   2051  -3235  -1926       C  
ATOM    991  NH1 ARG A 267      50.377  23.404  56.170  1.00155.40           N  
ANISOU  991  NH1 ARG A 267    19932  19461  19650   1915  -2901  -1653       N  
ATOM    992  NH2 ARG A 267      50.939  21.624  54.825  1.00158.10           N  
ANISOU  992  NH2 ARG A 267    20271  19647  20152   2165  -3241  -2115       N  
ATOM    993  N   LYS A 268      43.597  24.738  53.401  1.00142.73           N  
ANISOU  993  N   LYS A 268    18401  17956  17874   2887  -4417  -2440       N  
ATOM    994  CA  LYS A 268      43.000  24.469  52.078  1.00149.65           C  
ANISOU  994  CA  LYS A 268    19428  18841  18588   3266  -4819  -2814       C  
ATOM    995  C   LYS A 268      42.877  25.731  51.236  1.00151.43           C  
ANISOU  995  C   LYS A 268    20089  19234  18214   3596  -4748  -2796       C  
ATOM    996  O   LYS A 268      43.302  25.763  50.077  1.00154.27           O  
ANISOU  996  O   LYS A 268    20801  19661  18152   3921  -4807  -2975       O  
ATOM    997  CB  LYS A 268      41.576  23.870  52.276  1.00153.01           C  
ANISOU  997  CB  LYS A 268    19461  19151  19522   3230  -5245  -3014       C  
ATOM    998  CG  LYS A 268      41.118  22.819  51.263  1.00159.58           C  
ANISOU  998  CG  LYS A 268    20224  19887  20522   3472  -5739  -3468       C  
ATOM    999  CD  LYS A 268      39.661  23.004  50.818  1.00166.07           C  
ANISOU  999  CD  LYS A 268    20917  20709  21471   3681  -6168  -3723       C  
ATOM   1000  CE  LYS A 268      38.692  22.103  51.568  1.00170.92           C  
ANISOU 1000  CE  LYS A 268    20973  21122  22845   3414  -6408  -3813       C  
ATOM   1001  NZ  LYS A 268      38.580  20.721  50.983  1.00176.73           N  
ANISOU 1001  NZ  LYS A 268    21512  21674  23960   3481  -6810  -4211       N  
ATOM   1002  N   ILE A 269      42.288  26.772  51.812  1.00150.54           N  
ANISOU 1002  N   ILE A 269    19961  19181  18053   3528  -4615  -2576       N  
ATOM   1003  CA  ILE A 269      42.180  28.080  51.147  1.00153.67           C  
ANISOU 1003  CA  ILE A 269    20774  19711  17903   3819  -4506  -2497       C  
ATOM   1004  C   ILE A 269      43.558  28.582  50.714  1.00154.97           C  
ANISOU 1004  C   ILE A 269    21345  19945  17589   3886  -4093  -2341       C  
ATOM   1005  O   ILE A 269      43.759  28.942  49.546  1.00163.34           O  
ANISOU 1005  O   ILE A 269    22816  21081  18164   4245  -4121  -2449       O  
ATOM   1006  CB  ILE A 269      41.595  29.133  52.110  1.00152.26           C  
ANISOU 1006  CB  ILE A 269    20483  19564  17804   3646  -4316  -2223       C  
ATOM   1007  CG1 ILE A 269      40.169  28.743  52.546  1.00153.02           C  
ANISOU 1007  CG1 ILE A 269    20163  19597  18379   3585  -4684  -2369       C  
ATOM   1008  CG2 ILE A 269      41.612  30.530  51.482  1.00156.34           C  
ANISOU 1008  CG2 ILE A 269    21448  20186  17767   3928  -4153  -2100       C  
ATOM   1009  CD1 ILE A 269      39.800  29.194  53.940  1.00149.69           C  
ANISOU 1009  CD1 ILE A 269    19440  19165  18266   3244  -4449  -2096       C  
ATOM   1010  N   ILE A 270      44.504  28.608  51.651  1.00149.88           N  
ANISOU 1010  N   ILE A 270    20587  19274  17084   3550  -3706  -2091       N  
ATOM   1011  CA  ILE A 270      45.854  29.083  51.352  1.00152.46           C  
ANISOU 1011  CA  ILE A 270    21234  19650  17043   3567  -3282  -1942       C  
ATOM   1012  C   ILE A 270      46.507  28.309  50.184  1.00158.78           C  
ANISOU 1012  C   ILE A 270    22250  20459  17619   3820  -3378  -2199       C  
ATOM   1013  O   ILE A 270      47.113  28.920  49.300  1.00164.92           O  
ANISOU 1013  O   ILE A 270    23444  21313  17905   4063  -3159  -2172       O  
ATOM   1014  CB  ILE A 270      46.708  29.019  52.619  1.00147.92           C  
ANISOU 1014  CB  ILE A 270    20415  19033  16753   3156  -2940  -1696       C  
ATOM   1015  CG1 ILE A 270      46.239  30.082  53.597  1.00146.65           C  
ANISOU 1015  CG1 ILE A 270    20172  18901  16647   2976  -2758  -1433       C  
ATOM   1016  CG2 ILE A 270      48.177  29.257  52.310  1.00150.12           C  
ANISOU 1016  CG2 ILE A 270    20939  19338  16762   3151  -2538  -1605       C  
ATOM   1017  CD1 ILE A 270      46.588  29.804  55.042  1.00149.05           C  
ANISOU 1017  CD1 ILE A 270    20127  19164  17341   2573  -2589  -1244       C  
ATOM   1018  N   LYS A 271      46.381  26.985  50.185  1.00157.83           N  
ANISOU 1018  N   LYS A 271    21854  20252  17861   3767  -3688  -2442       N  
ATOM   1019  CA  LYS A 271      46.935  26.186  49.099  1.00160.24           C  
ANISOU 1019  CA  LYS A 271    22338  20561  17984   4017  -3814  -2728       C  
ATOM   1020  C   LYS A 271      46.279  26.531  47.761  1.00162.16           C  
ANISOU 1020  C   LYS A 271    22946  20899  17765   4487  -4082  -2957       C  
ATOM   1021  O   LYS A 271      46.963  26.661  46.727  1.00163.50           O  
ANISOU 1021  O   LYS A 271    23507  21153  17463   4771  -3949  -3043       O  
ATOM   1022  CB  LYS A 271      46.763  24.688  49.379  1.00164.43           C  
ANISOU 1022  CB  LYS A 271    22475  20948  19050   3877  -4150  -2970       C  
ATOM   1023  CG  LYS A 271      47.689  24.101  50.441  1.00163.50           C  
ANISOU 1023  CG  LYS A 271    22073  20733  19316   3495  -3901  -2794       C  
ATOM   1024  CD  LYS A 271      47.381  22.613  50.674  1.00166.14           C  
ANISOU 1024  CD  LYS A 271    22032  20893  20201   3381  -4266  -3026       C  
ATOM   1025  CE  LYS A 271      48.566  21.849  51.258  1.00164.09           C  
ANISOU 1025  CE  LYS A 271    21610  20538  20195   3145  -4058  -2946       C  
ATOM   1026  NZ  LYS A 271      48.569  20.389  50.919  1.00164.40           N  
ANISOU 1026  NZ  LYS A 271    21449  20414  20602   3186  -4399  -3264       N  
ATOM   1027  N   GLU A 272      44.956  26.674  47.793  1.00163.94           N  
ANISOU 1027  N   GLU A 272    23043  21117  18129   4577  -4457  -3057       N  
ATOM   1028  CA  GLU A 272      44.192  27.054  46.605  1.00173.44           C  
ANISOU 1028  CA  GLU A 272    24571  22412  18913   5040  -4774  -3277       C  
ATOM   1029  C   GLU A 272      44.704  28.344  46.005  1.00174.89           C  
ANISOU 1029  C   GLU A 272    25285  22721  18444   5272  -4402  -3043       C  
ATOM   1030  O   GLU A 272      44.998  28.401  44.811  1.00179.79           O  
ANISOU 1030  O   GLU A 272    26321  23431  18559   5656  -4434  -3191       O  
ATOM   1031  CB  GLU A 272      42.689  27.227  46.934  1.00180.97           C  
ANISOU 1031  CB  GLU A 272    25261  23335  20161   5056  -5176  -3363       C  
ATOM   1032  CG  GLU A 272      41.855  25.947  47.045  1.00188.08           C  
ANISOU 1032  CG  GLU A 272    25714  24111  21635   4994  -5688  -3715       C  
ATOM   1033  CD  GLU A 272      40.351  26.207  47.280  1.00191.24           C  
ANISOU 1033  CD  GLU A 272    25856  24487  22319   5039  -6067  -3817       C  
ATOM   1034  OE1 GLU A 272      39.637  25.306  47.775  1.00189.97           O  
ANISOU 1034  OE1 GLU A 272    25221  24189  22769   4848  -6369  -3997       O  
ATOM   1035  OE2 GLU A 272      39.858  27.337  46.983  1.00191.81           O  
ANISOU 1035  OE2 GLU A 272    26187  24664  22028   5264  -6055  -3712       O  
ATOM   1036  N   GLU A 273      44.819  29.380  46.825  1.00173.41           N  
ANISOU 1036  N   GLU A 273    25091  22532  18263   5047  -4039  -2677       N  
ATOM   1037  CA  GLU A 273      45.307  30.669  46.327  1.00177.87           C  
ANISOU 1037  CA  GLU A 273    26144  23175  18262   5235  -3649  -2421       C  
ATOM   1038  C   GLU A 273      46.768  30.599  45.883  1.00179.55           C  
ANISOU 1038  C   GLU A 273    26622  23413  18184   5238  -3206  -2342       C  
ATOM   1039  O   GLU A 273      47.153  31.239  44.890  1.00185.10           O  
ANISOU 1039  O   GLU A 273    27818  24191  18321   5559  -3006  -2286       O  
ATOM   1040  CB  GLU A 273      45.149  31.750  47.401  1.00177.02           C  
ANISOU 1040  CB  GLU A 273    25924  23034  18301   4957  -3354  -2069       C  
ATOM   1041  CG  GLU A 273      45.438  33.184  46.945  1.00180.77           C  
ANISOU 1041  CG  GLU A 273    26878  23549  18257   5151  -2989  -1796       C  
ATOM   1042  CD  GLU A 273      44.666  33.587  45.691  1.00185.49           C  
ANISOU 1042  CD  GLU A 273    27892  24220  18365   5672  -3292  -1935       C  
ATOM   1043  OE1 GLU A 273      43.516  33.144  45.501  1.00185.48           O  
ANISOU 1043  OE1 GLU A 273    27726  24235  18513   5839  -3824  -2195       O  
ATOM   1044  OE2 GLU A 273      45.223  34.352  44.888  1.00188.08           O  
ANISOU 1044  OE2 GLU A 273    28718  24585  18159   5924  -2993  -1782       O  
ATOM   1045  N   VAL A 274      47.577  29.811  46.592  1.00176.60           N  
ANISOU 1045  N   VAL A 274    25930  22974  18196   4898  -3050  -2339       N  
ATOM   1046  CA  VAL A 274      49.002  29.666  46.268  1.00176.42           C  
ANISOU 1046  CA  VAL A 274    26081  22964  17985   4868  -2627  -2286       C  
ATOM   1047  C   VAL A 274      49.211  29.021  44.896  1.00183.73           C  
ANISOU 1047  C   VAL A 274    27312  23963  18534   5271  -2797  -2596       C  
ATOM   1048  O   VAL A 274      50.177  29.335  44.187  1.00187.29           O  
ANISOU 1048  O   VAL A 274    28116  24471  18574   5425  -2416  -2533       O  
ATOM   1049  CB  VAL A 274      49.760  28.879  47.370  1.00168.85           C  
ANISOU 1049  CB  VAL A 274    24678  21914  17564   4433  -2492  -2244       C  
ATOM   1050  CG1 VAL A 274      51.111  28.369  46.896  1.00168.40           C  
ANISOU 1050  CG1 VAL A 274    24727  21864  17390   4452  -2199  -2318       C  
ATOM   1051  CG2 VAL A 274      49.968  29.763  48.588  1.00164.62           C  
ANISOU 1051  CG2 VAL A 274    23976  21340  17230   4076  -2156  -1894       C  
ATOM   1052  N   LYS A 275      48.316  28.118  44.523  1.00186.40           N  
ANISOU 1052  N   LYS A 275    27509  24295  19018   5445  -3356  -2942       N  
ATOM   1053  CA  LYS A 275      48.341  27.559  43.164  1.00189.01           C  
ANISOU 1053  CA  LYS A 275    28155  24709  18949   5887  -3593  -3283       C  
ATOM   1054  C   LYS A 275      48.176  28.637  42.094  1.00190.63           C  
ANISOU 1054  C   LYS A 275    28951  25045  18432   6322  -3475  -3189       C  
ATOM   1055  O   LYS A 275      48.733  28.521  41.011  1.00193.07           O  
ANISOU 1055  O   LYS A 275    29652  25449  18255   6653  -3368  -3315       O  
ATOM   1056  CB  LYS A 275      47.309  26.437  43.044  1.00193.75           C  
ANISOU 1056  CB  LYS A 275    28450  25256  19909   5975  -4257  -3691       C  
ATOM   1057  CG  LYS A 275      47.785  25.203  43.836  1.00194.51           C  
ANISOU 1057  CG  LYS A 275    28060  25211  20633   5609  -4303  -3801       C  
ATOM   1058  CD  LYS A 275      46.740  24.150  44.144  1.00198.02           C  
ANISOU 1058  CD  LYS A 275    28068  25532  21639   5535  -4884  -4107       C  
ATOM   1059  CE  LYS A 275      47.365  23.058  45.010  1.00197.48           C  
ANISOU 1059  CE  LYS A 275    27566  25302  22164   5151  -4827  -4120       C  
ATOM   1060  NZ  LYS A 275      46.810  21.669  44.835  1.00200.82           N  
ANISOU 1060  NZ  LYS A 275    27670  25584  23047   5182  -5353  -4534       N  
ATOM   1061  N   GLU A 276      47.467  29.704  42.425  1.00193.66           N  
ANISOU 1061  N   GLU A 276    29409  25429  18741   6318  -3458  -2947       N  
ATOM   1062  CA  GLU A 276      47.157  30.759  41.458  1.00205.45           C  
ANISOU 1062  CA  GLU A 276    31463  27022  19575   6748  -3399  -2837       C  
ATOM   1063  C   GLU A 276      48.245  31.802  41.298  1.00208.06           C  
ANISOU 1063  C   GLU A 276    32180  27364  19510   6724  -2709  -2454       C  
ATOM   1064  O   GLU A 276      48.148  32.694  40.451  1.00212.12           O  
ANISOU 1064  O   GLU A 276    33211  27943  19440   7084  -2574  -2316       O  
ATOM   1065  CB  GLU A 276      45.802  31.424  41.762  1.00208.76           C  
ANISOU 1065  CB  GLU A 276    31808  27427  20084   6821  -3751  -2790       C  
ATOM   1066  CG  GLU A 276      44.620  30.494  41.516  1.00212.77           C  
ANISOU 1066  CG  GLU A 276    32055  27942  20846   6997  -4475  -3223       C  
ATOM   1067  CD  GLU A 276      44.601  29.907  40.102  1.00218.40           C  
ANISOU 1067  CD  GLU A 276    33132  28769  21078   7507  -4790  -3591       C  
ATOM   1068  OE1 GLU A 276      44.388  30.656  39.119  1.00223.54           O  
ANISOU 1068  OE1 GLU A 276    34315  29529  21087   7962  -4809  -3553       O  
ATOM   1069  OE2 GLU A 276      44.811  28.687  39.971  1.00215.97           O  
ANISOU 1069  OE2 GLU A 276    32592  28440  21026   7467  -5020  -3923       O  
ATOM   1070  N   ILE A 277      49.311  31.688  42.101  1.00206.78           N  
ANISOU 1070  N   ILE A 277    31767  27126  19671   6306  -2263  -2281       N  
ATOM   1071  CA  ILE A 277      50.478  32.570  41.979  1.00208.37           C  
ANISOU 1071  CA  ILE A 277    32267  27315  19587   6239  -1577  -1952       C  
ATOM   1072  C   ILE A 277      51.488  32.057  40.959  1.00207.21           C  
ANISOU 1072  C   ILE A 277    32415  27246  19070   6467  -1329  -2092       C  
ATOM   1073  O   ILE A 277      52.175  31.080  41.205  1.00204.78           O  
ANISOU 1073  O   ILE A 277    31817  26919  19069   6278  -1304  -2269       O  
ATOM   1074  CB  ILE A 277      51.156  32.743  43.333  1.00209.01           C  
ANISOU 1074  CB  ILE A 277    31929  27283  20201   5696  -1227  -1723       C  
ATOM   1075  CG1 ILE A 277      50.160  33.380  44.312  1.00212.17           C  
ANISOU 1075  CG1 ILE A 277    32090  27622  20903   5500  -1417  -1566       C  
ATOM   1076  CG2 ILE A 277      52.404  33.594  43.203  1.00207.91           C  
ANISOU 1076  CG2 ILE A 277    32046  27110  19838   5610   -526  -1426       C  
ATOM   1077  CD1 ILE A 277      50.411  33.077  45.778  1.00210.58           C  
ANISOU 1077  CD1 ILE A 277    31343  27333  21333   4987  -1352  -1483       C  
ATOM   1078  N   LYS A 278      51.596  32.778  39.844  1.00208.41           N  
ANISOU 1078  N   LYS A 278    33154  27477  18555   6873  -1113  -1986       N  
ATOM   1079  CA  LYS A 278      52.350  32.361  38.661  1.00215.11           C  
ANISOU 1079  CA  LYS A 278    34383  28433  18914   7207   -917  -2139       C  
ATOM   1080  C   LYS A 278      53.674  33.118  38.490  1.00213.24           C  
ANISOU 1080  C   LYS A 278    34402  28161  18455   7107   -116  -1810       C  
ATOM   1081  O   LYS A 278      54.591  32.638  37.794  1.00221.69           O  
ANISOU 1081  O   LYS A 278    35639  29298  19291   7240    166  -1927       O  
ATOM   1082  CB  LYS A 278      51.479  32.592  37.408  1.00226.95           C  
ANISOU 1082  CB  LYS A 278    36417  30064  19746   7807  -1264  -2270       C  
ATOM   1083  CG  LYS A 278      49.973  32.308  37.519  1.00230.69           C  
ANISOU 1083  CG  LYS A 278    36719  30556  20373   7959  -2028  -2515       C  
ATOM   1084  CD  LYS A 278      49.586  30.826  37.456  1.00233.13           C  
ANISOU 1084  CD  LYS A 278    36669  30898  21010   7988  -2616  -3020       C  
ATOM   1085  CE  LYS A 278      48.121  30.649  37.080  1.00235.55           C  
ANISOU 1085  CE  LYS A 278    36986  31255  21254   8318  -3351  -3304       C  
ATOM   1086  NZ  LYS A 278      47.749  29.221  36.877  1.00235.97           N  
ANISOU 1086  NZ  LYS A 278    36728  31323  21605   8389  -3924  -3825       N  
ATOM   1087  N   ASP A 279      53.737  34.278  39.117  1.00204.84           N  
ANISOU 1087  N   ASP A 279    33354  26988  17488   6880    233  -1423       N  
ATOM   1088  CA  ASP A 279      54.907  35.180  38.968  1.00203.94           C  
ANISOU 1088  CA  ASP A 279    33490  26804  17193   6778   1015  -1078       C  
ATOM   1089  C   ASP A 279      55.926  34.999  40.085  1.00196.03           C  
ANISOU 1089  C   ASP A 279    31979  25687  16813   6235   1368  -1004       C  
ATOM   1090  O   ASP A 279      57.073  35.441  39.968  1.00198.01           O  
ANISOU 1090  O   ASP A 279    32329  25882  17023   6114   2000   -817       O  
ATOM   1091  CB  ASP A 279      54.436  36.633  38.923  1.00204.38           C  
ANISOU 1091  CB  ASP A 279    33898  26777  16978   6873   1222   -695       C  
ATOM   1092  CG  ASP A 279      53.722  37.053  40.177  1.00198.61           C  
ANISOU 1092  CG  ASP A 279    32762  25936  16762   6530    984   -588       C  
ATOM   1093  OD1 ASP A 279      52.878  36.270  40.634  1.00194.03           O  
ANISOU 1093  OD1 ASP A 279    31832  25403  16487   6479    392   -853       O  
ATOM   1094  OD2 ASP A 279      54.006  38.150  40.694  1.00197.22           O  
ANISOU 1094  OD2 ASP A 279    32616  25624  16694   6315   1398   -250       O  
ATOM   1095  N   ILE A 280      55.520  34.352  41.165  1.00188.82           N  
ANISOU 1095  N   ILE A 280    30523  24736  16481   5914    968  -1152       N  
ATOM   1096  CA  ILE A 280      56.448  34.084  42.279  1.00188.37           C  
ANISOU 1096  CA  ILE A 280    29969  24584  17017   5421   1226  -1110       C  
ATOM   1097  C   ILE A 280      56.542  32.577  42.529  1.00184.16           C  
ANISOU 1097  C   ILE A 280    29037  24092  16843   5332    834  -1473       C  
ATOM   1098  O   ILE A 280      55.542  31.850  42.426  1.00179.60           O  
ANISOU 1098  O   ILE A 280    28370  23564  16303   5482    244  -1718       O  
ATOM   1099  CB  ILE A 280      56.026  34.796  43.576  1.00190.09           C  
ANISOU 1099  CB  ILE A 280    29874  24690  17659   5053   1195   -888       C  
ATOM   1100  CG1 ILE A 280      55.779  36.306  43.341  1.00195.92           C  
ANISOU 1100  CG1 ILE A 280    31008  25362  18071   5160   1518   -542       C  
ATOM   1101  CG2 ILE A 280      57.075  34.558  44.658  1.00187.41           C  
ANISOU 1101  CG2 ILE A 280    29070  24265  17871   4587   1476   -850       C  
ATOM   1102  CD1 ILE A 280      56.991  37.129  42.916  1.00200.13           C  
ANISOU 1102  CD1 ILE A 280    31813  25817  18409   5130   2256   -293       C  
ATOM   1103  N   ASP A 281      57.749  32.112  42.854  1.00183.57           N  
ANISOU 1103  N   ASP A 281    28710  23979  17058   5089   1162  -1514       N  
ATOM   1104  CA  ASP A 281      57.951  30.731  43.257  1.00181.72           C  
ANISOU 1104  CA  ASP A 281    28056  23744  17244   4952    833  -1818       C  
ATOM   1105  C   ASP A 281      57.630  30.614  44.747  1.00172.29           C  
ANISOU 1105  C   ASP A 281    26354  22453  16655   4527    610  -1735       C  
ATOM   1106  O   ASP A 281      58.491  30.788  45.624  1.00172.83           O  
ANISOU 1106  O   ASP A 281    26135  22445  17087   4179    917  -1602       O  
ATOM   1107  CB  ASP A 281      59.362  30.222  42.971  1.00188.28           C  
ANISOU 1107  CB  ASP A 281    28818  24575  18142   4900   1243  -1921       C  
ATOM   1108  CG  ASP A 281      59.478  28.696  43.135  1.00190.32           C  
ANISOU 1108  CG  ASP A 281    28721  24832  18756   4864    843  -2281       C  
ATOM   1109  OD1 ASP A 281      58.487  28.037  43.547  1.00187.55           O  
ANISOU 1109  OD1 ASP A 281    28153  24462  18644   4839    269  -2430       O  
ATOM   1110  OD2 ASP A 281      60.561  28.152  42.833  1.00197.51           O  
ANISOU 1110  OD2 ASP A 281    29567  25749  19726   4864   1113  -2419       O  
ATOM   1111  N   VAL A 282      56.361  30.322  45.012  1.00164.04           N  
ANISOU 1111  N   VAL A 282    25203  21414  15707   4574     67  -1824       N  
ATOM   1112  CA  VAL A 282      55.891  30.115  46.375  1.00155.66           C  
ANISOU 1112  CA  VAL A 282    23681  20276  15186   4211   -185  -1760       C  
ATOM   1113  C   VAL A 282      55.179  28.775  46.475  1.00153.86           C  
ANISOU 1113  C   VAL A 282    23177  20037  15245   4243   -767  -2063       C  
ATOM   1114  O   VAL A 282      54.372  28.410  45.611  1.00150.03           O  
ANISOU 1114  O   VAL A 282    22883  19607  14513   4570  -1130  -2280       O  
ATOM   1115  CB  VAL A 282      54.965  31.251  46.854  1.00152.95           C  
ANISOU 1115  CB  VAL A 282    23413  19918  14780   4161   -217  -1511       C  
ATOM   1116  CG1 VAL A 282      53.783  31.445  45.933  1.00155.26           C  
ANISOU 1116  CG1 VAL A 282    24034  20281  14675   4554   -565  -1609       C  
ATOM   1117  CG2 VAL A 282      54.493  30.998  48.273  1.00148.51           C  
ANISOU 1117  CG2 VAL A 282    22379  19291  14756   3796   -453  -1452       C  
ATOM   1118  N   SER A 283      55.459  28.033  47.534  1.00155.76           N  
ANISOU 1118  N   SER A 283    22965  20194  16019   3912   -871  -2083       N  
ATOM   1119  CA  SER A 283      54.750  26.786  47.793  1.00160.94           C  
ANISOU 1119  CA  SER A 283    23318  20796  17036   3886  -1402  -2327       C  
ATOM   1120  C   SER A 283      54.368  26.669  49.258  1.00159.09           C  
ANISOU 1120  C   SER A 283    22660  20475  17312   3504  -1532  -2163       C  
ATOM   1121  O   SER A 283      54.872  27.420  50.101  1.00158.46           O  
ANISOU 1121  O   SER A 283    22494  20385  17325   3249  -1204  -1900       O  
ATOM   1122  CB  SER A 283      55.558  25.589  47.331  1.00166.52           C  
ANISOU 1122  CB  SER A 283    23936  21474  17860   3958  -1451  -2603       C  
ATOM   1123  OG  SER A 283      56.672  25.376  48.177  1.00169.63           O  
ANISOU 1123  OG  SER A 283    24055  21802  18594   3650  -1168  -2492       O  
ATOM   1124  N   VAL A 284      53.492  25.716  49.572  1.00160.15           N  
ANISOU 1124  N   VAL A 284    22524  20540  17786   3464  -2003  -2325       N  
ATOM   1125  CA  VAL A 284      53.098  25.436  50.954  1.00161.26           C  
ANISOU 1125  CA  VAL A 284    22257  20592  18420   3113  -2134  -2176       C  
ATOM   1126  C   VAL A 284      53.974  24.327  51.552  1.00166.48           C  
ANISOU 1126  C   VAL A 284    22609  21149  19494   2904  -2138  -2234       C  
ATOM   1127  O   VAL A 284      54.098  23.254  50.978  1.00171.55           O  
ANISOU 1127  O   VAL A 284    23203  21731  20245   3036  -2367  -2504       O  
ATOM   1128  CB  VAL A 284      51.608  25.061  51.071  1.00163.14           C  
ANISOU 1128  CB  VAL A 284    22342  20789  18855   3154  -2606  -2280       C  
ATOM   1129  CG1 VAL A 284      51.245  24.621  52.491  1.00159.68           C  
ANISOU 1129  CG1 VAL A 284    21477  20249  18942   2793  -2713  -2125       C  
ATOM   1130  CG2 VAL A 284      50.749  26.238  50.643  1.00165.29           C  
ANISOU 1130  CG2 VAL A 284    22888  21160  18755   3344  -2601  -2194       C  
ATOM   1131  N   GLU A 285      54.573  24.600  52.710  1.00172.43           N  
ANISOU 1131  N   GLU A 285    23157  21878  20477   2593  -1903  -1992       N  
ATOM   1132  CA  GLU A 285      55.366  23.621  53.428  1.00174.56           C  
ANISOU 1132  CA  GLU A 285    23125  22046  21151   2388  -1923  -2008       C  
ATOM   1133  C   GLU A 285      54.460  22.596  54.098  1.00167.95           C  
ANISOU 1133  C   GLU A 285    21975  21082  20756   2260  -2335  -2045       C  
ATOM   1134  O   GLU A 285      53.356  22.906  54.535  1.00164.12           O  
ANISOU 1134  O   GLU A 285    21420  20600  20336   2194  -2491  -1942       O  
ATOM   1135  CB  GLU A 285      56.287  24.282  54.444  1.00181.76           C  
ANISOU 1135  CB  GLU A 285    23931  22983  22144   2126  -1564  -1753       C  
ATOM   1136  CG  GLU A 285      57.383  23.349  54.979  1.00191.58           C  
ANISOU 1136  CG  GLU A 285    24923  24139  23729   1981  -1540  -1797       C  
ATOM   1137  CD  GLU A 285      57.595  23.427  56.487  1.00199.77           C  
ANISOU 1137  CD  GLU A 285    25685  25146  25069   1668  -1499  -1553       C  
ATOM   1138  OE1 GLU A 285      56.616  23.652  57.237  1.00201.28           O  
ANISOU 1138  OE1 GLU A 285    25785  25339  25351   1544  -1640  -1394       O  
ATOM   1139  OE2 GLU A 285      58.752  23.254  56.930  1.00210.89           O  
ANISOU 1139  OE2 GLU A 285    26968  26535  26626   1558  -1329  -1532       O  
ATOM   1140  N   LYS A 286      54.910  21.348  54.143  1.00164.06           N  
ANISOU 1140  N   LYS A 286    21287  20461  20585   2232  -2507  -2200       N  
ATOM   1141  CA  LYS A 286      54.201  20.286  54.865  1.00162.50           C  
ANISOU 1141  CA  LYS A 286    20770  20098  20873   2077  -2854  -2205       C  
ATOM   1142  C   LYS A 286      54.022  20.660  56.328  1.00154.68           C  
ANISOU 1142  C   LYS A 286    19575  19104  20091   1766  -2749  -1866       C  
ATOM   1143  O   LYS A 286      54.918  21.223  56.945  1.00147.77           O  
ANISOU 1143  O   LYS A 286    18704  18298  19144   1633  -2450  -1682       O  
ATOM   1144  CB  LYS A 286      54.956  18.961  54.724  1.00167.41           C  
ANISOU 1144  CB  LYS A 286    21236  20567  21805   2093  -2992  -2397       C  
ATOM   1145  CG  LYS A 286      54.170  17.717  55.135  1.00174.81           C  
ANISOU 1145  CG  LYS A 286    21883  21288  23247   1999  -3386  -2471       C  
ATOM   1146  CD  LYS A 286      55.056  16.508  55.037  1.00183.45           C  
ANISOU 1146  CD  LYS A 286    22841  22221  24640   2016  -3481  -2638       C  
ATOM   1147  CE  LYS A 286      56.055  16.377  56.196  1.00186.96           C  
ANISOU 1147  CE  LYS A 286    23114  22623  25297   1779  -3283  -2380       C  
ATOM   1148  NZ  LYS A 286      56.944  15.179  56.095  1.00190.48           N  
ANISOU 1148  NZ  LYS A 286    23420  22897  26053   1815  -3390  -2550       N  
ATOM   1149  N   GLU A 287      52.854  20.345  56.867  1.00157.08           N  
ANISOU 1149  N   GLU A 287    19694  19330  20657   1662  -2993  -1800       N  
ATOM   1150  CA  GLU A 287      52.496  20.737  58.245  1.00160.05           C  
ANISOU 1150  CA  GLU A 287    19896  19721  21194   1390  -2894  -1478       C  
ATOM   1151  C   GLU A 287      53.501  20.246  59.265  1.00159.80           C  
ANISOU 1151  C   GLU A 287    19694  19627  21396   1186  -2777  -1308       C  
ATOM   1152  O   GLU A 287      53.856  19.058  59.270  1.00170.29           O  
ANISOU 1152  O   GLU A 287    20873  20791  23035   1175  -2951  -1406       O  
ATOM   1153  CB  GLU A 287      51.085  20.218  58.610  1.00168.28           C  
ANISOU 1153  CB  GLU A 287    20723  20652  22561   1312  -3186  -1464       C  
ATOM   1154  CG  GLU A 287      50.487  20.811  59.861  1.00170.43           C  
ANISOU 1154  CG  GLU A 287    20865  20979  22911   1083  -3062  -1153       C  
ATOM   1155  CD  GLU A 287      48.939  20.579  59.926  1.00176.03           C  
ANISOU 1155  CD  GLU A 287    21403  21614  23866   1063  -3311  -1186       C  
ATOM   1156  OE1 GLU A 287      48.416  19.614  59.323  1.00183.71           O  
ANISOU 1156  OE1 GLU A 287    22261  22430  25111   1148  -3616  -1417       O  
ATOM   1157  OE2 GLU A 287      48.226  21.344  60.601  1.00170.90           O  
ANISOU 1157  OE2 GLU A 287    20709  21055  23171    958  -3205   -999       O  
ATOM   1158  N   LYS A 288      53.953  21.175  60.120  1.00159.49           N  
ANISOU 1158  N   LYS A 288    19680  19711  21206   1040  -2499  -1066       N  
ATOM   1159  CA  LYS A 288      54.880  20.881  61.209  1.00162.45           C  
ANISOU 1159  CA  LYS A 288    19904  20059  21760    856  -2393   -889       C  
ATOM   1160  C   LYS A 288      54.086  20.605  62.493  1.00155.29           C  
ANISOU 1160  C   LYS A 288    18792  19102  21107    645  -2487   -632       C  
ATOM   1161  O   LYS A 288      53.151  21.315  62.813  1.00156.07           O  
ANISOU 1161  O   LYS A 288    18908  19284  21106    594  -2447   -516       O  
ATOM   1162  CB  LYS A 288      55.811  22.042  61.530  1.00172.40           C  
ANISOU 1162  CB  LYS A 288    21279  21478  22744    807  -2056   -782       C  
ATOM   1163  CG  LYS A 288      56.543  22.691  60.363  1.00185.29           C  
ANISOU 1163  CG  LYS A 288    23148  23191  24062    990  -1846   -964       C  
ATOM   1164  CD  LYS A 288      57.572  23.714  60.899  1.00198.13           C  
ANISOU 1164  CD  LYS A 288    24812  24927  25538    887  -1507   -843       C  
ATOM   1165  CE  LYS A 288      57.744  24.988  60.027  1.00204.02           C  
ANISOU 1165  CE  LYS A 288    25833  25783  25901   1011  -1213   -888       C  
ATOM   1166  NZ  LYS A 288      58.164  26.174  60.828  1.00201.30           N  
ANISOU 1166  NZ  LYS A 288    25495  25529  25458    859   -935   -716       N  
ATOM   1167  N   PRO A 289      54.452  19.561  63.212  1.00152.78           N  
ANISOU 1167  N   PRO A 289    18289  18643  21117    536  -2603   -542       N  
ATOM   1168  CA  PRO A 289      53.674  19.201  64.406  1.00153.92           C  
ANISOU 1168  CA  PRO A 289    18256  18724  21502    348  -2673   -278       C  
ATOM   1169  C   PRO A 289      53.886  20.236  65.484  1.00147.75           C  
ANISOU 1169  C   PRO A 289    17510  18125  20501    218  -2434    -31       C  
ATOM   1170  O   PRO A 289      55.045  20.597  65.739  1.00146.62           O  
ANISOU 1170  O   PRO A 289    17418  18064  20226    213  -2287    -19       O  
ATOM   1171  CB  PRO A 289      54.291  17.867  64.815  1.00163.23           C  
ANISOU 1171  CB  PRO A 289    19279  19701  23039    300  -2828   -244       C  
ATOM   1172  CG  PRO A 289      55.729  17.955  64.342  1.00161.97           C  
ANISOU 1172  CG  PRO A 289    19208  19589  22744    406  -2731   -402       C  
ATOM   1173  CD  PRO A 289      55.746  18.855  63.138  1.00157.54           C  
ANISOU 1173  CD  PRO A 289    18851  19165  21842    570  -2609   -629       C  
ATOM   1174  N   GLY A 290      52.799  20.752  66.065  1.00145.56           N  
ANISOU 1174  N   GLY A 290    17198  17916  20190    125  -2393    130       N  
ATOM   1175  CA  GLY A 290      52.895  21.773  67.089  1.00145.44           C  
ANISOU 1175  CA  GLY A 290    17222  18081  19956     16  -2174    340       C  
ATOM   1176  C   GLY A 290      52.925  23.205  66.563  1.00146.45           C  
ANISOU 1176  C   GLY A 290    17539  18387  19718     97  -1978    249       C  
ATOM   1177  O   GLY A 290      53.186  24.140  67.320  1.00150.95           O  
ANISOU 1177  O   GLY A 290    18154  19101  20098     21  -1788    376       O  
ATOM   1178  N   SER A 291      52.596  23.373  65.288  1.00145.05           N  
ANISOU 1178  N   SER A 291    17478  18189  19443    259  -2036     32       N  
ATOM   1179  CA  SER A 291      52.575  24.697  64.679  1.00138.74           C  
ANISOU 1179  CA  SER A 291    16888  17528  18296    362  -1853    -39       C  
ATOM   1180  C   SER A 291      51.123  25.162  64.478  1.00130.63           C  
ANISOU 1180  C   SER A 291    15872  16532  17229    405  -1927    -35       C  
ATOM   1181  O   SER A 291      50.272  24.409  64.033  1.00130.26           O  
ANISOU 1181  O   SER A 291    15732  16380  17381    458  -2159   -130       O  
ATOM   1182  CB  SER A 291      53.247  24.685  63.315  1.00142.07           C  
ANISOU 1182  CB  SER A 291    17485  17925  18568    556  -1839   -279       C  
ATOM   1183  OG  SER A 291      53.066  25.916  62.663  1.00137.76           O  
ANISOU 1183  OG  SER A 291    17163  17486  17691    672  -1670   -323       O  
ATOM   1184  N   PRO A 292      50.848  26.424  64.807  1.00126.50           N  
ANISOU 1184  N   PRO A 292    15447  16145  16471    387  -1736     56       N  
ATOM   1185  CA  PRO A 292      49.512  27.002  64.587  1.00132.13           C  
ANISOU 1185  CA  PRO A 292    16176  16897  17129    452  -1795     45       C  
ATOM   1186  C   PRO A 292      49.450  27.724  63.238  1.00135.64           C  
ANISOU 1186  C   PRO A 292    16877  17370  17289    687  -1782   -134       C  
ATOM   1187  O   PRO A 292      48.546  28.521  62.985  1.00138.87           O  
ANISOU 1187  O   PRO A 292    17363  17833  17566    778  -1787   -145       O  
ATOM   1188  CB  PRO A 292      49.376  27.982  65.735  1.00132.46           C  
ANISOU 1188  CB  PRO A 292    16196  17066  17065    314  -1582    242       C  
ATOM   1189  CG  PRO A 292      50.781  28.267  66.164  1.00130.94           C  
ANISOU 1189  CG  PRO A 292    16070  16920  16761    241  -1389    292       C  
ATOM   1190  CD  PRO A 292      51.604  27.108  65.859  1.00126.55           C  
ANISOU 1190  CD  PRO A 292    15453  16255  16374    247  -1508    217       C  
ATOM   1191  N   ALA A 293      50.431  27.444  62.384  1.00136.83           N  
ANISOU 1191  N   ALA A 293    17167  17484  17338    798  -1757   -270       N  
ATOM   1192  CA  ALA A 293      50.656  28.170  61.157  1.00142.01           C  
ANISOU 1192  CA  ALA A 293    18113  18175  17667   1023  -1669   -403       C  
ATOM   1193  C   ALA A 293      50.631  27.331  59.884  1.00146.19           C  
ANISOU 1193  C   ALA A 293    18729  18629  18185   1238  -1887   -646       C  
ATOM   1194  O   ALA A 293      50.718  26.096  59.932  1.00147.22           O  
ANISOU 1194  O   ALA A 293    18683  18659  18596   1196  -2089   -732       O  
ATOM   1195  CB  ALA A 293      51.996  28.877  61.227  1.00140.00           C  
ANISOU 1195  CB  ALA A 293    17997  17968  17227    980  -1342   -347       C  
ATOM   1196  N   VAL A 294      50.489  28.021  58.748  1.00146.49           N  
ANISOU 1196  N   VAL A 294    19054  18713  17890   1482  -1848   -755       N  
ATOM   1197  CA  VAL A 294      50.669  27.438  57.439  1.00146.23           C  
ANISOU 1197  CA  VAL A 294    19183  18645  17730   1731  -1994   -996       C  
ATOM   1198  C   VAL A 294      51.932  28.105  56.881  1.00144.04           C  
ANISOU 1198  C   VAL A 294    19171  18417  17140   1808  -1641   -979       C  
ATOM   1199  O   VAL A 294      51.962  29.322  56.664  1.00141.51           O  
ANISOU 1199  O   VAL A 294    19079  18161  16524   1875  -1403   -874       O  
ATOM   1200  CB  VAL A 294      49.419  27.634  56.585  1.00147.98           C  
ANISOU 1200  CB  VAL A 294    19527  18884  17813   1976  -2256  -1139       C  
ATOM   1201  CG1 VAL A 294      49.545  26.845  55.285  1.00154.77           C  
ANISOU 1201  CG1 VAL A 294    20529  19708  18566   2245  -2471  -1426       C  
ATOM   1202  CG2 VAL A 294      48.170  27.219  57.371  1.00146.61           C  
ANISOU 1202  CG2 VAL A 294    19043  18663  17997   1840  -2519  -1108       C  
ATOM   1203  N   THR A 295      52.980  27.318  56.699  1.00143.60           N  
ANISOU 1203  N   THR A 295    19064  18314  17180   1787  -1592  -1074       N  
ATOM   1204  CA  THR A 295      54.280  27.866  56.353  1.00148.34           C  
ANISOU 1204  CA  THR A 295    19838  18948  17575   1807  -1221  -1050       C  
ATOM   1205  C   THR A 295      54.519  27.861  54.839  1.00152.24           C  
ANISOU 1205  C   THR A 295    20649  19463  17729   2122  -1179  -1240       C  
ATOM   1206  O   THR A 295      54.332  26.857  54.172  1.00161.67           O  
ANISOU 1206  O   THR A 295    21832  20621  18975   2275  -1443  -1461       O  
ATOM   1207  CB  THR A 295      55.371  27.122  57.130  1.00154.68           C  
ANISOU 1207  CB  THR A 295    20387  19697  18687   1598  -1153  -1034       C  
ATOM   1208  OG1 THR A 295      55.081  27.185  58.533  1.00156.83           O  
ANISOU 1208  OG1 THR A 295    20409  19966  19210   1339  -1196   -844       O  
ATOM   1209  CG2 THR A 295      56.744  27.756  56.859  1.00159.93           C  
ANISOU 1209  CG2 THR A 295    21179  20390  19196   1591   -745  -1017       C  
ATOM   1210  N   LEU A 296      54.902  29.004  54.314  1.00150.31           N  
ANISOU 1210  N   LEU A 296    20698  19275  17137   2223   -844  -1150       N  
ATOM   1211  CA  LEU A 296      55.170  29.170  52.899  1.00153.96           C  
ANISOU 1211  CA  LEU A 296    21516  19772  17207   2535   -731  -1280       C  
ATOM   1212  C   LEU A 296      56.647  29.225  52.639  1.00157.64           C  
ANISOU 1212  C   LEU A 296    22035  20231  17630   2499   -335  -1287       C  
ATOM   1213  O   LEU A 296      57.368  29.897  53.357  1.00149.82           O  
ANISOU 1213  O   LEU A 296    20954  19225  16744   2281    -21  -1120       O  
ATOM   1214  CB  LEU A 296      54.546  30.486  52.431  1.00154.33           C  
ANISOU 1214  CB  LEU A 296    21892  19869  16874   2696   -592  -1141       C  
ATOM   1215  CG  LEU A 296      53.095  30.677  52.859  1.00156.22           C  
ANISOU 1215  CG  LEU A 296    22046  20119  17190   2700   -931  -1102       C  
ATOM   1216  CD1 LEU A 296      52.692  32.113  52.568  1.00157.21           C  
ANISOU 1216  CD1 LEU A 296    22479  20275  16977   2823   -726   -927       C  
ATOM   1217  CD2 LEU A 296      52.231  29.628  52.182  1.00158.06           C  
ANISOU 1217  CD2 LEU A 296    22253  20351  17451   2914  -1398  -1363       C  
ATOM   1218  N   LEU A 297      57.096  28.492  51.630  1.00167.12           N  
ANISOU 1218  N   LEU A 297    23358  21439  18699   2713   -359  -1504       N  
ATOM   1219  CA  LEU A 297      58.480  28.595  51.157  1.00170.42           C  
ANISOU 1219  CA  LEU A 297    23866  21859  19025   2733     58  -1535       C  
ATOM   1220  C   LEU A 297      58.493  29.411  49.876  1.00165.08           C  
ANISOU 1220  C   LEU A 297    23658  21246  17817   3039    327  -1518       C  
ATOM   1221  O   LEU A 297      57.856  29.046  48.892  1.00156.95           O  
ANISOU 1221  O   LEU A 297    22864  20266  16502   3347     92  -1683       O  
ATOM   1222  CB  LEU A 297      59.153  27.241  50.932  1.00177.04           C  
ANISOU 1222  CB  LEU A 297    24519  22662  20083   2764    -79  -1786       C  
ATOM   1223  CG  LEU A 297      60.659  27.337  50.574  1.00184.80           C  
ANISOU 1223  CG  LEU A 297    25527  23644  21041   2753    379  -1823       C  
ATOM   1224  CD1 LEU A 297      61.490  28.023  51.662  1.00184.51           C  
ANISOU 1224  CD1 LEU A 297    25264  23568  21273   2428    696  -1621       C  
ATOM   1225  CD2 LEU A 297      61.226  25.958  50.257  1.00189.69           C  
ANISOU 1225  CD2 LEU A 297    25978  24227  21865   2829    206  -2104       C  
ATOM   1226  N   ILE A 298      59.229  30.519  49.917  1.00163.44           N  
ANISOU 1226  N   ILE A 298    23583  21026  17489   2953    820  -1317       N  
ATOM   1227  CA  ILE A 298      59.380  31.395  48.776  1.00165.54           C  
ANISOU 1227  CA  ILE A 298    24307  21327  17261   3216   1168  -1239       C  
ATOM   1228  C   ILE A 298      60.801  31.300  48.236  1.00169.41           C  
ANISOU 1228  C   ILE A 298    24844  21807  17715   3229   1636  -1295       C  
ATOM   1229  O   ILE A 298      61.773  31.631  48.927  1.00169.58           O  
ANISOU 1229  O   ILE A 298    24636  21764  18030   2954   1965  -1202       O  
ATOM   1230  CB  ILE A 298      59.075  32.861  49.105  1.00164.32           C  
ANISOU 1230  CB  ILE A 298    24317  21135  16981   3134   1426   -945       C  
ATOM   1231  CG1 ILE A 298      57.634  32.998  49.578  1.00163.01           C  
ANISOU 1231  CG1 ILE A 298    24111  20987  16838   3149    980   -902       C  
ATOM   1232  CG2 ILE A 298      59.311  33.737  47.878  1.00171.62           C  
ANISOU 1232  CG2 ILE A 298    25744  22071  17390   3419   1825   -836       C  
ATOM   1233  CD1 ILE A 298      57.286  34.418  50.011  1.00162.71           C  
ANISOU 1233  CD1 ILE A 298    24197  20900  16723   3059   1200   -629       C  
ATOM   1234  N   ARG A 299      60.901  30.880  46.980  1.00172.16           N  
ANISOU 1234  N   ARG A 299    25494  22224  17694   3563   1666  -1459       N  
ATOM   1235  CA  ARG A 299      62.148  30.955  46.239  1.00174.47           C  
ANISOU 1235  CA  ARG A 299    25926  22523  17840   3644   2180  -1494       C  
ATOM   1236  C   ARG A 299      62.304  32.327  45.624  1.00172.83           C  
ANISOU 1236  C   ARG A 299    26135  22301  17232   3754   2686  -1228       C  
ATOM   1237  O   ARG A 299      62.084  32.526  44.444  1.00175.61           O  
ANISOU 1237  O   ARG A 299    26934  22722  17065   4108   2795  -1235       O  
ATOM   1238  CB  ARG A 299      62.248  29.812  45.213  1.00183.92           C  
ANISOU 1238  CB  ARG A 299    27244  23804  18833   3955   1997  -1812       C  
ATOM   1239  CG  ARG A 299      63.396  28.842  45.456  1.00191.82           C  
ANISOU 1239  CG  ARG A 299    27894  24773  20214   3815   2095  -2018       C  
ATOM   1240  CD  ARG A 299      63.505  28.358  46.902  1.00193.34           C  
ANISOU 1240  CD  ARG A 299    27556  24875  21028   3434   1836  -2012       C  
ATOM   1241  NE  ARG A 299      64.065  27.007  46.986  1.00197.63           N  
ANISOU 1241  NE  ARG A 299    27801  25396  21893   3421   1629  -2296       N  
ATOM   1242  CZ  ARG A 299      63.372  25.869  46.847  1.00200.45           C  
ANISOU 1242  CZ  ARG A 299    28079  25753  22327   3552   1102  -2532       C  
ATOM   1243  NH1 ARG A 299      62.044  25.866  46.712  1.00201.39           N  
ANISOU 1243  NH1 ARG A 299    28344  25899  22274   3681    690  -2532       N  
ATOM   1244  NH2 ARG A 299      64.018  24.709  46.941  1.00202.56           N  
ANISOU 1244  NH2 ARG A 299    28073  25973  22918   3530    971  -2775       N  
ATOM   1245  N   ASN A 300      62.673  33.302  46.457  1.00171.68           N  
ANISOU 1245  N   ASN A 300    25846  22053  17330   3455   2994   -988       N  
ATOM   1246  CA  ASN A 300      62.950  34.655  45.994  1.00174.29           C  
ANISOU 1246  CA  ASN A 300    26524  22318  17378   3503   3532   -712       C  
ATOM   1247  C   ASN A 300      64.413  34.615  45.586  1.00176.08           C  
ANISOU 1247  C   ASN A 300    26708  22508  17686   3444   4106   -748       C  
ATOM   1248  O   ASN A 300      65.230  35.356  46.113  1.00178.35           O  
ANISOU 1248  O   ASN A 300    26829  22678  18257   3173   4536   -602       O  
ATOM   1249  CB  ASN A 300      62.689  35.716  47.083  1.00172.76           C  
ANISOU 1249  CB  ASN A 300    26173  22011  17453   3204   3595   -470       C  
ATOM   1250  CG  ASN A 300      63.060  37.148  46.654  1.00174.10           C  
ANISOU 1250  CG  ASN A 300    26677  22066  17405   3222   4187   -178       C  
ATOM   1251  OD1 ASN A 300      63.675  37.910  47.429  1.00169.76           O  
ANISOU 1251  OD1 ASN A 300    25912  21385  17201   2912   4505    -42       O  
ATOM   1252  ND2 ASN A 300      62.680  37.522  45.427  1.00180.16           N  
ANISOU 1252  ND2 ASN A 300    27976  22871  17604   3594   4327    -82       N  
ATOM   1253  N   PRO A 301      64.732  33.826  44.558  1.00176.33           N  
ANISOU 1253  N   PRO A 301    26917  22637  17440   3725   4144   -948       N  
ATOM   1254  CA  PRO A 301      65.902  32.994  44.516  1.00176.29           C  
ANISOU 1254  CA  PRO A 301    26631  22641  17710   3640   4339  -1165       C  
ATOM   1255  C   PRO A 301      66.312  32.382  45.889  1.00177.73           C  
ANISOU 1255  C   PRO A 301    26200  22761  18566   3257   4084  -1282       C  
ATOM   1256  O   PRO A 301      66.132  31.183  46.074  1.00177.27           O  
ANISOU 1256  O   PRO A 301    25919  22755  18680   3288   3639  -1529       O  
ATOM   1257  CB  PRO A 301      66.938  33.956  43.906  1.00175.49           C  
ANISOU 1257  CB  PRO A 301    26747  22467  17462   3639   5123   -976       C  
ATOM   1258  CG  PRO A 301      66.103  34.880  43.031  1.00178.10           C  
ANISOU 1258  CG  PRO A 301    27672  22818  17179   3942   5234   -736       C  
ATOM   1259  CD  PRO A 301      64.641  34.567  43.294  1.00178.08           C  
ANISOU 1259  CD  PRO A 301    27722  22889  17050   4065   4521   -790       C  
ATOM   1260  N   GLU A 302      66.844  33.162  46.820  1.00185.23           N  
ANISOU 1260  N   GLU A 302    26894  23598  19887   2919   4343  -1116       N  
ATOM   1261  CA  GLU A 302      67.087  32.607  48.134  1.00186.90           C  
ANISOU 1261  CA  GLU A 302    26576  23770  20665   2602   4037  -1215       C  
ATOM   1262  C   GLU A 302      65.789  32.215  48.818  1.00177.31           C  
ANISOU 1262  C   GLU A 302    25287  22596  19486   2585   3398  -1213       C  
ATOM   1263  O   GLU A 302      64.708  32.715  48.473  1.00178.83           O  
ANISOU 1263  O   GLU A 302    25798  22821  19328   2749   3245  -1088       O  
ATOM   1264  CB  GLU A 302      68.035  33.448  49.029  1.00195.81           C  
ANISOU 1264  CB  GLU A 302    27403  24775  22218   2249   4422  -1094       C  
ATOM   1265  CG  GLU A 302      67.434  34.562  49.891  1.00200.38           C  
ANISOU 1265  CG  GLU A 302    27977  25280  22876   2050   4390   -854       C  
ATOM   1266  CD  GLU A 302      67.115  35.830  49.112  1.00212.01           C  
ANISOU 1266  CD  GLU A 302    29912  26696  23944   2188   4794   -601       C  
ATOM   1267  OE1 GLU A 302      66.432  36.716  49.678  1.00211.91           O  
ANISOU 1267  OE1 GLU A 302    29957  26626  23930   2087   4719   -413       O  
ATOM   1268  OE2 GLU A 302      67.551  35.958  47.940  1.00225.17           O  
ANISOU 1268  OE2 GLU A 302    31895  28368  25290   2408   5198   -583       O  
ATOM   1269  N   GLU A 303      65.881  31.275  49.743  1.00169.38           N  
ANISOU 1269  N   GLU A 303    23868  21588  18900   2407   3023  -1358       N  
ATOM   1270  CA  GLU A 303      64.718  30.693  50.411  1.00168.36           C  
ANISOU 1270  CA  GLU A 303    23618  21487  18863   2380   2425  -1377       C  
ATOM   1271  C   GLU A 303      64.263  31.541  51.583  1.00161.59           C  
ANISOU 1271  C   GLU A 303    22617  20587  18189   2119   2364  -1162       C  
ATOM   1272  O   GLU A 303      65.064  31.888  52.463  1.00164.40           O  
ANISOU 1272  O   GLU A 303    22693  20887  18885   1852   2553  -1112       O  
ATOM   1273  CB  GLU A 303      65.048  29.338  50.999  1.00178.27           C  
ANISOU 1273  CB  GLU A 303    24486  22730  20516   2284   2076  -1587       C  
ATOM   1274  CG  GLU A 303      65.196  28.191  50.012  1.00192.23           C  
ANISOU 1274  CG  GLU A 303    26335  24536  22166   2548   1938  -1857       C  
ATOM   1275  CD  GLU A 303      65.774  26.940  50.676  1.00205.14           C  
ANISOU 1275  CD  GLU A 303    27554  26120  24270   2421   1674  -2047       C  
ATOM   1276  OE1 GLU A 303      66.641  27.097  51.575  1.00217.64           O  
ANISOU 1276  OE1 GLU A 303    28824  27649  26217   2167   1827  -1997       O  
ATOM   1277  OE2 GLU A 303      65.390  25.788  50.327  1.00210.12           O  
ANISOU 1277  OE2 GLU A 303    28155  26749  24930   2578   1301  -2257       O  
ATOM   1278  N   ILE A 304      62.973  31.850  51.601  1.00155.45           N  
ANISOU 1278  N   ILE A 304    22020  19842  17199   2210   2083  -1060       N  
ATOM   1279  CA  ILE A 304      62.373  32.600  52.704  1.00150.65           C  
ANISOU 1279  CA  ILE A 304    21287  19208  16741   1992   1981   -874       C  
ATOM   1280  C   ILE A 304      61.160  31.832  53.221  1.00147.59           C  
ANISOU 1280  C   ILE A 304    20770  18864  16441   2002   1416   -920       C  
ATOM   1281  O   ILE A 304      60.328  31.390  52.430  1.00152.93           O  
ANISOU 1281  O   ILE A 304    21647  19584  16872   2251   1159  -1011       O  
ATOM   1282  CB  ILE A 304      61.912  33.962  52.175  1.00151.42           C  
ANISOU 1282  CB  ILE A 304    21761  19285  16485   2105   2258   -671       C  
ATOM   1283  CG1 ILE A 304      63.110  34.750  51.619  1.00154.38           C  
ANISOU 1283  CG1 ILE A 304    22275  19589  16794   2088   2870   -601       C  
ATOM   1284  CG2 ILE A 304      61.237  34.741  53.289  1.00151.91           C  
ANISOU 1284  CG2 ILE A 304    21699  19322  16698   1902   2142   -504       C  
ATOM   1285  CD1 ILE A 304      62.731  35.943  50.787  1.00158.37           C  
ANISOU 1285  CD1 ILE A 304    23231  20054  16886   2273   3179   -402       C  
ATOM   1286  N   SER A 305      61.045  31.675  54.535  1.00143.15           N  
ANISOU 1286  N   SER A 305    19875  18287  16225   1741   1225   -865       N  
ATOM   1287  CA  SER A 305      59.897  30.994  55.116  1.00143.49           C  
ANISOU 1287  CA  SER A 305    19775  18356  16388   1719    743   -877       C  
ATOM   1288  C   SER A 305      58.942  31.984  55.779  1.00138.21           C  
ANISOU 1288  C   SER A 305    19147  17704  15662   1633    700   -686       C  
ATOM   1289  O   SER A 305      59.378  32.869  56.507  1.00137.31           O  
ANISOU 1289  O   SER A 305    18960  17569  15640   1445    944   -556       O  
ATOM   1290  CB  SER A 305      60.368  29.933  56.115  1.00150.44           C  
ANISOU 1290  CB  SER A 305    20264  19210  17687   1517    528   -946       C  
ATOM   1291  OG  SER A 305      60.881  30.529  57.293  1.00162.25           O  
ANISOU 1291  OG  SER A 305    21551  20697  19399   1256    675   -817       O  
ATOM   1292  N   VAL A 306      57.652  31.836  55.518  1.00134.99           N  
ANISOU 1292  N   VAL A 306    18841  17326  15120   1777    386   -693       N  
ATOM   1293  CA  VAL A 306      56.636  32.722  56.080  1.00135.16           C  
ANISOU 1293  CA  VAL A 306    18897  17368  15090   1728    321   -536       C  
ATOM   1294  C   VAL A 306      55.551  31.937  56.817  1.00140.29           C  
ANISOU 1294  C   VAL A 306    19300  18036  15965   1655   -111   -559       C  
ATOM   1295  O   VAL A 306      54.784  31.200  56.206  1.00142.16           O  
ANISOU 1295  O   VAL A 306    19574  18278  16161   1828   -420   -689       O  
ATOM   1296  CB  VAL A 306      56.018  33.556  54.965  1.00134.47           C  
ANISOU 1296  CB  VAL A 306    19208  17291  14592   2006    404   -501       C  
ATOM   1297  CG1 VAL A 306      55.027  34.559  55.548  1.00138.75           C  
ANISOU 1297  CG1 VAL A 306    19781  17840  15097   1962    360   -343       C  
ATOM   1298  CG2 VAL A 306      57.109  34.275  54.190  1.00133.85           C  
ANISOU 1298  CG2 VAL A 306    19388  17175  14291   2082    874   -455       C  
ATOM   1299  N   ASP A 307      55.492  32.087  58.131  1.00143.34           N  
ANISOU 1299  N   ASP A 307    19434  18431  16598   1402   -128   -440       N  
ATOM   1300  CA  ASP A 307      54.463  31.424  58.930  1.00143.78           C  
ANISOU 1300  CA  ASP A 307    19252  18500  16876   1310   -474   -421       C  
ATOM   1301  C   ASP A 307      53.186  32.273  58.957  1.00138.41           C  
ANISOU 1301  C   ASP A 307    18679  17856  16053   1386   -551   -338       C  
ATOM   1302  O   ASP A 307      53.188  33.396  59.474  1.00130.80           O  
ANISOU 1302  O   ASP A 307    17767  16914  15017   1302   -337   -203       O  
ATOM   1303  CB  ASP A 307      54.992  31.132  60.344  1.00152.63           C  
ANISOU 1303  CB  ASP A 307    20070  19626  18295   1028   -456   -325       C  
ATOM   1304  CG  ASP A 307      56.312  30.314  60.335  1.00162.99           C  
ANISOU 1304  CG  ASP A 307    21262  20895  19770    968   -392   -417       C  
ATOM   1305  OD1 ASP A 307      56.629  29.705  59.318  1.00168.95           O  
ANISOU 1305  OD1 ASP A 307    22115  21613  20463   1130   -429   -569       O  
ATOM   1306  OD2 ASP A 307      57.063  30.279  61.331  1.00168.24           O  
ANISOU 1306  OD2 ASP A 307    21735  21566  20621    775   -312   -355       O  
ATOM   1307  N   ILE A 308      52.131  31.776  58.319  1.00135.91           N  
ANISOU 1307  N   ILE A 308    18402  17537  15698   1566   -856   -444       N  
ATOM   1308  CA  ILE A 308      50.836  32.415  58.377  1.00133.26           C  
ANISOU 1308  CA  ILE A 308    18111  17233  15289   1647   -989   -397       C  
ATOM   1309  C   ILE A 308      50.062  31.788  59.528  1.00131.14           C  
ANISOU 1309  C   ILE A 308    17494  16967  15364   1447  -1209   -349       C  
ATOM   1310  O   ILE A 308      49.549  30.677  59.409  1.00127.64           O  
ANISOU 1310  O   ILE A 308    16885  16482  15128   1466  -1504   -462       O  
ATOM   1311  CB  ILE A 308      50.044  32.261  57.077  1.00136.59           C  
ANISOU 1311  CB  ILE A 308    18749  17652  15497   1968  -1226   -557       C  
ATOM   1312  CG1 ILE A 308      50.852  32.845  55.910  1.00139.06           C  
ANISOU 1312  CG1 ILE A 308    19442  17966  15426   2185   -973   -581       C  
ATOM   1313  CG2 ILE A 308      48.672  32.919  57.198  1.00138.42           C  
ANISOU 1313  CG2 ILE A 308    18986  17912  15694   2055  -1391   -522       C  
ATOM   1314  CD1 ILE A 308      51.304  34.283  56.106  1.00138.59           C  
ANISOU 1314  CD1 ILE A 308    19577  17905  15175   2139   -580   -386       C  
ATOM   1315  N   ILE A 309      50.020  32.496  60.641  1.00129.57           N  
ANISOU 1315  N   ILE A 309    17188  16810  15230   1256  -1047   -184       N  
ATOM   1316  CA  ILE A 309      49.478  31.977  61.891  1.00126.47           C  
ANISOU 1316  CA  ILE A 309    16482  16435  15135   1043  -1167    -95       C  
ATOM   1317  C   ILE A 309      48.010  32.313  62.053  1.00121.88           C  
ANISOU 1317  C   ILE A 309    15831  15881  14594   1097  -1327    -82       C  
ATOM   1318  O   ILE A 309      47.660  33.482  62.137  1.00121.71           O  
ANISOU 1318  O   ILE A 309    15934  15905  14403   1144  -1190    -17       O  
ATOM   1319  CB  ILE A 309      50.246  32.557  63.070  1.00130.04           C  
ANISOU 1319  CB  ILE A 309    16856  16937  15616    822   -910     57       C  
ATOM   1320  CG1 ILE A 309      51.742  32.255  62.928  1.00137.74           C  
ANISOU 1320  CG1 ILE A 309    17865  17881  16589    768   -754     23       C  
ATOM   1321  CG2 ILE A 309      49.671  32.023  64.382  1.00129.02           C  
ANISOU 1321  CG2 ILE A 309    16437  16842  15743    624  -1017    169       C  
ATOM   1322  CD1 ILE A 309      52.662  33.362  63.374  1.00142.79           C  
ANISOU 1322  CD1 ILE A 309    18584  18550  17117    673   -432     96       C  
ATOM   1323  N   LEU A 310      47.166  31.303  62.114  1.00118.18           N  
ANISOU 1323  N   LEU A 310    15149  15372  14382   1086  -1609   -149       N  
ATOM   1324  CA  LEU A 310      45.729  31.517  62.409  1.00119.42           C  
ANISOU 1324  CA  LEU A 310    15162  15550  14662   1105  -1761   -145       C  
ATOM   1325  C   LEU A 310      45.524  31.849  63.866  1.00118.67           C  
ANISOU 1325  C   LEU A 310    14871  15520  14696    869  -1598     46       C  
ATOM   1326  O   LEU A 310      45.886  31.051  64.715  1.00121.16           O  
ANISOU 1326  O   LEU A 310    14995  15820  15220    675  -1585    139       O  
ATOM   1327  CB  LEU A 310      44.897  30.268  62.097  1.00122.20           C  
ANISOU 1327  CB  LEU A 310    15295  15814  15321   1135  -2100   -285       C  
ATOM   1328  CG  LEU A 310      43.443  30.266  62.603  1.00123.21           C  
ANISOU 1328  CG  LEU A 310    15172  15945  15696   1094  -2244   -277       C  
ATOM   1329  CD1 LEU A 310      42.634  31.434  62.047  1.00123.21           C  
ANISOU 1329  CD1 LEU A 310    15332  16008  15474   1308  -2270   -340       C  
ATOM   1330  CD2 LEU A 310      42.774  28.924  62.275  1.00127.64           C  
ANISOU 1330  CD2 LEU A 310    15489  16380  16626   1098  -2571   -433       C  
ATOM   1331  N   ALA A 311      44.927  32.987  64.161  1.00118.96           N  
ANISOU 1331  N   ALA A 311    14962  15628  14609    902  -1484    104       N  
ATOM   1332  CA  ALA A 311      44.678  33.355  65.569  1.00117.52           C  
ANISOU 1332  CA  ALA A 311    14603  15526  14521    699  -1322    268       C  
ATOM   1333  C   ALA A 311      43.258  33.812  65.824  1.00117.93           C  
ANISOU 1333  C   ALA A 311    14524  15616  14665    745  -1393    260       C  
ATOM   1334  O   ALA A 311      42.595  34.307  64.938  1.00124.43           O  
ANISOU 1334  O   ALA A 311    15461  16421  15396    955  -1514    143       O  
ATOM   1335  CB  ALA A 311      45.648  34.453  65.979  1.00116.54           C  
ANISOU 1335  CB  ALA A 311    14658  15462  14158    647  -1029    352       C  
ATOM   1336  N   LEU A 312      42.796  33.643  67.056  1.00114.42           N  
ANISOU 1336  N   LEU A 312    13842  15231  14401    559  -1313    387       N  
ATOM   1337  CA  LEU A 312      41.502  34.160  67.517  1.00113.44           C  
ANISOU 1337  CA  LEU A 312    13561  15163  14379    573  -1313    395       C  
ATOM   1338  C   LEU A 312      41.762  35.336  68.422  1.00111.46           C  
ANISOU 1338  C   LEU A 312    13390  15026  13934    507  -1039    501       C  
ATOM   1339  O   LEU A 312      42.542  35.238  69.359  1.00109.68           O  
ANISOU 1339  O   LEU A 312    13145  14859  13669    339   -873    624       O  
ATOM   1340  CB  LEU A 312      40.723  33.129  68.313  1.00115.79           C  
ANISOU 1340  CB  LEU A 312    13518  15445  15029    408  -1377    468       C  
ATOM   1341  CG  LEU A 312      40.632  31.720  67.698  1.00121.12           C  
ANISOU 1341  CG  LEU A 312    14058  15979  15981    401  -1632    384       C  
ATOM   1342  CD1 LEU A 312      39.837  30.771  68.596  1.00120.59           C  
ANISOU 1342  CD1 LEU A 312    13646  15872  16301    212  -1641    492       C  
ATOM   1343  CD2 LEU A 312      40.024  31.760  66.302  1.00125.48           C  
ANISOU 1343  CD2 LEU A 312    14681  16456  16538    648  -1908    145       C  
ATOM   1344  N   GLU A 313      41.086  36.452  68.172  1.00117.89           N  
ANISOU 1344  N   GLU A 313    14288  15868  14635    652  -1007    442       N  
ATOM   1345  CA  GLU A 313      41.205  37.646  69.021  1.00124.43           C  
ANISOU 1345  CA  GLU A 313    15180  16790  15306    607   -759    511       C  
ATOM   1346  C   GLU A 313      40.032  37.807  70.007  1.00126.94           C  
ANISOU 1346  C   GLU A 313    15241  17201  15787    541   -704    550       C  
ATOM   1347  O   GLU A 313      38.880  37.810  69.599  1.00133.18           O  
ANISOU 1347  O   GLU A 313    15907  17967  16727    656   -850    462       O  
ATOM   1348  CB  GLU A 313      41.338  38.899  68.182  1.00132.23           C  
ANISOU 1348  CB  GLU A 313    16454  17732  16055    809   -712    436       C  
ATOM   1349  CG  GLU A 313      41.544  40.173  69.005  1.00137.83           C  
ANISOU 1349  CG  GLU A 313    17238  18504  16625    764   -460    483       C  
ATOM   1350  CD  GLU A 313      41.594  41.400  68.112  1.00146.66           C  
ANISOU 1350  CD  GLU A 313    18644  19534  17544    974   -414    425       C  
ATOM   1351  OE1 GLU A 313      40.513  41.913  67.714  1.00158.01           O  
ANISOU 1351  OE1 GLU A 313    20079  20953  19002   1153   -521    361       O  
ATOM   1352  OE2 GLU A 313      42.716  41.831  67.754  1.00147.56           O  
ANISOU 1352  OE2 GLU A 313    18987  19583  17494    971   -274    446       O  
ATOM   1353  N   SER A 314      40.346  37.950  71.288  1.00127.88           N  
ANISOU 1353  N   SER A 314    15285  17431  15872    369   -495    668       N  
ATOM   1354  CA  SER A 314      39.323  38.167  72.293  1.00133.04           C  
ANISOU 1354  CA  SER A 314    15717  18192  16637    309   -387    714       C  
ATOM   1355  C   SER A 314      39.578  39.449  73.077  1.00132.74           C  
ANISOU 1355  C   SER A 314    15791  18260  16382    308   -157    718       C  
ATOM   1356  O   SER A 314      40.663  39.622  73.649  1.00135.42           O  
ANISOU 1356  O   SER A 314    16247  18647  16558    210    -29    773       O  
ATOM   1357  CB  SER A 314      39.269  36.995  73.243  1.00137.03           C  
ANISOU 1357  CB  SER A 314    16000  18746  17319    110   -345    864       C  
ATOM   1358  OG  SER A 314      38.312  37.273  74.257  1.00144.09           O  
ANISOU 1358  OG  SER A 314    16697  19758  18291     55   -187    920       O  
ATOM   1359  N   LYS A 315      38.593  40.340  73.106  1.00134.48           N  
ANISOU 1359  N   LYS A 315    15965  18510  16621    425   -122    639       N  
ATOM   1360  CA  LYS A 315      38.763  41.634  73.772  1.00140.46           C  
ANISOU 1360  CA  LYS A 315    16830  19344  17194    448     80    608       C  
ATOM   1361  C   LYS A 315      38.447  41.619  75.247  1.00142.86           C  
ANISOU 1361  C   LYS A 315    16957  19822  17500    314    275    684       C  
ATOM   1362  O   LYS A 315      38.641  42.640  75.916  1.00144.01           O  
ANISOU 1362  O   LYS A 315    17183  20045  17487    326    441    639       O  
ATOM   1363  CB  LYS A 315      37.985  42.725  73.040  1.00152.12           C  
ANISOU 1363  CB  LYS A 315    18388  20749  18660    668     27    479       C  
ATOM   1364  CG  LYS A 315      38.507  43.045  71.640  1.00157.31           C  
ANISOU 1364  CG  LYS A 315    19321  21243  19206    832   -107    421       C  
ATOM   1365  CD  LYS A 315      37.352  43.428  70.687  1.00161.25           C  
ANISOU 1365  CD  LYS A 315    19814  21663  19789   1076   -296    311       C  
ATOM   1366  CE  LYS A 315      37.860  43.742  69.282  1.00160.04           C  
ANISOU 1366  CE  LYS A 315    19977  21358  19472   1269   -422    273       C  
ATOM   1367  NZ  LYS A 315      36.771  43.777  68.265  1.00160.32           N  
ANISOU 1367  NZ  LYS A 315    20002  21326  19585   1523   -685    164       N  
ATOM   1368  N   GLY A 316      37.999  40.460  75.752  1.00146.43           N  
ANISOU 1368  N   GLY A 316    17181  20327  18128    190    263    798       N  
ATOM   1369  CA  GLY A 316      37.734  40.269  77.173  1.00149.87           C  
ANISOU 1369  CA  GLY A 316    17466  20934  18541     61    470    912       C  
ATOM   1370  C   GLY A 316      39.001  40.332  78.019  1.00148.33           C  
ANISOU 1370  C   GLY A 316    17429  20834  18094    -41    583    986       C  
ATOM   1371  O   GLY A 316      40.107  40.504  77.508  1.00145.68           O  
ANISOU 1371  O   GLY A 316    17290  20420  17641    -32    510    943       O  
ATOM   1372  N   SER A 317      38.830  40.260  79.330  1.00148.91           N  
ANISOU 1372  N   SER A 317    17417  21083  18076   -124    769   1083       N  
ATOM   1373  CA  SER A 317      39.986  40.394  80.211  1.00144.54           C  
ANISOU 1373  CA  SER A 317    17012  20641  17263   -191    850   1123       C  
ATOM   1374  C   SER A 317      40.747  39.066  80.209  1.00136.83           C  
ANISOU 1374  C   SER A 317    16035  19615  16337   -306    742   1287       C  
ATOM   1375  O   SER A 317      40.168  37.968  80.029  1.00132.75           O  
ANISOU 1375  O   SER A 317    15359  19034  16045   -368    689   1419       O  
ATOM   1376  CB  SER A 317      39.580  40.838  81.616  1.00152.92           C  
ANISOU 1376  CB  SER A 317    18023  21925  18154   -203   1075   1152       C  
ATOM   1377  OG  SER A 317      38.224  40.488  81.906  1.00160.86           O  
ANISOU 1377  OG  SER A 317    18800  22983  19336   -210   1186   1230       O  
ATOM   1378  N   TRP A 318      42.056  39.201  80.397  1.00132.60           N  
ANISOU 1378  N   TRP A 318    15667  19093  15622   -331    706   1260       N  
ATOM   1379  CA  TRP A 318      43.011  38.099  80.229  1.00128.85           C  
ANISOU 1379  CA  TRP A 318    15223  18544  15189   -411    572   1369       C  
ATOM   1380  C   TRP A 318      42.728  36.969  81.188  1.00128.14           C  
ANISOU 1380  C   TRP A 318    15018  18540  15130   -506    623   1605       C  
ATOM   1381  O   TRP A 318      42.389  37.229  82.348  1.00126.25           O  
ANISOU 1381  O   TRP A 318    14760  18483  14725   -514    791   1676       O  
ATOM   1382  CB  TRP A 318      44.435  38.596  80.425  1.00126.72           C  
ANISOU 1382  CB  TRP A 318    15123  18298  14727   -413    546   1270       C  
ATOM   1383  CG  TRP A 318      44.910  39.485  79.336  1.00126.23           C  
ANISOU 1383  CG  TRP A 318    15185  18096  14679   -342    504   1079       C  
ATOM   1384  CD1 TRP A 318      44.148  40.243  78.491  1.00130.88           C  
ANISOU 1384  CD1 TRP A 318    15794  18596  15336   -245    521    975       C  
ATOM   1385  CD2 TRP A 318      46.261  39.747  78.991  1.00124.64           C  
ANISOU 1385  CD2 TRP A 318    15112  17822  14423   -353    456    977       C  
ATOM   1386  NE1 TRP A 318      44.942  40.946  77.637  1.00132.04           N  
ANISOU 1386  NE1 TRP A 318    16100  18614  15453   -194    501    842       N  
ATOM   1387  CE2 TRP A 318      46.251  40.668  77.924  1.00125.89           C  
ANISOU 1387  CE2 TRP A 318    15377  17841  14614   -270    477    836       C  
ATOM   1388  CE3 TRP A 318      47.486  39.319  79.503  1.00129.62           C  
ANISOU 1388  CE3 TRP A 318    15770  18489  14988   -418    402    988       C  
ATOM   1389  CZ2 TRP A 318      47.420  41.148  77.336  1.00124.57           C  
ANISOU 1389  CZ2 TRP A 318    15338  17559  14430   -269    482    720       C  
ATOM   1390  CZ3 TRP A 318      48.650  39.790  78.914  1.00129.76           C  
ANISOU 1390  CZ3 TRP A 318    15887  18400  15015   -417    382    844       C  
ATOM   1391  CH2 TRP A 318      48.605  40.703  77.842  1.00125.75           C  
ANISOU 1391  CH2 TRP A 318    15480  17745  14553   -351    442    717       C  
ATOM   1392  N   PRO A 319      42.897  35.715  80.737  1.00130.06           N  
ANISOU 1392  N   PRO A 319    15197  18646  15572   -570    489   1731       N  
ATOM   1393  CA  PRO A 319      42.648  34.561  81.633  1.00137.30           C  
ANISOU 1393  CA  PRO A 319    16015  19605  16548   -665    547   1992       C  
ATOM   1394  C   PRO A 319      43.475  34.677  82.912  1.00141.00           C  
ANISOU 1394  C   PRO A 319    16612  20261  16701   -671    626   2082       C  
ATOM   1395  O   PRO A 319      44.533  35.277  82.908  1.00142.80           O  
ANISOU 1395  O   PRO A 319    16983  20526  16746   -629    555   1938       O  
ATOM   1396  CB  PRO A 319      43.100  33.343  80.816  1.00135.76           C  
ANISOU 1396  CB  PRO A 319    15784  19200  16599   -714    343   2054       C  
ATOM   1397  CG  PRO A 319      43.964  33.909  79.744  1.00129.53           C  
ANISOU 1397  CG  PRO A 319    15127  18320  15768   -641    197   1830       C  
ATOM   1398  CD  PRO A 319      43.503  35.307  79.462  1.00125.76           C  
ANISOU 1398  CD  PRO A 319    14699  17906  15177   -552    286   1641       C  
ATOM   1399  N   ILE A 320      42.970  34.073  83.969  1.00143.35           N  
ANISOU 1399  N   ILE A 320    16852  20663  16949   -718    772   2318       N  
ATOM   1400  CA  ILE A 320      43.472  34.174  85.320  1.00149.50           C  
ANISOU 1400  CA  ILE A 320    17756  21657  17390   -694    872   2427       C  
ATOM   1401  C   ILE A 320      44.920  33.738  85.469  1.00150.81           C  
ANISOU 1401  C   ILE A 320    18063  21804  17431   -682    680   2438       C  
ATOM   1402  O   ILE A 320      45.645  34.159  86.378  1.00153.18           O  
ANISOU 1402  O   ILE A 320    18499  22283  17417   -622    681   2404       O  
ATOM   1403  CB  ILE A 320      42.615  33.216  86.173  1.00152.88           C  
ANISOU 1403  CB  ILE A 320    18087  22126  17871   -760   1057   2750       C  
ATOM   1404  CG1 ILE A 320      42.569  31.764  85.575  1.00155.02           C  
ANISOU 1404  CG1 ILE A 320    18248  22146  18504   -859    935   2945       C  
ATOM   1405  CG2 ILE A 320      41.207  33.783  86.302  1.00155.04           C  
ANISOU 1405  CG2 ILE A 320    18208  22473  18226   -760   1293   2723       C  
ATOM   1406  CD1 ILE A 320      43.570  30.755  86.126  1.00160.17           C  
ANISOU 1406  CD1 ILE A 320    19020  22770  19064   -872    825   3160       C  
ATOM   1407  N   SER A 321      45.303  32.807  84.595  1.00148.55           N  
ANISOU 1407  N   SER A 321    17730  21300  17411   -733    502   2482       N  
ATOM   1408  CA  SER A 321      46.635  32.199  84.639  1.00146.53           C  
ANISOU 1408  CA  SER A 321    17569  20992  17110   -723    307   2504       C  
ATOM   1409  C   SER A 321      47.712  33.233  84.358  1.00141.79           C  
ANISOU 1409  C   SER A 321    17075  20439  16357   -660    210   2214       C  
ATOM   1410  O   SER A 321      48.896  32.989  84.650  1.00152.74           O  
ANISOU 1410  O   SER A 321    18540  21843  17650   -634     67   2187       O  
ATOM   1411  CB  SER A 321      46.722  31.035  83.682  1.00145.89           C  
ANISOU 1411  CB  SER A 321    17399  20655  17376   -782    150   2579       C  
ATOM   1412  OG  SER A 321      45.761  31.191  82.662  1.00147.26           O  
ANISOU 1412  OG  SER A 321    17447  20701  17801   -807    174   2483       O  
ATOM   1413  N   THR A 322      47.297  34.377  83.819  1.00132.79           N  
ANISOU 1413  N   THR A 322    15930  19310  15213   -634    292   1999       N  
ATOM   1414  CA  THR A 322      48.222  35.464  83.492  1.00136.36           C  
ANISOU 1414  CA  THR A 322    16472  19773  15564   -588    243   1722       C  
ATOM   1415  C   THR A 322      48.194  36.564  84.509  1.00141.16           C  
ANISOU 1415  C   THR A 322    17149  20595  15889   -534    362   1611       C  
ATOM   1416  O   THR A 322      48.921  37.560  84.341  1.00150.03           O  
ANISOU 1416  O   THR A 322    18334  21720  16949   -502    339   1367       O  
ATOM   1417  CB  THR A 322      47.818  36.123  82.189  1.00138.73           C  
ANISOU 1417  CB  THR A 322    16751  19921  16036   -575    261   1553       C  
ATOM   1418  OG1 THR A 322      46.540  36.732  82.369  1.00145.43           O  
ANISOU 1418  OG1 THR A 322    17550  20843  16863   -552    419   1557       O  
ATOM   1419  CG2 THR A 322      47.733  35.105  81.103  1.00141.94           C  
ANISOU 1419  CG2 THR A 322    17095  20124  16712   -607    137   1623       C  
ATOM   1420  N   LYS A 323      47.367  36.422  85.555  1.00140.55           N  
ANISOU 1420  N   LYS A 323    17060  20691  15651   -520    502   1774       N  
ATOM   1421  CA  LYS A 323      47.163  37.495  86.529  1.00144.00           C  
ANISOU 1421  CA  LYS A 323    17560  21346  15804   -449    634   1651       C  
ATOM   1422  C   LYS A 323      48.477  37.898  87.219  1.00146.01           C  
ANISOU 1422  C   LYS A 323    17928  21714  15834   -394    504   1490       C  
ATOM   1423  O   LYS A 323      48.733  39.092  87.453  1.00141.11           O  
ANISOU 1423  O   LYS A 323    17353  21169  15092   -344    535   1233       O  
ATOM   1424  CB  LYS A 323      46.124  37.065  87.585  1.00148.02           C  
ANISOU 1424  CB  LYS A 323    18046  22033  16163   -438    824   1892       C  
ATOM   1425  CG  LYS A 323      45.231  38.179  88.116  1.00154.32           C  
ANISOU 1425  CG  LYS A 323    18835  22995  16802   -376   1035   1767       C  
ATOM   1426  CD  LYS A 323      45.829  38.959  89.263  1.00160.95           C  
ANISOU 1426  CD  LYS A 323    19811  24072  17269   -275   1045   1613       C  
ATOM   1427  CE  LYS A 323      45.251  40.376  89.320  1.00165.33           C  
ANISOU 1427  CE  LYS A 323    20356  24700  17762   -211   1185   1350       C  
ATOM   1428  NZ  LYS A 323      46.058  41.272  90.190  1.00167.86           N  
ANISOU 1428  NZ  LYS A 323    20801  25192  17784   -115   1129   1104       N  
ATOM   1429  N   GLU A 324      49.301  36.890  87.521  1.00152.17           N  
ANISOU 1429  N   GLU A 324    18740  22488  16590   -399    345   1629       N  
ATOM   1430  CA  GLU A 324      50.585  37.100  88.166  1.00155.46           C  
ANISOU 1430  CA  GLU A 324    19237  23001  16826   -336    175   1479       C  
ATOM   1431  C   GLU A 324      51.709  37.293  87.154  1.00148.80           C  
ANISOU 1431  C   GLU A 324    18353  21962  16220   -377     15   1262       C  
ATOM   1432  O   GLU A 324      52.842  37.598  87.525  1.00156.42           O  
ANISOU 1432  O   GLU A 324    19343  22974  17113   -336   -131   1074       O  
ATOM   1433  CB  GLU A 324      50.898  35.919  89.089  1.00163.33           C  
ANISOU 1433  CB  GLU A 324    20299  24100  17658   -291     75   1747       C  
ATOM   1434  CG  GLU A 324      49.921  35.755  90.238  1.00175.34           C  
ANISOU 1434  CG  GLU A 324    21891  25839  18891   -235    264   1973       C  
ATOM   1435  CD  GLU A 324      49.611  37.071  90.955  1.00188.34           C  
ANISOU 1435  CD  GLU A 324    23595  27704  20261   -152    390   1742       C  
ATOM   1436  OE1 GLU A 324      50.561  37.833  91.251  1.00194.58           O  
ANISOU 1436  OE1 GLU A 324    24435  28568  20925    -84    243   1454       O  
ATOM   1437  OE2 GLU A 324      48.417  37.343  91.229  1.00200.87           O  
ANISOU 1437  OE2 GLU A 324    25160  29380  21779   -153    635   1832       O  
ATOM   1438  N   GLY A 325      51.372  37.156  85.878  1.00139.83           N  
ANISOU 1438  N   GLY A 325    17149  20611  15366   -448     53   1272       N  
ATOM   1439  CA  GLY A 325      52.344  37.289  84.805  1.00134.00           C  
ANISOU 1439  CA  GLY A 325    16381  19678  14854   -485    -48   1095       C  
ATOM   1440  C   GLY A 325      52.646  38.726  84.447  1.00131.15           C  
ANISOU 1440  C   GLY A 325    16040  19281  14510   -480     33    797       C  
ATOM   1441  O   GLY A 325      52.096  39.643  85.039  1.00128.42           O  
ANISOU 1441  O   GLY A 325    15727  19058  14006   -443    147    709       O  
ATOM   1442  N   LEU A 326      53.510  38.905  83.455  1.00130.93           N  
ANISOU 1442  N   LEU A 326    15989  19068  14688   -517     -8    649       N  
ATOM   1443  CA  LEU A 326      53.898  40.239  82.946  1.00128.54           C  
ANISOU 1443  CA  LEU A 326    15707  18669  14463   -528     92    384       C  
ATOM   1444  C   LEU A 326      54.361  41.149  84.095  1.00125.83           C  
ANISOU 1444  C   LEU A 326    15372  18482  13954   -494     76    175       C  
ATOM   1445  O   LEU A 326      53.717  42.122  84.418  1.00123.77           O  
ANISOU 1445  O   LEU A 326    15150  18281  13595   -464    198     82       O  
ATOM   1446  CB  LEU A 326      52.731  40.845  82.179  1.00129.54           C  
ANISOU 1446  CB  LEU A 326    15877  18710  14632   -516    260    417       C  
ATOM   1447  CG  LEU A 326      53.054  42.111  81.384  1.00131.25           C  
ANISOU 1447  CG  LEU A 326    16142  18763  14964   -521    383    203       C  
ATOM   1448  CD1 LEU A 326      54.077  41.851  80.292  1.00133.51           C  
ANISOU 1448  CD1 LEU A 326    16423  18849  15454   -564    362    149       C  
ATOM   1449  CD2 LEU A 326      51.780  42.630  80.771  1.00132.41           C  
ANISOU 1449  CD2 LEU A 326    16342  18850  15114   -475    514    262       C  
ATOM   1450  N   PRO A 327      55.466  40.804  84.743  1.00124.93           N  
ANISOU 1450  N   PRO A 327    15217  18439  13811   -483    -96     86       N  
ATOM   1451  CA  PRO A 327      55.924  41.432  85.968  1.00129.74           C  
ANISOU 1451  CA  PRO A 327    15831  19229  14232   -424   -177   -110       C  
ATOM   1452  C   PRO A 327      56.809  42.641  85.710  1.00133.22           C  
ANISOU 1452  C   PRO A 327    16218  19549  14850   -462   -151   -459       C  
ATOM   1453  O   PRO A 327      57.883  42.756  86.288  1.00137.39           O  
ANISOU 1453  O   PRO A 327    16678  20125  15398   -445   -314   -668       O  
ATOM   1454  CB  PRO A 327      56.686  40.299  86.636  1.00129.71           C  
ANISOU 1454  CB  PRO A 327    15804  19331  14147   -379   -411    -13       C  
ATOM   1455  CG  PRO A 327      57.326  39.622  85.497  1.00125.82           C  
ANISOU 1455  CG  PRO A 327    15237  18619  13947   -450   -452     29       C  
ATOM   1456  CD  PRO A 327      56.291  39.634  84.422  1.00123.92           C  
ANISOU 1456  CD  PRO A 327    15032  18238  13812   -502   -259    181       C  
ATOM   1457  N   ILE A 328      56.326  43.572  84.905  1.00137.36           N  
ANISOU 1457  N   ILE A 328    16770  19915  15505   -504     49   -528       N  
ATOM   1458  CA  ILE A 328      57.114  44.713  84.421  1.00142.90           C  
ANISOU 1458  CA  ILE A 328    17425  20428  16441   -563    130   -817       C  
ATOM   1459  C   ILE A 328      57.067  45.916  85.348  1.00144.67           C  
ANISOU 1459  C   ILE A 328    17653  20743  16571   -523    146  -1085       C  
ATOM   1460  O   ILE A 328      57.671  46.954  85.052  1.00142.54           O  
ANISOU 1460  O   ILE A 328    17336  20301  16520   -576    223  -1342       O  
ATOM   1461  CB  ILE A 328      56.600  45.125  83.036  1.00141.04           C  
ANISOU 1461  CB  ILE A 328    17251  19953  16383   -608    348   -732       C  
ATOM   1462  CG1 ILE A 328      55.206  45.768  83.131  1.00141.03           C  
ANISOU 1462  CG1 ILE A 328    17348  20002  16235   -548    488   -660       C  
ATOM   1463  CG2 ILE A 328      56.554  43.904  82.129  1.00137.94           C  
ANISOU 1463  CG2 ILE A 328    16863  19487  16060   -626    315   -488       C  
ATOM   1464  CD1 ILE A 328      54.620  46.209  81.808  1.00138.39           C  
ANISOU 1464  CD1 ILE A 328    17096  19444  16041   -554    670   -576       C  
ATOM   1465  N   GLN A 329      56.334  45.775  86.452  1.00143.65           N  
ANISOU 1465  N   GLN A 329    17581  20872  16125   -427     91  -1025       N  
ATOM   1466  CA  GLN A 329      55.996  46.876  87.361  1.00147.08           C  
ANISOU 1466  CA  GLN A 329    18045  21426  16409   -359    125  -1258       C  
ATOM   1467  C   GLN A 329      57.135  47.749  87.849  1.00151.50           C  
ANISOU 1467  C   GLN A 329    18517  21945  17098   -369     11  -1655       C  
ATOM   1468  O   GLN A 329      56.898  48.913  88.236  1.00153.66           O  
ANISOU 1468  O   GLN A 329    18804  22211  17369   -340     83  -1899       O  
ATOM   1469  CB  GLN A 329      55.172  46.422  88.576  1.00148.95           C  
ANISOU 1469  CB  GLN A 329    18362  21986  16246   -238     76  -1125       C  
ATOM   1470  CG  GLN A 329      55.411  45.004  89.076  1.00151.55           C  
ANISOU 1470  CG  GLN A 329    18705  22483  16393   -199    -93   -881       C  
ATOM   1471  CD  GLN A 329      54.482  44.000  88.422  1.00151.40           C  
ANISOU 1471  CD  GLN A 329    18716  22424  16385   -236     15   -494       C  
ATOM   1472  OE1 GLN A 329      53.642  44.365  87.615  1.00149.50           O  
ANISOU 1472  OE1 GLN A 329    18483  22051  16267   -277    199   -422       O  
ATOM   1473  NE2 GLN A 329      54.628  42.727  88.771  1.00155.77           N  
ANISOU 1473  NE2 GLN A 329    19283  23077  16823   -212   -110   -252       N  
ATOM   1474  N   GLY A 330      58.353  47.182  87.867  1.00154.60           N  
ANISOU 1474  N   GLY A 330    18804  22311  17623   -404   -176  -1738       N  
ATOM   1475  CA  GLY A 330      59.540  47.890  88.326  1.00161.53           C  
ANISOU 1475  CA  GLY A 330    19552  23142  18676   -418   -320  -2138       C  
ATOM   1476  C   GLY A 330      60.407  48.371  87.162  1.00162.67           C  
ANISOU 1476  C   GLY A 330    19573  22943  19288   -569   -194  -2270       C  
ATOM   1477  O   GLY A 330      61.364  49.118  87.359  1.00160.05           O  
ANISOU 1477  O   GLY A 330    19102  22502  19206   -616   -255  -2620       O  
ATOM   1478  N   TRP A 331      60.040  47.921  85.957  1.00160.80           N  
ANISOU 1478  N   TRP A 331    19390  22540  19165   -638    -12  -1988       N  
ATOM   1479  CA  TRP A 331      60.842  48.131  84.774  1.00155.67           C  
ANISOU 1479  CA  TRP A 331    18654  21587  18904   -765    131  -2038       C  
ATOM   1480  C   TRP A 331      60.132  49.053  83.793  1.00152.27           C  
ANISOU 1480  C   TRP A 331    18335  20923  18596   -812    437  -1968       C  
ATOM   1481  O   TRP A 331      60.632  50.128  83.490  1.00157.13           O  
ANISOU 1481  O   TRP A 331    18897  21313  19490   -887    577  -2191       O  
ATOM   1482  CB  TRP A 331      61.229  46.786  84.151  1.00150.81           C  
ANISOU 1482  CB  TRP A 331    18009  20966  18326   -783     61  -1805       C  
ATOM   1483  CG  TRP A 331      61.802  46.856  82.760  1.00143.33           C  
ANISOU 1483  CG  TRP A 331    17020  19724  17711   -892    266  -1775       C  
ATOM   1484  CD1 TRP A 331      62.685  47.771  82.255  1.00141.03           C  
ANISOU 1484  CD1 TRP A 331    16622  19185  17778   -998    422  -2014       C  
ATOM   1485  CD2 TRP A 331      61.533  45.942  81.711  1.00136.92           C  
ANISOU 1485  CD2 TRP A 331    16281  18842  16900   -898    345  -1491       C  
ATOM   1486  NE1 TRP A 331      62.969  47.483  80.942  1.00136.45           N  
ANISOU 1486  NE1 TRP A 331    16061  18393  17388  -1062    621  -1872       N  
ATOM   1487  CE2 TRP A 331      62.268  46.363  80.586  1.00135.75           C  
ANISOU 1487  CE2 TRP A 331    16087  18418  17073   -993    561  -1564       C  
ATOM   1488  CE3 TRP A 331      60.725  44.802  81.611  1.00134.70           C  
ANISOU 1488  CE3 TRP A 331    16096  18695  16390   -830    261  -1187       C  
ATOM   1489  CZ2 TRP A 331      62.221  45.683  79.378  1.00136.72           C  
ANISOU 1489  CZ2 TRP A 331    16276  18422  17248  -1001    682  -1354       C  
ATOM   1490  CZ3 TRP A 331      60.677  44.130  80.421  1.00134.51           C  
ANISOU 1490  CZ3 TRP A 331    16116  18536  16455   -848    356  -1000       C  
ATOM   1491  CH2 TRP A 331      61.417  44.573  79.310  1.00136.65           C  
ANISOU 1491  CH2 TRP A 331    16360  18556  17004   -922    560  -1088       C  
ATOM   1492  N   LEU A 332      58.968  48.634  83.310  1.00144.35           N  
ANISOU 1492  N   LEU A 332    17483  19962  17399   -760    532  -1661       N  
ATOM   1493  CA  LEU A 332      58.181  49.485  82.415  1.00142.66           C  
ANISOU 1493  CA  LEU A 332    17397  19547  17259   -764    786  -1582       C  
ATOM   1494  C   LEU A 332      57.090  50.236  83.175  1.00141.99           C  
ANISOU 1494  C   LEU A 332    17392  19588  16968   -674    811  -1632       C  
ATOM   1495  O   LEU A 332      56.651  51.308  82.765  1.00141.46           O  
ANISOU 1495  O   LEU A 332    17398  19343  17005   -669    990  -1694       O  
ATOM   1496  CB  LEU A 332      57.597  48.657  81.288  1.00143.03           C  
ANISOU 1496  CB  LEU A 332    17546  19533  17263   -749    866  -1259       C  
ATOM   1497  CG  LEU A 332      58.716  48.081  80.412  1.00144.57           C  
ANISOU 1497  CG  LEU A 332    17671  19568  17688   -831    889  -1244       C  
ATOM   1498  CD1 LEU A 332      58.148  47.094  79.411  1.00146.77           C  
ANISOU 1498  CD1 LEU A 332    18048  19828  17888   -793    913   -948       C  
ATOM   1499  CD2 LEU A 332      59.520  49.158  79.704  1.00142.10           C  
ANISOU 1499  CD2 LEU A 332    17338  18957  17694   -920   1110  -1420       C  
ATOM   1500  N   GLY A 333      56.657  49.688  84.290  1.00145.08           N  
ANISOU 1500  N   GLY A 333    17775  20280  17067   -594    644  -1604       N  
ATOM   1501  CA  GLY A 333      55.723  50.396  85.157  1.00153.44           C  
ANISOU 1501  CA  GLY A 333    18890  21491  17919   -500    670  -1692       C  
ATOM   1502  C   GLY A 333      54.324  49.807  85.260  1.00157.19           C  
ANISOU 1502  C   GLY A 333    19453  22144  18128   -414    712  -1408       C  
ATOM   1503  O   GLY A 333      54.012  48.843  84.602  1.00161.93           O  
ANISOU 1503  O   GLY A 333    20073  22733  18717   -430    714  -1136       O  
ATOM   1504  N   THR A 334      53.483  50.472  86.023  1.00157.18           N  
ANISOU 1504  N   THR A 334    19490  22278  17953   -324    763  -1500       N  
ATOM   1505  CA  THR A 334      52.183  49.964  86.458  1.00154.35           C  
ANISOU 1505  CA  THR A 334    19176  22141  17328   -236    805  -1283       C  
ATOM   1506  C   THR A 334      51.083  50.348  85.442  1.00143.90           C  
ANISOU 1506  C   THR A 334    17906  20648  16120   -214    983  -1139       C  
ATOM   1507  O   THR A 334      50.153  49.588  85.123  1.00138.86           O  
ANISOU 1507  O   THR A 334    17275  20075  15410   -189   1015   -878       O  
ATOM   1508  CB  THR A 334      51.939  50.553  87.876  1.00165.44           C  
ANISOU 1508  CB  THR A 334    20586  23793  18479   -133    774  -1502       C  
ATOM   1509  OG1 THR A 334      51.861  51.997  87.816  1.00173.84           O  
ANISOU 1509  OG1 THR A 334    21660  24699  19690   -111    875  -1787       O  
ATOM   1510  CG2 THR A 334      53.074  50.096  88.839  1.00169.05           C  
ANISOU 1510  CG2 THR A 334    21004  24425  18802   -126    550  -1644       C  
ATOM   1511  N   LYS A 335      51.217  51.578  84.959  1.00141.48           N  
ANISOU 1511  N   LYS A 335    17634  20110  16012   -216   1089  -1331       N  
ATOM   1512  CA  LYS A 335      50.322  52.155  83.950  1.00143.09           C  
ANISOU 1512  CA  LYS A 335    17912  20112  16342   -171   1240  -1236       C  
ATOM   1513  C   LYS A 335      50.461  51.444  82.604  1.00140.54           C  
ANISOU 1513  C   LYS A 335    17631  19611  16154   -220   1250  -1000       C  
ATOM   1514  O   LYS A 335      49.502  51.263  81.850  1.00138.39           O  
ANISOU 1514  O   LYS A 335    17409  19284  15886   -157   1300   -819       O  
ATOM   1515  CB  LYS A 335      50.646  53.636  83.744  1.00147.83           C  
ANISOU 1515  CB  LYS A 335    18556  20465  17148   -167   1348  -1493       C  
ATOM   1516  CG  LYS A 335      50.610  54.509  84.980  1.00153.53           C  
ANISOU 1516  CG  LYS A 335    19238  21314  17781   -112   1334  -1794       C  
ATOM   1517  CD  LYS A 335      50.686  55.987  84.639  1.00155.94           C  
ANISOU 1517  CD  LYS A 335    19590  21326  18331    -97   1460  -2017       C  
ATOM   1518  CE  LYS A 335      52.058  56.387  84.113  1.00160.39           C  
ANISOU 1518  CE  LYS A 335    20134  21609  19196   -230   1477  -2153       C  
ATOM   1519  NZ  LYS A 335      53.218  55.990  84.972  1.00163.26           N  
ANISOU 1519  NZ  LYS A 335    20373  22118  19539   -309   1309  -2350       N  
ATOM   1520  N   VAL A 336      51.687  51.095  82.289  1.00138.80           N  
ANISOU 1520  N   VAL A 336    17387  19294  16057   -320   1196  -1031       N  
ATOM   1521  CA  VAL A 336      52.070  50.333  81.102  1.00137.51           C  
ANISOU 1521  CA  VAL A 336    17256  18983  16007   -369   1196   -844       C  
ATOM   1522  C   VAL A 336      51.435  48.945  81.149  1.00137.36           C  
ANISOU 1522  C   VAL A 336    17201  19153  15834   -348   1082   -594       C  
ATOM   1523  O   VAL A 336      50.724  48.536  80.244  1.00133.43           O  
ANISOU 1523  O   VAL A 336    16755  18585  15357   -305   1103   -412       O  
ATOM   1524  CB  VAL A 336      53.595  50.207  81.076  1.00136.68           C  
ANISOU 1524  CB  VAL A 336    17083  18788  16060   -482   1152   -977       C  
ATOM   1525  CG1 VAL A 336      54.041  49.516  79.785  1.00137.49           C  
ANISOU 1525  CG1 VAL A 336    17228  18723  16288   -523   1187   -808       C  
ATOM   1526  CG2 VAL A 336      54.225  51.592  81.219  1.00137.26           C  
ANISOU 1526  CG2 VAL A 336    17152  18674  16325   -520   1263  -1254       C  
ATOM   1527  N   ARG A 337      51.719  48.219  82.209  1.00137.74           N  
ANISOU 1527  N   ARG A 337    17163  19431  15738   -371    953   -593       N  
ATOM   1528  CA  ARG A 337      51.185  46.870  82.410  1.00139.05           C  
ANISOU 1528  CA  ARG A 337    17288  19766  15777   -363    855   -349       C  
ATOM   1529  C   ARG A 337      49.646  46.896  82.375  1.00146.90           C  
ANISOU 1529  C   ARG A 337    18291  20830  16691   -283    934   -214       C  
ATOM   1530  O   ARG A 337      49.012  46.017  81.778  1.00147.24           O  
ANISOU 1530  O   ARG A 337    18317  20858  16770   -278    905     -7       O  
ATOM   1531  CB  ARG A 337      51.632  46.364  83.773  1.00135.83           C  
ANISOU 1531  CB  ARG A 337    16820  19606  15182   -368    731   -383       C  
ATOM   1532  CG  ARG A 337      51.142  44.974  84.118  1.00134.87           C  
ANISOU 1532  CG  ARG A 337    16664  19645  14933   -364    649   -113       C  
ATOM   1533  CD  ARG A 337      51.853  44.387  85.320  1.00137.74           C  
ANISOU 1533  CD  ARG A 337    17003  20216  15115   -356    504   -125       C  
ATOM   1534  NE  ARG A 337      51.551  42.959  85.432  1.00138.48           N  
ANISOU 1534  NE  ARG A 337    17075  20390  15152   -367    430    166       N  
ATOM   1535  CZ  ARG A 337      50.414  42.442  85.902  1.00143.31           C  
ANISOU 1535  CZ  ARG A 337    17682  21139  15628   -336    505    380       C  
ATOM   1536  NH1 ARG A 337      49.451  43.225  86.361  1.00151.00           N  
ANISOU 1536  NH1 ARG A 337    18669  22219  16484   -279    656    326       N  
ATOM   1537  NH2 ARG A 337      50.234  41.121  85.926  1.00141.56           N  
ANISOU 1537  NH2 ARG A 337    17433  20939  15414   -363    442    648       N  
ATOM   1538  N   THR A 338      49.065  47.906  83.024  1.00155.40           N  
ANISOU 1538  N   THR A 338    19380  21979  17685   -219   1027   -355       N  
ATOM   1539  CA  THR A 338      47.624  48.040  83.074  1.00157.02           C  
ANISOU 1539  CA  THR A 338    19566  22257  17837   -135   1114   -267       C  
ATOM   1540  C   THR A 338      47.054  48.262  81.675  1.00155.24           C  
ANISOU 1540  C   THR A 338    19392  21801  17788    -91   1152   -192       C  
ATOM   1541  O   THR A 338      46.028  47.672  81.313  1.00156.98           O  
ANISOU 1541  O   THR A 338    19563  22051  18028    -50   1141    -32       O  
ATOM   1542  CB  THR A 338      47.207  49.158  83.998  1.00161.89           C  
ANISOU 1542  CB  THR A 338    20186  22979  18346    -61   1210   -469       C  
ATOM   1543  OG1 THR A 338      47.601  48.789  85.317  1.00169.30           O  
ANISOU 1543  OG1 THR A 338    21090  24171  19063    -71   1156   -512       O  
ATOM   1544  CG2 THR A 338      45.699  49.391  83.934  1.00163.84           C  
ANISOU 1544  CG2 THR A 338    20394  23274  18584     35   1314   -400       C  
ATOM   1545  N   ASN A 339      47.720  49.108  80.900  1.00152.91           N  
ANISOU 1545  N   ASN A 339    19198  21275  17625    -93   1196   -311       N  
ATOM   1546  CA  ASN A 339      47.281  49.373  79.536  1.00154.29           C  
ANISOU 1546  CA  ASN A 339    19469  21226  17926    -24   1231   -236       C  
ATOM   1547  C   ASN A 339      47.483  48.195  78.596  1.00142.53           C  
ANISOU 1547  C   ASN A 339    17987  19679  16486    -54   1131    -55       C  
ATOM   1548  O   ASN A 339      46.736  48.009  77.655  1.00141.03           O  
ANISOU 1548  O   ASN A 339    17840  19400  16342     30   1105     45       O  
ATOM   1549  CB  ASN A 339      48.016  50.573  78.965  1.00162.10           C  
ANISOU 1549  CB  ASN A 339    20587  21965  19038    -20   1339   -383       C  
ATOM   1550  CG  ASN A 339      47.528  51.872  79.542  1.00169.21           C  
ANISOU 1550  CG  ASN A 339    21505  22844  19940     51   1439   -558       C  
ATOM   1551  OD1 ASN A 339      46.612  51.904  80.359  1.00167.15           O  
ANISOU 1551  OD1 ASN A 339    21161  22773  19573    110   1434   -582       O  
ATOM   1552  ND2 ASN A 339      48.144  52.963  79.118  1.00176.80           N  
ANISOU 1552  ND2 ASN A 339    22572  23562  21042     47   1547   -686       N  
ATOM   1553  N   LEU A 340      48.515  47.407  78.844  1.00133.78           N  
ANISOU 1553  N   LEU A 340    16835  18619  15374   -161   1060    -35       N  
ATOM   1554  CA  LEU A 340      48.808  46.250  78.017  1.00137.31           C  
ANISOU 1554  CA  LEU A 340    17280  19012  15879   -191    960    111       C  
ATOM   1555  C   LEU A 340      47.806  45.148  78.276  1.00134.41           C  
ANISOU 1555  C   LEU A 340    16803  18792  15474   -177    861    280       C  
ATOM   1556  O   LEU A 340      47.342  44.510  77.340  1.00140.42           O  
ANISOU 1556  O   LEU A 340    17573  19472  16308   -135    790    385       O  
ATOM   1557  CB  LEU A 340      50.186  45.722  78.330  1.00145.21           C  
ANISOU 1557  CB  LEU A 340    18239  20027  16905   -300    905     69       C  
ATOM   1558  CG  LEU A 340      51.250  46.502  77.557  1.00153.70           C  
ANISOU 1558  CG  LEU A 340    19409  20882  18106   -328   1010    -55       C  
ATOM   1559  CD1 LEU A 340      52.594  46.488  78.279  1.00157.24           C  
ANISOU 1559  CD1 LEU A 340    19773  21366  18604   -434    981   -199       C  
ATOM   1560  CD2 LEU A 340      51.353  45.997  76.114  1.00154.16           C  
ANISOU 1560  CD2 LEU A 340    19563  20773  18238   -290   1013     54       C  
ATOM   1561  N   ARG A 341      47.452  44.932  79.542  1.00133.79           N  
ANISOU 1561  N   ARG A 341    16623  18925  15286   -205    862    300       N  
ATOM   1562  CA  ARG A 341      46.471  43.906  79.896  1.00141.02           C  
ANISOU 1562  CA  ARG A 341    17419  19971  16190   -208    813    477       C  
ATOM   1563  C   ARG A 341      45.024  44.315  79.568  1.00145.91           C  
ANISOU 1563  C   ARG A 341    17996  20579  16862   -111    869    491       C  
ATOM   1564  O   ARG A 341      44.103  43.469  79.687  1.00151.55           O  
ANISOU 1564  O   ARG A 341    18582  21363  17634   -117    838    630       O  
ATOM   1565  CB  ARG A 341      46.545  43.589  81.381  1.00144.68           C  
ANISOU 1565  CB  ARG A 341    17811  20668  16489   -254    835    515       C  
ATOM   1566  CG  ARG A 341      47.819  42.898  81.770  1.00144.08           C  
ANISOU 1566  CG  ARG A 341    17746  20626  16370   -331    729    534       C  
ATOM   1567  CD  ARG A 341      47.848  42.650  83.265  1.00147.53           C  
ANISOU 1567  CD  ARG A 341    18151  21308  16596   -338    740    575       C  
ATOM   1568  NE  ARG A 341      46.871  41.636  83.653  1.00147.15           N  
ANISOU 1568  NE  ARG A 341    18016  21363  16530   -349    764    816       N  
ATOM   1569  CZ  ARG A 341      47.040  40.314  83.523  1.00150.67           C  
ANISOU 1569  CZ  ARG A 341    18415  21776  17053   -406    663   1018       C  
ATOM   1570  NH1 ARG A 341      48.163  39.791  83.000  1.00153.04           N  
ANISOU 1570  NH1 ARG A 341    18746  21959  17442   -446    517   1004       N  
ATOM   1571  NH2 ARG A 341      46.062  39.500  83.920  1.00155.06           N  
ANISOU 1571  NH2 ARG A 341    18882  22406  17627   -425    722   1235       N  
ATOM   1572  N   ARG A 342      44.831  45.574  79.178  1.00144.63           N  
ANISOU 1572  N   ARG A 342    17927  20318  16708    -23    948    348       N  
ATOM   1573  CA  ARG A 342      43.536  46.046  78.704  1.00149.62           C  
ANISOU 1573  CA  ARG A 342    18530  20906  17411     97    972    338       C  
ATOM   1574  C   ARG A 342      43.346  45.700  77.238  1.00143.66           C  
ANISOU 1574  C   ARG A 342    17842  19964  16777    168    857    392       C  
ATOM   1575  O   ARG A 342      42.234  45.863  76.706  1.00149.03           O  
ANISOU 1575  O   ARG A 342    18482  20603  17537    285    817    393       O  
ATOM   1576  CB  ARG A 342      43.464  47.563  78.827  1.00159.47           C  
ANISOU 1576  CB  ARG A 342    19874  22091  18624    183   1089    164       C  
ATOM   1577  CG  ARG A 342      42.981  48.095  80.136  1.00169.55           C  
ANISOU 1577  CG  ARG A 342    21062  23560  19797    192   1202     76       C  
ATOM   1578  CD  ARG A 342      43.129  49.597  80.087  1.00175.44           C  
ANISOU 1578  CD  ARG A 342    21925  24185  20549    273   1295   -119       C  
ATOM   1579  NE  ARG A 342      42.803  50.263  81.332  1.00182.63           N  
ANISOU 1579  NE  ARG A 342    22773  25266  21351    297   1403   -258       N  
ATOM   1580  CZ  ARG A 342      42.792  51.582  81.482  1.00189.11           C  
ANISOU 1580  CZ  ARG A 342    23665  25997  22189    375   1488   -453       C  
ATOM   1581  NH1 ARG A 342      43.043  52.403  80.448  1.00189.04           N  
ANISOU 1581  NH1 ARG A 342    23800  25713  22313    435   1494   -503       N  
ATOM   1582  NH2 ARG A 342      42.495  52.118  82.675  1.00194.25           N  
ANISOU 1582  NH2 ARG A 342    24254  26826  22724    406   1578   -601       N  
ATOM   1583  N   GLU A 343      44.421  45.238  76.609  1.00137.78           N  
ANISOU 1583  N   GLU A 343    17192  19115  16041    113    797    420       N  
ATOM   1584  CA  GLU A 343      44.422  44.916  75.195  1.00136.68           C  
ANISOU 1584  CA  GLU A 343    17154  18806  15972    194    696    454       C  
ATOM   1585  C   GLU A 343      43.816  43.554  74.994  1.00126.92           C  
ANISOU 1585  C   GLU A 343    15769  17618  14834    174    541    567       C  
ATOM   1586  O   GLU A 343      43.739  42.792  75.987  1.00123.73           O  
ANISOU 1586  O   GLU A 343    15208  17361  14443     60    541    647       O  
ATOM   1587  CB  GLU A 343      45.850  44.765  74.688  1.00146.76           C  
ANISOU 1587  CB  GLU A 343    18557  19973  17231    129    710    441       C  
ATOM   1588  CG  GLU A 343      46.693  46.012  74.743  1.00161.79           C  
ANISOU 1588  CG  GLU A 343    20599  21777  19096    121    870    326       C  
ATOM   1589  CD  GLU A 343      47.298  46.279  73.404  1.00175.40           C  
ANISOU 1589  CD  GLU A 343    22518  23289  20834    189    909    327       C  
ATOM   1590  OE1 GLU A 343      48.478  45.895  73.197  1.00183.70           O  
ANISOU 1590  OE1 GLU A 343    23595  24290  21912     98    936    320       O  
ATOM   1591  OE2 GLU A 343      46.546  46.823  72.557  1.00185.91           O  
ANISOU 1591  OE2 GLU A 343    23977  24513  22147    347    907    340       O  
ATOM   1592  N   PRO A 344      43.442  43.207  73.753  1.00126.14           N  
ANISOU 1592  N   PRO A 344    15727  17394  14804    283    409    573       N  
ATOM   1593  CA  PRO A 344      42.889  41.864  73.569  1.00127.90           C  
ANISOU 1593  CA  PRO A 344    15786  17641  15167    253    245    653       C  
ATOM   1594  C   PRO A 344      43.961  40.796  73.702  1.00121.85           C  
ANISOU 1594  C   PRO A 344    15003  16877  14418    120    198    723       C  
ATOM   1595  O   PRO A 344      45.132  41.120  73.679  1.00113.44           O  
ANISOU 1595  O   PRO A 344    14065  15776  13259     78    272    691       O  
ATOM   1596  CB  PRO A 344      42.350  41.886  72.119  1.00133.43           C  
ANISOU 1596  CB  PRO A 344    16586  18199  15909    436     91    595       C  
ATOM   1597  CG  PRO A 344      42.659  43.227  71.574  1.00135.44           C  
ANISOU 1597  CG  PRO A 344    17081  18357  16022    562    197    524       C  
ATOM   1598  CD  PRO A 344      43.744  43.822  72.459  1.00131.59           C  
ANISOU 1598  CD  PRO A 344    16646  17908  15441    425    396    519       C  
ATOM   1599  N   PHE A 345      43.561  39.542  73.851  1.00121.60           N  
ANISOU 1599  N   PHE A 345    14800  16869  14532     55     78    812       N  
ATOM   1600  CA  PHE A 345      44.527  38.450  73.824  1.00120.69           C  
ANISOU 1600  CA  PHE A 345    14674  16722  14461    -43      1    876       C  
ATOM   1601  C   PHE A 345      44.167  37.495  72.700  1.00121.69           C  
ANISOU 1601  C   PHE A 345    14767  16722  14745     22   -199    858       C  
ATOM   1602  O   PHE A 345      43.122  37.623  72.066  1.00128.18           O  
ANISOU 1602  O   PHE A 345    15553  17502  15648    137   -291    800       O  
ATOM   1603  CB  PHE A 345      44.600  37.741  75.158  1.00123.49           C  
ANISOU 1603  CB  PHE A 345    14874  17203  14841   -191     45   1013       C  
ATOM   1604  CG  PHE A 345      43.303  37.142  75.571  1.00128.37           C  
ANISOU 1604  CG  PHE A 345    15286  17865  15621   -218     24   1108       C  
ATOM   1605  CD1 PHE A 345      42.383  37.899  76.297  1.00132.45           C  
ANISOU 1605  CD1 PHE A 345    15729  18502  16094   -200    163   1107       C  
ATOM   1606  CD2 PHE A 345      42.979  35.845  75.212  1.00129.29           C  
ANISOU 1606  CD2 PHE A 345    15269  17891  15963   -260   -123   1182       C  
ATOM   1607  CE1 PHE A 345      41.167  37.361  76.674  1.00134.52           C  
ANISOU 1607  CE1 PHE A 345    15774  18799  16536   -231    178   1190       C  
ATOM   1608  CE2 PHE A 345      41.775  35.294  75.607  1.00132.15           C  
ANISOU 1608  CE2 PHE A 345    15412  18271  16526   -303   -118   1268       C  
ATOM   1609  CZ  PHE A 345      40.861  36.055  76.335  1.00135.74           C  
ANISOU 1609  CZ  PHE A 345    15782  18852  16939   -291     43   1276       C  
ATOM   1610  N   TYR A 346      45.023  36.532  72.450  1.00119.08           N  
ANISOU 1610  N   TYR A 346    14442  16331  14471    -35   -286    885       N  
ATOM   1611  CA  TYR A 346      44.952  35.733  71.228  1.00119.45           C  
ANISOU 1611  CA  TYR A 346    14508  16244  14631     52   -478    818       C  
ATOM   1612  C   TYR A 346      45.098  34.247  71.493  1.00118.43           C  
ANISOU 1612  C   TYR A 346    14215  16072  14710    -55   -609    902       C  
ATOM   1613  O   TYR A 346      45.882  33.866  72.356  1.00114.47           O  
ANISOU 1613  O   TYR A 346    13678  15618  14194   -179   -545   1003       O  
ATOM   1614  CB  TYR A 346      46.033  36.195  70.270  1.00120.40           C  
ANISOU 1614  CB  TYR A 346    14865  16287  14595    140   -441    721       C  
ATOM   1615  CG  TYR A 346      45.879  37.635  69.868  1.00122.48           C  
ANISOU 1615  CG  TYR A 346    15314  16546  14677    261   -310    655       C  
ATOM   1616  CD1 TYR A 346      46.567  38.654  70.548  1.00124.57           C  
ANISOU 1616  CD1 TYR A 346    15657  16859  14813    195    -99    662       C  
ATOM   1617  CD2 TYR A 346      45.029  37.993  68.829  1.00125.59           C  
ANISOU 1617  CD2 TYR A 346    15804  16874  15038    451   -410    577       C  
ATOM   1618  CE1 TYR A 346      46.424  39.973  70.181  1.00128.25           C  
ANISOU 1618  CE1 TYR A 346    16295  17287  15148    301     27    608       C  
ATOM   1619  CE2 TYR A 346      44.870  39.311  68.456  1.00127.96           C  
ANISOU 1619  CE2 TYR A 346    16293  17149  15175    578   -293    538       C  
ATOM   1620  CZ  TYR A 346      45.562  40.300  69.122  1.00129.53           C  
ANISOU 1620  CZ  TYR A 346    16569  17374  15271    497    -63    561       C  
ATOM   1621  OH  TYR A 346      45.395  41.618  68.743  1.00133.06           O  
ANISOU 1621  OH  TYR A 346    17206  17762  15588    621     59    528       O  
ATOM   1622  N   LEU A 347      44.396  33.428  70.727  1.00121.08           N  
ANISOU 1622  N   LEU A 347    14458  16305  15242      3   -805    849       N  
ATOM   1623  CA  LEU A 347      44.465  31.988  70.876  1.00121.37           C  
ANISOU 1623  CA  LEU A 347    14333  16257  15525    -92   -942    916       C  
ATOM   1624  C   LEU A 347      44.811  31.352  69.531  1.00120.29           C  
ANISOU 1624  C   LEU A 347    14275  15979  15449     26  -1143    760       C  
ATOM   1625  O   LEU A 347      44.180  31.579  68.505  1.00122.57           O  
ANISOU 1625  O   LEU A 347    14617  16219  15733    185  -1271    611       O  
ATOM   1626  CB  LEU A 347      43.135  31.464  71.357  1.00121.31           C  
ANISOU 1626  CB  LEU A 347    14075  16239  15778   -156   -989    988       C  
ATOM   1627  CG  LEU A 347      43.058  31.650  72.858  1.00121.50           C  
ANISOU 1627  CG  LEU A 347    14012  16398  15754   -304   -779   1187       C  
ATOM   1628  CD1 LEU A 347      41.632  31.899  73.291  1.00122.41           C  
ANISOU 1628  CD1 LEU A 347    13937  16562  16009   -319   -717   1219       C  
ATOM   1629  CD2 LEU A 347      43.674  30.435  73.541  1.00124.07           C  
ANISOU 1629  CD2 LEU A 347    14255  16672  16211   -444   -799   1357       C  
ATOM   1630  N   VAL A 348      45.813  30.517  69.519  1.00116.39           N  
ANISOU 1630  N   VAL A 348    13791  15423  15009    -30  -1187    781       N  
ATOM   1631  CA  VAL A 348      46.215  29.844  68.289  1.00114.90           C  
ANISOU 1631  CA  VAL A 348    13675  15107  14874     86  -1367    621       C  
ATOM   1632  C   VAL A 348      46.017  28.365  68.498  1.00117.60           C  
ANISOU 1632  C   VAL A 348    13807  15321  15552     -5  -1541    665       C  
ATOM   1633  O   VAL A 348      45.985  27.927  69.630  1.00118.56           O  
ANISOU 1633  O   VAL A 348    13787  15460  15798   -165  -1473    854       O  
ATOM   1634  CB  VAL A 348      47.637  30.184  67.918  1.00113.63           C  
ANISOU 1634  CB  VAL A 348    13713  14957  14503    124  -1257    569       C  
ATOM   1635  CG1 VAL A 348      47.791  31.686  67.796  1.00110.86           C  
ANISOU 1635  CG1 VAL A 348    13556  14701  13863    193  -1056    546       C  
ATOM   1636  CG2 VAL A 348      48.614  29.609  68.913  1.00117.49           C  
ANISOU 1636  CG2 VAL A 348    14118  15459  15063    -33  -1195    698       C  
ATOM   1637  N   PRO A 349      45.875  27.579  67.419  1.00123.70           N  
ANISOU 1637  N   PRO A 349    14567  15958  16472    102  -1767    492       N  
ATOM   1638  CA  PRO A 349      45.823  26.119  67.574  1.00128.37           C  
ANISOU 1638  CA  PRO A 349    14963  16389  17420     12  -1938    519       C  
ATOM   1639  C   PRO A 349      47.090  25.550  68.205  1.00128.33           C  
ANISOU 1639  C   PRO A 349    14974  16364  17421    -92  -1866    644       C  
ATOM   1640  O   PRO A 349      48.197  25.898  67.789  1.00121.78           O  
ANISOU 1640  O   PRO A 349    14318  15574  16378    -22  -1800    564       O  
ATOM   1641  CB  PRO A 349      45.683  25.620  66.142  1.00131.91           C  
ANISOU 1641  CB  PRO A 349    15462  16719  17937    195  -2187    250       C  
ATOM   1642  CG  PRO A 349      45.017  26.743  65.429  1.00132.20           C  
ANISOU 1642  CG  PRO A 349    15640  16853  17735    365  -2184    123       C  
ATOM   1643  CD  PRO A 349      45.606  27.985  66.031  1.00129.30           C  
ANISOU 1643  CD  PRO A 349    15437  16647  17042    327  -1893    262       C  
ATOM   1644  N   LYS A 350      46.929  24.664  69.175  1.00134.36           N  
ANISOU 1644  N   LYS A 350    15555  17054  18440   -250  -1878    836       N  
ATOM   1645  CA  LYS A 350      48.057  23.945  69.758  1.00143.48           C  
ANISOU 1645  CA  LYS A 350    16710  18160  19646   -327  -1867    954       C  
ATOM   1646  C   LYS A 350      48.650  23.007  68.715  1.00149.26           C  
ANISOU 1646  C   LYS A 350    17453  18720  20537   -230  -2071    757       C  
ATOM   1647  O   LYS A 350      49.872  22.889  68.622  1.00156.73           O  
ANISOU 1647  O   LYS A 350    18492  19671  21387   -198  -2049    719       O  
ATOM   1648  CB  LYS A 350      47.569  23.071  70.924  1.00151.04           C  
ANISOU 1648  CB  LYS A 350    17478  19038  20872   -493  -1856   1220       C  
ATOM   1649  CG  LYS A 350      48.591  22.111  71.564  1.00155.43           C  
ANISOU 1649  CG  LYS A 350    18016  19501  21537   -558  -1894   1369       C  
ATOM   1650  CD  LYS A 350      47.876  21.033  72.365  1.00154.85           C  
ANISOU 1650  CD  LYS A 350    17756  19270  21809   -694  -1923   1610       C  
ATOM   1651  CE  LYS A 350      48.758  20.248  73.313  1.00151.06           C  
ANISOU 1651  CE  LYS A 350    17284  18730  21381   -758  -1921   1843       C  
ATOM   1652  NZ  LYS A 350      48.032  18.991  73.721  1.00150.96           N  
ANISOU 1652  NZ  LYS A 350    17090  18475  21791   -869  -1983   2041       N  
ATOM   1653  N   ASN A 351      47.775  22.271  68.019  1.00153.18           N  
ANISOU 1653  N   ASN A 351    17829  19058  21315   -189  -2276    628       N  
ATOM   1654  CA  ASN A 351      48.155  21.407  66.913  1.00163.81           C  
ANISOU 1654  CA  ASN A 351    19185  20241  22814    -68  -2497    388       C  
ATOM   1655  C   ASN A 351      49.295  20.418  67.286  1.00172.03           C  
ANISOU 1655  C   ASN A 351    20194  21161  24006   -122  -2535    460       C  
ATOM   1656  O   ASN A 351      50.169  20.089  66.472  1.00168.49           O  
ANISOU 1656  O   ASN A 351    19835  20661  23523     -2  -2617    266       O  
ATOM   1657  CB  ASN A 351      48.492  22.183  65.633  1.00166.28           C  
ANISOU 1657  CB  ASN A 351    19721  20648  22808    143  -2505    122       C  
ATOM   1658  CG  ASN A 351      48.483  21.302  64.369  1.00173.89           C  
ANISOU 1658  CG  ASN A 351    20686  21452  23929    303  -2769   -170       C  
ATOM   1659  OD1 ASN A 351      47.513  20.587  64.088  1.00184.69           O  
ANISOU 1659  OD1 ASN A 351    21888  22676  25609    308  -2991   -268       O  
ATOM   1660  ND2 ASN A 351      49.580  21.372  63.596  1.00175.87           N  
ANISOU 1660  ND2 ASN A 351    21119  21732  23971    441  -2738   -328       N  
ATOM   1661  N   ALA A 352      49.226  19.922  68.516  1.00184.73           N  
ANISOU 1661  N   ALA A 352    21676  22722  25791   -289  -2477    743       N  
ATOM   1662  CA  ALA A 352      50.075  18.813  68.919  1.00191.34           C  
ANISOU 1662  CA  ALA A 352    22453  23398  26848   -334  -2561    835       C  
ATOM   1663  C   ALA A 352      49.624  17.576  68.163  1.00197.15           C  
ANISOU 1663  C   ALA A 352    23047  23859  28001   -301  -2817    673       C  
ATOM   1664  O   ALA A 352      48.446  17.410  67.873  1.00198.88           O  
ANISOU 1664  O   ALA A 352    23141  23992  28429   -324  -2906    614       O  
ATOM   1665  CB  ALA A 352      49.975  18.590  70.423  1.00194.54           C  
ANISOU 1665  CB  ALA A 352    22782  23815  27316   -500  -2439   1202       C  
ATOM   1666  N   LYS A 353      50.555  16.676  67.882  1.00201.00           N  
ANISOU 1666  N   LYS A 353    23531  24192  28645   -248  -2946    590       N  
ATOM   1667  CA  LYS A 353      50.230  15.421  67.206  1.00207.54           C  
ANISOU 1667  CA  LYS A 353    24219  24731  29903   -214  -3205    419       C  
ATOM   1668  C   LYS A 353      50.481  14.213  68.109  1.00217.19           C  
ANISOU 1668  C   LYS A 353    25305  25713  31503   -338  -3263    667       C  
ATOM   1669  O   LYS A 353      51.045  13.210  67.669  1.00227.50           O  
ANISOU 1669  O   LYS A 353    26566  26804  33069   -275  -3444    533       O  
ATOM   1670  CB  LYS A 353      51.047  15.323  65.900  1.00207.65           C  
ANISOU 1670  CB  LYS A 353    24353  24739  29803     -7  -3329     52       C  
ATOM   1671  CG  LYS A 353      51.060  16.581  65.019  1.00207.53           C  
ANISOU 1671  CG  LYS A 353    24537  24973  29340    140  -3227   -153       C  
ATOM   1672  CD  LYS A 353      49.700  16.884  64.410  1.00214.19           C  
ANISOU 1672  CD  LYS A 353    25341  25822  30218    187  -3334   -292       C  
ATOM   1673  CE  LYS A 353      49.786  17.854  63.250  1.00219.62           C  
ANISOU 1673  CE  LYS A 353    26254  26692  30498    399  -3306   -551       C  
ATOM   1674  NZ  LYS A 353      48.467  17.968  62.562  1.00227.80           N  
ANISOU 1674  NZ  LYS A 353    27239  27703  31610    485  -3489   -732       N  
ATOM   1675  N   ASP A 354      50.077  14.332  69.371  1.00222.46           N  
ANISOU 1675  N   ASP A 354    25923  26418  32182   -500  -3101   1032       N  
ATOM   1676  CA  ASP A 354      50.452  13.398  70.435  1.00227.94           C  
ANISOU 1676  CA  ASP A 354    26555  26938  33113   -604  -3097   1350       C  
ATOM   1677  C   ASP A 354      49.445  12.265  70.622  1.00220.41           C  
ANISOU 1677  C   ASP A 354    25388  25656  32702   -728  -3194   1471       C  
ATOM   1678  O   ASP A 354      49.768  11.221  71.206  1.00225.50           O  
ANISOU 1678  O   ASP A 354    25975  26060  33644   -785  -3249   1680       O  
ATOM   1679  CB  ASP A 354      50.693  14.134  71.780  1.00236.56           C  
ANISOU 1679  CB  ASP A 354    27746  28263  33871   -687  -2855   1699       C  
ATOM   1680  CG  ASP A 354      49.633  15.215  72.095  1.00244.22           C  
ANISOU 1680  CG  ASP A 354    28716  29452  34622   -761  -2656   1776       C  
ATOM   1681  OD1 ASP A 354      48.511  15.163  71.552  1.00253.18           O  
ANISOU 1681  OD1 ASP A 354    29723  30502  35970   -793  -2701   1660       O  
ATOM   1682  OD2 ASP A 354      49.924  16.140  72.885  1.00246.66           O  
ANISOU 1682  OD2 ASP A 354    29144  30019  34555   -778  -2466   1931       O  
ATOM   1683  N   GLY A 355      48.209  12.495  70.191  1.00210.32           N  
ANISOU 1683  N   GLY A 355    23985  24360  31566   -774  -3203   1356       N  
ATOM   1684  CA  GLY A 355      47.144  11.507  70.300  1.00221.21           C  
ANISOU 1684  CA  GLY A 355    25120  25420  33509   -908  -3282   1432       C  
ATOM   1685  C   GLY A 355      46.299  11.643  71.548  1.00231.89           C  
ANISOU 1685  C   GLY A 355    26384  26794  34928  -1101  -3025   1841       C  
ATOM   1686  O   GLY A 355      45.467  10.777  71.836  1.00255.13           O  
ANISOU 1686  O   GLY A 355    29114  29451  38370  -1243  -3029   1980       O  
ATOM   1687  N   ASN A 356      46.502  12.736  72.281  1.00229.97           N  
ANISOU 1687  N   ASN A 356    26297  26884  34195  -1105  -2789   2025       N  
ATOM   1688  CA  ASN A 356      45.690  13.073  73.443  1.00232.43           C  
ANISOU 1688  CA  ASN A 356    26555  27286  34470  -1260  -2511   2384       C  
ATOM   1689  C   ASN A 356      44.196  13.155  73.161  1.00239.09           C  
ANISOU 1689  C   ASN A 356    27158  28053  35630  -1357  -2477   2299       C  
ATOM   1690  O   ASN A 356      43.766  13.383  72.041  1.00241.38           O  
ANISOU 1690  O   ASN A 356    27373  28335  36005  -1270  -2661   1927       O  
ATOM   1691  CB  ASN A 356      46.117  14.450  74.015  1.00227.02           C  
ANISOU 1691  CB  ASN A 356    26081  27010  33164  -1207  -2303   2465       C  
ATOM   1692  CG  ASN A 356      47.436  14.409  74.758  1.00228.51           C  
ANISOU 1692  CG  ASN A 356    26471  27295  33055  -1154  -2270   2656       C  
ATOM   1693  OD1 ASN A 356      48.014  13.347  75.003  1.00228.56           O  
ANISOU 1693  OD1 ASN A 356    26471  27072  33297  -1159  -2377   2790       O  
ATOM   1694  ND2 ASN A 356      47.916  15.580  75.130  1.00228.05           N  
ANISOU 1694  ND2 ASN A 356    26584  27568  32494  -1095  -2134   2657       N  
ATOM   1695  N   SER A 357      43.401  13.176  74.236  1.00243.18           N  
ANISOU 1695  N   SER A 357    27579  28579  36239  -1518  -2211   2646       N  
ATOM   1696  CA  SER A 357      42.001  13.611  74.168  1.00241.74           C  
ANISOU 1696  CA  SER A 357    27179  28428  36243  -1606  -2101   2588       C  
ATOM   1697  C   SER A 357      41.958  15.149  74.025  1.00233.81           C  
ANISOU 1697  C   SER A 357    26323  27824  34690  -1495  -2005   2439       C  
ATOM   1698  O   SER A 357      42.818  15.880  74.543  1.00232.67           O  
ANISOU 1698  O   SER A 357    26426  27940  34038  -1429  -1886   2552       O  
ATOM   1699  CB  SER A 357      41.150  13.155  75.370  1.00246.72           C  
ANISOU 1699  CB  SER A 357    27648  28940  37155  -1815  -1800   3011       C  
ATOM   1700  OG  SER A 357      40.393  11.984  75.036  1.00247.37           O  
ANISOU 1700  OG  SER A 357    27432  28613  37943  -1942  -1906   2978       O  
ATOM   1701  N   PHE A 358      40.944  15.624  73.295  1.00223.61           N  
ANISOU 1701  N   PHE A 358    24867  26559  33533  -1468  -2078   2167       N  
ATOM   1702  CA  PHE A 358      40.771  17.037  73.004  1.00210.15           C  
ANISOU 1702  CA  PHE A 358    23282  25180  31382  -1349  -2021   1993       C  
ATOM   1703  C   PHE A 358      42.027  17.589  72.295  1.00192.66           C  
ANISOU 1703  C   PHE A 358    21362  23124  28714  -1159  -2164   1783       C  
ATOM   1704  O   PHE A 358      42.344  18.774  72.328  1.00178.41           O  
ANISOU 1704  O   PHE A 358    19745  21600  26439  -1067  -2057   1739       O  
ATOM   1705  CB  PHE A 358      40.381  17.782  74.285  1.00216.08           C  
ANISOU 1705  CB  PHE A 358    24058  26159  31881  -1448  -1659   2316       C  
ATOM   1706  CG  PHE A 358      39.453  16.992  75.194  1.00229.28           C  
ANISOU 1706  CG  PHE A 358    25479  27644  33993  -1655  -1452   2625       C  
ATOM   1707  CD1 PHE A 358      38.143  16.706  74.814  1.00236.24           C  
ANISOU 1707  CD1 PHE A 358    26028  28355  35374  -1737  -1485   2494       C  
ATOM   1708  CD2 PHE A 358      39.903  16.496  76.426  1.00236.29           C  
ANISOU 1708  CD2 PHE A 358    26459  28511  34810  -1762  -1224   3051       C  
ATOM   1709  CE1 PHE A 358      37.297  16.000  75.663  1.00246.21           C  
ANISOU 1709  CE1 PHE A 358    27045  29433  37069  -1942  -1249   2791       C  
ATOM   1710  CE2 PHE A 358      39.086  15.778  77.265  1.00244.39           C  
ANISOU 1710  CE2 PHE A 358    27281  29358  36215  -1947   -993   3369       C  
ATOM   1711  CZ  PHE A 358      37.788  15.537  76.900  1.00250.72           C  
ANISOU 1711  CZ  PHE A 358    27744  29990  37527  -2050   -982   3249       C  
ATOM   1712  N   GLN A 359      42.651  16.716  71.532  1.00187.71           N  
ANISOU 1712  N   GLN A 359    20748  22292  28281  -1094  -2414   1612       N  
ATOM   1713  CA  GLN A 359      43.913  17.060  70.864  1.00180.52           C  
ANISOU 1713  CA  GLN A 359    20093  21495  27001   -924  -2526   1424       C  
ATOM   1714  C   GLN A 359      43.670  18.123  69.794  1.00168.86           C  
ANISOU 1714  C   GLN A 359    18719  20200  25238   -749  -2610   1092       C  
ATOM   1715  O   GLN A 359      44.474  19.012  69.678  1.00161.77           O  
ANISOU 1715  O   GLN A 359    18053  19516  23893   -649  -2526   1053       O  
ATOM   1716  CB  GLN A 359      44.539  15.842  70.233  1.00189.01           C  
ANISOU 1716  CB  GLN A 359    21136  22297  28382   -882  -2775   1287       C  
ATOM   1717  CG  GLN A 359      45.815  16.071  69.451  1.00193.23           C  
ANISOU 1717  CG  GLN A 359    21898  22921  28598   -704  -2885   1064       C  
ATOM   1718  CD  GLN A 359      46.134  14.881  68.551  1.00203.96           C  
ANISOU 1718  CD  GLN A 359    23184  23996  30315   -630  -3172    824       C  
ATOM   1719  OE1 GLN A 359      45.436  13.872  68.546  1.00216.79           O  
ANISOU 1719  OE1 GLN A 359    24586  25339  32443   -720  -3300    827       O  
ATOM   1720  NE2 GLN A 359      47.196  14.998  67.785  1.00203.89           N  
ANISOU 1720  NE2 GLN A 359    23353  24050  30065   -466  -3262    603       N  
ATOM   1721  N   GLY A 360      42.577  18.022  69.023  1.00164.99           N  
ANISOU 1721  N   GLY A 360    18057  19612  25018   -706  -2780    857       N  
ATOM   1722  CA  GLY A 360      42.283  18.957  68.005  1.00162.32           C  
ANISOU 1722  CA  GLY A 360    17829  19428  24418   -516  -2885    558       C  
ATOM   1723  C   GLY A 360      41.347  20.079  68.394  1.00159.75           C  
ANISOU 1723  C   GLY A 360    17465  19299  23931   -530  -2717    620       C  
ATOM   1724  O   GLY A 360      40.893  20.857  67.542  1.00163.66           O  
ANISOU 1724  O   GLY A 360    18029  19900  24255   -361  -2824    375       O  
ATOM   1725  N   GLU A 361      41.099  20.218  69.666  1.00158.37           N  
ANISOU 1725  N   GLU A 361    17210  19188  23773   -706  -2449    944       N  
ATOM   1726  CA  GLU A 361      40.272  21.306  70.190  1.00162.96           C  
ANISOU 1726  CA  GLU A 361    17756  19971  24189   -726  -2248   1023       C  
ATOM   1727  C   GLU A 361      41.026  22.144  71.229  1.00155.17           C  
ANISOU 1727  C   GLU A 361    16977  19223  22757   -772  -1952   1281       C  
ATOM   1728  O   GLU A 361      40.490  23.008  71.869  1.00155.97           O  
ANISOU 1728  O   GLU A 361    17065  19497  22698   -803  -1747   1384       O  
ATOM   1729  CB  GLU A 361      38.980  20.698  70.760  1.00177.44           C  
ANISOU 1729  CB  GLU A 361    19238  21655  26524   -895  -2189   1137       C  
ATOM   1730  CG  GLU A 361      38.093  19.977  69.727  1.00185.01           C  
ANISOU 1730  CG  GLU A 361    19945  22379  27970   -846  -2505    830       C  
ATOM   1731  CD  GLU A 361      38.404  18.479  69.518  1.00190.53           C  
ANISOU 1731  CD  GLU A 361    20516  22759  29116   -930  -2686    819       C  
ATOM   1732  OE1 GLU A 361      38.805  18.092  68.400  1.00191.08           O  
ANISOU 1732  OE1 GLU A 361    20658  22727  29215   -778  -2987    518       O  
ATOM   1733  OE2 GLU A 361      38.244  17.671  70.454  1.00195.47           O  
ANISOU 1733  OE2 GLU A 361    20976  23223  30067  -1138  -2524   1109       O  
ATOM   1734  N   THR A 362      42.308  21.852  71.400  1.00150.63           N  
ANISOU 1734  N   THR A 362    16582  18649  21999   -769  -1944   1364       N  
ATOM   1735  CA  THR A 362      43.199  22.518  72.332  1.00148.09           C  
ANISOU 1735  CA  THR A 362    16453  18530  21281   -798  -1721   1566       C  
ATOM   1736  C   THR A 362      43.824  23.773  71.722  1.00135.48           C  
ANISOU 1736  C   THR A 362    15100  17127  19246   -642  -1699   1376       C  
ATOM   1737  O   THR A 362      44.464  23.708  70.660  1.00134.72           O  
ANISOU 1737  O   THR A 362    15124  16978  19082   -513  -1860   1156       O  
ATOM   1738  CB  THR A 362      44.325  21.594  72.808  1.00160.74           C  
ANISOU 1738  CB  THR A 362    18116  20032  22924   -856  -1747   1728       C  
ATOM   1739  OG1 THR A 362      43.818  20.282  73.038  1.00176.04           O  
ANISOU 1739  OG1 THR A 362    19844  21715  25328   -973  -1822   1856       O  
ATOM   1740  CG2 THR A 362      44.923  22.110  74.080  1.00163.69           C  
ANISOU 1740  CG2 THR A 362    18613  20600  22978   -916  -1517   1986       C  
ATOM   1741  N   TRP A 363      43.645  24.906  72.407  1.00128.40           N  
ANISOU 1741  N   TRP A 363    14277  16446  18061   -653  -1482   1466       N  
ATOM   1742  CA  TRP A 363      44.195  26.171  71.962  1.00130.08           C  
ANISOU 1742  CA  TRP A 363    14715  16824  17886   -526  -1420   1320       C  
ATOM   1743  C   TRP A 363      45.255  26.647  72.936  1.00128.07           C  
ANISOU 1743  C   TRP A 363    14601  16719  17339   -579  -1241   1472       C  
ATOM   1744  O   TRP A 363      45.174  26.359  74.124  1.00130.42           O  
ANISOU 1744  O   TRP A 363    14829  17067  17657   -697  -1119   1705       O  
ATOM   1745  CB  TRP A 363      43.081  27.211  71.783  1.00131.61           C  
ANISOU 1745  CB  TRP A 363    14878  17121  18006   -460  -1355   1233       C  
ATOM   1746  CG  TRP A 363      42.045  26.822  70.729  1.00133.05           C  
ANISOU 1746  CG  TRP A 363    14919  17164  18467   -372  -1579   1032       C  
ATOM   1747  CD1 TRP A 363      41.044  25.889  70.861  1.00137.42           C  
ANISOU 1747  CD1 TRP A 363    15195  17573  19445   -462  -1670   1064       C  
ATOM   1748  CD2 TRP A 363      41.914  27.359  69.407  1.00126.51           C  
ANISOU 1748  CD2 TRP A 363    14221  16327  17521   -167  -1744    765       C  
ATOM   1749  NE1 TRP A 363      40.302  25.813  69.707  1.00135.77           N  
ANISOU 1749  NE1 TRP A 363    14913  17267  19402   -324  -1911    800       N  
ATOM   1750  CE2 TRP A 363      40.816  26.705  68.796  1.00129.94           C  
ANISOU 1750  CE2 TRP A 363    14440  16620  18308   -128  -1968    619       C  
ATOM   1751  CE3 TRP A 363      42.617  28.316  68.684  1.00121.56           C  
ANISOU 1751  CE3 TRP A 363    13872  15785  16529     -8  -1718    640       C  
ATOM   1752  CZ2 TRP A 363      40.426  26.985  67.496  1.00128.86           C  
ANISOU 1752  CZ2 TRP A 363    14381  16450  18129     87  -2196    343       C  
ATOM   1753  CZ3 TRP A 363      42.219  28.591  67.398  1.00123.09           C  
ANISOU 1753  CZ3 TRP A 363    14160  15938  16670    199  -1908    402       C  
ATOM   1754  CH2 TRP A 363      41.136  27.930  66.814  1.00125.94           C  
ANISOU 1754  CH2 TRP A 363    14323  16181  17347    258  -2160    250       C  
ATOM   1755  N   ARG A 364      46.263  27.358  72.414  1.00126.14           N  
ANISOU 1755  N   ARG A 364    14557  16541  16829   -484  -1226   1332       N  
ATOM   1756  CA  ARG A 364      47.306  27.939  73.233  1.00123.80           C  
ANISOU 1756  CA  ARG A 364    14381  16384  16272   -520  -1078   1413       C  
ATOM   1757  C   ARG A 364      47.211  29.469  73.193  1.00113.17           C  
ANISOU 1757  C   ARG A 364    13167  15194  14639   -456   -919   1320       C  
ATOM   1758  O   ARG A 364      46.960  30.059  72.134  1.00107.82           O  
ANISOU 1758  O   ARG A 364    12577  14486  13903   -339   -951   1146       O  
ATOM   1759  CB  ARG A 364      48.699  27.521  72.742  1.00128.41           C  
ANISOU 1759  CB  ARG A 364    15059  16897  16832   -479  -1165   1321       C  
ATOM   1760  CG  ARG A 364      49.832  28.030  73.634  1.00135.95           C  
ANISOU 1760  CG  ARG A 364    16099  17983  17570   -519  -1047   1381       C  
ATOM   1761  CD  ARG A 364      51.195  27.488  73.251  1.00146.69           C  
ANISOU 1761  CD  ARG A 364    17500  19263  18969   -488  -1137   1294       C  
ATOM   1762  NE  ARG A 364      51.662  28.011  71.960  1.00153.27           N  
ANISOU 1762  NE  ARG A 364    18451  20054  19728   -379  -1125   1062       N  
ATOM   1763  CZ  ARG A 364      51.483  27.435  70.766  1.00158.62           C  
ANISOU 1763  CZ  ARG A 364    19138  20594  20534   -291  -1253    927       C  
ATOM   1764  NH1 ARG A 364      50.785  26.301  70.599  1.00160.30           N  
ANISOU 1764  NH1 ARG A 364    19224  20673  21007   -304  -1428    967       N  
ATOM   1765  NH2 ARG A 364      52.004  28.036  69.693  1.00161.10           N  
ANISOU 1765  NH2 ARG A 364    19597  20900  20713   -180  -1196    739       N  
ATOM   1766  N   LEU A 365      47.424  30.097  74.341  1.00110.78           N  
ANISOU 1766  N   LEU A 365    12890  15048  14153   -519   -757   1431       N  
ATOM   1767  CA  LEU A 365      47.512  31.550  74.392  1.00113.32           C  
ANISOU 1767  CA  LEU A 365    13338  15497  14220   -467   -604   1333       C  
ATOM   1768  C   LEU A 365      48.715  32.049  73.602  1.00113.55           C  
ANISOU 1768  C   LEU A 365    13528  15487  14129   -399   -600   1169       C  
ATOM   1769  O   LEU A 365      49.732  31.388  73.502  1.00118.75           O  
ANISOU 1769  O   LEU A 365    14193  16087  14839   -419   -672   1159       O  
ATOM   1770  CB  LEU A 365      47.594  32.038  75.814  1.00117.34           C  
ANISOU 1770  CB  LEU A 365    13840  16181  14563   -540   -453   1457       C  
ATOM   1771  CG  LEU A 365      46.270  31.917  76.558  1.00122.38           C  
ANISOU 1771  CG  LEU A 365    14342  16888  15268   -589   -373   1603       C  
ATOM   1772  CD1 LEU A 365      46.513  31.809  78.057  1.00124.76           C  
ANISOU 1772  CD1 LEU A 365    14632  17342  15426   -665   -261   1786       C  
ATOM   1773  CD2 LEU A 365      45.419  33.125  76.222  1.00125.89           C  
ANISOU 1773  CD2 LEU A 365    14814  17392  15627   -512   -276   1479       C  
ATOM   1774  N   SER A 366      48.598  33.256  73.056  1.00112.38           N  
ANISOU 1774  N   SER A 366    13507  15363  13828   -316   -498   1044       N  
ATOM   1775  CA  SER A 366      49.683  33.959  72.385  1.00116.43           C  
ANISOU 1775  CA  SER A 366    14181  15839  14217   -262   -420    907       C  
ATOM   1776  C   SER A 366      49.747  35.408  72.803  1.00123.22           C  
ANISOU 1776  C   SER A 366    15135  16786  14895   -257   -231    860       C  
ATOM   1777  O   SER A 366      48.732  36.055  72.954  1.00131.07           O  
ANISOU 1777  O   SER A 366    16129  17829  15842   -220   -181    872       O  
ATOM   1778  CB  SER A 366      49.565  33.925  70.874  1.00113.91           C  
ANISOU 1778  CB  SER A 366    13975  15394  13909   -126   -485    784       C  
ATOM   1779  OG  SER A 366      50.566  34.765  70.287  1.00111.19           O  
ANISOU 1779  OG  SER A 366    13801  15016  13428    -77   -341    678       O  
ATOM   1780  N   PHE A 367      50.958  35.928  72.945  1.00125.86           N  
ANISOU 1780  N   PHE A 367    15537  17124  15158   -290   -130    786       N  
ATOM   1781  CA  PHE A 367      51.161  37.328  73.340  1.00125.33           C  
ANISOU 1781  CA  PHE A 367    15552  17109  14959   -295     48    714       C  
ATOM   1782  C   PHE A 367      52.191  38.009  72.457  1.00122.23           C  
ANISOU 1782  C   PHE A 367    15296  16600  14543   -260    175    587       C  
ATOM   1783  O   PHE A 367      52.962  38.842  72.944  1.00120.27           O  
ANISOU 1783  O   PHE A 367    15063  16368  14265   -316    305    508       O  
ATOM   1784  CB  PHE A 367      51.586  37.425  74.799  1.00126.79           C  
ANISOU 1784  CB  PHE A 367    15642  17435  15094   -396     69    745       C  
ATOM   1785  CG  PHE A 367      50.617  36.786  75.716  1.00124.70           C  
ANISOU 1785  CG  PHE A 367    15263  17286  14829   -430     -2    897       C  
ATOM   1786  CD1 PHE A 367      49.436  37.441  76.033  1.00123.97           C  
ANISOU 1786  CD1 PHE A 367    15164  17268  14672   -398     75    924       C  
ATOM   1787  CD2 PHE A 367      50.834  35.504  76.202  1.00122.19           C  
ANISOU 1787  CD2 PHE A 367    14843  16987  14597   -485   -134   1024       C  
ATOM   1788  CE1 PHE A 367      48.497  36.850  76.859  1.00122.84           C  
ANISOU 1788  CE1 PHE A 367    14900  17226  14545   -434     51   1072       C  
ATOM   1789  CE2 PHE A 367      49.901  34.902  77.019  1.00120.39           C  
ANISOU 1789  CE2 PHE A 367    14515  16844  14382   -521   -161   1194       C  
ATOM   1790  CZ  PHE A 367      48.735  35.576  77.357  1.00120.66           C  
ANISOU 1790  CZ  PHE A 367    14531  16962  14349   -501    -54   1218       C  
ATOM   1791  N   SER A 368      52.161  37.724  71.167  1.00119.24           N  
ANISOU 1791  N   SER A 368    15020  16104  14181   -162    150    558       N  
ATOM   1792  CA  SER A 368      53.186  38.239  70.259  1.00122.48           C  
ANISOU 1792  CA  SER A 368    15569  16398  14570   -125    304    460       C  
ATOM   1793  C   SER A 368      53.057  39.758  70.087  1.00122.47           C  
ANISOU 1793  C   SER A 368    15718  16348  14465    -86    516    420       C  
ATOM   1794  O   SER A 368      54.042  40.465  69.856  1.00121.72           O  
ANISOU 1794  O   SER A 368    15692  16169  14385   -118    707    347       O  
ATOM   1795  CB  SER A 368      53.075  37.480  68.950  1.00123.83           C  
ANISOU 1795  CB  SER A 368    15829  16475  14743     -3    216    444       C  
ATOM   1796  OG  SER A 368      52.995  36.090  69.215  1.00121.69           O  
ANISOU 1796  OG  SER A 368    15402  16233  14601    -42      2    483       O  
ATOM   1797  N   HIS A 369      51.829  40.252  70.206  1.00120.14           N  
ANISOU 1797  N   HIS A 369    15459  16091  14096    -16    486    466       N  
ATOM   1798  CA  HIS A 369      51.560  41.688  70.161  1.00120.81           C  
ANISOU 1798  CA  HIS A 369    15677  16124  14099     30    663    437       C  
ATOM   1799  C   HIS A 369      52.251  42.460  71.300  1.00117.74           C  
ANISOU 1799  C   HIS A 369    15205  15779  13750   -105    792    369       C  
ATOM   1800  O   HIS A 369      52.912  43.483  71.096  1.00119.55           O  
ANISOU 1800  O   HIS A 369    15532  15897  13994   -121    990    298       O  
ATOM   1801  CB  HIS A 369      50.051  41.939  70.177  1.00123.78           C  
ANISOU 1801  CB  HIS A 369    16064  16548  14417    138    570    485       C  
ATOM   1802  CG  HIS A 369      49.365  41.472  71.419  1.00126.68           C  
ANISOU 1802  CG  HIS A 369    16221  17079  14832     50    460    530       C  
ATOM   1803  ND1 HIS A 369      49.293  40.150  71.786  1.00123.87           N  
ANISOU 1803  ND1 HIS A 369    15704  16799  14561    -18    296    594       N  
ATOM   1804  CD2 HIS A 369      48.690  42.160  72.367  1.00131.40           C  
ANISOU 1804  CD2 HIS A 369    16753  17772  15399     29    510    527       C  
ATOM   1805  CE1 HIS A 369      48.620  40.042  72.914  1.00129.73           C  
ANISOU 1805  CE1 HIS A 369    16300  17677  15314    -82    269    651       C  
ATOM   1806  NE2 HIS A 369      48.238  41.247  73.287  1.00133.77           N  
ANISOU 1806  NE2 HIS A 369    16863  18215  15747    -51    397    602       N  
ATOM   1807  N   THR A 370      52.096  41.935  72.496  1.00113.49           N  
ANISOU 1807  N   THR A 370    14488  15398  13233   -197    676    389       N  
ATOM   1808  CA  THR A 370      52.661  42.520  73.690  1.00115.24           C  
ANISOU 1808  CA  THR A 370    14620  15700  13464   -303    738    307       C  
ATOM   1809  C   THR A 370      54.191  42.443  73.663  1.00118.39           C  
ANISOU 1809  C   THR A 370    14977  16033  13971   -394    795    205       C  
ATOM   1810  O   THR A 370      54.874  43.384  74.079  1.00122.86           O  
ANISOU 1810  O   THR A 370    15533  16559  14587   -454    922     77       O  
ATOM   1811  CB  THR A 370      52.071  41.745  74.855  1.00113.28           C  
ANISOU 1811  CB  THR A 370    14218  15646  13175   -347    584    388       C  
ATOM   1812  OG1 THR A 370      50.645  41.830  74.757  1.00116.13           O  
ANISOU 1812  OG1 THR A 370    14593  16046  13481   -265    558    469       O  
ATOM   1813  CG2 THR A 370      52.519  42.294  76.174  1.00114.89           C  
ANISOU 1813  CG2 THR A 370    14345  15972  13334   -422    615    299       C  
ATOM   1814  N   GLU A 371      54.713  41.317  73.189  1.00118.85           N  
ANISOU 1814  N   GLU A 371    14990  16072  14094   -401    696    243       N  
ATOM   1815  CA  GLU A 371      56.155  41.125  73.093  1.00122.59           C  
ANISOU 1815  CA  GLU A 371    15396  16481  14700   -476    742    138       C  
ATOM   1816  C   GLU A 371      56.752  42.104  72.070  1.00123.18           C  
ANISOU 1816  C   GLU A 371    15608  16365  14829   -458    998     58       C  
ATOM   1817  O   GLU A 371      57.844  42.628  72.253  1.00121.25           O  
ANISOU 1817  O   GLU A 371    15299  16050  14720   -544   1125    -71       O  
ATOM   1818  CB  GLU A 371      56.450  39.702  72.663  1.00123.90           C  
ANISOU 1818  CB  GLU A 371    15500  16649  14926   -460    586    197       C  
ATOM   1819  CG  GLU A 371      56.113  38.665  73.725  1.00125.33           C  
ANISOU 1819  CG  GLU A 371    15538  16984  15096   -495    355    290       C  
ATOM   1820  CD  GLU A 371      55.969  37.261  73.177  1.00128.29           C  
ANISOU 1820  CD  GLU A 371    15879  17329  15536   -456    191    382       C  
ATOM   1821  OE1 GLU A 371      56.500  36.983  72.096  1.00137.22           O  
ANISOU 1821  OE1 GLU A 371    17062  18340  16733   -413    234    327       O  
ATOM   1822  OE2 GLU A 371      55.314  36.419  73.820  1.00127.73           O  
ANISOU 1822  OE2 GLU A 371    15728  17345  15457   -467     27    508       O  
ATOM   1823  N   LYS A 372      56.013  42.330  70.993  1.00126.11           N  
ANISOU 1823  N   LYS A 372    16167  16646  15101   -338   1070    141       N  
ATOM   1824  CA  LYS A 372      56.393  43.321  70.007  1.00130.70           C  
ANISOU 1824  CA  LYS A 372    16930  17041  15688   -294   1335    115       C  
ATOM   1825  C   LYS A 372      56.481  44.695  70.652  1.00123.06           C  
ANISOU 1825  C   LYS A 372    15967  16016  14771   -359   1496     35       C  
ATOM   1826  O   LYS A 372      57.491  45.399  70.498  1.00121.99           O  
ANISOU 1826  O   LYS A 372    15828  15739  14782   -437   1713    -60       O  
ATOM   1827  CB  LYS A 372      55.412  43.343  68.840  1.00142.32           C  
ANISOU 1827  CB  LYS A 372    18629  18451  16993   -114   1338    226       C  
ATOM   1828  CG  LYS A 372      55.871  44.168  67.636  1.00150.02           C  
ANISOU 1828  CG  LYS A 372    19841  19226  17932    -34   1621    241       C  
ATOM   1829  CD  LYS A 372      54.908  44.002  66.461  1.00154.10           C  
ANISOU 1829  CD  LYS A 372    20595  19711  18242    183   1561    345       C  
ATOM   1830  CE  LYS A 372      55.294  44.843  65.258  1.00154.89           C  
ANISOU 1830  CE  LYS A 372    20982  19618  18251    295   1853    395       C  
ATOM   1831  NZ  LYS A 372      54.421  44.665  64.074  1.00154.57           N  
ANISOU 1831  NZ  LYS A 372    21200  19558  17971    543   1770    483       N  
ATOM   1832  N   TYR A 373      55.438  45.061  71.397  1.00116.42           N  
ANISOU 1832  N   TYR A 373    15115  15280  13839   -330   1396     60       N  
ATOM   1833  CA  TYR A 373      55.434  46.347  72.089  1.00119.59           C  
ANISOU 1833  CA  TYR A 373    15513  15636  14288   -379   1522    -38       C  
ATOM   1834  C   TYR A 373      56.638  46.477  73.034  1.00120.52           C  
ANISOU 1834  C   TYR A 373    15436  15780  14577   -536   1533   -213       C  
ATOM   1835  O   TYR A 373      57.284  47.531  73.100  1.00120.43           O  
ANISOU 1835  O   TYR A 373    15425  15618  14712   -602   1721   -339       O  
ATOM   1836  CB  TYR A 373      54.178  46.524  72.946  1.00122.03           C  
ANISOU 1836  CB  TYR A 373    15790  16101  14474   -329   1386     -9       C  
ATOM   1837  CG  TYR A 373      54.188  47.832  73.731  1.00126.64           C  
ANISOU 1837  CG  TYR A 373    16360  16646  15109   -369   1500   -144       C  
ATOM   1838  CD1 TYR A 373      54.761  47.923  75.010  1.00128.31           C  
ANISOU 1838  CD1 TYR A 373    16395  16979  15375   -479   1434   -298       C  
ATOM   1839  CD2 TYR A 373      53.663  48.987  73.173  1.00132.86           C  
ANISOU 1839  CD2 TYR A 373    17323  17265  15893   -281   1664   -132       C  
ATOM   1840  CE1 TYR A 373      54.789  49.127  75.704  1.00134.17           C  
ANISOU 1840  CE1 TYR A 373    17124  17679  16176   -506   1524   -459       C  
ATOM   1841  CE2 TYR A 373      53.685  50.192  73.854  1.00139.34           C  
ANISOU 1841  CE2 TYR A 373    18130  18021  16791   -314   1768   -272       C  
ATOM   1842  CZ  TYR A 373      54.244  50.268  75.114  1.00141.44           C  
ANISOU 1842  CZ  TYR A 373    18208  18411  17121   -430   1698   -447       C  
ATOM   1843  OH  TYR A 373      54.224  51.502  75.734  1.00150.67           O  
ANISOU 1843  OH  TYR A 373    19371  19503  18373   -448   1793   -614       O  
ATOM   1844  N   ILE A 374      56.915  45.418  73.787  1.00122.66           N  
ANISOU 1844  N   ILE A 374    15535  16229  14840   -587   1320   -225       N  
ATOM   1845  CA  ILE A 374      58.018  45.441  74.743  1.00130.13           C  
ANISOU 1845  CA  ILE A 374    16289  17228  15927   -704   1268   -402       C  
ATOM   1846  C   ILE A 374      59.364  45.591  74.057  1.00135.44           C  
ANISOU 1846  C   ILE A 374    16913  17715  16830   -781   1436   -511       C  
ATOM   1847  O   ILE A 374      60.200  46.382  74.487  1.00139.92           O  
ANISOU 1847  O   ILE A 374    17376  18200  17585   -875   1533   -701       O  
ATOM   1848  CB  ILE A 374      58.098  44.164  75.574  1.00131.17           C  
ANISOU 1848  CB  ILE A 374    16273  17570  15992   -716    998   -362       C  
ATOM   1849  CG1 ILE A 374      56.866  44.018  76.466  1.00129.54           C  
ANISOU 1849  CG1 ILE A 374    16081  17560  15577   -661    860   -263       C  
ATOM   1850  CG2 ILE A 374      59.331  44.197  76.482  1.00133.78           C  
ANISOU 1850  CG2 ILE A 374    16414  17947  16466   -808    917   -564       C  
ATOM   1851  CD1 ILE A 374      56.570  42.573  76.812  1.00129.21           C  
ANISOU 1851  CD1 ILE A 374    15969  17671  15451   -642    642   -109       C  
ATOM   1852  N   LEU A 375      59.576  44.832  72.993  1.00138.59           N  
ANISOU 1852  N   LEU A 375    17375  18048  17234   -739   1477   -408       N  
ATOM   1853  CA  LEU A 375      60.807  44.941  72.219  1.00143.49           C  
ANISOU 1853  CA  LEU A 375    17959  18492  18068   -800   1684   -495       C  
ATOM   1854  C   LEU A 375      60.981  46.353  71.682  1.00144.87           C  
ANISOU 1854  C   LEU A 375    18257  18438  18348   -828   2010   -536       C  
ATOM   1855  O   LEU A 375      62.110  46.863  71.624  1.00148.70           O  
ANISOU 1855  O   LEU A 375    18628  18774  19096   -939   2197   -686       O  
ATOM   1856  CB  LEU A 375      60.775  43.956  71.035  1.00145.66           C  
ANISOU 1856  CB  LEU A 375    18338  18737  18267   -710   1695   -363       C  
ATOM   1857  CG  LEU A 375      61.454  42.615  71.302  1.00146.05           C  
ANISOU 1857  CG  LEU A 375    18199  18894  18398   -735   1485   -403       C  
ATOM   1858  CD1 LEU A 375      62.965  42.812  71.240  1.00150.63           C  
ANISOU 1858  CD1 LEU A 375    18604  19361  19266   -843   1640   -588       C  
ATOM   1859  CD2 LEU A 375      61.077  41.986  72.626  1.00143.22           C  
ANISOU 1859  CD2 LEU A 375    17698  18747  17973   -754   1168   -398       C  
ATOM   1860  N   ASN A 376      59.879  46.995  71.307  1.00142.46           N  
ANISOU 1860  N   ASN A 376    18171  18087  17867   -726   2079   -409       N  
ATOM   1861  CA  ASN A 376      59.988  48.354  70.776  1.00148.09           C  
ANISOU 1861  CA  ASN A 376    19032  18556  18679   -736   2392   -418       C  
ATOM   1862  C   ASN A 376      59.855  49.451  71.808  1.00141.13           C  
ANISOU 1862  C   ASN A 376    18071  17649  17902   -808   2397   -566       C  
ATOM   1863  O   ASN A 376      60.126  50.620  71.516  1.00143.41           O  
ANISOU 1863  O   ASN A 376    18436  17702  18349   -847   2659   -610       O  
ATOM   1864  CB  ASN A 376      59.016  48.532  69.640  1.00161.82           C  
ANISOU 1864  CB  ASN A 376    21076  20214  20191   -563   2488   -207       C  
ATOM   1865  CG  ASN A 376      59.241  47.502  68.569  1.00175.85           C  
ANISOU 1865  CG  ASN A 376    22939  22004  21869   -481   2493   -100       C  
ATOM   1866  OD1 ASN A 376      60.352  47.385  68.038  1.00186.49           O  
ANISOU 1866  OD1 ASN A 376    24246  23239  23372   -547   2693   -148       O  
ATOM   1867  ND2 ASN A 376      58.218  46.703  68.290  1.00188.61           N  
ANISOU 1867  ND2 ASN A 376    24647  23764  23250   -340   2267     18       N  
ATOM   1868  N   ASN A 377      59.481  49.078  73.029  1.00135.12           N  
ANISOU 1868  N   ASN A 377    17159  17121  17060   -823   2117   -647       N  
ATOM   1869  CA  ASN A 377      59.428  50.024  74.144  1.00138.37           C  
ANISOU 1869  CA  ASN A 377    17472  17547  17553   -881   2085   -833       C  
ATOM   1870  C   ASN A 377      60.069  49.406  75.376  1.00146.99           C  
ANISOU 1870  C   ASN A 377    18309  18848  18692   -960   1834  -1012       C  
ATOM   1871  O   ASN A 377      59.382  49.089  76.337  1.00149.17           O  
ANISOU 1871  O   ASN A 377    18548  19355  18774   -911   1612  -1011       O  
ATOM   1872  CB  ASN A 377      57.978  50.420  74.452  1.00130.82           C  
ANISOU 1872  CB  ASN A 377    16653  16685  16364   -759   2007   -739       C  
ATOM   1873  CG  ASN A 377      57.283  51.070  73.271  1.00125.43           C  
ANISOU 1873  CG  ASN A 377    16235  15799  15620   -646   2214   -568       C  
ATOM   1874  OD1 ASN A 377      56.997  52.261  73.292  1.00123.25           O  
ANISOU 1874  OD1 ASN A 377    16051  15362  15416   -628   2361   -616       O  
ATOM   1875  ND2 ASN A 377      57.001  50.290  72.237  1.00121.31           N  
ANISOU 1875  ND2 ASN A 377    15846  15281  14962   -554   2211   -375       N  
ATOM   1876  N   HIS A 378      61.392  49.275  75.350  1.00154.48           N  
ANISOU 1876  N   HIS A 378    19082  19710  19901  -1072   1880  -1169       N  
ATOM   1877  CA  HIS A 378      62.144  48.414  76.254  1.00154.08           C  
ANISOU 1877  CA  HIS A 378    18799  19848  19895  -1117   1618  -1308       C  
ATOM   1878  C   HIS A 378      62.918  49.094  77.373  1.00160.18           C  
ANISOU 1878  C   HIS A 378    19361  20633  20866  -1203   1527  -1627       C  
ATOM   1879  O   HIS A 378      63.577  48.418  78.181  1.00161.85           O  
ANISOU 1879  O   HIS A 378    19383  21007  21103  -1218   1279  -1761       O  
ATOM   1880  CB  HIS A 378      63.048  47.552  75.381  1.00148.88           C  
ANISOU 1880  CB  HIS A 378    18074  19112  19380  -1151   1682  -1261       C  
ATOM   1881  CG  HIS A 378      64.072  48.344  74.642  1.00149.58           C  
ANISOU 1881  CG  HIS A 378    18106  18915  19810  -1259   2001  -1385       C  
ATOM   1882  ND1 HIS A 378      63.940  48.730  73.323  1.00147.87           N  
ANISOU 1882  ND1 HIS A 378    18090  18480  19611  -1238   2328  -1223       N  
ATOM   1883  CD2 HIS A 378      65.245  48.854  75.071  1.00151.13           C  
ANISOU 1883  CD2 HIS A 378    18062  19002  20358  -1388   2050  -1661       C  
ATOM   1884  CE1 HIS A 378      65.016  49.423  72.969  1.00147.80           C  
ANISOU 1884  CE1 HIS A 378    17968  18231  19956  -1362   2600  -1373       C  
ATOM   1885  NE2 HIS A 378      65.814  49.517  74.021  1.00150.17           N  
ANISOU 1885  NE2 HIS A 378    17982  18588  20488  -1463   2432  -1652       N  
ATOM   1886  N   GLY A 379      62.860  50.410  77.467  1.00165.79           N  
ANISOU 1886  N   GLY A 379    20098  21170  21722  -1248   1700  -1767       N  
ATOM   1887  CA  GLY A 379      63.645  51.111  78.492  1.00171.60           C  
ANISOU 1887  CA  GLY A 379    20616  21893  22689  -1330   1604  -2119       C  
ATOM   1888  C   GLY A 379      62.848  51.505  79.716  1.00177.85           C  
ANISOU 1888  C   GLY A 379    21436  22892  23245  -1250   1398  -2223       C  
ATOM   1889  O   GLY A 379      61.620  51.531  79.697  1.00179.93           O  
ANISOU 1889  O   GLY A 379    21892  23253  23220  -1148   1406  -2028       O  
ATOM   1890  N   ILE A 380      63.544  51.807  80.805  1.00182.68           N  
ANISOU 1890  N   ILE A 380    21848  23584  23979  -1283   1206  -2550       N  
ATOM   1891  CA  ILE A 380      62.898  52.485  81.935  1.00180.85           C  
ANISOU 1891  CA  ILE A 380    21644  23500  23567  -1209   1066  -2718       C  
ATOM   1892  C   ILE A 380      62.704  53.917  81.557  1.00182.03           C  
ANISOU 1892  C   ILE A 380    21854  23355  23954  -1264   1332  -2831       C  
ATOM   1893  O   ILE A 380      61.706  54.530  81.917  1.00181.05           O  
ANISOU 1893  O   ILE A 380    21865  23279  23644  -1180   1349  -2818       O  
ATOM   1894  CB  ILE A 380      63.643  52.499  83.290  1.00178.20           C  
ANISOU 1894  CB  ILE A 380    21100  23349  23257  -1194    752  -3078       C  
ATOM   1895  CG1 ILE A 380      65.159  52.599  83.109  1.00179.16           C  
ANISOU 1895  CG1 ILE A 380    20952  23282  23836  -1326    746  -3351       C  
ATOM   1896  CG2 ILE A 380      63.262  51.297  84.121  1.00175.78           C  
ANISOU 1896  CG2 ILE A 380    20832  23420  22534  -1062    449  -2939       C  
ATOM   1897  CD1 ILE A 380      65.844  53.162  84.325  1.00183.44           C  
ANISOU 1897  CD1 ILE A 380    21287  23900  24510  -1320    490  -3800       C  
ATOM   1898  N   GLU A 381      63.691  54.435  80.816  1.00181.82           N  
ANISOU 1898  N   GLU A 381    21717  23006  24361  -1407   1554  -2940       N  
ATOM   1899  CA  GLU A 381      63.646  55.781  80.242  1.00178.54           C  
ANISOU 1899  CA  GLU A 381    21367  22228  24242  -1481   1870  -3003       C  
ATOM   1900  C   GLU A 381      62.965  55.709  78.905  1.00168.28           C  
ANISOU 1900  C   GLU A 381    20329  20772  22836  -1443   2156  -2615       C  
ATOM   1901  O   GLU A 381      63.278  54.840  78.103  1.00160.11           O  
ANISOU 1901  O   GLU A 381    19318  19744  21772  -1455   2221  -2411       O  
ATOM   1902  CB  GLU A 381      65.040  56.396  80.082  1.00183.00           C  
ANISOU 1902  CB  GLU A 381    21679  22494  25357  -1661   2009  -3297       C  
ATOM   1903  CG  GLU A 381      65.698  56.731  81.429  1.00184.65           C  
ANISOU 1903  CG  GLU A 381    21619  22813  25723  -1687   1710  -3756       C  
ATOM   1904  CD  GLU A 381      67.113  57.236  81.342  1.00183.96           C  
ANISOU 1904  CD  GLU A 381    21225  22446  26224  -1869   1802  -4086       C  
ATOM   1905  OE1 GLU A 381      67.681  57.172  80.255  1.00195.41           O  
ANISOU 1905  OE1 GLU A 381    22653  23644  27949  -1983   2108  -3940       O  
ATOM   1906  OE2 GLU A 381      67.645  57.770  82.345  1.00171.98           O  
ANISOU 1906  OE2 GLU A 381    19485  20944  24915  -1896   1587  -4510       O  
ATOM   1907  N   LYS A 382      62.094  56.667  78.624  1.00165.85           N  
ANISOU 1907  N   LYS A 382    20216  20304  22492  -1387   2328  -2534       N  
ATOM   1908  CA  LYS A 382      61.302  56.671  77.397  1.00164.06           C  
ANISOU 1908  CA  LYS A 382    20272  19945  22115  -1305   2561  -2171       C  
ATOM   1909  C   LYS A 382      62.188  56.981  76.170  1.00164.26           C  
ANISOU 1909  C   LYS A 382    20327  19613  22470  -1417   2918  -2079       C  
ATOM   1910  O   LYS A 382      61.805  56.745  75.018  1.00155.98           O  
ANISOU 1910  O   LYS A 382    19507  18472  21286  -1347   3107  -1771       O  
ATOM   1911  CB  LYS A 382      60.158  57.668  77.565  1.00164.96           C  
ANISOU 1911  CB  LYS A 382    20566  19988  22121  -1196   2613  -2149       C  
ATOM   1912  CG  LYS A 382      59.218  57.360  78.749  1.00162.02           C  
ANISOU 1912  CG  LYS A 382    20172  19980  21408  -1075   2306  -2225       C  
ATOM   1913  CD  LYS A 382      58.574  58.584  79.441  1.00160.65           C  
ANISOU 1913  CD  LYS A 382    20031  19733  21274  -1016   2314  -2425       C  
ATOM   1914  CE  LYS A 382      57.717  58.159  80.653  1.00156.33           C  
ANISOU 1914  CE  LYS A 382    19449  19585  20361   -893   2031  -2500       C  
ATOM   1915  NZ  LYS A 382      57.253  59.208  81.610  1.00155.28           N  
ANISOU 1915  NZ  LYS A 382    19293  19459  20244   -833   1983  -2779       N  
ATOM   1916  N   THR A 383      63.384  57.495  76.411  1.00168.29           N  
ANISOU 1916  N   THR A 383    20602  19924  23414  -1586   3015  -2355       N  
ATOM   1917  CA  THR A 383      64.246  57.898  75.310  1.00172.59           C  
ANISOU 1917  CA  THR A 383    21155  20105  24313  -1708   3407  -2279       C  
ATOM   1918  C   THR A 383      65.297  56.849  74.991  1.00174.31           C  
ANISOU 1918  C   THR A 383    21186  20405  24636  -1791   3396  -2289       C  
ATOM   1919  O   THR A 383      66.117  57.020  74.082  1.00178.81           O  
ANISOU 1919  O   THR A 383    21733  20708  25499  -1897   3733  -2232       O  
ATOM   1920  CB  THR A 383      64.892  59.236  75.637  1.00174.70           C  
ANISOU 1920  CB  THR A 383    21271  20028  25078  -1858   3589  -2569       C  
ATOM   1921  OG1 THR A 383      65.213  59.234  77.026  1.00172.16           O  
ANISOU 1921  OG1 THR A 383    20670  19904  24837  -1896   3240  -2957       O  
ATOM   1922  CG2 THR A 383      63.933  60.379  75.346  1.00177.27           C  
ANISOU 1922  CG2 THR A 383    21866  20122  25366  -1775   3773  -2444       C  
ATOM   1923  N   CYS A 384      65.216  55.727  75.676  1.00171.03           N  
ANISOU 1923  N   CYS A 384    20662  20356  23964  -1728   3030  -2329       N  
ATOM   1924  CA  CYS A 384      66.116  54.578  75.428  1.00170.24           C  
ANISOU 1924  CA  CYS A 384    20390  20371  23922  -1773   2961  -2330       C  
ATOM   1925  C   CYS A 384      66.009  54.120  73.977  1.00166.00           C  
ANISOU 1925  C   CYS A 384    20076  19724  23272  -1726   3249  -1992       C  
ATOM   1926  O   CYS A 384      64.927  53.745  73.510  1.00157.70           O  
ANISOU 1926  O   CYS A 384    19301  18788  21828  -1574   3212  -1711       O  
ATOM   1927  CB  CYS A 384      65.798  53.380  76.352  1.00170.00           C  
ANISOU 1927  CB  CYS A 384    20281  20755  23554  -1671   2512  -2349       C  
ATOM   1928  SG  CYS A 384      67.077  52.079  76.480  1.00176.74           S  
ANISOU 1928  SG  CYS A 384    20837  21753  24564  -1727   2323  -2472       S  
ATOM   1929  N   CYS A 385      67.133  54.193  73.271  1.00167.85           N  
ANISOU 1929  N   CYS A 385    20182  19729  23862  -1853   3542  -2040       N  
ATOM   1930  CA  CYS A 385      67.246  53.811  71.851  1.00168.77           C  
ANISOU 1930  CA  CYS A 385    20498  19721  23904  -1812   3866  -1756       C  
ATOM   1931  C   CYS A 385      66.507  54.746  70.904  1.00176.25           C  
ANISOU 1931  C   CYS A 385    21807  20417  24743  -1741   4211  -1493       C  
ATOM   1932  O   CYS A 385      66.341  54.433  69.716  1.00180.09           O  
ANISOU 1932  O   CYS A 385    22541  20839  25045  -1648   4443  -1220       O  
ATOM   1933  CB  CYS A 385      66.797  52.347  71.616  1.00163.39           C  
ANISOU 1933  CB  CYS A 385    19904  19353  22823  -1667   3608  -1575       C  
ATOM   1934  SG  CYS A 385      67.834  51.053  72.329  1.00156.03           S  
ANISOU 1934  SG  CYS A 385    18595  18662  22027  -1724   3281  -1802       S  
ATOM   1935  N   GLU A 386      66.058  55.883  71.420  1.00181.19           N  
ANISOU 1935  N   GLU A 386    22476  20900  25468  -1763   4235  -1578       N  
ATOM   1936  CA  GLU A 386      65.309  56.860  70.625  1.00184.24           C  
ANISOU 1936  CA  GLU A 386    23208  21028  25763  -1677   4531  -1336       C  
ATOM   1937  C   GLU A 386      66.271  57.853  69.994  1.00196.51           C  
ANISOU 1937  C   GLU A 386    24728  22148  27786  -1838   5019  -1361       C  
ATOM   1938  O   GLU A 386      67.461  57.836  70.280  1.00202.57           O  
ANISOU 1938  O   GLU A 386    25166  22824  28975  -2026   5101  -1605       O  
ATOM   1939  CB  GLU A 386      64.309  57.648  71.488  1.00180.05           C  
ANISOU 1939  CB  GLU A 386    22745  20532  25132  -1610   4329  -1419       C  
ATOM   1940  CG  GLU A 386      62.934  57.031  71.719  1.00174.23           C  
ANISOU 1940  CG  GLU A 386    22196  20118  23883  -1401   4000  -1259       C  
ATOM   1941  CD  GLU A 386      61.954  58.051  72.300  1.00172.94           C  
ANISOU 1941  CD  GLU A 386    22143  19900  23668  -1325   3928  -1307       C  
ATOM   1942  OE1 GLU A 386      62.390  59.211  72.500  1.00177.24           O  
ANISOU 1942  OE1 GLU A 386    22623  20142  24575  -1436   4127  -1468       O  
ATOM   1943  OE2 GLU A 386      60.753  57.742  72.542  1.00163.39           O  
ANISOU 1943  OE2 GLU A 386    21070  18921  22089  -1158   3691  -1197       O  
ATOM   1944  N   SER A 387      65.716  58.758  69.175  1.00203.15           N  
ANISOU 1944  N   SER A 387    25906  22710  28569  -1757   5337  -1111       N  
ATOM   1945  CA  SER A 387      66.487  59.726  68.407  1.00206.54           C  
ANISOU 1945  CA  SER A 387    26384  22689  29400  -1886   5868  -1043       C  
ATOM   1946  C   SER A 387      67.155  60.779  69.313  1.00208.51           C  
ANISOU 1946  C   SER A 387    26318  22679  30224  -2107   5922  -1392       C  
ATOM   1947  O   SER A 387      68.234  61.308  69.002  1.00209.32           O  
ANISOU 1947  O   SER A 387    26249  22452  30829  -2304   6301  -1480       O  
ATOM   1948  CB  SER A 387      65.590  60.408  67.350  1.00204.22           C  
ANISOU 1948  CB  SER A 387    26580  22177  28837  -1699   6147   -659       C  
ATOM   1949  OG  SER A 387      64.238  59.947  67.415  1.00197.15           O  
ANISOU 1949  OG  SER A 387    25927  21577  27404  -1454   5791   -508       O  
ATOM   1950  N   SER A 388      66.504  61.104  70.417  1.00207.77           N  
ANISOU 1950  N   SER A 388    26145  22724  30072  -2072   5559  -1599       N  
ATOM   1951  CA  SER A 388      67.088  62.048  71.362  1.00209.92           C  
ANISOU 1951  CA  SER A 388    26110  22787  30863  -2259   5540  -1982       C  
ATOM   1952  C   SER A 388      67.454  61.344  72.662  1.00206.68           C  
ANISOU 1952  C   SER A 388    25322  22733  30474  -2312   5059  -2366       C  
ATOM   1953  O   SER A 388      67.439  61.949  73.749  1.00206.97           O  
ANISOU 1953  O   SER A 388    25165  22768  30704  -2364   4834  -2702       O  
ATOM   1954  CB  SER A 388      66.166  63.251  71.576  1.00213.72           C  
ANISOU 1954  CB  SER A 388    26805  23054  31343  -2180   5574  -1953       C  
ATOM   1955  OG  SER A 388      66.656  64.381  70.877  1.00223.02           O  
ANISOU 1955  OG  SER A 388    28062  23710  32965  -2301   6072  -1867       O  
ATOM   1956  N   GLY A 389      67.762  60.066  72.551  1.00205.34           N  
ANISOU 1956  N   GLY A 389    25065  22868  30085  -2279   4891  -2317       N  
ATOM   1957  CA  GLY A 389      68.145  59.280  73.730  1.00206.54           C  
ANISOU 1957  CA  GLY A 389    24886  23368  30220  -2303   4429  -2641       C  
ATOM   1958  C   GLY A 389      69.426  58.493  73.501  1.00211.04           C  
ANISOU 1958  C   GLY A 389    25159  23960  31066  -2430   4482  -2759       C  
ATOM   1959  O   GLY A 389      70.202  58.791  72.618  1.00215.41           O  
ANISOU 1959  O   GLY A 389    25674  24209  31963  -2554   4908  -2691       O  
ATOM   1960  N   ALA A 390      69.635  57.483  74.327  1.00208.11           N  
ANISOU 1960  N   ALA A 390    24578  23950  30543  -2389   4052  -2934       N  
ATOM   1961  CA  ALA A 390      70.877  56.698  74.279  1.00204.12           C  
ANISOU 1961  CA  ALA A 390    23743  23489  30321  -2492   4028  -3102       C  
ATOM   1962  C   ALA A 390      70.574  55.224  74.030  1.00203.62           C  
ANISOU 1962  C   ALA A 390    23785  23776  29804  -2342   3804  -2881       C  
ATOM   1963  O   ALA A 390      69.556  54.662  74.519  1.00211.30           O  
ANISOU 1963  O   ALA A 390    24936  25059  30289  -2178   3468  -2756       O  
ATOM   1964  CB  ALA A 390      71.652  56.853  75.561  1.00202.33           C  
ANISOU 1964  CB  ALA A 390    23106  23335  30433  -2586   3690  -3583       C  
ATOM   1965  N   LYS A 391      71.481  54.570  73.319  1.00201.47           N  
ANISOU 1965  N   LYS A 391    23376  23452  29721  -2402   3985  -2853       N  
ATOM   1966  CA  LYS A 391      71.330  53.141  73.033  1.00197.47           C  
ANISOU 1966  CA  LYS A 391    22936  23239  28855  -2269   3784  -2675       C  
ATOM   1967  C   LYS A 391      71.706  52.307  74.275  1.00190.72           C  
ANISOU 1967  C   LYS A 391    21787  22694  27983  -2240   3259  -2948       C  
ATOM   1968  O   LYS A 391      72.609  52.625  75.038  1.00191.46           O  
ANISOU 1968  O   LYS A 391    21531  22738  28475  -2352   3131  -3313       O  
ATOM   1969  CB  LYS A 391      72.149  52.703  71.800  1.00200.89           C  
ANISOU 1969  CB  LYS A 391    23342  23515  29473  -2319   4171  -2553       C  
ATOM   1970  CG  LYS A 391      71.354  52.029  70.665  1.00199.92           C  
ANISOU 1970  CG  LYS A 391    23610  23474  28876  -2150   4309  -2148       C  
ATOM   1971  CD  LYS A 391      71.066  50.541  70.904  1.00198.73           C  
ANISOU 1971  CD  LYS A 391    23455  23681  28372  -2006   3900  -2086       C  
ATOM   1972  CE  LYS A 391      69.963  49.924  70.025  1.00196.19           C  
ANISOU 1972  CE  LYS A 391    23535  23478  27530  -1813   3911  -1720       C  
ATOM   1973  NZ  LYS A 391      69.171  48.849  70.726  1.00189.29           N  
ANISOU 1973  NZ  LYS A 391    22693  22948  26277  -1677   3415  -1666       N  
ATOM   1974  N   CYS A 392      70.979  51.189  74.404  1.00178.97           N  
ANISOU 1974  N   CYS A 392    20460  21519  26019  -2074   2958  -2748       N  
ATOM   1975  CA  CYS A 392      71.290  50.072  75.268  1.00171.59           C  
ANISOU 1975  CA  CYS A 392    19328  20884  24984  -2006   2506  -2879       C  
ATOM   1976  C   CYS A 392      71.823  48.911  74.423  1.00178.02           C  
ANISOU 1976  C   CYS A 392    20102  21733  25803  -1972   2573  -2751       C  
ATOM   1977  O   CYS A 392      71.854  48.937  73.188  1.00187.74           O  
ANISOU 1977  O   CYS A 392    21486  22793  27053  -1984   2956  -2552       O  
ATOM   1978  CB  CYS A 392      70.018  49.608  75.993  1.00159.27           C  
ANISOU 1978  CB  CYS A 392    17994  19627  22891  -1843   2152  -2711       C  
ATOM   1979  SG  CYS A 392      68.717  48.978  74.887  1.00147.27           S  
ANISOU 1979  SG  CYS A 392    16897  18173  20886  -1698   2287  -2236       S  
ATOM   1980  N   CYS A 393      72.187  47.837  75.106  1.00179.24           N  
ANISOU 1980  N   CYS A 393    20076  22125  25902  -1903   2181  -2853       N  
ATOM   1981  CA  CYS A 393      72.658  46.630  74.431  1.00179.03           C  
ANISOU 1981  CA  CYS A 393    19998  22153  25871  -1849   2178  -2754       C  
ATOM   1982  C   CYS A 393      71.737  45.414  74.608  1.00178.70           C  
ANISOU 1982  C   CYS A 393    20163  22386  25349  -1676   1853  -2500       C  
ATOM   1983  O   CYS A 393      72.192  44.287  74.520  1.00182.83           O  
ANISOU 1983  O   CYS A 393    20574  23007  25885  -1615   1684  -2496       O  
ATOM   1984  CB  CYS A 393      74.061  46.312  74.932  1.00176.86           C  
ANISOU 1984  CB  CYS A 393    19291  21868  26039  -1918   2023  -3102       C  
ATOM   1985  SG  CYS A 393      74.102  46.033  76.699  1.00174.11           S  
ANISOU 1985  SG  CYS A 393    18759  21798  25593  -1839   1405  -3351       S  
ATOM   1986  N   ARG A 394      70.463  45.695  74.887  1.00176.83           N  
ANISOU 1986  N   ARG A 394    20203  22251  24731  -1604   1775  -2306       N  
ATOM   1987  CA  ARG A 394      69.473  44.664  75.166  1.00174.77           C  
ANISOU 1987  CA  ARG A 394    20125  22235  24042  -1457   1480  -2069       C  
ATOM   1988  C   ARG A 394      69.227  43.768  73.946  1.00165.27           C  
ANISOU 1988  C   ARG A 394    19085  21001  22707  -1384   1618  -1825       C  
ATOM   1989  O   ARG A 394      69.459  42.553  73.979  1.00165.06           O  
ANISOU 1989  O   ARG A 394    18984  21091  22639  -1313   1398  -1787       O  
ATOM   1990  CB  ARG A 394      68.168  45.336  75.595  1.00182.78           C  
ANISOU 1990  CB  ARG A 394    21383  23324  24738  -1412   1450  -1933       C  
ATOM   1991  CG  ARG A 394      68.188  45.988  76.978  1.00191.39           C  
ANISOU 1991  CG  ARG A 394    22351  24524  25843  -1433   1222  -2160       C  
ATOM   1992  CD  ARG A 394      66.756  46.293  77.407  1.00195.75           C  
ANISOU 1992  CD  ARG A 394    23155  25211  26008  -1349   1152  -1980       C  
ATOM   1993  NE  ARG A 394      66.551  46.815  78.763  1.00193.23           N  
ANISOU 1993  NE  ARG A 394    22773  25046  25598  -1329    921  -2163       N  
ATOM   1994  CZ  ARG A 394      66.637  48.089  79.133  1.00191.98           C  
ANISOU 1994  CZ  ARG A 394    22575  24773  25595  -1395   1027  -2378       C  
ATOM   1995  NH1 ARG A 394      66.986  49.051  78.267  1.00189.84           N  
ANISOU 1995  NH1 ARG A 394    22307  24199  25623  -1504   1384  -2433       N  
ATOM   1996  NH2 ARG A 394      66.387  48.395  80.405  1.00194.01           N  
ANISOU 1996  NH2 ARG A 394    22792  25214  25706  -1343    776  -2544       N  
ATOM   1997  N   LYS A 395      68.769  44.410  72.869  1.00156.20           N  
ANISOU 1997  N   LYS A 395    18167  19684  21496  -1388   1979  -1671       N  
ATOM   1998  CA  LYS A 395      68.461  43.751  71.604  1.00154.67           C  
ANISOU 1998  CA  LYS A 395    18173  19448  21144  -1298   2142  -1455       C  
ATOM   1999  C   LYS A 395      69.676  42.991  71.080  1.00157.53           C  
ANISOU 1999  C   LYS A 395    18325  19752  21774  -1321   2215  -1575       C  
ATOM   2000  O   LYS A 395      69.571  41.922  70.484  1.00153.89           O  
ANISOU 2000  O   LYS A 395    17930  19354  21186  -1221   2144  -1464       O  
ATOM   2001  CB  LYS A 395      68.078  44.804  70.582  1.00157.02           C  
ANISOU 2001  CB  LYS A 395    18723  19538  21400  -1305   2557  -1328       C  
ATOM   2002  CG  LYS A 395      66.830  45.585  70.943  1.00157.85           C  
ANISOU 2002  CG  LYS A 395    19049  19674  21249  -1261   2511  -1204       C  
ATOM   2003  CD  LYS A 395      66.176  46.160  69.700  1.00157.41           C  
ANISOU 2003  CD  LYS A 395    19327  19460  21020  -1181   2836   -987       C  
ATOM   2004  CE  LYS A 395      64.748  46.581  69.958  1.00153.38           C  
ANISOU 2004  CE  LYS A 395    19048  19027  20200  -1084   2712   -832       C  
ATOM   2005  NZ  LYS A 395      64.009  46.708  68.675  1.00154.35           N  
ANISOU 2005  NZ  LYS A 395    19507  19057  20079   -941   2912   -599       N  
ATOM   2006  N   GLU A 396      70.843  43.598  71.292  1.00161.15           N  
ANISOU 2006  N   GLU A 396    18513  20076  22638  -1455   2370  -1826       N  
ATOM   2007  CA  GLU A 396      72.115  43.020  70.875  1.00158.47           C  
ANISOU 2007  CA  GLU A 396    17913  19665  22630  -1493   2467  -1990       C  
ATOM   2008  C   GLU A 396      72.360  41.692  71.591  1.00149.15           C  
ANISOU 2008  C   GLU A 396    16555  18692  21422  -1410   2013  -2055       C  
ATOM   2009  O   GLU A 396      72.698  40.687  70.937  1.00143.83           O  
ANISOU 2009  O   GLU A 396    15856  18030  20762  -1336   2012  -2018       O  
ATOM   2010  CB  GLU A 396      73.253  44.018  71.163  1.00164.62           C  
ANISOU 2010  CB  GLU A 396    18389  20258  23898  -1668   2680  -2280       C  
ATOM   2011  CG  GLU A 396      73.235  45.309  70.328  1.00172.26           C  
ANISOU 2011  CG  GLU A 396    19506  20957  24986  -1768   3203  -2215       C  
ATOM   2012  CD  GLU A 396      71.930  46.138  70.446  1.00178.99           C  
ANISOU 2012  CD  GLU A 396    20696  21810  25502  -1727   3218  -2014       C  
ATOM   2013  OE1 GLU A 396      71.299  46.188  71.538  1.00179.85           O  
ANISOU 2013  OE1 GLU A 396    20804  22086  25444  -1698   2856  -2050       O  
ATOM   2014  OE2 GLU A 396      71.505  46.728  69.425  1.00186.88           O  
ANISOU 2014  OE2 GLU A 396    21977  22645  26382  -1706   3595  -1809       O  
ATOM   2015  N   CYS A 397      72.180  41.691  72.912  1.00145.94           N  
ANISOU 2015  N   CYS A 397    16044  18440  20965  -1407   1636  -2146       N  
ATOM   2016  CA  CYS A 397      72.316  40.462  73.706  1.00147.27           C  
ANISOU 2016  CA  CYS A 397    16086  18806  21064  -1308   1185  -2167       C  
ATOM   2017  C   CYS A 397      71.290  39.412  73.277  1.00142.44           C  
ANISOU 2017  C   CYS A 397    15735  18301  20082  -1174   1058  -1867       C  
ATOM   2018  O   CYS A 397      71.607  38.208  73.231  1.00143.27           O  
ANISOU 2018  O   CYS A 397    15754  18466  20213  -1091    851  -1850       O  
ATOM   2019  CB  CYS A 397      72.106  40.734  75.205  1.00152.74           C  
ANISOU 2019  CB  CYS A 397    16702  19664  21667  -1300    823  -2271       C  
ATOM   2020  SG  CYS A 397      73.372  41.687  76.047  1.00171.97           S  
ANISOU 2020  SG  CYS A 397    18762  22025  24551  -1420    782  -2700       S  
ATOM   2021  N   LEU A 398      70.065  39.850  72.984  1.00139.73           N  
ANISOU 2021  N   LEU A 398    15694  17971  19426  -1148   1165  -1645       N  
ATOM   2022  CA  LEU A 398      69.051  38.929  72.470  1.00139.10           C  
ANISOU 2022  CA  LEU A 398    15847  17966  19038  -1029   1067  -1383       C  
ATOM   2023  C   LEU A 398      69.518  38.282  71.183  1.00135.06           C  
ANISOU 2023  C   LEU A 398    15356  17343  18617   -981   1260  -1367       C  
ATOM   2024  O   LEU A 398      69.355  37.067  71.006  1.00129.24           O  
ANISOU 2024  O   LEU A 398    14630  16669  17805   -884   1054  -1284       O  
ATOM   2025  CB  LEU A 398      67.746  39.656  72.209  1.00142.15           C  
ANISOU 2025  CB  LEU A 398    16527  18352  19129  -1008   1195  -1189       C  
ATOM   2026  CG  LEU A 398      66.637  38.800  71.599  1.00142.85           C  
ANISOU 2026  CG  LEU A 398    16844  18500  18932   -886   1103   -945       C  
ATOM   2027  CD1 LEU A 398      66.391  37.507  72.365  1.00143.82           C  
ANISOU 2027  CD1 LEU A 398    16885  18777  18983   -825    712   -871       C  
ATOM   2028  CD2 LEU A 398      65.372  39.621  71.539  1.00140.18           C  
ANISOU 2028  CD2 LEU A 398    16748  18174  18338   -863   1189   -793       C  
ATOM   2029  N   LYS A 399      70.111  39.087  70.299  1.00136.01           N  
ANISOU 2029  N   LYS A 399    15480  17289  18906  -1044   1665  -1449       N  
ATOM   2030  CA  LYS A 399      70.602  38.586  69.017  1.00140.96           C  
ANISOU 2030  CA  LYS A 399    16145  17812  19599   -989   1911  -1445       C  
ATOM   2031  C   LYS A 399      71.706  37.569  69.211  1.00142.81           C  
ANISOU 2031  C   LYS A 399    16080  18070  20112   -975   1743  -1625       C  
ATOM   2032  O   LYS A 399      71.626  36.461  68.675  1.00142.64           O  
ANISOU 2032  O   LYS A 399    16102  18079  20014   -862   1636  -1567       O  
ATOM   2033  CB  LYS A 399      71.105  39.721  68.135  1.00146.36           C  
ANISOU 2033  CB  LYS A 399    16884  18298  20425  -1068   2416  -1489       C  
ATOM   2034  CG  LYS A 399      70.007  40.554  67.495  1.00152.85           C  
ANISOU 2034  CG  LYS A 399    18074  19063  20937  -1022   2635  -1271       C  
ATOM   2035  CD  LYS A 399      70.638  41.732  66.766  1.00164.13           C  
ANISOU 2035  CD  LYS A 399    19537  20268  22554  -1114   3148  -1310       C  
ATOM   2036  CE  LYS A 399      69.607  42.796  66.385  1.00174.43           C  
ANISOU 2036  CE  LYS A 399    21183  21492  23597  -1082   3342  -1110       C  
ATOM   2037  NZ  LYS A 399      70.210  44.133  66.102  1.00180.37           N  
ANISOU 2037  NZ  LYS A 399    21924  22005  24603  -1213   3791  -1159       N  
ATOM   2038  N   LEU A 400      72.746  37.952  69.961  1.00144.99           N  
ANISOU 2038  N   LEU A 400    16039  18318  20731  -1082   1710  -1864       N  
ATOM   2039  CA  LEU A 400      73.876  37.053  70.245  1.00146.57           C  
ANISOU 2039  CA  LEU A 400    15913  18535  21239  -1062   1522  -2069       C  
ATOM   2040  C   LEU A 400      73.416  35.722  70.840  1.00143.98           C  
ANISOU 2040  C   LEU A 400    15605  18365  20736   -932   1052  -1962       C  
ATOM   2041  O   LEU A 400      73.886  34.648  70.441  1.00143.93           O  
ANISOU 2041  O   LEU A 400    15502  18348  20835   -844    959  -2001       O  
ATOM   2042  CB  LEU A 400      74.820  37.674  71.240  1.00150.28           C  
ANISOU 2042  CB  LEU A 400    16050  18991  22056  -1174   1430  -2341       C  
ATOM   2043  CG  LEU A 400      75.621  38.861  70.751  1.00158.06           C  
ANISOU 2043  CG  LEU A 400    16895  19781  23379  -1327   1881  -2518       C  
ATOM   2044  CD1 LEU A 400      76.319  39.530  71.922  1.00165.71           C  
ANISOU 2044  CD1 LEU A 400    17550  20752  24659  -1433   1702  -2798       C  
ATOM   2045  CD2 LEU A 400      76.617  38.452  69.684  1.00159.92           C  
ANISOU 2045  CD2 LEU A 400    16975  19886  23900  -1326   2195  -2628       C  
ATOM   2046  N   MET A 401      72.496  35.803  71.796  1.00140.44           N  
ANISOU 2046  N   MET A 401    15281  18049  20030   -918    776  -1824       N  
ATOM   2047  CA  MET A 401      71.985  34.604  72.447  1.00137.53           C  
ANISOU 2047  CA  MET A 401    14948  17814  19492   -807    357  -1684       C  
ATOM   2048  C   MET A 401      71.227  33.724  71.453  1.00133.12           C  
ANISOU 2048  C   MET A 401    14609  17228  18740   -707    390  -1484       C  
ATOM   2049  O   MET A 401      71.441  32.498  71.387  1.00126.68           O  
ANISOU 2049  O   MET A 401    13724  16418  17990   -613    171  -1470       O  
ATOM   2050  CB  MET A 401      71.074  34.991  73.604  1.00139.37           C  
ANISOU 2050  CB  MET A 401    15296  18193  19464   -817    134  -1559       C  
ATOM   2051  CG  MET A 401      70.728  33.857  74.539  1.00143.73           C  
ANISOU 2051  CG  MET A 401    15845  18880  19882   -717   -291  -1427       C  
ATOM   2052  SD  MET A 401      72.206  33.107  75.270  1.00154.00           S  
ANISOU 2052  SD  MET A 401    16798  20199  21516   -661   -601  -1668       S  
ATOM   2053  CE  MET A 401      71.521  32.314  76.707  1.00157.93           C  
ANISOU 2053  CE  MET A 401    17387  20883  21734   -554  -1064  -1459       C  
ATOM   2054  N   LYS A 402      70.354  34.367  70.676  1.00135.88           N  
ANISOU 2054  N   LYS A 402    15221  17538  18867   -716    652  -1346       N  
ATOM   2055  CA  LYS A 402      69.622  33.701  69.607  1.00143.03           C  
ANISOU 2055  CA  LYS A 402    16348  18411  19586   -612    706  -1196       C  
ATOM   2056  C   LYS A 402      70.548  32.943  68.688  1.00144.66           C  
ANISOU 2056  C   LYS A 402    16443  18525  19995   -547    809  -1332       C  
ATOM   2057  O   LYS A 402      70.279  31.783  68.343  1.00139.68           O  
ANISOU 2057  O   LYS A 402    15851  17898  19321   -437    622  -1275       O  
ATOM   2058  CB  LYS A 402      68.754  34.678  68.797  1.00149.79           C  
ANISOU 2058  CB  LYS A 402    17491  19221  20202   -614   1008  -1074       C  
ATOM   2059  CG  LYS A 402      67.229  34.512  68.992  1.00152.35           C  
ANISOU 2059  CG  LYS A 402    18044  19632  20209   -557    823   -846       C  
ATOM   2060  CD  LYS A 402      66.433  35.761  68.573  1.00158.54           C  
ANISOU 2060  CD  LYS A 402    19065  20383  20787   -572   1080   -753       C  
ATOM   2061  CE  LYS A 402      66.505  36.122  67.079  1.00168.43           C  
ANISOU 2061  CE  LYS A 402    20519  21514  21962   -498   1427   -748       C  
ATOM   2062  NZ  LYS A 402      65.982  35.086  66.120  1.00171.08           N  
ANISOU 2062  NZ  LYS A 402    21002  21852  22146   -343   1329   -683       N  
ATOM   2063  N   TYR A 403      71.637  33.599  68.284  1.00147.80           N  
ANISOU 2063  N   TYR A 403    16690  18829  20635   -616   1121  -1521       N  
ATOM   2064  CA  TYR A 403      72.582  33.027  67.319  1.00151.19           C  
ANISOU 2064  CA  TYR A 403    17008  19168  21268   -557   1306  -1671       C  
ATOM   2065  C   TYR A 403      73.295  31.839  67.916  1.00148.38           C  
ANISOU 2065  C   TYR A 403    16381  18844  21152   -502    958  -1793       C  
ATOM   2066  O   TYR A 403      73.343  30.772  67.295  1.00151.83           O  
ANISOU 2066  O   TYR A 403    16835  19255  21596   -381    876  -1801       O  
ATOM   2067  CB  TYR A 403      73.624  34.067  66.902  1.00156.28           C  
ANISOU 2067  CB  TYR A 403    17510  19696  22170   -667   1741  -1846       C  
ATOM   2068  CG  TYR A 403      74.674  33.604  65.889  1.00163.82           C  
ANISOU 2068  CG  TYR A 403    18331  20557  23355   -617   2012  -2013       C  
ATOM   2069  CD1 TYR A 403      74.360  33.439  64.547  1.00166.92           C  
ANISOU 2069  CD1 TYR A 403    18984  20904  23532   -506   2296  -1931       C  
ATOM   2070  CD2 TYR A 403      75.998  33.373  66.275  1.00170.33           C  
ANISOU 2070  CD2 TYR A 403    18762  21342  24612   -668   1990  -2272       C  
ATOM   2071  CE1 TYR A 403      75.327  33.049  63.620  1.00172.57           C  
ANISOU 2071  CE1 TYR A 403    19585  21544  24437   -449   2578  -2092       C  
ATOM   2072  CE2 TYR A 403      76.965  32.973  65.362  1.00173.81           C  
ANISOU 2072  CE2 TYR A 403    19057  21697  25283   -621   2264  -2439       C  
ATOM   2073  CZ  TYR A 403      76.635  32.813  64.042  1.00175.51           C  
ANISOU 2073  CZ  TYR A 403    19546  21876  25263   -514   2572  -2345       C  
ATOM   2074  OH  TYR A 403      77.609  32.413  63.159  1.00180.20           O  
ANISOU 2074  OH  TYR A 403    19997  22399  26072   -458   2864  -2520       O  
ATOM   2075  N   LEU A 404      73.860  32.043  69.106  1.00143.63           N  
ANISOU 2075  N   LEU A 404    15534  18290  20747   -575    745  -1903       N  
ATOM   2076  CA  LEU A 404      74.498  30.970  69.857  1.00146.44           C  
ANISOU 2076  CA  LEU A 404    15645  18684  21311   -505    358  -2001       C  
ATOM   2077  C   LEU A 404      73.612  29.724  69.827  1.00144.46           C  
ANISOU 2077  C   LEU A 404    15567  18468  20851   -377     55  -1796       C  
ATOM   2078  O   LEU A 404      74.058  28.639  69.420  1.00145.53           O  
ANISOU 2078  O   LEU A 404    15607  18549  21139   -272    -57  -1864       O  
ATOM   2079  CB  LEU A 404      74.694  31.439  71.294  1.00147.59           C  
ANISOU 2079  CB  LEU A 404    15638  18924  21514   -570     94  -2056       C  
ATOM   2080  CG  LEU A 404      75.222  30.457  72.328  1.00151.46           C  
ANISOU 2080  CG  LEU A 404    15919  19479  22149   -479   -367  -2118       C  
ATOM   2081  CD1 LEU A 404      76.629  30.013  71.990  1.00154.45           C  
ANISOU 2081  CD1 LEU A 404    15964  19768  22951   -442   -341  -2402       C  
ATOM   2082  CD2 LEU A 404      75.251  31.161  73.680  1.00153.86           C  
ANISOU 2082  CD2 LEU A 404    16146  19898  22413   -532   -582  -2163       C  
ATOM   2083  N   LEU A 405      72.349  29.898  70.224  1.00142.91           N  
ANISOU 2083  N   LEU A 405    15614  18350  20335   -389    -56  -1556       N  
ATOM   2084  CA  LEU A 405      71.423  28.774  70.255  1.00146.35           C  
ANISOU 2084  CA  LEU A 405    16198  18801  20607   -292   -331  -1352       C  
ATOM   2085  C   LEU A 405      71.154  28.180  68.865  1.00144.19           C  
ANISOU 2085  C   LEU A 405    16062  18433  20289   -199   -179  -1352       C  
ATOM   2086  O   LEU A 405      71.063  26.953  68.724  1.00138.82           O  
ANISOU 2086  O   LEU A 405    15361  17706  19676    -97   -411  -1324       O  
ATOM   2087  CB  LEU A 405      70.093  29.152  70.882  1.00149.28           C  
ANISOU 2087  CB  LEU A 405    16783  19267  20667   -332   -428  -1108       C  
ATOM   2088  CG  LEU A 405      69.203  27.926  71.126  1.00155.67           C  
ANISOU 2088  CG  LEU A 405    17689  20079  21378   -251   -736   -898       C  
ATOM   2089  CD1 LEU A 405      69.613  27.203  72.402  1.00156.94           C  
ANISOU 2089  CD1 LEU A 405    17694  20289  21647   -221  -1094   -857       C  
ATOM   2090  CD2 LEU A 405      67.726  28.301  71.117  1.00158.46           C  
ANISOU 2090  CD2 LEU A 405    18287  20485  21433   -279   -701   -676       C  
ATOM   2091  N   GLU A 406      71.009  29.043  67.851  1.00146.41           N  
ANISOU 2091  N   GLU A 406    16497  18681  20450   -221    199  -1382       N  
ATOM   2092  CA  GLU A 406      70.769  28.559  66.502  1.00150.35           C  
ANISOU 2092  CA  GLU A 406    17155  19110  20859   -106    350  -1400       C  
ATOM   2093  C   GLU A 406      71.880  27.644  66.016  1.00147.00           C  
ANISOU 2093  C   GLU A 406    16527  18609  20714    -19    343  -1608       C  
ATOM   2094  O   GLU A 406      71.600  26.542  65.529  1.00145.20           O  
ANISOU 2094  O   GLU A 406    16349  18338  20482    103    171  -1606       O  
ATOM   2095  CB  GLU A 406      70.348  29.627  65.473  1.00158.11           C  
ANISOU 2095  CB  GLU A 406    18390  20075  21607   -109    750  -1364       C  
ATOM   2096  CG  GLU A 406      68.928  30.225  65.643  1.00164.51           C  
ANISOU 2096  CG  GLU A 406    19463  20945  22095   -127    705  -1144       C  
ATOM   2097  CD  GLU A 406      67.784  29.228  65.939  1.00168.94           C  
ANISOU 2097  CD  GLU A 406    20110  21543  22535    -59    331   -989       C  
ATOM   2098  OE1 GLU A 406      67.809  28.076  65.518  1.00173.14           O  
ANISOU 2098  OE1 GLU A 406    20615  22027  23143     44    159  -1034       O  
ATOM   2099  OE2 GLU A 406      66.812  29.599  66.629  1.00164.44           O  
ANISOU 2099  OE2 GLU A 406    19628  21041  21810   -113    209   -822       O  
ATOM   2100  N   GLN A 407      73.123  28.083  66.196  1.00147.06           N  
ANISOU 2100  N   GLN A 407    16286  18594  20996    -84    510  -1801       N  
ATOM   2101  CA  GLN A 407      74.296  27.312  65.791  1.00152.33           C  
ANISOU 2101  CA  GLN A 407    16710  19189  21977     -7    529  -2031       C  
ATOM   2102  C   GLN A 407      74.396  25.996  66.566  1.00152.02           C  
ANISOU 2102  C   GLN A 407    16514  19143  22101     75     51  -2025       C  
ATOM   2103  O   GLN A 407      74.528  24.905  65.966  1.00151.76           O  
ANISOU 2103  O   GLN A 407    16465  19039  22154    208    -50  -2094       O  
ATOM   2104  CB  GLN A 407      75.557  28.143  66.123  1.00157.35           C  
ANISOU 2104  CB  GLN A 407    17055  19807  22924   -121    752  -2239       C  
ATOM   2105  CG  GLN A 407      75.745  29.456  65.369  1.00161.83           C  
ANISOU 2105  CG  GLN A 407    17715  20333  23436   -217   1279  -2271       C  
ATOM   2106  CD  GLN A 407      75.990  29.176  63.930  1.00172.63           C  
ANISOU 2106  CD  GLN A 407    19197  21637  24756   -108   1621  -2343       C  
ATOM   2107  OE1 GLN A 407      75.064  29.224  63.130  1.00184.11           O  
ANISOU 2107  OE1 GLN A 407    20988  23103  25861    -28   1728  -2193       O  
ATOM   2108  NE2 GLN A 407      77.226  28.794  63.592  1.00180.72           N  
ANISOU 2108  NE2 GLN A 407    19939  22601  26125    -79   1766  -2589       N  
ATOM   2109  N   LEU A 408      74.333  26.104  67.896  1.00151.67           N  
ANISOU 2109  N   LEU A 408    16370  19165  22092      9   -237  -1941       N  
ATOM   2110  CA  LEU A 408      74.388  24.922  68.751  1.00153.51           C  
ANISOU 2110  CA  LEU A 408    16487  19387  22450     93   -693  -1886       C  
ATOM   2111  C   LEU A 408      73.274  23.924  68.418  1.00154.08           C  
ANISOU 2111  C   LEU A 408    16781  19413  22348    181   -886  -1689       C  
ATOM   2112  O   LEU A 408      73.406  22.726  68.693  1.00159.89           O  
ANISOU 2112  O   LEU A 408    17432  20076  23243    281  -1197  -1672       O  
ATOM   2113  CB  LEU A 408      74.264  25.311  70.218  1.00154.70           C  
ANISOU 2113  CB  LEU A 408    16583  19641  22552     22   -948  -1777       C  
ATOM   2114  CG  LEU A 408      75.572  25.534  70.953  1.00158.31           C  
ANISOU 2114  CG  LEU A 408    16714  20118  23316     12  -1045  -2007       C  
ATOM   2115  CD1 LEU A 408      75.295  26.326  72.229  1.00159.94           C  
ANISOU 2115  CD1 LEU A 408    16937  20455  23377    -70  -1196  -1920       C  
ATOM   2116  CD2 LEU A 408      76.234  24.205  71.267  1.00163.57           C  
ANISOU 2116  CD2 LEU A 408    17192  20715  24239    159  -1397  -2075       C  
ATOM   2117  N   LYS A 409      72.177  24.425  67.833  1.00148.82           N  
ANISOU 2117  N   LYS A 409    16387  18774  21380    148   -712  -1547       N  
ATOM   2118  CA  LYS A 409      71.056  23.569  67.428  1.00148.82           C  
ANISOU 2118  CA  LYS A 409    16583  18723  21237    224   -880  -1393       C  
ATOM   2119  C   LYS A 409      71.265  22.941  66.053  1.00150.47           C  
ANISOU 2119  C   LYS A 409    16836  18833  21501    355   -754  -1563       C  
ATOM   2120  O   LYS A 409      70.845  21.804  65.813  1.00150.63           O  
ANISOU 2120  O   LYS A 409    16886  18761  21582    453   -991  -1538       O  
ATOM   2121  CB  LYS A 409      69.738  24.354  67.345  1.00149.38           C  
ANISOU 2121  CB  LYS A 409    16917  18867  20972    157   -775  -1195       C  
ATOM   2122  CG  LYS A 409      68.771  24.152  68.488  1.00150.60           C  
ANISOU 2122  CG  LYS A 409    17126  19073  21020     99  -1051   -938       C  
ATOM   2123  CD  LYS A 409      67.527  25.005  68.304  1.00152.98           C  
ANISOU 2123  CD  LYS A 409    17660  19447  21018     41   -912   -784       C  
ATOM   2124  CE  LYS A 409      66.537  24.442  67.278  1.00155.55           C  
ANISOU 2124  CE  LYS A 409    18161  19700  21241    130   -938   -750       C  
ATOM   2125  NZ  LYS A 409      65.936  23.129  67.661  1.00159.50           N  
ANISOU 2125  NZ  LYS A 409    18623  20111  21867    168  -1276   -626       N  
ATOM   2126  N   LYS A 410      71.891  23.683  65.141  1.00153.10           N  
ANISOU 2126  N   LYS A 410    17181  19179  21809    360   -370  -1735       N  
ATOM   2127  CA  LYS A 410      72.170  23.141  63.827  1.00158.37           C  
ANISOU 2127  CA  LYS A 410    17903  19775  22494    504   -217  -1914       C  
ATOM   2128  C   LYS A 410      73.243  22.067  63.872  1.00154.35           C  
ANISOU 2128  C   LYS A 410    17124  19175  22344    597   -374  -2114       C  
ATOM   2129  O   LYS A 410      73.243  21.170  63.027  1.00150.84           O  
ANISOU 2129  O   LYS A 410    16716  18650  21943    743   -419  -2236       O  
ATOM   2130  CB  LYS A 410      72.354  24.270  62.793  1.00168.09           C  
ANISOU 2130  CB  LYS A 410    19289  21047  23528    497    271  -1988       C  
ATOM   2131  CG  LYS A 410      71.018  24.631  62.098  1.00174.99           C  
ANISOU 2131  CG  LYS A 410    20520  21957  24010    545    331  -1836       C  
ATOM   2132  CD  LYS A 410      70.256  25.945  62.443  1.00179.99           C  
ANISOU 2132  CD  LYS A 410    21332  22670  24386    423    481  -1640       C  
ATOM   2133  CE  LYS A 410      68.806  25.686  62.908  1.00181.97           C  
ANISOU 2133  CE  LYS A 410    21736  22951  24452    416    165  -1427       C  
ATOM   2134  NZ  LYS A 410      67.895  26.817  62.554  1.00184.74           N  
ANISOU 2134  NZ  LYS A 410    22355  23360  24476    397    364  -1292       N  
ATOM   2135  N   GLU A 411      74.106  22.126  64.878  1.00154.46           N  
ANISOU 2135  N   GLU A 411    16872  19199  22615    529   -492  -2157       N  
ATOM   2136  CA  GLU A 411      75.162  21.116  65.014  1.00159.28           C  
ANISOU 2136  CA  GLU A 411    17202  19719  23595    631   -676  -2351       C  
ATOM   2137  C   GLU A 411      74.742  19.897  65.843  1.00152.43           C  
ANISOU 2137  C   GLU A 411    16301  18772  22842    694  -1170  -2207       C  
ATOM   2138  O   GLU A 411      75.255  18.790  65.640  1.00150.37           O  
ANISOU 2138  O   GLU A 411    15902  18393  22839    827  -1354  -2340       O  
ATOM   2139  CB  GLU A 411      76.433  21.724  65.629  1.00166.95           C  
ANISOU 2139  CB  GLU A 411    17866  20727  24839    557   -578  -2516       C  
ATOM   2140  CG  GLU A 411      77.576  20.720  65.790  1.00171.82           C  
ANISOU 2140  CG  GLU A 411    18165  21251  25865    678   -781  -2738       C  
ATOM   2141  CD  GLU A 411      78.954  21.382  65.982  1.00173.78           C  
ANISOU 2141  CD  GLU A 411    18078  21523  26427    622   -578  -2994       C  
ATOM   2142  OE1 GLU A 411      79.033  22.623  66.191  1.00171.78           O  
ANISOU 2142  OE1 GLU A 411    17823  21349  26095    471   -325  -2982       O  
ATOM   2143  OE2 GLU A 411      79.982  20.653  65.952  1.00175.54           O  
ANISOU 2143  OE2 GLU A 411    18014  21671  27012    730   -684  -3223       O  
ATOM   2144  N   PHE A 412      73.827  20.095  66.786  1.00148.39           N  
ANISOU 2144  N   PHE A 412    15913  18315  22152    605  -1370  -1933       N  
ATOM   2145  CA  PHE A 412      73.431  19.007  67.680  1.00149.84           C  
ANISOU 2145  CA  PHE A 412    16075  18417  22439    651  -1803  -1751       C  
ATOM   2146  C   PHE A 412      71.929  18.750  67.696  1.00151.87           C  
ANISOU 2146  C   PHE A 412    16586  18653  22461    617  -1916  -1487       C  
ATOM   2147  O   PHE A 412      71.129  19.597  68.031  1.00150.75           O  
ANISOU 2147  O   PHE A 412    16597  18623  22056    506  -1820  -1314       O  
ATOM   2148  CB  PHE A 412      73.939  19.270  69.093  1.00148.98           C  
ANISOU 2148  CB  PHE A 412    15814  18383  22407    599  -2005  -1667       C  
ATOM   2149  CG  PHE A 412      75.430  19.315  69.188  1.00150.76           C  
ANISOU 2149  CG  PHE A 412    15737  18602  22942    651  -1986  -1945       C  
ATOM   2150  CD1 PHE A 412      76.183  18.161  69.055  1.00155.02           C  
ANISOU 2150  CD1 PHE A 412    16091  19002  23805    803  -2198  -2089       C  
ATOM   2151  CD2 PHE A 412      76.085  20.522  69.408  1.00152.62           C  
ANISOU 2151  CD2 PHE A 412    15851  18957  23179    549  -1756  -2079       C  
ATOM   2152  CE1 PHE A 412      77.575  18.202  69.152  1.00161.97           C  
ANISOU 2152  CE1 PHE A 412    16658  19877  25005    859  -2189  -2368       C  
ATOM   2153  CE2 PHE A 412      77.460  20.582  69.500  1.00158.69           C  
ANISOU 2153  CE2 PHE A 412    16302  19712  24280    589  -1737  -2360       C  
ATOM   2154  CZ  PHE A 412      78.215  19.422  69.375  1.00164.43           C  
ANISOU 2154  CZ  PHE A 412    16832  20314  25328    748  -1955  -2509       C  
ATOM   2155  N   GLN A 413      71.641  17.478  67.472  1.00157.18           N  
ANISOU 2155  N   GLN A 413    17261  19161  23297    720  -2160  -1466       N  
ATOM   2156  CA  GLN A 413      70.280  16.881  67.441  1.00157.90           C  
ANISOU 2156  CA  GLN A 413    17532  19167  23293    707  -2327  -1252       C  
ATOM   2157  C   GLN A 413      69.735  16.784  68.830  1.00147.94           C  
ANISOU 2157  C   GLN A 413    16290  17929  21990    621  -2551   -932       C  
ATOM   2158  O   GLN A 413      68.513  16.642  69.016  1.00144.50           O  
ANISOU 2158  O   GLN A 413    16000  17469  21431    560  -2619   -709       O  
ATOM   2159  CB  GLN A 413      70.375  15.434  66.899  1.00172.47           C  
ANISOU 2159  CB  GLN A 413    19314  20788  25428    849  -2553  -1361       C  
ATOM   2160  CG  GLN A 413      69.309  14.383  67.303  1.00184.29           C  
ANISOU 2160  CG  GLN A 413    20880  22111  27029    843  -2855  -1125       C  
ATOM   2161  CD  GLN A 413      68.246  14.165  66.250  1.00202.94           C  
ANISOU 2161  CD  GLN A 413    23396  24405  29305    866  -2817  -1185       C  
ATOM   2162  OE1 GLN A 413      68.561  14.048  65.074  1.00221.97           O  
ANISOU 2162  OE1 GLN A 413    25821  26789  31726    979  -2703  -1468       O  
ATOM   2163  NE2 GLN A 413      66.981  14.100  66.665  1.00215.03           N  
ANISOU 2163  NE2 GLN A 413    25037  25908  30753    770  -2914   -933       N  
ATOM   2164  N   GLU A 414      70.606  16.922  69.820  1.00144.51           N  
ANISOU 2164  N   GLU A 414    15712  17553  21641    620  -2654   -912       N  
ATOM   2165  CA  GLU A 414      70.206  16.755  71.219  1.00144.23           C  
ANISOU 2165  CA  GLU A 414    15707  17548  21542    575  -2884   -606       C  
ATOM   2166  C   GLU A 414      69.441  17.982  71.700  1.00136.07           C  
ANISOU 2166  C   GLU A 414    14817  16714  20166    434  -2706   -450       C  
ATOM   2167  O   GLU A 414      68.883  18.003  72.803  1.00132.01           O  
ANISOU 2167  O   GLU A 414    14376  16260  19520    385  -2835   -180       O  
ATOM   2168  CB  GLU A 414      71.421  16.446  72.091  1.00153.63           C  
ANISOU 2168  CB  GLU A 414    16706  18739  22926    661  -3096   -663       C  
ATOM   2169  CG  GLU A 414      72.022  15.065  71.818  1.00160.71           C  
ANISOU 2169  CG  GLU A 414    17472  19407  24181    816  -3338   -754       C  
ATOM   2170  CD  GLU A 414      72.919  15.016  70.584  1.00167.70           C  
ANISOU 2170  CD  GLU A 414    18210  20241  25267    896  -3168  -1136       C  
ATOM   2171  OE1 GLU A 414      73.888  14.217  70.598  1.00171.82           O  
ANISOU 2171  OE1 GLU A 414    18543  20640  26101   1033  -3348  -1291       O  
ATOM   2172  OE2 GLU A 414      72.676  15.773  69.608  1.00175.28           O  
ANISOU 2172  OE2 GLU A 414    19245  21281  26070    835  -2850  -1280       O  
ATOM   2173  N   LEU A 415      69.364  18.991  70.848  1.00131.21           N  
ANISOU 2173  N   LEU A 415    14260  16195  19396    378  -2397   -610       N  
ATOM   2174  CA  LEU A 415      68.778  20.292  71.255  1.00129.91           C  
ANISOU 2174  CA  LEU A 415    14215  16215  18929    253  -2205   -507       C  
ATOM   2175  C   LEU A 415      67.611  20.636  70.351  1.00129.31           C  
ANISOU 2175  C   LEU A 415    14331  16137  18663    213  -2025   -462       C  
ATOM   2176  O   LEU A 415      67.279  21.790  70.166  1.00129.20           O  
ANISOU 2176  O   LEU A 415    14417  16245  18428    140  -1790   -473       O  
ATOM   2177  CB  LEU A 415      69.875  21.350  71.154  1.00132.15           C  
ANISOU 2177  CB  LEU A 415    14380  16606  19223    225  -1991   -745       C  
ATOM   2178  CG  LEU A 415      71.128  21.034  71.973  1.00137.48           C  
ANISOU 2178  CG  LEU A 415    14826  17283  20124    284  -2190   -853       C  
ATOM   2179  CD1 LEU A 415      72.270  21.986  71.664  1.00137.98           C  
ANISOU 2179  CD1 LEU A 415    14721  17411  20291    252  -1956  -1144       C  
ATOM   2180  CD2 LEU A 415      70.814  21.054  73.462  1.00141.12           C  
ANISOU 2180  CD2 LEU A 415    15321  17843  20455    262  -2432   -616       C  
ATOM   2181  N   ASP A 416      66.894  19.623  69.907  1.00132.09           N  
ANISOU 2181  N   ASP A 416    14736  16344  19108    263  -2170   -392       N  
ATOM   2182  CA  ASP A 416      65.680  19.846  69.088  1.00134.91           C  
ANISOU 2182  CA  ASP A 416    15263  16692  19302    244  -2063   -357       C  
ATOM   2183  C   ASP A 416      64.504  20.272  69.932  1.00130.51           C  
ANISOU 2183  C   ASP A 416    14807  16222  18558    135  -2083    -82       C  
ATOM   2184  O   ASP A 416      63.495  20.728  69.395  1.00140.12           O  
ANISOU 2184  O   ASP A 416    16153  17469  19614    110  -1976    -54       O  
ATOM   2185  CB  ASP A 416      65.338  18.596  68.270  1.00142.66           C  
ANISOU 2185  CB  ASP A 416    16241  17474  20489    342  -2230   -429       C  
ATOM   2186  CG  ASP A 416      66.483  18.145  67.369  1.00148.59           C  
ANISOU 2186  CG  ASP A 416    16895  18143  21418    470  -2195   -725       C  
ATOM   2187  OD1 ASP A 416      67.509  18.852  67.304  1.00146.18           O  
ANISOU 2187  OD1 ASP A 416    16522  17936  21081    471  -2007   -873       O  
ATOM   2188  OD2 ASP A 416      66.353  17.061  66.751  1.00159.35           O  
ANISOU 2188  OD2 ASP A 416    18235  19334  22977    567  -2354   -820       O  
ATOM   2189  N   ALA A 417      64.611  20.121  71.259  1.00122.80           N  
ANISOU 2189  N   ALA A 417    13775  15290  17593     87  -2222    118       N  
ATOM   2190  CA  ALA A 417      63.574  20.573  72.193  1.00122.97           C  
ANISOU 2190  CA  ALA A 417    13887  15419  17417    -11  -2211    383       C  
ATOM   2191  C   ALA A 417      63.592  22.083  72.340  1.00120.06           C  
ANISOU 2191  C   ALA A 417    13586  15252  16780    -77  -1974    326       C  
ATOM   2192  O   ALA A 417      62.573  22.705  72.664  1.00118.70           O  
ANISOU 2192  O   ALA A 417    13514  15173  16412   -148  -1886    471       O  
ATOM   2193  CB  ALA A 417      63.805  19.931  73.532  1.00126.08           C  
ANISOU 2193  CB  ALA A 417    14225  15806  17873    -10  -2421    605       C  
ATOM   2194  N   PHE A 418      64.756  22.672  72.112  1.00122.02           N  
ANISOU 2194  N   PHE A 418    13760  15551  17048    -55  -1864    107       N  
ATOM   2195  CA  PHE A 418      64.955  24.101  72.338  1.00126.50           C  
ANISOU 2195  CA  PHE A 418    14363  16279  17420   -124  -1645     35       C  
ATOM   2196  C   PHE A 418      64.578  24.934  71.128  1.00131.96           C  
ANISOU 2196  C   PHE A 418    15177  16971  17989   -130  -1373    -87       C  
ATOM   2197  O   PHE A 418      64.877  24.597  70.008  1.00139.51           O  
ANISOU 2197  O   PHE A 418    16142  17830  19035    -58  -1306   -239       O  
ATOM   2198  CB  PHE A 418      66.389  24.399  72.760  1.00127.20           C  
ANISOU 2198  CB  PHE A 418    14290  16410  17628   -111  -1651   -144       C  
ATOM   2199  CG  PHE A 418      66.798  23.681  74.011  1.00127.56           C  
ANISOU 2199  CG  PHE A 418    14238  16475  17753    -75  -1941    -27       C  
ATOM   2200  CD1 PHE A 418      66.539  24.217  75.268  1.00124.92           C  
ANISOU 2200  CD1 PHE A 418    13940  16294  17227   -117  -2005    113       C  
ATOM   2201  CD2 PHE A 418      67.416  22.429  73.936  1.00130.30           C  
ANISOU 2201  CD2 PHE A 418    14472  16682  18352     21  -2161    -51       C  
ATOM   2202  CE1 PHE A 418      66.914  23.528  76.418  1.00127.47           C  
ANISOU 2202  CE1 PHE A 418    14208  16642  17579    -53  -2281    237       C  
ATOM   2203  CE2 PHE A 418      67.779  21.730  75.084  1.00130.81           C  
ANISOU 2203  CE2 PHE A 418    14473  16750  18476     80  -2443     83       C  
ATOM   2204  CZ  PHE A 418      67.525  22.283  76.329  1.00129.30           C  
ANISOU 2204  CZ  PHE A 418    14340  16725  18061     48  -2503    236       C  
ATOM   2205  N   CYS A 419      63.927  26.077  71.403  1.00135.14           N  
ANISOU 2205  N   CYS A 419    15688  17491  18166   -202  -1214    -18       N  
ATOM   2206  CA  CYS A 419      63.550  27.084  70.399  1.00137.97           C  
ANISOU 2206  CA  CYS A 419    16191  17862  18369   -202   -944   -105       C  
ATOM   2207  C   CYS A 419      63.992  28.476  70.874  1.00132.14           C  
ANISOU 2207  C   CYS A 419    15451  17227  17527   -282   -740   -168       C  
ATOM   2208  O   CYS A 419      64.440  28.625  72.001  1.00126.98           O  
ANISOU 2208  O   CYS A 419    14689  16653  16902   -332   -838   -150       O  
ATOM   2209  CB  CYS A 419      62.028  27.018  70.086  1.00141.57           C  
ANISOU 2209  CB  CYS A 419    16796  18314  18678   -189   -976     45       C  
ATOM   2210  SG  CYS A 419      60.831  27.405  71.373  1.00132.08           S  
ANISOU 2210  SG  CYS A 419    15627  17237  17319   -279  -1045    294       S  
ATOM   2211  N   SER A 420      63.886  29.488  70.032  1.00130.72           N  
ANISOU 2211  N   SER A 420    15396  17038  17233   -283   -467   -248       N  
ATOM   2212  CA  SER A 420      64.338  30.807  70.442  1.00134.50           C  
ANISOU 2212  CA  SER A 420    15862  17576  17664   -366   -263   -321       C  
ATOM   2213  C   SER A 420      63.406  31.488  71.440  1.00128.54           C  
ANISOU 2213  C   SER A 420    15170  16938  16728   -428   -306   -177       C  
ATOM   2214  O   SER A 420      63.832  32.438  72.098  1.00130.49           O  
ANISOU 2214  O   SER A 420    15368  17245  16967   -499   -215   -248       O  
ATOM   2215  CB  SER A 420      64.605  31.692  69.228  1.00144.07           C  
ANISOU 2215  CB  SER A 420    17195  18713  18831   -346     72   -434       C  
ATOM   2216  OG  SER A 420      63.598  31.499  68.248  1.00154.10           O  
ANISOU 2216  OG  SER A 420    18667  19946  19934   -251     98   -353       O  
ATOM   2217  N   TYR A 421      62.182  30.984  71.619  1.00125.94           N  
ANISOU 2217  N   TYR A 421    14926  16641  16283   -403   -449      5       N  
ATOM   2218  CA  TYR A 421      61.280  31.564  72.578  1.00132.07           C  
ANISOU 2218  CA  TYR A 421    15748  17535  16894   -454   -473    140       C  
ATOM   2219  C   TYR A 421      61.752  31.376  74.018  1.00130.04           C  
ANISOU 2219  C   TYR A 421    15364  17387  16655   -498   -639    175       C  
ATOM   2220  O   TYR A 421      61.352  32.115  74.920  1.00131.95           O  
ANISOU 2220  O   TYR A 421    15632  17751  16751   -539   -617    221       O  
ATOM   2221  CB  TYR A 421      59.836  31.013  72.417  1.00137.90           C  
ANISOU 2221  CB  TYR A 421    16576  18273  17546   -420   -573    322       C  
ATOM   2222  CG  TYR A 421      58.853  31.859  73.212  1.00140.27           C  
ANISOU 2222  CG  TYR A 421    16937  18695  17664   -465   -518    432       C  
ATOM   2223  CD1 TYR A 421      58.326  33.032  72.669  1.00142.82           C  
ANISOU 2223  CD1 TYR A 421    17389  19019  17857   -452   -319    386       C  
ATOM   2224  CD2 TYR A 421      58.528  31.559  74.530  1.00138.16           C  
ANISOU 2224  CD2 TYR A 421    16605  18541  17345   -507   -648    575       C  
ATOM   2225  CE1 TYR A 421      57.486  33.852  73.417  1.00138.90           C  
ANISOU 2225  CE1 TYR A 421    16933  18629  17210   -484   -263    460       C  
ATOM   2226  CE2 TYR A 421      57.693  32.387  75.266  1.00136.88           C  
ANISOU 2226  CE2 TYR A 421    16495  18503  17008   -538   -571    650       C  
ATOM   2227  CZ  TYR A 421      57.193  33.529  74.705  1.00136.73           C  
ANISOU 2227  CZ  TYR A 421    16581  18479  16890   -528   -383    579       C  
ATOM   2228  OH  TYR A 421      56.381  34.332  75.452  1.00137.80           O  
ANISOU 2228  OH  TYR A 421    16754  18731  16870   -549   -313    635       O  
ATOM   2229  N   HIS A 422      62.587  30.368  74.237  1.00121.60           N  
ANISOU 2229  N   HIS A 422    14168  16280  15754   -469   -819    149       N  
ATOM   2230  CA  HIS A 422      63.182  30.123  75.541  1.00115.41           C  
ANISOU 2230  CA  HIS A 422    13274  15594  14982   -474  -1008    167       C  
ATOM   2231  C   HIS A 422      64.173  31.228  75.853  1.00116.34           C  
ANISOU 2231  C   HIS A 422    13307  15763  15133   -516   -900    -57       C  
ATOM   2232  O   HIS A 422      64.216  31.764  76.966  1.00127.56           O  
ANISOU 2232  O   HIS A 422    14709  17318  16440   -535   -967    -64       O  
ATOM   2233  CB  HIS A 422      63.990  28.836  75.483  1.00110.45           C  
ANISOU 2233  CB  HIS A 422    12522  14875  14566   -412  -1217    153       C  
ATOM   2234  CG  HIS A 422      63.167  27.602  75.415  1.00106.84           C  
ANISOU 2234  CG  HIS A 422    12111  14346  14136   -374  -1375    371       C  
ATOM   2235  ND1 HIS A 422      63.324  26.656  74.432  1.00107.73           N  
ANISOU 2235  ND1 HIS A 422    12194  14299  14438   -322  -1426    330       N  
ATOM   2236  CD2 HIS A 422      62.186  27.147  76.220  1.00105.64           C  
ANISOU 2236  CD2 HIS A 422    12021  14246  13869   -383  -1483    625       C  
ATOM   2237  CE1 HIS A 422      62.467  25.669  74.628  1.00108.43           C  
ANISOU 2237  CE1 HIS A 422    12316  14328  14553   -308  -1575    542       C  
ATOM   2238  NE2 HIS A 422      61.767  25.939  75.712  1.00108.16           N  
ANISOU 2238  NE2 HIS A 422    12335  14417  14343   -351  -1599    736       N  
ATOM   2239  N   VAL A 423      64.980  31.557  74.849  1.00109.81           N  
ANISOU 2239  N   VAL A 423    12426  14823  14474   -527   -725   -252       N  
ATOM   2240  CA  VAL A 423      65.911  32.673  74.909  1.00111.34           C  
ANISOU 2240  CA  VAL A 423    12523  15014  14767   -588   -560   -483       C  
ATOM   2241  C   VAL A 423      65.165  33.994  75.171  1.00111.51           C  
ANISOU 2241  C   VAL A 423    12671  15098  14600   -649   -383   -464       C  
ATOM   2242  O   VAL A 423      65.557  34.783  76.044  1.00114.71           O  
ANISOU 2242  O   VAL A 423    13000  15580  15003   -693   -399   -585       O  
ATOM   2243  CB  VAL A 423      66.733  32.767  73.619  1.00113.64           C  
ANISOU 2243  CB  VAL A 423    12762  15151  15263   -591   -331   -651       C  
ATOM   2244  CG1 VAL A 423      67.552  34.066  73.571  1.00116.38           C  
ANISOU 2244  CG1 VAL A 423    13020  15458  15738   -680    -86   -869       C  
ATOM   2245  CG2 VAL A 423      67.655  31.567  73.521  1.00117.17           C  
ANISOU 2245  CG2 VAL A 423    13039  15544  15934   -527   -515   -727       C  
ATOM   2246  N   LYS A 424      64.097  34.218  74.411  1.00109.65           N  
ANISOU 2246  N   LYS A 424    12621  14824  14218   -637   -234   -332       N  
ATOM   2247  CA  LYS A 424      63.288  35.419  74.539  1.00113.99           C  
ANISOU 2247  CA  LYS A 424    13301  15412  14596   -674    -67   -302       C  
ATOM   2248  C   LYS A 424      62.663  35.554  75.924  1.00115.20           C  
ANISOU 2248  C   LYS A 424    13457  15738  14575   -682   -233   -211       C  
ATOM   2249  O   LYS A 424      62.686  36.640  76.527  1.00118.09           O  
ANISOU 2249  O   LYS A 424    13823  16162  14883   -724   -154   -310       O  
ATOM   2250  CB  LYS A 424      62.191  35.340  73.489  1.00117.29           C  
ANISOU 2250  CB  LYS A 424    13908  15766  14890   -622     41   -160       C  
ATOM   2251  CG  LYS A 424      61.483  36.650  73.228  1.00124.66           C  
ANISOU 2251  CG  LYS A 424    14993  16684  15688   -636    262   -154       C  
ATOM   2252  CD  LYS A 424      60.867  36.676  71.810  1.00127.51           C  
ANISOU 2252  CD  LYS A 424    15536  16932  15978   -557    409    -91       C  
ATOM   2253  CE  LYS A 424      60.072  37.954  71.608  1.00128.21           C  
ANISOU 2253  CE  LYS A 424    15788  17000  15922   -547    597    -62       C  
ATOM   2254  NZ  LYS A 424      59.149  37.903  70.413  1.00128.53           N  
ANISOU 2254  NZ  LYS A 424    16029  16972  15832   -431    657     32       N  
ATOM   2255  N   THR A 425      62.111  34.451  76.433  1.00115.56           N  
ANISOU 2255  N   THR A 425    13506  15858  14542   -637   -451    -24       N  
ATOM   2256  CA  THR A 425      61.480  34.433  77.753  1.00122.95           C  
ANISOU 2256  CA  THR A 425    14464  16967  15284   -628   -588    101       C  
ATOM   2257  C   THR A 425      62.502  34.721  78.849  1.00124.25           C  
ANISOU 2257  C   THR A 425    14509  17235  15465   -627   -721    -58       C  
ATOM   2258  O   THR A 425      62.293  35.582  79.720  1.00128.36           O  
ANISOU 2258  O   THR A 425    15054  17881  15834   -637   -706   -117       O  
ATOM   2259  CB  THR A 425      60.771  33.097  78.019  1.00128.21           C  
ANISOU 2259  CB  THR A 425    15152  17656  15905   -585   -768    354       C  
ATOM   2260  OG1 THR A 425      59.975  32.764  76.891  1.00128.09           O  
ANISOU 2260  OG1 THR A 425    15211  17522  15932   -578   -681    442       O  
ATOM   2261  CG2 THR A 425      59.847  33.183  79.228  1.00135.43           C  
ANISOU 2261  CG2 THR A 425    16128  18743  16584   -577   -821    528       C  
ATOM   2262  N   ALA A 426      63.606  33.992  78.796  1.00124.34           N  
ANISOU 2262  N   ALA A 426    14385  17193  15666   -602   -867   -149       N  
ATOM   2263  CA  ALA A 426      64.698  34.211  79.724  1.00127.95           C  
ANISOU 2263  CA  ALA A 426    14699  17731  16184   -583  -1029   -342       C  
ATOM   2264  C   ALA A 426      65.161  35.673  79.720  1.00123.85           C  
ANISOU 2264  C   ALA A 426    14126  17197  15733   -655   -852   -609       C  
ATOM   2265  O   ALA A 426      65.378  36.261  80.782  1.00130.04           O  
ANISOU 2265  O   ALA A 426    14873  18112  16423   -641   -959   -733       O  
ATOM   2266  CB  ALA A 426      65.869  33.337  79.357  1.00132.69           C  
ANISOU 2266  CB  ALA A 426    15136  18230  17050   -548  -1165   -447       C  
ATOM   2267  N   ILE A 427      65.318  36.258  78.534  1.00117.39           N  
ANISOU 2267  N   ILE A 427    13312  16212  15077   -724   -580   -701       N  
ATOM   2268  CA  ILE A 427      65.804  37.628  78.463  1.00120.66           C  
ANISOU 2268  CA  ILE A 427    13668  16564  15610   -804   -383   -942       C  
ATOM   2269  C   ILE A 427      64.762  38.644  78.936  1.00117.14           C  
ANISOU 2269  C   ILE A 427    13373  16200  14933   -820   -282   -892       C  
ATOM   2270  O   ILE A 427      65.117  39.719  79.421  1.00120.14           O  
ANISOU 2270  O   ILE A 427    13693  16584  15369   -866   -226  -1102       O  
ATOM   2271  CB  ILE A 427      66.423  38.007  77.112  1.00124.21           C  
ANISOU 2271  CB  ILE A 427    14079  16799  16317   -870    -91  -1053       C  
ATOM   2272  CG1 ILE A 427      67.395  39.187  77.321  1.00129.46           C  
ANISOU 2272  CG1 ILE A 427    14581  17383  17223   -962     40  -1355       C  
ATOM   2273  CG2 ILE A 427      65.351  38.339  76.089  1.00122.56           C  
ANISOU 2273  CG2 ILE A 427    14098  16506  15962   -869    155   -872       C  
ATOM   2274  CD1 ILE A 427      68.329  39.443  76.178  1.00132.79           C  
ANISOU 2274  CD1 ILE A 427    14899  17593  17960  -1032    319  -1492       C  
ATOM   2275  N   PHE A 428      63.485  38.295  78.809  1.00115.79           N  
ANISOU 2275  N   PHE A 428    13378  16085  14529   -780   -266   -634       N  
ATOM   2276  CA  PHE A 428      62.438  39.094  79.434  1.00121.83           C  
ANISOU 2276  CA  PHE A 428    14266  16960  15061   -772   -212   -578       C  
ATOM   2277  C   PHE A 428      62.622  39.097  80.937  1.00125.15           C  
ANISOU 2277  C   PHE A 428    14631  17587  15332   -728   -438   -646       C  
ATOM   2278  O   PHE A 428      62.557  40.154  81.580  1.00123.26           O  
ANISOU 2278  O   PHE A 428    14396  17411  15025   -739   -397   -805       O  
ATOM   2279  CB  PHE A 428      61.019  38.637  79.116  1.00120.57           C  
ANISOU 2279  CB  PHE A 428    14267  16835  14708   -732   -174   -300       C  
ATOM   2280  CG  PHE A 428      60.545  38.989  77.741  1.00116.28           C  
ANISOU 2280  CG  PHE A 428    13831  16122  14227   -744     53   -252       C  
ATOM   2281  CD1 PHE A 428      60.792  40.242  77.190  1.00116.88           C  
ANISOU 2281  CD1 PHE A 428    13946  16069  14392   -787    288   -403       C  
ATOM   2282  CD2 PHE A 428      59.812  38.071  77.001  1.00113.99           C  
ANISOU 2282  CD2 PHE A 428    13616  15792  13902   -700     25    -54       C  
ATOM   2283  CE1 PHE A 428      60.355  40.550  75.924  1.00116.67           C  
ANISOU 2283  CE1 PHE A 428    14055  15891  14383   -768    492   -337       C  
ATOM   2284  CE2 PHE A 428      59.365  38.374  75.737  1.00114.47           C  
ANISOU 2284  CE2 PHE A 428    13795  15713  13984   -678    201    -22       C  
ATOM   2285  CZ  PHE A 428      59.636  39.612  75.196  1.00116.04           C  
ANISOU 2285  CZ  PHE A 428    14058  15798  14231   -703    436   -152       C  
ATOM   2286  N   HIS A 429      62.861  37.913  81.495  1.00130.00           N  
ANISOU 2286  N   HIS A 429    15205  18300  15890   -663   -684   -529       N  
ATOM   2287  CA  HIS A 429      63.089  37.799  82.930  1.00138.54           C  
ANISOU 2287  CA  HIS A 429    16262  19588  16787   -586   -924   -573       C  
ATOM   2288  C   HIS A 429      64.324  38.593  83.368  1.00140.13           C  
ANISOU 2288  C   HIS A 429    16299  19786  17155   -600  -1006   -937       C  
ATOM   2289  O   HIS A 429      64.319  39.225  84.430  1.00144.80           O  
ANISOU 2289  O   HIS A 429    16899  20534  17582   -553  -1107  -1077       O  
ATOM   2290  CB  HIS A 429      63.213  36.328  83.361  1.00144.43           C  
ANISOU 2290  CB  HIS A 429    17006  20403  17466   -501  -1171   -361       C  
ATOM   2291  CG  HIS A 429      61.913  35.575  83.475  1.00145.57           C  
ANISOU 2291  CG  HIS A 429    17302  20608  17398   -473  -1143     -7       C  
ATOM   2292  ND1 HIS A 429      61.129  35.605  84.609  1.00150.53           N  
ANISOU 2292  ND1 HIS A 429    18043  21440  17709   -410  -1187    139       N  
ATOM   2293  CD2 HIS A 429      61.301  34.713  82.631  1.00142.28           C  
ANISOU 2293  CD2 HIS A 429    16925  20070  17062   -497  -1082    218       C  
ATOM   2294  CE1 HIS A 429      60.077  34.825  84.447  1.00146.95           C  
ANISOU 2294  CE1 HIS A 429    17679  20976  17178   -413  -1128    449       C  
ATOM   2295  NE2 HIS A 429      60.161  34.268  83.256  1.00141.19           N  
ANISOU 2295  NE2 HIS A 429    16900  20046  16697   -466  -1083    491       N  
ATOM   2296  N   MET A 430      65.368  38.581  82.546  1.00138.65           N  
ANISOU 2296  N   MET A 430    15954  19420  17308   -662   -955  -1109       N  
ATOM   2297  CA  MET A 430      66.581  39.334  82.859  1.00140.09           C  
ANISOU 2297  CA  MET A 430    15932  19560  17732   -696  -1013  -1478       C  
ATOM   2298  C   MET A 430      66.348  40.837  82.815  1.00136.78           C  
ANISOU 2298  C   MET A 430    15533  19079  17358   -780   -788  -1668       C  
ATOM   2299  O   MET A 430      66.806  41.578  83.692  1.00141.73           O  
ANISOU 2299  O   MET A 430    16066  19779  18004   -767   -907  -1939       O  
ATOM   2300  CB  MET A 430      67.679  39.021  81.846  1.00145.04           C  
ANISOU 2300  CB  MET A 430    16374  19983  18750   -760   -933  -1606       C  
ATOM   2301  CG  MET A 430      68.692  38.031  82.353  1.00151.51           C  
ANISOU 2301  CG  MET A 430    17020  20861  19685   -672  -1256  -1691       C  
ATOM   2302  SD  MET A 430      69.835  38.752  83.565  1.00164.41           S  
ANISOU 2302  SD  MET A 430    18421  22593  21452   -634  -1526  -2117       S  
ATOM   2303  CE  MET A 430      69.049  38.424  85.122  1.00164.20           C  
ANISOU 2303  CE  MET A 430    18592  22880  20915   -463  -1845  -1961       C  
ATOM   2304  N   TRP A 431      65.636  41.294  81.790  1.00134.32           N  
ANISOU 2304  N   TRP A 431    15348  18620  17067   -852   -477  -1536       N  
ATOM   2305  CA  TRP A 431      65.307  42.715  81.666  1.00136.53           C  
ANISOU 2305  CA  TRP A 431    15675  18807  17390   -923   -244  -1675       C  
ATOM   2306  C   TRP A 431      64.443  43.171  82.816  1.00136.22           C  
ANISOU 2306  C   TRP A 431    15748  18977  17030   -850   -352  -1669       C  
ATOM   2307  O   TRP A 431      64.510  44.318  83.217  1.00136.00           O  
ANISOU 2307  O   TRP A 431    15693  18924  17054   -880   -289  -1898       O  
ATOM   2308  CB  TRP A 431      64.611  43.012  80.368  1.00135.81           C  
ANISOU 2308  CB  TRP A 431    15738  18536  17327   -973     77  -1493       C  
ATOM   2309  CG  TRP A 431      65.471  42.876  79.194  1.00137.39           C  
ANISOU 2309  CG  TRP A 431    15850  18516  17835  -1045    259  -1539       C  
ATOM   2310  CD1 TRP A 431      66.832  42.996  79.146  1.00141.10           C  
ANISOU 2310  CD1 TRP A 431    16085  18880  18645  -1112    255  -1799       C  
ATOM   2311  CD2 TRP A 431      65.043  42.619  77.860  1.00131.82           C  
ANISOU 2311  CD2 TRP A 431    15286  17668  17130  -1048    488  -1336       C  
ATOM   2312  NE1 TRP A 431      67.275  42.816  77.867  1.00140.21           N  
ANISOU 2312  NE1 TRP A 431    15961  18570  18740  -1163    500  -1752       N  
ATOM   2313  CE2 TRP A 431      66.195  42.591  77.051  1.00133.15           C  
ANISOU 2313  CE2 TRP A 431    15314  17655  17621  -1115    642  -1469       C  
ATOM   2314  CE3 TRP A 431      63.796  42.412  77.269  1.00127.42           C  
ANISOU 2314  CE3 TRP A 431    14954  17123  16336   -989    572  -1069       C  
ATOM   2315  CZ2 TRP A 431      66.137  42.357  75.682  1.00129.92           C  
ANISOU 2315  CZ2 TRP A 431    15014  17090  17258  -1113    884  -1334       C  
ATOM   2316  CZ3 TRP A 431      63.731  42.187  75.917  1.00126.52           C  
ANISOU 2316  CZ3 TRP A 431    14941  16852  16277   -981    774   -952       C  
ATOM   2317  CH2 TRP A 431      64.899  42.161  75.130  1.00127.81           C  
ANISOU 2317  CH2 TRP A 431    14993  16849  16720  -1037    935  -1078       C  
ATOM   2318  N   THR A 432      63.637  42.264  83.352  1.00137.49           N  
ANISOU 2318  N   THR A 432    16032  19335  16872   -753   -502  -1410       N  
ATOM   2319  CA  THR A 432      62.834  42.576  84.530  1.00143.40           C  
ANISOU 2319  CA  THR A 432    16888  20313  17283   -666   -597  -1389       C  
ATOM   2320  C   THR A 432      63.709  42.595  85.782  1.00143.69           C  
ANISOU 2320  C   THR A 432    16813  20520  17261   -586   -894  -1639       C  
ATOM   2321  O   THR A 432      63.427  43.321  86.746  1.00142.86           O  
ANISOU 2321  O   THR A 432    16752  20566  16961   -525   -954  -1791       O  
ATOM   2322  CB  THR A 432      61.748  41.517  84.739  1.00148.40           C  
ANISOU 2322  CB  THR A 432    17671  21095  17616   -591   -644  -1017       C  
ATOM   2323  OG1 THR A 432      61.123  41.231  83.486  1.00152.21           O  
ANISOU 2323  OG1 THR A 432    18220  21411  18199   -650   -441   -806       O  
ATOM   2324  CG2 THR A 432      60.706  41.999  85.700  1.00151.30           C  
ANISOU 2324  CG2 THR A 432    18167  21666  17652   -519   -623   -967       C  
ATOM   2325  N   GLN A 433      64.765  41.783  85.768  1.00147.89           N  
ANISOU 2325  N   GLN A 433    17202  21031  17956   -568  -1095  -1695       N  
ATOM   2326  CA  GLN A 433      65.710  41.722  86.884  1.00155.29           C  
ANISOU 2326  CA  GLN A 433    18016  22118  18866   -470  -1424  -1952       C  
ATOM   2327  C   GLN A 433      66.635  42.912  86.941  1.00153.11           C  
ANISOU 2327  C   GLN A 433    17543  21725  18904   -542  -1414  -2396       C  
ATOM   2328  O   GLN A 433      66.841  43.481  88.005  1.00155.38           O  
ANISOU 2328  O   GLN A 433    17804  22164  19067   -460  -1605  -2651       O  
ATOM   2329  CB  GLN A 433      66.513  40.434  86.901  1.00163.71           C  
ANISOU 2329  CB  GLN A 433    18989  23200  20013   -402  -1673  -1870       C  
ATOM   2330  CG  GLN A 433      66.055  39.470  87.962  1.00170.81           C  
ANISOU 2330  CG  GLN A 433    20043  24352  20502   -232  -1925  -1624       C  
ATOM   2331  CD  GLN A 433      67.058  38.359  88.159  1.00178.62           C  
ANISOU 2331  CD  GLN A 433    20917  25351  21599   -137  -2231  -1623       C  
ATOM   2332  OE1 GLN A 433      68.211  38.579  88.564  1.00185.73           O  
ANISOU 2332  OE1 GLN A 433    21626  26261  22682    -89  -2465  -1957       O  
ATOM   2333  NE2 GLN A 433      66.637  37.152  87.839  1.00183.04           N  
ANISOU 2333  NE2 GLN A 433    21574  25888  22084   -109  -2238  -1262       N  
ATOM   2334  N   ASP A 434      67.190  43.285  85.786  1.00153.32           N  
ANISOU 2334  N   ASP A 434    17435  21475  19344   -693  -1180  -2492       N  
ATOM   2335  CA  ASP A 434      68.025  44.481  85.671  1.00156.79           C  
ANISOU 2335  CA  ASP A 434    17673  21737  20160   -800  -1090  -2892       C  
ATOM   2336  C   ASP A 434      67.280  45.532  84.831  1.00152.20           C  
ANISOU 2336  C   ASP A 434    17210  20957  19660   -921   -692  -2829       C  
ATOM   2337  O   ASP A 434      67.517  45.644  83.628  1.00149.90           O  
ANISOU 2337  O   ASP A 434    16886  20421  19648  -1039   -414  -2763       O  
ATOM   2338  CB  ASP A 434      69.358  44.099  85.041  1.00163.84           C  
ANISOU 2338  CB  ASP A 434    18300  22453  21499   -875  -1112  -3059       C  
ATOM   2339  CG  ASP A 434      70.071  42.994  85.818  1.00168.51           C  
ANISOU 2339  CG  ASP A 434    18781  23229  22017   -732  -1526  -3101       C  
ATOM   2340  OD1 ASP A 434      70.930  42.329  85.220  1.00173.63           O  
ANISOU 2340  OD1 ASP A 434    19254  23759  22955   -762  -1548  -3126       O  
ATOM   2341  OD2 ASP A 434      69.764  42.774  87.012  1.00166.76           O  
ANISOU 2341  OD2 ASP A 434    18659  23267  21435   -575  -1822  -3100       O  
ATOM   2342  N   PRO A 435      66.386  46.312  85.469  1.00153.91           N  
ANISOU 2342  N   PRO A 435    17574  21279  19623   -876   -664  -2853       N  
ATOM   2343  CA  PRO A 435      65.529  47.262  84.783  1.00157.15           C  
ANISOU 2343  CA  PRO A 435    18127  21525  20057   -952   -325  -2766       C  
ATOM   2344  C   PRO A 435      66.291  48.473  84.299  1.00158.14           C  
ANISOU 2344  C   PRO A 435    18094  21355  20635  -1094   -121  -3073       C  
ATOM   2345  O   PRO A 435      65.955  49.038  83.236  1.00162.79           O  
ANISOU 2345  O   PRO A 435    18771  21701  21378  -1187    219  -2951       O  
ATOM   2346  CB  PRO A 435      64.494  47.625  85.847  1.00156.60           C  
ANISOU 2346  CB  PRO A 435    18220  21696  19585   -833   -423  -2751       C  
ATOM   2347  CG  PRO A 435      64.593  46.548  86.867  1.00154.92           C  
ANISOU 2347  CG  PRO A 435    18017  21784  19059   -690   -762  -2680       C  
ATOM   2348  CD  PRO A 435      66.056  46.292  86.896  1.00156.44           C  
ANISOU 2348  CD  PRO A 435    17961  21901  19578   -723   -953  -2943       C  
ATOM   2349  N   GLN A 436      67.318  48.854  85.057  1.00157.95           N  
ANISOU 2349  N   GLN A 436    17839  21341  20834  -1105   -329  -3466       N  
ATOM   2350  CA  GLN A 436      68.095  50.069  84.747  1.00163.81           C  
ANISOU 2350  CA  GLN A 436    18389  21786  22065  -1253   -149  -3808       C  
ATOM   2351  C   GLN A 436      68.777  49.996  83.384  1.00167.16           C  
ANISOU 2351  C   GLN A 436    18712  21902  22899  -1408    164  -3724       C  
ATOM   2352  O   GLN A 436      69.417  48.985  83.035  1.00171.06           O  
ANISOU 2352  O   GLN A 436    19099  22425  23471  -1405     85  -3645       O  
ATOM   2353  CB  GLN A 436      69.085  50.386  85.858  1.00170.32           C  
ANISOU 2353  CB  GLN A 436    18952  22691  23068  -1224   -481  -4277       C  
ATOM   2354  CG  GLN A 436      68.468  51.206  86.969  1.00175.94           C  
ANISOU 2354  CG  GLN A 436    19757  23561  23532  -1125   -630  -4484       C  
ATOM   2355  CD  GLN A 436      68.199  52.650  86.559  1.00181.37           C  
ANISOU 2355  CD  GLN A 436    20456  23954  24502  -1249   -316  -4634       C  
ATOM   2356  OE1 GLN A 436      68.875  53.211  85.695  1.00188.40           O  
ANISOU 2356  OE1 GLN A 436    21193  24501  25889  -1423    -52  -4732       O  
ATOM   2357  NE2 GLN A 436      67.198  53.261  87.183  1.00180.85           N  
ANISOU 2357  NE2 GLN A 436    20576  24011  24125  -1153   -328  -4646       N  
ATOM   2358  N   ASP A 437      68.615  51.079  82.618  1.00170.68           N  
ANISOU 2358  N   ASP A 437    19206  22050  23594  -1529    534  -3733       N  
ATOM   2359  CA  ASP A 437      69.213  51.198  81.292  1.00174.62           C  
ANISOU 2359  CA  ASP A 437    19645  22232  24468  -1673    902  -3645       C  
ATOM   2360  C   ASP A 437      70.723  51.247  81.418  1.00178.42           C  
ANISOU 2360  C   ASP A 437    19749  22583  25458  -1784    840  -4007       C  
ATOM   2361  O   ASP A 437      71.452  50.811  80.515  1.00185.96           O  
ANISOU 2361  O   ASP A 437    20589  23384  26680  -1866   1034  -3943       O  
ATOM   2362  CB  ASP A 437      68.715  52.471  80.601  1.00177.09           C  
ANISOU 2362  CB  ASP A 437    20106  22246  24931  -1761   1297  -3591       C  
ATOM   2363  CG  ASP A 437      67.212  52.447  80.307  1.00175.38           C  
ANISOU 2363  CG  ASP A 437    20251  22127  24255  -1645   1383  -3229       C  
ATOM   2364  OD1 ASP A 437      66.601  51.357  80.294  1.00178.00           O  
ANISOU 2364  OD1 ASP A 437    20718  22702  24209  -1531   1230  -2963       O  
ATOM   2365  OD2 ASP A 437      66.637  53.536  80.084  1.00174.99           O  
ANISOU 2365  OD2 ASP A 437    20339  21895  24255  -1668   1604  -3220       O  
ATOM   2366  N   SER A 438      71.186  51.779  82.548  1.00176.73           N  
ANISOU 2366  N   SER A 438    19333  22435  25382  -1775    564  -4408       N  
ATOM   2367  CA  SER A 438      72.614  51.830  82.854  1.00182.87           C  
ANISOU 2367  CA  SER A 438    19708  23116  26656  -1860    423  -4817       C  
ATOM   2368  C   SER A 438      73.203  50.434  82.972  1.00187.03           C  
ANISOU 2368  C   SER A 438    20114  23853  27093  -1768    142  -4762       C  
ATOM   2369  O   SER A 438      74.404  50.246  82.725  1.00196.94           O  
ANISOU 2369  O   SER A 438    21047  24976  28805  -1854    143  -4988       O  
ATOM   2370  CB  SER A 438      72.853  52.625  84.141  1.00185.16           C  
ANISOU 2370  CB  SER A 438    19836  23481  27035  -1825    108  -5273       C  
ATOM   2371  OG  SER A 438      72.265  52.000  85.263  1.00183.24           O  
ANISOU 2371  OG  SER A 438    19738  23636  26248  -1611   -316  -5243       O  
ATOM   2372  N   GLN A 439      72.359  49.471  83.355  1.00183.30           N  
ANISOU 2372  N   GLN A 439    19890  23691  26063  -1593    -88  -4466       N  
ATOM   2373  CA  GLN A 439      72.775  48.068  83.485  1.00180.46           C  
ANISOU 2373  CA  GLN A 439    19465  23529  25571  -1483   -365  -4358       C  
ATOM   2374  C   GLN A 439      72.787  47.399  82.129  1.00175.36           C  
ANISOU 2374  C   GLN A 439    18890  22736  25003  -1547    -48  -4039       C  
ATOM   2375  O   GLN A 439      73.111  46.211  82.040  1.00170.44           O  
ANISOU 2375  O   GLN A 439    18220  22229  24307  -1466   -224  -3924       O  
ATOM   2376  CB  GLN A 439      71.832  47.250  84.398  1.00180.21           C  
ANISOU 2376  CB  GLN A 439    19686  23862  24923  -1276   -703  -4129       C  
ATOM   2377  CG  GLN A 439      71.714  47.690  85.847  1.00184.26           C  
ANISOU 2377  CG  GLN A 439    20191  24601  25217  -1152  -1061  -4400       C  
ATOM   2378  CD  GLN A 439      70.640  46.902  86.597  1.00185.59           C  
ANISOU 2378  CD  GLN A 439    20658  25107  24751   -958  -1282  -4090       C  
ATOM   2379  OE1 GLN A 439      69.443  47.166  86.470  1.00187.36           O  
ANISOU 2379  OE1 GLN A 439    21148  25374  24665   -947  -1093  -3834       O  
ATOM   2380  NE2 GLN A 439      71.071  45.918  87.375  1.00187.81           N  
ANISOU 2380  NE2 GLN A 439    20889  25618  24852   -801  -1674  -4107       N  
ATOM   2381  N   TRP A 440      72.460  48.158  81.083  1.00179.22           N  
ANISOU 2381  N   TRP A 440    19495  22964  25634  -1676    408  -3906       N  
ATOM   2382  CA  TRP A 440      72.520  47.658  79.717  1.00186.51           C  
ANISOU 2382  CA  TRP A 440    20497  23730  26635  -1728    745  -3634       C  
ATOM   2383  C   TRP A 440      73.223  48.683  78.815  1.00193.35           C  
ANISOU 2383  C   TRP A 440    21223  24228  28010  -1919   1199  -3774       C  
ATOM   2384  O   TRP A 440      72.750  48.985  77.722  1.00202.56           O  
ANISOU 2384  O   TRP A 440    22608  25219  29134  -1965   1597  -3513       O  
ATOM   2385  CB  TRP A 440      71.115  47.310  79.180  1.00183.96           C  
ANISOU 2385  CB  TRP A 440    20574  23497  25826  -1639    862  -3194       C  
ATOM   2386  CG  TRP A 440      70.410  46.288  80.011  1.00182.00           C  
ANISOU 2386  CG  TRP A 440    20454  23577  25121  -1472    472  -3029       C  
ATOM   2387  CD1 TRP A 440      69.483  46.522  80.980  1.00185.38           C  
ANISOU 2387  CD1 TRP A 440    21038  24207  25187  -1379    273  -2991       C  
ATOM   2388  CD2 TRP A 440      70.596  44.870  79.972  1.00179.56           C  
ANISOU 2388  CD2 TRP A 440    20123  23417  24683  -1375    252  -2880       C  
ATOM   2389  NE1 TRP A 440      69.059  45.340  81.538  1.00186.51           N  
ANISOU 2389  NE1 TRP A 440    21269  24615  24979  -1239    -31  -2801       N  
ATOM   2390  CE2 TRP A 440      69.733  44.310  80.941  1.00182.55           C  
ANISOU 2390  CE2 TRP A 440    20660  24076  24623  -1235    -62  -2730       C  
ATOM   2391  CE3 TRP A 440      71.396  44.015  79.208  1.00179.07           C  
ANISOU 2391  CE3 TRP A 440    19924  23271  24842  -1390    304  -2856       C  
ATOM   2392  CZ2 TRP A 440      69.658  42.933  81.172  1.00182.41           C  
ANISOU 2392  CZ2 TRP A 440    20672  24232  24402  -1117   -326  -2543       C  
ATOM   2393  CZ3 TRP A 440      71.324  42.647  79.448  1.00182.25           C  
ANISOU 2393  CZ3 TRP A 440    20349  23854  25041  -1263     14  -2697       C  
ATOM   2394  CH2 TRP A 440      70.452  42.122  80.410  1.00183.64           C  
ANISOU 2394  CH2 TRP A 440    20691  24284  24797  -1134   -293  -2531       C  
ATOM   2395  N   ASP A 441      74.353  49.211  79.287  1.00191.82           N  
ANISOU 2395  N   ASP A 441    20664  23914  28302  -2023   1136  -4187       N  
ATOM   2396  CA  ASP A 441      75.137  50.104  78.455  1.00196.16           C  
ANISOU 2396  CA  ASP A 441    21035  24094  29402  -2221   1586  -4326       C  
ATOM   2397  C   ASP A 441      75.970  49.264  77.495  1.00197.84           C  
ANISOU 2397  C   ASP A 441    21102  24225  29844  -2257   1781  -4252       C  
ATOM   2398  O   ASP A 441      76.529  48.248  77.880  1.00200.64           O  
ANISOU 2398  O   ASP A 441    21270  24760  30204  -2173   1458  -4351       O  
ATOM   2399  CB  ASP A 441      76.036  51.021  79.255  1.00201.08           C  
ANISOU 2399  CB  ASP A 441    21289  24582  30529  -2337   1473  -4819       C  
ATOM   2400  CG  ASP A 441      76.588  52.149  78.400  1.00206.97           C  
ANISOU 2400  CG  ASP A 441    21909  24899  31829  -2560   2007  -4909       C  
ATOM   2401  OD1 ASP A 441      77.576  51.934  77.663  1.00204.53           O  
ANISOU 2401  OD1 ASP A 441    21358  24405  31946  -2673   2271  -4971       O  
ATOM   2402  OD2 ASP A 441      76.010  53.245  78.432  1.00215.34           O  
ANISOU 2402  OD2 ASP A 441    23125  25795  32899  -2619   2190  -4897       O  
ATOM   2403  N   PRO A 442      76.030  49.673  76.222  1.00198.92           N  
ANISOU 2403  N   PRO A 442    21344  24087  30146  -2365   2318  -4063       N  
ATOM   2404  CA  PRO A 442      76.906  49.099  75.206  1.00199.68           C  
ANISOU 2404  CA  PRO A 442    21290  24055  30523  -2420   2609  -4026       C  
ATOM   2405  C   PRO A 442      78.330  48.798  75.679  1.00201.50           C  
ANISOU 2405  C   PRO A 442    21008  24262  31288  -2489   2432  -4441       C  
ATOM   2406  O   PRO A 442      78.858  47.735  75.368  1.00206.21           O  
ANISOU 2406  O   PRO A 442    21482  24955  31913  -2423   2351  -4424       O  
ATOM   2407  CB  PRO A 442      76.938  50.200  74.150  1.00200.39           C  
ANISOU 2407  CB  PRO A 442    21491  23782  30864  -2574   3230  -3910       C  
ATOM   2408  CG  PRO A 442      75.544  50.723  74.183  1.00198.32           C  
ANISOU 2408  CG  PRO A 442    21659  23566  30125  -2491   3236  -3632       C  
ATOM   2409  CD  PRO A 442      75.132  50.685  75.621  1.00197.77           C  
ANISOU 2409  CD  PRO A 442    21531  23753  29859  -2408   2693  -3825       C  
ATOM   2410  N   ARG A 443      78.927  49.716  76.426  1.00200.70           N  
ANISOU 2410  N   ARG A 443    20604  24033  31619  -2610   2352  -4828       N  
ATOM   2411  CA  ARG A 443      80.277  49.507  76.961  1.00205.56           C  
ANISOU 2411  CA  ARG A 443    20696  24624  32781  -2668   2134  -5277       C  
ATOM   2412  C   ARG A 443      80.375  48.304  77.899  1.00198.66           C  
ANISOU 2412  C   ARG A 443    19737  24112  31633  -2463   1504  -5370       C  
ATOM   2413  O   ARG A 443      81.462  47.776  78.112  1.00198.48           O  
ANISOU 2413  O   ARG A 443    19322  24103  31987  -2458   1317  -5658       O  
ATOM   2414  CB  ARG A 443      80.793  50.763  77.646  1.00213.76           C  
ANISOU 2414  CB  ARG A 443    21437  25457  34323  -2825   2121  -5699       C  
ATOM   2415  CG  ARG A 443      81.174  51.827  76.651  1.00218.43           C  
ANISOU 2415  CG  ARG A 443    21961  25619  35412  -3062   2782  -5682       C  
ATOM   2416  CD  ARG A 443      81.525  53.154  77.298  1.00220.97           C  
ANISOU 2416  CD  ARG A 443    22030  25697  36230  -3226   2792  -6073       C  
ATOM   2417  NE  ARG A 443      81.248  54.234  76.353  1.00223.16           N  
ANISOU 2417  NE  ARG A 443    22494  25594  36700  -3398   3430  -5859       N  
ATOM   2418  CZ  ARG A 443      80.030  54.628  75.944  1.00223.76           C  
ANISOU 2418  CZ  ARG A 443    23072  25658  36286  -3336   3628  -5459       C  
ATOM   2419  NH1 ARG A 443      78.907  54.064  76.392  1.00219.30           N  
ANISOU 2419  NH1 ARG A 443    22868  25439  35015  -3122   3261  -5227       N  
ATOM   2420  NH2 ARG A 443      79.933  55.615  75.054  1.00226.00           N  
ANISOU 2420  NH2 ARG A 443    23496  25562  36810  -3489   4219  -5280       N  
ATOM   2421  N   ASN A 444      79.237  47.883  78.438  1.00193.73           N  
ANISOU 2421  N   ASN A 444    19476  23763  30369  -2290   1196  -5117       N  
ATOM   2422  CA  ASN A 444      79.186  46.701  79.291  1.00197.24           C  
ANISOU 2422  CA  ASN A 444    19916  24543  30482  -2080    635  -5118       C  
ATOM   2423  C   ASN A 444      78.588  45.524  78.534  1.00197.70           C  
ANISOU 2423  C   ASN A 444    20263  24722  30130  -1964    699  -4686       C  
ATOM   2424  O   ASN A 444      77.905  44.707  79.141  1.00196.45           O  
ANISOU 2424  O   ASN A 444    20311  24834  29495  -1788    328  -4503       O  
ATOM   2425  CB  ASN A 444      78.275  46.937  80.522  1.00201.40           C  
ANISOU 2425  CB  ASN A 444    20660  25320  30542  -1950    228  -5118       C  
ATOM   2426  CG  ASN A 444      78.337  48.340  81.063  1.00208.03           C  
ANISOU 2426  CG  ASN A 444    21391  26016  31635  -2066    279  -5430       C  
ATOM   2427  OD1 ASN A 444      79.312  49.054  80.856  1.00220.92           O  
ANISOU 2427  OD1 ASN A 444    22675  27388  33876  -2233    467  -5761       O  
ATOM   2428  ND2 ASN A 444      77.282  48.742  81.769  1.00206.88           N  
ANISOU 2428  ND2 ASN A 444    21534  26031  31040  -1977    118  -5334       N  
ATOM   2429  N   LEU A 445      78.829  45.458  77.225  1.00198.98           N  
ANISOU 2429  N   LEU A 445    20447  24678  30476  -2057   1176  -4529       N  
ATOM   2430  CA  LEU A 445      78.212  44.411  76.412  1.00193.59           C  
ANISOU 2430  CA  LEU A 445    20055  24090  29407  -1944   1258  -4139       C  
ATOM   2431  C   LEU A 445      78.573  43.018  76.910  1.00187.06           C  
ANISOU 2431  C   LEU A 445    19104  23485  28483  -1777    801  -4167       C  
ATOM   2432  O   LEU A 445      77.698  42.259  77.340  1.00178.03           O  
ANISOU 2432  O   LEU A 445    18221  22566  26856  -1623    497  -3923       O  
ATOM   2433  CB  LEU A 445      78.634  44.547  74.947  1.00198.42           C  
ANISOU 2433  CB  LEU A 445    20665  24450  30276  -2053   1833  -4035       C  
ATOM   2434  CG  LEU A 445      78.080  43.540  73.942  1.00197.39           C  
ANISOU 2434  CG  LEU A 445    20823  24384  29789  -1936   1963  -3676       C  
ATOM   2435  CD1 LEU A 445      76.562  43.659  73.806  1.00194.29           C  
ANISOU 2435  CD1 LEU A 445    20909  24091  28822  -1854   1968  -3308       C  
ATOM   2436  CD2 LEU A 445      78.768  43.807  72.605  1.00200.57           C  
ANISOU 2436  CD2 LEU A 445    21155  24530  30520  -2045   2542  -3667       C  
ATOM   2437  N   SER A 446      79.878  42.720  76.881  1.00188.26           N  
ANISOU 2437  N   SER A 446    18841  23557  29130  -1809    757  -4476       N  
ATOM   2438  CA  SER A 446      80.428  41.416  77.225  1.00190.57           C  
ANISOU 2438  CA  SER A 446    18963  24006  29435  -1651    360  -4538       C  
ATOM   2439  C   SER A 446      79.902  40.889  78.559  1.00189.85           C  
ANISOU 2439  C   SER A 446    18991  24201  28943  -1469   -235  -4504       C  
ATOM   2440  O   SER A 446      79.508  39.722  78.697  1.00194.40           O  
ANISOU 2440  O   SER A 446    19728  24942  29194  -1304   -504  -4275       O  
ATOM   2441  CB  SER A 446      81.955  41.502  77.302  1.00195.83           C  
ANISOU 2441  CB  SER A 446    19098  24542  30765  -1721    341  -4981       C  
ATOM   2442  OG  SER A 446      82.498  42.108  76.141  1.00204.36           O  
ANISOU 2442  OG  SER A 446    20045  25344  32256  -1907    938  -5030       O  
ATOM   2443  N   SER A 447      79.938  41.763  79.556  1.00190.75           N  
ANISOU 2443  N   SER A 447    19015  24361  29099  -1497   -435  -4747       N  
ATOM   2444  CA  SER A 447      79.475  41.394  80.891  1.00195.26           C  
ANISOU 2444  CA  SER A 447    19707  25212  29269  -1315   -978  -4738       C  
ATOM   2445  C   SER A 447      77.980  41.153  80.880  1.00189.71           C  
ANISOU 2445  C   SER A 447    19485  24652  27942  -1244   -943  -4289       C  
ATOM   2446  O   SER A 447      77.513  40.159  81.445  1.00193.00           O  
ANISOU 2446  O   SER A 447    20070  25280  27978  -1068  -1287  -4082       O  
ATOM   2447  CB  SER A 447      79.871  42.464  81.907  1.00202.14           C  
ANISOU 2447  CB  SER A 447    20373  26096  30334  -1354  -1178  -5140       C  
ATOM   2448  OG  SER A 447      79.800  43.743  81.320  1.00203.90           O  
ANISOU 2448  OG  SER A 447    20574  26076  30821  -1570   -718  -5225       O  
ATOM   2449  N   CYS A 448      77.235  42.045  80.227  1.00182.05           N  
ANISOU 2449  N   CYS A 448    18728  23552  26888  -1377   -525  -4134       N  
ATOM   2450  CA  CYS A 448      75.781  41.910  80.123  1.00177.20           C  
ANISOU 2450  CA  CYS A 448    18546  23051  25729  -1320   -458  -3729       C  
ATOM   2451  C   CYS A 448      75.443  40.569  79.517  1.00165.06           C  
ANISOU 2451  C   CYS A 448    17161  21573  23978  -1217   -491  -3406       C  
ATOM   2452  O   CYS A 448      74.639  39.797  80.092  1.00156.81           O  
ANISOU 2452  O   CYS A 448    16334  20731  22513  -1078   -768  -3162       O  
ATOM   2453  CB  CYS A 448      75.169  42.983  79.211  1.00183.51           C  
ANISOU 2453  CB  CYS A 448    19529  23651  26545  -1470     43  -3606       C  
ATOM   2454  SG  CYS A 448      74.954  44.611  79.954  1.00208.50           S  
ANISOU 2454  SG  CYS A 448    22676  26756  29788  -1569     97  -3855       S  
ATOM   2455  N   PHE A 449      76.050  40.283  78.363  1.00161.57           N  
ANISOU 2455  N   PHE A 449    16606  20950  23833  -1284   -197  -3409       N  
ATOM   2456  CA  PHE A 449      75.844  39.001  77.685  1.00159.48           C  
ANISOU 2456  CA  PHE A 449    16456  20712  23426  -1185   -219  -3154       C  
ATOM   2457  C   PHE A 449      76.175  37.832  78.607  1.00155.43           C  
ANISOU 2457  C   PHE A 449    15838  20379  22837  -1017   -729  -3177       C  
ATOM   2458  O   PHE A 449      75.550  36.760  78.519  1.00152.87           O  
ANISOU 2458  O   PHE A 449    15708  20143  22229   -901   -876  -2893       O  
ATOM   2459  CB  PHE A 449      76.736  38.922  76.446  1.00163.40           C  
ANISOU 2459  CB  PHE A 449    16769  20994  24320  -1268    146  -3256       C  
ATOM   2460  CG  PHE A 449      76.539  37.674  75.619  1.00164.45           C  
ANISOU 2460  CG  PHE A 449    17023  21133  24325  -1165    161  -3029       C  
ATOM   2461  CD1 PHE A 449      75.304  37.411  75.013  1.00167.42           C  
ANISOU 2461  CD1 PHE A 449    17774  21538  24297  -1122    286  -2678       C  
ATOM   2462  CD2 PHE A 449      77.573  36.769  75.430  1.00161.82           C  
ANISOU 2462  CD2 PHE A 449    16419  20769  24295  -1103     42  -3187       C  
ATOM   2463  CE1 PHE A 449      75.116  36.263  74.237  1.00164.26           C  
ANISOU 2463  CE1 PHE A 449    17477  21133  23801  -1023    283  -2503       C  
ATOM   2464  CE2 PHE A 449      77.390  35.635  74.655  1.00161.89           C  
ANISOU 2464  CE2 PHE A 449    16538  20770  24202  -1002     56  -3003       C  
ATOM   2465  CZ  PHE A 449      76.172  35.376  74.060  1.00162.15           C  
ANISOU 2465  CZ  PHE A 449    16945  20828  23837   -964    171  -2668       C  
ATOM   2466  N   ASP A 450      77.167  38.019  79.470  1.00156.42           N  
ANISOU 2466  N   ASP A 450    15655  20543  23234   -994  -1005  -3518       N  
ATOM   2467  CA  ASP A 450      77.536  36.950  80.386  1.00161.85           C  
ANISOU 2467  CA  ASP A 450    16254  21398  23843   -808  -1512  -3545       C  
ATOM   2468  C   ASP A 450      76.448  36.783  81.419  1.00163.22           C  
ANISOU 2468  C   ASP A 450    16734  21798  23484   -690  -1795  -3304       C  
ATOM   2469  O   ASP A 450      76.054  35.659  81.728  1.00169.21           O  
ANISOU 2469  O   ASP A 450    17640  22670  23980   -543  -2049  -3053       O  
ATOM   2470  CB  ASP A 450      78.876  37.227  81.038  1.00166.44           C  
ANISOU 2470  CB  ASP A 450    16421  21966  24850   -792  -1761  -3997       C  
ATOM   2471  CG  ASP A 450      79.498  35.976  81.565  1.00167.80           C  
ANISOU 2471  CG  ASP A 450    16457  22239  25058   -593  -2211  -4030       C  
ATOM   2472  OD1 ASP A 450      79.606  35.875  82.795  1.00175.72           O  
ANISOU 2472  OD1 ASP A 450    17445  23423  25898   -446  -2659  -4131       O  
ATOM   2473  OD2 ASP A 450      79.836  35.078  80.754  1.00161.78           O  
ANISOU 2473  OD2 ASP A 450    15628  21378  24460   -564  -2125  -3944       O  
ATOM   2474  N   LYS A 451      75.944  37.905  81.931  1.00163.54           N  
ANISOU 2474  N   LYS A 451    16871  21891  23376   -757  -1724  -3373       N  
ATOM   2475  CA  LYS A 451      74.912  37.888  82.965  1.00168.01           C  
ANISOU 2475  CA  LYS A 451    17717  22684  23435   -648  -1953  -3175       C  
ATOM   2476  C   LYS A 451      73.758  37.026  82.495  1.00163.51           C  
ANISOU 2476  C   LYS A 451    17465  22150  22510   -606  -1857  -2715       C  
ATOM   2477  O   LYS A 451      73.461  35.987  83.105  1.00163.46           O  
ANISOU 2477  O   LYS A 451    17575  22286  22244   -453  -2157  -2505       O  
ATOM   2478  CB  LYS A 451      74.446  39.314  83.316  1.00178.12           C  
ANISOU 2478  CB  LYS A 451    19066  23972  24640   -748  -1789  -3313       C  
ATOM   2479  CG  LYS A 451      73.652  39.400  84.618  1.00191.62           C  
ANISOU 2479  CG  LYS A 451    20990  25944  25871   -611  -2077  -3226       C  
ATOM   2480  CD  LYS A 451      73.736  40.792  85.271  1.00205.03           C  
ANISOU 2480  CD  LYS A 451    22616  27661  27623   -667  -2069  -3556       C  
ATOM   2481  CE  LYS A 451      73.220  40.784  86.711  1.00212.91           C  
ANISOU 2481  CE  LYS A 451    23782  28953  28158   -487  -2425  -3551       C  
ATOM   2482  NZ  LYS A 451      73.416  42.093  87.382  1.00215.03           N  
ANISOU 2482  NZ  LYS A 451    23953  29240  28507   -520  -2465  -3934       N  
ATOM   2483  N   LEU A 452      73.156  37.437  81.380  1.00162.26           N  
ANISOU 2483  N   LEU A 452    17438  21845  22368   -736  -1442  -2568       N  
ATOM   2484  CA  LEU A 452      72.131  36.652  80.704  1.00158.57           C  
ANISOU 2484  CA  LEU A 452    17230  21369  21648   -710  -1323  -2182       C  
ATOM   2485  C   LEU A 452      72.552  35.187  80.617  1.00154.90           C  
ANISOU 2485  C   LEU A 452    16701  20909  21244   -592  -1564  -2075       C  
ATOM   2486  O   LEU A 452      71.817  34.293  81.080  1.00149.57           O  
ANISOU 2486  O   LEU A 452    16207  20347  20273   -486  -1767  -1792       O  
ATOM   2487  CB  LEU A 452      71.941  37.201  79.290  1.00158.17           C  
ANISOU 2487  CB  LEU A 452    17234  21113  21748   -844   -865  -2146       C  
ATOM   2488  CG  LEU A 452      71.033  36.440  78.331  1.00156.13           C  
ANISOU 2488  CG  LEU A 452    17206  20808  21306   -818   -720  -1818       C  
ATOM   2489  CD1 LEU A 452      69.597  36.432  78.821  1.00154.06           C  
ANISOU 2489  CD1 LEU A 452    17222  20685  20626   -777   -779  -1535       C  
ATOM   2490  CD2 LEU A 452      71.144  37.046  76.952  1.00155.86           C  
ANISOU 2490  CD2 LEU A 452    17197  20572  21448   -921   -288  -1851       C  
ATOM   2491  N   LEU A 453      73.740  34.961  80.046  1.00158.67           N  
ANISOU 2491  N   LEU A 453    16909  21250  22125   -613  -1531  -2306       N  
ATOM   2492  CA  LEU A 453      74.248  33.601  79.869  1.00166.01           C  
ANISOU 2492  CA  LEU A 453    17748  22153  23173   -496  -1746  -2245       C  
ATOM   2493  C   LEU A 453      74.158  32.860  81.185  1.00165.88           C  
ANISOU 2493  C   LEU A 453    17781  22320  22925   -327  -2210  -2146       C  
ATOM   2494  O   LEU A 453      73.531  31.797  81.279  1.00153.52           O  
ANISOU 2494  O   LEU A 453    16390  20789  21149   -231  -2353  -1842       O  
ATOM   2495  CB  LEU A 453      75.694  33.586  79.368  1.00176.69           C  
ANISOU 2495  CB  LEU A 453    18743  23366  25022   -523  -1699  -2584       C  
ATOM   2496  CG  LEU A 453      75.908  32.692  78.159  1.00182.32           C  
ANISOU 2496  CG  LEU A 453    19432  23932  25907   -510  -1530  -2502       C  
ATOM   2497  CD1 LEU A 453      75.359  33.369  76.912  1.00181.65           C  
ANISOU 2497  CD1 LEU A 453    19504  23720  25794   -646  -1035  -2414       C  
ATOM   2498  CD2 LEU A 453      77.385  32.411  77.994  1.00188.64           C  
ANISOU 2498  CD2 LEU A 453    19850  24640  27183   -484  -1601  -2834       C  
ATOM   2499  N   ALA A 454      74.748  33.458  82.214  1.00176.23           N  
ANISOU 2499  N   ALA A 454    18950  23744  24266   -287  -2438  -2401       N  
ATOM   2500  CA  ALA A 454      74.727  32.875  83.555  1.00180.44           C  
ANISOU 2500  CA  ALA A 454    19550  24473  24535    -97  -2890  -2329       C  
ATOM   2501  C   ALA A 454      73.310  32.514  83.929  1.00179.43           C  
ANISOU 2501  C   ALA A 454    19784  24464  23925    -58  -2878  -1909       C  
ATOM   2502  O   ALA A 454      73.029  31.353  84.223  1.00182.69           O  
ANISOU 2502  O   ALA A 454    20317  24911  24183     69  -3087  -1639       O  
ATOM   2503  CB  ALA A 454      75.323  33.831  84.592  1.00183.65           C  
ANISOU 2503  CB  ALA A 454    19809  25006  24963    -65  -3096  -2675       C  
ATOM   2504  N   PHE A 455      72.418  33.507  83.865  1.00173.17           N  
ANISOU 2504  N   PHE A 455    19152  23711  22933   -172  -2613  -1856       N  
ATOM   2505  CA  PHE A 455      71.016  33.318  84.206  1.00163.17           C  
ANISOU 2505  CA  PHE A 455    18200  22557  21237   -151  -2556  -1487       C  
ATOM   2506  C   PHE A 455      70.467  32.082  83.516  1.00151.93           C  
ANISOU 2506  C   PHE A 455    16892  21032  19799   -133  -2516  -1151       C  
ATOM   2507  O   PHE A 455      69.882  31.204  84.184  1.00141.14           O  
ANISOU 2507  O   PHE A 455    15691  19758  18174    -23  -2704   -856       O  
ATOM   2508  CB  PHE A 455      70.175  34.553  83.853  1.00161.81           C  
ANISOU 2508  CB  PHE A 455    18146  22377  20957   -296  -2210  -1499       C  
ATOM   2509  CG  PHE A 455      68.715  34.415  84.175  1.00162.90           C  
ANISOU 2509  CG  PHE A 455    18573  22630  20692   -279  -2133  -1148       C  
ATOM   2510  CD1 PHE A 455      68.308  34.266  85.483  1.00175.00           C  
ANISOU 2510  CD1 PHE A 455    20239  24383  21868   -153  -2361  -1035       C  
ATOM   2511  CD2 PHE A 455      67.745  34.459  83.179  1.00157.39           C  
ANISOU 2511  CD2 PHE A 455    18010  21822  19968   -379  -1828   -942       C  
ATOM   2512  CE1 PHE A 455      66.951  34.153  85.804  1.00178.01           C  
ANISOU 2512  CE1 PHE A 455    20865  24869  21899   -144  -2253   -714       C  
ATOM   2513  CE2 PHE A 455      66.405  34.334  83.487  1.00160.36           C  
ANISOU 2513  CE2 PHE A 455    18611  22297  20019   -366  -1760   -644       C  
ATOM   2514  CZ  PHE A 455      66.008  34.177  84.801  1.00168.51           C  
ANISOU 2514  CZ  PHE A 455    19756  23544  20726   -258  -1956   -526       C  
ATOM   2515  N   PHE A 456      70.694  32.005  82.202  1.00151.98           N  
ANISOU 2515  N   PHE A 456    16811  20842  20092   -233  -2271  -1204       N  
ATOM   2516  CA  PHE A 456      70.116  30.930  81.405  1.00155.57           C  
ANISOU 2516  CA  PHE A 456    17374  21182  20553   -224  -2209   -929       C  
ATOM   2517  C   PHE A 456      70.560  29.580  81.951  1.00157.14           C  
ANISOU 2517  C   PHE A 456    17532  21385  20787    -69  -2562   -812       C  
ATOM   2518  O   PHE A 456      69.747  28.654  82.113  1.00155.89           O  
ANISOU 2518  O   PHE A 456    17544  21225  20461    -16  -2643   -485       O  
ATOM   2519  CB  PHE A 456      70.556  31.071  79.944  1.00158.92           C  
ANISOU 2519  CB  PHE A 456    17686  21408  21288   -319  -1924  -1076       C  
ATOM   2520  CG  PHE A 456      69.686  30.309  78.983  1.00154.42           C  
ANISOU 2520  CG  PHE A 456    17274  20730  20669   -329  -1790   -823       C  
ATOM   2521  CD1 PHE A 456      68.617  30.931  78.356  1.00146.93           C  
ANISOU 2521  CD1 PHE A 456    16507  19763  19554   -415  -1510   -702       C  
ATOM   2522  CD2 PHE A 456      69.953  28.983  78.681  1.00154.83           C  
ANISOU 2522  CD2 PHE A 456    17280  20686  20862   -240  -1960   -732       C  
ATOM   2523  CE1 PHE A 456      67.817  30.241  77.455  1.00143.24           C  
ANISOU 2523  CE1 PHE A 456    16171  19198  19054   -411  -1419   -507       C  
ATOM   2524  CE2 PHE A 456      69.152  28.286  77.795  1.00150.51           C  
ANISOU 2524  CE2 PHE A 456    16864  20030  20292   -245  -1859   -538       C  
ATOM   2525  CZ  PHE A 456      68.079  28.918  77.184  1.00146.44           C  
ANISOU 2525  CZ  PHE A 456    16525  19511  19604   -329  -1596   -432       C  
ATOM   2526  N   LEU A 457      71.852  29.478  82.244  1.00157.45           N  
ANISOU 2526  N   LEU A 457    17336  21416  21071      5  -2775  -1083       N  
ATOM   2527  CA  LEU A 457      72.412  28.226  82.749  1.00157.26           C  
ANISOU 2527  CA  LEU A 457    17255  21379  21114    176  -3137  -1002       C  
ATOM   2528  C   LEU A 457      71.710  27.829  84.022  1.00155.30           C  
ANISOU 2528  C   LEU A 457    17233  21301  20470    298  -3377   -711       C  
ATOM   2529  O   LEU A 457      71.345  26.668  84.192  1.00152.18           O  
ANISOU 2529  O   LEU A 457    16956  20856  20006    392  -3525   -414       O  
ATOM   2530  CB  LEU A 457      73.910  28.361  82.969  1.00162.85           C  
ANISOU 2530  CB  LEU A 457    17653  22075  22145    248  -3345  -1384       C  
ATOM   2531  CG  LEU A 457      74.667  28.371  81.635  1.00166.65           C  
ANISOU 2531  CG  LEU A 457    17902  22357  23060    153  -3105  -1617       C  
ATOM   2532  CD1 LEU A 457      75.903  29.258  81.688  1.00170.24           C  
ANISOU 2532  CD1 LEU A 457    18035  22805  23841    113  -3099  -2062       C  
ATOM   2533  CD2 LEU A 457      75.017  26.942  81.216  1.00171.05           C  
ANISOU 2533  CD2 LEU A 457    18404  22777  23809    271  -3273  -1512       C  
ATOM   2534  N   GLU A 458      71.472  28.806  84.890  1.00158.80           N  
ANISOU 2534  N   GLU A 458    17749  21934  20653    296  -3389   -787       N  
ATOM   2535  CA  GLU A 458      70.795  28.546  86.153  1.00164.79           C  
ANISOU 2535  CA  GLU A 458    18743  22885  20985    423  -3581   -520       C  
ATOM   2536  C   GLU A 458      69.409  28.002  85.884  1.00158.85           C  
ANISOU 2536  C   GLU A 458    18233  22091  20030    361  -3379    -98       C  
ATOM   2537  O   GLU A 458      68.965  27.057  86.555  1.00159.21           O  
ANISOU 2537  O   GLU A 458    18443  22172  19875    476  -3541    230       O  
ATOM   2538  CB  GLU A 458      70.664  29.853  86.950  1.00176.27           C  
ANISOU 2538  CB  GLU A 458    20234  24544  22196    409  -3554   -715       C  
ATOM   2539  CG  GLU A 458      70.125  29.721  88.359  1.00189.37           C  
ANISOU 2539  CG  GLU A 458    22128  26441  23381    571  -3760   -505       C  
ATOM   2540  CD  GLU A 458      71.044  28.942  89.277  1.00205.24           C  
ANISOU 2540  CD  GLU A 458    24105  28528  25349    811  -4209   -533       C  
ATOM   2541  OE1 GLU A 458      72.210  28.649  88.907  1.00213.13           O  
ANISOU 2541  OE1 GLU A 458    24851  29410  26718    853  -4392   -789       O  
ATOM   2542  OE2 GLU A 458      70.594  28.597  90.397  1.00220.14           O  
ANISOU 2542  OE2 GLU A 458    26228  30596  26820    976  -4382   -289       O  
ATOM   2543  N   CYS A 459      68.738  28.574  84.883  1.00150.08           N  
ANISOU 2543  N   CYS A 459    17137  20891  18992    184  -3028   -106       N  
ATOM   2544  CA  CYS A 459      67.403  28.114  84.517  1.00142.69           C  
ANISOU 2544  CA  CYS A 459    16393  19902  17920    115  -2836    246       C  
ATOM   2545  C   CYS A 459      67.455  26.645  84.115  1.00141.35           C  
ANISOU 2545  C   CYS A 459    16217  19554  17933    173  -2967    462       C  
ATOM   2546  O   CYS A 459      66.545  25.881  84.422  1.00140.57           O  
ANISOU 2546  O   CYS A 459    16279  19440  17691    193  -2975    811       O  
ATOM   2547  CB  CYS A 459      66.784  29.014  83.457  1.00137.71           C  
ANISOU 2547  CB  CYS A 459    15767  19201  17353    -53  -2477    157       C  
ATOM   2548  SG  CYS A 459      66.706  30.742  84.034  1.00130.29           S  
ANISOU 2548  SG  CYS A 459    14841  18446  16217   -110  -2339    -88       S  
ATOM   2549  N   LEU A 460      68.542  26.261  83.449  1.00143.65           N  
ANISOU 2549  N   LEU A 460    16310  19703  18566    201  -3061    241       N  
ATOM   2550  CA  LEU A 460      68.738  24.873  83.066  1.00148.44           C  
ANISOU 2550  CA  LEU A 460    16887  20126  19387    274  -3213    393       C  
ATOM   2551  C   LEU A 460      69.095  24.034  84.283  1.00154.40           C  
ANISOU 2551  C   LEU A 460    17702  20944  20020    461  -3568    571       C  
ATOM   2552  O   LEU A 460      68.643  22.899  84.409  1.00149.10           O  
ANISOU 2552  O   LEU A 460    17137  20160  19355    518  -3664    883       O  
ATOM   2553  CB  LEU A 460      69.848  24.715  82.028  1.00150.67           C  
ANISOU 2553  CB  LEU A 460    16930  20247  20069    269  -3205     83       C  
ATOM   2554  CG  LEU A 460      69.654  25.285  80.629  1.00148.98           C  
ANISOU 2554  CG  LEU A 460    16666  19925  20014    121  -2860    -77       C  
ATOM   2555  CD1 LEU A 460      70.941  25.176  79.838  1.00149.97           C  
ANISOU 2555  CD1 LEU A 460    16542  19928  20512    144  -2861   -402       C  
ATOM   2556  CD2 LEU A 460      68.537  24.553  79.908  1.00149.48           C  
ANISOU 2556  CD2 LEU A 460    16876  19858  20061     75  -2742    185       C  
ATOM   2557  N   ARG A 461      69.891  24.601  85.187  1.00163.94           N  
ANISOU 2557  N   ARG A 461    18849  22323  21118    563  -3767    372       N  
ATOM   2558  CA  ARG A 461      70.361  23.851  86.347  1.00169.57           C  
ANISOU 2558  CA  ARG A 461    19625  23108  21693    781  -4143    509       C  
ATOM   2559  C   ARG A 461      69.217  23.569  87.304  1.00166.31           C  
ANISOU 2559  C   ARG A 461    19513  22814  20861    825  -4125    935       C  
ATOM   2560  O   ARG A 461      69.122  22.477  87.873  1.00170.50           O  
ANISOU 2560  O   ARG A 461    20172  23288  21320    965  -4321   1246       O  
ATOM   2561  CB  ARG A 461      71.444  24.673  87.024  1.00175.94           C  
ANISOU 2561  CB  ARG A 461    20283  24085  22480    880  -4358    138       C  
ATOM   2562  CG  ARG A 461      72.311  23.904  87.974  1.00185.41           C  
ANISOU 2562  CG  ARG A 461    21468  25328  23649   1137  -4804    154       C  
ATOM   2563  CD  ARG A 461      73.168  24.872  88.739  1.00197.46           C  
ANISOU 2563  CD  ARG A 461    22868  27058  25097   1229  -5012   -223       C  
ATOM   2564  NE  ARG A 461      72.416  25.747  89.637  1.00210.02           N  
ANISOU 2564  NE  ARG A 461    24672  28896  26229   1227  -4938   -154       N  
ATOM   2565  CZ  ARG A 461      71.864  25.370  90.794  1.00214.64           C  
ANISOU 2565  CZ  ARG A 461    25544  29648  26360   1395  -5095    164       C  
ATOM   2566  NH1 ARG A 461      71.934  24.111  91.239  1.00222.79           N  
ANISOU 2566  NH1 ARG A 461    26710  30614  27324   1581  -5338    486       N  
ATOM   2567  NH2 ARG A 461      71.227  26.272  91.539  1.00213.81           N  
ANISOU 2567  NH2 ARG A 461    25608  29776  25854   1389  -4997    169       N  
ATOM   2568  N   THR A 462      68.346  24.559  87.459  1.00158.21           N  
ANISOU 2568  N   THR A 462    18597  21939  19574    708  -3869    952       N  
ATOM   2569  CA  THR A 462      67.185  24.422  88.324  1.00156.61           C  
ANISOU 2569  CA  THR A 462    18664  21864  18975    730  -3783   1336       C  
ATOM   2570  C   THR A 462      66.056  23.732  87.576  1.00158.80           C  
ANISOU 2570  C   THR A 462    19015  21952  19371    591  -3538   1652       C  
ATOM   2571  O   THR A 462      65.076  23.307  88.186  1.00169.57           O  
ANISOU 2571  O   THR A 462    20575  23353  20500    601  -3457   2025       O  
ATOM   2572  CB  THR A 462      66.697  25.791  88.814  1.00152.66           C  
ANISOU 2572  CB  THR A 462    18235  21606  18163    671  -3610   1197       C  
ATOM   2573  OG1 THR A 462      66.562  26.683  87.706  1.00144.64           O  
ANISOU 2573  OG1 THR A 462    17077  20512  17365    477  -3337    940       O  
ATOM   2574  CG2 THR A 462      67.678  26.368  89.779  1.00156.56           C  
ANISOU 2574  CG2 THR A 462    18691  22304  18491    837  -3892    922       C  
ATOM   2575  N   GLU A 463      66.214  23.621  86.254  1.00155.86           N  
ANISOU 2575  N   GLU A 463    18476  21373  19369    469  -3420   1487       N  
ATOM   2576  CA  GLU A 463      65.169  23.117  85.375  1.00152.14           C  
ANISOU 2576  CA  GLU A 463    18041  20721  19044    332  -3196   1693       C  
ATOM   2577  C   GLU A 463      63.900  23.939  85.589  1.00142.34           C  
ANISOU 2577  C   GLU A 463    16932  19622  17527    217  -2914   1818       C  
ATOM   2578  O   GLU A 463      62.814  23.390  85.768  1.00132.40           O  
ANISOU 2578  O   GLU A 463    15791  18315  16197    174  -2803   2151       O  
ATOM   2579  CB  GLU A 463      64.933  21.618  85.610  1.00161.00           C  
ANISOU 2579  CB  GLU A 463    19239  21660  20272    409  -3346   2050       C  
ATOM   2580  CG  GLU A 463      66.205  20.759  85.603  1.00170.96           C  
ANISOU 2580  CG  GLU A 463    20386  22791  21779    564  -3667   1949       C  
ATOM   2581  CD  GLU A 463      65.869  19.236  85.735  1.00181.07           C  
ANISOU 2581  CD  GLU A 463    21750  23837  23211    628  -3792   2325       C  
ATOM   2582  OE1 GLU A 463      66.606  18.493  86.464  1.00193.45           O  
ANISOU 2582  OE1 GLU A 463    23352  25373  24776    817  -4089   2432       O  
ATOM   2583  OE2 GLU A 463      64.862  18.750  85.141  1.00178.32           O  
ANISOU 2583  OE2 GLU A 463    21434  23320  22999    502  -3608   2521       O  
ATOM   2584  N   LYS A 464      64.063  25.247  85.585  1.00143.11           N  
ANISOU 2584  N   LYS A 464    16993  19880  17501    170  -2801   1542       N  
ATOM   2585  CA  LYS A 464      62.968  26.144  85.886  1.00146.83           C  
ANISOU 2585  CA  LYS A 464    17580  20505  17701     87  -2556   1616       C  
ATOM   2586  C   LYS A 464      63.082  27.428  85.083  1.00144.96           C  
ANISOU 2586  C   LYS A 464    17248  20287  17542    -23  -2362   1277       C  
ATOM   2587  O   LYS A 464      63.875  28.324  85.406  1.00151.68           O  
ANISOU 2587  O   LYS A 464    18033  21254  18341      6  -2419    990       O  
ATOM   2588  CB  LYS A 464      62.957  26.439  87.384  1.00157.96           C  
ANISOU 2588  CB  LYS A 464    19134  22170  18713    214  -2664   1714       C  
ATOM   2589  CG  LYS A 464      61.702  27.127  87.890  1.00166.90           C  
ANISOU 2589  CG  LYS A 464    20410  23469  19536    156  -2414   1864       C  
ATOM   2590  CD  LYS A 464      60.573  26.134  88.094  1.00178.85           C  
ANISOU 2590  CD  LYS A 464    22042  24905  21008    130  -2303   2306       C  
ATOM   2591  CE  LYS A 464      59.187  26.776  87.941  1.00185.90           C  
ANISOU 2591  CE  LYS A 464    22981  25859  21791      4  -1979   2398       C  
ATOM   2592  NZ  LYS A 464      58.947  27.859  88.937  1.00189.98           N  
ANISOU 2592  NZ  LYS A 464    23605  26663  21914     61  -1897   2317       N  
ATOM   2593  N   LEU A 465      62.310  27.479  84.004  1.00139.93           N  
ANISOU 2593  N   LEU A 465    16600  19514  17052   -144  -2144   1309       N  
ATOM   2594  CA  LEU A 465      62.158  28.696  83.222  1.00138.27           C  
ANISOU 2594  CA  LEU A 465    16352  19308  16875   -244  -1917   1064       C  
ATOM   2595  C   LEU A 465      60.681  28.958  83.081  1.00134.79           C  
ANISOU 2595  C   LEU A 465    16020  18892  16302   -320  -1697   1255       C  
ATOM   2596  O   LEU A 465      60.025  28.397  82.175  1.00128.43           O  
ANISOU 2596  O   LEU A 465    15208  17928  15662   -374  -1618   1364       O  
ATOM   2597  CB  LEU A 465      62.808  28.547  81.867  1.00139.78           C  
ANISOU 2597  CB  LEU A 465    16418  19299  17390   -286  -1876    865       C  
ATOM   2598  CG  LEU A 465      62.602  29.678  80.854  1.00141.74           C  
ANISOU 2598  CG  LEU A 465    16658  19505  17689   -380  -1613    661       C  
ATOM   2599  CD1 LEU A 465      62.873  31.061  81.431  1.00140.90           C  
ANISOU 2599  CD1 LEU A 465    16552  19549  17435   -401  -1528    456       C  
ATOM   2600  CD2 LEU A 465      63.474  29.435  79.626  1.00143.41           C  
ANISOU 2600  CD2 LEU A 465    16754  19535  18198   -391  -1583    464       C  
ATOM   2601  N   ASP A 466      60.153  29.801  83.981  1.00138.85           N  
ANISOU 2601  N   ASP A 466    16621  19606  16526   -312  -1611   1276       N  
ATOM   2602  CA  ASP A 466      58.735  30.161  84.007  1.00143.35           C  
ANISOU 2602  CA  ASP A 466    17278  20230  16958   -372  -1396   1439       C  
ATOM   2603  C   ASP A 466      58.321  30.935  82.780  1.00132.74           C  
ANISOU 2603  C   ASP A 466    15903  18779  15752   -458  -1199   1276       C  
ATOM   2604  O   ASP A 466      59.070  31.732  82.298  1.00124.31           O  
ANISOU 2604  O   ASP A 466    14787  17683  14760   -473  -1164   1009       O  
ATOM   2605  CB  ASP A 466      58.418  31.069  85.184  1.00159.83           C  
ANISOU 2605  CB  ASP A 466    19455  22564  18709   -330  -1336   1421       C  
ATOM   2606  CG  ASP A 466      58.451  30.348  86.473  1.00177.60           C  
ANISOU 2606  CG  ASP A 466    21797  24954  20728   -227  -1478   1653       C  
ATOM   2607  OD1 ASP A 466      57.705  29.340  86.586  1.00184.11           O  
ANISOU 2607  OD1 ASP A 466    22665  25713  21573   -238  -1450   1978       O  
ATOM   2608  OD2 ASP A 466      59.225  30.792  87.359  1.00195.39           O  
ANISOU 2608  OD2 ASP A 466    24078  27373  22789   -129  -1620   1505       O  
ATOM   2609  N   HIS A 467      57.104  30.708  82.291  1.00132.08           N  
ANISOU 2609  N   HIS A 467    15846  18631  15706   -508  -1069   1440       N  
ATOM   2610  CA  HIS A 467      56.608  31.510  81.180  1.00126.65           C  
ANISOU 2610  CA  HIS A 467    15159  17860  15100   -557   -896   1296       C  
ATOM   2611  C   HIS A 467      56.400  32.929  81.692  1.00117.40           C  
ANISOU 2611  C   HIS A 467    14040  16845  13721   -559   -754   1155       C  
ATOM   2612  O   HIS A 467      55.888  33.119  82.800  1.00118.67           O  
ANISOU 2612  O   HIS A 467    14248  17179  13660   -536   -729   1263       O  
ATOM   2613  CB  HIS A 467      55.323  31.024  80.574  1.00130.19           C  
ANISOU 2613  CB  HIS A 467    15609  18214  15640   -592   -820   1465       C  
ATOM   2614  CG  HIS A 467      54.996  31.702  79.296  1.00127.53           C  
ANISOU 2614  CG  HIS A 467    15286  17772  15395   -604   -701   1303       C  
ATOM   2615  ND1 HIS A 467      53.836  32.408  79.097  1.00128.60           N  
ANISOU 2615  ND1 HIS A 467    15458  17944  15459   -613   -554   1319       N  
ATOM   2616  CD2 HIS A 467      55.711  31.826  78.171  1.00125.82           C  
ANISOU 2616  CD2 HIS A 467    15065  17421  15317   -591   -702   1122       C  
ATOM   2617  CE1 HIS A 467      53.835  32.905  77.877  1.00129.28           C  
ANISOU 2617  CE1 HIS A 467    15578  17915  15627   -595   -491   1166       C  
ATOM   2618  NE2 HIS A 467      54.962  32.563  77.292  1.00127.89           N  
ANISOU 2618  NE2 HIS A 467    15386  17637  15568   -583   -563   1051       N  
ATOM   2619  N   TYR A 468      56.772  33.918  80.881  1.00110.51           N  
ANISOU 2619  N   TYR A 468    13166  15902  12919   -580   -645    920       N  
ATOM   2620  CA  TYR A 468      56.780  35.317  81.310  1.00114.98           C  
ANISOU 2620  CA  TYR A 468    13770  16574  13343   -583   -521    743       C  
ATOM   2621  C   TYR A 468      55.394  35.883  81.535  1.00119.58           C  
ANISOU 2621  C   TYR A 468    14418  17240  13776   -582   -369    841       C  
ATOM   2622  O   TYR A 468      55.210  36.851  82.277  1.00126.27           O  
ANISOU 2622  O   TYR A 468    15301  18221  14454   -566   -293    745       O  
ATOM   2623  CB  TYR A 468      57.518  36.181  80.294  1.00114.31           C  
ANISOU 2623  CB  TYR A 468    13671  16346  13416   -613   -414    497       C  
ATOM   2624  CG  TYR A 468      57.855  37.557  80.833  1.00113.83           C  
ANISOU 2624  CG  TYR A 468    13618  16359  13273   -623   -322    278       C  
ATOM   2625  CD1 TYR A 468      58.826  37.718  81.810  1.00112.49           C  
ANISOU 2625  CD1 TYR A 468    13380  16295  13065   -608   -455    129       C  
ATOM   2626  CD2 TYR A 468      57.187  38.695  80.385  1.00113.81           C  
ANISOU 2626  CD2 TYR A 468    13689  16312  13242   -636   -123    207       C  
ATOM   2627  CE1 TYR A 468      59.136  38.980  82.317  1.00112.89           C  
ANISOU 2627  CE1 TYR A 468    13422  16399  13070   -617   -391   -106       C  
ATOM   2628  CE2 TYR A 468      57.490  39.952  80.889  1.00115.03           C  
ANISOU 2628  CE2 TYR A 468    13845  16506  13353   -647    -42     -3       C  
ATOM   2629  CZ  TYR A 468      58.474  40.091  81.851  1.00113.69           C  
ANISOU 2629  CZ  TYR A 468    13594  16436  13167   -644   -176   -171       C  
ATOM   2630  OH  TYR A 468      58.761  41.326  82.364  1.00113.99           O  
ANISOU 2630  OH  TYR A 468    13619  16502  13188   -654   -115   -410       O  
ATOM   2631  N   PHE A 469      54.409  35.297  80.872  1.00120.28           N  
ANISOU 2631  N   PHE A 469    14509  17243  13947   -593   -331   1006       N  
ATOM   2632  CA  PHE A 469      53.028  35.740  80.975  1.00121.84           C  
ANISOU 2632  CA  PHE A 469    14735  17501  14058   -589   -194   1094       C  
ATOM   2633  C   PHE A 469      52.200  34.782  81.798  1.00120.58           C  
ANISOU 2633  C   PHE A 469    14543  17433  13838   -595   -220   1360       C  
ATOM   2634  O   PHE A 469      51.174  35.165  82.383  1.00119.61           O  
ANISOU 2634  O   PHE A 469    14426  17428  13589   -588    -95   1439       O  
ATOM   2635  CB  PHE A 469      52.402  35.823  79.616  1.00122.85           C  
ANISOU 2635  CB  PHE A 469    14871  17462  14341   -585   -135   1071       C  
ATOM   2636  CG  PHE A 469      53.029  36.839  78.750  1.00126.74           C  
ANISOU 2636  CG  PHE A 469    15426  17852  14874   -570    -53    852       C  
ATOM   2637  CD1 PHE A 469      54.269  36.605  78.170  1.00128.40           C  
ANISOU 2637  CD1 PHE A 469    15628  17954  15204   -582   -108    741       C  
ATOM   2638  CD2 PHE A 469      52.404  38.044  78.528  1.00131.06           C  
ANISOU 2638  CD2 PHE A 469    16040  18403  15354   -541     96    760       C  
ATOM   2639  CE1 PHE A 469      54.861  37.555  77.366  1.00129.86           C  
ANISOU 2639  CE1 PHE A 469    15872  18029  15439   -577     13    558       C  
ATOM   2640  CE2 PHE A 469      52.990  39.001  77.723  1.00132.80           C  
ANISOU 2640  CE2 PHE A 469    16335  18501  15620   -528    199    586       C  
ATOM   2641  CZ  PHE A 469      54.223  38.759  77.140  1.00130.20           C  
ANISOU 2641  CZ  PHE A 469    15999  18059  15409   -552    172    492       C  
ATOM   2642  N   ILE A 470      52.637  33.532  81.845  1.00121.34           N  
ANISOU 2642  N   ILE A 470    14602  17462  14039   -607   -366   1504       N  
ATOM   2643  CA  ILE A 470      51.968  32.472  82.609  1.00125.47           C  
ANISOU 2643  CA  ILE A 470    15100  18029  14544   -620   -385   1794       C  
ATOM   2644  C   ILE A 470      52.957  31.870  83.602  1.00126.64           C  
ANISOU 2644  C   ILE A 470    15284  18260  14571   -580   -531   1876       C  
ATOM   2645  O   ILE A 470      53.587  30.893  83.294  1.00123.19           O  
ANISOU 2645  O   ILE A 470    14814  17694  14296   -580   -685   1936       O  
ATOM   2646  CB  ILE A 470      51.311  31.412  81.718  1.00127.55           C  
ANISOU 2646  CB  ILE A 470    15281  18093  15086   -664   -427   1930       C  
ATOM   2647  CG1 ILE A 470      50.530  32.061  80.575  1.00125.59           C  
ANISOU 2647  CG1 ILE A 470    15009  17755  14954   -667   -341   1789       C  
ATOM   2648  CG2 ILE A 470      50.387  30.554  82.567  1.00131.63           C  
ANISOU 2648  CG2 ILE A 470    15760  18648  15602   -698   -371   2234       C  
ATOM   2649  CD1 ILE A 470      50.534  31.267  79.303  1.00126.06           C  
ANISOU 2649  CD1 ILE A 470    15017  17595  15284   -672   -458   1758       C  
ATOM   2650  N   PRO A 471      53.066  32.443  84.802  1.00131.22           N  
ANISOU 2650  N   PRO A 471    15937  19060  14860   -528   -495   1871       N  
ATOM   2651  CA  PRO A 471      54.080  32.002  85.778  1.00136.63           C  
ANISOU 2651  CA  PRO A 471    16675  19848  15388   -453   -669   1910       C  
ATOM   2652  C   PRO A 471      53.961  30.564  86.227  1.00138.15           C  
ANISOU 2652  C   PRO A 471    16885  19987  15619   -440   -759   2240       C  
ATOM   2653  O   PRO A 471      54.993  30.003  86.561  1.00143.76           O  
ANISOU 2653  O   PRO A 471    17614  20686  16320   -375   -962   2245       O  
ATOM   2654  CB  PRO A 471      53.887  32.975  86.944  1.00142.66           C  
ANISOU 2654  CB  PRO A 471    17529  20874  15800   -386   -583   1841       C  
ATOM   2655  CG  PRO A 471      52.928  34.019  86.453  1.00140.41           C  
ANISOU 2655  CG  PRO A 471    17219  20594  15533   -436   -366   1723       C  
ATOM   2656  CD  PRO A 471      52.099  33.366  85.414  1.00133.80           C  
ANISOU 2656  CD  PRO A 471    16303  19559  14973   -517   -299   1866       C  
ATOM   2657  N   LYS A 472      52.738  29.996  86.269  1.00135.05           N  
ANISOU 2657  N   LYS A 472    16475  19550  15287   -496   -609   2507       N  
ATOM   2658  CA  LYS A 472      52.557  28.599  86.648  1.00139.04           C  
ANISOU 2658  CA  LYS A 472    16989  19956  15881   -500   -663   2845       C  
ATOM   2659  C   LYS A 472      53.037  27.627  85.560  1.00137.43           C  
ANISOU 2659  C   LYS A 472    16689  19473  16053   -542   -832   2831       C  
ATOM   2660  O   LYS A 472      53.274  26.442  85.825  1.00141.14           O  
ANISOU 2660  O   LYS A 472    17169  19826  16631   -525   -947   3060       O  
ATOM   2661  CB  LYS A 472      51.101  28.285  87.010  1.00140.86           C  
ANISOU 2661  CB  LYS A 472    17199  20199  16120   -564   -426   3125       C  
ATOM   2662  CG  LYS A 472      50.039  28.277  85.896  1.00141.31           C  
ANISOU 2662  CG  LYS A 472    17106  20083  16501   -676   -309   3085       C  
ATOM   2663  CD  LYS A 472      48.754  27.575  86.420  1.00149.24           C  
ANISOU 2663  CD  LYS A 472    18058  21059  17587   -745   -106   3421       C  
ATOM   2664  CE  LYS A 472      47.439  28.210  85.993  1.00149.00           C  
ANISOU 2664  CE  LYS A 472    17904  21041  17667   -812    103   3351       C  
ATOM   2665  NZ  LYS A 472      46.228  27.657  86.687  1.00148.43           N  
ANISOU 2665  NZ  LYS A 472    17764  20976  17654   -878    344   3665       N  
ATOM   2666  N   PHE A 473      53.150  28.117  84.338  1.00134.73           N  
ANISOU 2666  N   PHE A 473    16266  19020  15905   -584   -840   2570       N  
ATOM   2667  CA  PHE A 473      53.638  27.319  83.237  1.00134.62           C  
ANISOU 2667  CA  PHE A 473    16170  18762  16215   -605   -989   2502       C  
ATOM   2668  C   PHE A 473      55.153  27.302  83.247  1.00127.44           C  
ANISOU 2668  C   PHE A 473    15273  17854  15293   -532  -1183   2327       C  
ATOM   2669  O   PHE A 473      55.795  28.274  82.861  1.00116.96           O  
ANISOU 2669  O   PHE A 473    13939  16583  13915   -518  -1172   2045       O  
ATOM   2670  CB  PHE A 473      53.140  27.831  81.899  1.00136.10           C  
ANISOU 2670  CB  PHE A 473    16291  18839  16582   -654   -913   2299       C  
ATOM   2671  CG  PHE A 473      53.330  26.854  80.773  1.00136.19           C  
ANISOU 2671  CG  PHE A 473    16223  18600  16923   -668  -1046   2265       C  
ATOM   2672  CD1 PHE A 473      52.763  25.570  80.837  1.00140.99           C  
ANISOU 2672  CD1 PHE A 473    16768  19044  17754   -707  -1105   2506       C  
ATOM   2673  CD2 PHE A 473      54.015  27.220  79.655  1.00132.69           C  
ANISOU 2673  CD2 PHE A 473    15768  18074  16574   -642  -1094   1996       C  
ATOM   2674  CE1 PHE A 473      52.891  24.689  79.795  1.00142.82           C  
ANISOU 2674  CE1 PHE A 473    16922  19040  18300   -712  -1238   2443       C  
ATOM   2675  CE2 PHE A 473      54.160  26.348  78.584  1.00136.66           C  
ANISOU 2675  CE2 PHE A 473    16209  18361  17355   -636  -1210   1938       C  
ATOM   2676  CZ  PHE A 473      53.620  25.067  78.665  1.00141.29           C  
ANISOU 2676  CZ  PHE A 473    16728  18790  18166   -666  -1301   2148       C  
ATOM   2677  N   ASN A 474      55.742  26.165  83.635  1.00130.36           N  
ANISOU 2677  N   ASN A 474    15645  18136  15749   -484  -1362   2490       N  
ATOM   2678  CA  ASN A 474      57.181  25.953  83.507  1.00132.26           C  
ANISOU 2678  CA  ASN A 474    15855  18336  16061   -408  -1575   2315       C  
ATOM   2679  C   ASN A 474      57.568  25.401  82.146  1.00129.00           C  
ANISOU 2679  C   ASN A 474    15336  17684  15994   -434  -1649   2166       C  
ATOM   2680  O   ASN A 474      56.932  24.460  81.668  1.00128.35           O  
ANISOU 2680  O   ASN A 474    15217  17418  16132   -474  -1661   2321       O  
ATOM   2681  CB  ASN A 474      57.726  25.006  84.562  1.00138.43           C  
ANISOU 2681  CB  ASN A 474    16696  19133  16767   -310  -1763   2542       C  
ATOM   2682  CG  ASN A 474      59.205  24.709  84.355  1.00142.34           C  
ANISOU 2682  CG  ASN A 474    17125  19564  17392   -222  -2007   2341       C  
ATOM   2683  OD1 ASN A 474      59.967  25.541  83.846  1.00141.04           O  
ANISOU 2683  OD1 ASN A 474    16888  19439  17260   -223  -2012   2013       O  
ATOM   2684  ND2 ASN A 474      59.612  23.519  84.728  1.00151.38           N  
ANISOU 2684  ND2 ASN A 474    18283  20592  18640   -144  -2199   2538       N  
ATOM   2685  N   LEU A 475      58.620  25.975  81.560  1.00129.54           N  
ANISOU 2685  N   LEU A 475    15351  17751  16116   -408  -1694   1860       N  
ATOM   2686  CA  LEU A 475      59.023  25.634  80.204  1.00130.72           C  
ANISOU 2686  CA  LEU A 475    15416  17704  16547   -419  -1719   1680       C  
ATOM   2687  C   LEU A 475      60.132  24.614  80.199  1.00133.97           C  
ANISOU 2687  C   LEU A 475    15754  17992  17155   -342  -1946   1658       C  
ATOM   2688  O   LEU A 475      60.387  23.985  79.162  1.00135.19           O  
ANISOU 2688  O   LEU A 475    15840  17959  17567   -335  -1993   1560       O  
ATOM   2689  CB  LEU A 475      59.532  26.835  79.421  1.00131.28           C  
ANISOU 2689  CB  LEU A 475    15466  17816  16596   -437  -1587   1363       C  
ATOM   2690  CG  LEU A 475      58.501  27.724  78.766  1.00131.71           C  
ANISOU 2690  CG  LEU A 475    15579  17892  16572   -497  -1369   1320       C  
ATOM   2691  CD1 LEU A 475      57.379  28.066  79.728  1.00135.27           C  
ANISOU 2691  CD1 LEU A 475    16099  18489  16807   -529  -1281   1523       C  
ATOM   2692  CD2 LEU A 475      59.170  28.999  78.257  1.00131.79           C  
ANISOU 2692  CD2 LEU A 475    15592  17948  16531   -505  -1231   1037       C  
ATOM   2693  N   PHE A 476      60.805  24.477  81.347  1.00138.53           N  
ANISOU 2693  N   PHE A 476    16351  18681  17602   -266  -2096   1728       N  
ATOM   2694  CA  PHE A 476      61.923  23.521  81.475  1.00143.47           C  
ANISOU 2694  CA  PHE A 476    16904  19199  18410   -166  -2346   1706       C  
ATOM   2695  C   PHE A 476      61.519  22.357  82.372  1.00145.97           C  
ANISOU 2695  C   PHE A 476    17298  19456  18708   -112  -2485   2073       C  
ATOM   2696  O   PHE A 476      62.367  21.793  83.074  1.00151.95           O  
ANISOU 2696  O   PHE A 476    18055  20214  19462      6  -2710   2126       O  
ATOM   2697  CB  PHE A 476      63.190  24.212  82.018  1.00145.94           C  
ANISOU 2697  CB  PHE A 476    17157  19659  18632    -89  -2458   1462       C  
ATOM   2698  CG  PHE A 476      63.940  25.053  81.004  1.00143.62           C  
ANISOU 2698  CG  PHE A 476    16742  19339  18485   -133  -2345   1092       C  
ATOM   2699  CD1 PHE A 476      63.658  25.030  79.627  1.00139.29           C  
ANISOU 2699  CD1 PHE A 476    16160  18637  18124   -200  -2186    988       C  
ATOM   2700  CD2 PHE A 476      64.983  25.856  81.440  1.00145.88           C  
ANISOU 2700  CD2 PHE A 476    16945  19750  18731    -96  -2402    837       C  
ATOM   2701  CE1 PHE A 476      64.376  25.822  78.742  1.00136.19           C  
ANISOU 2701  CE1 PHE A 476    15682  18225  17840   -229  -2047    678       C  
ATOM   2702  CE2 PHE A 476      65.709  26.638  80.547  1.00143.98           C  
ANISOU 2702  CE2 PHE A 476    16581  19466  18655   -147  -2264    511       C  
ATOM   2703  CZ  PHE A 476      65.407  26.614  79.196  1.00138.22           C  
ANISOU 2703  CZ  PHE A 476    15846  18587  18084   -214  -2069    450       C  
ATOM   2704  N   SER A 477      60.239  21.987  82.366  1.00145.73           N  
ANISOU 2704  N   SER A 477    17330  19361  18678   -192  -2355   2332       N  
ATOM   2705  CA  SER A 477      59.811  20.823  83.101  1.00155.13           C  
ANISOU 2705  CA  SER A 477    18587  20444  19908   -161  -2443   2703       C  
ATOM   2706  C   SER A 477      60.344  19.543  82.449  1.00159.20           C  
ANISOU 2706  C   SER A 477    19013  20672  20804   -117  -2636   2706       C  
ATOM   2707  O   SER A 477      60.852  19.543  81.323  1.00156.06           O  
ANISOU 2707  O   SER A 477    18500  20161  20633   -123  -2668   2422       O  
ATOM   2708  CB  SER A 477      58.291  20.776  83.299  1.00156.35           C  
ANISOU 2708  CB  SER A 477    18801  20594  20011   -272  -2225   2973       C  
ATOM   2709  OG  SER A 477      57.621  20.581  82.091  1.00158.60           O  
ANISOU 2709  OG  SER A 477    18985  20697  20575   -372  -2141   2876       O  
ATOM   2710  N   GLN A 478      60.251  18.452  83.196  1.00168.54           N  
ANISOU 2710  N   GLN A 478    20260  21733  22042    -59  -2758   3035       N  
ATOM   2711  CA  GLN A 478      60.658  17.148  82.695  1.00174.46           C  
ANISOU 2711  CA  GLN A 478    20935  22181  23171    -12  -2948   3078       C  
ATOM   2712  C   GLN A 478      59.642  16.670  81.661  1.00176.64           C  
ANISOU 2712  C   GLN A 478    21131  22230  23754   -143  -2830   3086       C  
ATOM   2713  O   GLN A 478      59.983  15.906  80.748  1.00183.90           O  
ANISOU 2713  O   GLN A 478    21945  22910  25018   -124  -2954   2944       O  
ATOM   2714  CB  GLN A 478      60.812  16.141  83.851  1.00179.22           C  
ANISOU 2714  CB  GLN A 478    21654  22700  23739     96  -3104   3461       C  
ATOM   2715  CG  GLN A 478      61.447  14.792  83.490  1.00179.38           C  
ANISOU 2715  CG  GLN A 478    21606  22402  24148    184  -3347   3501       C  
ATOM   2716  CD  GLN A 478      62.932  14.859  83.179  1.00179.97           C  
ANISOU 2716  CD  GLN A 478    21576  22497  24305    326  -3584   3167       C  
ATOM   2717  OE1 GLN A 478      63.527  15.928  83.153  1.00175.90           O  
ANISOU 2717  OE1 GLN A 478    21022  22221  23590    345  -3561   2882       O  
ATOM   2718  NE2 GLN A 478      63.530  13.700  82.931  1.00184.05           N  
ANISOU 2718  NE2 GLN A 478    22030  22745  25153    425  -3807   3192       N  
ATOM   2719  N   GLU A 479      58.401  17.140  81.792  1.00174.59           N  
ANISOU 2719  N   GLU A 479    20910  22049  23375   -265  -2602   3222       N  
ATOM   2720  CA  GLU A 479      57.328  16.756  80.887  1.00176.45           C  
ANISOU 2720  CA  GLU A 479    21055  22088  23898   -386  -2503   3219       C  
ATOM   2721  C   GLU A 479      57.592  17.231  79.471  1.00164.79           C  
ANISOU 2721  C   GLU A 479    19482  20588  22542   -392  -2508   2808       C  
ATOM   2722  O   GLU A 479      57.224  16.562  78.502  1.00170.62           O  
ANISOU 2722  O   GLU A 479    20128  21097  23601   -421  -2561   2715       O  
ATOM   2723  CB  GLU A 479      55.975  17.313  81.338  1.00188.43           C  
ANISOU 2723  CB  GLU A 479    22611  23728  25253   -504  -2250   3409       C  
ATOM   2724  CG  GLU A 479      55.443  16.700  82.631  1.00204.80           C  
ANISOU 2724  CG  GLU A 479    24781  25783  27249   -518  -2180   3862       C  
ATOM   2725  CD  GLU A 479      55.848  17.491  83.865  1.00217.27           C  
ANISOU 2725  CD  GLU A 479    26521  27681  28350   -433  -2128   3967       C  
ATOM   2726  OE1 GLU A 479      57.042  17.495  84.213  1.00221.47           O  
ANISOU 2726  OE1 GLU A 479    27109  28286  28753   -297  -2322   3882       O  
ATOM   2727  OE2 GLU A 479      54.972  18.113  84.490  1.00235.24           O  
ANISOU 2727  OE2 GLU A 479    28858  30136  30384   -492  -1902   4113       O  
ATOM   2728  N   LEU A 480      58.223  18.388  79.353  1.00153.43           N  
ANISOU 2728  N   LEU A 480    18069  19381  20845   -357  -2450   2562       N  
ATOM   2729  CA  LEU A 480      58.457  19.039  78.063  1.00151.60           C  
ANISOU 2729  CA  LEU A 480    17783  19161  20656   -358  -2395   2198       C  
ATOM   2730  C   LEU A 480      59.887  18.800  77.550  1.00144.51           C  
ANISOU 2730  C   LEU A 480    16821  18204  19882   -253  -2545   1944       C  
ATOM   2731  O   LEU A 480      60.094  18.544  76.368  1.00146.12           O  
ANISOU 2731  O   LEU A 480    16961  18274  20282   -228  -2569   1713       O  
ATOM   2732  CB  LEU A 480      58.208  20.536  78.212  1.00154.93           C  
ANISOU 2732  CB  LEU A 480    18269  19849  20746   -399  -2193   2092       C  
ATOM   2733  CG  LEU A 480      56.887  20.944  78.894  1.00158.81           C  
ANISOU 2733  CG  LEU A 480    18818  20450  21069   -488  -2025   2327       C  
ATOM   2734  CD1 LEU A 480      56.809  22.461  79.012  1.00159.23           C  
ANISOU 2734  CD1 LEU A 480    18933  20755  20811   -505  -1847   2178       C  
ATOM   2735  CD2 LEU A 480      55.642  20.416  78.214  1.00158.99           C  
ANISOU 2735  CD2 LEU A 480    18780  20299  21327   -564  -1979   2394       C  
ATOM   2736  N   ILE A 481      60.870  18.905  78.440  1.00139.71           N  
ANISOU 2736  N   ILE A 481    16225  17704  19152   -178  -2646   1969       N  
ATOM   2737  CA  ILE A 481      62.261  18.677  78.068  1.00140.42           C  
ANISOU 2737  CA  ILE A 481    16221  17744  19387    -74  -2792   1725       C  
ATOM   2738  C   ILE A 481      62.958  17.702  79.010  1.00150.49           C  
ANISOU 2738  C   ILE A 481    17489  18938  20753     34  -3041   1907       C  
ATOM   2739  O   ILE A 481      62.837  17.819  80.231  1.00158.79           O  
ANISOU 2739  O   ILE A 481    18634  20119  21578     57  -3078   2144       O  
ATOM   2740  CB  ILE A 481      63.056  19.984  78.010  1.00134.96           C  
ANISOU 2740  CB  ILE A 481    15508  17270  18500    -68  -2684   1451       C  
ATOM   2741  CG1 ILE A 481      62.338  20.961  77.078  1.00134.89           C  
ANISOU 2741  CG1 ILE A 481    15537  17323  18391   -159  -2432   1304       C  
ATOM   2742  CG2 ILE A 481      64.483  19.717  77.541  1.00133.57           C  
ANISOU 2742  CG2 ILE A 481    15195  17023  18532     30  -2808   1178       C  
ATOM   2743  CD1 ILE A 481      63.070  22.267  76.782  1.00134.43           C  
ANISOU 2743  CD1 ILE A 481    15457  17423  18198   -169  -2277   1023       C  
ATOM   2744  N   ASP A 482      63.694  16.754  78.440  1.00157.54           N  
ANISOU 2744  N   ASP A 482    18279  19620  21959    120  -3214   1790       N  
ATOM   2745  CA  ASP A 482      64.408  15.758  79.237  1.00166.91           C  
ANISOU 2745  CA  ASP A 482    19454  20694  23269    248  -3478   1950       C  
ATOM   2746  C   ASP A 482      65.644  16.376  79.886  1.00162.26           C  
ANISOU 2746  C   ASP A 482    18822  20302  22527    355  -3590   1787       C  
ATOM   2747  O   ASP A 482      66.328  17.192  79.266  1.00157.40           O  
ANISOU 2747  O   ASP A 482    18101  19789  21912    346  -3503   1445       O  
ATOM   2748  CB  ASP A 482      64.805  14.561  78.371  1.00176.16           C  
ANISOU 2748  CB  ASP A 482    20514  21562  24854    316  -3634   1843       C  
ATOM   2749  CG  ASP A 482      65.502  13.449  79.168  1.00183.41           C  
ANISOU 2749  CG  ASP A 482    21426  22323  25935    465  -3923   2029       C  
ATOM   2750  OD1 ASP A 482      65.322  13.366  80.409  1.00189.12           O  
ANISOU 2750  OD1 ASP A 482    22276  23125  26453    501  -3992   2349       O  
ATOM   2751  OD2 ASP A 482      66.241  12.649  78.549  1.00186.08           O  
ANISOU 2751  OD2 ASP A 482    21643  22458  26600    563  -4083   1854       O  
ATOM   2752  N   ARG A 483      65.909  15.963  81.125  1.00161.45           N  
ANISOU 2752  N   ARG A 483    18799  20238  22304    462  -3782   2034       N  
ATOM   2753  CA  ARG A 483      67.080  16.364  81.887  1.00162.34           C  
ANISOU 2753  CA  ARG A 483    18869  20520  22293    600  -3968   1895       C  
ATOM   2754  C   ARG A 483      68.340  16.307  81.068  1.00159.56           C  
ANISOU 2754  C   ARG A 483    18296  20092  22235    673  -4068   1500       C  
ATOM   2755  O   ARG A 483      69.089  17.279  80.999  1.00156.96           O  
ANISOU 2755  O   ARG A 483    17860  19936  21841    672  -4023   1197       O  
ATOM   2756  CB  ARG A 483      67.286  15.428  83.065  1.00171.36           C  
ANISOU 2756  CB  ARG A 483    20123  21604  23382    761  -4238   2223       C  
ATOM   2757  CG  ARG A 483      66.792  16.005  84.357  1.00180.09           C  
ANISOU 2757  CG  ARG A 483    21424  22956  24043    779  -4205   2477       C  
ATOM   2758  CD  ARG A 483      66.999  14.909  85.422  1.00190.65           C  
ANISOU 2758  CD  ARG A 483    22903  24194  25341    965  -4473   2839       C  
ATOM   2759  NE  ARG A 483      66.672  15.411  86.742  1.00200.39           N  
ANISOU 2759  NE  ARG A 483    24347  25686  26105   1032  -4469   3076       N  
ATOM   2760  CZ  ARG A 483      65.855  14.804  87.644  1.00209.60           C  
ANISOU 2760  CZ  ARG A 483    25746  26819  27071   1066  -4431   3558       C  
ATOM   2761  NH1 ARG A 483      65.215  13.671  87.351  1.00211.08           N  
ANISOU 2761  NH1 ARG A 483    25970  26697  27534   1011  -4382   3866       N  
ATOM   2762  NH2 ARG A 483      65.645  15.402  88.806  1.00215.86           N  
ANISOU 2762  NH2 ARG A 483    26730  27891  27393   1144  -4413   3714       N  
ATOM   2763  N   LYS A 484      68.528  15.162  80.419  1.00163.02           N  
ANISOU 2763  N   LYS A 484    18660  20256  23022    728  -4184   1499       N  
ATOM   2764  CA  LYS A 484      69.723  14.868  79.602  1.00167.05           C  
ANISOU 2764  CA  LYS A 484    18952  20655  23863    820  -4285   1138       C  
ATOM   2765  C   LYS A 484      69.982  15.975  78.580  1.00163.18           C  
ANISOU 2765  C   LYS A 484    18347  20285  23365    712  -4012    764       C  
ATOM   2766  O   LYS A 484      71.132  16.328  78.311  1.00164.45           O  
ANISOU 2766  O   LYS A 484    18324  20495  23664    773  -4040    440       O  
ATOM   2767  CB  LYS A 484      69.609  13.518  78.866  1.00170.42           C  
ANISOU 2767  CB  LYS A 484    19335  20753  24661    868  -4389   1182       C  
ATOM   2768  CG  LYS A 484      69.288  12.277  79.695  1.00176.32           C  
ANISOU 2768  CG  LYS A 484    20197  21298  25498    964  -4630   1575       C  
ATOM   2769  CD  LYS A 484      70.242  11.976  80.837  1.00180.08           C  
ANISOU 2769  CD  LYS A 484    20673  21823  25926   1163  -4940   1663       C  
ATOM   2770  CE  LYS A 484      69.607  10.922  81.727  1.00181.08           C  
ANISOU 2770  CE  LYS A 484    20992  21770  26039   1227  -5092   2149       C  
ATOM   2771  NZ  LYS A 484      70.505  10.402  82.795  1.00183.11           N  
ANISOU 2771  NZ  LYS A 484    21283  22021  26267   1466  -5438   2277       N  
ATOM   2772  N   SER A 485      68.906  16.500  78.001  1.00157.17           N  
ANISOU 2772  N   SER A 485    17693  19559  22462    558  -3743    816       N  
ATOM   2773  CA  SER A 485      69.009  17.586  77.036  1.00153.90           C  
ANISOU 2773  CA  SER A 485    17224  19251  21998    461  -3459    518       C  
ATOM   2774  C   SER A 485      69.549  18.846  77.708  1.00146.29           C  
ANISOU 2774  C   SER A 485    16226  18536  20818    434  -3393    389       C  
ATOM   2775  O   SER A 485      70.524  19.440  77.253  1.00140.77           O  
ANISOU 2775  O   SER A 485    15366  17884  20235    441  -3310     67       O  
ATOM   2776  CB  SER A 485      67.646  17.869  76.405  1.00157.07           C  
ANISOU 2776  CB  SER A 485    17772  19641  22264    327  -3228    636       C  
ATOM   2777  OG  SER A 485      66.959  16.654  76.108  1.00160.60           O  
ANISOU 2777  OG  SER A 485    18261  19859  22900    345  -3338    816       O  
ATOM   2778  N   LYS A 486      68.911  19.237  78.798  1.00144.22           N  
ANISOU 2778  N   LYS A 486    16108  18426  20260    404  -3421    633       N  
ATOM   2779  CA  LYS A 486      69.295  20.417  79.559  1.00149.05           C  
ANISOU 2779  CA  LYS A 486    16709  19277  20646    386  -3387    520       C  
ATOM   2780  C   LYS A 486      70.747  20.355  80.043  1.00154.03           C  
ANISOU 2780  C   LYS A 486    17147  19941  21433    520  -3629    287       C  
ATOM   2781  O   LYS A 486      71.467  21.360  80.028  1.00155.62           O  
ANISOU 2781  O   LYS A 486    17218  20265  21646    490  -3549     -3       O  
ATOM   2782  CB  LYS A 486      68.334  20.597  80.736  1.00153.38           C  
ANISOU 2782  CB  LYS A 486    17461  19971  20843    370  -3417    851       C  
ATOM   2783  CG  LYS A 486      66.914  20.919  80.303  1.00154.91           C  
ANISOU 2783  CG  LYS A 486    17805  20167  20886    225  -3152   1026       C  
ATOM   2784  CD  LYS A 486      65.999  21.236  81.477  1.00159.79           C  
ANISOU 2784  CD  LYS A 486    18604  20954  21154    205  -3131   1321       C  
ATOM   2785  CE  LYS A 486      65.503  19.990  82.205  1.00163.15           C  
ANISOU 2785  CE  LYS A 486    19141  21270  21575    277  -3301   1708       C  
ATOM   2786  NZ  LYS A 486      64.417  19.301  81.461  1.00160.90           N  
ANISOU 2786  NZ  LYS A 486    18895  20787  21451    180  -3175   1890       N  
ATOM   2787  N   GLU A 487      71.162  19.161  80.463  1.00161.35           N  
ANISOU 2787  N   GLU A 487    18049  20742  22512    672  -3930    411       N  
ATOM   2788  CA  GLU A 487      72.525  18.924  80.937  1.00169.83           C  
ANISOU 2788  CA  GLU A 487    18932  21826  23768    835  -4217    201       C  
ATOM   2789  C   GLU A 487      73.514  19.037  79.777  1.00169.55           C  
ANISOU 2789  C   GLU A 487    18633  21688  24101    821  -4103   -197       C  
ATOM   2790  O   GLU A 487      74.556  19.678  79.897  1.00177.38           O  
ANISOU 2790  O   GLU A 487    19416  22768  25210    848  -4138   -513       O  
ATOM   2791  CB  GLU A 487      72.630  17.544  81.607  1.00178.23           C  
ANISOU 2791  CB  GLU A 487    20061  22748  24908   1017  -4562    470       C  
ATOM   2792  CG  GLU A 487      71.838  17.406  82.913  1.00183.87           C  
ANISOU 2792  CG  GLU A 487    21039  23576  25246   1067  -4684    875       C  
ATOM   2793  CD  GLU A 487      71.733  15.972  83.420  1.00190.47           C  
ANISOU 2793  CD  GLU A 487    21985  24216  26167   1223  -4953   1215       C  
ATOM   2794  OE1 GLU A 487      72.613  15.147  83.088  1.00198.01           O  
ANISOU 2794  OE1 GLU A 487    22782  24990  27462   1355  -5167   1083       O  
ATOM   2795  OE2 GLU A 487      70.801  15.670  84.196  1.00192.34           O  
ANISOU 2795  OE2 GLU A 487    22465  24474  26140   1223  -4949   1620       O  
ATOM   2796  N   PHE A 488      73.182  18.387  78.665  1.00161.80           N  
ANISOU 2796  N   PHE A 488    17653  20513  23309    784  -3968   -190       N  
ATOM   2797  CA  PHE A 488      73.980  18.475  77.450  1.00157.98           C  
ANISOU 2797  CA  PHE A 488    16957  19934  23132    771  -3798   -545       C  
ATOM   2798  C   PHE A 488      74.202  19.940  77.046  1.00152.82           C  
ANISOU 2798  C   PHE A 488    16234  19434  22394    629  -3474   -796       C  
ATOM   2799  O   PHE A 488      75.331  20.363  76.782  1.00153.13           O  
ANISOU 2799  O   PHE A 488    16031  19488  22664    646  -3424  -1127       O  
ATOM   2800  CB  PHE A 488      73.327  17.705  76.305  1.00152.70           C  
ANISOU 2800  CB  PHE A 488    16366  19069  22581    745  -3667   -483       C  
ATOM   2801  CG  PHE A 488      74.058  17.839  75.001  1.00151.67           C  
ANISOU 2801  CG  PHE A 488    16060  18863  22702    742  -3446   -837       C  
ATOM   2802  CD1 PHE A 488      75.186  17.073  74.736  1.00155.53           C  
ANISOU 2802  CD1 PHE A 488    16320  19224  23549    885  -3605  -1061       C  
ATOM   2803  CD2 PHE A 488      73.627  18.736  74.041  1.00150.20           C  
ANISOU 2803  CD2 PHE A 488    15945  18734  22388    610  -3070   -943       C  
ATOM   2804  CE1 PHE A 488      75.871  17.207  73.532  1.00155.20           C  
ANISOU 2804  CE1 PHE A 488    16115  19124  23729    888  -3363  -1391       C  
ATOM   2805  CE2 PHE A 488      74.289  18.866  72.833  1.00150.36           C  
ANISOU 2805  CE2 PHE A 488    15834  18691  22602    620  -2832  -1246       C  
ATOM   2806  CZ  PHE A 488      75.415  18.097  72.579  1.00151.26           C  
ANISOU 2806  CZ  PHE A 488    15713  18689  23070    755  -2966  -1473       C  
ATOM   2807  N   LEU A 489      73.118  20.700  77.035  1.00145.47           N  
ANISOU 2807  N   LEU A 489    15510  18604  21158    492  -3255   -633       N  
ATOM   2808  CA  LEU A 489      73.176  22.106  76.701  1.00142.94           C  
ANISOU 2808  CA  LEU A 489    15165  18406  20737    357  -2944   -820       C  
ATOM   2809  C   LEU A 489      74.024  22.906  77.680  1.00145.76           C  
ANISOU 2809  C   LEU A 489    15372  18915  21093    371  -3063   -999       C  
ATOM   2810  O   LEU A 489      74.802  23.769  77.267  1.00143.45           O  
ANISOU 2810  O   LEU A 489    14899  18643  20963    305  -2871  -1302       O  
ATOM   2811  CB  LEU A 489      71.776  22.695  76.656  1.00136.40           C  
ANISOU 2811  CB  LEU A 489    14596  17653  19574    234  -2743   -584       C  
ATOM   2812  CG  LEU A 489      71.728  24.145  76.174  1.00130.81           C  
ANISOU 2812  CG  LEU A 489    13897  17037  18769     98  -2396   -755       C  
ATOM   2813  CD1 LEU A 489      72.383  24.307  74.808  1.00129.41           C  
ANISOU 2813  CD1 LEU A 489    13599  16744  18828     76  -2126  -1017       C  
ATOM   2814  CD2 LEU A 489      70.295  24.602  76.147  1.00127.46           C  
ANISOU 2814  CD2 LEU A 489    13725  16673  18029      6  -2240   -512       C  
ATOM   2815  N   SER A 490      73.877  22.612  78.971  1.00149.29           N  
ANISOU 2815  N   SER A 490    15896  19461  21363    463  -3378   -816       N  
ATOM   2816  CA  SER A 490      74.682  23.271  79.994  1.00154.92           C  
ANISOU 2816  CA  SER A 490    16474  20328  22057    516  -3566  -1002       C  
ATOM   2817  C   SER A 490      76.156  23.028  79.738  1.00158.62           C  
ANISOU 2817  C   SER A 490    16610  20717  22942    606  -3695  -1355       C  
ATOM   2818  O   SER A 490      76.988  23.923  79.899  1.00157.08           O  
ANISOU 2818  O   SER A 490    16201  20595  22887    569  -3659  -1672       O  
ATOM   2819  CB  SER A 490      74.358  22.734  81.383  1.00163.60           C  
ANISOU 2819  CB  SER A 490    17732  21535  22891    659  -3926   -731       C  
ATOM   2820  OG  SER A 490      72.971  22.758  81.631  1.00172.61           O  
ANISOU 2820  OG  SER A 490    19168  22730  23684    587  -3806   -375       O  
ATOM   2821  N   LYS A 491      76.468  21.800  79.328  1.00165.35           N  
ANISOU 2821  N   LYS A 491    17401  21405  24020    723  -3844  -1312       N  
ATOM   2822  CA  LYS A 491      77.835  21.400  79.013  1.00172.30           C  
ANISOU 2822  CA  LYS A 491    17951  22186  25327    828  -3970  -1641       C  
ATOM   2823  C   LYS A 491      78.385  22.196  77.840  1.00168.49           C  
ANISOU 2823  C   LYS A 491    17266  21653  25096    686  -3563  -1970       C  
ATOM   2824  O   LYS A 491      79.416  22.857  77.969  1.00169.85           O  
ANISOU 2824  O   LYS A 491    17158  21867  25510    672  -3551  -2304       O  
ATOM   2825  CB  LYS A 491      77.908  19.889  78.708  1.00178.10           C  
ANISOU 2825  CB  LYS A 491    18693  22730  26247    980  -4180  -1507       C  
ATOM   2826  CG  LYS A 491      79.234  19.290  78.217  1.00187.67           C  
ANISOU 2826  CG  LYS A 491    19566  23807  27930   1107  -4292  -1836       C  
ATOM   2827  CD  LYS A 491      78.951  17.952  77.488  1.00191.81           C  
ANISOU 2827  CD  LYS A 491    20161  24111  28606   1193  -4336  -1694       C  
ATOM   2828  CE  LYS A 491      80.048  17.456  76.524  1.00195.54           C  
ANISOU 2828  CE  LYS A 491    20324  24431  29540   1273  -4277  -2044       C  
ATOM   2829  NZ  LYS A 491      79.465  16.526  75.505  1.00191.17           N  
ANISOU 2829  NZ  LYS A 491    19896  23688  29049   1285  -4159  -1933       N  
ATOM   2830  N   LYS A 492      77.704  22.137  76.693  1.00160.65           N  
ANISOU 2830  N   LYS A 492    16415  20567  24056    586  -3227  -1880       N  
ATOM   2831  CA  LYS A 492      78.152  22.851  75.496  1.00156.20           C  
ANISOU 2831  CA  LYS A 492    15714  19949  23683    467  -2798  -2145       C  
ATOM   2832  C   LYS A 492      78.293  24.364  75.719  1.00150.38           C  
ANISOU 2832  C   LYS A 492    14922  19330  22882    311  -2561  -2298       C  
ATOM   2833  O   LYS A 492      79.331  24.962  75.389  1.00152.11           O  
ANISOU 2833  O   LYS A 492    14858  19521  23413    261  -2389  -2626       O  
ATOM   2834  CB  LYS A 492      77.228  22.551  74.323  1.00155.57           C  
ANISOU 2834  CB  LYS A 492    15864  19776  23467    416  -2518  -1986       C  
ATOM   2835  CG  LYS A 492      77.349  21.119  73.798  1.00161.47           C  
ANISOU 2835  CG  LYS A 492    16587  20360  24401    562  -2683  -1957       C  
ATOM   2836  CD  LYS A 492      78.643  20.903  73.000  1.00170.92           C  
ANISOU 2836  CD  LYS A 492    17473  21459  26009    625  -2560  -2320       C  
ATOM   2837  CE  LYS A 492      79.022  19.420  72.866  1.00181.51           C  
ANISOU 2837  CE  LYS A 492    18722  22644  27600    813  -2852  -2335       C  
ATOM   2838  NZ  LYS A 492      80.433  19.292  72.316  1.00185.88           N  
ANISOU 2838  NZ  LYS A 492    18912  23127  28587    887  -2764  -2726       N  
ATOM   2839  N   ILE A 493      77.254  24.957  76.301  1.00144.42           N  
ANISOU 2839  N   ILE A 493    14426  18695  21752    234  -2551  -2064       N  
ATOM   2840  CA  ILE A 493      77.266  26.370  76.660  1.00145.60           C  
ANISOU 2840  CA  ILE A 493    14553  18952  21816     99  -2373  -2186       C  
ATOM   2841  C   ILE A 493      78.440  26.728  77.547  1.00151.08           C  
ANISOU 2841  C   ILE A 493    14937  19707  22756    146  -2614  -2488       C  
ATOM   2842  O   ILE A 493      79.153  27.697  77.266  1.00151.18           O  
ANISOU 2842  O   ILE A 493    14732  19696  23011     35  -2381  -2782       O  
ATOM   2843  CB  ILE A 493      75.973  26.840  77.342  1.00145.01           C  
ANISOU 2843  CB  ILE A 493    14792  19010  21295     46  -2395  -1892       C  
ATOM   2844  CG1 ILE A 493      74.833  26.868  76.315  1.00145.87           C  
ANISOU 2844  CG1 ILE A 493    15166  19056  21200    -37  -2078  -1671       C  
ATOM   2845  CG2 ILE A 493      76.152  28.249  77.929  1.00144.25           C  
ANISOU 2845  CG2 ILE A 493    14633  19025  21151    -61  -2297  -2068       C  
ATOM   2846  CD1 ILE A 493      73.458  27.189  76.878  1.00144.07           C  
ANISOU 2846  CD1 ILE A 493    15236  18941  20561    -81  -2087  -1367       C  
ATOM   2847  N   GLU A 494      78.629  25.967  78.620  1.00157.09           N  
ANISOU 2847  N   GLU A 494    15683  20540  23463    316  -3079  -2418       N  
ATOM   2848  CA  GLU A 494      79.740  26.207  79.551  1.00164.56           C  
ANISOU 2848  CA  GLU A 494    16340  21559  24625    407  -3395  -2717       C  
ATOM   2849  C   GLU A 494      81.071  26.149  78.832  1.00162.91           C  
ANISOU 2849  C   GLU A 494    15729  21217  24950    406  -3293  -3100       C  
ATOM   2850  O   GLU A 494      81.943  26.998  79.047  1.00165.19           O  
ANISOU 2850  O   GLU A 494    15727  21524  25512    346  -3261  -3448       O  
ATOM   2851  CB  GLU A 494      79.763  25.111  80.614  1.00174.59           C  
ANISOU 2851  CB  GLU A 494    17685  22891  25758    640  -3919  -2542       C  
ATOM   2852  CG  GLU A 494      78.852  25.383  81.797  1.00182.38           C  
ANISOU 2852  CG  GLU A 494    18969  24065  26261    679  -4114  -2278       C  
ATOM   2853  CD  GLU A 494      79.543  26.230  82.849  1.00192.95           C  
ANISOU 2853  CD  GLU A 494    20139  25562  27609    730  -4357  -2569       C  
ATOM   2854  OE1 GLU A 494      79.630  25.781  84.009  1.00202.49           O  
ANISOU 2854  OE1 GLU A 494    21425  26894  28614    930  -4790  -2484       O  
ATOM   2855  OE2 GLU A 494      80.044  27.321  82.518  1.00195.89           O  
ANISOU 2855  OE2 GLU A 494    20296  25924  28208    582  -4126  -2895       O  
ATOM   2856  N   TYR A 495      81.232  25.138  77.982  1.00162.87           N  
ANISOU 2856  N   TYR A 495    15695  21071  25117    473  -3238  -3052       N  
ATOM   2857  CA  TYR A 495      82.428  25.015  77.147  1.00168.32           C  
ANISOU 2857  CA  TYR A 495    16015  21627  26311    473  -3073  -3401       C  
ATOM   2858  C   TYR A 495      82.692  26.289  76.376  1.00169.05           C  
ANISOU 2858  C   TYR A 495    15981  21681  26566    254  -2561  -3619       C  
ATOM   2859  O   TYR A 495      83.769  26.886  76.508  1.00173.74           O  
ANISOU 2859  O   TYR A 495    16208  22255  27548    211  -2527  -3983       O  
ATOM   2860  CB  TYR A 495      82.338  23.843  76.176  1.00170.74           C  
ANISOU 2860  CB  TYR A 495    16375  21788  26709    560  -2999  -3295       C  
ATOM   2861  CG  TYR A 495      83.469  23.773  75.178  1.00172.15           C  
ANISOU 2861  CG  TYR A 495    16202  21836  27370    551  -2738  -3645       C  
ATOM   2862  CD1 TYR A 495      84.665  23.139  75.499  1.00176.07           C  
ANISOU 2862  CD1 TYR A 495    16331  22283  28284    710  -3040  -3922       C  
ATOM   2863  CD2 TYR A 495      83.336  24.326  73.909  1.00170.92           C  
ANISOU 2863  CD2 TYR A 495    16087  21607  27245    399  -2184  -3693       C  
ATOM   2864  CE1 TYR A 495      85.704  23.060  74.587  1.00178.37           C  
ANISOU 2864  CE1 TYR A 495    16278  22456  29038    705  -2778  -4253       C  
ATOM   2865  CE2 TYR A 495      84.372  24.249  72.986  1.00173.32           C  
ANISOU 2865  CE2 TYR A 495    16078  21798  27976    398  -1903  -4002       C  
ATOM   2866  CZ  TYR A 495      85.549  23.618  73.332  1.00175.52           C  
ANISOU 2866  CZ  TYR A 495    15969  22030  28689    543  -2191  -4287       C  
ATOM   2867  OH  TYR A 495      86.572  23.540  72.422  1.00174.99           O  
ANISOU 2867  OH  TYR A 495    15572  21854  29063    542  -1889  -4602       O  
ATOM   2868  N   GLU A 496      81.716  26.694  75.566  1.00169.11           N  
ANISOU 2868  N   GLU A 496    16287  21666  26299    122  -2167  -3397       N  
ATOM   2869  CA  GLU A 496      81.811  27.918  74.758  1.00174.43           C  
ANISOU 2869  CA  GLU A 496    16919  22285  27068    -80  -1638  -3530       C  
ATOM   2870  C   GLU A 496      82.144  29.143  75.610  1.00175.36           C  
ANISOU 2870  C   GLU A 496    16885  22475  27267   -191  -1668  -3726       C  
ATOM   2871  O   GLU A 496      82.875  30.033  75.176  1.00175.94           O  
ANISOU 2871  O   GLU A 496    16711  22463  27674   -329  -1339  -3996       O  
ATOM   2872  CB  GLU A 496      80.483  28.175  74.043  1.00177.43           C  
ANISOU 2872  CB  GLU A 496    17718  22665  27029   -164  -1328  -3203       C  
ATOM   2873  CG  GLU A 496      80.188  27.218  72.892  1.00180.31           C  
ANISOU 2873  CG  GLU A 496    18221  22932  27355    -88  -1175  -3078       C  
ATOM   2874  CD  GLU A 496      81.187  27.321  71.762  1.00186.69           C  
ANISOU 2874  CD  GLU A 496    18785  23613  28534   -119   -786  -3349       C  
ATOM   2875  OE1 GLU A 496      81.616  28.459  71.445  1.00192.92           O  
ANISOU 2875  OE1 GLU A 496    19456  24365  29477   -270   -411  -3511       O  
ATOM   2876  OE2 GLU A 496      81.549  26.273  71.185  1.00184.49           O  
ANISOU 2876  OE2 GLU A 496    18431  23260  28405      8   -836  -3402       O  
ATOM   2877  N   ARG A 497      81.580  29.183  76.814  1.00174.41           N  
ANISOU 2877  N   ARG A 497    16921  22506  26841   -127  -2049  -3588       N  
ATOM   2878  CA  ARG A 497      81.725  30.317  77.719  1.00174.29           C  
ANISOU 2878  CA  ARG A 497    16816  22581  26825   -208  -2129  -3760       C  
ATOM   2879  C   ARG A 497      83.143  30.388  78.268  1.00177.42           C  
ANISOU 2879  C   ARG A 497    16747  22962  27702   -151  -2381  -4191       C  
ATOM   2880  O   ARG A 497      83.671  31.473  78.532  1.00171.75           O  
ANISOU 2880  O   ARG A 497    15803  22228  27225   -273  -2281  -4482       O  
ATOM   2881  CB  ARG A 497      80.759  30.155  78.880  1.00169.97           C  
ANISOU 2881  CB  ARG A 497    16573  22217  25788   -110  -2498  -3492       C  
ATOM   2882  CG  ARG A 497      80.656  31.362  79.780  1.00167.49           C  
ANISOU 2882  CG  ARG A 497    16250  22015  25373   -186  -2556  -3634       C  
ATOM   2883  CD  ARG A 497      80.174  30.949  81.139  1.00163.93           C  
ANISOU 2883  CD  ARG A 497    15984  21766  24535    -12  -3045  -3474       C  
ATOM   2884  NE  ARG A 497      79.524  32.059  81.815  1.00160.25           N  
ANISOU 2884  NE  ARG A 497    15678  21422  23787    -92  -3004  -3468       N  
ATOM   2885  CZ  ARG A 497      78.960  31.975  83.015  1.00158.41           C  
ANISOU 2885  CZ  ARG A 497    15650  21388  23148     37  -3346  -3327       C  
ATOM   2886  NH1 ARG A 497      78.959  30.822  83.688  1.00159.00           N  
ANISOU 2886  NH1 ARG A 497    15813  21554  23043    253  -3754  -3150       N  
ATOM   2887  NH2 ARG A 497      78.402  33.055  83.554  1.00154.53           N  
ANISOU 2887  NH2 ARG A 497    15285  21000  22427    -38  -3271  -3362       N  
ATOM   2888  N   ASN A 498      83.754  29.220  78.443  1.00182.74           N  
ANISOU 2888  N   ASN A 498    17265  23627  28541     39  -2723  -4242       N  
ATOM   2889  CA  ASN A 498      85.099  29.161  78.990  1.00188.03           C  
ANISOU 2889  CA  ASN A 498    17477  24286  29676    131  -3026  -4658       C  
ATOM   2890  C   ASN A 498      86.184  29.078  77.930  1.00189.28           C  
ANISOU 2890  C   ASN A 498    17246  24264  30406     65  -2702  -4957       C  
ATOM   2891  O   ASN A 498      87.365  28.944  78.258  1.00201.75           O  
ANISOU 2891  O   ASN A 498    18395  25813  32446    144  -2931  -5328       O  
ATOM   2892  CB  ASN A 498      85.179  28.044  80.031  1.00192.62           C  
ANISOU 2892  CB  ASN A 498    18107  24980  30097    409  -3658  -4561       C  
ATOM   2893  CG  ASN A 498      84.184  28.249  81.173  1.00194.52           C  
ANISOU 2893  CG  ASN A 498    18714  25415  29778    473  -3948  -4292       C  
ATOM   2894  OD1 ASN A 498      83.637  29.350  81.370  1.00190.96           O  
ANISOU 2894  OD1 ASN A 498    18392  25031  29131    320  -3750  -4283       O  
ATOM   2895  ND2 ASN A 498      83.936  27.183  81.925  1.00197.51           N  
ANISOU 2895  ND2 ASN A 498    19270  25878  29897    706  -4401  -4061       N  
ATOM   2896  N   ASN A 499      85.799  29.190  76.648  1.00183.23           N  
ANISOU 2896  N   ASN A 499    16622  23380  29614    -71  -2158  -4813       N  
ATOM   2897  CA  ASN A 499      86.750  29.010  75.558  1.00185.69           C  
ANISOU 2897  CA  ASN A 499    16614  23530  30410   -114  -1801  -5054       C  
ATOM   2898  C   ASN A 499      86.770  30.128  74.522  1.00185.84           C  
ANISOU 2898  C   ASN A 499    16616  23425  30568   -361  -1123  -5113       C  
ATOM   2899  O   ASN A 499      87.304  29.935  73.425  1.00191.50           O  
ANISOU 2899  O   ASN A 499    17185  24014  31562   -397   -724  -5213       O  
ATOM   2900  CB  ASN A 499      86.539  27.630  74.910  1.00183.85           C  
ANISOU 2900  CB  ASN A 499    16524  23254  30076     50  -1861  -4859       C  
ATOM   2901  CG  ASN A 499      87.027  26.487  75.792  1.00185.30           C  
ANISOU 2901  CG  ASN A 499    16559  23486  30361    305  -2486  -4921       C  
ATOM   2902  OD1 ASN A 499      86.572  26.323  76.925  1.00183.22           O  
ANISOU 2902  OD1 ASN A 499    16464  23352  29798    410  -2943  -4770       O  
ATOM   2903  ND2 ASN A 499      87.969  25.694  75.277  1.00187.50           N  
ANISOU 2903  ND2 ASN A 499    16525  23658  31057    418  -2502  -5143       N  
ATOM   2904  N   GLY A 500      86.250  31.310  74.871  1.00180.25           N  
ANISOU 2904  N   GLY A 500    16048  22749  29690   -523   -980  -5065       N  
ATOM   2905  CA  GLY A 500      86.255  32.442  73.973  1.00177.65           C  
ANISOU 2905  CA  GLY A 500    15722  22283  29495   -753   -349  -5099       C  
ATOM   2906  C   GLY A 500      85.288  32.327  72.800  1.00172.36           C  
ANISOU 2906  C   GLY A 500    15481  21571  28435   -786     84  -4739       C  
ATOM   2907  O   GLY A 500      85.467  32.944  71.755  1.00170.01           O  
ANISOU 2907  O   GLY A 500    15179  21136  28277   -923    655  -4758       O  
ATOM   2908  N   PHE A 501      84.266  31.494  72.990  1.00172.03           N  
ANISOU 2908  N   PHE A 501    15809  21646  27906   -645   -204  -4411       N  
ATOM   2909  CA  PHE A 501      83.188  31.296  72.022  1.00173.54           C  
ANISOU 2909  CA  PHE A 501    16434  21825  27677   -643     88  -4066       C  
ATOM   2910  C   PHE A 501      83.678  30.993  70.603  1.00173.70           C  
ANISOU 2910  C   PHE A 501    16395  21712  27887   -642    554  -4128       C  
ATOM   2911  O   PHE A 501      83.470  31.770  69.667  1.00166.94           O  
ANISOU 2911  O   PHE A 501    15687  20769  26971   -762   1082  -4060       O  
ATOM   2912  CB  PHE A 501      82.219  32.459  72.107  1.00176.26           C  
ANISOU 2912  CB  PHE A 501    17081  22193  27695   -786    304  -3873       C  
ATOM   2913  CG  PHE A 501      81.663  32.673  73.499  1.00178.36           C  
ANISOU 2913  CG  PHE A 501    17435  22611  27722   -761   -153  -3805       C  
ATOM   2914  CD1 PHE A 501      80.401  32.194  73.840  1.00175.08           C  
ANISOU 2914  CD1 PHE A 501    17404  22319  26799   -674   -387  -3459       C  
ATOM   2915  CD2 PHE A 501      82.414  33.327  74.480  1.00182.89           C  
ANISOU 2915  CD2 PHE A 501    17694  23207  28586   -813   -354  -4102       C  
ATOM   2916  CE1 PHE A 501      79.897  32.379  75.118  1.00172.87           C  
ANISOU 2916  CE1 PHE A 501    17213  22189  26279   -640   -772  -3389       C  
ATOM   2917  CE2 PHE A 501      81.909  33.513  75.757  1.00182.27           C  
ANISOU 2917  CE2 PHE A 501    17720  23288  28246   -763   -773  -4050       C  
ATOM   2918  CZ  PHE A 501      80.645  33.052  76.071  1.00174.78           C  
ANISOU 2918  CZ  PHE A 501    17175  22468  26764   -677   -961  -3682       C  
ATOM   2919  N   PRO A 502      84.372  29.856  70.455  1.00182.01           N  
ANISOU 2919  N   PRO A 502    17230  22747  29175   -491    358  -4267       N  
ATOM   2920  CA  PRO A 502      84.849  29.421  69.134  1.00187.29           C  
ANISOU 2920  CA  PRO A 502    17844  23310  30008   -453    768  -4345       C  
ATOM   2921  C   PRO A 502      83.756  29.312  68.086  1.00182.45           C  
ANISOU 2921  C   PRO A 502    17702  22695  28924   -428   1063  -4035       C  
ATOM   2922  O   PRO A 502      83.992  29.655  66.928  1.00188.13           O  
ANISOU 2922  O   PRO A 502    18462  23327  29689   -472   1593  -4069       O  
ATOM   2923  CB  PRO A 502      85.449  28.033  69.408  1.00192.13           C  
ANISOU 2923  CB  PRO A 502    18231  23932  30835   -249    342  -4480       C  
ATOM   2924  CG  PRO A 502      84.846  27.600  70.705  1.00190.13           C  
ANISOU 2924  CG  PRO A 502    18099  23799  30339   -159   -274  -4319       C  
ATOM   2925  CD  PRO A 502      84.716  28.866  71.493  1.00187.41           C  
ANISOU 2925  CD  PRO A 502    17735  23508  29961   -322   -260  -4347       C  
ATOM   2926  N   ILE A 503      82.569  28.853  68.502  1.00175.31           N  
ANISOU 2926  N   ILE A 503    17147  21888  27575   -352    723  -3740       N  
ATOM   2927  CA  ILE A 503      81.427  28.601  67.619  1.00171.87           C  
ANISOU 2927  CA  ILE A 503    17151  21462  26690   -299    886  -3457       C  
ATOM   2928  C   ILE A 503      81.025  29.822  66.786  1.00165.48           C  
ANISOU 2928  C   ILE A 503    16571  20608  25694   -432   1437  -3358       C  
ATOM   2929  O   ILE A 503      80.425  29.678  65.699  1.00164.43           O  
ANISOU 2929  O   ILE A 503    16743  20456  25277   -369   1702  -3212       O  
ATOM   2930  CB  ILE A 503      80.195  28.166  68.428  1.00173.77           C  
ANISOU 2930  CB  ILE A 503    17678  21808  26536   -243    438  -3166       C  
ATOM   2931  CG1 ILE A 503      79.068  27.692  67.488  1.00177.97           C  
ANISOU 2931  CG1 ILE A 503    18608  22337  26672   -161    540  -2921       C  
ATOM   2932  CG2 ILE A 503      79.700  29.291  69.341  1.00171.37           C  
ANISOU 2932  CG2 ILE A 503    17454  21579  26078   -384    392  -3070       C  
ATOM   2933  CD1 ILE A 503      78.065  26.754  68.153  1.00179.62           C  
ANISOU 2933  CD1 ILE A 503    19010  22610  26628    -64     60  -2682       C  
ATOM   2934  N   PHE A 504      81.364  31.015  67.280  1.00159.98           N  
ANISOU 2934  N   PHE A 504    15734  19886  25164   -603   1599  -3446       N  
ATOM   2935  CA  PHE A 504      81.028  32.243  66.584  1.00161.72           C  
ANISOU 2935  CA  PHE A 504    16162  20034  25248   -735   2117  -3344       C  
ATOM   2936  C   PHE A 504      81.821  32.417  65.253  1.00170.08           C  
ANISOU 2936  C   PHE A 504    17148  20965  26510   -746   2708  -3467       C  
ATOM   2937  O   PHE A 504      81.674  33.440  64.578  1.00179.75           O  
ANISOU 2937  O   PHE A 504    18541  22103  27652   -847   3199  -3378       O  
ATOM   2938  CB  PHE A 504      81.173  33.459  67.500  1.00160.25           C  
ANISOU 2938  CB  PHE A 504    15839  19831  25218   -914   2118  -3418       C  
ATOM   2939  CG  PHE A 504      80.107  33.575  68.577  1.00158.30           C  
ANISOU 2939  CG  PHE A 504    15801  19716  24628   -907   1688  -3226       C  
ATOM   2940  CD1 PHE A 504      78.785  33.221  68.362  1.00159.39           C  
ANISOU 2940  CD1 PHE A 504    16353  19937  24270   -819   1573  -2914       C  
ATOM   2941  CD2 PHE A 504      80.434  34.119  69.810  1.00159.23           C  
ANISOU 2941  CD2 PHE A 504    15692  19875  24932   -991   1420  -3378       C  
ATOM   2942  CE1 PHE A 504      77.810  33.362  69.359  1.00159.75           C  
ANISOU 2942  CE1 PHE A 504    16573  20104  24021   -819   1224  -2740       C  
ATOM   2943  CE2 PHE A 504      79.481  34.284  70.817  1.00159.08           C  
ANISOU 2943  CE2 PHE A 504    15868  19988  24584   -979   1064  -3212       C  
ATOM   2944  CZ  PHE A 504      78.168  33.901  70.592  1.00159.23           C  
ANISOU 2944  CZ  PHE A 504    16292  20088  24119   -898    983  -2884       C  
ATOM   2945  N   ASP A 505      82.640  31.422  64.884  1.00171.56           N  
ANISOU 2945  N   ASP A 505    17095  21136  26951   -631   2670  -3659       N  
ATOM   2946  CA  ASP A 505      83.287  31.344  63.571  1.00171.21           C  
ANISOU 2946  CA  ASP A 505    17022  21000  27027   -591   3204  -3760       C  
ATOM   2947  C   ASP A 505      82.842  30.058  62.864  1.00166.36           C  
ANISOU 2947  C   ASP A 505    16626  20447  26136   -364   3048  -3687       C  
ATOM   2948  O   ASP A 505      82.117  30.105  61.878  1.00159.87           O  
ANISOU 2948  O   ASP A 505    16192  19634  24915   -286   3305  -3504       O  
ATOM   2949  CB  ASP A 505      84.819  31.362  63.742  1.00174.93           C  
ANISOU 2949  CB  ASP A 505    16940  21383  28143   -661   3342  -4126       C  
ATOM   2950  CG  ASP A 505      85.260  32.071  65.018  1.00176.13           C  
ANISOU 2950  CG  ASP A 505    16762  21521  28638   -823   3094  -4281       C  
ATOM   2951  OD1 ASP A 505      84.792  33.191  65.274  1.00170.08           O  
ANISOU 2951  OD1 ASP A 505    16143  20723  27753   -974   3245  -4158       O  
ATOM   2952  OD2 ASP A 505      86.072  31.503  65.768  1.00183.76           O  
ANISOU 2952  OD2 ASP A 505    17325  22505  29988   -781   2727  -4538       O  
TER    2953      ASP A 505                                                      
ATOM   2954  N   LYS B 149      60.965  72.964 106.347  1.00227.71           N  
ANISOU 2954  N   LYS B 149    26906  31459  28152   1968  -3176 -14320       N  
ATOM   2955  CA  LYS B 149      61.044  74.336 105.781  1.00230.94           C  
ANISOU 2955  CA  LYS B 149    27108  31220  29416   1771  -3015 -14674       C  
ATOM   2956  C   LYS B 149      59.927  74.501 104.733  1.00228.75           C  
ANISOU 2956  C   LYS B 149    26981  30678  29252   1630  -2454 -14048       C  
ATOM   2957  O   LYS B 149      58.787  74.940 105.032  1.00228.98           O  
ANISOU 2957  O   LYS B 149    27203  30839  28959   1819  -2263 -14037       O  
ATOM   2958  CB  LYS B 149      62.450  74.610 105.195  1.00230.44           C  
ANISOU 2958  CB  LYS B 149    26669  30648  30237   1460  -3174 -14942       C  
ATOM   2959  CG  LYS B 149      63.604  74.223 106.110  1.00234.37           C  
ANISOU 2959  CG  LYS B 149    26998  31429  30621   1588  -3747 -15472       C  
ATOM   2960  CD  LYS B 149      64.943  74.184 105.374  1.00234.16           C  
ANISOU 2960  CD  LYS B 149    26596  30948  31426   1253  -3837 -15561       C  
ATOM   2961  CE  LYS B 149      66.006  73.542 106.244  1.00238.34           C  
ANISOU 2961  CE  LYS B 149    26984  31840  31734   1410  -4413 -15971       C  
ATOM   2962  NZ  LYS B 149      66.125  74.272 107.547  1.00246.42           N  
ANISOU 2962  NZ  LYS B 149    27982  33080  32567   1721  -4872 -16819       N  
ATOM   2963  N   LEU B 150      60.227  74.071 103.505  1.00230.94           N  
ANISOU 2963  N   LEU B 150    27182  30622  29943   1320  -2196 -13505       N  
ATOM   2964  CA  LEU B 150      59.239  74.011 102.443  1.00234.07           C  
ANISOU 2964  CA  LEU B 150    27736  30814  30384   1198  -1705 -12846       C  
ATOM   2965  C   LEU B 150      58.281  72.842 102.572  1.00236.08           C  
ANISOU 2965  C   LEU B 150    28271  31615  29811   1359  -1568 -12243       C  
ATOM   2966  O   LEU B 150      57.148  72.916 102.093  1.00237.36           O  
ANISOU 2966  O   LEU B 150    28600  31749  29835   1384  -1218 -11840       O  
ATOM   2967  CB  LEU B 150      59.933  73.894 101.103  1.00233.53           C  
ANISOU 2967  CB  LEU B 150    27507  30232  30991    834  -1489 -12482       C  
ATOM   2968  CG  LEU B 150      60.557  75.208 100.642  1.00236.69           C  
ANISOU 2968  CG  LEU B 150    27662  29947  32320    625  -1427 -12909       C  
ATOM   2969  CD1 LEU B 150      61.670  74.928  99.648  1.00237.58           C  
ANISOU 2969  CD1 LEU B 150    27553  29659  33054    287  -1343 -12706       C  
ATOM   2970  CD2 LEU B 150      59.491  76.089 100.005  1.00233.54           C  
ANISOU 2970  CD2 LEU B 150    27406  29190  32136    615  -1032 -12704       C  
ATOM   2971  N   LYS B 151      58.723  71.770 103.214  1.00239.78           N  
ANISOU 2971  N   LYS B 151    28785  32565  29753   1473  -1843 -12183       N  
ATOM   2972  CA  LYS B 151      57.925  70.582 103.468  1.00236.97           C  
ANISOU 2972  CA  LYS B 151    28685  32745  28606   1631  -1746 -11640       C  
ATOM   2973  C   LYS B 151      56.664  70.935 104.281  1.00233.16           C  
ANISOU 2973  C   LYS B 151    28421  32606  27563   1929  -1629 -11738       C  
ATOM   2974  O   LYS B 151      55.581  70.376 104.071  1.00232.92           O  
ANISOU 2974  O   LYS B 151    28580  32796  27121   1989  -1332 -11213       O  
ATOM   2975  CB  LYS B 151      58.783  69.541 104.213  1.00242.45           C  
ANISOU 2975  CB  LYS B 151    29379  33869  28871   1740  -2137 -11701       C  
ATOM   2976  CG  LYS B 151      60.168  69.282 103.590  1.00244.42           C  
ANISOU 2976  CG  LYS B 151    29363  33798  29707   1479  -2320 -11752       C  
ATOM   2977  CD  LYS B 151      61.335  70.002 104.301  1.00252.41           C  
ANISOU 2977  CD  LYS B 151    30126  34695  31083   1519  -2766 -12557       C  
ATOM   2978  CE  LYS B 151      62.278  70.705 103.314  1.00253.13           C  
ANISOU 2978  CE  LYS B 151    29886  34118  32173   1170  -2693 -12735       C  
ATOM   2979  NZ  LYS B 151      63.378  71.504 103.920  1.00256.87           N  
ANISOU 2979  NZ  LYS B 151    30067  34402  33127   1174  -3096 -13544       N  
ATOM   2980  N   LYS B 152      56.841  71.852 105.228  1.00230.10           N  
ANISOU 2980  N   LYS B 152    27987  32264  27175   2119  -1872 -12440       N  
ATOM   2981  CA  LYS B 152      55.741  72.304 106.050  1.00231.68           C  
ANISOU 2981  CA  LYS B 152    28371  32770  26885   2415  -1774 -12630       C  
ATOM   2982  C   LYS B 152      54.741  73.110 105.223  1.00225.00           C  
ANISOU 2982  C   LYS B 152    27532  31530  26424   2320  -1357 -12437       C  
ATOM   2983  O   LYS B 152      53.522  73.012 105.423  1.00224.77           O  
ANISOU 2983  O   LYS B 152    27682  31762  25958   2490  -1099 -12197       O  
ATOM   2984  CB  LYS B 152      56.309  73.095 107.231  1.00243.15           C  
ANISOU 2984  CB  LYS B 152    29757  34343  28284   2642  -2180 -13482       C  
ATOM   2985  CG  LYS B 152      57.127  72.218 108.179  1.00250.70           C  
ANISOU 2985  CG  LYS B 152    30763  35790  28701   2819  -2611 -13649       C  
ATOM   2986  CD  LYS B 152      58.415  72.911 108.614  1.00261.65           C  
ANISOU 2986  CD  LYS B 152    31899  36961  30555   2808  -3082 -14423       C  
ATOM   2987  CE  LYS B 152      59.519  71.991 109.055  1.00267.33           C  
ANISOU 2987  CE  LYS B 152    32569  37961  31043   2853  -3508 -14486       C  
ATOM   2988  NZ  LYS B 152      60.666  72.786 109.625  1.00275.89           N  
ANISOU 2988  NZ  LYS B 152    33393  38865  32564   2893  -3999 -15349       N  
ATOM   2989  N   VAL B 153      55.267  73.885 104.279  1.00219.98           N  
ANISOU 2989  N   VAL B 153    26702  30260  26619   2052  -1285 -12527       N  
ATOM   2990  CA  VAL B 153      54.411  74.634 103.356  1.00218.66           C  
ANISOU 2990  CA  VAL B 153    26551  29658  26871   1951   -900 -12296       C  
ATOM   2991  C   VAL B 153      53.590  73.662 102.512  1.00217.61           C  
ANISOU 2991  C   VAL B 153    26564  29644  26471   1872   -567 -11481       C  
ATOM   2992  O   VAL B 153      52.388  73.839 102.335  1.00221.47           O  
ANISOU 2992  O   VAL B 153    27175  30179  26792   1978   -288 -11244       O  
ATOM   2993  CB  VAL B 153      55.172  75.567 102.393  1.00215.91           C  
ANISOU 2993  CB  VAL B 153    25992  28573  27470   1660   -844 -12452       C  
ATOM   2994  CG1 VAL B 153      54.187  76.551 101.754  1.00215.36           C  
ANISOU 2994  CG1 VAL B 153    25977  28100  27749   1660   -506 -12359       C  
ATOM   2995  CG2 VAL B 153      56.249  76.344 103.118  1.00221.26           C  
ANISOU 2995  CG2 VAL B 153    26461  29090  28515   1671  -1215 -13239       C  
ATOM   2996  N   LEU B 154      54.248  72.623 102.010  1.00218.94           N  
ANISOU 2996  N   LEU B 154    26707  29866  26614   1695   -615 -11079       N  
ATOM   2997  CA  LEU B 154      53.571  71.597 101.226  1.00217.42           C  
ANISOU 2997  CA  LEU B 154    26639  29797  26171   1616   -344 -10331       C  
ATOM   2998  C   LEU B 154      52.516  70.863 102.044  1.00212.70           C  
ANISOU 2998  C   LEU B 154    26236  29805  24773   1876   -276 -10121       C  
ATOM   2999  O   LEU B 154      51.480  70.461 101.507  1.00207.51           O  
ANISOU 2999  O   LEU B 154    25681  29205  23957   1877     20  -9623       O  
ATOM   3000  CB  LEU B 154      54.563  70.582 100.663  1.00222.59           C  
ANISOU 3000  CB  LEU B 154    27222  30428  26923   1401   -449 -10006       C  
ATOM   3001  CG  LEU B 154      55.445  71.059  99.478  1.00228.30           C  
ANISOU 3001  CG  LEU B 154    27768  30524  28449   1089   -372  -9972       C  
ATOM   3002  CD1 LEU B 154      56.169  69.850  98.862  1.00223.28           C  
ANISOU 3002  CD1 LEU B 154    27096  29945  27795    907   -409  -9534       C  
ATOM   3003  CD2 LEU B 154      54.639  71.766  98.387  1.00229.67           C  
ANISOU 3003  CD2 LEU B 154    27995  30252  29017    995     -1  -9689       C  
ATOM   3004  N   ASP B 155      52.776  70.702 103.342  1.00213.86           N  
ANISOU 3004  N   ASP B 155    26434  30397  24424   2104   -548 -10510       N  
ATOM   3005  CA  ASP B 155      51.779  70.148 104.248  1.00216.03           C  
ANISOU 3005  CA  ASP B 155    26905  31245  23929   2378   -457 -10374       C  
ATOM   3006  C   ASP B 155      50.568  71.066 104.361  1.00220.48           C  
ANISOU 3006  C   ASP B 155    27515  31754  24501   2531   -194 -10516       C  
ATOM   3007  O   ASP B 155      49.424  70.605 104.357  1.00220.52           O  
ANISOU 3007  O   ASP B 155    27636  32013  24138   2628     85 -10126       O  
ATOM   3008  CB  ASP B 155      52.347  69.895 105.646  1.00219.49           C  
ANISOU 3008  CB  ASP B 155    27417  32161  23818   2625   -812 -10804       C  
ATOM   3009  CG  ASP B 155      53.369  68.789 105.678  1.00219.82           C  
ANISOU 3009  CG  ASP B 155    27448  32367  23704   2539  -1071 -10600       C  
ATOM   3010  OD1 ASP B 155      53.265  67.838 104.879  1.00216.00           O  
ANISOU 3010  OD1 ASP B 155    26983  31851  23234   2363   -906  -9985       O  
ATOM   3011  OD2 ASP B 155      54.292  68.870 106.512  1.00226.91           O  
ANISOU 3011  OD2 ASP B 155    28314  33426  24475   2659  -1461 -11077       O  
ATOM   3012  N   LYS B 156      50.817  72.368 104.463  1.00227.37           N  
ANISOU 3012  N   LYS B 156    28280  32281  25826   2552   -284 -11085       N  
ATOM   3013  CA  LYS B 156      49.729  73.358 104.513  1.00233.58           C  
ANISOU 3013  CA  LYS B 156    29091  32945  26712   2697    -51 -11268       C  
ATOM   3014  C   LYS B 156      48.903  73.358 103.221  1.00231.33           C  
ANISOU 3014  C   LYS B 156    28800  32317  26776   2534    308 -10711       C  
ATOM   3015  O   LYS B 156      47.708  73.597 103.244  1.00236.18           O  
ANISOU 3015  O   LYS B 156    29475  33020  27242   2679    560 -10601       O  
ATOM   3016  CB  LYS B 156      50.320  74.763 104.780  1.00240.27           C  
ANISOU 3016  CB  LYS B 156    29804  33402  28082   2718   -249 -12000       C  
ATOM   3017  CG  LYS B 156      49.318  75.913 104.879  1.00245.83           C  
ANISOU 3017  CG  LYS B 156    30518  33928  28959   2881    -53 -12282       C  
ATOM   3018  CD  LYS B 156      49.887  77.179 105.556  1.00253.96           C  
ANISOU 3018  CD  LYS B 156    31440  34729  30324   2985   -311 -13114       C  
ATOM   3019  CE  LYS B 156      50.258  78.295 104.578  1.00253.45           C  
ANISOU 3019  CE  LYS B 156    31217  33894  31189   2759   -251 -13258       C  
ATOM   3020  NZ  LYS B 156      50.360  79.627 105.247  1.00256.42           N  
ANISOU 3020  NZ  LYS B 156    31508  34045  31873   2912   -409 -14039       N  
ATOM   3021  N   LEU B 157      49.559  73.121 102.083  1.00227.40           N  
ANISOU 3021  N   LEU B 157    28224  31418  26757   2244    326 -10384       N  
ATOM   3022  CA  LEU B 157      48.896  73.200 100.788  1.00221.53           C  
ANISOU 3022  CA  LEU B 157    27486  30305  26378   2099    628  -9894       C  
ATOM   3023  C   LEU B 157      48.127  71.930 100.436  1.00214.50           C  
ANISOU 3023  C   LEU B 157    26695  29749  25054   2092    818  -9234       C  
ATOM   3024  O   LEU B 157      47.313  71.915  99.502  1.00211.50           O  
ANISOU 3024  O   LEU B 157    26338  29170  24851   2040   1067  -8832       O  
ATOM   3025  CB  LEU B 157      49.889  73.544  99.688  1.00221.36           C  
ANISOU 3025  CB  LEU B 157    27358  29700  27048   1807    601  -9826       C  
ATOM   3026  CG  LEU B 157      50.644  74.882  99.836  1.00228.49           C  
ANISOU 3026  CG  LEU B 157    28131  30146  28536   1764    460 -10444       C  
ATOM   3027  CD1 LEU B 157      51.323  75.230  98.532  1.00227.61           C  
ANISOU 3027  CD1 LEU B 157    27940  29411  29129   1473    570 -10230       C  
ATOM   3028  CD2 LEU B 157      49.786  76.065 100.296  1.00231.04           C  
ANISOU 3028  CD2 LEU B 157    28473  30362  28946   1980    541 -10848       C  
ATOM   3029  N   ARG B 158      48.375  70.877 101.193  1.00214.05           N  
ANISOU 3029  N   ARG B 158    26697  30190  24440   2156    688  -9136       N  
ATOM   3030  CA  ARG B 158      47.774  69.571 100.924  1.00214.98           C  
ANISOU 3030  CA  ARG B 158    26897  30620  24164   2131    846  -8518       C  
ATOM   3031  C   ARG B 158      46.259  69.613 101.078  1.00217.48           C  
ANISOU 3031  C   ARG B 158    27271  31144  24217   2309   1137  -8343       C  
ATOM   3032  O   ARG B 158      45.745  70.182 102.008  1.00221.53           O  
ANISOU 3032  O   ARG B 158    27812  31876  24479   2537   1161  -8711       O  
ATOM   3033  CB  ARG B 158      48.364  68.511 101.850  1.00218.14           C  
ANISOU 3033  CB  ARG B 158    27365  31509  24007   2196    639  -8492       C  
ATOM   3034  CG  ARG B 158      47.510  67.260 102.003  1.00218.70           C  
ANISOU 3034  CG  ARG B 158    27544  32006  23546   2257    826  -7953       C  
ATOM   3035  CD  ARG B 158      48.181  66.146 102.789  1.00221.73           C  
ANISOU 3035  CD  ARG B 158    28014  32813  23419   2305    619  -7855       C  
ATOM   3036  NE  ARG B 158      49.616  66.068 102.453  1.00220.43           N  
ANISOU 3036  NE  ARG B 158    27763  32409  23581   2130    318  -7993       N  
ATOM   3037  CZ  ARG B 158      50.626  66.214 103.308  1.00222.25           C  
ANISOU 3037  CZ  ARG B 158    27987  32779  23678   2219    -18  -8439       C  
ATOM   3038  NH1 ARG B 158      50.415  66.397 104.619  1.00229.23           N  
ANISOU 3038  NH1 ARG B 158    28982  34078  24033   2502   -124  -8793       N  
ATOM   3039  NH2 ARG B 158      51.867  66.160 102.846  1.00219.15           N  
ANISOU 3039  NH2 ARG B 158    27471  32114  23680   2033   -255  -8540       N  
ATOM   3040  N   LEU B 159      45.553  68.995 100.153  1.00214.41           N  
ANISOU 3040  N   LEU B 159    26885  30684  23894   2209   1354  -7795       N  
ATOM   3041  CA  LEU B 159      44.105  68.856 100.290  1.00210.43           C  
ANISOU 3041  CA  LEU B 159    26402  30407  23142   2367   1629  -7589       C  
ATOM   3042  C   LEU B 159      43.770  67.743 101.264  1.00206.00           C  
ANISOU 3042  C   LEU B 159    25920  30437  21911   2486   1674  -7401       C  
ATOM   3043  O   LEU B 159      44.566  66.846 101.520  1.00199.70           O  
ANISOU 3043  O   LEU B 159    25174  29832  20870   2409   1512  -7257       O  
ATOM   3044  CB  LEU B 159      43.449  68.602  98.933  1.00209.41           C  
ANISOU 3044  CB  LEU B 159    26234  29982  23349   2231   1818  -7095       C  
ATOM   3045  CG  LEU B 159      43.697  69.633  97.824  1.00210.63           C  
ANISOU 3045  CG  LEU B 159    26348  29528  24151   2121   1816  -7176       C  
ATOM   3046  CD1 LEU B 159      42.704  69.421  96.696  1.00211.96           C  
ANISOU 3046  CD1 LEU B 159    26505  29513  24516   2090   2020  -6723       C  
ATOM   3047  CD2 LEU B 159      43.586  71.045  98.322  1.00210.35           C  
ANISOU 3047  CD2 LEU B 159    26288  29307  24327   2273   1796  -7732       C  
ATOM   3048  N   LYS B 160      42.572  67.839 101.818  1.00206.06           N  
ANISOU 3048  N   LYS B 160    25937  30720  21634   2684   1909  -7409       N  
ATOM   3049  CA  LYS B 160      42.081  66.934 102.859  1.00208.45           C  
ANISOU 3049  CA  LYS B 160    26326  31591  21281   2835   2026  -7258       C  
ATOM   3050  C   LYS B 160      40.993  66.052 102.287  1.00202.87           C  
ANISOU 3050  C   LYS B 160    25570  30972  20540   2774   2316  -6691       C  
ATOM   3051  O   LYS B 160      40.086  66.557 101.630  1.00201.64           O  
ANISOU 3051  O   LYS B 160    25311  30592  20709   2784   2497  -6634       O  
ATOM   3052  CB  LYS B 160      41.512  67.731 104.038  1.00218.04           C  
ANISOU 3052  CB  LYS B 160    27581  33088  22176   3128   2113  -7737       C  
ATOM   3053  CG  LYS B 160      42.453  68.769 104.648  1.00225.35           C  
ANISOU 3053  CG  LYS B 160    28535  33910  23177   3222   1822  -8392       C  
ATOM   3054  CD  LYS B 160      43.627  68.163 105.419  1.00228.26           C  
ANISOU 3054  CD  LYS B 160    29016  34551  23159   3235   1520  -8510       C  
ATOM   3055  CE  LYS B 160      44.803  69.133 105.549  1.00229.25           C  
ANISOU 3055  CE  LYS B 160    29098  34391  23613   3216   1168  -9097       C  
ATOM   3056  NZ  LYS B 160      46.111  68.417 105.618  1.00227.14           N  
ANISOU 3056  NZ  LYS B 160    28861  34169  23271   3092    848  -9048       N  
ATOM   3057  N   ARG B 161      41.098  64.742 102.524  1.00199.63           N  
ANISOU 3057  N   ARG B 161    25223  30864  19762   2715   2342  -6285       N  
ATOM   3058  CA  ARG B 161      40.308  63.766 101.787  1.00198.03           C  
ANISOU 3058  CA  ARG B 161    24950  30661  19631   2591   2555  -5716       C  
ATOM   3059  C   ARG B 161      38.813  63.853 102.054  1.00196.86           C  
ANISOU 3059  C   ARG B 161    24718  30703  19377   2738   2907  -5637       C  
ATOM   3060  O   ARG B 161      37.999  63.349 101.271  1.00196.97           O  
ANISOU 3060  O   ARG B 161    24616  30617  19606   2644   3083  -5254       O  
ATOM   3061  CB  ARG B 161      40.858  62.324 101.980  1.00202.72           C  
ANISOU 3061  CB  ARG B 161    25631  31496  19894   2484   2484  -5305       C  
ATOM   3062  CG  ARG B 161      40.311  61.420 103.095  1.00210.12           C  
ANISOU 3062  CG  ARG B 161    26664  32952  20218   2625   2683  -5097       C  
ATOM   3063  CD  ARG B 161      40.878  60.014 102.922  1.00214.17           C  
ANISOU 3063  CD  ARG B 161    27242  33554  20577   2471   2593  -4629       C  
ATOM   3064  NE  ARG B 161      40.292  58.995 103.816  1.00220.77           N  
ANISOU 3064  NE  ARG B 161    28171  34828  20883   2571   2826  -4308       N  
ATOM   3065  CZ  ARG B 161      40.766  57.745 104.020  1.00224.56           C  
ANISOU 3065  CZ  ARG B 161    28754  35471  21095   2501   2763  -3927       C  
ATOM   3066  NH1 ARG B 161      41.873  57.313 103.406  1.00223.06           N  
ANISOU 3066  NH1 ARG B 161    28579  35063  21108   2335   2456  -3832       N  
ATOM   3067  NH2 ARG B 161      40.130  56.934 104.865  1.00229.60           N  
ANISOU 3067  NH2 ARG B 161    29485  36487  21263   2608   3026  -3639       N  
ATOM   3068  N   LYS B 162      38.457  64.468 103.184  1.00199.35           N  
ANISOU 3068  N   LYS B 162    25083  31306  19355   2979   3006  -6016       N  
ATOM   3069  CA  LYS B 162      37.050  64.690 103.520  1.00206.00           C  
ANISOU 3069  CA  LYS B 162    25826  32333  20110   3143   3359  -6017       C  
ATOM   3070  C   LYS B 162      36.485  65.774 102.614  1.00211.10           C  
ANISOU 3070  C   LYS B 162    26320  32555  21333   3147   3384  -6199       C  
ATOM   3071  O   LYS B 162      35.450  65.579 101.950  1.00216.40           O  
ANISOU 3071  O   LYS B 162    26839  33131  22251   3118   3591  -5928       O  
ATOM   3072  CB  LYS B 162      36.949  65.064 104.998  1.00209.65           C  
ANISOU 3072  CB  LYS B 162    26408  33226  20022   3415   3443  -6404       C  
ATOM   3073  CG  LYS B 162      35.561  65.240 105.596  1.00210.38           C  
ANISOU 3073  CG  LYS B 162    26415  33599  19919   3618   3843  -6440       C  
ATOM   3074  CD  LYS B 162      35.648  66.502 106.434  1.00211.62           C  
ANISOU 3074  CD  LYS B 162    26631  33829  19944   3872   3784  -7091       C  
ATOM   3075  CE  LYS B 162      34.625  66.563 107.539  1.00216.12           C  
ANISOU 3075  CE  LYS B 162    27211  34853  20050   4137   4149  -7218       C  
ATOM   3076  NZ  LYS B 162      33.246  66.938 107.093  1.00216.46           N  
ANISOU 3076  NZ  LYS B 162    27018  34790  20434   4187   4479  -7166       N  
ATOM   3077  N   ASP B 163      37.178  66.917 102.594  1.00214.98           N  
ANISOU 3077  N   ASP B 163    26850  32778  22052   3190   3161  -6665       N  
ATOM   3078  CA  ASP B 163      36.836  68.046 101.722  1.00217.73           C  
ANISOU 3078  CA  ASP B 163    27093  32661  22971   3197   3143  -6858       C  
ATOM   3079  C   ASP B 163      36.738  67.547 100.285  1.00209.49           C  
ANISOU 3079  C   ASP B 163    25976  31270  22349   2979   3123  -6390       C  
ATOM   3080  O   ASP B 163      35.758  67.831  99.572  1.00214.51           O  
ANISOU 3080  O   ASP B 163    26488  31715  23299   3015   3265  -6271       O  
ATOM   3081  CB  ASP B 163      37.943  69.123 101.719  1.00223.09           C  
ANISOU 3081  CB  ASP B 163    27840  33019  23904   3186   2856  -7331       C  
ATOM   3082  CG  ASP B 163      37.941  69.998 102.979  1.00234.94           C  
ANISOU 3082  CG  ASP B 163    29389  34745  25131   3439   2842  -7925       C  
ATOM   3083  OD1 ASP B 163      36.978  70.787 103.177  1.00240.87           O  
ANISOU 3083  OD1 ASP B 163    30061  35482  25973   3629   3022  -8164       O  
ATOM   3084  OD2 ASP B 163      38.925  69.922 103.761  1.00239.82           O  
ANISOU 3084  OD2 ASP B 163    30121  35545  25455   3461   2631  -8180       O  
ATOM   3085  N   ILE B 164      37.772  66.817  99.876  1.00199.23           N  
ANISOU 3085  N   ILE B 164    24753  29894  21048   2773   2930  -6150       N  
ATOM   3086  CA  ILE B 164      37.854  66.235  98.534  1.00191.28           C  
ANISOU 3086  CA  ILE B 164    23706  28583  20385   2562   2884  -5709       C  
ATOM   3087  C   ILE B 164      36.632  65.354  98.250  1.00188.36           C  
ANISOU 3087  C   ILE B 164    23220  28392  19954   2567   3123  -5292       C  
ATOM   3088  O   ILE B 164      36.001  65.477  97.193  1.00184.02           O  
ANISOU 3088  O   ILE B 164    22577  27564  19779   2533   3165  -5104       O  
ATOM   3089  CB  ILE B 164      39.133  65.416  98.360  1.00187.02           C  
ANISOU 3089  CB  ILE B 164    23262  28036  19759   2362   2669  -5522       C  
ATOM   3090  CG1 ILE B 164      40.347  66.355  98.399  1.00187.33           C  
ANISOU 3090  CG1 ILE B 164    23367  27800  20007   2326   2426  -5934       C  
ATOM   3091  CG2 ILE B 164      39.123  64.667  97.033  1.00182.37           C  
ANISOU 3091  CG2 ILE B 164    22636  27197  19459   2164   2651  -5047       C  
ATOM   3092  CD1 ILE B 164      41.643  65.718  98.850  1.00186.76           C  
ANISOU 3092  CD1 ILE B 164    23379  27871  19710   2219   2200  -5953       C  
ATOM   3093  N   SER B 165      36.313  64.479  99.197  1.00189.38           N  
ANISOU 3093  N   SER B 165    23357  28978  19620   2615   3274  -5154       N  
ATOM   3094  CA  SER B 165      35.202  63.555  99.035  1.00189.17           C  
ANISOU 3094  CA  SER B 165    23199  29135  19542   2599   3520  -4759       C  
ATOM   3095  C   SER B 165      33.862  64.254  98.831  1.00192.78           C  
ANISOU 3095  C   SER B 165    23479  29521  20245   2754   3732  -4875       C  
ATOM   3096  O   SER B 165      33.138  63.959  97.870  1.00190.06           O  
ANISOU 3096  O   SER B 165    22993  28994  20226   2693   3784  -4605       O  
ATOM   3097  CB  SER B 165      35.146  62.614 100.225  1.00192.10           C  
ANISOU 3097  CB  SER B 165    23633  30000  19353   2643   3676  -4623       C  
ATOM   3098  OG  SER B 165      34.145  61.650 100.036  1.00193.90           O  
ANISOU 3098  OG  SER B 165    23720  30370  19582   2592   3924  -4215       O  
ATOM   3099  N   GLU B 166      33.538  65.196  99.713  1.00200.22           N  
ANISOU 3099  N   GLU B 166    24424  30601  21046   2968   3834  -5301       N  
ATOM   3100  CA  GLU B 166      32.265  65.922  99.611  1.00207.29           C  
ANISOU 3100  CA  GLU B 166    25141  31443  22176   3144   4038  -5460       C  
ATOM   3101  C   GLU B 166      32.167  66.761  98.346  1.00216.49           C  
ANISOU 3101  C   GLU B 166    26253  32091  23911   3128   3876  -5513       C  
ATOM   3102  O   GLU B 166      31.187  66.640  97.572  1.00226.35           O  
ANISOU 3102  O   GLU B 166    27332  33207  25462   3144   3965  -5314       O  
ATOM   3103  CB  GLU B 166      32.070  66.803 100.835  1.00207.08           C  
ANISOU 3103  CB  GLU B 166    25150  31659  21871   3387   4158  -5948       C  
ATOM   3104  CG  GLU B 166      31.866  66.022 102.126  1.00208.60           C  
ANISOU 3104  CG  GLU B 166    25391  32403  21462   3465   4395  -5883       C  
ATOM   3105  CD  GLU B 166      32.106  66.862 103.382  1.00214.75           C  
ANISOU 3105  CD  GLU B 166    26292  33430  21871   3699   4417  -6407       C  
ATOM   3106  OE1 GLU B 166      32.639  67.997 103.286  1.00216.58           O  
ANISOU 3106  OE1 GLU B 166    26580  33391  22319   3768   4200  -6835       O  
ATOM   3107  OE2 GLU B 166      31.791  66.389 104.502  1.00219.03           O  
ANISOU 3107  OE2 GLU B 166    26888  34441  21892   3823   4654  -6401       O  
ATOM   3108  N   ALA B 167      33.177  67.605  98.137  1.00220.46           N  
ANISOU 3108  N   ALA B 167    26900  32296  24568   3103   3638  -5780       N  
ATOM   3109  CA  ALA B 167      33.235  68.473  96.954  1.00221.38           C  
ANISOU 3109  CA  ALA B 167    27017  31885  25209   3090   3488  -5825       C  
ATOM   3110  C   ALA B 167      33.060  67.646  95.686  1.00223.90           C  
ANISOU 3110  C   ALA B 167    27293  32014  25762   2928   3433  -5338       C  
ATOM   3111  O   ALA B 167      32.201  67.951  94.848  1.00227.71           O  
ANISOU 3111  O   ALA B 167    27672  32270  26578   3006   3460  -5247       O  
ATOM   3112  CB  ALA B 167      34.544  69.235  96.919  1.00217.20           C  
ANISOU 3112  CB  ALA B 167    26655  31074  24797   3021   3255  -6102       C  
ATOM   3113  N   ALA B 168      33.863  66.587  95.562  1.00225.67           N  
ANISOU 3113  N   ALA B 168    27599  32340  25804   2723   3342  -5040       N  
ATOM   3114  CA  ALA B 168      33.750  65.675  94.422  1.00227.81           C  
ANISOU 3114  CA  ALA B 168    27834  32469  26253   2568   3283  -4586       C  
ATOM   3115  C   ALA B 168      32.347  65.063  94.262  1.00224.81           C  
ANISOU 3115  C   ALA B 168    27241  32259  25915   2636   3473  -4358       C  
ATOM   3116  O   ALA B 168      31.849  64.963  93.137  1.00227.16           O  
ANISOU 3116  O   ALA B 168    27469  32307  26533   2624   3410  -4152       O  
ATOM   3117  CB  ALA B 168      34.771  64.563  94.538  1.00229.14           C  
ANISOU 3117  CB  ALA B 168    28104  32787  26172   2359   3183  -4336       C  
ATOM   3118  N   GLU B 169      31.737  64.638  95.374  1.00217.40           N  
ANISOU 3118  N   GLU B 169    26201  31741  24658   2710   3703  -4395       N  
ATOM   3119  CA  GLU B 169      30.373  64.103  95.331  1.00213.12           C  
ANISOU 3119  CA  GLU B 169    25416  31366  24191   2773   3923  -4216       C  
ATOM   3120  C   GLU B 169      29.439  65.087  94.615  1.00212.21           C  
ANISOU 3120  C   GLU B 169    25166  30964  24499   2948   3913  -4385       C  
ATOM   3121  O   GLU B 169      28.903  64.797  93.520  1.00212.18           O  
ANISOU 3121  O   GLU B 169    25054  30746  24816   2923   3830  -4156       O  
ATOM   3122  CB  GLU B 169      29.855  63.736  96.729  1.00217.60           C  
ANISOU 3122  CB  GLU B 169    25908  32413  24355   2858   4225  -4289       C  
ATOM   3123  CG  GLU B 169      28.792  62.641  96.766  1.00221.96           C  
ANISOU 3123  CG  GLU B 169    26228  33192  24912   2811   4471  -3957       C  
ATOM   3124  CD  GLU B 169      28.015  62.597  98.078  1.00230.05           C  
ANISOU 3124  CD  GLU B 169    27147  34641  25619   2953   4839  -4085       C  
ATOM   3125  OE1 GLU B 169      27.731  63.650  98.702  1.00234.28           O  
ANISOU 3125  OE1 GLU B 169    27682  35241  26093   3161   4934  -4484       O  
ATOM   3126  OE2 GLU B 169      27.632  61.482  98.498  1.00233.58           O  
ANISOU 3126  OE2 GLU B 169    27505  35361  25883   2863   5063  -3778       O  
ATOM   3127  N   THR B 170      29.262  66.253  95.236  1.00213.64           N  
ANISOU 3127  N   THR B 170    25359  31137  24677   3142   3976  -4799       N  
ATOM   3128  CA  THR B 170      28.361  67.279  94.703  1.00216.01           C  
ANISOU 3128  CA  THR B 170    25535  31174  25364   3346   3973  -5003       C  
ATOM   3129  C   THR B 170      28.693  67.622  93.226  1.00216.71           C  
ANISOU 3129  C   THR B 170    25724  30767  25848   3300   3699  -4854       C  
ATOM   3130  O   THR B 170      27.835  67.551  92.337  1.00224.96           O  
ANISOU 3130  O   THR B 170    26629  31649  27195   3371   3659  -4704       O  
ATOM   3131  CB  THR B 170      28.500  68.579  95.513  1.00214.61           C  
ANISOU 3131  CB  THR B 170    25428  30975  25138   3537   4011  -5501       C  
ATOM   3132  OG1 THR B 170      28.643  68.267  96.907  1.00211.97           O  
ANISOU 3132  OG1 THR B 170    25110  31092  24334   3559   4205  -5649       O  
ATOM   3133  CG2 THR B 170      27.297  69.480  95.310  1.00217.53           C  
ANISOU 3133  CG2 THR B 170    25609  31205  25836   3788   4096  -5725       C  
ATOM   3134  N   VAL B 171      29.961  67.964  92.997  1.00211.05           N  
ANISOU 3134  N   VAL B 171    25250  29823  25112   3187   3516  -4897       N  
ATOM   3135  CA  VAL B 171      30.437  68.343  91.679  1.00208.82           C  
ANISOU 3135  CA  VAL B 171    25111  29072  25156   3139   3294  -4759       C  
ATOM   3136  C   VAL B 171      30.092  67.307  90.609  1.00202.70           C  
ANISOU 3136  C   VAL B 171    24274  28251  24491   3039   3215  -4328       C  
ATOM   3137  O   VAL B 171      29.477  67.658  89.597  1.00201.52           O  
ANISOU 3137  O   VAL B 171    24095  27821  24652   3155   3119  -4249       O  
ATOM   3138  CB  VAL B 171      31.924  68.723  91.653  1.00213.56           C  
ANISOU 3138  CB  VAL B 171    25956  29464  25722   2994   3149  -4849       C  
ATOM   3139  CG1 VAL B 171      32.333  69.111  90.230  1.00212.99           C  
ANISOU 3139  CG1 VAL B 171    26034  28897  25993   2954   2972  -4669       C  
ATOM   3140  CG2 VAL B 171      32.214  69.906  92.591  1.00217.98           C  
ANISOU 3140  CG2 VAL B 171    26564  29996  26259   3119   3186  -5331       C  
ATOM   3141  N   ASN B 172      30.450  66.045  90.852  1.00195.44           N  
ANISOU 3141  N   ASN B 172    23336  27604  23317   2845   3244  -4067       N  
ATOM   3142  CA  ASN B 172      30.104  64.957  89.939  1.00188.19           C  
ANISOU 3142  CA  ASN B 172    22337  26672  22493   2743   3173  -3682       C  
ATOM   3143  C   ASN B 172      28.598  64.857  89.662  1.00185.87           C  
ANISOU 3143  C   ASN B 172    21772  26431  22417   2904   3253  -3652       C  
ATOM   3144  O   ASN B 172      28.181  64.572  88.528  1.00186.30           O  
ANISOU 3144  O   ASN B 172    21783  26284  22715   2925   3105  -3451       O  
ATOM   3145  CB  ASN B 172      30.574  63.602  90.514  1.00183.60           C  
ANISOU 3145  CB  ASN B 172    21739  26426  21592   2531   3240  -3444       C  
ATOM   3146  CG  ASN B 172      32.074  63.344  90.325  1.00177.35           C  
ANISOU 3146  CG  ASN B 172    21188  25527  20669   2339   3083  -3353       C  
ATOM   3147  OD1 ASN B 172      32.592  63.380  89.219  1.00173.53           O  
ANISOU 3147  OD1 ASN B 172    20829  24731  20373   2274   2907  -3209       O  
ATOM   3148  ND2 ASN B 172      32.764  63.024  91.408  1.00176.09           N  
ANISOU 3148  ND2 ASN B 172    21091  25643  20173   2256   3149  -3427       N  
ATOM   3149  N   LYS B 173      27.787  65.048  90.697  1.00182.17           N  
ANISOU 3149  N   LYS B 173    21112  26244  21856   3023   3484  -3857       N  
ATOM   3150  CA  LYS B 173      26.336  65.026  90.494  1.00181.22           C  
ANISOU 3150  CA  LYS B 173    20694  26172  21987   3184   3578  -3872       C  
ATOM   3151  C   LYS B 173      25.874  66.083  89.489  1.00183.38           C  
ANISOU 3151  C   LYS B 173    20987  26050  22639   3398   3391  -4000       C  
ATOM   3152  O   LYS B 173      25.258  65.762  88.457  1.00180.00           O  
ANISOU 3152  O   LYS B 173    20456  25464  22473   3447   3244  -3824       O  
ATOM   3153  CB  LYS B 173      25.594  65.194  91.827  1.00182.39           C  
ANISOU 3153  CB  LYS B 173    20646  26683  21972   3294   3895  -4108       C  
ATOM   3154  CG  LYS B 173      25.660  63.993  92.752  1.00179.50           C  
ANISOU 3154  CG  LYS B 173    20203  26733  21265   3123   4125  -3915       C  
ATOM   3155  CD  LYS B 173      24.838  64.245  94.005  1.00183.80           C  
ANISOU 3155  CD  LYS B 173    20562  27623  21650   3266   4470  -4149       C  
ATOM   3156  CE  LYS B 173      24.998  63.121  95.011  1.00184.79           C  
ANISOU 3156  CE  LYS B 173    20672  28160  21377   3114   4724  -3945       C  
ATOM   3157  NZ  LYS B 173      24.309  63.414  96.309  1.00190.64           N  
ANISOU 3157  NZ  LYS B 173    21286  29260  21887   3267   5092  -4178       N  
ATOM   3158  N   VAL B 174      26.202  67.334  89.786  1.00190.12           N  
ANISOU 3158  N   VAL B 174    21984  26731  23519   3532   3382  -4308       N  
ATOM   3159  CA  VAL B 174      25.857  68.462  88.909  1.00198.03           C  
ANISOU 3159  CA  VAL B 174    23050  27321  24869   3752   3214  -4436       C  
ATOM   3160  C   VAL B 174      26.359  68.247  87.464  1.00198.99           C  
ANISOU 3160  C   VAL B 174    23371  27091  25143   3688   2945  -4136       C  
ATOM   3161  O   VAL B 174      25.587  68.373  86.494  1.00208.09           O  
ANISOU 3161  O   VAL B 174    24454  28042  26565   3850   2797  -4050       O  
ATOM   3162  CB  VAL B 174      26.572  69.736  89.425  1.00199.65           C  
ANISOU 3162  CB  VAL B 174    23460  27342  25054   3826   3224  -4770       C  
ATOM   3163  CG1 VAL B 174      26.381  70.917  88.460  1.00200.09           C  
ANISOU 3163  CG1 VAL B 174    23638  26909  25475   4036   3048  -4859       C  
ATOM   3164  CG2 VAL B 174      26.132  70.080  90.846  1.00203.90           C  
ANISOU 3164  CG2 VAL B 174    23840  28214  25416   3927   3475  -5117       C  
ATOM   3165  N   VAL B 175      27.648  67.936  87.331  1.00195.26           N  
ANISOU 3165  N   VAL B 175    23145  26552  24491   3468   2879  -3991       N  
ATOM   3166  CA  VAL B 175      28.243  67.684  86.022  1.00195.33           C  
ANISOU 3166  CA  VAL B 175    23364  26255  24597   3393   2663  -3704       C  
ATOM   3167  C   VAL B 175      27.490  66.595  85.240  1.00195.21           C  
ANISOU 3167  C   VAL B 175    23185  26330  24655   3385   2563  -3420       C  
ATOM   3168  O   VAL B 175      27.219  66.749  84.046  1.00195.49           O  
ANISOU 3168  O   VAL B 175    23303  26087  24887   3507   2366  -3285       O  
ATOM   3169  CB  VAL B 175      29.722  67.320  86.160  1.00194.87           C  
ANISOU 3169  CB  VAL B 175    23531  26189  24320   3132   2649  -3600       C  
ATOM   3170  CG1 VAL B 175      30.299  66.866  84.826  1.00192.67           C  
ANISOU 3170  CG1 VAL B 175    23445  25651  24109   3042   2463  -3278       C  
ATOM   3171  CG2 VAL B 175      30.496  68.518  86.704  1.00196.21           C  
ANISOU 3171  CG2 VAL B 175    23868  26174  24507   3156   2693  -3900       C  
ATOM   3172  N   GLU B 176      27.157  65.503  85.921  1.00194.75           N  
ANISOU 3172  N   GLU B 176    22903  26652  24440   3251   2696  -3335       N  
ATOM   3173  CA  GLU B 176      26.430  64.411  85.278  1.00194.06           C  
ANISOU 3173  CA  GLU B 176    22619  26655  24458   3222   2612  -3094       C  
ATOM   3174  C   GLU B 176      25.070  64.897  84.751  1.00190.05           C  
ANISOU 3174  C   GLU B 176    21896  26036  24277   3498   2532  -3207       C  
ATOM   3175  O   GLU B 176      24.717  64.626  83.602  1.00193.08           O  
ANISOU 3175  O   GLU B 176    22282  26237  24840   3579   2303  -3053       O  
ATOM   3176  CB  GLU B 176      26.325  63.204  86.222  1.00199.85           C  
ANISOU 3176  CB  GLU B 176    23147  27798  24987   3021   2813  -2986       C  
ATOM   3177  CG  GLU B 176      26.261  61.846  85.547  1.00206.05           C  
ANISOU 3177  CG  GLU B 176    23846  28636  25807   2865   2703  -2670       C  
ATOM   3178  CD  GLU B 176      24.893  61.516  84.954  1.00214.53           C  
ANISOU 3178  CD  GLU B 176    24608  29701  27202   3006   2629  -2650       C  
ATOM   3179  OE1 GLU B 176      24.832  60.805  83.921  1.00219.62           O  
ANISOU 3179  OE1 GLU B 176    25249  30225  27972   2970   2412  -2450       O  
ATOM   3180  OE2 GLU B 176      23.875  61.957  85.518  1.00218.65           O  
ANISOU 3180  OE2 GLU B 176    24875  30339  27862   3158   2782  -2853       O  
ATOM   3181  N   ARG B 177      24.336  65.634  85.583  1.00185.53           N  
ANISOU 3181  N   ARG B 177    21145  25571  23777   3660   2705  -3494       N  
ATOM   3182  CA  ARG B 177      23.059  66.181  85.151  1.00188.33           C  
ANISOU 3182  CA  ARG B 177    21278  25815  24464   3943   2627  -3639       C  
ATOM   3183  C   ARG B 177      23.179  67.080  83.906  1.00188.80           C  
ANISOU 3183  C   ARG B 177    21589  25425  24718   4153   2337  -3623       C  
ATOM   3184  O   ARG B 177      22.400  66.955  82.952  1.00187.08           O  
ANISOU 3184  O   ARG B 177    21271  25074  24735   4323   2122  -3551       O  
ATOM   3185  CB  ARG B 177      22.363  66.960  86.276  1.00192.88           C  
ANISOU 3185  CB  ARG B 177    21650  26556  25078   4098   2875  -3983       C  
ATOM   3186  CG  ARG B 177      21.481  66.090  87.179  1.00196.86           C  
ANISOU 3186  CG  ARG B 177    21763  27475  25559   4027   3146  -4000       C  
ATOM   3187  CD  ARG B 177      20.618  66.897  88.146  1.00204.64           C  
ANISOU 3187  CD  ARG B 177    22518  28611  26625   4230   3391  -4353       C  
ATOM   3188  NE  ARG B 177      19.612  67.721  87.453  1.00213.02           N  
ANISOU 3188  NE  ARG B 177    23425  29425  28085   4541   3226  -4530       N  
ATOM   3189  CZ  ARG B 177      18.610  68.379  88.045  1.00225.01           C  
ANISOU 3189  CZ  ARG B 177    24671  31035  29788   4765   3393  -4838       C  
ATOM   3190  NH1 ARG B 177      18.429  68.335  89.372  1.00232.58           N  
ANISOU 3190  NH1 ARG B 177    25476  32342  30549   4721   3760  -5014       N  
ATOM   3191  NH2 ARG B 177      17.767  69.093  87.305  1.00227.55           N  
ANISOU 3191  NH2 ARG B 177    24872  31100  30484   5057   3191  -4978       N  
ATOM   3192  N   LEU B 178      24.165  67.968  83.924  1.00192.39           N  
ANISOU 3192  N   LEU B 178    22375  25646  25079   4143   2330  -3687       N  
ATOM   3193  CA  LEU B 178      24.375  68.861  82.801  1.00197.51           C  
ANISOU 3193  CA  LEU B 178    23303  25847  25891   4330   2104  -3641       C  
ATOM   3194  C   LEU B 178      24.742  68.145  81.505  1.00194.82           C  
ANISOU 3194  C   LEU B 178    23144  25351  25526   4272   1867  -3304       C  
ATOM   3195  O   LEU B 178      24.182  68.444  80.451  1.00195.94           O  
ANISOU 3195  O   LEU B 178    23345  25252  25851   4509   1640  -3237       O  
ATOM   3196  CB  LEU B 178      25.451  69.871  83.129  1.00202.30           C  
ANISOU 3196  CB  LEU B 178    24213  26225  26425   4282   2182  -3765       C  
ATOM   3197  CG  LEU B 178      24.917  70.919  84.091  1.00210.88           C  
ANISOU 3197  CG  LEU B 178    25165  27335  27624   4458   2335  -4146       C  
ATOM   3198  CD1 LEU B 178      26.095  71.616  84.766  1.00213.86           C  
ANISOU 3198  CD1 LEU B 178    25771  27609  27876   4324   2453  -4308       C  
ATOM   3199  CD2 LEU B 178      23.965  71.898  83.370  1.00212.82           C  
ANISOU 3199  CD2 LEU B 178    25396  27262  28201   4818   2177  -4250       C  
ATOM   3200  N   LEU B 179      25.675  67.201  81.588  1.00193.09           N  
ANISOU 3200  N   LEU B 179    23018  25275  25071   3978   1912  -3103       N  
ATOM   3201  CA  LEU B 179      26.072  66.398  80.425  1.00194.10           C  
ANISOU 3201  CA  LEU B 179    23304  25295  25147   3905   1707  -2795       C  
ATOM   3202  C   LEU B 179      24.861  65.658  79.849  1.00198.42           C  
ANISOU 3202  C   LEU B 179    23574  25952  25863   4040   1537  -2734       C  
ATOM   3203  O   LEU B 179      24.574  65.743  78.647  1.00201.52           O  
ANISOU 3203  O   LEU B 179    24090  26115  26360   4229   1278  -2620       O  
ATOM   3204  CB  LEU B 179      27.122  65.380  80.884  1.00189.48           C  
ANISOU 3204  CB  LEU B 179    22767  24927  24299   3560   1819  -2639       C  
ATOM   3205  CG  LEU B 179      27.767  64.443  79.860  1.00183.82           C  
ANISOU 3205  CG  LEU B 179    22220  24137  23484   3428   1653  -2334       C  
ATOM   3206  CD1 LEU B 179      28.654  65.210  78.897  1.00182.17           C  
ANISOU 3206  CD1 LEU B 179    22414  23538  23265   3489   1555  -2231       C  
ATOM   3207  CD2 LEU B 179      28.607  63.391  80.568  1.00179.65           C  
ANISOU 3207  CD2 LEU B 179    21651  23879  22726   3104   1784  -2227       C  
ATOM   3208  N   ARG B 180      24.153  64.954  80.721  1.00202.52           N  
ANISOU 3208  N   ARG B 180    23719  26817  26411   3952   1686  -2818       N  
ATOM   3209  CA  ARG B 180      22.984  64.172  80.330  1.00207.10           C  
ANISOU 3209  CA  ARG B 180    23961  27524  27203   4039   1559  -2792       C  
ATOM   3210  C   ARG B 180      21.938  65.040  79.617  1.00207.38           C  
ANISOU 3210  C   ARG B 180    23928  27335  27530   4414   1346  -2942       C  
ATOM   3211  O   ARG B 180      21.428  64.663  78.564  1.00216.56           O  
ANISOU 3211  O   ARG B 180    25057  28392  28832   4556   1062  -2851       O  
ATOM   3212  CB  ARG B 180      22.388  63.573  81.613  1.00216.56           C  
ANISOU 3212  CB  ARG B 180    24768  29105  28410   3898   1849  -2901       C  
ATOM   3213  CG  ARG B 180      21.413  62.437  81.459  1.00227.36           C  
ANISOU 3213  CG  ARG B 180    25746  30661  29979   3857   1807  -2834       C  
ATOM   3214  CD  ARG B 180      21.739  61.354  82.453  1.00237.51           C  
ANISOU 3214  CD  ARG B 180    26886  32272  31082   3541   2082  -2714       C  
ATOM   3215  NE  ARG B 180      21.170  60.074  82.084  1.00250.09           N  
ANISOU 3215  NE  ARG B 180    28198  33973  32849   3431   2004  -2564       N  
ATOM   3216  CZ  ARG B 180      21.260  58.935  82.816  1.00258.32           C  
ANISOU 3216  CZ  ARG B 180    29064  35278  33807   3162   2225  -2418       C  
ATOM   3217  NH1 ARG B 180      21.892  58.929  83.987  1.00261.50           N  
ANISOU 3217  NH1 ARG B 180    29557  35889  33909   2997   2531  -2403       N  
ATOM   3218  NH2 ARG B 180      20.686  57.819  82.376  1.00260.73           N  
ANISOU 3218  NH2 ARG B 180    29098  35625  34339   3076   2130  -2298       N  
ATOM   3219  N   ARG B 181      21.622  66.194  80.199  1.00202.24           N  
ANISOU 3219  N   ARG B 181    23258  26614  26971   4586   1468  -3188       N  
ATOM   3220  CA  ARG B 181      20.731  67.146  79.545  1.00203.62           C  
ANISOU 3220  CA  ARG B 181    23410  26537  27418   4964   1260  -3335       C  
ATOM   3221  C   ARG B 181      21.288  67.571  78.174  1.00202.57           C  
ANISOU 3221  C   ARG B 181    23709  26019  27237   5116    964  -3138       C  
ATOM   3222  O   ARG B 181      20.557  67.686  77.198  1.00201.65           O  
ANISOU 3222  O   ARG B 181    23579  25743  27294   5394    671  -3121       O  
ATOM   3223  CB  ARG B 181      20.589  68.378  80.434  1.00205.73           C  
ANISOU 3223  CB  ARG B 181    23665  26752  27750   5093   1461  -3621       C  
ATOM   3224  CG  ARG B 181      19.912  69.582  79.804  1.00209.41           C  
ANISOU 3224  CG  ARG B 181    24201  26887  28477   5490   1260  -3770       C  
ATOM   3225  CD  ARG B 181      18.405  69.422  79.655  1.00211.90           C  
ANISOU 3225  CD  ARG B 181    24083  27308  29119   5740   1131  -3933       C  
ATOM   3226  NE  ARG B 181      17.780  70.752  79.639  1.00213.82           N  
ANISOU 3226  NE  ARG B 181    24329  27309  29602   6096   1068  -4181       N  
ATOM   3227  CZ  ARG B 181      17.596  71.521  78.563  1.00214.52           C  
ANISOU 3227  CZ  ARG B 181    24663  27020  29823   6419    759  -4136       C  
ATOM   3228  NH1 ARG B 181      17.936  71.104  77.337  1.00214.31           N  
ANISOU 3228  NH1 ARG B 181    24908  26822  29698   6456    469  -3854       N  
ATOM   3229  NH2 ARG B 181      17.040  72.711  78.723  1.00216.32           N  
ANISOU 3229  NH2 ARG B 181    24869  27045  30277   6725    742  -4378       N  
ATOM   3230  N   MET B 182      22.598  67.768  78.116  1.00203.44           N  
ANISOU 3230  N   MET B 182    24199  25990  27107   4934   1050  -2990       N  
ATOM   3231  CA  MET B 182      23.238  68.188  76.889  1.00208.50           C  
ANISOU 3231  CA  MET B 182    25276  26267  27676   5052    845  -2781       C  
ATOM   3232  C   MET B 182      23.093  67.126  75.802  1.00207.46           C  
ANISOU 3232  C   MET B 182    25163  26171  27491   5062    580  -2554       C  
ATOM   3233  O   MET B 182      23.192  67.432  74.604  1.00208.36           O  
ANISOU 3233  O   MET B 182    25582  26004  27579   5275    340  -2403       O  
ATOM   3234  CB  MET B 182      24.717  68.509  77.109  1.00212.65           C  
ANISOU 3234  CB  MET B 182    26154  26656  27985   4811   1030  -2675       C  
ATOM   3235  CG  MET B 182      25.298  69.486  76.089  1.00216.81           C  
ANISOU 3235  CG  MET B 182    27137  26725  28514   4987    921  -2536       C  
ATOM   3236  SD  MET B 182      24.656  71.159  76.214  1.00225.14           S  
ANISOU 3236  SD  MET B 182    28254  27450  29839   5343    917  -2773       S  
ATOM   3237  CE  MET B 182      25.091  71.595  77.908  1.00227.48           C  
ANISOU 3237  CE  MET B 182    28366  27929  30135   5106   1268  -3082       C  
ATOM   3238  N   GLN B 183      22.857  65.878  76.223  1.00206.41           N  
ANISOU 3238  N   GLN B 183    24713  26375  27337   4842    627  -2532       N  
ATOM   3239  CA  GLN B 183      22.578  64.785  75.293  1.00201.60           C  
ANISOU 3239  CA  GLN B 183    24042  25826  26730   4850    366  -2373       C  
ATOM   3240  C   GLN B 183      21.087  64.612  75.062  1.00198.91           C  
ANISOU 3240  C   GLN B 183    23312  25565  26699   5103    156  -2541       C  
ATOM   3241  O   GLN B 183      20.630  64.467  73.919  1.00186.98           O  
ANISOU 3241  O   GLN B 183    21867  23917  25259   5344   -188  -2487       O  
ATOM   3242  CB  GLN B 183      23.013  63.419  75.869  1.00199.91           C  
ANISOU 3242  CB  GLN B 183    23640  25923  26393   4475    515  -2265       C  
ATOM   3243  CG  GLN B 183      24.387  63.306  76.477  1.00197.06           C  
ANISOU 3243  CG  GLN B 183    23509  25606  25756   4159    766  -2149       C  
ATOM   3244  CD  GLN B 183      25.484  63.577  75.480  1.00196.33           C  
ANISOU 3244  CD  GLN B 183    23890  25232  25474   4167    658  -1944       C  
ATOM   3245  OE1 GLN B 183      25.252  63.639  74.277  1.00202.16           O  
ANISOU 3245  OE1 GLN B 183    24804  25774  26233   4389    391  -1845       O  
ATOM   3246  NE2 GLN B 183      26.693  63.724  75.971  1.00191.87           N  
ANISOU 3246  NE2 GLN B 183    23532  24648  24720   3930    868  -1882       N  
ATOM   3247  N   LYS B 184      20.338  64.598  76.168  1.00207.12           N  
ANISOU 3247  N   LYS B 184    23936  26837  27921   5050    369  -2755       N  
ATOM   3248  CA  LYS B 184      18.891  64.322  76.175  1.00216.73           C  
ANISOU 3248  CA  LYS B 184    24677  28180  29488   5232    242  -2947       C  
ATOM   3249  C   LYS B 184      18.163  65.328  75.276  1.00224.37           C  
ANISOU 3249  C   LYS B 184    25740  28863  30646   5680    -76  -3063       C  
ATOM   3250  O   LYS B 184      18.238  65.177  74.037  1.00221.88           O  
ANISOU 3250  O   LYS B 184    25662  28363  30277   5855   -423  -2926       O  
ATOM   3251  CB  LYS B 184      18.388  64.267  77.651  1.00220.73           C  
ANISOU 3251  CB  LYS B 184    24774  28983  30110   5078    623  -3144       C  
ATOM   3252  CG  LYS B 184      16.903  64.230  78.020  1.00227.07           C  
ANISOU 3252  CG  LYS B 184    25035  29932  31308   5245    634  -3400       C  
ATOM   3253  CD  LYS B 184      16.746  64.557  79.516  1.00230.45           C  
ANISOU 3253  CD  LYS B 184    25237  30597  31725   5120   1078  -3577       C  
ATOM   3254  CE  LYS B 184      15.516  65.400  79.875  1.00236.88           C  
ANISOU 3254  CE  LYS B 184    25710  31411  32881   5420   1116  -3901       C  
ATOM   3255  NZ  LYS B 184      14.259  64.693  79.539  1.00240.89           N  
ANISOU 3255  NZ  LYS B 184    25717  32020  33787   5515    966  -3998       N  
ATOM   3256  N   ARG B 185      17.525  66.362  75.842  1.00233.26           N  
ANISOU 3256  N   ARG B 185    26726  29938  31962   5886     24  -3305       N  
ATOM   3257  CA  ARG B 185      16.571  67.186  75.080  1.00239.00           C  
ANISOU 3257  CA  ARG B 185    27427  30434  32945   6337   -298  -3452       C  
ATOM   3258  C   ARG B 185      17.188  67.540  73.735  1.00245.58           C  
ANISOU 3258  C   ARG B 185    28793  30935  33578   6535   -615  -3223       C  
ATOM   3259  O   ARG B 185      18.325  68.034  73.697  1.00257.55           O  
ANISOU 3259  O   ARG B 185    30754  32275  34825   6424   -473  -3052       O  
ATOM   3260  CB  ARG B 185      16.186  68.457  75.844  1.00235.69           C  
ANISOU 3260  CB  ARG B 185    26943  29928  32681   6519   -114  -3703       C  
ATOM   3261  CG  ARG B 185      15.282  68.192  77.033  1.00231.77           C  
ANISOU 3261  CG  ARG B 185    25877  29753  32430   6431    158  -3971       C  
ATOM   3262  CD  ARG B 185      14.593  69.458  77.477  1.00231.50           C  
ANISOU 3262  CD  ARG B 185    25732  29596  32630   6735    216  -4265       C  
ATOM   3263  NE  ARG B 185      14.382  69.492  78.916  1.00230.33           N  
ANISOU 3263  NE  ARG B 185    25261  29734  32518   6557    648  -4476       N  
ATOM   3264  CZ  ARG B 185      13.840  70.519  79.573  1.00231.67           C  
ANISOU 3264  CZ  ARG B 185    25291  29864  32868   6765    791  -4770       C  
ATOM   3265  NH1 ARG B 185      13.435  71.605  78.926  1.00233.64           N  
ANISOU 3265  NH1 ARG B 185    25681  29780  33310   7158    528  -4882       N  
ATOM   3266  NH2 ARG B 185      13.693  70.457  80.891  1.00231.45           N  
ANISOU 3266  NH2 ARG B 185    24989  30132  32819   6595   1202  -4953       N  
ATOM   3267  N   GLU B 186      16.455  67.254  72.652  1.00241.77           N  
ANISOU 3267  N   GLU B 186    28260  30374  33226   6824  -1034  -3222       N  
ATOM   3268  CA  GLU B 186      17.062  67.158  71.317  1.00231.18           C  
ANISOU 3268  CA  GLU B 186    27402  28808  31627   6961  -1339  -2963       C  
ATOM   3269  C   GLU B 186      17.835  68.408  70.952  1.00230.81           C  
ANISOU 3269  C   GLU B 186    27912  28400  31384   7122  -1290  -2820       C  
ATOM   3270  O   GLU B 186      17.357  69.302  70.240  1.00232.66           O  
ANISOU 3270  O   GLU B 186    28339  28360  31698   7536  -1547  -2845       O  
ATOM   3271  CB  GLU B 186      16.064  66.726  70.218  1.00226.33           C  
ANISOU 3271  CB  GLU B 186    26643  28171  31181   7304  -1839  -3030       C  
ATOM   3272  CG  GLU B 186      16.021  65.213  70.014  1.00218.24           C  
ANISOU 3272  CG  GLU B 186    25363  27401  30157   7063  -1941  -2985       C  
ATOM   3273  CD  GLU B 186      17.409  64.570  69.988  1.00209.30           C  
ANISOU 3273  CD  GLU B 186    24575  26308  28642   6691  -1734  -2696       C  
ATOM   3274  OE1 GLU B 186      18.377  65.198  69.493  1.00203.42           O  
ANISOU 3274  OE1 GLU B 186    24373  25327  27587   6737  -1696  -2482       O  
ATOM   3275  OE2 GLU B 186      17.544  63.438  70.484  1.00206.50           O  
ANISOU 3275  OE2 GLU B 186    23939  26208  28313   6347  -1592  -2680       O  
ATOM   3276  N   SER B 187      19.049  68.420  71.494  1.00222.64           N  
ANISOU 3276  N   SER B 187    27114  27368  30108   6775   -947  -2672       N  
ATOM   3277  CA  SER B 187      19.941  69.552  71.419  1.00214.36           C  
ANISOU 3277  CA  SER B 187    26537  25995  28915   6813   -790  -2553       C  
ATOM   3278  C   SER B 187      20.694  69.440  70.117  1.00209.62           C  
ANISOU 3278  C   SER B 187    26450  25164  28031   6902   -977  -2234       C  
ATOM   3279  O   SER B 187      20.484  68.498  69.350  1.00206.27           O  
ANISOU 3279  O   SER B 187    25998  24857  27518   6944  -1236  -2142       O  
ATOM   3280  CB  SER B 187      20.897  69.526  72.619  1.00207.69           C  
ANISOU 3280  CB  SER B 187    25664  25282  27964   6390   -354  -2573       C  
ATOM   3281  OG  SER B 187      21.519  68.260  72.741  1.00198.91           O  
ANISOU 3281  OG  SER B 187    24484  24432  26660   6033   -270  -2431       O  
ATOM   3282  N   GLU B 188      21.621  70.391  69.916  1.00209.01           N  
ANISOU 3282  N   GLU B 188    26837  24757  27817   6911   -815  -2072       N  
ATOM   3283  CA  GLU B 188      22.614  70.337  68.853  1.00213.26           C  
ANISOU 3283  CA  GLU B 188    27901  25072  28052   6912   -854  -1738       C  
ATOM   3284  C   GLU B 188      24.022  70.107  69.441  1.00212.62           C  
ANISOU 3284  C   GLU B 188    27959  25028  27798   6455   -475  -1616       C  
ATOM   3285  O   GLU B 188      24.958  69.879  68.704  1.00207.36           O  
ANISOU 3285  O   GLU B 188    27664  24235  26886   6370   -442  -1351       O  
ATOM   3286  CB  GLU B 188      22.548  71.588  67.962  1.00220.74           C  
ANISOU 3286  CB  GLU B 188    29306  25570  28995   7321   -986  -1606       C  
ATOM   3287  CG  GLU B 188      22.399  72.945  68.673  1.00225.25           C  
ANISOU 3287  CG  GLU B 188    29880  25890  29815   7422   -803  -1769       C  
ATOM   3288  CD  GLU B 188      20.967  73.466  68.715  1.00231.06           C  
ANISOU 3288  CD  GLU B 188    30340  26608  30844   7828  -1070  -2021       C  
ATOM   3289  OE1 GLU B 188      20.320  73.356  69.784  1.00232.20           O  
ANISOU 3289  OE1 GLU B 188    29993  27004  31226   7728   -974  -2330       O  
ATOM   3290  OE2 GLU B 188      20.477  74.000  67.684  1.00234.71           O  
ANISOU 3290  OE2 GLU B 188    31077  26803  31296   8265  -1375  -1914       O  
ATOM   3291  N   PHE B 189      24.134  70.090  70.765  1.00220.25           N  
ANISOU 3291  N   PHE B 189    28605  26194  28886   6171   -202  -1822       N  
ATOM   3292  CA  PHE B 189      25.320  69.737  71.453  1.00226.07           C  
ANISOU 3292  CA  PHE B 189    29380  27034  29482   5749    108  -1765       C  
ATOM   3293  C   PHE B 189      25.202  68.268  71.907  1.00222.15           C  
ANISOU 3293  C   PHE B 189    28520  26973  28913   5474    103  -1795       C  
ATOM   3294  O   PHE B 189      25.967  67.778  72.754  1.00221.45           O  
ANISOU 3294  O   PHE B 189    28331  27076  28732   5112    348  -1807       O  
ATOM   3295  CB  PHE B 189      25.508  70.635  72.671  1.00236.13           C  
ANISOU 3295  CB  PHE B 189    30539  28268  30912   5634    391  -1995       C  
ATOM   3296  CG  PHE B 189      25.535  72.098  72.350  1.00245.03           C  
ANISOU 3296  CG  PHE B 189    31970  28953  32177   5898    406  -2003       C  
ATOM   3297  CD1 PHE B 189      26.737  72.736  72.092  1.00244.15           C  
ANISOU 3297  CD1 PHE B 189    32258  28514  31992   5778    594  -1836       C  
ATOM   3298  CD2 PHE B 189      24.357  72.846  72.342  1.00254.88           C  
ANISOU 3298  CD2 PHE B 189    33082  30097  33662   6263    245  -2189       C  
ATOM   3299  CE1 PHE B 189      26.774  74.097  71.806  1.00249.89           C  
ANISOU 3299  CE1 PHE B 189    33268  28794  32881   6010    629  -1830       C  
ATOM   3300  CE2 PHE B 189      24.383  74.204  72.069  1.00259.31           C  
ANISOU 3300  CE2 PHE B 189    33929  30225  34369   6513    260  -2192       C  
ATOM   3301  CZ  PHE B 189      25.596  74.834  71.796  1.00257.84           C  
ANISOU 3301  CZ  PHE B 189    34163  29693  34111   6383    457  -2002       C  
ATOM   3302  N   LYS B 190      24.266  67.541  71.325  1.00218.41           N  
ANISOU 3302  N   LYS B 190    27853  26642  28489   5648   -187  -1804       N  
ATOM   3303  CA  LYS B 190      24.164  66.138  71.541  1.00210.61           C  
ANISOU 3303  CA  LYS B 190    26565  25997  27457   5412   -220  -1794       C  
ATOM   3304  C   LYS B 190      25.375  65.448  70.886  1.00196.59           C  
ANISOU 3304  C   LYS B 190    25115  24186  25394   5204   -197  -1522       C  
ATOM   3305  O   LYS B 190      25.790  65.784  69.775  1.00192.23           O  
ANISOU 3305  O   LYS B 190    24974  23372  24690   5383   -326  -1331       O  
ATOM   3306  CB  LYS B 190      22.869  65.639  70.917  1.00217.24           C  
ANISOU 3306  CB  LYS B 190    27144  26931  28467   5688   -575  -1886       C  
ATOM   3307  CG  LYS B 190      22.516  64.190  71.164  1.00218.79           C  
ANISOU 3307  CG  LYS B 190    26948  27464  28716   5470   -630  -1917       C  
ATOM   3308  CD  LYS B 190      21.204  63.875  70.458  1.00222.20           C  
ANISOU 3308  CD  LYS B 190    27125  27927  29372   5787  -1016  -2045       C  
ATOM   3309  CE  LYS B 190      20.606  62.552  70.897  1.00219.75           C  
ANISOU 3309  CE  LYS B 190    26314  27936  29241   5577  -1037  -2141       C  
ATOM   3310  NZ  LYS B 190      19.890  62.686  72.194  1.00219.54           N  
ANISOU 3310  NZ  LYS B 190    25824  28111  29477   5469   -780  -2362       N  
ATOM   3311  N   GLY B 191      25.953  64.490  71.597  1.00188.45           N  
ANISOU 3311  N   GLY B 191    23904  23415  24281   4832    -19  -1500       N  
ATOM   3312  CA  GLY B 191      27.165  63.847  71.159  1.00182.44           C  
ANISOU 3312  CA  GLY B 191    23407  22636  23273   4604     43  -1275       C  
ATOM   3313  C   GLY B 191      28.396  64.451  71.824  1.00176.63           C  
ANISOU 3313  C   GLY B 191    22870  21797  22445   4360    369  -1242       C  
ATOM   3314  O   GLY B 191      29.522  64.011  71.595  1.00167.06           O  
ANISOU 3314  O   GLY B 191    21858  20561  21053   4143    467  -1076       O  
ATOM   3315  N   VAL B 192      28.177  65.456  72.663  1.00179.09           N  
ANISOU 3315  N   VAL B 192    23102  22044  22897   4399    528  -1425       N  
ATOM   3316  CA  VAL B 192      29.254  66.062  73.405  1.00179.75           C  
ANISOU 3316  CA  VAL B 192    23319  22039  22939   4174    814  -1458       C  
ATOM   3317  C   VAL B 192      29.811  65.027  74.410  1.00177.44           C  
ANISOU 3317  C   VAL B 192    22785  22091  22541   3805    974  -1489       C  
ATOM   3318  O   VAL B 192      29.069  64.172  74.897  1.00173.46           O  
ANISOU 3318  O   VAL B 192    21940  21893  22073   3753    927  -1560       O  
ATOM   3319  CB  VAL B 192      28.798  67.353  74.117  1.00184.29           C  
ANISOU 3319  CB  VAL B 192    23836  22478  23707   4322    925  -1693       C  
ATOM   3320  CG1 VAL B 192      28.129  67.052  75.463  1.00185.21           C  
ANISOU 3320  CG1 VAL B 192    23515  22947  23907   4217   1037  -1948       C  
ATOM   3321  CG2 VAL B 192      29.959  68.311  74.300  1.00185.71           C  
ANISOU 3321  CG2 VAL B 192    24308  22370  23881   4206   1140  -1684       C  
ATOM   3322  N   GLU B 193      31.113  65.076  74.667  1.00181.74           N  
ANISOU 3322  N   GLU B 193    23510  22572  22969   3557   1154  -1424       N  
ATOM   3323  CA  GLU B 193      31.711  64.227  75.671  1.00185.40           C  
ANISOU 3323  CA  GLU B 193    23780  23338  23325   3235   1297  -1463       C  
ATOM   3324  C   GLU B 193      32.506  64.988  76.703  1.00185.64           C  
ANISOU 3324  C   GLU B 193    23839  23333  23362   3079   1525  -1633       C  
ATOM   3325  O   GLU B 193      32.837  66.156  76.520  1.00197.12           O  
ANISOU 3325  O   GLU B 193    25503  24474  24917   3174   1591  -1691       O  
ATOM   3326  CB  GLU B 193      32.502  63.097  75.022  1.00190.36           C  
ANISOU 3326  CB  GLU B 193    24514  24024  23789   3057   1235  -1231       C  
ATOM   3327  CG  GLU B 193      31.558  62.096  74.379  1.00196.48           C  
ANISOU 3327  CG  GLU B 193    25131  24949  24573   3169   1005  -1143       C  
ATOM   3328  CD  GLU B 193      32.246  61.028  73.579  1.00197.55           C  
ANISOU 3328  CD  GLU B 193    25391  25106  24561   3045    909   -929       C  
ATOM   3329  OE1 GLU B 193      33.330  60.555  73.979  1.00198.19           O  
ANISOU 3329  OE1 GLU B 193    25512  25262  24530   2778   1044   -869       O  
ATOM   3330  OE2 GLU B 193      31.672  60.657  72.546  1.00196.91           O  
ANISOU 3330  OE2 GLU B 193    25360  24971  24482   3235    681   -840       O  
ATOM   3331  N   GLN B 194      32.804  64.320  77.796  1.00175.03           N  
ANISOU 3331  N   GLN B 194    22285  22302  21915   2848   1636  -1716       N  
ATOM   3332  CA  GLN B 194      33.402  64.966  78.969  1.00169.42           C  
ANISOU 3332  CA  GLN B 194    21544  21633  21193   2723   1822  -1940       C  
ATOM   3333  C   GLN B 194      34.910  64.732  79.030  1.00162.69           C  
ANISOU 3333  C   GLN B 194    20856  20723  20236   2464   1900  -1868       C  
ATOM   3334  O   GLN B 194      35.388  63.673  78.597  1.00157.09           O  
ANISOU 3334  O   GLN B 194    20168  20112  19406   2321   1840  -1664       O  
ATOM   3335  CB  GLN B 194      32.766  64.372  80.212  1.00168.94           C  
ANISOU 3335  CB  GLN B 194    21157  21982  21049   2657   1900  -2084       C  
ATOM   3336  CG  GLN B 194      33.149  65.056  81.510  1.00170.75           C  
ANISOU 3336  CG  GLN B 194    21334  22307  21236   2590   2070  -2362       C  
ATOM   3337  CD  GLN B 194      32.412  64.474  82.700  1.00172.81           C  
ANISOU 3337  CD  GLN B 194    21295  22983  21379   2563   2172  -2481       C  
ATOM   3338  OE1 GLN B 194      31.484  63.678  82.543  1.00177.36           O  
ANISOU 3338  OE1 GLN B 194    21674  23742  21971   2607   2131  -2370       O  
ATOM   3339  NE2 GLN B 194      32.834  64.845  83.898  1.00171.72           N  
ANISOU 3339  NE2 GLN B 194    21121  22998  21124   2492   2311  -2711       N  
ATOM   3340  N   LEU B 195      35.642  65.702  79.559  1.00165.51           N  
ANISOU 3340  N   LEU B 195    21306  20914  20663   2409   2021  -2054       N  
ATOM   3341  CA  LEU B 195      37.084  65.569  79.683  1.00169.19           C  
ANISOU 3341  CA  LEU B 195    21890  21313  21081   2166   2094  -2034       C  
ATOM   3342  C   LEU B 195      37.528  66.470  80.846  1.00171.21           C  
ANISOU 3342  C   LEU B 195    22092  21560  21400   2111   2210  -2364       C  
ATOM   3343  O   LEU B 195      37.581  67.682  80.706  1.00171.24           O  
ANISOU 3343  O   LEU B 195    22213  21242  21606   2215   2264  -2499       O  
ATOM   3344  CB  LEU B 195      37.723  65.982  78.367  1.00173.44           C  
ANISOU 3344  CB  LEU B 195    22723  21446  21728   2192   2093  -1831       C  
ATOM   3345  CG  LEU B 195      39.137  65.468  78.107  1.00175.79           C  
ANISOU 3345  CG  LEU B 195    23127  21689  21974   1942   2147  -1713       C  
ATOM   3346  CD1 LEU B 195      39.628  66.147  76.813  1.00178.34           C  
ANISOU 3346  CD1 LEU B 195    23762  21566  22432   2013   2203  -1528       C  
ATOM   3347  CD2 LEU B 195      40.105  65.674  79.285  1.00176.20           C  
ANISOU 3347  CD2 LEU B 195    23074  21833  22041   1732   2241  -1963       C  
ATOM   3348  N   ASN B 196      37.831  65.862  81.969  1.00171.21           N  
ANISOU 3348  N   ASN B 196    21922  21904  21224   1962   2237  -2490       N  
ATOM   3349  CA  ASN B 196      38.252  66.620  83.141  1.00174.47           C  
ANISOU 3349  CA  ASN B 196    22277  22359  21653   1924   2316  -2834       C  
ATOM   3350  C   ASN B 196      39.681  67.087  83.014  1.00182.44           C  
ANISOU 3350  C   ASN B 196    23427  23100  22789   1753   2349  -2905       C  
ATOM   3351  O   ASN B 196      40.580  66.278  82.773  1.00182.30           O  
ANISOU 3351  O   ASN B 196    23439  23137  22688   1566   2320  -2749       O  
ATOM   3352  CB  ASN B 196      38.059  65.783  84.380  1.00171.03           C  
ANISOU 3352  CB  ASN B 196    21638  22400  20945   1853   2329  -2931       C  
ATOM   3353  CG  ASN B 196      36.667  65.240  84.485  1.00167.81           C  
ANISOU 3353  CG  ASN B 196    21060  22249  20449   1995   2332  -2842       C  
ATOM   3354  OD1 ASN B 196      35.710  65.969  84.297  1.00164.79           O  
ANISOU 3354  OD1 ASN B 196    20646  21752  20214   2199   2349  -2932       O  
ATOM   3355  ND2 ASN B 196      36.548  63.941  84.747  1.00166.94           N  
ANISOU 3355  ND2 ASN B 196    20831  22466  20130   1887   2316  -2660       N  
ATOM   3356  N   THR B 197      39.903  68.390  83.191  1.00193.36           N  
ANISOU 3356  N   THR B 197    24879  24181  24405   1813   2411  -3155       N  
ATOM   3357  CA  THR B 197      41.250  68.998  83.095  1.00199.19           C  
ANISOU 3357  CA  THR B 197    25723  24608  25351   1647   2463  -3266       C  
ATOM   3358  C   THR B 197      41.583  69.864  84.317  1.00201.75           C  
ANISOU 3358  C   THR B 197    25949  24945  25758   1637   2484  -3714       C  
ATOM   3359  O   THR B 197      40.739  70.102  85.151  1.00199.50           O  
ANISOU 3359  O   THR B 197    25550  24881  25369   1784   2477  -3927       O  
ATOM   3360  CB  THR B 197      41.309  69.902  81.848  1.00203.05           C  
ANISOU 3360  CB  THR B 197    26439  24572  26138   1729   2536  -3108       C  
ATOM   3361  OG1 THR B 197      40.393  70.992  81.995  1.00206.18           O  
ANISOU 3361  OG1 THR B 197    26848  24794  26694   1957   2558  -3282       O  
ATOM   3362  CG2 THR B 197      40.904  69.130  80.609  1.00202.13           C  
ANISOU 3362  CG2 THR B 197    26445  24441  25914   1788   2495  -2695       C  
ATOM   3363  N   GLY B 198      42.801  70.343  84.399  1.00198.61           N  
ANISOU 3363  N   GLY B 198    25589  24307  25566   1473   2512  -3870       N  
ATOM   3364  CA  GLY B 198      43.201  71.333  85.392  1.00195.38           C  
ANISOU 3364  CA  GLY B 198    25104  23810  25318   1470   2515  -4326       C  
ATOM   3365  C   GLY B 198      43.782  70.734  86.689  1.00192.97           C  
ANISOU 3365  C   GLY B 198    24636  23927  24755   1364   2412  -4592       C  
ATOM   3366  O   GLY B 198      43.905  69.510  86.812  1.00195.62           O  
ANISOU 3366  O   GLY B 198    24922  24613  24790   1281   2350  -4392       O  
ATOM   3367  N   SER B 199      44.066  71.599  87.654  1.00189.84           N  
ANISOU 3367  N   SER B 199    24167  23496  24467   1393   2384  -5044       N  
ATOM   3368  CA  SER B 199      44.860  71.219  88.822  1.00187.01           C  
ANISOU 3368  CA  SER B 199    23685  23455  23912   1297   2261  -5344       C  
ATOM   3369  C   SER B 199      44.246  70.067  89.620  1.00180.39           C  
ANISOU 3369  C   SER B 199    22771  23210  22559   1366   2202  -5251       C  
ATOM   3370  O   SER B 199      44.959  69.183  90.103  1.00176.43           O  
ANISOU 3370  O   SER B 199    22219  22989  21825   1248   2100  -5234       O  
ATOM   3371  CB  SER B 199      45.075  72.424  89.733  1.00192.87           C  
ANISOU 3371  CB  SER B 199    24366  24066  24846   1369   2226  -5886       C  
ATOM   3372  OG  SER B 199      45.771  73.452  89.077  1.00196.47           O  
ANISOU 3372  OG  SER B 199    24876  23956  25817   1274   2288  -5985       O  
ATOM   3373  N   TYR B 200      42.924  70.085  89.776  1.00178.83           N  
ANISOU 3373  N   TYR B 200    22557  23191  22198   1562   2274  -5192       N  
ATOM   3374  CA  TYR B 200      42.296  69.038  90.565  1.00178.05           C  
ANISOU 3374  CA  TYR B 200    22378  23634  21639   1623   2264  -5099       C  
ATOM   3375  C   TYR B 200      42.499  67.668  89.950  1.00171.99           C  
ANISOU 3375  C   TYR B 200    21624  23018  20707   1481   2236  -4653       C  
ATOM   3376  O   TYR B 200      42.761  66.713  90.685  1.00165.29           O  
ANISOU 3376  O   TYR B 200    20726  22555  19522   1429   2176  -4613       O  
ATOM   3377  CB  TYR B 200      40.806  69.268  90.822  1.00182.31           C  
ANISOU 3377  CB  TYR B 200    22861  24336  22070   1851   2375  -5113       C  
ATOM   3378  CG  TYR B 200      40.174  68.047  91.493  1.00184.47           C  
ANISOU 3378  CG  TYR B 200    23049  25141  21900   1880   2410  -4932       C  
ATOM   3379  CD1 TYR B 200      40.215  67.880  92.872  1.00187.79           C  
ANISOU 3379  CD1 TYR B 200    23418  25968  21966   1945   2407  -5195       C  
ATOM   3380  CD2 TYR B 200      39.594  67.019  90.737  1.00181.34           C  
ANISOU 3380  CD2 TYR B 200    22632  24832  21438   1838   2445  -4490       C  
ATOM   3381  CE1 TYR B 200      39.669  66.744  93.481  1.00187.08           C  
ANISOU 3381  CE1 TYR B 200    23268  26342  21470   1966   2473  -4990       C  
ATOM   3382  CE2 TYR B 200      39.057  65.880  91.337  1.00179.22           C  
ANISOU 3382  CE2 TYR B 200    22274  25008  20810   1843   2496  -4308       C  
ATOM   3383  CZ  TYR B 200      39.096  65.742  92.703  1.00182.11           C  
ANISOU 3383  CZ  TYR B 200    22602  25760  20831   1902   2526  -4538       C  
ATOM   3384  OH  TYR B 200      38.605  64.606  93.319  1.00181.14           O  
ANISOU 3384  OH  TYR B 200    22413  26063  20347   1903   2606  -4328       O  
ATOM   3385  N   TYR B 201      42.410  67.568  88.627  1.00171.35           N  
ANISOU 3385  N   TYR B 201    21621  22633  20849   1432   2272  -4326       N  
ATOM   3386  CA  TYR B 201      42.531  66.275  87.955  1.00168.11           C  
ANISOU 3386  CA  TYR B 201    21224  22347  20301   1314   2241  -3913       C  
ATOM   3387  C   TYR B 201      43.969  65.902  87.635  1.00171.10           C  
ANISOU 3387  C   TYR B 201    21644  22595  20770   1098   2165  -3863       C  
ATOM   3388  O   TYR B 201      44.217  64.805  87.116  1.00173.08           O  
ANISOU 3388  O   TYR B 201    21904  22944  20912    992   2127  -3549       O  
ATOM   3389  CB  TYR B 201      41.718  66.307  86.693  1.00164.52           C  
ANISOU 3389  CB  TYR B 201    20842  21659  20009   1394   2297  -3607       C  
ATOM   3390  CG  TYR B 201      40.292  66.503  87.030  1.00163.18           C  
ANISOU 3390  CG  TYR B 201    20587  21657  19754   1602   2356  -3649       C  
ATOM   3391  CD1 TYR B 201      39.532  65.410  87.416  1.00162.40           C  
ANISOU 3391  CD1 TYR B 201    20370  21958  19376   1625   2366  -3474       C  
ATOM   3392  CD2 TYR B 201      39.700  67.773  87.035  1.00159.98           C  
ANISOU 3392  CD2 TYR B 201    20202  21016  19564   1777   2413  -3878       C  
ATOM   3393  CE1 TYR B 201      38.198  65.559  87.765  1.00161.58           C  
ANISOU 3393  CE1 TYR B 201    20152  22023  19219   1810   2445  -3524       C  
ATOM   3394  CE2 TYR B 201      38.377  67.931  87.382  1.00160.33           C  
ANISOU 3394  CE2 TYR B 201    20141  21232  19544   1977   2471  -3937       C  
ATOM   3395  CZ  TYR B 201      37.634  66.806  87.745  1.00161.29           C  
ANISOU 3395  CZ  TYR B 201    20126  21764  19391   1987   2494  -3760       C  
ATOM   3396  OH  TYR B 201      36.322  66.850  88.098  1.00164.25           O  
ANISOU 3396  OH  TYR B 201    20359  22331  19716   2167   2575  -3806       O  
ATOM   3397  N   GLU B 202      44.896  66.791  87.969  1.00177.69           N  
ANISOU 3397  N   GLU B 202    22482  23211  21819   1036   2139  -4190       N  
ATOM   3398  CA  GLU B 202      46.315  66.526  87.800  1.00183.14           C  
ANISOU 3398  CA  GLU B 202    23167  23781  22638    832   2068  -4214       C  
ATOM   3399  C   GLU B 202      46.940  66.274  89.160  1.00183.92           C  
ANISOU 3399  C   GLU B 202    23158  24211  22509    808   1924  -4533       C  
ATOM   3400  O   GLU B 202      48.106  65.906  89.243  1.00178.34           O  
ANISOU 3400  O   GLU B 202    22409  23493  21856    656   1823  -4590       O  
ATOM   3401  CB  GLU B 202      46.939  67.714  87.103  1.00191.31           C  
ANISOU 3401  CB  GLU B 202    24266  24284  24138    769   2151  -4344       C  
ATOM   3402  CG  GLU B 202      46.427  67.842  85.667  1.00194.10           C  
ANISOU 3402  CG  GLU B 202    24768  24315  24664    804   2284  -3972       C  
ATOM   3403  CD  GLU B 202      46.551  69.239  85.069  1.00200.58           C  
ANISOU 3403  CD  GLU B 202    25690  24607  25912    832   2411  -4085       C  
ATOM   3404  OE1 GLU B 202      46.655  70.228  85.834  1.00208.02           O  
ANISOU 3404  OE1 GLU B 202    26573  25444  27021    873   2402  -4478       O  
ATOM   3405  OE2 GLU B 202      46.526  69.349  83.818  1.00201.77           O  
ANISOU 3405  OE2 GLU B 202    25994  24440  26229    826   2522  -3775       O  
ATOM   3406  N   HIS B 203      46.145  66.451  90.222  1.00187.53           N  
ANISOU 3406  N   HIS B 203    23576  24978  22699    976   1915  -4741       N  
ATOM   3407  CA  HIS B 203      46.587  66.321  91.602  1.00188.90           C  
ANISOU 3407  CA  HIS B 203    23683  25496  22595   1015   1778  -5074       C  
ATOM   3408  C   HIS B 203      47.633  67.383  91.945  1.00198.08           C  
ANISOU 3408  C   HIS B 203    24803  26388  24070    959   1682  -5535       C  
ATOM   3409  O   HIS B 203      48.609  67.113  92.641  1.00206.11           O  
ANISOU 3409  O   HIS B 203    25759  27554  24997    895   1509  -5756       O  
ATOM   3410  CB  HIS B 203      47.112  64.890  91.887  1.00178.45           C  
ANISOU 3410  CB  HIS B 203    22340  24517  20946    921   1662  -4841       C  
ATOM   3411  CG  HIS B 203      46.395  63.793  91.149  1.00167.86           C  
ANISOU 3411  CG  HIS B 203    21029  23286  19465    897   1749  -4339       C  
ATOM   3412  ND1 HIS B 203      45.183  63.290  91.559  1.00166.56           N  
ANISOU 3412  ND1 HIS B 203    20853  23438  18992   1030   1840  -4178       N  
ATOM   3413  CD2 HIS B 203      46.752  63.057  90.070  1.00160.59           C  
ANISOU 3413  CD2 HIS B 203    20134  22211  18672    756   1752  -3984       C  
ATOM   3414  CE1 HIS B 203      44.820  62.296  90.766  1.00160.59           C  
ANISOU 3414  CE1 HIS B 203    20104  22705  18207    964   1880  -3755       C  
ATOM   3415  NE2 HIS B 203      45.744  62.158  89.832  1.00158.73           N  
ANISOU 3415  NE2 HIS B 203    19901  22183  18223    807   1822  -3636       N  
ATOM   3416  N   VAL B 204      47.420  68.595  91.441  1.00199.18           N  
ANISOU 3416  N   VAL B 204    24968  26111  24600    989   1787  -5683       N  
ATOM   3417  CA  VAL B 204      48.270  69.717  91.807  1.00194.67           C  
ANISOU 3417  CA  VAL B 204    24339  25247  24379    946   1716  -6155       C  
ATOM   3418  C   VAL B 204      47.431  70.868  92.368  1.00195.24           C  
ANISOU 3418  C   VAL B 204    24415  25255  24511   1147   1770  -6501       C  
ATOM   3419  O   VAL B 204      47.872  72.020  92.478  1.00191.60           O  
ANISOU 3419  O   VAL B 204    23920  24444  24433   1136   1755  -6878       O  
ATOM   3420  CB  VAL B 204      49.157  70.182  90.645  1.00189.47           C  
ANISOU 3420  CB  VAL B 204    23694  24043  24251    747   1795  -6052       C  
ATOM   3421  CG1 VAL B 204      49.865  68.968  90.055  1.00183.26           C  
ANISOU 3421  CG1 VAL B 204    22903  23353  23372    574   1761  -5690       C  
ATOM   3422  CG2 VAL B 204      48.333  70.924  89.599  1.00188.17           C  
ANISOU 3422  CG2 VAL B 204    23649  23487  24358    813   2002  -5831       C  
ATOM   3423  N   LYS B 205      46.174  70.561  92.690  1.00196.00           N  
ANISOU 3423  N   LYS B 205    24542  25669  24257   1332   1848  -6370       N  
ATOM   3424  CA  LYS B 205      45.324  71.548  93.360  1.00199.27           C  
ANISOU 3424  CA  LYS B 205    24944  26099  24668   1548   1898  -6720       C  
ATOM   3425  C   LYS B 205      45.861  71.754  94.758  1.00202.04           C  
ANISOU 3425  C   LYS B 205    25231  26736  24800   1618   1729  -7229       C  
ATOM   3426  O   LYS B 205      46.328  70.815  95.402  1.00199.39           O  
ANISOU 3426  O   LYS B 205    24880  26791  24089   1585   1603  -7200       O  
ATOM   3427  CB  LYS B 205      43.851  71.103  93.363  1.00196.74           C  
ANISOU 3427  CB  LYS B 205    24642  26067  24042   1725   2040  -6454       C  
ATOM   3428  CG  LYS B 205      42.846  72.167  93.810  1.00194.90           C  
ANISOU 3428  CG  LYS B 205    24389  25786  23875   1959   2130  -6764       C  
ATOM   3429  CD  LYS B 205      42.655  73.267  92.771  1.00191.39           C  
ANISOU 3429  CD  LYS B 205    23998  24756  23963   1971   2214  -6746       C  
ATOM   3430  CE  LYS B 205      42.083  74.534  93.359  1.00193.74           C  
ANISOU 3430  CE  LYS B 205    24266  24920  24424   2178   2247  -7198       C  
ATOM   3431  NZ  LYS B 205      43.021  75.287  94.224  1.00196.43           N  
ANISOU 3431  NZ  LYS B 205    24563  25175  24893   2152   2114  -7744       N  
ATOM   3432  N   ILE B 206      45.773  72.992  95.221  1.00206.93           N  
ANISOU 3432  N   ILE B 206    25822  27151  25649   1733   1715  -7699       N  
ATOM   3433  CA  ILE B 206      46.452  73.448  96.455  1.00211.23           C  
ANISOU 3433  CA  ILE B 206    26303  27855  26100   1799   1517  -8284       C  
ATOM   3434  C   ILE B 206      45.422  74.011  97.419  1.00209.70           C  
ANISOU 3434  C   ILE B 206    26115  27920  25641   2079   1569  -8615       C  
ATOM   3435  O   ILE B 206      44.354  74.454  96.979  1.00212.59           O  
ANISOU 3435  O   ILE B 206    26504  28149  26120   2193   1754  -8486       O  
ATOM   3436  CB  ILE B 206      47.448  74.583  96.074  1.00216.97           C  
ANISOU 3436  CB  ILE B 206    26966  28001  27470   1660   1445  -8629       C  
ATOM   3437  CG1 ILE B 206      46.806  75.641  95.155  1.00216.62           C  
ANISOU 3437  CG1 ILE B 206    26968  27428  27910   1689   1643  -8552       C  
ATOM   3438  CG2 ILE B 206      48.612  74.030  95.327  1.00216.06           C  
ANISOU 3438  CG2 ILE B 206    26818  27681  27594   1388   1388  -8389       C  
ATOM   3439  CD1 ILE B 206      47.443  77.012  95.191  1.00218.28           C  
ANISOU 3439  CD1 ILE B 206    27114  27117  28703   1647   1595  -9033       C  
ATOM   3440  N   SER B 207      45.755  74.005  98.723  1.00209.00           N  
ANISOU 3440  N   SER B 207    26005  28204  25200   2205   1398  -9054       N  
ATOM   3441  CA  SER B 207      44.810  74.498  99.736  1.00217.74           C  
ANISOU 3441  CA  SER B 207    27126  29609  25994   2492   1458  -9398       C  
ATOM   3442  C   SER B 207      43.446  73.796  99.846  1.00219.83           C  
ANISOU 3442  C   SER B 207    27434  30273  25817   2644   1693  -9026       C  
ATOM   3443  O   SER B 207      43.151  73.164 100.874  1.00225.26           O  
ANISOU 3443  O   SER B 207    28160  31504  25924   2792   1694  -9076       O  
ATOM   3444  CB  SER B 207      44.635  76.017  99.568  1.00223.44           C  
ANISOU 3444  CB  SER B 207    27803  29846  27245   2566   1485  -9821       C  
ATOM   3445  OG  SER B 207      45.853  76.636  99.165  1.00222.53           O  
ANISOU 3445  OG  SER B 207    27629  29250  27672   2369   1328 -10052       O  
ATOM   3446  N   ALA B 208      42.615  73.921  98.807  1.00220.41           N  
ANISOU 3446  N   ALA B 208    27501  30075  26170   2619   1891  -8666       N  
ATOM   3447  CA  ALA B 208      41.253  73.407  98.822  1.00217.93           C  
ANISOU 3447  CA  ALA B 208    27181  30064  25559   2762   2118  -8360       C  
ATOM   3448  C   ALA B 208      40.775  72.977  97.430  1.00210.27           C  
ANISOU 3448  C   ALA B 208    26209  28826  24856   2634   2244  -7794       C  
ATOM   3449  O   ALA B 208      41.273  73.484  96.419  1.00211.62           O  
ANISOU 3449  O   ALA B 208    26403  28493  25509   2496   2202  -7713       O  
ATOM   3450  CB  ALA B 208      40.311  74.463  99.366  1.00223.22           C  
ANISOU 3450  CB  ALA B 208    27811  30726  26276   3023   2230  -8758       C  
ATOM   3451  N   PRO B 209      39.830  72.032  97.394  1.00201.57           N  
ANISOU 3451  N   PRO B 209    25083  28064  23440   2682   2399  -7412       N  
ATOM   3452  CA  PRO B 209      39.195  71.642  96.143  1.00195.90           C  
ANISOU 3452  CA  PRO B 209    24349  27132  22949   2610   2505  -6924       C  
ATOM   3453  C   PRO B 209      37.993  72.510  95.782  1.00195.77           C  
ANISOU 3453  C   PRO B 209    24277  26913  23194   2804   2647  -6998       C  
ATOM   3454  O   PRO B 209      36.860  72.045  95.793  1.00193.04           O  
ANISOU 3454  O   PRO B 209    23850  26806  22689   2914   2801  -6795       O  
ATOM   3455  CB  PRO B 209      38.770  70.197  96.422  1.00192.23           C  
ANISOU 3455  CB  PRO B 209    23857  27148  22033   2575   2588  -6537       C  
ATOM   3456  CG  PRO B 209      38.427  70.196  97.868  1.00194.91           C  
ANISOU 3456  CG  PRO B 209    24177  27956  21921   2757   2656  -6849       C  
ATOM   3457  CD  PRO B 209      39.366  71.180  98.509  1.00199.58           C  
ANISOU 3457  CD  PRO B 209    24820  28417  22594   2796   2482  -7390       C  
ATOM   3458  N   ASN B 210      38.252  73.761  95.448  1.00197.08           N  
ANISOU 3458  N   ASN B 210    24475  26618  23787   2844   2594  -7285       N  
ATOM   3459  CA  ASN B 210      37.219  74.750  95.169  1.00202.46           C  
ANISOU 3459  CA  ASN B 210    25115  27056  24754   3053   2696  -7424       C  
ATOM   3460  C   ASN B 210      37.194  75.209  93.709  1.00204.67           C  
ANISOU 3460  C   ASN B 210    25468  26774  25522   2996   2683  -7143       C  
ATOM   3461  O   ASN B 210      36.442  76.125  93.367  1.00211.04           O  
ANISOU 3461  O   ASN B 210    26263  27297  26622   3175   2737  -7252       O  
ATOM   3462  CB  ASN B 210      37.486  75.951  96.090  1.00208.19           C  
ANISOU 3462  CB  ASN B 210    25833  27689  25581   3191   2647  -8043       C  
ATOM   3463  CG  ASN B 210      38.872  76.550  95.900  1.00208.91           C  
ANISOU 3463  CG  ASN B 210    25999  27382  25994   3015   2477  -8257       C  
ATOM   3464  OD1 ASN B 210      39.779  75.902  95.384  1.00202.36           O  
ANISOU 3464  OD1 ASN B 210    25220  26480  25185   2784   2396  -7986       O  
ATOM   3465  ND2 ASN B 210      39.038  77.793  96.319  1.00215.21           N  
ANISOU 3465  ND2 ASN B 210    26787  27907  27074   3125   2430  -8760       N  
ATOM   3466  N   GLU B 211      38.015  74.589  92.883  1.00205.37           N  
ANISOU 3466  N   GLU B 211    25641  26709  25681   2768   2613  -6795       N  
ATOM   3467  CA  GLU B 211      38.079  74.962  91.453  1.00207.02           C  
ANISOU 3467  CA  GLU B 211    25959  26395  26304   2715   2612  -6493       C  
ATOM   3468  C   GLU B 211      38.164  73.711  90.575  1.00210.61           C  
ANISOU 3468  C   GLU B 211    26451  26957  26612   2562   2602  -5956       C  
ATOM   3469  O   GLU B 211      39.042  72.859  90.771  1.00208.92           O  
ANISOU 3469  O   GLU B 211    26244  26939  26195   2366   2541  -5850       O  
ATOM   3470  CB  GLU B 211      39.324  75.811  91.142  1.00204.68           C  
ANISOU 3470  CB  GLU B 211    25763  25611  26393   2567   2545  -6673       C  
ATOM   3471  CG  GLU B 211      39.316  77.263  91.625  1.00208.06           C  
ANISOU 3471  CG  GLU B 211    26183  25723  27147   2704   2544  -7172       C  
ATOM   3472  CD  GLU B 211      40.665  77.986  91.476  1.00210.59           C  
ANISOU 3472  CD  GLU B 211    26560  25596  27856   2516   2480  -7385       C  
ATOM   3473  OE1 GLU B 211      40.755  79.170  91.882  1.00211.59           O  
ANISOU 3473  OE1 GLU B 211    26671  25431  28293   2606   2468  -7816       O  
ATOM   3474  OE2 GLU B 211      41.648  77.399  90.960  1.00213.37           O  
ANISOU 3474  OE2 GLU B 211    26959  25871  28241   2278   2448  -7144       O  
ATOM   3475  N   PHE B 212      37.254  73.608  89.626  1.00217.37           N  
ANISOU 3475  N   PHE B 212    27327  27684  27578   2666   2643  -5644       N  
ATOM   3476  CA  PHE B 212      37.192  72.432  88.761  1.00217.53           C  
ANISOU 3476  CA  PHE B 212    27375  27808  27469   2554   2621  -5161       C  
ATOM   3477  C   PHE B 212      37.057  72.852  87.300  1.00217.72           C  
ANISOU 3477  C   PHE B 212    27551  27353  27817   2596   2604  -4875       C  
ATOM   3478  O   PHE B 212      36.309  73.759  86.954  1.00216.30           O  
ANISOU 3478  O   PHE B 212    27400  26909  27875   2802   2625  -4953       O  
ATOM   3479  CB  PHE B 212      36.053  71.538  89.210  1.00217.00           C  
ANISOU 3479  CB  PHE B 212    27141  28210  27096   2656   2676  -5045       C  
ATOM   3480  CG  PHE B 212      36.243  71.006  90.591  1.00216.55           C  
ANISOU 3480  CG  PHE B 212    26978  28635  26664   2613   2714  -5253       C  
ATOM   3481  CD1 PHE B 212      36.884  69.808  90.800  1.00213.75           C  
ANISOU 3481  CD1 PHE B 212    26623  28567  26023   2422   2676  -5040       C  
ATOM   3482  CD2 PHE B 212      35.829  71.729  91.688  1.00220.68           C  
ANISOU 3482  CD2 PHE B 212    27422  29315  27111   2779   2783  -5671       C  
ATOM   3483  CE1 PHE B 212      37.067  69.298  92.090  1.00216.57           C  
ANISOU 3483  CE1 PHE B 212    26915  29375  25997   2407   2705  -5208       C  
ATOM   3484  CE2 PHE B 212      36.039  71.252  92.978  1.00222.92           C  
ANISOU 3484  CE2 PHE B 212    27643  30055  26998   2764   2818  -5863       C  
ATOM   3485  CZ  PHE B 212      36.654  70.043  93.181  1.00222.47           C  
ANISOU 3485  CZ  PHE B 212    27603  30288  26638   2583   2778  -5621       C  
ATOM   3486  N   ASP B 213      37.792  72.197  86.425  1.00215.18           N  
ANISOU 3486  N   ASP B 213    27342  26915  27498   2418   2565  -4541       N  
ATOM   3487  CA  ASP B 213      37.755  72.464  84.986  1.00213.33           C  
ANISOU 3487  CA  ASP B 213    27293  26259  27503   2457   2555  -4226       C  
ATOM   3488  C   ASP B 213      37.222  71.239  84.225  1.00211.43           C  
ANISOU 3488  C   ASP B 213    27040  26231  27062   2454   2499  -3819       C  
ATOM   3489  O   ASP B 213      37.837  70.168  84.241  1.00209.76           O  
ANISOU 3489  O   ASP B 213    26804  26245  26647   2260   2471  -3648       O  
ATOM   3490  CB  ASP B 213      39.132  72.935  84.497  1.00213.33           C  
ANISOU 3490  CB  ASP B 213    27459  25857  27738   2266   2585  -4210       C  
ATOM   3491  CG  ASP B 213      39.436  74.404  84.866  1.00214.90           C  
ANISOU 3491  CG  ASP B 213    27700  25671  28281   2323   2639  -4575       C  
ATOM   3492  OD1 ASP B 213      40.586  74.843  84.619  1.00216.56           O  
ANISOU 3492  OD1 ASP B 213    28003  25549  28728   2149   2683  -4618       O  
ATOM   3493  OD2 ASP B 213      38.553  75.119  85.395  1.00213.44           O  
ANISOU 3493  OD2 ASP B 213    27441  25497  28157   2534   2645  -4830       O  
ATOM   3494  N   VAL B 214      36.066  71.381  83.581  1.00209.91           N  
ANISOU 3494  N   VAL B 214    26848  25968  26940   2678   2466  -3685       N  
ATOM   3495  CA  VAL B 214      35.521  70.279  82.814  1.00205.42           C  
ANISOU 3495  CA  VAL B 214    26256  25569  26225   2692   2386  -3337       C  
ATOM   3496  C   VAL B 214      35.225  70.670  81.386  1.00208.34           C  
ANISOU 3496  C   VAL B 214    26835  25550  26774   2849   2318  -3081       C  
ATOM   3497  O   VAL B 214      34.446  71.598  81.147  1.00213.84           O  
ANISOU 3497  O   VAL B 214    27566  26022  27661   3092   2302  -3171       O  
ATOM   3498  CB  VAL B 214      34.288  69.617  83.410  1.00204.15           C  
ANISOU 3498  CB  VAL B 214    25836  25826  25904   2804   2375  -3375       C  
ATOM   3499  CG1 VAL B 214      33.872  68.427  82.544  1.00200.06           C  
ANISOU 3499  CG1 VAL B 214    25291  25441  25282   2785   2274  -3021       C  
ATOM   3500  CG2 VAL B 214      34.597  69.153  84.815  1.00205.56           C  
ANISOU 3500  CG2 VAL B 214    25846  26411  25845   2662   2460  -3586       C  
ATOM   3501  N   MET B 215      35.813  69.931  80.452  1.00208.64           N  
ANISOU 3501  N   MET B 215    27015  25525  26732   2729   2271  -2762       N  
ATOM   3502  CA  MET B 215      35.582  70.175  79.017  1.00211.22           C  
ANISOU 3502  CA  MET B 215    27581  25513  27160   2891   2200  -2482       C  
ATOM   3503  C   MET B 215      34.426  69.363  78.475  1.00208.27           C  
ANISOU 3503  C   MET B 215    27103  25351  26676   3058   2043  -2309       C  
ATOM   3504  O   MET B 215      34.397  68.134  78.565  1.00205.98           O  
ANISOU 3504  O   MET B 215    26675  25388  26197   2929   1989  -2191       O  
ATOM   3505  CB  MET B 215      36.820  69.878  78.188  1.00211.50           C  
ANISOU 3505  CB  MET B 215    27847  25340  27171   2704   2245  -2236       C  
ATOM   3506  CG  MET B 215      37.778  71.044  78.138  1.00216.66           C  
ANISOU 3506  CG  MET B 215    28688  25565  28067   2636   2393  -2333       C  
ATOM   3507  SD  MET B 215      39.343  70.619  77.327  1.00219.75           S  
ANISOU 3507  SD  MET B 215    29292  25754  28449   2371   2500  -2077       S  
ATOM   3508  CE  MET B 215      38.813  70.272  75.656  1.00219.79           C  
ANISOU 3508  CE  MET B 215    29569  25593  28347   2586   2412  -1652       C  
ATOM   3509  N   PHE B 216      33.471  70.060  77.889  1.00207.25           N  
ANISOU 3509  N   PHE B 216    27038  25015  26692   3354   1957  -2300       N  
ATOM   3510  CA  PHE B 216      32.436  69.423  77.054  1.00206.52           C  
ANISOU 3510  CA  PHE B 216    26901  25019  26547   3553   1765  -2117       C  
ATOM   3511  C   PHE B 216      32.889  69.585  75.618  1.00204.59           C  
ANISOU 3511  C   PHE B 216    27018  24423  26293   3644   1694  -1817       C  
ATOM   3512  O   PHE B 216      32.660  70.622  75.011  1.00202.98           O  
ANISOU 3512  O   PHE B 216    27033  23854  26237   3875   1674  -1786       O  
ATOM   3513  CB  PHE B 216      31.104  70.121  77.280  1.00215.93           C  
ANISOU 3513  CB  PHE B 216    27937  26195  27909   3855   1692  -2310       C  
ATOM   3514  CG  PHE B 216      30.378  69.678  78.520  1.00223.67           C  
ANISOU 3514  CG  PHE B 216    28529  27595  28858   3807   1750  -2554       C  
ATOM   3515  CD1 PHE B 216      31.054  69.320  79.683  1.00223.02           C  
ANISOU 3515  CD1 PHE B 216    28317  27777  28643   3540   1915  -2696       C  
ATOM   3516  CD2 PHE B 216      28.989  69.644  78.524  1.00234.62           C  
ANISOU 3516  CD2 PHE B 216    29680  29110  30353   4049   1643  -2646       C  
ATOM   3517  CE1 PHE B 216      30.358  68.922  80.815  1.00229.42           C  
ANISOU 3517  CE1 PHE B 216    28801  28975  29391   3519   1996  -2895       C  
ATOM   3518  CE2 PHE B 216      28.281  69.245  79.659  1.00239.77           C  
ANISOU 3518  CE2 PHE B 216    29969  30145  30987   4010   1740  -2857       C  
ATOM   3519  CZ  PHE B 216      28.963  68.881  80.804  1.00237.24           C  
ANISOU 3519  CZ  PHE B 216    29553  30089  30496   3746   1929  -2969       C  
ATOM   3520  N   LYS B 217      33.553  68.563  75.098  1.00207.52           N  
ANISOU 3520  N   LYS B 217    27462  24902  26482   3469   1668  -1594       N  
ATOM   3521  CA  LYS B 217      34.120  68.600  73.751  1.00214.35           C  
ANISOU 3521  CA  LYS B 217    28686  25470  27285   3531   1636  -1298       C  
ATOM   3522  C   LYS B 217      33.144  67.988  72.742  1.00211.39           C  
ANISOU 3522  C   LYS B 217    28336  25168  26812   3785   1379  -1132       C  
ATOM   3523  O   LYS B 217      32.481  67.008  73.042  1.00210.17           O  
ANISOU 3523  O   LYS B 217    27899  25360  26595   3758   1250  -1181       O  
ATOM   3524  CB  LYS B 217      35.417  67.780  73.715  1.00217.42           C  
ANISOU 3524  CB  LYS B 217    29132  25946  27531   3210   1746  -1169       C  
ATOM   3525  CG  LYS B 217      35.236  66.266  73.875  1.00216.09           C  
ANISOU 3525  CG  LYS B 217    28734  26193  27177   3074   1626  -1112       C  
ATOM   3526  CD  LYS B 217      36.438  65.616  74.548  1.00213.13           C  
ANISOU 3526  CD  LYS B 217    28278  25981  26718   2724   1765  -1134       C  
ATOM   3527  CE  LYS B 217      36.156  64.180  74.978  1.00211.38           C  
ANISOU 3527  CE  LYS B 217    27789  26179  26347   2589   1662  -1113       C  
ATOM   3528  NZ  LYS B 217      36.225  63.216  73.834  1.00207.75           N  
ANISOU 3528  NZ  LYS B 217    27445  25732  25758   2616   1521   -863       N  
ATOM   3529  N   LEU B 218      33.090  68.561  71.551  1.00207.64           N  
ANISOU 3529  N   LEU B 218    28205  24358  26328   4031   1307   -936       N  
ATOM   3530  CA  LEU B 218      32.192  68.066  70.515  1.00205.10           C  
ANISOU 3530  CA  LEU B 218    27945  24081  25902   4314   1025   -796       C  
ATOM   3531  C   LEU B 218      32.918  67.940  69.215  1.00206.62           C  
ANISOU 3531  C   LEU B 218    28549  24049  25908   4372   1020   -489       C  
ATOM   3532  O   LEU B 218      33.433  68.933  68.710  1.00209.80           O  
ANISOU 3532  O   LEU B 218    29296  24069  26349   4463   1160   -361       O  
ATOM   3533  CB  LEU B 218      31.035  69.037  70.378  1.00206.08           C  
ANISOU 3533  CB  LEU B 218    28070  24034  26196   4682    883   -904       C  
ATOM   3534  CG  LEU B 218      29.896  68.591  69.464  1.00208.34           C  
ANISOU 3534  CG  LEU B 218    28341  24395  26424   5018    537   -842       C  
ATOM   3535  CD1 LEU B 218      29.296  67.246  69.886  1.00205.85           C  
ANISOU 3535  CD1 LEU B 218    27609  24523  26080   4891    391   -951       C  
ATOM   3536  CD2 LEU B 218      28.844  69.681  69.481  1.00211.87           C  
ANISOU 3536  CD2 LEU B 218    28769  24651  27079   5372    420   -982       C  
ATOM   3537  N   GLU B 219      33.003  66.732  68.676  1.00204.10           N  
ANISOU 3537  N   GLU B 219    28204  23950  25391   4315    883   -368       N  
ATOM   3538  CA  GLU B 219      33.745  66.522  67.422  1.00204.39           C  
ANISOU 3538  CA  GLU B 219    28641  23805  25211   4371    895    -81       C  
ATOM   3539  C   GLU B 219      33.051  67.207  66.236  1.00206.70           C  
ANISOU 3539  C   GLU B 219    29276  23828  25432   4814    706     68       C  
ATOM   3540  O   GLU B 219      31.890  67.108  66.100  1.00201.17           O  
ANISOU 3540  O   GLU B 219    28433  23234  24768   5072    426    -30       O  
ATOM   3541  CB  GLU B 219      33.873  65.027  67.141  1.00204.47           C  
ANISOU 3541  CB  GLU B 219    28518  24133  25038   4238    753    -27       C  
ATOM   3542  CG  GLU B 219      35.023  64.672  66.193  1.00208.77           C  
ANISOU 3542  CG  GLU B 219    29410  24550  25362   4156    874    225       C  
ATOM   3543  CD  GLU B 219      34.643  64.500  64.733  1.00212.29           C  
ANISOU 3543  CD  GLU B 219    30191  24895  25575   4503    650    421       C  
ATOM   3544  OE1 GLU B 219      33.536  63.998  64.450  1.00215.41           O  
ANISOU 3544  OE1 GLU B 219    30438  25463  25943   4729    315    337       O  
ATOM   3545  OE2 GLU B 219      35.480  64.830  63.860  1.00212.26           O  
ANISOU 3545  OE2 GLU B 219    30596  24644  25408   4549    815    654       O  
ATOM   3546  N   VAL B 220      33.783  68.041  65.548  1.00215.09           N  
ANISOU 3546  N   VAL B 220    30766  24519  26440   4888    895    283       N  
ATOM   3547  CA  VAL B 220      33.225  68.815  64.462  1.00227.53           C  
ANISOU 3547  CA  VAL B 220    32722  25796  27930   5319    753    456       C  
ATOM   3548  C   VAL B 220      34.045  68.536  63.193  1.00223.02           C  
ANISOU 3548  C   VAL B 220    32608  25078  27052   5382    831    783       C  
ATOM   3549  O   VAL B 220      35.117  69.182  62.935  1.00228.15           O  
ANISOU 3549  O   VAL B 220    33570  25411  27703   5263   1174    977       O  
ATOM   3550  CB  VAL B 220      33.083  70.306  64.760  1.00241.94           C  
ANISOU 3550  CB  VAL B 220    34682  27245  29997   5453    900    426       C  
ATOM   3551  CG1 VAL B 220      32.507  71.024  63.525  1.00250.38           C  
ANISOU 3551  CG1 VAL B 220    36194  28002  30936   5937    728    650       C  
ATOM   3552  CG2 VAL B 220      32.169  70.506  65.969  1.00243.71           C  
ANISOU 3552  CG2 VAL B 220    34447  27656  30494   5432    800     79       C  
ATOM   3553  N   PRO B 221      33.524  67.565  62.424  1.00212.83           N  
ANISOU 3553  N   PRO B 221    31333  24017  25516   5568    519    825       N  
ATOM   3554  CA  PRO B 221      34.216  67.098  61.200  1.00209.73           C  
ANISOU 3554  CA  PRO B 221    31347  23562  24779   5651    552   1102       C  
ATOM   3555  C   PRO B 221      34.386  68.139  60.081  1.00215.27           C  
ANISOU 3555  C   PRO B 221    32638  23846  25309   5995    649   1408       C  
ATOM   3556  O   PRO B 221      33.630  69.105  60.016  1.00218.16           O  
ANISOU 3556  O   PRO B 221    33111  23995  25782   6293    540   1403       O  
ATOM   3557  CB  PRO B 221      33.297  65.965  60.727  1.00204.37           C  
ANISOU 3557  CB  PRO B 221    30502  23215  23933   5848    111    999       C  
ATOM   3558  CG  PRO B 221      31.934  66.450  61.070  1.00203.68           C  
ANISOU 3558  CG  PRO B 221    30193  23148  24046   6120   -180    801       C  
ATOM   3559  CD  PRO B 221      32.087  67.211  62.365  1.00206.52           C  
ANISOU 3559  CD  PRO B 221    30291  23430  24747   5862     87    645       C  
ATOM   3560  N   ARG B 222      35.284  67.816  59.167  1.00216.95           N  
ANISOU 3560  N   ARG B 222    33215  23981  25232   5981    818   1666       N  
ATOM   3561  CA  ARG B 222      35.442  68.507  57.882  1.00224.58           C  
ANISOU 3561  CA  ARG B 222    34794  24615  25918   6345    888   2005       C  
ATOM   3562  C   ARG B 222      35.588  70.014  57.974  1.00229.73           C  
ANISOU 3562  C   ARG B 222    35711  24802  26773   6435   1157   2151       C  
ATOM   3563  O   ARG B 222      34.861  70.777  57.305  1.00236.20           O  
ANISOU 3563  O   ARG B 222    36857  25393  27495   6875    987   2286       O  
ATOM   3564  CB  ARG B 222      34.231  68.212  56.993  1.00230.01           C  
ANISOU 3564  CB  ARG B 222    35622  25428  26340   6851    383   1996       C  
ATOM   3565  CG  ARG B 222      33.806  66.757  56.866  1.00229.02           C  
ANISOU 3565  CG  ARG B 222    35204  25746  26064   6833     23   1804       C  
ATOM   3566  CD  ARG B 222      32.296  66.640  56.989  1.00232.43           C  
ANISOU 3566  CD  ARG B 222    35359  26350  26604   7144   -485   1555       C  
ATOM   3567  NE  ARG B 222      31.693  65.752  56.005  1.00236.02           N  
ANISOU 3567  NE  ARG B 222    35907  27019  26751   7467   -919   1525       N  
ATOM   3568  CZ  ARG B 222      30.397  65.750  55.678  1.00240.53           C  
ANISOU 3568  CZ  ARG B 222    36388  27671  27330   7871  -1406   1366       C  
ATOM   3569  NH1 ARG B 222      29.522  66.596  56.248  1.00240.88           N  
ANISOU 3569  NH1 ARG B 222    36244  27602  27675   8015  -1517   1232       N  
ATOM   3570  NH2 ARG B 222      29.956  64.888  54.756  1.00243.64           N  
ANISOU 3570  NH2 ARG B 222    36871  28260  27442   8149  -1805   1318       N  
ATOM   3571  N   ILE B 223      36.526  70.446  58.800  1.00229.38           N  
ANISOU 3571  N   ILE B 223    35523  24604  27024   6029   1562   2114       N  
ATOM   3572  CA  ILE B 223      36.768  71.899  58.967  1.00236.12           C  
ANISOU 3572  CA  ILE B 223    36596  24975  28141   6062   1854   2230       C  
ATOM   3573  C   ILE B 223      38.098  72.372  58.412  1.00235.41           C  
ANISOU 3573  C   ILE B 223    36897  24526  28022   5900   2354   2549       C  
ATOM   3574  O   ILE B 223      39.015  71.584  58.240  1.00231.82           O  
ANISOU 3574  O   ILE B 223    36422  24221  27435   5639   2540   2608       O  
ATOM   3575  CB  ILE B 223      36.696  72.281  60.447  1.00238.14           C  
ANISOU 3575  CB  ILE B 223    36365  25267  28848   5754   1923   1889       C  
ATOM   3576  CG1 ILE B 223      37.526  71.324  61.305  1.00233.56           C  
ANISOU 3576  CG1 ILE B 223    35379  25009  28353   5260   2063   1694       C  
ATOM   3577  CG2 ILE B 223      35.241  72.271  60.894  1.00240.73           C  
ANISOU 3577  CG2 ILE B 223    36402  25803  29260   6013   1491   1627       C  
ATOM   3578  CD1 ILE B 223      37.809  71.912  62.683  1.00231.98           C  
ANISOU 3578  CD1 ILE B 223    34817  24747  28577   4939   2245   1415       C  
ATOM   3579  N   GLU B 224      38.152  73.660  58.104  1.00238.92           N  
ANISOU 3579  N   GLU B 224    37693  24482  28601   6075   2567   2757       N  
ATOM   3580  CA  GLU B 224      39.391  74.311  57.673  1.00240.78           C  
ANISOU 3580  CA  GLU B 224    38278  24293  28912   5904   3102   3060       C  
ATOM   3581  C   GLU B 224      39.619  75.568  58.526  1.00239.86           C  
ANISOU 3581  C   GLU B 224    38049  23767  29318   5729   3361   2957       C  
ATOM   3582  O   GLU B 224      38.712  76.386  58.716  1.00248.31           O  
ANISOU 3582  O   GLU B 224    39149  24658  30539   6000   3171   2892       O  
ATOM   3583  CB  GLU B 224      39.309  74.703  56.189  1.00251.12           C  
ANISOU 3583  CB  GLU B 224    40261  25324  29827   6345   3162   3513       C  
ATOM   3584  CG  GLU B 224      38.757  73.606  55.277  1.00256.98           C  
ANISOU 3584  CG  GLU B 224    41155  26456  30028   6657   2784   3575       C  
ATOM   3585  CD  GLU B 224      39.249  73.642  53.843  1.00270.02           C  
ANISOU 3585  CD  GLU B 224    43451  27921  31223   6928   2993   4024       C  
ATOM   3586  OE1 GLU B 224      39.352  74.770  53.345  1.00282.62           O  
ANISOU 3586  OE1 GLU B 224    45491  29040  32850   7135   3242   4335       O  
ATOM   3587  OE2 GLU B 224      39.518  72.557  53.263  1.00273.23           O  
ANISOU 3587  OE2 GLU B 224    43909  28649  31254   6934   2914   4055       O  
ATOM   3588  N   LEU B 225      40.827  75.690  59.067  1.00231.98           N  
ANISOU 3588  N   LEU B 225    36893  22632  28616   5275   3775   2908       N  
ATOM   3589  CA  LEU B 225      41.156  76.826  59.902  1.00229.95           C  
ANISOU 3589  CA  LEU B 225    36499  21988  28884   5072   4025   2769       C  
ATOM   3590  C   LEU B 225      41.860  77.905  59.115  1.00231.50           C  
ANISOU 3590  C   LEU B 225    37188  21566  29204   5131   4480   3160       C  
ATOM   3591  O   LEU B 225      42.817  77.650  58.396  1.00232.67           O  
ANISOU 3591  O   LEU B 225    37584  21609  29209   5009   4822   3440       O  
ATOM   3592  CB  LEU B 225      42.037  76.433  61.057  1.00225.36           C  
ANISOU 3592  CB  LEU B 225    35420  21585  28618   4548   4187   2438       C  
ATOM   3593  CG  LEU B 225      41.460  75.336  61.935  1.00221.64           C  
ANISOU 3593  CG  LEU B 225    34452  21717  28044   4441   3796   2066       C  
ATOM   3594  CD1 LEU B 225      42.269  75.245  63.213  1.00218.77           C  
ANISOU 3594  CD1 LEU B 225    33626  21450  28045   3967   3954   1721       C  
ATOM   3595  CD2 LEU B 225      39.977  75.540  62.255  1.00223.63           C  
ANISOU 3595  CD2 LEU B 225    34584  22115  28267   4779   3369   1885       C  
ATOM   3596  N   GLN B 226      41.408  79.136  59.286  1.00231.23           N  
ANISOU 3596  N   GLN B 226    37282  21103  29470   5306   4511   3175       N  
ATOM   3597  CA  GLN B 226      42.215  80.283  58.826  1.00236.97           C  
ANISOU 3597  CA  GLN B 226    38384  21173  30481   5254   5014   3490       C  
ATOM   3598  C   GLN B 226      42.854  80.950  60.011  1.00241.86           C  
ANISOU 3598  C   GLN B 226    38611  21557  31727   4837   5247   3162       C  
ATOM   3599  O   GLN B 226      42.166  81.559  60.805  1.00244.52           O  
ANISOU 3599  O   GLN B 226    38728  21827  32348   4907   5041   2874       O  
ATOM   3600  CB  GLN B 226      41.403  81.279  57.993  1.00239.63           C  
ANISOU 3600  CB  GLN B 226    39241  21088  30717   5767   4947   3820       C  
ATOM   3601  CG  GLN B 226      42.283  82.067  57.011  1.00244.73           C  
ANISOU 3601  CG  GLN B 226    40442  21138  31406   5792   5493   4328       C  
ATOM   3602  CD  GLN B 226      41.957  83.556  56.882  1.00247.99           C  
ANISOU 3602  CD  GLN B 226    41170  20892  32159   6028   5636   4512       C  
ATOM   3603  OE1 GLN B 226      41.623  84.031  55.802  1.00250.80           O  
ANISOU 3603  OE1 GLN B 226    42108  20950  32233   6448   5683   4957       O  
ATOM   3604  NE2 GLN B 226      42.092  84.304  57.968  1.00246.26           N  
ANISOU 3604  NE2 GLN B 226    40590  20430  32547   5765   5716   4176       N  
ATOM   3605  N   GLU B 227      44.154  80.821  60.142  1.00246.55           N  
ANISOU 3605  N   GLU B 227    39098  22036  32541   4414   5660   3175       N  
ATOM   3606  CA  GLU B 227      44.894  81.425  61.269  1.00249.44           C  
ANISOU 3606  CA  GLU B 227    39071  22173  33530   3992   5884   2830       C  
ATOM   3607  C   GLU B 227      44.593  82.910  61.380  1.00253.84           C  
ANISOU 3607  C   GLU B 227    39808  22115  34522   4139   6012   2868       C  
ATOM   3608  O   GLU B 227      44.774  83.643  60.435  1.00261.36           O  
ANISOU 3608  O   GLU B 227    41247  22567  35492   4319   6311   3299       O  
ATOM   3609  CB  GLU B 227      46.423  81.224  61.107  1.00253.87           C  
ANISOU 3609  CB  GLU B 227    39590  22575  34293   3563   6377   2932       C  
ATOM   3610  CG  GLU B 227      47.297  81.681  62.287  1.00256.73           C  
ANISOU 3610  CG  GLU B 227    39490  22760  35293   3098   6572   2524       C  
ATOM   3611  CD  GLU B 227      48.799  81.367  62.131  1.00262.67           C  
ANISOU 3611  CD  GLU B 227    40143  23403  36255   2675   7023   2589       C  
ATOM   3612  OE1 GLU B 227      49.205  80.590  61.240  1.00265.13           O  
ANISOU 3612  OE1 GLU B 227    40669  23884  36184   2697   7165   2896       O  
ATOM   3613  OE2 GLU B 227      49.610  81.901  62.923  1.00268.64           O  
ANISOU 3613  OE2 GLU B 227    40582  23901  37586   2315   7235   2304       O  
ATOM   3614  N   TYR B 228      44.083  83.323  62.533  1.00249.46           N  
ANISOU 3614  N   TYR B 228    38872  21612  34297   4086   5775   2419       N  
ATOM   3615  CA  TYR B 228      43.783  84.726  62.787  1.00251.94           C  
ANISOU 3615  CA  TYR B 228    39292  21353  35079   4208   5865   2375       C  
ATOM   3616  C   TYR B 228      45.090  85.500  62.866  1.00254.85           C  
ANISOU 3616  C   TYR B 228    39670  21154  36006   3832   6400   2425       C  
ATOM   3617  O   TYR B 228      45.758  85.525  63.905  1.00253.62           O  
ANISOU 3617  O   TYR B 228    39064  21042  36258   3437   6468   2005       O  
ATOM   3618  CB  TYR B 228      42.948  84.931  64.046  1.00249.39           C  
ANISOU 3618  CB  TYR B 228    38531  21258  34965   4236   5489   1839       C  
ATOM   3619  CG  TYR B 228      42.315  86.312  64.183  1.00252.07           C  
ANISOU 3619  CG  TYR B 228    39022  21059  35691   4492   5477   1804       C  
ATOM   3620  CD1 TYR B 228      41.477  86.815  63.193  1.00253.23           C  
ANISOU 3620  CD1 TYR B 228    39655  20937  35624   4979   5384   2195       C  
ATOM   3621  CD2 TYR B 228      42.514  87.089  65.332  1.00251.21           C  
ANISOU 3621  CD2 TYR B 228    38564  20733  36151   4273   5520   1351       C  
ATOM   3622  CE1 TYR B 228      40.889  88.060  63.322  1.00255.80           C  
ANISOU 3622  CE1 TYR B 228    40117  20762  36312   5228   5358   2161       C  
ATOM   3623  CE2 TYR B 228      41.913  88.329  65.476  1.00254.07           C  
ANISOU 3623  CE2 TYR B 228    39051  20604  36879   4516   5493   1293       C  
ATOM   3624  CZ  TYR B 228      41.099  88.811  64.466  1.00257.72           C  
ANISOU 3624  CZ  TYR B 228    39998  20783  37138   4993   5416   1707       C  
ATOM   3625  OH  TYR B 228      40.513  90.046  64.584  1.00264.96           O  
ANISOU 3625  OH  TYR B 228    41050  21188  38433   5250   5386   1662       O  
ATOM   3626  N   TYR B 229      45.441  86.102  61.728  1.00260.11           N  
ANISOU 3626  N   TYR B 229    40862  21295  36671   3972   6774   2950       N  
ATOM   3627  CA  TYR B 229      46.713  86.801  61.549  1.00265.24           C  
ANISOU 3627  CA  TYR B 229    41591  21357  37831   3634   7355   3107       C  
ATOM   3628  C   TYR B 229      47.904  85.838  61.640  1.00268.71           C  
ANISOU 3628  C   TYR B 229    41763  22097  38238   3198   7584   3035       C  
ATOM   3629  O   TYR B 229      47.998  84.862  60.894  1.00266.94           O  
ANISOU 3629  O   TYR B 229    41712  22234  37479   3276   7575   3297       O  
ATOM   3630  CB  TYR B 229      46.886  87.951  62.571  1.00262.66           C  
ANISOU 3630  CB  TYR B 229    40974  20569  38255   3433   7437   2718       C  
ATOM   3631  CG  TYR B 229      45.901  89.067  62.518  1.00263.21           C  
ANISOU 3631  CG  TYR B 229    41293  20218  38498   3815   7295   2775       C  
ATOM   3632  CD1 TYR B 229      44.897  89.189  63.476  1.00259.50           C  
ANISOU 3632  CD1 TYR B 229    40511  20013  38074   3971   6826   2314       C  
ATOM   3633  CD2 TYR B 229      46.010  90.055  61.548  1.00267.85           C  
ANISOU 3633  CD2 TYR B 229    42420  20106  39244   4014   7658   3284       C  
ATOM   3634  CE1 TYR B 229      44.008  90.253  63.439  1.00263.22           C  
ANISOU 3634  CE1 TYR B 229    41194  20071  38746   4329   6700   2346       C  
ATOM   3635  CE2 TYR B 229      45.131  91.121  61.507  1.00271.69           C  
ANISOU 3635  CE2 TYR B 229    43139  20162  39926   4373   7528   3339       C  
ATOM   3636  CZ  TYR B 229      44.131  91.215  62.453  1.00269.73           C  
ANISOU 3636  CZ  TYR B 229    42561  20195  39730   4532   7038   2857       C  
ATOM   3637  OH  TYR B 229      43.243  92.261  62.418  1.00275.33           O  
ANISOU 3637  OH  TYR B 229    43483  20483  40645   4904   6894   2890       O  
ATOM   3638  N   GLU B 230      48.832  86.109  62.549  1.00274.71           N  
ANISOU 3638  N   GLU B 230    42093  22703  39581   2747   7779   2661       N  
ATOM   3639  CA  GLU B 230      49.986  85.250  62.748  1.00274.69           C  
ANISOU 3639  CA  GLU B 230    41780  22967  39621   2326   7970   2534       C  
ATOM   3640  C   GLU B 230      50.174  85.066  64.240  1.00276.39           C  
ANISOU 3640  C   GLU B 230    41364  23478  40174   2016   7702   1870       C  
ATOM   3641  O   GLU B 230      51.283  84.919  64.745  1.00278.14           O  
ANISOU 3641  O   GLU B 230    41241  23668  40772   1599   7910   1627       O  
ATOM   3642  CB  GLU B 230      51.218  85.855  62.074  1.00276.95           C  
ANISOU 3642  CB  GLU B 230    42263  22636  40327   2074   8625   2858       C  
ATOM   3643  CG  GLU B 230      51.083  85.924  60.556  1.00278.85           C  
ANISOU 3643  CG  GLU B 230    43166  22640  40141   2394   8917   3547       C  
ATOM   3644  CD  GLU B 230      51.738  87.148  59.951  1.00287.12           C  
ANISOU 3644  CD  GLU B 230    44543  22848  41701   2322   9522   3913       C  
ATOM   3645  OE1 GLU B 230      52.475  87.000  58.955  1.00291.87           O  
ANISOU 3645  OE1 GLU B 230    45461  23258  42177   2271   9997   4365       O  
ATOM   3646  OE2 GLU B 230      51.509  88.267  60.456  1.00289.99           O  
ANISOU 3646  OE2 GLU B 230    44858  22727  42595   2324   9538   3758       O  
ATOM   3647  N   THR B 231      49.046  85.026  64.933  1.00275.47           N  
ANISOU 3647  N   THR B 231    41099  23681  39884   2246   7222   1576       N  
ATOM   3648  CA  THR B 231      49.017  84.834  66.377  1.00267.87           C  
ANISOU 3648  CA  THR B 231    39581  23060  39137   2032   6917    950       C  
ATOM   3649  C   THR B 231      49.414  83.414  66.741  1.00253.23           C  
ANISOU 3649  C   THR B 231    37406  21880  36928   1822   6739    777       C  
ATOM   3650  O   THR B 231      49.926  83.154  67.828  1.00243.31           O  
ANISOU 3650  O   THR B 231    35691  20852  35904   1524   6633    312       O  
ATOM   3651  CB  THR B 231      47.618  85.146  66.915  1.00270.50           C  
ANISOU 3651  CB  THR B 231    39882  23565  39329   2378   6483    733       C  
ATOM   3652  OG1 THR B 231      46.662  84.338  66.214  1.00272.83           O  
ANISOU 3652  OG1 THR B 231    40418  24279  38965   2730   6211   1021       O  
ATOM   3653  CG2 THR B 231      47.291  86.630  66.695  1.00275.40           C  
ANISOU 3653  CG2 THR B 231    40773  23476  40390   2566   6650    840       C  
ATOM   3654  N   GLY B 232      49.120  82.479  65.844  1.00245.75           N  
ANISOU 3654  N   GLY B 232    36710  21265  35398   2006   6672   1140       N  
ATOM   3655  CA  GLY B 232      49.382  81.071  66.088  1.00238.54           C  
ANISOU 3655  CA  GLY B 232    35533  20991  34110   1854   6480   1019       C  
ATOM   3656  C   GLY B 232      48.359  80.438  66.981  1.00233.39           C  
ANISOU 3656  C   GLY B 232    34594  20919  33162   1986   5967    677       C  
ATOM   3657  O   GLY B 232      48.133  79.232  66.874  1.00227.68           O  
ANISOU 3657  O   GLY B 232    33796  20731  31981   2019   5746    713       O  
ATOM   3658  N   ALA B 233      47.746  81.251  67.856  1.00235.36           N  
ANISOU 3658  N   ALA B 233    34682  21052  33690   2062   5797    346       N  
ATOM   3659  CA  ALA B 233      46.823  80.747  68.858  1.00231.18           C  
ANISOU 3659  CA  ALA B 233    33837  21055  32946   2159   5359    -25       C  
ATOM   3660  C   ALA B 233      45.374  80.824  68.410  1.00233.13           C  
ANISOU 3660  C   ALA B 233    34317  21403  32855   2609   5083    144       C  
ATOM   3661  O   ALA B 233      44.525  80.026  68.843  1.00228.83           O  
ANISOU 3661  O   ALA B 233    33582  21394  31969   2733   4729    -10       O  
ATOM   3662  CB  ALA B 233      46.979  81.531  70.154  1.00230.38           C  
ANISOU 3662  CB  ALA B 233    33391  20824  33319   1991   5317   -540       C  
ATOM   3663  N   PHE B 234      45.115  81.767  67.504  1.00241.43           N  
ANISOU 3663  N   PHE B 234    35788  21930  34014   2855   5256    479       N  
ATOM   3664  CA  PHE B 234      43.758  82.119  67.129  1.00245.42           C  
ANISOU 3664  CA  PHE B 234    36516  22418  34313   3307   4996    602       C  
ATOM   3665  C   PHE B 234      43.428  81.778  65.686  1.00241.00           C  
ANISOU 3665  C   PHE B 234    36432  21819  33318   3613   5010   1133       C  
ATOM   3666  O   PHE B 234      44.225  81.987  64.766  1.00243.29           O  
ANISOU 3666  O   PHE B 234    37056  21754  33629   3556   5363   1508       O  
ATOM   3667  CB  PHE B 234      43.533  83.609  67.376  1.00257.53           C  
ANISOU 3667  CB  PHE B 234    38148  23364  36337   3419   5108    505       C  
ATOM   3668  CG  PHE B 234      43.637  84.023  68.822  1.00262.04           C  
ANISOU 3668  CG  PHE B 234    38267  23989  37306   3202   5027    -67       C  
ATOM   3669  CD1 PHE B 234      42.766  83.511  69.776  1.00260.01           C  
ANISOU 3669  CD1 PHE B 234    37663  24269  36858   3283   4654   -447       C  
ATOM   3670  CD2 PHE B 234      44.565  84.986  69.218  1.00268.91           C  
ANISOU 3670  CD2 PHE B 234    39066  24345  38759   2938   5328   -234       C  
ATOM   3671  CE1 PHE B 234      42.843  83.921  71.106  1.00259.75           C  
ANISOU 3671  CE1 PHE B 234    37247  24295  37150   3117   4583   -978       C  
ATOM   3672  CE2 PHE B 234      44.636  85.406  70.546  1.00268.97           C  
ANISOU 3672  CE2 PHE B 234    38672  24399  39122   2770   5224   -794       C  
ATOM   3673  CZ  PHE B 234      43.776  84.865  71.489  1.00263.81           C  
ANISOU 3673  CZ  PHE B 234    37703  24316  38215   2870   4850  -1164       C  
ATOM   3674  N   TYR B 235      42.211  81.271  65.489  1.00233.92           N  
ANISOU 3674  N   TYR B 235    35564  21287  32028   3957   4621   1154       N  
ATOM   3675  CA  TYR B 235      41.790  80.774  64.196  1.00232.33           C  
ANISOU 3675  CA  TYR B 235    35766  21158  31348   4277   4536   1588       C  
ATOM   3676  C   TYR B 235      40.344  81.129  63.906  1.00227.87           C  
ANISOU 3676  C   TYR B 235    35356  20602  30621   4768   4178   1626       C  
ATOM   3677  O   TYR B 235      39.556  81.414  64.812  1.00220.29           O  
ANISOU 3677  O   TYR B 235    34091  19768  29838   4839   3936   1267       O  
ATOM   3678  CB  TYR B 235      41.958  79.266  64.143  1.00231.03           C  
ANISOU 3678  CB  TYR B 235    35412  21594  30773   4139   4377   1563       C  
ATOM   3679  CG  TYR B 235      43.401  78.899  64.219  1.00234.19           C  
ANISOU 3679  CG  TYR B 235    35719  21958  31302   3706   4733   1585       C  
ATOM   3680  CD1 TYR B 235      44.137  78.677  63.062  1.00237.61           C  
ANISOU 3680  CD1 TYR B 235    36526  22216  31536   3706   5020   2004       C  
ATOM   3681  CD2 TYR B 235      44.058  78.837  65.446  1.00233.66           C  
ANISOU 3681  CD2 TYR B 235    35198  22009  31572   3310   4794   1180       C  
ATOM   3682  CE1 TYR B 235      45.485  78.373  63.124  1.00237.86           C  
ANISOU 3682  CE1 TYR B 235    36450  22195  31730   3308   5369   2012       C  
ATOM   3683  CE2 TYR B 235      45.405  78.546  65.517  1.00234.35           C  
ANISOU 3683  CE2 TYR B 235    35180  22040  31823   2922   5108   1179       C  
ATOM   3684  CZ  TYR B 235      46.114  78.313  64.358  1.00236.00           C  
ANISOU 3684  CZ  TYR B 235    35733  22072  31863   2915   5401   1592       C  
ATOM   3685  OH  TYR B 235      47.452  78.017  64.391  1.00234.48           O  
ANISOU 3685  OH  TYR B 235    35419  21818  31854   2537   5726   1589       O  
ATOM   3686  N   LEU B 236      40.008  81.164  62.623  1.00231.43           N  
ANISOU 3686  N   LEU B 236    36293  20899  30741   5126   4154   2059       N  
ATOM   3687  CA  LEU B 236      38.639  81.264  62.192  1.00236.20           C  
ANISOU 3687  CA  LEU B 236    37049  21588  31107   5623   3756   2116       C  
ATOM   3688  C   LEU B 236      38.241  79.929  61.640  1.00232.62           C  
ANISOU 3688  C   LEU B 236    36584  21674  30127   5747   3463   2194       C  
ATOM   3689  O   LEU B 236      39.067  79.295  61.028  1.00230.82           O  
ANISOU 3689  O   LEU B 236    36520  21516  29663   5594   3660   2425       O  
ATOM   3690  CB  LEU B 236      38.385  82.425  61.227  1.00247.84           C  
ANISOU 3690  CB  LEU B 236    39083  22463  32622   6010   3874   2504       C  
ATOM   3691  CG  LEU B 236      37.740  83.635  61.926  1.00257.25           C  
ANISOU 3691  CG  LEU B 236    40168  23307  34267   6153   3800   2269       C  
ATOM   3692  CD1 LEU B 236      38.652  84.216  63.012  1.00259.04           C  
ANISOU 3692  CD1 LEU B 236    40078  23300  35045   5691   4125   1968       C  
ATOM   3693  CD2 LEU B 236      37.348  84.702  60.920  1.00266.26           C  
ANISOU 3693  CD2 LEU B 236    41882  23877  35406   6598   3854   2675       C  
ATOM   3694  N   VAL B 237      37.036  79.475  61.961  1.00231.66           N  
ANISOU 3694  N   VAL B 237    36209  21938  29870   5979   3011   1957       N  
ATOM   3695  CA  VAL B 237      36.616  78.102  61.642  1.00228.86           C  
ANISOU 3695  CA  VAL B 237    35726  22140  29089   6041   2698   1938       C  
ATOM   3696  C   VAL B 237      35.660  78.064  60.482  1.00228.93           C  
ANISOU 3696  C   VAL B 237    36109  22136  28737   6578   2378   2190       C  
ATOM   3697  O   VAL B 237      34.558  78.570  60.600  1.00229.88           O  
ANISOU 3697  O   VAL B 237    36185  22210  28949   6912   2085   2069       O  
ATOM   3698  CB  VAL B 237      35.915  77.475  62.854  1.00228.16           C  
ANISOU 3698  CB  VAL B 237    35036  22538  29116   5902   2410   1471       C  
ATOM   3699  CG1 VAL B 237      35.454  76.053  62.532  1.00225.98           C  
ANISOU 3699  CG1 VAL B 237    34608  22802  28453   5958   2091   1449       C  
ATOM   3700  CG2 VAL B 237      36.837  77.493  64.066  1.00227.30           C  
ANISOU 3700  CG2 VAL B 237    34557  22476  29329   5399   2687   1192       C  
ATOM   3701  N   LYS B 238      36.072  77.406  59.392  1.00227.30           N  
ANISOU 3701  N   LYS B 238    36246  22004  28112   6666   2413   2510       N  
ATOM   3702  CA  LYS B 238      35.230  77.244  58.213  1.00231.66           C  
ANISOU 3702  CA  LYS B 238    37180  22588  28250   7191   2080   2746       C  
ATOM   3703  C   LYS B 238      34.908  75.784  58.005  1.00233.36           C  
ANISOU 3703  C   LYS B 238    37179  23370  28116   7189   1752   2624       C  
ATOM   3704  O   LYS B 238      35.576  74.914  58.562  1.00234.88           O  
ANISOU 3704  O   LYS B 238    37046  23862  28336   6770   1877   2471       O  
ATOM   3705  CB  LYS B 238      35.943  77.750  56.962  1.00234.30           C  
ANISOU 3705  CB  LYS B 238    38184  22506  28332   7371   2393   3253       C  
ATOM   3706  CG  LYS B 238      35.855  79.249  56.700  1.00241.13           C  
ANISOU 3706  CG  LYS B 238    39441  22752  29425   7615   2586   3487       C  
ATOM   3707  CD  LYS B 238      36.768  79.611  55.513  1.00244.88           C  
ANISOU 3707  CD  LYS B 238    40563  22837  29642   7704   3000   4019       C  
ATOM   3708  CE  LYS B 238      36.257  80.743  54.585  1.00251.56           C  
ANISOU 3708  CE  LYS B 238    42022  23177  30380   8238   2985   4402       C  
ATOM   3709  NZ  LYS B 238      36.790  80.527  53.217  1.00253.74           N  
ANISOU 3709  NZ  LYS B 238    42922  23347  30138   8457   3186   4896       N  
ATOM   3710  N   PHE B 239      33.836  75.537  57.238  1.00239.80           N  
ANISOU 3710  N   PHE B 239    38156  24321  28635   7671   1306   2669       N  
ATOM   3711  CA  PHE B 239      33.447  74.176  56.895  1.00241.86           C  
ANISOU 3711  CA  PHE B 239    38248  25078  28567   7726    954   2559       C  
ATOM   3712  C   PHE B 239      33.747  73.886  55.447  1.00242.09           C  
ANISOU 3712  C   PHE B 239    38850  25046  28084   8028    941   2931       C  
ATOM   3713  O   PHE B 239      33.542  74.736  54.588  1.00251.11           O  
ANISOU 3713  O   PHE B 239    40511  25835  29062   8434    945   3229       O  
ATOM   3714  CB  PHE B 239      31.947  73.992  57.115  1.00246.91           C  
ANISOU 3714  CB  PHE B 239    38582  25964  29268   8054    406   2269       C  
ATOM   3715  CG  PHE B 239      31.591  73.612  58.506  1.00250.13           C  
ANISOU 3715  CG  PHE B 239    38316  26675  30047   7717    343   1844       C  
ATOM   3716  CD1 PHE B 239      31.753  72.304  58.940  1.00247.31           C  
ANISOU 3716  CD1 PHE B 239    37557  26775  29630   7402    266   1648       C  
ATOM   3717  CD2 PHE B 239      31.098  74.562  59.387  1.00256.64           C  
ANISOU 3717  CD2 PHE B 239    38917  27320  31271   7725    371   1643       C  
ATOM   3718  CE1 PHE B 239      31.415  71.938  60.232  1.00245.09           C  
ANISOU 3718  CE1 PHE B 239    36680  26779  29663   7105    229   1283       C  
ATOM   3719  CE2 PHE B 239      30.761  74.209  60.689  1.00254.59           C  
ANISOU 3719  CE2 PHE B 239    38051  27361  31317   7430    334   1252       C  
ATOM   3720  CZ  PHE B 239      30.921  72.893  61.108  1.00248.41           C  
ANISOU 3720  CZ  PHE B 239    36892  27041  30449   7122    270   1086       C  
ATOM   3721  N   LYS B 240      34.216  72.674  55.181  1.00235.01           N  
ANISOU 3721  N   LYS B 240    37868  24498  26924   7846    921   2912       N  
ATOM   3722  CA  LYS B 240      34.089  72.107  53.849  1.00237.82           C  
ANISOU 3722  CA  LYS B 240    38655  24956  26746   8220    709   3133       C  
ATOM   3723  C   LYS B 240      32.585  71.875  53.646  1.00239.30           C  
ANISOU 3723  C   LYS B 240    38701  25362  26860   8670     71   2915       C  
ATOM   3724  O   LYS B 240      31.949  72.561  52.852  1.00244.61           O  
ANISOU 3724  O   LYS B 240    39785  25813  27343   9179   -140   3092       O  
ATOM   3725  CB  LYS B 240      34.857  70.796  53.703  1.00238.94           C  
ANISOU 3725  CB  LYS B 240    38667  25448  26670   7918    791   3095       C  
ATOM   3726  CG  LYS B 240      36.362  70.904  53.843  1.00241.01           C  
ANISOU 3726  CG  LYS B 240    39038  25530  27006   7482   1397   3286       C  
ATOM   3727  CD  LYS B 240      37.001  69.510  54.022  1.00238.46           C  
ANISOU 3727  CD  LYS B 240    38412  25611  26581   7128   1417   3136       C  
ATOM   3728  CE  LYS B 240      38.316  69.537  54.817  1.00234.64           C  
ANISOU 3728  CE  LYS B 240    37708  25040  26402   6559   1935   3121       C  
ATOM   3729  NZ  LYS B 240      39.400  68.651  54.315  1.00233.68           N  
ANISOU 3729  NZ  LYS B 240    37689  25056  26041   6348   2180   3240       N  
ATOM   3730  N   ARG B 241      32.020  70.976  54.450  1.00236.69           N  
ANISOU 3730  N   ARG B 241    37763  25440  26729   8470   -214   2525       N  
ATOM   3731  CA  ARG B 241      30.718  70.384  54.178  1.00238.50           C  
ANISOU 3731  CA  ARG B 241    37786  25959  26873   8829   -822   2285       C  
ATOM   3732  C   ARG B 241      29.626  70.717  55.194  1.00237.50           C  
ANISOU 3732  C   ARG B 241    37139  25905  27192   8843  -1069   1938       C  
ATOM   3733  O   ARG B 241      29.643  70.202  56.296  1.00232.24           O  
ANISOU 3733  O   ARG B 241    35923  25483  26834   8437   -998   1661       O  
ATOM   3734  CB  ARG B 241      30.877  68.850  54.047  1.00236.00           C  
ANISOU 3734  CB  ARG B 241    37211  26085  26372   8640   -998   2127       C  
ATOM   3735  CG  ARG B 241      32.052  68.372  53.186  1.00235.30           C  
ANISOU 3735  CG  ARG B 241    37551  25979  25873   8552   -713   2416       C  
ATOM   3736  CD  ARG B 241      31.692  67.899  51.768  1.00235.49           C  
ANISOU 3736  CD  ARG B 241    38014  26094  25367   9051  -1075   2542       C  
ATOM   3737  NE  ARG B 241      31.652  68.991  50.787  1.00237.76           N  
ANISOU 3737  NE  ARG B 241    38974  26006  25357   9523  -1019   2899       N  
ATOM   3738  CZ  ARG B 241      30.563  69.656  50.371  1.00239.20           C  
ANISOU 3738  CZ  ARG B 241    39331  26060  25491  10045  -1416   2894       C  
ATOM   3739  NH1 ARG B 241      29.338  69.391  50.837  1.00236.02           N  
ANISOU 3739  NH1 ARG B 241    38454  25873  25348  10183  -1917   2525       N  
ATOM   3740  NH2 ARG B 241      30.694  70.626  49.476  1.00244.65           N  
ANISOU 3740  NH2 ARG B 241    40682  26388  25884  10445  -1299   3272       N  
ATOM   3741  N   ILE B 242      28.701  71.594  54.811  1.00243.14           N  
ANISOU 3741  N   ILE B 242    38048  26403  27931   9325  -1343   1964       N  
ATOM   3742  CA  ILE B 242      27.391  71.719  55.486  1.00247.48           C  
ANISOU 3742  CA  ILE B 242    38109  27088  28834   9480  -1723   1602       C  
ATOM   3743  C   ILE B 242      26.593  70.390  55.301  1.00253.50           C  
ANISOU 3743  C   ILE B 242    38491  28310  29515   9561  -2212   1319       C  
ATOM   3744  O   ILE B 242      25.925  70.249  54.283  1.00259.99           O  
ANISOU 3744  O   ILE B 242    39560  29156  30066  10046  -2645   1352       O  
ATOM   3745  CB  ILE B 242      26.613  72.987  54.962  1.00250.61           C  
ANISOU 3745  CB  ILE B 242    38859  27111  29248  10038  -1929   1721       C  
ATOM   3746  CG1 ILE B 242      25.315  73.237  55.759  1.00251.92           C  
ANISOU 3746  CG1 ILE B 242    38490  27385  29843  10176  -2262   1331       C  
ATOM   3747  CG2 ILE B 242      26.311  72.945  53.459  1.00251.59           C  
ANISOU 3747  CG2 ILE B 242    39556  27163  28871  10611  -2276   1969       C  
ATOM   3748  CD1 ILE B 242      24.580  74.502  55.351  1.00256.18           C  
ANISOU 3748  CD1 ILE B 242    39336  27546  30453  10704  -2455   1424       C  
ATOM   3749  N   PRO B 243      26.658  69.414  56.273  1.00255.32           N  
ANISOU 3749  N   PRO B 243    38130  28894  29985   9098  -2153   1041       N  
ATOM   3750  CA  PRO B 243      26.199  68.011  56.022  1.00258.02           C  
ANISOU 3750  CA  PRO B 243    38160  29642  30233   9088  -2524    830       C  
ATOM   3751  C   PRO B 243      24.817  67.845  55.409  1.00266.12           C  
ANISOU 3751  C   PRO B 243    39080  30774  31259   9601  -3144    627       C  
ATOM   3752  O   PRO B 243      24.662  67.142  54.400  1.00263.22           O  
ANISOU 3752  O   PRO B 243    38911  30535  30566   9863  -3481    649       O  
ATOM   3753  CB  PRO B 243      26.230  67.348  57.417  1.00251.63           C  
ANISOU 3753  CB  PRO B 243    36682  29113  29811   8555  -2346    547       C  
ATOM   3754  CG  PRO B 243      26.320  68.448  58.386  1.00249.29           C  
ANISOU 3754  CG  PRO B 243    36286  28601  29830   8407  -2025    523       C  
ATOM   3755  CD  PRO B 243      27.055  69.567  57.686  1.00251.92           C  
ANISOU 3755  CD  PRO B 243    37270  28504  29943   8593  -1773    884       C  
ATOM   3756  N   ARG B 244      23.815  68.461  56.034  1.00273.52           N  
ANISOU 3756  N   ARG B 244    39680  31668  32573   9745  -3305    400       N  
ATOM   3757  CA  ARG B 244      22.502  68.573  55.415  1.00281.65           C  
ANISOU 3757  CA  ARG B 244    40655  32722  33636  10294  -3888    222       C  
ATOM   3758  C   ARG B 244      21.780  69.811  55.998  1.00290.79           C  
ANISOU 3758  C   ARG B 244    41692  33643  35150  10490  -3885    126       C  
ATOM   3759  O   ARG B 244      22.193  70.943  55.690  1.00299.51           O  
ANISOU 3759  O   ARG B 244    43294  34374  36132  10674  -3682    405       O  
ATOM   3760  CB  ARG B 244      21.756  67.222  55.573  1.00275.19           C  
ANISOU 3760  CB  ARG B 244    39257  32315  32987  10202  -4264   -134       C  
ATOM   3761  CG  ARG B 244      20.734  66.931  54.488  1.00276.14           C  
ANISOU 3761  CG  ARG B 244    39451  32505  32964  10772  -4922   -273       C  
ATOM   3762  CD  ARG B 244      20.590  65.432  54.201  1.00269.77           C  
ANISOU 3762  CD  ARG B 244    38343  32047  32111  10646  -5208   -480       C  
ATOM   3763  NE  ARG B 244      20.000  65.216  52.880  1.00272.82           N  
ANISOU 3763  NE  ARG B 244    39028  32447  32183  11221  -5794   -520       N  
ATOM   3764  CZ  ARG B 244      19.920  64.042  52.249  1.00272.14           C  
ANISOU 3764  CZ  ARG B 244    38868  32599  31933  11263  -6125   -662       C  
ATOM   3765  NH1 ARG B 244      20.421  62.928  52.791  1.00265.86           N  
ANISOU 3765  NH1 ARG B 244    37716  32038  31260  10750  -5917   -755       N  
ATOM   3766  NH2 ARG B 244      19.360  63.986  51.039  1.00278.67           N  
ANISOU 3766  NH2 ARG B 244    40008  33419  32453  11843  -6681   -712       N  
ATOM   3767  N   GLY B 245      20.743  69.648  56.821  1.00292.53           N  
ANISOU 3767  N   GLY B 245    41277  34052  35818  10457  -4078   -251       N  
ATOM   3768  CA  GLY B 245      20.237  70.732  57.662  1.00293.37           C  
ANISOU 3768  CA  GLY B 245    41177  33973  36314  10503  -3950   -379       C  
ATOM   3769  C   GLY B 245      21.306  71.161  58.652  1.00290.24           C  
ANISOU 3769  C   GLY B 245    40791  33466  36019   9995  -3328   -262       C  
ATOM   3770  O   GLY B 245      21.452  72.352  58.920  1.00291.86           O  
ANISOU 3770  O   GLY B 245    41202  33345  36346  10078  -3113   -168       O  
ATOM   3771  N   ASN B 246      22.031  70.168  59.187  1.00284.60           N  
ANISOU 3771  N   ASN B 246    39842  33020  35272   9484  -3069   -285       N  
ATOM   3772  CA  ASN B 246      23.249  70.339  60.008  1.00280.94           C  
ANISOU 3772  CA  ASN B 246    39421  32495  34829   8972  -2501   -159       C  
ATOM   3773  C   ASN B 246      22.968  71.005  61.358  1.00278.13           C  
ANISOU 3773  C   ASN B 246    38661  32120  34896   8766  -2255   -396       C  
ATOM   3774  O   ASN B 246      22.450  72.129  61.410  1.00279.41           O  
ANISOU 3774  O   ASN B 246    38916  32013  35235   9062  -2303   -432       O  
ATOM   3775  CB  ASN B 246      24.341  71.130  59.269  1.00285.78           C  
ANISOU 3775  CB  ASN B 246    40726  32721  35133   9039  -2223    244       C  
ATOM   3776  CG  ASN B 246      25.642  71.268  60.082  1.00283.27           C  
ANISOU 3776  CG  ASN B 246    40424  32335  34870   8503  -1657    347       C  
ATOM   3777  OD1 ASN B 246      25.959  70.443  60.947  1.00273.79           O  
ANISOU 3777  OD1 ASN B 246    38811  31434  33779   8065  -1498    183       O  
ATOM   3778  ND2 ASN B 246      26.417  72.313  59.779  1.00290.27           N  
ANISOU 3778  ND2 ASN B 246    41796  32810  35683   8544  -1355    625       N  
ATOM   3779  N   PRO B 247      23.368  70.337  62.456  1.00268.87           N  
ANISOU 3779  N   PRO B 247    37071  31220  33867   8265  -1977   -547       N  
ATOM   3780  CA  PRO B 247      23.228  70.964  63.769  1.00268.12           C  
ANISOU 3780  CA  PRO B 247    36636  31121  34116   8057  -1705   -767       C  
ATOM   3781  C   PRO B 247      23.736  72.427  63.922  1.00269.14           C  
ANISOU 3781  C   PRO B 247    37120  30816  34322   8129  -1430   -647       C  
ATOM   3782  O   PRO B 247      23.130  73.185  64.710  1.00275.03           O  
ANISOU 3782  O   PRO B 247    37616  31498  35385   8200  -1386   -879       O  
ATOM   3783  CB  PRO B 247      24.047  70.032  64.672  1.00260.80           C  
ANISOU 3783  CB  PRO B 247    35432  30490  33170   7496  -1389   -811       C  
ATOM   3784  CG  PRO B 247      24.001  68.698  64.009  1.00257.13           C  
ANISOU 3784  CG  PRO B 247    34905  30290  32500   7461  -1630   -758       C  
ATOM   3785  CD  PRO B 247      23.785  68.919  62.550  1.00259.20           C  
ANISOU 3785  CD  PRO B 247    35627  30346  32511   7919  -1960   -561       C  
ATOM   3786  N   LEU B 248      24.859  72.715  63.271  1.00264.25           N  
ANISOU 3786  N   LEU B 248    37023  29932  33445   8064  -1217   -315       N  
ATOM   3787  CA  LEU B 248      25.699  73.856  63.540  1.00260.48           C  
ANISOU 3787  CA  LEU B 248    36849  29067  33053   7959   -845   -181       C  
ATOM   3788  C   LEU B 248      25.477  74.977  62.556  1.00260.21           C  
ANISOU 3788  C   LEU B 248    37330  28575  32962   8431   -961     49       C  
ATOM   3789  O   LEU B 248      26.213  75.974  62.574  1.00263.67           O  
ANISOU 3789  O   LEU B 248    38099  28615  33467   8380   -651    219       O  
ATOM   3790  CB  LEU B 248      27.157  73.377  63.482  1.00258.46           C  
ANISOU 3790  CB  LEU B 248    36804  28813  32582   7541   -493     40       C  
ATOM   3791  CG  LEU B 248      27.404  71.985  64.089  1.00257.14           C  
ANISOU 3791  CG  LEU B 248    36224  29122  32356   7141   -467   -104       C  
ATOM   3792  CD1 LEU B 248      28.801  71.487  63.782  1.00258.11           C  
ANISOU 3792  CD1 LEU B 248    36607  29224  32237   6813   -184    140       C  
ATOM   3793  CD2 LEU B 248      27.046  71.963  65.569  1.00253.87           C  
ANISOU 3793  CD2 LEU B 248    35264  28939  32253   6880   -346   -456       C  
ATOM   3794  N   SER B 249      24.445  74.840  61.726  1.00256.76           N  
ANISOU 3794  N   SER B 249    36950  28180  32427   8897  -1411     46       N  
ATOM   3795  CA  SER B 249      24.088  75.859  60.715  1.00258.55           C  
ANISOU 3795  CA  SER B 249    37684  27989  32564   9427  -1596    274       C  
ATOM   3796  C   SER B 249      23.647  77.141  61.348  1.00258.77           C  
ANISOU 3796  C   SER B 249    37644  27705  32970   9573  -1515    131       C  
ATOM   3797  O   SER B 249      23.889  78.218  60.805  1.00260.51           O  
ANISOU 3797  O   SER B 249    38347  27459  33175   9826  -1427    382       O  
ATOM   3798  CB  SER B 249      22.952  75.351  59.826  1.00259.54           C  
ANISOU 3798  CB  SER B 249    37788  28288  32536   9907  -2165    214       C  
ATOM   3799  OG  SER B 249      23.344  74.187  59.124  1.00256.63           O  
ANISOU 3799  OG  SER B 249    37526  28180  31800   9821  -2274    343       O  
ATOM   3800  N   HIS B 250      22.985  76.983  62.496  1.00256.90           N  
ANISOU 3800  N   HIS B 250    36804  27733  33071   9416  -1537   -271       N  
ATOM   3801  CA  HIS B 250      22.422  78.072  63.292  1.00261.27           C  
ANISOU 3801  CA  HIS B 250    37162  28079  34028   9535  -1480   -511       C  
ATOM   3802  C   HIS B 250      23.565  78.834  63.978  1.00264.20           C  
ANISOU 3802  C   HIS B 250    37687  28162  34534   9169   -973   -444       C  
ATOM   3803  O   HIS B 250      23.354  79.918  64.543  1.00272.25           O  
ANISOU 3803  O   HIS B 250    38668  28899  35873   9258   -863   -590       O  
ATOM   3804  CB  HIS B 250      21.465  77.542  64.387  1.00257.07           C  
ANISOU 3804  CB  HIS B 250    35912  27972  33788   9420  -1592   -971       C  
ATOM   3805  CG  HIS B 250      20.604  76.385  63.970  1.00253.21           C  
ANISOU 3805  CG  HIS B 250    35124  27885  33198   9558  -1993  -1084       C  
ATOM   3806  ND1 HIS B 250      20.983  75.072  64.158  1.00245.50           N  
ANISOU 3806  ND1 HIS B 250    33911  27309  32056   9185  -1937  -1099       N  
ATOM   3807  CD2 HIS B 250      19.374  76.345  63.405  1.00255.43           C  
ANISOU 3807  CD2 HIS B 250    35276  28217  33559  10024  -2465  -1212       C  
ATOM   3808  CE1 HIS B 250      20.031  74.275  63.709  1.00246.21           C  
ANISOU 3808  CE1 HIS B 250    33746  27665  32138   9406  -2347  -1228       C  
ATOM   3809  NE2 HIS B 250      19.045  75.022  63.248  1.00252.81           N  
ANISOU 3809  NE2 HIS B 250    34630  28302  33122   9914  -2680  -1308       N  
ATOM   3810  N   PHE B 251      24.750  78.220  63.983  1.00257.88           N  
ANISOU 3810  N   PHE B 251    37009  27454  33519   8750   -681   -267       N  
ATOM   3811  CA  PHE B 251      25.911  78.782  64.631  1.00251.05           C  
ANISOU 3811  CA  PHE B 251    36242  26357  32786   8363   -217   -228       C  
ATOM   3812  C   PHE B 251      26.878  79.349  63.617  1.00247.66           C  
ANISOU 3812  C   PHE B 251    36454  25471  32175   8424    -14    215       C  
ATOM   3813  O   PHE B 251      27.991  79.775  64.003  1.00244.96           O  
ANISOU 3813  O   PHE B 251    36231  24899  31942   8081    391    289       O  
ATOM   3814  CB  PHE B 251      26.597  77.761  65.528  1.00244.64           C  
ANISOU 3814  CB  PHE B 251    35059  25963  31928   7823      0   -386       C  
ATOM   3815  CG  PHE B 251      25.710  77.225  66.605  1.00241.28           C  
ANISOU 3815  CG  PHE B 251    34016  25975  31682   7734   -126   -799       C  
ATOM   3816  CD1 PHE B 251      24.916  78.075  67.376  1.00242.12           C  
ANISOU 3816  CD1 PHE B 251    33867  25996  32129   7896   -153  -1105       C  
ATOM   3817  CD2 PHE B 251      25.681  75.869  66.855  1.00236.83           C  
ANISOU 3817  CD2 PHE B 251    33128  25899  30956   7487   -195   -876       C  
ATOM   3818  CE1 PHE B 251      24.099  77.569  68.370  1.00240.57           C  
ANISOU 3818  CE1 PHE B 251    33103  26213  32088   7814   -228  -1474       C  
ATOM   3819  CE2 PHE B 251      24.870  75.355  67.846  1.00235.74           C  
ANISOU 3819  CE2 PHE B 251    32429  26155  30986   7396   -270  -1226       C  
ATOM   3820  CZ  PHE B 251      24.067  76.201  68.605  1.00238.54           C  
ANISOU 3820  CZ  PHE B 251    32531  26441  31662   7561   -278  -1524       C  
ATOM   3821  N   LEU B 252      26.398  79.474  62.371  1.00246.04           N  
ANISOU 3821  N   LEU B 252    36651  25101  31730   8888   -294    487       N  
ATOM   3822  CA  LEU B 252      27.195  80.032  61.282  1.00244.66           C  
ANISOU 3822  CA  LEU B 252    37140  24481  31337   9024   -110    953       C  
ATOM   3823  C   LEU B 252      26.930  81.516  61.068  1.00249.74           C  
ANISOU 3823  C   LEU B 252    38116  24550  32222   9368    -68   1070       C  
ATOM   3824  O   LEU B 252      25.809  81.956  61.101  1.00258.07           O  
ANISOU 3824  O   LEU B 252    39055  25569  33430   9756   -395    902       O  
ATOM   3825  CB  LEU B 252      26.990  79.266  59.974  1.00242.98           C  
ANISOU 3825  CB  LEU B 252    37257  24417  30645   9329   -404   1230       C  
ATOM   3826  CG  LEU B 252      27.633  77.873  59.913  1.00236.29           C  
ANISOU 3826  CG  LEU B 252    36262  24007  29509   8967   -345   1244       C  
ATOM   3827  CD1 LEU B 252      27.048  77.007  58.800  1.00236.84           C  
ANISOU 3827  CD1 LEU B 252    36496  24324  29166   9323   -771   1358       C  
ATOM   3828  CD2 LEU B 252      29.142  77.962  59.754  1.00233.43           C  
ANISOU 3828  CD2 LEU B 252    36219  23425  29046   8595    156   1535       C  
ATOM   3829  N   GLU B 253      27.998  82.279  60.842  1.00244.91           N  
ANISOU 3829  N   GLU B 253    37913  23473  31669   9215    348   1363       N  
ATOM   3830  CA  GLU B 253      27.909  83.676  60.425  1.00243.82           C  
ANISOU 3830  CA  GLU B 253    38205  22709  31722   9544    434   1582       C  
ATOM   3831  C   GLU B 253      28.547  83.785  59.042  1.00240.36           C  
ANISOU 3831  C   GLU B 253    38465  21962  30896   9740    566   2144       C  
ATOM   3832  O   GLU B 253      29.491  84.557  58.843  1.00242.01           O  
ANISOU 3832  O   GLU B 253    39040  21688  31224   9598    993   2429       O  
ATOM   3833  CB  GLU B 253      28.618  84.590  61.456  1.00242.77           C  
ANISOU 3833  CB  GLU B 253    37924  22238  32079   9176    855   1414       C  
ATOM   3834  CG  GLU B 253      27.698  85.265  62.472  1.00244.09           C  
ANISOU 3834  CG  GLU B 253    37676  22382  32684   9294    693    970       C  
ATOM   3835  CD  GLU B 253      27.048  86.548  61.952  1.00252.06           C  
ANISOU 3835  CD  GLU B 253    39047  22837  33887   9810    563   1120       C  
ATOM   3836  OE1 GLU B 253      26.342  86.506  60.922  1.00256.53           O  
ANISOU 3836  OE1 GLU B 253    39930  23366  34174  10304    227   1359       O  
ATOM   3837  OE2 GLU B 253      27.211  87.615  62.587  1.00256.28           O  
ANISOU 3837  OE2 GLU B 253    39546  22965  34864   9746    773    978       O  
ATOM   3838  N   GLY B 254      28.079  82.942  58.135  1.00233.56           N  
ANISOU 3838  N   GLY B 254    37758  21407  29577  10032    220   2281       N  
ATOM   3839  CA  GLY B 254      28.658  82.851  56.792  1.00232.96           C  
ANISOU 3839  CA  GLY B 254    38338  21140  29035  10232    322   2798       C  
ATOM   3840  C   GLY B 254      29.103  81.439  56.497  1.00228.22           C  
ANISOU 3840  C   GLY B 254    37633  21042  28037   9993    290   2807       C  
ATOM   3841  O   GLY B 254      28.295  80.543  56.509  1.00221.80           O  
ANISOU 3841  O   GLY B 254    36506  20692  27074  10120   -137   2563       O  
ATOM   3842  N   GLU B 255      30.391  81.290  56.238  1.00232.58           N  
ANISOU 3842  N   GLU B 255    38440  21468  28461   9650    756   3084       N  
ATOM   3843  CA  GLU B 255      31.101  80.033  56.129  1.00234.62           C  
ANISOU 3843  CA  GLU B 255    38572  22142  28428   9308    854   3085       C  
ATOM   3844  C   GLU B 255      31.851  79.777  57.415  1.00237.57           C  
ANISOU 3844  C   GLU B 255    38423  22665  29177   8677   1176   2783       C  
ATOM   3845  O   GLU B 255      32.478  78.719  57.569  1.00238.14           O  
ANISOU 3845  O   GLU B 255    38289  23097  29094   8323   1272   2719       O  
ATOM   3846  CB  GLU B 255      32.167  80.162  54.996  1.00234.87           C  
ANISOU 3846  CB  GLU B 255    39259  21876  28103   9334   1235   3612       C  
ATOM   3847  CG  GLU B 255      31.724  80.559  53.602  1.00238.42           C  
ANISOU 3847  CG  GLU B 255    40387  22084  28117   9953   1045   4025       C  
ATOM   3848  CD  GLU B 255      32.391  81.837  53.049  1.00242.88           C  
ANISOU 3848  CD  GLU B 255    41562  21968  28750  10064   1506   4496       C  
ATOM   3849  OE1 GLU B 255      33.254  82.460  53.704  1.00240.58           O  
ANISOU 3849  OE1 GLU B 255    41174  21352  28882   9646   1994   4506       O  
ATOM   3850  OE2 GLU B 255      31.995  82.232  51.960  1.00247.04           O  
ANISOU 3850  OE2 GLU B 255    42665  22277  28919  10595   1353   4846       O  
ATOM   3851  N   VAL B 256      31.701  80.736  58.340  1.00241.68           N  
ANISOU 3851  N   VAL B 256    38723  22921  30184   8577   1295   2573       N  
ATOM   3852  CA  VAL B 256      32.476  80.841  59.569  1.00238.89           C  
ANISOU 3852  CA  VAL B 256    37959  22574  30233   8027   1640   2304       C  
ATOM   3853  C   VAL B 256      31.634  80.458  60.768  1.00232.19           C  
ANISOU 3853  C   VAL B 256    36463  22138  29619   7922   1359   1789       C  
ATOM   3854  O   VAL B 256      30.651  81.104  61.065  1.00231.87           O  
ANISOU 3854  O   VAL B 256    36308  21998  29792   8214   1124   1608       O  
ATOM   3855  CB  VAL B 256      32.922  82.297  59.808  1.00246.26           C  
ANISOU 3855  CB  VAL B 256    39108  22872  31584   7995   1992   2403       C  
ATOM   3856  CG1 VAL B 256      34.077  82.316  60.806  1.00245.33           C  
ANISOU 3856  CG1 VAL B 256    38683  22725  31805   7396   2413   2211       C  
ATOM   3857  CG2 VAL B 256      33.279  82.989  58.488  1.00251.95           C  
ANISOU 3857  CG2 VAL B 256    40550  23081  32095   8309   2182   2953       C  
ATOM   3858  N   LEU B 257      32.060  79.445  61.513  1.00223.37           N  
ANISOU 3858  N   LEU B 257    34916  21465  28486   7495   1416   1551       N  
ATOM   3859  CA  LEU B 257      31.390  79.065  62.771  1.00218.17           C  
ANISOU 3859  CA  LEU B 257    33635  21202  28055   7336   1233   1073       C  
ATOM   3860  C   LEU B 257      31.557  80.113  63.865  1.00220.97           C  
ANISOU 3860  C   LEU B 257    33788  21288  28883   7161   1458    813       C  
ATOM   3861  O   LEU B 257      32.686  80.442  64.230  1.00215.73           O  
ANISOU 3861  O   LEU B 257    33167  20408  28390   6802   1840    843       O  
ATOM   3862  CB  LEU B 257      31.956  77.730  63.253  1.00208.92           C  
ANISOU 3862  CB  LEU B 257    32122  20531  26728   6911   1284    941       C  
ATOM   3863  CG  LEU B 257      31.319  77.041  64.460  1.00202.45           C  
ANISOU 3863  CG  LEU B 257    30679  20201  26042   6727   1109    505       C  
ATOM   3864  CD1 LEU B 257      29.870  76.676  64.200  1.00203.87           C  
ANISOU 3864  CD1 LEU B 257    30690  20633  26137   7121    650    381       C  
ATOM   3865  CD2 LEU B 257      32.099  75.791  64.799  1.00196.41           C  
ANISOU 3865  CD2 LEU B 257    29685  19835  25105   6304   1216    467       C  
ATOM   3866  N   SER B 258      30.433  80.632  64.361  1.00229.47           N  
ANISOU 3866  N   SER B 258    34637  22372  30179   7428   1213    543       N  
ATOM   3867  CA  SER B 258      30.450  81.707  65.360  1.00236.35           C  
ANISOU 3867  CA  SER B 258    35331  22970  31502   7336   1385    265       C  
ATOM   3868  C   SER B 258      30.578  81.150  66.771  1.00238.60           C  
ANISOU 3868  C   SER B 258    35044  23683  31927   6935   1454   -169       C  
ATOM   3869  O   SER B 258      29.732  80.394  67.210  1.00239.71           O  
ANISOU 3869  O   SER B 258    34806  24289  31982   6982   1200   -405       O  
ATOM   3870  CB  SER B 258      29.180  82.573  65.297  1.00237.12           C  
ANISOU 3870  CB  SER B 258    35433  22869  31791   7821   1103    147       C  
ATOM   3871  OG  SER B 258      29.126  83.479  66.393  1.00232.42           O  
ANISOU 3871  OG  SER B 258    34588  22088  31630   7718   1246   -196       O  
ATOM   3872  N   ALA B 259      31.618  81.589  67.485  1.00239.95           N  
ANISOU 3872  N   ALA B 259    35162  23670  32337   6560   1800   -279       N  
ATOM   3873  CA  ALA B 259      31.923  81.103  68.813  1.00233.48           C  
ANISOU 3873  CA  ALA B 259    33864  23230  31618   6173   1893   -667       C  
ATOM   3874  C   ALA B 259      30.926  81.685  69.828  1.00235.99           C  
ANISOU 3874  C   ALA B 259    33831  23626  32209   6328   1760  -1095       C  
ATOM   3875  O   ALA B 259      30.537  81.042  70.807  1.00233.24           O  
ANISOU 3875  O   ALA B 259    33040  23751  31828   6186   1684  -1421       O  
ATOM   3876  CB  ALA B 259      33.350  81.469  69.187  1.00230.71           C  
ANISOU 3876  CB  ALA B 259    33585  22619  31453   5765   2273   -665       C  
ATOM   3877  N   THR B 260      30.521  82.913  69.583  1.00243.47           N  
ANISOU 3877  N   THR B 260    34988  24094  33425   6631   1749  -1082       N  
ATOM   3878  CA  THR B 260      29.649  83.625  70.528  1.00249.66           C  
ANISOU 3878  CA  THR B 260    35465  24878  34514   6794   1656  -1500       C  
ATOM   3879  C   THR B 260      28.221  83.136  70.475  1.00255.06           C  
ANISOU 3879  C   THR B 260    35903  25929  35080   7129   1301  -1623       C  
ATOM   3880  O   THR B 260      27.598  83.052  71.541  1.00258.47           O  
ANISOU 3880  O   THR B 260    35898  26672  35634   7101   1252  -2029       O  
ATOM   3881  CB  THR B 260      29.731  85.147  70.399  1.00253.48           C  
ANISOU 3881  CB  THR B 260    36223  24700  35388   6987   1775  -1491       C  
ATOM   3882  OG1 THR B 260      31.103  85.529  70.484  1.00252.36           O  
ANISOU 3882  OG1 THR B 260    36261  24227  35396   6631   2123  -1398       O  
ATOM   3883  CG2 THR B 260      28.957  85.842  71.538  1.00253.47           C  
ANISOU 3883  CG2 THR B 260    35859  24732  35716   7101   1713  -1992       C  
ATOM   3884  N   LYS B 261      27.711  82.756  69.301  1.00255.88           N  
ANISOU 3884  N   LYS B 261    36249  26030  34942   7434   1058  -1302       N  
ATOM   3885  CA  LYS B 261      26.376  82.189  69.167  1.00255.16           C  
ANISOU 3885  CA  LYS B 261    35898  26296  34753   7745    692  -1421       C  
ATOM   3886  C   LYS B 261      26.288  80.822  69.874  1.00250.92           C  
ANISOU 3886  C   LYS B 261    34903  26407  34026   7436    666  -1615       C  
ATOM   3887  O   LYS B 261      25.381  80.537  70.670  1.00245.30           O  
ANISOU 3887  O   LYS B 261    33739  26045  33416   7481    550  -1952       O  
ATOM   3888  CB  LYS B 261      26.047  82.001  67.685  1.00255.29           C  
ANISOU 3888  CB  LYS B 261    36318  26167  34511   8110    435  -1019       C  
ATOM   3889  CG  LYS B 261      25.877  83.311  66.941  1.00260.81           C  
ANISOU 3889  CG  LYS B 261    37469  26250  35376   8508    401   -812       C  
ATOM   3890  CD  LYS B 261      25.433  83.126  65.495  1.00262.37           C  
ANISOU 3890  CD  LYS B 261    38074  26338  35276   8934    102   -434       C  
ATOM   3891  CE  LYS B 261      24.990  84.460  64.900  1.00268.66           C  
ANISOU 3891  CE  LYS B 261    39256  26554  36266   9405     10   -283       C  
ATOM   3892  NZ  LYS B 261      24.264  84.349  63.613  1.00270.32           N  
ANISOU 3892  NZ  LYS B 261    39806  26700  36204   9923   -374      0       N  
ATOM   3893  N   MET B 262      27.247  79.978  69.517  1.00252.66           N  
ANISOU 3893  N   MET B 262    35263  26763  33973   7133    787  -1374       N  
ATOM   3894  CA  MET B 262      27.371  78.654  70.100  1.00254.18           C  
ANISOU 3894  CA  MET B 262    35091  27514  33972   6809    792  -1491       C  
ATOM   3895  C   MET B 262      27.444  78.760  71.621  1.00251.02           C  
ANISOU 3895  C   MET B 262    34275  27340  33760   6536    983  -1899       C  
ATOM   3896  O   MET B 262      26.707  78.084  72.347  1.00251.67           O  
ANISOU 3896  O   MET B 262    33929  27866  33828   6499    893  -2147       O  
ATOM   3897  CB  MET B 262      28.608  77.973  69.540  1.00256.64           C  
ANISOU 3897  CB  MET B 262    35665  27829  34018   6509    953  -1179       C  
ATOM   3898  CG  MET B 262      28.464  76.472  69.427  1.00256.57           C  
ANISOU 3898  CG  MET B 262    35435  28324  33725   6366    806  -1138       C  
ATOM   3899  SD  MET B 262      29.555  75.834  68.136  1.00258.35           S  
ANISOU 3899  SD  MET B 262    36118  28437  33606   6263    865   -679       S  
ATOM   3900  CE  MET B 262      29.275  74.080  68.332  1.00253.71           C  
ANISOU 3900  CE  MET B 262    35150  28471  32774   6066    687   -748       C  
ATOM   3901  N   LEU B 263      28.313  79.654  72.085  1.00247.06           N  
ANISOU 3901  N   LEU B 263    33909  26513  33448   6364   1249  -1971       N  
ATOM   3902  CA  LEU B 263      28.501  79.867  73.520  1.00241.07           C  
ANISOU 3902  CA  LEU B 263    32810  25931  32852   6122   1430  -2374       C  
ATOM   3903  C   LEU B 263      27.225  80.366  74.181  1.00239.25           C  
ANISOU 3903  C   LEU B 263    32269  25801  32833   6405   1302  -2724       C  
ATOM   3904  O   LEU B 263      26.918  79.983  75.308  1.00240.49           O  
ANISOU 3904  O   LEU B 263    32030  26356  32988   6264   1360  -3048       O  
ATOM   3905  CB  LEU B 263      29.660  80.822  73.812  1.00241.05           C  
ANISOU 3905  CB  LEU B 263    33020  25505  33062   5916   1706  -2411       C  
ATOM   3906  CG  LEU B 263      30.108  80.899  75.286  1.00235.44           C  
ANISOU 3906  CG  LEU B 263    31985  25012  32457   5615   1889  -2827       C  
ATOM   3907  CD1 LEU B 263      30.859  79.648  75.716  1.00224.96           C  
ANISOU 3907  CD1 LEU B 263    30492  24137  30845   5227   1968  -2800       C  
ATOM   3908  CD2 LEU B 263      30.922  82.152  75.548  1.00238.84           C  
ANISOU 3908  CD2 LEU B 263    32598  24929  33221   5534   2095  -2948       C  
ATOM   3909  N   SER B 264      26.464  81.194  73.475  1.00235.62           N  
ANISOU 3909  N   SER B 264    31990  24990  32542   6819   1130  -2653       N  
ATOM   3910  CA  SER B 264      25.191  81.722  73.995  1.00234.38           C  
ANISOU 3910  CA  SER B 264    31540  24892  32619   7136    989  -2984       C  
ATOM   3911  C   SER B 264      24.111  80.659  74.148  1.00232.59           C  
ANISOU 3911  C   SER B 264    30913  25197  32263   7221    786  -3089       C  
ATOM   3912  O   SER B 264      23.403  80.638  75.158  1.00237.89           O  
ANISOU 3912  O   SER B 264    31171  26158  33057   7234    820  -3454       O  
ATOM   3913  CB  SER B 264      24.679  82.886  73.145  1.00236.18           C  
ANISOU 3913  CB  SER B 264    32084  24580  33074   7580    836  -2864       C  
ATOM   3914  OG  SER B 264      25.527  84.001  73.275  1.00237.43           O  
ANISOU 3914  OG  SER B 264    32519  24236  33457   7501   1059  -2863       O  
ATOM   3915  N   LYS B 265      23.978  79.783  73.156  1.00227.67           N  
ANISOU 3915  N   LYS B 265    30402  24696  31404   7281    586  -2784       N  
ATOM   3916  CA  LYS B 265      23.003  78.692  73.243  1.00225.63           C  
ANISOU 3916  CA  LYS B 265    29750  24923  31056   7332    390  -2876       C  
ATOM   3917  C   LYS B 265      23.399  77.703  74.352  1.00221.34           C  
ANISOU 3917  C   LYS B 265    28854  24871  30373   6898    607  -3036       C  
ATOM   3918  O   LYS B 265      22.559  77.268  75.146  1.00221.94           O  
ANISOU 3918  O   LYS B 265    28483  25321  30521   6896    605  -3304       O  
ATOM   3919  CB  LYS B 265      22.848  77.968  71.904  1.00225.15           C  
ANISOU 3919  CB  LYS B 265    29907  24864  30774   7490    110  -2531       C  
ATOM   3920  CG  LYS B 265      21.611  77.073  71.796  1.00227.51           C  
ANISOU 3920  CG  LYS B 265    29806  25548  31087   7660   -172  -2652       C  
ATOM   3921  CD  LYS B 265      20.309  77.866  71.700  1.00236.26           C  
ANISOU 3921  CD  LYS B 265    30754  26516  32495   8126   -409  -2868       C  
ATOM   3922  CE  LYS B 265      19.116  76.949  71.460  1.00239.26           C  
ANISOU 3922  CE  LYS B 265    30736  27248  32923   8298   -713  -2978       C  
ATOM   3923  NZ  LYS B 265      19.082  76.400  70.070  1.00241.53           N  
ANISOU 3923  NZ  LYS B 265    31310  27465  32994   8494  -1047  -2671       N  
ATOM   3924  N   PHE B 266      24.681  77.371  74.389  1.00219.55           N  
ANISOU 3924  N   PHE B 266    28837  24628  29953   6544    801  -2862       N  
ATOM   3925  CA  PHE B 266      25.270  76.536  75.425  1.00218.57           C  
ANISOU 3925  CA  PHE B 266    28460  24909  29677   6131   1015  -2984       C  
ATOM   3926  C   PHE B 266      24.897  77.082  76.826  1.00217.77           C  
ANISOU 3926  C   PHE B 266    28032  24959  29749   6103   1189  -3409       C  
ATOM   3927  O   PHE B 266      24.383  76.359  77.698  1.00216.64           O  
ANISOU 3927  O   PHE B 266    27498  25267  29547   5993   1249  -3602       O  
ATOM   3928  CB  PHE B 266      26.798  76.569  75.237  1.00218.70           C  
ANISOU 3928  CB  PHE B 266    28814  24724  29558   5822   1204  -2777       C  
ATOM   3929  CG  PHE B 266      27.545  75.457  75.930  1.00217.83           C  
ANISOU 3929  CG  PHE B 266    28528  25017  29219   5410   1351  -2782       C  
ATOM   3930  CD1 PHE B 266      27.311  74.120  75.584  1.00216.31           C  
ANISOU 3930  CD1 PHE B 266    28199  25175  28812   5322   1227  -2614       C  
ATOM   3931  CD2 PHE B 266      28.543  75.739  76.873  1.00217.29           C  
ANISOU 3931  CD2 PHE B 266    28451  24952  29157   5116   1596  -2948       C  
ATOM   3932  CE1 PHE B 266      28.017  73.087  76.207  1.00211.28           C  
ANISOU 3932  CE1 PHE B 266    27418  24886  27971   4954   1358  -2599       C  
ATOM   3933  CE2 PHE B 266      29.254  74.705  77.489  1.00212.84           C  
ANISOU 3933  CE2 PHE B 266    27746  24754  28369   4762   1705  -2940       C  
ATOM   3934  CZ  PHE B 266      28.990  73.381  77.156  1.00209.05           C  
ANISOU 3934  CZ  PHE B 266    27136  24615  27674   4682   1593  -2753       C  
ATOM   3935  N   ARG B 267      25.145  78.374  76.994  1.00218.52           N  
ANISOU 3935  N   ARG B 267    28308  24655  30064   6219   1276  -3547       N  
ATOM   3936  CA  ARG B 267      24.863  79.058  78.235  1.00221.50           C  
ANISOU 3936  CA  ARG B 267    28436  25107  30615   6230   1432  -3968       C  
ATOM   3937  C   ARG B 267      23.394  79.002  78.597  1.00223.36           C  
ANISOU 3937  C   ARG B 267    28287  25593  30984   6508   1323  -4212       C  
ATOM   3938  O   ARG B 267      23.034  78.728  79.743  1.00217.93           O  
ANISOU 3938  O   ARG B 267    27246  25285  30273   6410   1471  -4510       O  
ATOM   3939  CB  ARG B 267      25.387  80.499  78.156  1.00229.11           C  
ANISOU 3939  CB  ARG B 267    29696  25515  31839   6334   1509  -4048       C  
ATOM   3940  CG  ARG B 267      25.677  81.159  79.495  1.00232.31           C  
ANISOU 3940  CG  ARG B 267    29933  25963  32371   6213   1721  -4477       C  
ATOM   3941  CD  ARG B 267      26.189  82.571  79.293  1.00234.95           C  
ANISOU 3941  CD  ARG B 267    30565  25690  33014   6318   1777  -4540       C  
ATOM   3942  NE  ARG B 267      26.044  83.385  80.495  1.00233.85           N  
ANISOU 3942  NE  ARG B 267    30224  25555  33072   6348   1904  -5025       N  
ATOM   3943  CZ  ARG B 267      26.830  83.311  81.569  1.00228.65           C  
ANISOU 3943  CZ  ARG B 267    29456  25090  32331   6055   2086  -5291       C  
ATOM   3944  NH1 ARG B 267      27.856  82.458  81.614  1.00225.46           N  
ANISOU 3944  NH1 ARG B 267    29113  24883  31666   5696   2167  -5113       N  
ATOM   3945  NH2 ARG B 267      26.601  84.104  82.609  1.00227.20           N  
ANISOU 3945  NH2 ARG B 267    29102  24901  32323   6139   2175  -5755       N  
ATOM   3946  N   LYS B 268      22.541  79.234  77.607  1.00229.17           N  
ANISOU 3946  N   LYS B 268    29090  26127  31854   6864   1066  -4082       N  
ATOM   3947  CA  LYS B 268      21.070  79.189  77.776  1.00231.27           C  
ANISOU 3947  CA  LYS B 268    28975  26593  32302   7169    919  -4304       C  
ATOM   3948  C   LYS B 268      20.599  77.834  78.289  1.00227.27           C  
ANISOU 3948  C   LYS B 268    28054  26662  31636   6974    958  -4346       C  
ATOM   3949  O   LYS B 268      19.852  77.755  79.276  1.00231.34           O  
ANISOU 3949  O   LYS B 268    28162  27486  32248   6994   1084  -4662       O  
ATOM   3950  CB  LYS B 268      20.400  79.454  76.413  1.00232.30           C  
ANISOU 3950  CB  LYS B 268    29301  26418  32545   7565    575  -4082       C  
ATOM   3951  CG  LYS B 268      19.113  80.236  76.379  1.00235.90           C  
ANISOU 3951  CG  LYS B 268    29558  26743  33330   8011    397  -4329       C  
ATOM   3952  CD  LYS B 268      18.826  80.526  74.898  1.00235.19           C  
ANISOU 3952  CD  LYS B 268    29813  26281  33267   8374     49  -4026       C  
ATOM   3953  CE  LYS B 268      19.235  81.907  74.316  1.00235.59           C  
ANISOU 3953  CE  LYS B 268    30343  25704  33467   8621     18  -3907       C  
ATOM   3954  NZ  LYS B 268      18.354  83.023  74.769  1.00238.67           N  
ANISOU 3954  NZ  LYS B 268    30563  25890  34230   8968    -24  -4248       N  
ATOM   3955  N   ILE B 269      21.029  76.766  77.618  1.00220.77           N  
ANISOU 3955  N   ILE B 269    27334  25973  30577   6790    866  -4026       N  
ATOM   3956  CA  ILE B 269      20.712  75.398  78.046  1.00218.19           C  
ANISOU 3956  CA  ILE B 269    26646  26153  30102   6567    912  -4019       C  
ATOM   3957  C   ILE B 269      21.154  75.169  79.496  1.00219.08           C  
ANISOU 3957  C   ILE B 269    26550  26597  30092   6252   1253  -4238       C  
ATOM   3958  O   ILE B 269      20.357  74.718  80.333  1.00222.30           O  
ANISOU 3958  O   ILE B 269    26541  27377  30545   6235   1370  -4449       O  
ATOM   3959  CB  ILE B 269      21.452  74.371  77.175  1.00213.39           C  
ANISOU 3959  CB  ILE B 269    26261  25583  29233   6360    804  -3641       C  
ATOM   3960  CG1 ILE B 269      21.019  74.481  75.699  1.00215.79           C  
ANISOU 3960  CG1 ILE B 269    26794  25603  29592   6687    448  -3415       C  
ATOM   3961  CG2 ILE B 269      21.228  72.948  77.695  1.00209.15           C  
ANISOU 3961  CG2 ILE B 269    25361  25543  28561   6094    878  -3630       C  
ATOM   3962  CD1 ILE B 269      22.124  74.140  74.708  1.00213.39           C  
ANISOU 3962  CD1 ILE B 269    26939  25108  29030   6552    388  -3037       C  
ATOM   3963  N   ILE B 270      22.417  75.478  79.787  1.00218.70           N  
ANISOU 3963  N   ILE B 270    26791  26414  29891   6013   1414  -4189       N  
ATOM   3964  CA  ILE B 270      22.948  75.289  81.135  1.00218.91           C  
ANISOU 3964  CA  ILE B 270    26669  26743  29763   5733   1702  -4398       C  
ATOM   3965  C   ILE B 270      22.130  76.030  82.209  1.00220.24           C  
ANISOU 3965  C   ILE B 270    26550  27027  30104   5910   1848  -4822       C  
ATOM   3966  O   ILE B 270      21.836  75.465  83.264  1.00225.55           O  
ANISOU 3966  O   ILE B 270    26917  28128  30654   5781   2045  -4994       O  
ATOM   3967  CB  ILE B 270      24.430  75.710  81.167  1.00217.59           C  
ANISOU 3967  CB  ILE B 270    26868  26327  29478   5503   1803  -4319       C  
ATOM   3968  CG1 ILE B 270      25.255  74.693  80.375  1.00211.37           C  
ANISOU 3968  CG1 ILE B 270    26276  25571  28462   5263   1728  -3932       C  
ATOM   3969  CG2 ILE B 270      24.962  75.793  82.599  1.00219.76           C  
ANISOU 3969  CG2 ILE B 270    27016  26858  29624   5286   2059  -4613       C  
ATOM   3970  CD1 ILE B 270      26.565  75.237  79.880  1.00209.45           C  
ANISOU 3970  CD1 ILE B 270    26442  24941  28199   5131   1760  -3775       C  
ATOM   3971  N   LYS B 271      21.764  77.281  81.938  1.00216.50           N  
ANISOU 3971  N   LYS B 271    26183  26169  29907   6214   1764  -4982       N  
ATOM   3972  CA  LYS B 271      20.959  78.042  82.890  1.00218.65           C  
ANISOU 3972  CA  LYS B 271    26186  26522  30369   6416   1891  -5404       C  
ATOM   3973  C   LYS B 271      19.590  77.387  83.098  1.00223.63           C  
ANISOU 3973  C   LYS B 271    26361  27519  31088   6561   1879  -5504       C  
ATOM   3974  O   LYS B 271      19.100  77.285  84.238  1.00225.45           O  
ANISOU 3974  O   LYS B 271    26267  28099  31293   6538   2109  -5796       O  
ATOM   3975  CB  LYS B 271      20.771  79.484  82.415  1.00219.94           C  
ANISOU 3975  CB  LYS B 271    26556  26155  30853   6745   1766  -5529       C  
ATOM   3976  CG  LYS B 271      22.003  80.384  82.570  1.00217.43           C  
ANISOU 3976  CG  LYS B 271    26600  25467  30547   6615   1860  -5573       C  
ATOM   3977  CD  LYS B 271      21.755  81.789  82.031  1.00221.68           C  
ANISOU 3977  CD  LYS B 271    27347  25438  31442   6952   1737  -5662       C  
ATOM   3978  CE  LYS B 271      22.552  82.875  82.730  1.00222.90           C  
ANISOU 3978  CE  LYS B 271    27659  25306  31724   6883   1897  -5942       C  
ATOM   3979  NZ  LYS B 271      22.526  84.138  81.947  1.00226.50           N  
ANISOU 3979  NZ  LYS B 271    28410  25122  32525   7164   1768  -5899       N  
ATOM   3980  N   GLU B 272      18.985  76.955  81.993  1.00227.81           N  
ANISOU 3980  N   GLU B 272    26866  27963  31726   6717   1614  -5270       N  
ATOM   3981  CA  GLU B 272      17.696  76.264  82.043  1.00233.75           C  
ANISOU 3981  CA  GLU B 272    27165  29028  32619   6844   1567  -5347       C  
ATOM   3982  C   GLU B 272      17.746  75.054  82.955  1.00234.98           C  
ANISOU 3982  C   GLU B 272    27032  29707  32542   6514   1825  -5338       C  
ATOM   3983  O   GLU B 272      16.913  74.910  83.846  1.00239.55           O  
ANISOU 3983  O   GLU B 272    27212  30598  33205   6556   2025  -5592       O  
ATOM   3984  CB  GLU B 272      17.253  75.796  80.633  1.00234.82           C  
ANISOU 3984  CB  GLU B 272    27361  29006  32853   7010   1202  -5063       C  
ATOM   3985  CG  GLU B 272      16.635  76.858  79.724  1.00238.96           C  
ANISOU 3985  CG  GLU B 272    28025  29094  33672   7455    904  -5107       C  
ATOM   3986  CD  GLU B 272      16.140  76.319  78.373  1.00238.28           C  
ANISOU 3986  CD  GLU B 272    27984  28906  33643   7646    519  -4852       C  
ATOM   3987  OE1 GLU B 272      15.863  77.141  77.480  1.00238.97           O  
ANISOU 3987  OE1 GLU B 272    28305  28603  33890   8002    246  -4805       O  
ATOM   3988  OE2 GLU B 272      16.036  75.102  78.172  1.00235.92           O  
ANISOU 3988  OE2 GLU B 272    27510  28897  33230   7462    471  -4701       O  
ATOM   3989  N   GLU B 273      18.725  74.187  82.737  1.00233.91           N  
ANISOU 3989  N   GLU B 273    27100  29659  32116   6194   1834  -5040       N  
ATOM   3990  CA  GLU B 273      18.849  72.990  83.572  1.00235.22           C  
ANISOU 3990  CA  GLU B 273    27030  30296  32045   5877   2071  -4987       C  
ATOM   3991  C   GLU B 273      19.198  73.331  85.025  1.00234.08           C  
ANISOU 3991  C   GLU B 273    26826  30388  31724   5754   2415  -5262       C  
ATOM   3992  O   GLU B 273      18.710  72.674  85.961  1.00232.49           O  
ANISOU 3992  O   GLU B 273    26301  30603  31432   5650   2664  -5360       O  
ATOM   3993  CB  GLU B 273      19.906  72.046  82.981  1.00238.27           C  
ANISOU 3993  CB  GLU B 273    27681  30684  32165   5579   1983  -4612       C  
ATOM   3994  CG  GLU B 273      20.005  70.674  83.635  1.00242.14           C  
ANISOU 3994  CG  GLU B 273    27947  31620  32434   5265   2172  -4490       C  
ATOM   3995  CD  GLU B 273      18.669  69.947  83.731  1.00247.97           C  
ANISOU 3995  CD  GLU B 273    28208  32625  33384   5346   2196  -4541       C  
ATOM   3996  OE1 GLU B 273      17.823  70.094  82.820  1.00254.02           O  
ANISOU 3996  OE1 GLU B 273    28860  33215  34440   5598   1935  -4542       O  
ATOM   3997  OE2 GLU B 273      18.461  69.230  84.735  1.00250.45           O  
ANISOU 3997  OE2 GLU B 273    28255  33323  33579   5162   2481  -4585       O  
ATOM   3998  N   VAL B 274      20.015  74.367  85.220  1.00232.26           N  
ANISOU 3998  N   VAL B 274    26905  29889  31454   5777   2434  -5393       N  
ATOM   3999  CA  VAL B 274      20.425  74.792  86.564  1.00227.09           C  
ANISOU 3999  CA  VAL B 274    26231  29427  30624   5688   2715  -5696       C  
ATOM   4000  C   VAL B 274      19.239  75.290  87.394  1.00223.95           C  
ANISOU 4000  C   VAL B 274    25473  29217  30401   5935   2890  -6075       C  
ATOM   4001  O   VAL B 274      19.205  75.116  88.619  1.00216.92           O  
ANISOU 4001  O   VAL B 274    24423  28691  29304   5848   3179  -6285       O  
ATOM   4002  CB  VAL B 274      21.544  75.874  86.509  1.00227.52           C  
ANISOU 4002  CB  VAL B 274    26679  29091  30675   5674   2664  -5789       C  
ATOM   4003  CG1 VAL B 274      21.703  76.630  87.843  1.00229.40           C  
ANISOU 4003  CG1 VAL B 274    26864  29459  30839   5704   2896  -6219       C  
ATOM   4004  CG2 VAL B 274      22.867  75.213  86.138  1.00224.22           C  
ANISOU 4004  CG2 VAL B 274    26555  28634  30002   5349   2613  -5473       C  
ATOM   4005  N   LYS B 275      18.271  75.908  86.734  1.00224.47           N  
ANISOU 4005  N   LYS B 275    25416  29039  30832   6258   2718  -6165       N  
ATOM   4006  CA  LYS B 275      17.021  76.279  87.410  1.00227.97           C  
ANISOU 4006  CA  LYS B 275    25459  29667  31491   6509   2874  -6513       C  
ATOM   4007  C   LYS B 275      16.294  75.061  87.986  1.00226.05           C  
ANISOU 4007  C   LYS B 275    24804  29931  31153   6370   3099  -6461       C  
ATOM   4008  O   LYS B 275      15.646  75.164  89.022  1.00230.43           O  
ANISOU 4008  O   LYS B 275    25061  30784  31704   6441   3390  -6749       O  
ATOM   4009  CB  LYS B 275      16.133  77.094  86.465  1.00230.69           C  
ANISOU 4009  CB  LYS B 275    25750  29633  32269   6893   2595  -6588       C  
ATOM   4010  CG  LYS B 275      16.723  78.495  86.235  1.00232.09           C  
ANISOU 4010  CG  LYS B 275    26291  29322  32569   7065   2475  -6731       C  
ATOM   4011  CD  LYS B 275      16.197  79.266  85.047  1.00232.73           C  
ANISOU 4011  CD  LYS B 275    26484  28929  33011   7414   2138  -6672       C  
ATOM   4012  CE  LYS B 275      16.950  80.594  84.947  1.00232.97           C  
ANISOU 4012  CE  LYS B 275    26906  28473  33140   7520   2084  -6785       C  
ATOM   4013  NZ  LYS B 275      16.376  81.530  83.952  1.00234.84           N  
ANISOU 4013  NZ  LYS B 275    27262  28224  33741   7913   1792  -6773       N  
ATOM   4014  N   GLU B 276      16.462  73.905  87.356  1.00219.77           N  
ANISOU 4014  N   GLU B 276    24003  29229  30268   6160   2991  -6095       N  
ATOM   4015  CA  GLU B 276      15.747  72.698  87.759  1.00217.38           C  
ANISOU 4015  CA  GLU B 276    23303  29347  29943   6019   3185  -6004       C  
ATOM   4016  C   GLU B 276      16.409  71.928  88.895  1.00216.92           C  
ANISOU 4016  C   GLU B 276    23266  29693  29458   5701   3526  -5942       C  
ATOM   4017  O   GLU B 276      15.858  70.935  89.383  1.00218.78           O  
ANISOU 4017  O   GLU B 276    23186  30288  29651   5568   3753  -5859       O  
ATOM   4018  CB  GLU B 276      15.477  71.781  86.555  1.00211.92           C  
ANISOU 4018  CB  GLU B 276    22545  28566  29407   5969   2897  -5674       C  
ATOM   4019  CG  GLU B 276      14.469  72.362  85.577  1.00213.45           C  
ANISOU 4019  CG  GLU B 276    22588  28470  30042   6330   2587  -5774       C  
ATOM   4020  CD  GLU B 276      13.140  72.715  86.247  1.00219.04           C  
ANISOU 4020  CD  GLU B 276    22808  29356  31059   6565   2779  -6129       C  
ATOM   4021  OE1 GLU B 276      12.400  71.792  86.670  1.00219.80           O  
ANISOU 4021  OE1 GLU B 276    22481  29790  31241   6456   2981  -6123       O  
ATOM   4022  OE2 GLU B 276      12.834  73.929  86.364  1.00223.20           O  
ANISOU 4022  OE2 GLU B 276    23367  29674  31765   6859   2744  -6421       O  
ATOM   4023  N   ILE B 277      17.584  72.385  89.333  1.00213.98           N  
ANISOU 4023  N   ILE B 277    23261  29256  28783   5585   3563  -5983       N  
ATOM   4024  CA  ILE B 277      18.267  71.786  90.480  1.00211.43           C  
ANISOU 4024  CA  ILE B 277    22996  29310  28025   5329   3857  -5966       C  
ATOM   4025  C   ILE B 277      17.820  72.367  91.816  1.00211.94           C  
ANISOU 4025  C   ILE B 277    22895  29650  27982   5465   4194  -6361       C  
ATOM   4026  O   ILE B 277      18.172  73.507  92.123  1.00210.39           O  
ANISOU 4026  O   ILE B 277    22878  29270  27789   5616   4166  -6664       O  
ATOM   4027  CB  ILE B 277      19.789  71.942  90.340  1.00212.24           C  
ANISOU 4027  CB  ILE B 277    23551  29232  27855   5135   3718  -5845       C  
ATOM   4028  CG1 ILE B 277      20.241  71.229  89.054  1.00212.52           C  
ANISOU 4028  CG1 ILE B 277    23745  29048  27955   4987   3429  -5435       C  
ATOM   4029  CG2 ILE B 277      20.498  71.360  91.577  1.00212.87           C  
ANISOU 4029  CG2 ILE B 277    23696  29713  27471   4907   3990  -5859       C  
ATOM   4030  CD1 ILE B 277      21.513  71.765  88.447  1.00211.00           C  
ANISOU 4030  CD1 ILE B 277    23985  28489  27694   4907   3213  -5343       C  
ATOM   4031  N   LYS B 278      17.108  71.568  92.599  1.00213.80           N  
ANISOU 4031  N   LYS B 278    22807  30311  28114   5404   4519  -6350       N  
ATOM   4032  CA  LYS B 278      16.404  72.025  93.805  1.00220.97           C  
ANISOU 4032  CA  LYS B 278    23484  31517  28955   5572   4882  -6717       C  
ATOM   4033  C   LYS B 278      17.105  71.609  95.124  1.00220.17           C  
ANISOU 4033  C   LYS B 278    23527  31826  28300   5399   5200  -6746       C  
ATOM   4034  O   LYS B 278      16.889  72.227  96.170  1.00217.96           O  
ANISOU 4034  O   LYS B 278    23205  31751  27858   5554   5455  -7101       O  
ATOM   4035  CB  LYS B 278      14.978  71.451  93.815  1.00226.24           C  
ANISOU 4035  CB  LYS B 278    23646  32391  29922   5654   5084  -6703       C  
ATOM   4036  CG  LYS B 278      14.262  71.278  92.460  1.00225.64           C  
ANISOU 4036  CG  LYS B 278    23371  32014  30345   5744   4759  -6546       C  
ATOM   4037  CD  LYS B 278      13.600  72.552  91.967  1.00226.88           C  
ANISOU 4037  CD  LYS B 278    23450  31839  30914   6112   4556  -6869       C  
ATOM   4038  CE  LYS B 278      12.482  72.224  90.951  1.00227.18           C  
ANISOU 4038  CE  LYS B 278    23127  31735  31454   6249   4344  -6784       C  
ATOM   4039  NZ  LYS B 278      11.844  73.414  90.348  1.00230.52           N  
ANISOU 4039  NZ  LYS B 278    23492  31804  32288   6629   4088  -7061       N  
ATOM   4040  N   ASP B 279      17.910  70.571  95.007  1.00220.13           N  
ANISOU 4040  N   ASP B 279    23694  31925  28020   5103   5157  -6377       N  
ATOM   4041  CA  ASP B 279      18.558  69.960  96.186  1.00223.68           C  
ANISOU 4041  CA  ASP B 279    24279  32781  27926   4931   5433  -6328       C  
ATOM   4042  C   ASP B 279      19.975  70.482  96.413  1.00222.35           C  
ANISOU 4042  C   ASP B 279    24544  32490  27448   4859   5246  -6429       C  
ATOM   4043  O   ASP B 279      20.552  70.309  97.496  1.00223.59           O  
ANISOU 4043  O   ASP B 279    24848  32961  27144   4798   5431  -6516       O  
ATOM   4044  CB  ASP B 279      18.584  68.438  96.052  1.00222.25           C  
ANISOU 4044  CB  ASP B 279    24010  32813  27622   4652   5526  -5869       C  
ATOM   4045  CG  ASP B 279      19.365  67.981  94.846  1.00219.33           C  
ANISOU 4045  CG  ASP B 279    23844  32124  27365   4464   5139  -5536       C  
ATOM   4046  OD1 ASP B 279      19.163  68.596  93.766  1.00218.90           O  
ANISOU 4046  OD1 ASP B 279    23791  31681  27697   4589   4837  -5578       O  
ATOM   4047  OD2 ASP B 279      20.185  67.036  94.981  1.00220.52           O  
ANISOU 4047  OD2 ASP B 279    24167  32411  27209   4211   5137  -5240       O  
ATOM   4048  N   ILE B 280      20.540  71.117  95.391  1.00220.31           N  
ANISOU 4048  N   ILE B 280    24488  31773  27445   4873   4879  -6418       N  
ATOM   4049  CA  ILE B 280      21.886  71.704  95.531  1.00216.41           C  
ANISOU 4049  CA  ILE B 280    24373  31102  26748   4801   4696  -6540       C  
ATOM   4050  C   ILE B 280      21.828  73.207  95.260  1.00216.15           C  
ANISOU 4050  C   ILE B 280    24418  30678  27030   5047   4540  -6917       C  
ATOM   4051  O   ILE B 280      21.072  73.675  94.375  1.00217.37           O  
ANISOU 4051  O   ILE B 280    24443  30531  27616   5215   4408  -6916       O  
ATOM   4052  CB  ILE B 280      22.898  71.050  94.572  1.00210.51           C  
ANISOU 4052  CB  ILE B 280    23858  30132  25991   4542   4420  -6147       C  
ATOM   4053  CG1 ILE B 280      22.905  69.505  94.730  1.00208.83           C  
ANISOU 4053  CG1 ILE B 280    23555  30264  25525   4301   4551  -5748       C  
ATOM   4054  CG2 ILE B 280      24.292  71.649  94.794  1.00207.21           C  
ANISOU 4054  CG2 ILE B 280    23789  29546  25394   4458   4262  -6299       C  
ATOM   4055  CD1 ILE B 280      23.349  68.975  96.081  1.00210.10           C  
ANISOU 4055  CD1 ILE B 280    23782  30877  25167   4206   4807  -5792       C  
ATOM   4056  N   ASP B 281      22.618  73.962  96.033  1.00215.51           N  
ANISOU 4056  N   ASP B 281    24545  30594  26742   5082   4544  -7250       N  
ATOM   4057  CA  ASP B 281      22.761  75.393  95.796  1.00219.96           C  
ANISOU 4057  CA  ASP B 281    25223  30739  27613   5281   4382  -7606       C  
ATOM   4058  C   ASP B 281      23.809  75.595  94.713  1.00211.42           C  
ANISOU 4058  C   ASP B 281    24427  29186  26713   5125   4063  -7386       C  
ATOM   4059  O   ASP B 281      25.012  75.725  94.975  1.00211.36           O  
ANISOU 4059  O   ASP B 281    24666  29113  26528   4970   3972  -7445       O  
ATOM   4060  CB  ASP B 281      23.118  76.159  97.061  1.00230.68           C  
ANISOU 4060  CB  ASP B 281    26659  32265  28722   5397   4511  -8098       C  
ATOM   4061  CG  ASP B 281      22.997  77.690  96.871  1.00240.07           C  
ANISOU 4061  CG  ASP B 281    27896  33014  30303   5647   4382  -8513       C  
ATOM   4062  OD1 ASP B 281      22.727  78.164  95.733  1.00242.78           O  
ANISOU 4062  OD1 ASP B 281    28250  32902  31091   5724   4185  -8384       O  
ATOM   4063  OD2 ASP B 281      23.166  78.422  97.874  1.00247.14           O  
ANISOU 4063  OD2 ASP B 281    28828  34018  31055   5783   4474  -8976       O  
ATOM   4064  N   VAL B 282      23.338  75.615  93.478  1.00206.13           N  
ANISOU 4064  N   VAL B 282    23720  28190  26407   5178   3893  -7136       N  
ATOM   4065  CA  VAL B 282      24.197  75.878  92.323  1.00203.64           C  
ANISOU 4065  CA  VAL B 282    23680  27394  26296   5072   3615  -6906       C  
ATOM   4066  C   VAL B 282      23.606  77.022  91.501  1.00207.31           C  
ANISOU 4066  C   VAL B 282    24159  27378  27231   5345   3464  -7025       C  
ATOM   4067  O   VAL B 282      22.395  77.077  91.251  1.00210.95           O  
ANISOU 4067  O   VAL B 282    24377  27868  27904   5562   3486  -7047       O  
ATOM   4068  CB  VAL B 282      24.393  74.639  91.437  1.00199.23           C  
ANISOU 4068  CB  VAL B 282    23148  26884  25667   4852   3512  -6396       C  
ATOM   4069  CG1 VAL B 282      23.048  74.051  90.988  1.00202.32           C  
ANISOU 4069  CG1 VAL B 282    23235  27413  26224   4975   3545  -6230       C  
ATOM   4070  CG2 VAL B 282      25.287  74.978  90.244  1.00195.70           C  
ANISOU 4070  CG2 VAL B 282    23002  25939  25413   4765   3255  -6172       C  
ATOM   4071  N   SER B 283      24.457  77.946  91.089  1.00208.93           N  
ANISOU 4071  N   SER B 283    24640  27126  27617   5341   3311  -7105       N  
ATOM   4072  CA  SER B 283      24.022  79.025  90.211  1.00213.33           C  
ANISOU 4072  CA  SER B 283    25271  27166  28616   5592   3154  -7156       C  
ATOM   4073  C   SER B 283      25.021  79.268  89.097  1.00211.13           C  
ANISOU 4073  C   SER B 283    25331  26400  28487   5462   2956  -6865       C  
ATOM   4074  O   SER B 283      26.152  78.786  89.162  1.00204.88           O  
ANISOU 4074  O   SER B 283    24706  25652  27484   5179   2953  -6723       O  
ATOM   4075  CB  SER B 283      23.759  80.306  91.006  1.00219.79           C  
ANISOU 4075  CB  SER B 283    26043  27853  29610   5828   3231  -7680       C  
ATOM   4076  OG  SER B 283      24.970  80.877  91.457  1.00221.45           O  
ANISOU 4076  OG  SER B 283    26481  27888  29770   5684   3219  -7885       O  
ATOM   4077  N   VAL B 284      24.607  80.028  88.089  1.00217.77           N  
ANISOU 4077  N   VAL B 284    26277  26774  29691   5683   2799  -6779       N  
ATOM   4078  CA  VAL B 284      25.481  80.395  86.968  1.00221.21           C  
ANISOU 4078  CA  VAL B 284    27061  26695  30293   5603   2642  -6492       C  
ATOM   4079  C   VAL B 284      26.150  81.749  87.238  1.00229.30           C  
ANISOU 4079  C   VAL B 284    28274  27273  31576   5651   2657  -6802       C  
ATOM   4080  O   VAL B 284      25.476  82.735  87.523  1.00238.30           O  
ANISOU 4080  O   VAL B 284    29333  28233  32975   5925   2663  -7121       O  
ATOM   4081  CB  VAL B 284      24.715  80.436  85.629  1.00221.75           C  
ANISOU 4081  CB  VAL B 284    27190  26479  30584   5828   2451  -6177       C  
ATOM   4082  CG1 VAL B 284      25.613  80.945  84.507  1.00220.91           C  
ANISOU 4082  CG1 VAL B 284    27480  25818  30637   5779   2329  -5889       C  
ATOM   4083  CG2 VAL B 284      24.168  79.058  85.296  1.00219.24           C  
ANISOU 4083  CG2 VAL B 284    26687  26567  30044   5749   2411  -5877       C  
ATOM   4084  N   GLU B 285      27.479  81.789  87.138  1.00232.33           N  
ANISOU 4084  N   GLU B 285    28892  27461  31920   5384   2661  -6716       N  
ATOM   4085  CA  GLU B 285      28.231  83.023  87.279  1.00240.96           C  
ANISOU 4085  CA  GLU B 285    30168  28074  33312   5386   2669  -6975       C  
ATOM   4086  C   GLU B 285      28.062  83.891  86.026  1.00239.04           C  
ANISOU 4086  C   GLU B 285    30167  27195  33461   5580   2557  -6745       C  
ATOM   4087  O   GLU B 285      27.949  83.381  84.911  1.00235.02           O  
ANISOU 4087  O   GLU B 285    29793  26587  32916   5587   2463  -6297       O  
ATOM   4088  CB  GLU B 285      29.707  82.740  87.551  1.00250.31           C  
ANISOU 4088  CB  GLU B 285    31490  29252  34363   5029   2709  -6958       C  
ATOM   4089  CG  GLU B 285      30.505  83.955  88.015  1.00265.80           C  
ANISOU 4089  CG  GLU B 285    33557  30803  36632   5001   2736  -7344       C  
ATOM   4090  CD  GLU B 285      31.863  84.105  87.331  1.00276.99           C  
ANISOU 4090  CD  GLU B 285    35232  31795  38215   4732   2726  -7119       C  
ATOM   4091  OE1 GLU B 285      31.999  83.760  86.134  1.00281.84           O  
ANISOU 4091  OE1 GLU B 285    36032  32191  38863   4686   2689  -6638       O  
ATOM   4092  OE2 GLU B 285      32.803  84.605  87.996  1.00289.31           O  
ANISOU 4092  OE2 GLU B 285    36804  33229  39891   4576   2757  -7448       O  
ATOM   4093  N   LYS B 286      28.033  85.195  86.223  1.00241.72           N  
ANISOU 4093  N   LYS B 286    30571  27106  34164   5753   2564  -7058       N  
ATOM   4094  CA  LYS B 286      27.967  86.146  85.111  1.00243.68           C  
ANISOU 4094  CA  LYS B 286    31087  26692  34806   5943   2478  -6852       C  
ATOM   4095  C   LYS B 286      29.176  85.974  84.200  1.00239.61           C  
ANISOU 4095  C   LYS B 286    30889  25839  34311   5678   2488  -6446       C  
ATOM   4096  O   LYS B 286      30.285  85.747  84.669  1.00239.61           O  
ANISOU 4096  O   LYS B 286    30911  25907  34223   5364   2576  -6529       O  
ATOM   4097  CB  LYS B 286      27.875  87.593  85.616  1.00250.62           C  
ANISOU 4097  CB  LYS B 286    31976  27147  36098   6136   2505  -7297       C  
ATOM   4098  CG  LYS B 286      27.374  88.573  84.560  1.00254.74           C  
ANISOU 4098  CG  LYS B 286    32721  27045  37022   6445   2403  -7109       C  
ATOM   4099  CD  LYS B 286      27.863  89.993  84.790  1.00260.60           C  
ANISOU 4099  CD  LYS B 286    33601  27182  38231   6501   2452  -7416       C  
ATOM   4100  CE  LYS B 286      29.332  90.155  84.421  1.00261.00           C  
ANISOU 4100  CE  LYS B 286    33916  26849  38403   6162   2541  -7232       C  
ATOM   4101  NZ  LYS B 286      29.782  91.581  84.276  1.00266.71           N  
ANISOU 4101  NZ  LYS B 286    34833  26830  39675   6231   2585  -7398       N  
ATOM   4102  N   GLU B 287      28.942  86.073  82.894  1.00241.01           N  
ANISOU 4102  N   GLU B 287    31311  25665  34596   5823   2397  -6012       N  
ATOM   4103  CA  GLU B 287      29.977  85.835  81.888  1.00243.92           C  
ANISOU 4103  CA  GLU B 287    31997  25732  34948   5607   2427  -5568       C  
ATOM   4104  C   GLU B 287      31.216  86.713  82.108  1.00248.98           C  
ANISOU 4104  C   GLU B 287    32800  25903  35899   5391   2568  -5721       C  
ATOM   4105  O   GLU B 287      31.092  87.942  82.267  1.00253.72           O  
ANISOU 4105  O   GLU B 287    33459  26046  36896   5558   2590  -5968       O  
ATOM   4106  CB  GLU B 287      29.419  86.059  80.470  1.00243.61           C  
ANISOU 4106  CB  GLU B 287    32232  25321  35004   5884   2305  -5125       C  
ATOM   4107  CG  GLU B 287      30.351  85.657  79.303  1.00239.12           C  
ANISOU 4107  CG  GLU B 287    32008  24507  34338   5700   2344  -4606       C  
ATOM   4108  CD  GLU B 287      29.636  85.531  77.977  1.00236.97           C  
ANISOU 4108  CD  GLU B 287    31970  24069  33999   6000   2183  -4169       C  
ATOM   4109  OE1 GLU B 287      28.652  86.285  77.773  1.00240.63           O  
ANISOU 4109  OE1 GLU B 287    32449  24308  34672   6375   2060  -4248       O  
ATOM   4110  OE2 GLU B 287      30.044  84.674  77.144  1.00231.62           O  
ANISOU 4110  OE2 GLU B 287    31458  23491  33055   5878   2163  -3765       O  
ATOM   4111  N   LYS B 288      32.378  86.056  82.113  1.00244.47           N  
ANISOU 4111  N   LYS B 288    32278  25442  35166   5026   2655  -5584       N  
ATOM   4112  CA  LYS B 288      33.661  86.722  82.262  1.00241.09           C  
ANISOU 4112  CA  LYS B 288    31971  24595  35036   4772   2791  -5704       C  
ATOM   4113  C   LYS B 288      34.246  86.969  80.864  1.00241.24           C  
ANISOU 4113  C   LYS B 288    32364  24068  35226   4733   2866  -5190       C  
ATOM   4114  O   LYS B 288      34.252  86.072  80.034  1.00239.02           O  
ANISOU 4114  O   LYS B 288    32202  23960  34652   4696   2836  -4755       O  
ATOM   4115  CB  LYS B 288      34.710  85.881  83.018  1.00235.02           C  
ANISOU 4115  CB  LYS B 288    31046  24224  34027   4390   2846  -5844       C  
ATOM   4116  CG  LYS B 288      34.268  84.972  84.157  1.00231.22           C  
ANISOU 4116  CG  LYS B 288    30244  24473  33134   4359   2783  -6124       C  
ATOM   4117  CD  LYS B 288      35.331  83.869  84.342  1.00226.89           C  
ANISOU 4117  CD  LYS B 288    29654  24264  32287   3997   2813  -5997       C  
ATOM   4118  CE  LYS B 288      35.219  83.132  85.650  1.00225.48           C  
ANISOU 4118  CE  LYS B 288    29191  24733  31746   3919   2780  -6331       C  
ATOM   4119  NZ  LYS B 288      36.388  82.188  85.784  1.00223.11           N  
ANISOU 4119  NZ  LYS B 288    28881  24670  31220   3573   2795  -6213       N  
ATOM   4120  N   PRO B 289      34.771  88.165  80.630  1.00244.44           N  
ANISOU 4120  N   PRO B 289    32954  23817  36102   4735   2978  -5246       N  
ATOM   4121  CA  PRO B 289      35.346  88.451  79.319  1.00246.20           C  
ANISOU 4121  CA  PRO B 289    33556  23498  36491   4702   3097  -4740       C  
ATOM   4122  C   PRO B 289      36.602  87.628  79.094  1.00243.43           C  
ANISOU 4122  C   PRO B 289    33240  23271  35981   4306   3226  -4527       C  
ATOM   4123  O   PRO B 289      37.453  87.604  79.983  1.00243.78           O  
ANISOU 4123  O   PRO B 289    33085  23416  36124   4020   3289  -4875       O  
ATOM   4124  CB  PRO B 289      35.684  89.931  79.423  1.00250.29           C  
ANISOU 4124  CB  PRO B 289    34188  23313  37597   4747   3215  -4954       C  
ATOM   4125  CG  PRO B 289      35.983  90.150  80.871  1.00249.84           C  
ANISOU 4125  CG  PRO B 289    33790  23476  37659   4590   3200  -5591       C  
ATOM   4126  CD  PRO B 289      35.170  89.153  81.644  1.00246.36           C  
ANISOU 4126  CD  PRO B 289    33054  23820  36730   4667   3035  -5787       C  
ATOM   4127  N   GLY B 290      36.692  86.939  77.957  1.00241.11           N  
ANISOU 4127  N   GLY B 290    33182  22996  35432   4307   3245  -3993       N  
ATOM   4128  CA  GLY B 290      37.831  86.111  77.652  1.00238.48           C  
ANISOU 4128  CA  GLY B 290    32888  22784  34937   3957   3369  -3767       C  
ATOM   4129  C   GLY B 290      37.737  84.676  78.152  1.00235.24           C  
ANISOU 4129  C   GLY B 290    32224  23121  34036   3819   3239  -3809       C  
ATOM   4130  O   GLY B 290      38.730  83.936  78.115  1.00226.99           O  
ANISOU 4130  O   GLY B 290    31149  22235  32861   3509   3323  -3706       O  
ATOM   4131  N   SER B 291      36.546  84.262  78.578  1.00239.98           N  
ANISOU 4131  N   SER B 291    32639  24162  34378   4049   3045  -3942       N  
ATOM   4132  CA  SER B 291      36.335  82.909  79.053  1.00237.84           C  
ANISOU 4132  CA  SER B 291    32128  24579  33659   3940   2932  -3963       C  
ATOM   4133  C   SER B 291      35.594  82.062  78.003  1.00237.49           C  
ANISOU 4133  C   SER B 291    32213  24726  33293   4121   2808  -3520       C  
ATOM   4134  O   SER B 291      34.622  82.521  77.415  1.00241.09           O  
ANISOU 4134  O   SER B 291    32793  25000  33810   4456   2707  -3398       O  
ATOM   4135  CB  SER B 291      35.510  82.899  80.330  1.00237.57           C  
ANISOU 4135  CB  SER B 291    31759  24963  33542   4048   2826  -4426       C  
ATOM   4136  OG  SER B 291      35.195  81.557  80.702  1.00229.11           O  
ANISOU 4136  OG  SER B 291    30477  24538  32036   3967   2736  -4383       O  
ATOM   4137  N   PRO B 292      36.041  80.829  77.784  1.00233.89           N  
ANISOU 4137  N   PRO B 292    31721  24635  32508   3915   2794  -3304       N  
ATOM   4138  CA  PRO B 292      35.354  79.915  76.856  1.00234.15           C  
ANISOU 4138  CA  PRO B 292    31842  24896  32227   4073   2650  -2933       C  
ATOM   4139  C   PRO B 292      34.371  79.022  77.610  1.00232.37           C  
ANISOU 4139  C   PRO B 292    31274  25277  31736   4139   2487  -3118       C  
ATOM   4140  O   PRO B 292      33.909  77.985  77.092  1.00231.20           O  
ANISOU 4140  O   PRO B 292    31099  25437  31308   4184   2360  -2879       O  
ATOM   4141  CB  PRO B 292      36.494  79.088  76.279  1.00231.93           C  
ANISOU 4141  CB  PRO B 292    31692  24652  31776   3784   2750  -2636       C  
ATOM   4142  CG  PRO B 292      37.603  79.201  77.263  1.00230.29           C  
ANISOU 4142  CG  PRO B 292    31321  24472  31705   3448   2893  -2934       C  
ATOM   4143  CD  PRO B 292      37.462  80.506  77.965  1.00231.40           C  
ANISOU 4143  CD  PRO B 292    31408  24297  32213   3537   2946  -3300       C  
ATOM   4144  N   ALA B 293      34.061  79.412  78.843  1.00231.09           N  
ANISOU 4144  N   ALA B 293    30848  25285  31667   4141   2502  -3550       N  
ATOM   4145  CA  ALA B 293      33.334  78.564  79.780  1.00225.55           C  
ANISOU 4145  CA  ALA B 293    29802  25179  30716   4138   2423  -3758       C  
ATOM   4146  C   ALA B 293      32.047  79.189  80.328  1.00222.99           C  
ANISOU 4146  C   ALA B 293    29290  24917  30516   4446   2355  -4051       C  
ATOM   4147  O   ALA B 293      31.823  80.401  80.219  1.00229.30           O  
ANISOU 4147  O   ALA B 293    30202  25294  31626   4644   2370  -4184       O  
ATOM   4148  CB  ALA B 293      34.234  78.207  80.951  1.00224.54           C  
ANISOU 4148  CB  ALA B 293    29493  25334  30485   3825   2524  -4031       C  
ATOM   4149  N   VAL B 294      31.212  78.337  80.918  1.00213.54           N  
ANISOU 4149  N   VAL B 294    27799  24241  29093   4483   2295  -4146       N  
ATOM   4150  CA  VAL B 294      30.073  78.760  81.709  1.00210.20           C  
ANISOU 4150  CA  VAL B 294    27119  23993  28753   4720   2279  -4485       C  
ATOM   4151  C   VAL B 294      30.405  78.337  83.144  1.00211.75           C  
ANISOU 4151  C   VAL B 294    27064  24635  28754   4507   2402  -4811       C  
ATOM   4152  O   VAL B 294      30.547  77.150  83.441  1.00208.68           O  
ANISOU 4152  O   VAL B 294    26543  24680  28064   4318   2415  -4698       O  
ATOM   4153  CB  VAL B 294      28.772  78.166  81.163  1.00204.20           C  
ANISOU 4153  CB  VAL B 294    26218  23443  27923   4960   2128  -4323       C  
ATOM   4154  CG1 VAL B 294      27.589  78.811  81.841  1.00205.74           C  
ANISOU 4154  CG1 VAL B 294    26164  23719  28287   5243   2124  -4674       C  
ATOM   4155  CG2 VAL B 294      28.685  78.393  79.654  1.00202.99           C  
ANISOU 4155  CG2 VAL B 294    26374  22881  27872   5139   1979  -3946       C  
ATOM   4156  N   THR B 295      30.607  79.316  84.010  1.00218.14           N  
ANISOU 4156  N   THR B 295    27835  25315  29733   4539   2487  -5210       N  
ATOM   4157  CA  THR B 295      31.133  79.051  85.345  1.00220.04           C  
ANISOU 4157  CA  THR B 295    27905  25920  29776   4346   2591  -5537       C  
ATOM   4158  C   THR B 295      30.005  78.919  86.374  1.00222.94           C  
ANISOU 4158  C   THR B 295    27967  26727  30011   4522   2643  -5840       C  
ATOM   4159  O   THR B 295      29.121  79.767  86.456  1.00231.37           O  
ANISOU 4159  O   THR B 295    28963  27642  31305   4802   2636  -6055       O  
ATOM   4160  CB  THR B 295      32.162  80.116  85.727  1.00222.90           C  
ANISOU 4160  CB  THR B 295    28402  25904  30383   4248   2646  -5822       C  
ATOM   4161  OG1 THR B 295      33.182  80.141  84.712  1.00221.77           O  
ANISOU 4161  OG1 THR B 295    28525  25366  30369   4071   2636  -5496       O  
ATOM   4162  CG2 THR B 295      32.784  79.806  87.084  1.00223.26           C  
ANISOU 4162  CG2 THR B 295    28292  26340  30195   4061   2711  -6172       C  
ATOM   4163  N   LEU B 296      30.035  77.831  87.122  1.00218.31           N  
ANISOU 4163  N   LEU B 296    27205  26676  29064   4363   2706  -5837       N  
ATOM   4164  CA  LEU B 296      29.026  77.537  88.114  1.00216.93           C  
ANISOU 4164  CA  LEU B 296    26742  26965  28716   4495   2806  -6073       C  
ATOM   4165  C   LEU B 296      29.586  77.805  89.498  1.00209.90           C  
ANISOU 4165  C   LEU B 296    25793  26309  27647   4414   2917  -6490       C  
ATOM   4166  O   LEU B 296      30.720  77.428  89.800  1.00202.20           O  
ANISOU 4166  O   LEU B 296    24921  25409  26497   4165   2910  -6471       O  
ATOM   4167  CB  LEU B 296      28.648  76.072  88.024  1.00218.43           C  
ANISOU 4167  CB  LEU B 296    26784  27598  28610   4375   2822  -5756       C  
ATOM   4168  CG  LEU B 296      28.283  75.622  86.605  1.00220.00           C  
ANISOU 4168  CG  LEU B 296    27060  27592  28936   4417   2673  -5329       C  
ATOM   4169  CD1 LEU B 296      28.066  74.114  86.559  1.00216.83           C  
ANISOU 4169  CD1 LEU B 296    26511  27614  28260   4256   2683  -5037       C  
ATOM   4170  CD2 LEU B 296      27.054  76.371  86.063  1.00224.34           C  
ANISOU 4170  CD2 LEU B 296    27531  27914  29794   4762   2599  -5396       C  
ATOM   4171  N   LEU B 297      28.795  78.468  90.331  1.00210.24           N  
ANISOU 4171  N   LEU B 297    25673  26471  27737   4642   3008  -6883       N  
ATOM   4172  CA  LEU B 297      29.118  78.581  91.750  1.00212.57           C  
ANISOU 4172  CA  LEU B 297    25887  27102  27777   4612   3122  -7297       C  
ATOM   4173  C   LEU B 297      28.250  77.630  92.540  1.00213.05           C  
ANISOU 4173  C   LEU B 297    25702  27767  27478   4654   3284  -7285       C  
ATOM   4174  O   LEU B 297      27.024  77.704  92.492  1.00215.86           O  
ANISOU 4174  O   LEU B 297    25863  28216  27937   4870   3360  -7314       O  
ATOM   4175  CB  LEU B 297      28.952  80.012  92.295  1.00217.09           C  
ANISOU 4175  CB  LEU B 297    26456  27410  28615   4835   3137  -7809       C  
ATOM   4176  CG  LEU B 297      29.472  80.208  93.728  1.00219.05           C  
ANISOU 4176  CG  LEU B 297    26666  27968  28594   4807   3214  -8278       C  
ATOM   4177  CD1 LEU B 297      30.932  79.847  93.940  1.00215.38           C  
ANISOU 4177  CD1 LEU B 297    26360  27514  27961   4513   3129  -8252       C  
ATOM   4178  CD2 LEU B 297      29.414  81.734  94.012  1.00225.45           C  
ANISOU 4178  CD2 LEU B 297    27507  28380  29774   5019   3185  -8772       C  
ATOM   4179  N   ILE B 298      28.902  76.724  93.256  1.00211.22           N  
ANISOU 4179  N   ILE B 298    25478  27934  26839   4446   3341  -7232       N  
ATOM   4180  CA  ILE B 298      28.225  75.746  94.097  1.00209.93           C  
ANISOU 4180  CA  ILE B 298    25115  28354  26292   4453   3530  -7188       C  
ATOM   4181  C   ILE B 298      28.463  76.066  95.564  1.00212.08           C  
ANISOU 4181  C   ILE B 298    25370  28958  26251   4520   3656  -7638       C  
ATOM   4182  O   ILE B 298      29.596  76.052  96.046  1.00214.73           O  
ANISOU 4182  O   ILE B 298    25862  29331  26395   4374   3576  -7762       O  
ATOM   4183  CB  ILE B 298      28.676  74.304  93.830  1.00205.12           C  
ANISOU 4183  CB  ILE B 298    24532  27998  25406   4187   3516  -6735       C  
ATOM   4184  CG1 ILE B 298      28.432  73.938  92.369  1.00202.61           C  
ANISOU 4184  CG1 ILE B 298    24236  27376  25367   4136   3379  -6307       C  
ATOM   4185  CG2 ILE B 298      27.947  73.341  94.780  1.00206.02           C  
ANISOU 4185  CG2 ILE B 298    24441  28695  25139   4201   3750  -6692       C  
ATOM   4186  CD1 ILE B 298      28.836  72.521  92.014  1.00198.70           C  
ANISOU 4186  CD1 ILE B 298    23758  27093  24643   3885   3351  -5869       C  
ATOM   4187  N   ARG B 299      27.380  76.330  96.270  1.00213.96           N  
ANISOU 4187  N   ARG B 299    25411  29452  26431   4753   3850  -7891       N  
ATOM   4188  CA  ARG B 299      27.397  76.427  97.726  1.00217.78           C  
ANISOU 4188  CA  ARG B 299    25861  30363  26522   4848   4019  -8280       C  
ATOM   4189  C   ARG B 299      27.269  75.054  98.340  1.00217.97           C  
ANISOU 4189  C   ARG B 299    25816  30943  26059   4721   4202  -8002       C  
ATOM   4190  O   ARG B 299      26.220  74.668  98.811  1.00219.59           O  
ANISOU 4190  O   ARG B 299    25815  31489  26128   4842   4453  -7986       O  
ATOM   4191  CB  ARG B 299      26.347  77.422  98.237  1.00222.77           C  
ANISOU 4191  CB  ARG B 299    26326  31000  27316   5173   4166  -8715       C  
ATOM   4192  CG  ARG B 299      26.930  78.651  98.931  1.00227.18           C  
ANISOU 4192  CG  ARG B 299    27006  31387  27925   5305   4085  -9284       C  
ATOM   4193  CD  ARG B 299      28.115  79.288  98.217  1.00228.12           C  
ANISOU 4193  CD  ARG B 299    27349  30963  28361   5155   3802  -9298       C  
ATOM   4194  NE  ARG B 299      28.100  80.740  98.330  1.00234.81           N  
ANISOU 4194  NE  ARG B 299    28225  31415  29577   5357   3726  -9783       N  
ATOM   4195  CZ  ARG B 299      27.460  81.566  97.508  1.00237.21           C  
ANISOU 4195  CZ  ARG B 299    28486  31266  30378   5519   3677  -9789       C  
ATOM   4196  NH1 ARG B 299      26.777  81.121  96.442  1.00235.24           N  
ANISOU 4196  NH1 ARG B 299    28166  30886  30325   5516   3669  -9340       N  
ATOM   4197  NH2 ARG B 299      27.534  82.868  97.690  1.00242.24           N  
ANISOU 4197  NH2 ARG B 299    29161  31535  31343   5694   3609 -10242       N  
ATOM   4198  N   ASN B 300      28.368  74.294  98.307  1.00218.28           N  
ANISOU 4198  N   ASN B 300    26025  31054  25856   4470   4080  -7767       N  
ATOM   4199  CA  ASN B 300      28.421  72.983  98.934  1.00220.89           C  
ANISOU 4199  CA  ASN B 300    26336  31885  25706   4340   4230  -7494       C  
ATOM   4200  C   ASN B 300      28.810  73.278 100.376  1.00227.38           C  
ANISOU 4200  C   ASN B 300    27247  33065  26082   4455   4318  -7915       C  
ATOM   4201  O   ASN B 300      29.827  72.803 100.861  1.00224.87           O  
ANISOU 4201  O   ASN B 300    27097  32919  25425   4322   4218  -7892       O  
ATOM   4202  CB  ASN B 300      29.440  72.044  98.248  1.00215.37           C  
ANISOU 4202  CB  ASN B 300    25782  31091  24956   4041   4040  -7068       C  
ATOM   4203  CG  ASN B 300      29.587  70.676  98.960  1.00211.81           C  
ANISOU 4203  CG  ASN B 300    25336  31142  23998   3911   4181  -6786       C  
ATOM   4204  OD1 ASN B 300      30.689  70.182  99.138  1.00201.58           O  
ANISOU 4204  OD1 ASN B 300    24211  29910  22470   3743   4038  -6693       O  
ATOM   4205  ND2 ASN B 300      28.465  70.069  99.367  1.00218.19           N  
ANISOU 4205  ND2 ASN B 300    25951  32294  24657   3991   4470  -6647       N  
ATOM   4206  N   PRO B 301      27.939  73.967 101.106  1.00237.41           N  
ANISOU 4206  N   PRO B 301    28394  34496  27315   4720   4518  -8290       N  
ATOM   4207  CA  PRO B 301      28.312  75.008 102.021  1.00245.55           C  
ANISOU 4207  CA  PRO B 301    29520  35551  28226   4904   4478  -8871       C  
ATOM   4208  C   PRO B 301      29.522  75.877 101.561  1.00244.21           C  
ANISOU 4208  C   PRO B 301    29534  34892  28361   4813   4132  -9099       C  
ATOM   4209  O   PRO B 301      29.315  77.024 101.184  1.00250.22           O  
ANISOU 4209  O   PRO B 301    30265  35249  29555   4944   4052  -9389       O  
ATOM   4210  CB  PRO B 301      28.539  74.217 103.320  1.00248.80           C  
ANISOU 4210  CB  PRO B 301    30013  36568  27951   4921   4647  -8900       C  
ATOM   4211  CG  PRO B 301      27.583  73.031 103.183  1.00245.96           C  
ANISOU 4211  CG  PRO B 301    29481  36513  27459   4856   4936  -8409       C  
ATOM   4212  CD  PRO B 301      26.996  73.074 101.787  1.00240.55           C  
ANISOU 4212  CD  PRO B 301    28632  35404  27362   4778   4862  -8113       C  
ATOM   4213  N   GLU B 302      30.742  75.360 101.591  1.00237.02           N  
ANISOU 4213  N   GLU B 302    28795  33999  27260   4597   3942  -8976       N  
ATOM   4214  CA  GLU B 302      31.836  76.122 101.028  1.00233.69           C  
ANISOU 4214  CA  GLU B 302    28505  33079  27206   4482   3648  -9142       C  
ATOM   4215  C   GLU B 302      31.659  76.323  99.536  1.00227.25           C  
ANISOU 4215  C   GLU B 302    27662  31735  26946   4375   3564  -8805       C  
ATOM   4216  O   GLU B 302      30.941  75.563  98.870  1.00224.25           O  
ANISOU 4216  O   GLU B 302    27186  31416  26602   4325   3668  -8361       O  
ATOM   4217  CB  GLU B 302      33.245  75.622 101.432  1.00234.70           C  
ANISOU 4217  CB  GLU B 302    28801  33326  27048   4289   3445  -9154       C  
ATOM   4218  CG  GLU B 302      33.904  74.529 100.584  1.00232.30           C  
ANISOU 4218  CG  GLU B 302    28556  32955  26752   3993   3342  -8600       C  
ATOM   4219  CD  GLU B 302      33.380  73.133 100.883  1.00234.83           C  
ANISOU 4219  CD  GLU B 302    28831  33772  26621   3946   3530  -8172       C  
ATOM   4220  OE1 GLU B 302      33.704  72.198 100.117  1.00235.86           O  
ANISOU 4220  OE1 GLU B 302    28982  33843  26789   3725   3473  -7695       O  
ATOM   4221  OE2 GLU B 302      32.654  72.949 101.889  1.00238.68           O  
ANISOU 4221  OE2 GLU B 302    29266  34706  26717   4128   3750  -8307       O  
ATOM   4222  N   GLU B 303      32.263  77.385  99.017  1.00226.38           N  
ANISOU 4222  N   GLU B 303    27634  31096  27280   4360   3381  -9031       N  
ATOM   4223  CA  GLU B 303      32.101  77.789  97.619  1.00223.90           C  
ANISOU 4223  CA  GLU B 303    27336  30233  27501   4309   3305  -8758       C  
ATOM   4224  C   GLU B 303      33.046  77.022  96.704  1.00225.10           C  
ANISOU 4224  C   GLU B 303    27608  30212  27707   4010   3168  -8304       C  
ATOM   4225  O   GLU B 303      34.255  76.979  96.941  1.00223.98           O  
ANISOU 4225  O   GLU B 303    27576  30022  27504   3841   3029  -8409       O  
ATOM   4226  CB  GLU B 303      32.456  79.248  97.428  1.00221.87           C  
ANISOU 4226  CB  GLU B 303    27146  29439  27716   4400   3187  -9160       C  
ATOM   4227  CG  GLU B 303      31.501  80.284  97.937  1.00224.38           C  
ANISOU 4227  CG  GLU B 303    27356  29713  28184   4712   3285  -9598       C  
ATOM   4228  CD  GLU B 303      31.970  81.699  97.581  1.00227.77           C  
ANISOU 4228  CD  GLU B 303    27870  29514  29155   4767   3146  -9936       C  
ATOM   4229  OE1 GLU B 303      32.939  81.923  96.809  1.00226.25           O  
ANISOU 4229  OE1 GLU B 303    27815  28875  29273   4564   3001  -9788       O  
ATOM   4230  OE2 GLU B 303      31.329  82.651  98.065  1.00233.02           O  
ANISOU 4230  OE2 GLU B 303    28459  30102  29973   5025   3200 -10366       O  
ATOM   4231  N   ILE B 304      32.483  76.452  95.649  1.00226.01           N  
ANISOU 4231  N   ILE B 304    27691  30224  27958   3961   3197  -7830       N  
ATOM   4232  CA  ILE B 304      33.257  75.735  94.643  1.00218.66           C  
ANISOU 4232  CA  ILE B 304    26872  29106  27100   3704   3081  -7380       C  
ATOM   4233  C   ILE B 304      32.920  76.295  93.262  1.00215.08           C  
ANISOU 4233  C   ILE B 304    26477  28121  27122   3748   3025  -7150       C  
ATOM   4234  O   ILE B 304      31.747  76.450  92.936  1.00212.55           O  
ANISOU 4234  O   ILE B 304    26047  27787  26922   3941   3096  -7083       O  
ATOM   4235  CB  ILE B 304      32.895  74.251  94.685  1.00215.41           C  
ANISOU 4235  CB  ILE B 304    26380  29147  26315   3601   3164  -6971       C  
ATOM   4236  CG1 ILE B 304      33.184  73.671  96.074  1.00215.88           C  
ANISOU 4236  CG1 ILE B 304    26414  29744  25864   3585   3236  -7161       C  
ATOM   4237  CG2 ILE B 304      33.634  73.495  93.602  1.00211.50           C  
ANISOU 4237  CG2 ILE B 304    25995  28459  25906   3356   3043  -6518       C  
ATOM   4238  CD1 ILE B 304      32.617  72.290  96.329  1.00213.58           C  
ANISOU 4238  CD1 ILE B 304    26023  29927  25198   3530   3378  -6800       C  
ATOM   4239  N   SER B 305      33.935  76.600  92.456  1.00215.74           N  
ANISOU 4239  N   SER B 305    26729  27769  27473   3582   2903  -7030       N  
ATOM   4240  CA  SER B 305      33.699  77.110  91.115  1.00220.08           C  
ANISOU 4240  CA  SER B 305    27383  27808  28429   3630   2857  -6774       C  
ATOM   4241  C   SER B 305      33.995  76.040  90.059  1.00216.26           C  
ANISOU 4241  C   SER B 305    26979  27315  27873   3444   2807  -6234       C  
ATOM   4242  O   SER B 305      35.020  75.362  90.141  1.00216.75           O  
ANISOU 4242  O   SER B 305    27099  27486  27768   3205   2765  -6119       O  
ATOM   4243  CB  SER B 305      34.545  78.358  90.869  1.00227.68           C  
ANISOU 4243  CB  SER B 305    28494  28215  29799   3604   2798  -7016       C  
ATOM   4244  OG  SER B 305      35.928  78.031  90.743  1.00233.05           O  
ANISOU 4244  OG  SER B 305    29279  28799  30469   3322   2733  -6937       O  
ATOM   4245  N   VAL B 306      33.093  75.881  89.097  1.00213.40           N  
ANISOU 4245  N   VAL B 306    26611  26835  27633   3570   2796  -5930       N  
ATOM   4246  CA  VAL B 306      33.249  74.869  88.061  1.00206.18           C  
ANISOU 4246  CA  VAL B 306    25770  25922  26647   3432   2736  -5441       C  
ATOM   4247  C   VAL B 306      33.131  75.481  86.669  1.00204.00           C  
ANISOU 4247  C   VAL B 306    25678  25119  26712   3530   2663  -5201       C  
ATOM   4248  O   VAL B 306      32.055  75.936  86.269  1.00205.65           O  
ANISOU 4248  O   VAL B 306    25844  25206  27085   3782   2642  -5196       O  
ATOM   4249  CB  VAL B 306      32.210  73.755  88.231  1.00203.72           C  
ANISOU 4249  CB  VAL B 306    25256  26073  26076   3483   2775  -5254       C  
ATOM   4250  CG1 VAL B 306      32.429  72.650  87.217  1.00195.13           C  
ANISOU 4250  CG1 VAL B 306    24233  24998  24909   3331   2694  -4786       C  
ATOM   4251  CG2 VAL B 306      32.255  73.211  89.651  1.00205.97           C  
ANISOU 4251  CG2 VAL B 306    25384  26873  26001   3418   2883  -5476       C  
ATOM   4252  N   ASP B 307      34.223  75.492  85.919  1.00200.45           N  
ANISOU 4252  N   ASP B 307    25437  24357  26367   3347   2628  -4998       N  
ATOM   4253  CA  ASP B 307      34.193  75.987  84.548  1.00200.74           C  
ANISOU 4253  CA  ASP B 307    25694  23904  26671   3436   2581  -4715       C  
ATOM   4254  C   ASP B 307      33.755  74.870  83.588  1.00199.02           C  
ANISOU 4254  C   ASP B 307    25496  23840  26280   3436   2500  -4277       C  
ATOM   4255  O   ASP B 307      34.447  73.848  83.452  1.00198.78           O  
ANISOU 4255  O   ASP B 307    25481  24004  26041   3208   2490  -4066       O  
ATOM   4256  CB  ASP B 307      35.569  76.567  84.170  1.00201.17           C  
ANISOU 4256  CB  ASP B 307    25964  23528  26942   3243   2621  -4701       C  
ATOM   4257  CG  ASP B 307      36.050  77.661  85.144  1.00202.79           C  
ANISOU 4257  CG  ASP B 307    26125  23565  27358   3231   2677  -5177       C  
ATOM   4258  OD1 ASP B 307      35.225  78.206  85.897  1.00201.50           O  
ANISOU 4258  OD1 ASP B 307    25824  23514  27221   3431   2683  -5499       O  
ATOM   4259  OD2 ASP B 307      37.257  77.980  85.155  1.00205.36           O  
ANISOU 4259  OD2 ASP B 307    26542  23642  27842   3024   2713  -5250       O  
ATOM   4260  N   ILE B 308      32.577  75.041  82.993  1.00200.44           N  
ANISOU 4260  N   ILE B 308    25652  23954  26551   3703   2428  -4176       N  
ATOM   4261  CA  ILE B 308      32.119  74.130  81.963  1.00202.59           C  
ANISOU 4261  CA  ILE B 308    25957  24302  26714   3743   2315  -3794       C  
ATOM   4262  C   ILE B 308      32.547  74.716  80.624  1.00202.45           C  
ANISOU 4262  C   ILE B 308    26275  23766  26881   3816   2264  -3526       C  
ATOM   4263  O   ILE B 308      31.925  75.651  80.121  1.00200.60           O  
ANISOU 4263  O   ILE B 308    26145  23202  26870   4083   2215  -3544       O  
ATOM   4264  CB  ILE B 308      30.600  73.924  81.981  1.00207.04           C  
ANISOU 4264  CB  ILE B 308    26296  25082  27286   4003   2237  -3830       C  
ATOM   4265  CG1 ILE B 308      30.158  73.410  83.356  1.00207.95           C  
ANISOU 4265  CG1 ILE B 308    26089  25701  27222   3938   2346  -4092       C  
ATOM   4266  CG2 ILE B 308      30.180  72.974  80.852  1.00206.05           C  
ANISOU 4266  CG2 ILE B 308    26206  25010  27072   4046   2084  -3457       C  
ATOM   4267  CD1 ILE B 308      30.868  72.165  83.826  1.00205.31           C  
ANISOU 4267  CD1 ILE B 308    25686  25740  26579   3638   2395  -3967       C  
ATOM   4268  N   ILE B 309      33.616  74.168  80.073  1.00203.54           N  
ANISOU 4268  N   ILE B 309    26582  23834  26918   3586   2287  -3276       N  
ATOM   4269  CA  ILE B 309      34.266  74.719  78.893  1.00206.75           C  
ANISOU 4269  CA  ILE B 309    27331  23749  27475   3606   2305  -3018       C  
ATOM   4270  C   ILE B 309      33.735  74.073  77.622  1.00208.55           C  
ANISOU 4270  C   ILE B 309    27695  23965  27577   3757   2160  -2642       C  
ATOM   4271  O   ILE B 309      33.887  72.869  77.424  1.00210.94           O  
ANISOU 4271  O   ILE B 309    27932  24571  27644   3618   2103  -2464       O  
ATOM   4272  CB  ILE B 309      35.766  74.471  78.964  1.00206.06           C  
ANISOU 4272  CB  ILE B 309    27341  23590  27360   3274   2428  -2964       C  
ATOM   4273  CG1 ILE B 309      36.329  75.096  80.256  1.00207.12           C  
ANISOU 4273  CG1 ILE B 309    27329  23747  27620   3133   2533  -3379       C  
ATOM   4274  CG2 ILE B 309      36.440  75.039  77.726  1.00207.64           C  
ANISOU 4274  CG2 ILE B 309    27896  23275  27722   3289   2498  -2676       C  
ATOM   4275  CD1 ILE B 309      37.422  74.279  80.918  1.00203.66           C  
ANISOU 4275  CD1 ILE B 309    26781  23588  27011   2807   2577  -3441       C  
ATOM   4276  N   LEU B 310      33.123  74.871  76.759  1.00211.66           N  
ANISOU 4276  N   LEU B 310    28289  24003  28126   4054   2085  -2529       N  
ATOM   4277  CA  LEU B 310      32.692  74.374  75.438  1.00212.50           C  
ANISOU 4277  CA  LEU B 310    28585  24048  28105   4236   1923  -2174       C  
ATOM   4278  C   LEU B 310      33.881  74.198  74.519  1.00210.57           C  
ANISOU 4278  C   LEU B 310    28666  23557  27782   4074   2021  -1859       C  
ATOM   4279  O   LEU B 310      34.591  75.164  74.267  1.00219.52           O  
ANISOU 4279  O   LEU B 310    30042  24258  29106   4051   2177  -1821       O  
ATOM   4280  CB  LEU B 310      31.723  75.344  74.762  1.00219.01           C  
ANISOU 4280  CB  LEU B 310    29563  24541  29106   4638   1798  -2141       C  
ATOM   4281  CG  LEU B 310      31.419  75.094  73.270  1.00221.45           C  
ANISOU 4281  CG  LEU B 310    30168  24682  29288   4876   1625  -1768       C  
ATOM   4282  CD1 LEU B 310      30.810  73.716  73.040  1.00218.67           C  
ANISOU 4282  CD1 LEU B 310    29612  24777  28695   4878   1424  -1684       C  
ATOM   4283  CD2 LEU B 310      30.513  76.181  72.725  1.00227.73           C  
ANISOU 4283  CD2 LEU B 310    31126  25124  30275   5291   1498  -1764       C  
ATOM   4284  N   ALA B 311      34.086  73.000  74.000  1.00201.57           N  
ANISOU 4284  N   ALA B 311    27531  22667  26389   3968   1944  -1637       N  
ATOM   4285  CA  ALA B 311      35.233  72.774  73.102  1.00196.78           C  
ANISOU 4285  CA  ALA B 311    27226  21847  25692   3817   2057  -1340       C  
ATOM   4286  C   ALA B 311      34.838  72.049  71.823  1.00198.21           C  
ANISOU 4286  C   ALA B 311    27598  22066  25645   4002   1879  -1018       C  
ATOM   4287  O   ALA B 311      33.860  71.311  71.794  1.00203.74           O  
ANISOU 4287  O   ALA B 311    28107  23077  26227   4136   1657  -1044       O  
ATOM   4288  CB  ALA B 311      36.296  71.982  73.827  1.00190.12           C  
ANISOU 4288  CB  ALA B 311    26213  21261  24761   3429   2181  -1417       C  
ATOM   4289  N   LEU B 312      35.605  72.273  70.761  1.00195.20           N  
ANISOU 4289  N   LEU B 312    27593  21361  25212   4014   1985   -724       N  
ATOM   4290  CA  LEU B 312      35.453  71.540  69.504  1.00189.46           C  
ANISOU 4290  CA  LEU B 312    27093  20671  24222   4170   1839   -416       C  
ATOM   4291  C   LEU B 312      36.602  70.578  69.373  1.00182.76           C  
ANISOU 4291  C   LEU B 312    26254  19972  23212   3850   1966   -292       C  
ATOM   4292  O   LEU B 312      37.756  70.981  69.493  1.00177.44           O  
ANISOU 4292  O   LEU B 312    25690  19077  22649   3620   2231   -262       O  
ATOM   4293  CB  LEU B 312      35.489  72.477  68.293  1.00194.30           C  
ANISOU 4293  CB  LEU B 312    28179  20806  24841   4456   1884   -136       C  
ATOM   4294  CG  LEU B 312      34.627  73.723  68.372  1.00202.90           C  
ANISOU 4294  CG  LEU B 312    29338  21601  26153   4766   1822   -232       C  
ATOM   4295  CD1 LEU B 312      34.806  74.567  67.123  1.00208.12           C  
ANISOU 4295  CD1 LEU B 312    30515  21773  26785   5034   1894    102       C  
ATOM   4296  CD2 LEU B 312      33.170  73.360  68.593  1.00204.32           C  
ANISOU 4296  CD2 LEU B 312    29246  22085  26301   5026   1489   -405       C  
ATOM   4297  N   GLU B 313      36.297  69.321  69.065  1.00183.32           N  
ANISOU 4297  N   GLU B 313    26213  20390  23047   3846   1774   -222       N  
ATOM   4298  CA  GLU B 313      37.339  68.306  68.833  1.00181.60           C  
ANISOU 4298  CA  GLU B 313    26012  20321  22663   3575   1865    -93       C  
ATOM   4299  C   GLU B 313      37.606  68.026  67.345  1.00181.25           C  
ANISOU 4299  C   GLU B 313    26355  20119  22389   3742   1839    235       C  
ATOM   4300  O   GLU B 313      36.689  67.717  66.609  1.00181.50           O  
ANISOU 4300  O   GLU B 313    26471  20223  22265   4036   1581    320       O  
ATOM   4301  CB  GLU B 313      36.988  67.015  69.546  1.00182.23           C  
ANISOU 4301  CB  GLU B 313    25708  20885  22645   3417   1702   -237       C  
ATOM   4302  CG  GLU B 313      38.053  65.940  69.434  1.00180.01           C  
ANISOU 4302  CG  GLU B 313    25408  20767  22220   3133   1781   -135       C  
ATOM   4303  CD  GLU B 313      37.622  64.651  70.098  1.00179.11           C  
ANISOU 4303  CD  GLU B 313    24931  21102  22019   3002   1611   -249       C  
ATOM   4304  OE1 GLU B 313      36.907  63.856  69.456  1.00176.76           O  
ANISOU 4304  OE1 GLU B 313    24614  20958  21587   3158   1381   -163       O  
ATOM   4305  OE2 GLU B 313      37.999  64.431  71.271  1.00182.06           O  
ANISOU 4305  OE2 GLU B 313    25042  21668  22464   2750   1703   -427       O  
ATOM   4306  N   SER B 314      38.859  68.125  66.935  1.00178.85           N  
ANISOU 4306  N   SER B 314    26273  19611  22070   3559   2106    398       N  
ATOM   4307  CA  SER B 314      39.219  67.880  65.543  1.00181.57           C  
ANISOU 4307  CA  SER B 314    27008  19807  22171   3710   2135    714       C  
ATOM   4308  C   SER B 314      40.297  66.808  65.443  1.00184.95           C  
ANISOU 4308  C   SER B 314    27377  20420  22475   3417   2249    775       C  
ATOM   4309  O   SER B 314      41.365  66.932  66.065  1.00186.49           O  
ANISOU 4309  O   SER B 314    27460  20555  22842   3095   2505    699       O  
ATOM   4310  CB  SER B 314      39.721  69.139  64.882  1.00181.90           C  
ANISOU 4310  CB  SER B 314    27458  19346  22308   3823   2406    921       C  
ATOM   4311  OG  SER B 314      40.139  68.837  63.569  1.00180.61           O  
ANISOU 4311  OG  SER B 314    27683  19071  21870   3959   2471   1236       O  
ATOM   4312  N   LYS B 315      40.017  65.742  64.685  1.00186.80           N  
ANISOU 4312  N   LYS B 315    27665  20880  22429   3534   2042    885       N  
ATOM   4313  CA  LYS B 315      40.953  64.624  64.584  1.00184.76           C  
ANISOU 4313  CA  LYS B 315    27329  20818  22052   3279   2114    925       C  
ATOM   4314  C   LYS B 315      42.001  64.806  63.501  1.00187.40           C  
ANISOU 4314  C   LYS B 315    28057  20887  22258   3283   2389   1195       C  
ATOM   4315  O   LYS B 315      42.862  63.927  63.342  1.00190.53           O  
ANISOU 4315  O   LYS B 315    28407  21417  22566   3081   2478   1231       O  
ATOM   4316  CB  LYS B 315      40.164  63.328  64.380  1.00185.18           C  
ANISOU 4316  CB  LYS B 315    27207  21245  21905   3378   1760    877       C  
ATOM   4317  CG  LYS B 315      39.430  62.880  65.640  1.00187.26           C  
ANISOU 4317  CG  LYS B 315    27004  21821  22323   3251   1577    610       C  
ATOM   4318  CD  LYS B 315      38.168  62.102  65.333  1.00189.73           C  
ANISOU 4318  CD  LYS B 315    27182  22380  22526   3479   1202    560       C  
ATOM   4319  CE  LYS B 315      37.367  61.762  66.585  1.00192.47           C  
ANISOU 4319  CE  LYS B 315    27072  23008  23049   3366   1072    314       C  
ATOM   4320  NZ  LYS B 315      35.967  61.314  66.281  1.00197.49           N  
ANISOU 4320  NZ  LYS B 315    27563  23807  23665   3631    723    245       N  
ATOM   4321  N   GLY B 316      41.938  65.918  62.765  1.00191.84           N  
ANISOU 4321  N   GLY B 316    29004  21070  22813   3514   2537   1388       N  
ATOM   4322  CA  GLY B 316      42.931  66.265  61.765  1.00194.93           C  
ANISOU 4322  CA  GLY B 316    29797  21160  23106   3523   2870   1670       C  
ATOM   4323  C   GLY B 316      44.304  66.546  62.361  1.00198.57           C  
ANISOU 4323  C   GLY B 316    30130  21463  23853   3121   3262   1620       C  
ATOM   4324  O   GLY B 316      44.478  66.512  63.589  1.00206.77           O  
ANISOU 4324  O   GLY B 316    30779  22630  25152   2851   3248   1350       O  
ATOM   4325  N   SER B 317      45.294  66.767  61.510  1.00199.86           N  
ANISOU 4325  N   SER B 317    30604  21368  23966   3082   3608   1864       N  
ATOM   4326  CA  SER B 317      46.643  66.970  62.032  1.00199.21           C  
ANISOU 4326  CA  SER B 317    30362  21135  24191   2692   3977   1796       C  
ATOM   4327  C   SER B 317      46.757  68.394  62.568  1.00196.04           C  
ANISOU 4327  C   SER B 317    29976  20335  24174   2628   4197   1742       C  
ATOM   4328  O   SER B 317      46.093  69.324  62.071  1.00195.46           O  
ANISOU 4328  O   SER B 317    30208  19979  24077   2916   4205   1901       O  
ATOM   4329  CB  SER B 317      47.725  66.614  61.009  1.00204.92           C  
ANISOU 4329  CB  SER B 317    31346  21744  24769   2632   4299   2045       C  
ATOM   4330  OG  SER B 317      47.228  66.719  59.695  1.00216.62           O  
ANISOU 4330  OG  SER B 317    33303  23118  25881   3013   4281   2353       O  
ATOM   4331  N   TRP B 318      47.597  68.533  63.584  1.00188.99           N  
ANISOU 4331  N   TRP B 318    28748  19420  23637   2264   4353   1503       N  
ATOM   4332  CA  TRP B 318      47.711  69.768  64.376  1.00186.15           C  
ANISOU 4332  CA  TRP B 318    28287  18742  23699   2153   4501   1338       C  
ATOM   4333  C   TRP B 318      48.158  70.929  63.519  1.00184.14           C  
ANISOU 4333  C   TRP B 318    28432  17932  23601   2237   4892   1622       C  
ATOM   4334  O   TRP B 318      49.002  70.761  62.653  1.00183.53           O  
ANISOU 4334  O   TRP B 318    28575  17703  23452   2181   5194   1868       O  
ATOM   4335  CB  TRP B 318      48.701  69.589  65.524  1.00186.45           C  
ANISOU 4335  CB  TRP B 318    27902  18870  24068   1743   4594   1023       C  
ATOM   4336  CG  TRP B 318      48.223  68.670  66.584  1.00186.94           C  
ANISOU 4336  CG  TRP B 318    27570  19428  24028   1660   4233    728       C  
ATOM   4337  CD1 TRP B 318      47.285  67.669  66.462  1.00187.44           C  
ANISOU 4337  CD1 TRP B 318    27590  19892  23733   1839   3891    751       C  
ATOM   4338  CD2 TRP B 318      48.660  68.645  67.937  1.00188.89           C  
ANISOU 4338  CD2 TRP B 318    27413  19822  24535   1383   4182    367       C  
ATOM   4339  NE1 TRP B 318      47.113  67.043  67.669  1.00186.98           N  
ANISOU 4339  NE1 TRP B 318    27131  20204  23707   1678   3666    454       N  
ATOM   4340  CE2 TRP B 318      47.936  67.627  68.593  1.00189.02           C  
ANISOU 4340  CE2 TRP B 318    27179  20328  24311   1413   3829    217       C  
ATOM   4341  CE3 TRP B 318      49.570  69.405  68.673  1.00190.16           C  
ANISOU 4341  CE3 TRP B 318    27397  19739  25113   1124   4390    144       C  
ATOM   4342  CZ2 TRP B 318      48.116  67.327  69.938  1.00189.85           C  
ANISOU 4342  CZ2 TRP B 318    26900  20701  24531   1206   3696   -115       C  
ATOM   4343  CZ3 TRP B 318      49.757  69.106  70.016  1.00189.77           C  
ANISOU 4343  CZ3 TRP B 318    26952  19968  25181    925   4220   -223       C  
ATOM   4344  CH2 TRP B 318      49.022  68.080  70.638  1.00189.40           C  
ANISOU 4344  CH2 TRP B 318    26698  20423  24839    977   3881   -337       C  
ATOM   4345  N   PRO B 319      47.598  72.131  63.765  1.00183.55           N  
ANISOU 4345  N   PRO B 319    28451  17534  23754   2373   4909   1591       N  
ATOM   4346  CA  PRO B 319      47.979  73.310  62.960  1.00184.49           C  
ANISOU 4346  CA  PRO B 319    28972  17072  24052   2465   5297   1888       C  
ATOM   4347  C   PRO B 319      49.494  73.527  63.013  1.00181.57           C  
ANISOU 4347  C   PRO B 319    28515  16429  24042   2084   5753   1891       C  
ATOM   4348  O   PRO B 319      50.141  73.158  63.986  1.00175.71           O  
ANISOU 4348  O   PRO B 319    27349  15868  23545   1752   5731   1565       O  
ATOM   4349  CB  PRO B 319      47.256  74.458  63.640  1.00189.81           C  
ANISOU 4349  CB  PRO B 319    29594  17496  25027   2572   5201   1714       C  
ATOM   4350  CG  PRO B 319      46.905  73.955  65.017  1.00188.25           C  
ANISOU 4350  CG  PRO B 319    28889  17721  24916   2408   4875   1262       C  
ATOM   4351  CD  PRO B 319      46.732  72.484  64.907  1.00185.28           C  
ANISOU 4351  CD  PRO B 319    28377  17886  24135   2405   4618   1256       C  
ATOM   4352  N   ILE B 320      50.012  74.141  61.963  1.00184.50           N  
ANISOU 4352  N   ILE B 320    29293  16364  24444   2154   6160   2261       N  
ATOM   4353  CA  ILE B 320      51.421  74.311  61.701  1.00187.97           C  
ANISOU 4353  CA  ILE B 320    29723  16512  25184   1841   6653   2354       C  
ATOM   4354  C   ILE B 320      52.158  75.058  62.794  1.00190.44           C  
ANISOU 4354  C   ILE B 320    29656  16562  26138   1478   6818   2014       C  
ATOM   4355  O   ILE B 320      53.377  74.913  62.980  1.00188.30           O  
ANISOU 4355  O   ILE B 320    29162  16201  26179   1132   7109   1917       O  
ATOM   4356  CB  ILE B 320      51.522  75.165  60.417  1.00193.56           C  
ANISOU 4356  CB  ILE B 320    31003  16709  25831   2065   7059   2844       C  
ATOM   4357  CG1 ILE B 320      50.689  76.496  60.519  1.00201.31           C  
ANISOU 4357  CG1 ILE B 320    32199  17272  27018   2301   7023   2901       C  
ATOM   4358  CG2 ILE B 320      51.046  74.348  59.220  1.00190.33           C  
ANISOU 4358  CG2 ILE B 320    30991  16559  24765   2407   6947   3184       C  
ATOM   4359  CD1 ILE B 320      51.428  77.751  60.972  1.00206.09           C  
ANISOU 4359  CD1 ILE B 320    32715  17293  28297   2040   7416   2823       C  
ATOM   4360  N   SER B 321      51.409  75.931  63.468  1.00195.59           N  
ANISOU 4360  N   SER B 321    30248  17057  27008   1579   6639   1829       N  
ATOM   4361  CA  SER B 321      51.970  76.806  64.501  1.00199.12           C  
ANISOU 4361  CA  SER B 321    30371  17208  28076   1289   6764   1480       C  
ATOM   4362  C   SER B 321      52.492  75.998  65.670  1.00196.19           C  
ANISOU 4362  C   SER B 321    29461  17265  27817    974   6548   1027       C  
ATOM   4363  O   SER B 321      53.273  76.524  66.487  1.00196.04           O  
ANISOU 4363  O   SER B 321    29130  17041  28315    675   6677    711       O  
ATOM   4364  CB  SER B 321      50.942  77.834  64.953  1.00201.13           C  
ANISOU 4364  CB  SER B 321    30690  17249  28481   1512   6575   1364       C  
ATOM   4365  OG  SER B 321      49.648  77.350  64.683  1.00199.24           O  
ANISOU 4365  OG  SER B 321    30611  17359  27728   1883   6186   1466       O  
ATOM   4366  N   THR B 322      52.075  74.732  65.737  1.00192.93           N  
ANISOU 4366  N   THR B 322    28944  17427  26934   1050   6217    995       N  
ATOM   4367  CA  THR B 322      52.495  73.831  66.817  1.00191.08           C  
ANISOU 4367  CA  THR B 322    28232  17642  26726    791   5980    606       C  
ATOM   4368  C   THR B 322      53.568  72.885  66.388  1.00191.78           C  
ANISOU 4368  C   THR B 322    28242  17879  26744    579   6156    698       C  
ATOM   4369  O   THR B 322      53.997  72.052  67.198  1.00187.12           O  
ANISOU 4369  O   THR B 322    27277  17659  26158    374   5964    410       O  
ATOM   4370  CB  THR B 322      51.335  72.948  67.238  1.00188.88           C  
ANISOU 4370  CB  THR B 322    27855  17914  25995    996   5499    504       C  
ATOM   4371  OG1 THR B 322      50.975  72.101  66.125  1.00185.34           O  
ANISOU 4371  OG1 THR B 322    27694  17660  25064   1209   5453    857       O  
ATOM   4372  CG2 THR B 322      50.168  73.797  67.621  1.00192.87           C  
ANISOU 4372  CG2 THR B 322    28430  18318  26533   1240   5307    412       C  
ATOM   4373  N   LYS B 323      54.010  72.977  65.125  1.00199.41           N  
ANISOU 4373  N   LYS B 323    29564  18571  27630    641   6519   1100       N  
ATOM   4374  CA  LYS B 323      54.948  72.004  64.559  1.00206.90           C  
ANISOU 4374  CA  LYS B 323    30480  19682  28447    490   6696   1222       C  
ATOM   4375  C   LYS B 323      56.263  71.960  65.344  1.00209.91           C  
ANISOU 4375  C   LYS B 323    30424  20007  29324     76   6858    898       C  
ATOM   4376  O   LYS B 323      56.829  70.873  65.576  1.00209.51           O  
ANISOU 4376  O   LYS B 323    30119  20316  29168    -77   6747    768       O  
ATOM   4377  CB  LYS B 323      55.213  72.308  63.077  1.00214.94           C  
ANISOU 4377  CB  LYS B 323    31988  20357  29322    641   7122   1710       C  
ATOM   4378  CG  LYS B 323      55.435  71.076  62.191  1.00217.58           C  
ANISOU 4378  CG  LYS B 323    32463  21018  29187    722   7128   1930       C  
ATOM   4379  CD  LYS B 323      56.871  70.580  62.172  1.00220.89           C  
ANISOU 4379  CD  LYS B 323    32632  21427  29867    383   7441   1852       C  
ATOM   4380  CE  LYS B 323      56.910  69.094  61.827  1.00220.14           C  
ANISOU 4380  CE  LYS B 323    32493  21831  29319    437   7230   1877       C  
ATOM   4381  NZ  LYS B 323      58.292  68.565  61.848  1.00221.48           N  
ANISOU 4381  NZ  LYS B 323    32390  22010  29750    119   7506   1774       N  
ATOM   4382  N   GLU B 324      56.730  73.141  65.753  1.00214.94           N  
ANISOU 4382  N   GLU B 324    30967  20183  30517    -91   7098    754       N  
ATOM   4383  CA  GLU B 324      57.959  73.267  66.520  1.00218.46           C  
ANISOU 4383  CA  GLU B 324    30982  20515  31508   -474   7239    405       C  
ATOM   4384  C   GLU B 324      57.706  73.209  68.021  1.00212.90           C  
ANISOU 4384  C   GLU B 324    29859  20096  30935   -570   6810   -104       C  
ATOM   4385  O   GLU B 324      58.645  73.195  68.818  1.00214.22           O  
ANISOU 4385  O   GLU B 324    29631  20258  31504   -860   6814   -463       O  
ATOM   4386  CB  GLU B 324      58.679  74.562  66.151  1.00229.45           C  
ANISOU 4386  CB  GLU B 324    32468  21226  33486   -625   7746    498       C  
ATOM   4387  CG  GLU B 324      59.143  74.610  64.703  1.00239.88           C  
ANISOU 4387  CG  GLU B 324    34182  22248  34712   -571   8249   1001       C  
ATOM   4388  CD  GLU B 324      59.842  73.333  64.242  1.00245.21           C  
ANISOU 4388  CD  GLU B 324    34770  23278  35120   -661   8304   1081       C  
ATOM   4389  OE1 GLU B 324      60.681  72.778  64.993  1.00252.52           O  
ANISOU 4389  OE1 GLU B 324    35238  24405  36300   -942   8210    727       O  
ATOM   4390  OE2 GLU B 324      59.531  72.858  63.127  1.00247.61           O  
ANISOU 4390  OE2 GLU B 324    35468  23672  34940   -430   8417   1486       O  
ATOM   4391  N   GLY B 325      56.436  73.133  68.397  1.00205.53           N  
ANISOU 4391  N   GLY B 325    29012  19432  29647   -313   6435   -139       N  
ATOM   4392  CA  GLY B 325      56.046  73.087  69.792  1.00198.45           C  
ANISOU 4392  CA  GLY B 325    27772  18831  28797   -354   6040   -590       C  
ATOM   4393  C   GLY B 325      56.190  71.701  70.406  1.00187.97           C  
ANISOU 4393  C   GLY B 325    26159  18099  27160   -432   5713   -768       C  
ATOM   4394  O   GLY B 325      56.598  70.764  69.733  1.00180.12           O  
ANISOU 4394  O   GLY B 325    25220  17278  25937   -459   5782   -555       O  
ATOM   4395  N   LEU B 326      55.841  71.592  71.682  1.00187.02           N  
ANISOU 4395  N   LEU B 326    25749  18279  27028   -454   5365  -1154       N  
ATOM   4396  CA  LEU B 326      55.902  70.327  72.427  1.00184.71           C  
ANISOU 4396  CA  LEU B 326    25186  18550  26443   -514   5031  -1337       C  
ATOM   4397  C   LEU B 326      57.288  69.667  72.298  1.00185.83           C  
ANISOU 4397  C   LEU B 326    25119  18714  26771   -780   5172  -1387       C  
ATOM   4398  O   LEU B 326      57.433  68.624  71.695  1.00182.98           O  
ANISOU 4398  O   LEU B 326    24820  18585  26116   -760   5163  -1165       O  
ATOM   4399  CB  LEU B 326      54.794  69.400  71.939  1.00183.24           C  
ANISOU 4399  CB  LEU B 326    25202  18738  25680   -258   4816  -1054       C  
ATOM   4400  CG  LEU B 326      54.553  68.137  72.753  1.00182.24           C  
ANISOU 4400  CG  LEU B 326    24833  19189  25221   -271   4450  -1209       C  
ATOM   4401  CD1 LEU B 326      54.113  68.467  74.173  1.00183.35           C  
ANISOU 4401  CD1 LEU B 326    24730  19524  25411   -271   4188  -1602       C  
ATOM   4402  CD2 LEU B 326      53.495  67.330  72.015  1.00181.41           C  
ANISOU 4402  CD2 LEU B 326    24957  19341  24628    -23   4305   -887       C  
ATOM   4403  N   PRO B 327      58.326  70.306  72.825  1.00192.49           N  
ANISOU 4403  N   PRO B 327    25708  19289  28140  -1025   5309  -1692       N  
ATOM   4404  CA  PRO B 327      59.712  69.924  72.612  1.00193.57           C  
ANISOU 4404  CA  PRO B 327    25636  19334  28577  -1284   5509  -1750       C  
ATOM   4405  C   PRO B 327      60.195  68.901  73.641  1.00188.97           C  
ANISOU 4405  C   PRO B 327    24683  19218  27898  -1400   5158  -2078       C  
ATOM   4406  O   PRO B 327      61.246  69.078  74.245  1.00185.91           O  
ANISOU 4406  O   PRO B 327    23970  18735  27930  -1625   5168  -2415       O  
ATOM   4407  CB  PRO B 327      60.431  71.256  72.764  1.00200.26           C  
ANISOU 4407  CB  PRO B 327    26374  19629  30083  -1469   5795  -1957       C  
ATOM   4408  CG  PRO B 327      59.655  71.921  73.851  1.00201.97           C  
ANISOU 4408  CG  PRO B 327    26509  19909  30321  -1371   5503  -2282       C  
ATOM   4409  CD  PRO B 327      58.227  71.577  73.560  1.00198.53           C  
ANISOU 4409  CD  PRO B 327    26379  19745  29306  -1060   5317  -2000       C  
ATOM   4410  N   ILE B 328      59.469  67.804  73.773  1.00186.34           N  
ANISOU 4410  N   ILE B 328    24402  19369  27028  -1243   4858  -1962       N  
ATOM   4411  CA  ILE B 328      59.691  66.800  74.811  1.00185.84           C  
ANISOU 4411  CA  ILE B 328    24043  19781  26786  -1298   4488  -2228       C  
ATOM   4412  C   ILE B 328      60.695  65.728  74.421  1.00182.11           C  
ANISOU 4412  C   ILE B 328    23432  19446  26314  -1435   4531  -2158       C  
ATOM   4413  O   ILE B 328      60.960  64.805  75.202  1.00173.60           O  
ANISOU 4413  O   ILE B 328    22121  18750  25086  -1474   4228  -2344       O  
ATOM   4414  CB  ILE B 328      58.355  66.125  75.153  1.00186.69           C  
ANISOU 4414  CB  ILE B 328    24272  20323  26335  -1062   4165  -2117       C  
ATOM   4415  CG1 ILE B 328      57.874  65.217  74.002  1.00184.21           C  
ANISOU 4415  CG1 ILE B 328    24218  20140  25632   -925   4221  -1679       C  
ATOM   4416  CG2 ILE B 328      57.327  67.192  75.484  1.00189.74           C  
ANISOU 4416  CG2 ILE B 328    24792  20569  26728   -907   4137  -2184       C  
ATOM   4417  CD1 ILE B 328      56.559  64.512  74.259  1.00179.57           C  
ANISOU 4417  CD1 ILE B 328    23724  19953  24550   -706   3918  -1566       C  
ATOM   4418  N   GLN B 329      61.227  65.841  73.207  1.00184.36           N  
ANISOU 4418  N   GLN B 329    23874  19423  26748  -1490   4912  -1880       N  
ATOM   4419  CA  GLN B 329      62.039  64.798  72.565  1.00183.81           C  
ANISOU 4419  CA  GLN B 329    23745  19469  26623  -1575   5008  -1738       C  
ATOM   4420  C   GLN B 329      63.205  64.242  73.361  1.00187.07           C  
ANISOU 4420  C   GLN B 329    23739  20035  27303  -1783   4856  -2087       C  
ATOM   4421  O   GLN B 329      63.653  63.112  73.092  1.00185.93           O  
ANISOU 4421  O   GLN B 329    23518  20128  26999  -1803   4790  -2006       O  
ATOM   4422  CB  GLN B 329      62.543  65.203  71.172  1.00186.34           C  
ANISOU 4422  CB  GLN B 329    24294  19381  27124  -1614   5510  -1419       C  
ATOM   4423  CG  GLN B 329      62.801  66.686  70.938  1.00193.12           C  
ANISOU 4423  CG  GLN B 329    25226  19691  28460  -1703   5876  -1438       C  
ATOM   4424  CD  GLN B 329      61.579  67.405  70.401  1.00195.60           C  
ANISOU 4424  CD  GLN B 329    25950  19842  28524  -1462   5945  -1150       C  
ATOM   4425  OE1 GLN B 329      60.543  66.784  70.171  1.00188.02           O  
ANISOU 4425  OE1 GLN B 329    25208  19189  27042  -1229   5718   -947       O  
ATOM   4426  NE2 GLN B 329      61.698  68.714  70.195  1.00203.19           N  
ANISOU 4426  NE2 GLN B 329    27010  20306  29884  -1514   6253  -1139       N  
ATOM   4427  N   GLY B 330      63.713  65.042  74.306  1.00194.10           N  
ANISOU 4427  N   GLY B 330    24359  20774  28614  -1925   4793  -2487       N  
ATOM   4428  CA  GLY B 330      64.841  64.657  75.145  1.00199.47           C  
ANISOU 4428  CA  GLY B 330    24621  21573  29594  -2107   4613  -2878       C  
ATOM   4429  C   GLY B 330      64.396  64.238  76.546  1.00201.50           C  
ANISOU 4429  C   GLY B 330    24714  22263  29581  -2020   4105  -3181       C  
ATOM   4430  O   GLY B 330      65.195  63.738  77.331  1.00209.56           O  
ANISOU 4430  O   GLY B 330    25419  23475  30728  -2114   3864  -3491       O  
ATOM   4431  N   TRP B 331      63.109  64.458  76.825  1.00200.63           N  
ANISOU 4431  N   TRP B 331    24832  22300  29097  -1825   3958  -3080       N  
ATOM   4432  CA  TRP B 331      62.560  64.284  78.148  1.00201.91           C  
ANISOU 4432  CA  TRP B 331    24883  22828  29004  -1726   3546  -3353       C  
ATOM   4433  C   TRP B 331      61.569  63.132  78.181  1.00189.42           C  
ANISOU 4433  C   TRP B 331    23464  21698  26807  -1538   3313  -3083       C  
ATOM   4434  O   TRP B 331      61.789  62.151  78.887  1.00184.39           O  
ANISOU 4434  O   TRP B 331    22668  21432  25959  -1529   3018  -3189       O  
ATOM   4435  CB  TRP B 331      61.952  65.603  78.645  1.00214.88           C  
ANISOU 4435  CB  TRP B 331    26585  24253  30804  -1672   3568  -3551       C  
ATOM   4436  CG  TRP B 331      61.090  65.497  79.874  1.00220.91           C  
ANISOU 4436  CG  TRP B 331    27323  25400  31211  -1514   3198  -3762       C  
ATOM   4437  CD1 TRP B 331      61.304  64.729  80.990  1.00223.73           C  
ANISOU 4437  CD1 TRP B 331    27479  26180  31347  -1493   2832  -4010       C  
ATOM   4438  CD2 TRP B 331      59.887  66.209  80.104  1.00224.72           C  
ANISOU 4438  CD2 TRP B 331    27994  25869  31518  -1343   3181  -3740       C  
ATOM   4439  NE1 TRP B 331      60.286  64.908  81.890  1.00225.54           N  
ANISOU 4439  NE1 TRP B 331    27775  26669  31248  -1320   2615  -4126       N  
ATOM   4440  CE2 TRP B 331      59.401  65.814  81.370  1.00225.56           C  
ANISOU 4440  CE2 TRP B 331    28000  26413  31286  -1230   2822  -3977       C  
ATOM   4441  CE3 TRP B 331      59.158  67.136  79.353  1.00225.58           C  
ANISOU 4441  CE3 TRP B 331    28358  25638  31714  -1258   3436  -3534       C  
ATOM   4442  CZ2 TRP B 331      58.221  66.316  81.901  1.00225.62           C  
ANISOU 4442  CZ2 TRP B 331    28132  26533  31060  -1047   2733  -4029       C  
ATOM   4443  CZ3 TRP B 331      57.990  67.636  79.874  1.00225.67           C  
ANISOU 4443  CZ3 TRP B 331    28485  25750  31510  -1071   3317  -3593       C  
ATOM   4444  CH2 TRP B 331      57.528  67.225  81.142  1.00226.16           C  
ANISOU 4444  CH2 TRP B 331    28420  26258  31252   -973   2977  -3847       C  
ATOM   4445  N   LEU B 332      60.492  63.247  77.414  1.00184.19           N  
ANISOU 4445  N   LEU B 332    23114  20989  25880  -1383   3441  -2738       N  
ATOM   4446  CA  LEU B 332      59.515  62.155  77.325  1.00182.43           C  
ANISOU 4446  CA  LEU B 332    23034  21154  25125  -1213   3243  -2472       C  
ATOM   4447  C   LEU B 332      59.754  61.286  76.097  1.00181.96           C  
ANISOU 4447  C   LEU B 332    23107  21077  24951  -1214   3397  -2122       C  
ATOM   4448  O   LEU B 332      59.409  60.108  76.074  1.00186.16           O  
ANISOU 4448  O   LEU B 332    23654  21935  25140  -1139   3207  -1968       O  
ATOM   4449  CB  LEU B 332      58.104  62.708  77.338  1.00184.39           C  
ANISOU 4449  CB  LEU B 332    23507  21418  25134  -1017   3221  -2354       C  
ATOM   4450  CG  LEU B 332      57.816  63.396  78.680  1.00189.36           C  
ANISOU 4450  CG  LEU B 332    23992  22148  25809   -992   3029  -2727       C  
ATOM   4451  CD1 LEU B 332      56.479  64.118  78.627  1.00189.38           C  
ANISOU 4451  CD1 LEU B 332    24201  22098  25656   -801   3055  -2636       C  
ATOM   4452  CD2 LEU B 332      57.861  62.420  79.850  1.00187.74           C  
ANISOU 4452  CD2 LEU B 332    23593  22415  25326   -979   2683  -2903       C  
ATOM   4453  N   GLY B 333      60.372  61.855  75.075  1.00180.88           N  
ANISOU 4453  N   GLY B 333    23065  20550  25110  -1298   3754  -1999       N  
ATOM   4454  CA  GLY B 333      60.790  61.065  73.923  1.00176.79           C  
ANISOU 4454  CA  GLY B 333    22655  20005  24511  -1308   3929  -1712       C  
ATOM   4455  C   GLY B 333      60.063  61.348  72.619  1.00171.59           C  
ANISOU 4455  C   GLY B 333    22375  19149  23669  -1151   4177  -1328       C  
ATOM   4456  O   GLY B 333      59.152  62.145  72.584  1.00170.60           O  
ANISOU 4456  O   GLY B 333    22439  18907  23474  -1022   4199  -1262       O  
ATOM   4457  N   THR B 334      60.431  60.610  71.593  1.00168.55           N  
ANISOU 4457  N   THR B 334    22100  18764  23173  -1138   4323  -1090       N  
ATOM   4458  CA  THR B 334      60.065  60.883  70.206  1.00169.14           C  
ANISOU 4458  CA  THR B 334    22543  18610  23111  -1001   4615   -733       C  
ATOM   4459  C   THR B 334      58.734  60.173  69.849  1.00158.69           C  
ANISOU 4459  C   THR B 334    21450  17567  21275   -745   4367   -503       C  
ATOM   4460  O   THR B 334      57.845  60.689  69.143  1.00154.52           O  
ANISOU 4460  O   THR B 334    21236  16906  20567   -551   4448   -279       O  
ATOM   4461  CB  THR B 334      61.267  60.414  69.338  1.00175.04           C  
ANISOU 4461  CB  THR B 334    23258  19232  24017  -1124   4908   -642       C  
ATOM   4462  OG1 THR B 334      61.461  59.001  69.456  1.00176.53           O  
ANISOU 4462  OG1 THR B 334    23303  19782  23987  -1121   4659   -660       O  
ATOM   4463  CG2 THR B 334      62.574  61.097  69.765  1.00178.14           C  
ANISOU 4463  CG2 THR B 334    23360  19347  24974  -1390   5137   -909       C  
ATOM   4464  N   LYS B 335      58.649  58.945  70.358  1.00154.03           N  
ANISOU 4464  N   LYS B 335    20684  17361  20478   -749   4053   -570       N  
ATOM   4465  CA  LYS B 335      57.472  58.085  70.183  1.00156.34           C  
ANISOU 4465  CA  LYS B 335    21106  17950  20344   -547   3779   -405       C  
ATOM   4466  C   LYS B 335      56.264  58.637  70.928  1.00154.58           C  
ANISOU 4466  C   LYS B 335    20905  17818  20008   -427   3581   -470       C  
ATOM   4467  O   LYS B 335      55.112  58.523  70.478  1.00156.75           O  
ANISOU 4467  O   LYS B 335    21378  18169  20008   -219   3474   -294       O  
ATOM   4468  CB  LYS B 335      57.766  56.682  70.704  1.00161.47           C  
ANISOU 4468  CB  LYS B 335    21523  18954  20874   -612   3506   -484       C  
ATOM   4469  CG  LYS B 335      58.954  55.974  70.077  1.00169.05           C  
ANISOU 4469  CG  LYS B 335    22412  19872  21944   -722   3653   -456       C  
ATOM   4470  CD  LYS B 335      58.998  54.498  70.465  1.00172.60           C  
ANISOU 4470  CD  LYS B 335    22687  20670  22220   -729   3347   -484       C  
ATOM   4471  CE  LYS B 335      59.311  54.277  71.946  1.00178.78           C  
ANISOU 4471  CE  LYS B 335    23152  21660  23115   -857   3092   -752       C  
ATOM   4472  NZ  LYS B 335      60.562  54.966  72.407  1.00186.05           N  
ANISOU 4472  NZ  LYS B 335    23858  22393  24439  -1053   3248  -1003       N  
ATOM   4473  N   VAL B 336      56.528  59.188  72.090  1.00154.91           N  
ANISOU 4473  N   VAL B 336    20725  17870  20262   -550   3514   -747       N  
ATOM   4474  CA  VAL B 336      55.549  59.858  72.946  1.00159.46           C  
ANISOU 4474  CA  VAL B 336    21284  18512  20788   -460   3364   -874       C  
ATOM   4475  C   VAL B 336      54.989  61.080  72.227  1.00162.18           C  
ANISOU 4475  C   VAL B 336    21903  18510  21208   -329   3582   -743       C  
ATOM   4476  O   VAL B 336      53.784  61.215  72.054  1.00154.86           O  
ANISOU 4476  O   VAL B 336    21130  17645  20061   -126   3474   -626       O  
ATOM   4477  CB  VAL B 336      56.260  60.306  74.235  1.00163.48           C  
ANISOU 4477  CB  VAL B 336    21509  19043  21563   -634   3299  -1236       C  
ATOM   4478  CG1 VAL B 336      55.272  60.939  75.211  1.00165.98           C  
ANISOU 4478  CG1 VAL B 336    21795  19466  21803   -533   3139  -1400       C  
ATOM   4479  CG2 VAL B 336      56.985  59.117  74.855  1.00161.76           C  
ANISOU 4479  CG2 VAL B 336    21041  19129  21290   -755   3098  -1349       C  
ATOM   4480  N   ARG B 337      55.868  61.978  71.835  1.00169.91           N  
ANISOU 4480  N   ARG B 337    22927  19109  22520   -443   3890   -768       N  
ATOM   4481  CA  ARG B 337      55.485  63.202  71.133  1.00177.81           C  
ANISOU 4481  CA  ARG B 337    24202  19719  23636   -331   4137   -625       C  
ATOM   4482  C   ARG B 337      54.704  62.862  69.856  1.00175.70           C  
ANISOU 4482  C   ARG B 337    24282  19445  23030    -90   4171   -259       C  
ATOM   4483  O   ARG B 337      53.695  63.512  69.535  1.00176.45           O  
ANISOU 4483  O   ARG B 337    24601  19427  23015    120   4154   -139       O  
ATOM   4484  CB  ARG B 337      56.748  63.960  70.734  1.00185.05           C  
ANISOU 4484  CB  ARG B 337    25108  20224  24977   -523   4514   -654       C  
ATOM   4485  CG  ARG B 337      56.479  65.273  70.026  1.00191.51           C  
ANISOU 4485  CG  ARG B 337    26218  20584  25963   -427   4812   -490       C  
ATOM   4486  CD  ARG B 337      57.723  66.135  69.921  1.00196.46           C  
ANISOU 4486  CD  ARG B 337    26758  20782  27105   -659   5183   -586       C  
ATOM   4487  NE  ARG B 337      57.357  67.471  69.445  1.00204.96           N  
ANISOU 4487  NE  ARG B 337    28099  21405  28369   -564   5440   -452       N  
ATOM   4488  CZ  ARG B 337      57.079  67.791  68.179  1.00210.21           C  
ANISOU 4488  CZ  ARG B 337    29161  21815  28893   -394   5704    -65       C  
ATOM   4489  NH1 ARG B 337      57.162  66.879  67.210  1.00211.34           N  
ANISOU 4489  NH1 ARG B 337    29484  22111  28702   -305   5761    211       N  
ATOM   4490  NH2 ARG B 337      56.738  69.046  67.872  1.00212.88           N  
ANISOU 4490  NH2 ARG B 337    29730  21728  29425   -302   5914     42       N  
ATOM   4491  N   THR B 338      55.186  61.845  69.136  1.00171.44           N  
ANISOU 4491  N   THR B 338    23781  19027  22331   -109   4202   -103       N  
ATOM   4492  CA  THR B 338      54.546  61.432  67.899  1.00169.94           C  
ANISOU 4492  CA  THR B 338    23914  18850  21803    126   4212    211       C  
ATOM   4493  C   THR B 338      53.135  60.927  68.168  1.00169.55           C  
ANISOU 4493  C   THR B 338    23877  19107  21435    335   3845    228       C  
ATOM   4494  O   THR B 338      52.202  61.231  67.430  1.00172.74           O  
ANISOU 4494  O   THR B 338    24556  19435  21641    585   3814    417       O  
ATOM   4495  CB  THR B 338      55.367  60.391  67.181  1.00167.16           C  
ANISOU 4495  CB  THR B 338    23567  18593  21353     61   4297    321       C  
ATOM   4496  OG1 THR B 338      56.594  61.011  66.793  1.00165.16           O  
ANISOU 4496  OG1 THR B 338    23329  18005  21418   -109   4698    334       O  
ATOM   4497  CG2 THR B 338      54.626  59.871  65.954  1.00168.03           C  
ANISOU 4497  CG2 THR B 338    24008  18765  21071    333   4247    607       C  
ATOM   4498  N   ASN B 339      52.989  60.139  69.223  1.00167.37           N  
ANISOU 4498  N   ASN B 339    23299  19175  21118    238   3568     34       N  
ATOM   4499  CA  ASN B 339      51.670  59.620  69.592  1.00168.01           C  
ANISOU 4499  CA  ASN B 339    23339  19552  20946    405   3244     34       C  
ATOM   4500  C   ASN B 339      50.730  60.670  70.131  1.00167.15           C  
ANISOU 4500  C   ASN B 339    23255  19358  20896    522   3197    -56       C  
ATOM   4501  O   ASN B 339      49.535  60.572  69.971  1.00172.78           O  
ANISOU 4501  O   ASN B 339    24043  20183  21420    730   3018     16       O  
ATOM   4502  CB  ASN B 339      51.809  58.515  70.620  1.00169.36           C  
ANISOU 4502  CB  ASN B 339    23191  20093  21065    263   3003   -126       C  
ATOM   4503  CG  ASN B 339      52.326  57.234  70.006  1.00173.70           C  
ANISOU 4503  CG  ASN B 339    23729  20787  21481    224   2953     -9       C  
ATOM   4504  OD1 ASN B 339      52.559  57.144  68.792  1.00176.69           O  
ANISOU 4504  OD1 ASN B 339    24340  21012  21780    312   3097    181       O  
ATOM   4505  ND2 ASN B 339      52.505  56.227  70.838  1.00181.01           N  
ANISOU 4505  ND2 ASN B 339    24397  22007  22369    107   2750   -120       N  
ATOM   4506  N   LEU B 340      51.276  61.677  70.792  1.00163.28           N  
ANISOU 4506  N   LEU B 340    22678  18665  20696    390   3350   -241       N  
ATOM   4507  CA  LEU B 340      50.471  62.758  71.352  1.00167.37           C  
ANISOU 4507  CA  LEU B 340    23209  19073  21309    496   3323   -363       C  
ATOM   4508  C   LEU B 340      49.958  63.650  70.241  1.00167.07           C  
ANISOU 4508  C   LEU B 340    23522  18695  21262    715   3479   -135       C  
ATOM   4509  O   LEU B 340      48.801  64.051  70.264  1.00161.53           O  
ANISOU 4509  O   LEU B 340    22901  18008  20464    930   3347   -117       O  
ATOM   4510  CB  LEU B 340      51.299  63.589  72.290  1.00174.70           C  
ANISOU 4510  CB  LEU B 340    23955  19844  22576    294   3445   -644       C  
ATOM   4511  CG  LEU B 340      51.360  62.970  73.678  1.00177.50           C  
ANISOU 4511  CG  LEU B 340    23980  20572  22888    169   3212   -920       C  
ATOM   4512  CD1 LEU B 340      52.644  63.380  74.411  1.00180.24           C  
ANISOU 4512  CD1 LEU B 340    24122  20801  23558    -76   3315  -1194       C  
ATOM   4513  CD2 LEU B 340      50.108  63.329  74.489  1.00177.87           C  
ANISOU 4513  CD2 LEU B 340    23968  20788  22826    325   3032  -1050       C  
ATOM   4514  N   ARG B 341      50.807  63.952  69.258  1.00171.64           N  
ANISOU 4514  N   ARG B 341    24314  18965  21935    675   3766     47       N  
ATOM   4515  CA  ARG B 341      50.402  64.783  68.125  1.00178.35           C  
ANISOU 4515  CA  ARG B 341    25549  19473  22744    901   3940    308       C  
ATOM   4516  C   ARG B 341      49.509  64.047  67.117  1.00173.62           C  
ANISOU 4516  C   ARG B 341    25182  19038  21747   1178   3762    557       C  
ATOM   4517  O   ARG B 341      48.973  64.683  66.184  1.00174.34           O  
ANISOU 4517  O   ARG B 341    25615  18891  21735   1429   3836    777       O  
ATOM   4518  CB  ARG B 341      51.625  65.307  67.383  1.00185.28           C  
ANISOU 4518  CB  ARG B 341    26591  19968  23839    768   4346    446       C  
ATOM   4519  CG  ARG B 341      52.424  66.298  68.195  1.00191.43           C  
ANISOU 4519  CG  ARG B 341    27186  20473  25076    532   4547    210       C  
ATOM   4520  CD  ARG B 341      53.639  66.740  67.425  1.00198.91           C  
ANISOU 4520  CD  ARG B 341    28265  21036  26272    383   4974    356       C  
ATOM   4521  NE  ARG B 341      53.268  67.575  66.292  1.00209.73           N  
ANISOU 4521  NE  ARG B 341    30069  22034  27585    606   5213    683       N  
ATOM   4522  CZ  ARG B 341      52.966  68.880  66.355  1.00223.51           C  
ANISOU 4522  CZ  ARG B 341    31952  23395  29574    677   5353    691       C  
ATOM   4523  NH1 ARG B 341      52.970  69.556  67.513  1.00225.60           N  
ANISOU 4523  NH1 ARG B 341    31946  23594  30176    541   5276    359       N  
ATOM   4524  NH2 ARG B 341      52.641  69.518  65.236  1.00231.58           N  
ANISOU 4524  NH2 ARG B 341    33405  24093  30491    907   5563   1035       N  
ATOM   4525  N   ARG B 342      49.355  62.745  67.298  1.00169.88           N  
ANISOU 4525  N   ARG B 342    24531  18950  21065   1144   3522    518       N  
ATOM   4526  CA  ARG B 342      48.424  61.943  66.500  1.00172.81           C  
ANISOU 4526  CA  ARG B 342    25050  19518  21091   1396   3286    684       C  
ATOM   4527  C   ARG B 342      47.015  62.051  67.065  1.00166.34           C  
ANISOU 4527  C   ARG B 342    24123  18872  20204   1574   2989    580       C  
ATOM   4528  O   ARG B 342      46.058  61.600  66.424  1.00162.09           O  
ANISOU 4528  O   ARG B 342    23700  18454  19430   1820   2770    689       O  
ATOM   4529  CB  ARG B 342      48.835  60.479  66.527  1.00179.34           C  
ANISOU 4529  CB  ARG B 342    25698  20667  21777   1270   3147    663       C  
ATOM   4530  CG  ARG B 342      49.816  60.132  65.425  1.00187.68           C  
ANISOU 4530  CG  ARG B 342    26966  21590  22751   1247   3375    849       C  
ATOM   4531  CD  ARG B 342      50.304  58.707  65.570  1.00191.43           C  
ANISOU 4531  CD  ARG B 342    27227  22367  23138   1104   3238    789       C  
ATOM   4532  NE  ARG B 342      50.769  58.162  64.299  1.00198.58           N  
ANISOU 4532  NE  ARG B 342    28380  23223  23846   1201   3352    984       N  
ATOM   4533  CZ  ARG B 342      51.543  57.079  64.180  1.00198.18           C  
ANISOU 4533  CZ  ARG B 342    28203  23331  23762   1066   3346    957       C  
ATOM   4534  NH1 ARG B 342      51.974  56.426  65.275  1.00198.68           N  
ANISOU 4534  NH1 ARG B 342    27897  23606  23986    825   3225    759       N  
ATOM   4535  NH2 ARG B 342      51.898  56.658  62.964  1.00195.27           N  
ANISOU 4535  NH2 ARG B 342    28090  22910  23192   1190   3463   1128       N  
ATOM   4536  N   GLU B 343      46.915  62.637  68.252  1.00163.95           N  
ANISOU 4536  N   GLU B 343    23590  18584  20117   1454   2984    351       N  
ATOM   4537  CA  GLU B 343      45.657  62.747  68.968  1.00165.75           C  
ANISOU 4537  CA  GLU B 343    23662  18999  20317   1589   2741    212       C  
ATOM   4538  C   GLU B 343      44.908  63.940  68.410  1.00167.15           C  
ANISOU 4538  C   GLU B 343    24102  18872  20534   1858   2784    302       C  
ATOM   4539  O   GLU B 343      45.534  64.793  67.751  1.00165.97           O  
ANISOU 4539  O   GLU B 343    24219  18351  20489   1875   3042    437       O  
ATOM   4540  CB  GLU B 343      45.905  63.116  70.414  1.00169.40           C  
ANISOU 4540  CB  GLU B 343    23827  19548  20989   1386   2762    -75       C  
ATOM   4541  CG  GLU B 343      46.630  62.105  71.238  1.00172.57           C  
ANISOU 4541  CG  GLU B 343    23946  20244  21378   1127   2706   -206       C  
ATOM   4542  CD  GLU B 343      45.867  61.844  72.503  1.00181.49           C  
ANISOU 4542  CD  GLU B 343    24790  21691  22475   1111   2516   -417       C  
ATOM   4543  OE1 GLU B 343      46.208  62.440  73.553  1.00192.84           O  
ANISOU 4543  OE1 GLU B 343    26074  23122  24071    987   2575   -653       O  
ATOM   4544  OE2 GLU B 343      44.886  61.075  72.413  1.00186.49           O  
ANISOU 4544  OE2 GLU B 343    25359  22568  22928   1237   2313   -351       O  
ATOM   4545  N   PRO B 344      43.590  64.038  68.706  1.00169.91           N  
ANISOU 4545  N   PRO B 344    24369  19361  20828   2065   2549    225       N  
ATOM   4546  CA  PRO B 344      42.881  65.199  68.217  1.00172.44           C  
ANISOU 4546  CA  PRO B 344    24929  19382  21205   2338   2570    296       C  
ATOM   4547  C   PRO B 344      43.306  66.473  68.942  1.00176.86           C  
ANISOU 4547  C   PRO B 344    25464  19660  22075   2230   2786    138       C  
ATOM   4548  O   PRO B 344      43.951  66.392  69.998  1.00177.73           O  
ANISOU 4548  O   PRO B 344    25310  19880  22337   1961   2855    -82       O  
ATOM   4549  CB  PRO B 344      41.413  64.883  68.531  1.00170.97           C  
ANISOU 4549  CB  PRO B 344    24570  19458  20929   2550   2256    194       C  
ATOM   4550  CG  PRO B 344      41.410  63.562  69.221  1.00169.98           C  
ANISOU 4550  CG  PRO B 344    24115  19754  20713   2359   2108     84       C  
ATOM   4551  CD  PRO B 344      42.785  63.332  69.705  1.00171.00           C  
ANISOU 4551  CD  PRO B 344    24162  19884  20926   2032   2311     34       C  
ATOM   4552  N   PHE B 345      42.955  67.635  68.394  1.00184.04           N  
ANISOU 4552  N   PHE B 345    26645  20200  23083   2448   2877    239       N  
ATOM   4553  CA  PHE B 345      43.185  68.877  69.106  1.00189.10           C  
ANISOU 4553  CA  PHE B 345    27244  20556  24049   2376   3046     61       C  
ATOM   4554  C   PHE B 345      41.862  69.593  69.310  1.00190.75           C  
ANISOU 4554  C   PHE B 345    27454  20721  24298   2668   2871    -29       C  
ATOM   4555  O   PHE B 345      40.835  69.163  68.783  1.00185.04           O  
ANISOU 4555  O   PHE B 345    26786  20156  23362   2929   2634     71       O  
ATOM   4556  CB  PHE B 345      44.184  69.754  68.381  1.00194.56           C  
ANISOU 4556  CB  PHE B 345    28239  20763  24922   2318   3385    246       C  
ATOM   4557  CG  PHE B 345      43.748  70.130  67.011  1.00201.28           C  
ANISOU 4557  CG  PHE B 345    29522  21347  25608   2636   3416    588       C  
ATOM   4558  CD1 PHE B 345      44.055  69.311  65.927  1.00201.40           C  
ANISOU 4558  CD1 PHE B 345    29756  21438  25328   2694   3432    862       C  
ATOM   4559  CD2 PHE B 345      43.003  71.282  66.802  1.00207.63           C  
ANISOU 4559  CD2 PHE B 345    30525  21834  26530   2904   3410    630       C  
ATOM   4560  CE1 PHE B 345      43.636  69.645  64.646  1.00205.52           C  
ANISOU 4560  CE1 PHE B 345    30709  21734  25643   3024   3442   1178       C  
ATOM   4561  CE2 PHE B 345      42.583  71.615  65.529  1.00211.03           C  
ANISOU 4561  CE2 PHE B 345    31382  22025  26772   3231   3414    959       C  
ATOM   4562  CZ  PHE B 345      42.896  70.797  64.450  1.00209.94           C  
ANISOU 4562  CZ  PHE B 345    31478  21979  26307   3297   3428   1235       C  
ATOM   4563  N   TYR B 346      41.879  70.680  70.060  1.00192.78           N  
ANISOU 4563  N   TYR B 346    27637  20760  24847   2635   2975   -239       N  
ATOM   4564  CA  TYR B 346      40.644  71.274  70.554  1.00194.64           C  
ANISOU 4564  CA  TYR B 346    27774  21025  25152   2873   2801   -413       C  
ATOM   4565  C   TYR B 346      40.601  72.778  70.376  1.00198.36           C  
ANISOU 4565  C   TYR B 346    28464  20991  25910   3015   2956   -413       C  
ATOM   4566  O   TYR B 346      41.637  73.436  70.532  1.00193.13           O  
ANISOU 4566  O   TYR B 346    27860  20016  25503   2810   3216   -449       O  
ATOM   4567  CB  TYR B 346      40.496  70.936  72.026  1.00194.20           C  
ANISOU 4567  CB  TYR B 346    27303  21334  25151   2692   2716   -776       C  
ATOM   4568  CG  TYR B 346      40.399  69.458  72.279  1.00187.43           C  
ANISOU 4568  CG  TYR B 346    26220  20968  24026   2573   2554   -770       C  
ATOM   4569  CD1 TYR B 346      41.525  68.716  72.603  1.00181.86           C  
ANISOU 4569  CD1 TYR B 346    25404  20412  23280   2262   2647   -789       C  
ATOM   4570  CD2 TYR B 346      39.177  68.797  72.170  1.00183.09           C  
ANISOU 4570  CD2 TYR B 346    25560  20711  23292   2776   2305   -747       C  
ATOM   4571  CE1 TYR B 346      41.437  67.352  72.830  1.00175.18           C  
ANISOU 4571  CE1 TYR B 346    24364  19991  22204   2160   2498   -769       C  
ATOM   4572  CE2 TYR B 346      39.077  67.439  72.405  1.00177.67           C  
ANISOU 4572  CE2 TYR B 346    24661  20442  22401   2657   2170   -735       C  
ATOM   4573  CZ  TYR B 346      40.213  66.719  72.737  1.00174.16           C  
ANISOU 4573  CZ  TYR B 346    24133  20133  21906   2351   2268   -736       C  
ATOM   4574  OH  TYR B 346      40.109  65.365  72.969  1.00170.79           O  
ANISOU 4574  OH  TYR B 346    23506  20095  21290   2242   2133   -712       O  
ATOM   4575  N   LEU B 347      39.419  73.317  70.096  1.00204.65           N  
ANISOU 4575  N   LEU B 347    29356  21700  26700   3359   2792   -392       N  
ATOM   4576  CA  LEU B 347      39.259  74.745  69.920  1.00210.96           C  
ANISOU 4576  CA  LEU B 347    30370  22007  27778   3534   2911   -386       C  
ATOM   4577  C   LEU B 347      38.166  75.256  70.859  1.00217.12           C  
ANISOU 4577  C   LEU B 347    30896  22898  28699   3697   2737   -713       C  
ATOM   4578  O   LEU B 347      37.041  74.761  70.902  1.00224.75           O  
ANISOU 4578  O   LEU B 347    31724  24171  29499   3907   2477   -762       O  
ATOM   4579  CB  LEU B 347      38.880  75.024  68.491  1.00212.33           C  
ANISOU 4579  CB  LEU B 347    30978  21896  27801   3862   2883     -1       C  
ATOM   4580  CG  LEU B 347      40.138  75.028  67.640  1.00212.28           C  
ANISOU 4580  CG  LEU B 347    31277  21604  27773   3696   3185    302       C  
ATOM   4581  CD1 LEU B 347      39.812  74.571  66.235  1.00213.28           C  
ANISOU 4581  CD1 LEU B 347    31773  21720  27543   3978   3090    688       C  
ATOM   4582  CD2 LEU B 347      40.783  76.407  67.656  1.00217.01           C  
ANISOU 4582  CD2 LEU B 347    32063  21626  28763   3638   3497    323       C  
ATOM   4583  N   VAL B 348      38.468  76.283  71.608  1.00219.11           N  
ANISOU 4583  N   VAL B 348    31078  22888  29285   3611   2883   -957       N  
ATOM   4584  CA  VAL B 348      37.481  76.870  72.510  1.00221.78           C  
ANISOU 4584  CA  VAL B 348    31188  23300  29775   3776   2749  -1291       C  
ATOM   4585  C   VAL B 348      37.223  78.282  72.054  1.00223.48           C  
ANISOU 4585  C   VAL B 348    31677  22952  30281   4022   2828  -1231       C  
ATOM   4586  O   VAL B 348      38.054  78.841  71.368  1.00222.01           O  
ANISOU 4586  O   VAL B 348    31791  22325  30235   3959   3049  -1002       O  
ATOM   4587  CB  VAL B 348      37.957  76.818  73.950  1.00223.89           C  
ANISOU 4587  CB  VAL B 348    31099  23800  30168   3488   2813  -1701       C  
ATOM   4588  CG1 VAL B 348      38.274  75.368  74.316  1.00219.27           C  
ANISOU 4588  CG1 VAL B 348    30287  23747  29277   3253   2740  -1701       C  
ATOM   4589  CG2 VAL B 348      39.155  77.750  74.168  1.00227.57           C  
ANISOU 4589  CG2 VAL B 348    31656  23827  30983   3264   3076  -1798       C  
ATOM   4590  N   PRO B 349      36.072  78.869  72.408  1.00228.56           N  
ANISOU 4590  N   PRO B 349    32222  23588  31031   4310   2664  -1424       N  
ATOM   4591  CA  PRO B 349      35.843  80.291  72.091  1.00237.52           C  
ANISOU 4591  CA  PRO B 349    33601  24154  32490   4546   2739  -1403       C  
ATOM   4592  C   PRO B 349      36.863  81.216  72.732  1.00240.22           C  
ANISOU 4592  C   PRO B 349    33925  24125  33220   4288   3005  -1612       C  
ATOM   4593  O   PRO B 349      37.150  81.091  73.922  1.00241.66           O  
ANISOU 4593  O   PRO B 349    33775  24556  33489   4059   3025  -1996       O  
ATOM   4594  CB  PRO B 349      34.455  80.550  72.682  1.00240.43           C  
ANISOU 4594  CB  PRO B 349    33733  24715  32904   4841   2501  -1686       C  
ATOM   4595  CG  PRO B 349      33.787  79.223  72.651  1.00235.43           C  
ANISOU 4595  CG  PRO B 349    32888  24656  31907   4872   2277  -1649       C  
ATOM   4596  CD  PRO B 349      34.867  78.242  72.977  1.00228.71           C  
ANISOU 4596  CD  PRO B 349    31921  24092  30884   4464   2405  -1630       C  
ATOM   4597  N   LYS B 350      37.384  82.154  71.964  1.00241.69           N  
ANISOU 4597  N   LYS B 350    34466  23714  33648   4338   3205  -1370       N  
ATOM   4598  CA  LYS B 350      38.263  83.203  72.501  1.00243.15           C  
ANISOU 4598  CA  LYS B 350    34640  23447  34296   4128   3457  -1578       C  
ATOM   4599  C   LYS B 350      37.461  84.111  73.413  1.00247.75           C  
ANISOU 4599  C   LYS B 350    35028  23944  35159   4307   3344  -1993       C  
ATOM   4600  O   LYS B 350      37.944  84.509  74.466  1.00249.10           O  
ANISOU 4600  O   LYS B 350    34952  24096  35596   4093   3422  -2397       O  
ATOM   4601  CB  LYS B 350      38.808  84.071  71.356  1.00243.79           C  
ANISOU 4601  CB  LYS B 350    35181  22854  34594   4201   3706  -1172       C  
ATOM   4602  CG  LYS B 350      39.625  85.314  71.747  1.00244.08           C  
ANISOU 4602  CG  LYS B 350    35243  22299  35195   4023   3980  -1347       C  
ATOM   4603  CD  LYS B 350      39.709  86.282  70.580  1.00246.10           C  
ANISOU 4603  CD  LYS B 350    35984  21871  35650   4230   4182   -915       C  
ATOM   4604  CE  LYS B 350      40.766  87.361  70.731  1.00247.01           C  
ANISOU 4604  CE  LYS B 350    36165  21347  36340   3983   4531   -981       C  
ATOM   4605  NZ  LYS B 350      40.530  88.447  69.731  1.00250.21           N  
ANISOU 4605  NZ  LYS B 350    37037  21070  36960   4271   4687   -593       N  
ATOM   4606  N   ASN B 351      36.279  84.513  72.942  1.00249.80           N  
ANISOU 4606  N   ASN B 351    35426  24104  35383   4721   3163  -1889       N  
ATOM   4607  CA  ASN B 351      35.325  85.315  73.708  1.00249.89           C  
ANISOU 4607  CA  ASN B 351    35252  24066  35628   4960   3026  -2267       C  
ATOM   4608  C   ASN B 351      35.961  86.586  74.320  1.00253.54           C  
ANISOU 4608  C   ASN B 351    35705  24010  36616   4835   3228  -2555       C  
ATOM   4609  O   ASN B 351      35.625  87.015  75.424  1.00251.88           O  
ANISOU 4609  O   ASN B 351    35205  23902  36595   4844   3166  -3033       O  
ATOM   4610  CB  ASN B 351      34.596  84.482  74.792  1.00243.01           C  
ANISOU 4610  CB  ASN B 351    33931  23880  34521   4940   2823  -2646       C  
ATOM   4611  CG  ASN B 351      33.317  85.158  75.315  1.00242.91           C  
ANISOU 4611  CG  ASN B 351    33755  23874  34664   5288   2648  -2954       C  
ATOM   4612  OD1 ASN B 351      32.444  85.563  74.544  1.00241.06           O  
ANISOU 4612  OD1 ASN B 351    33713  23423  34453   5662   2510  -2757       O  
ATOM   4613  ND2 ASN B 351      33.208  85.272  76.640  1.00242.66           N  
ANISOU 4613  ND2 ASN B 351    33366  24104  34729   5182   2650  -3452       N  
ATOM   4614  N   ALA B 352      36.855  87.194  73.545  1.00256.72           N  
ANISOU 4614  N   ALA B 352    36442  23840  37260   4735   3477  -2252       N  
ATOM   4615  CA  ALA B 352      37.359  88.517  73.879  1.00261.17           C  
ANISOU 4615  CA  ALA B 352    37058  23788  38386   4670   3669  -2453       C  
ATOM   4616  C   ALA B 352      36.217  89.509  73.714  1.00264.14           C  
ANISOU 4616  C   ALA B 352    37561  23837  38960   5112   3528  -2491       C  
ATOM   4617  O   ALA B 352      35.364  89.353  72.851  1.00265.42           O  
ANISOU 4617  O   ALA B 352    37949  24019  38878   5458   3371  -2161       O  
ATOM   4618  CB  ALA B 352      38.522  88.901  72.984  1.00262.28           C  
ANISOU 4618  CB  ALA B 352    37538  23370  38747   4473   3998  -2062       C  
ATOM   4619  N   LYS B 353      36.226  90.564  74.523  1.00264.00           N  
ANISOU 4619  N   LYS B 353    37405  23493  39410   5113   3572  -2905       N  
ATOM   4620  CA  LYS B 353      35.219  91.612  74.429  1.00264.10           C  
ANISOU 4620  CA  LYS B 353    37527  23134  39685   5525   3453  -2981       C  
ATOM   4621  C   LYS B 353      35.833  92.947  74.001  1.00265.10           C  
ANISOU 4621  C   LYS B 353    37957  22394  40375   5520   3703  -2853       C  
ATOM   4622  O   LYS B 353      35.513  93.997  74.570  1.00266.28           O  
ANISOU 4622  O   LYS B 353    38024  22190  40957   5653   3683  -3200       O  
ATOM   4623  CB  LYS B 353      34.478  91.739  75.772  1.00263.76           C  
ANISOU 4623  CB  LYS B 353    37049  23458  39707   5605   3265  -3611       C  
ATOM   4624  CG  LYS B 353      34.017  90.424  76.412  1.00256.74           C  
ANISOU 4624  CG  LYS B 353    35808  23425  38315   5534   3081  -3792       C  
ATOM   4625  CD  LYS B 353      32.916  89.725  75.619  1.00252.43           C  
ANISOU 4625  CD  LYS B 353    35352  23190  37367   5864   2855  -3460       C  
ATOM   4626  CE  LYS B 353      32.203  88.669  76.442  1.00247.66           C  
ANISOU 4626  CE  LYS B 353    34340  23365  36394   5854   2671  -3740       C  
ATOM   4627  NZ  LYS B 353      31.019  88.154  75.710  1.00247.76           N  
ANISOU 4627  NZ  LYS B 353    34398  23610  36126   6209   2429  -3487       N  
ATOM   4628  N   ASP B 354      36.724  92.894  73.015  1.00261.27           N  
ANISOU 4628  N   ASP B 354    37811  21563  39893   5361   3955  -2362       N  
ATOM   4629  CA  ASP B 354      37.595  94.009  72.645  1.00264.07           C  
ANISOU 4629  CA  ASP B 354    38424  21107  40803   5234   4281  -2215       C  
ATOM   4630  C   ASP B 354      37.013  94.899  71.550  1.00266.43           C  
ANISOU 4630  C   ASP B 354    39207  20788  41233   5647   4311  -1759       C  
ATOM   4631  O   ASP B 354      37.438  96.049  71.373  1.00269.69           O  
ANISOU 4631  O   ASP B 354    39819  20461  42187   5635   4542  -1700       O  
ATOM   4632  CB  ASP B 354      39.009  93.512  72.234  1.00262.34           C  
ANISOU 4632  CB  ASP B 354    38287  20814  40575   4794   4604  -1948       C  
ATOM   4633  CG  ASP B 354      38.991  92.264  71.330  1.00259.94           C  
ANISOU 4633  CG  ASP B 354    38161  20968  39634   4817   4563  -1472       C  
ATOM   4634  OD1 ASP B 354      37.968  91.993  70.664  1.00260.15           O  
ANISOU 4634  OD1 ASP B 354    38394  21166  39284   5209   4340  -1198       O  
ATOM   4635  OD2 ASP B 354      40.011  91.543  71.291  1.00259.17           O  
ANISOU 4635  OD2 ASP B 354    37985  21061  39426   4446   4740  -1395       O  
ATOM   4636  N   GLY B 355      36.090  94.343  70.768  1.00263.26           N  
ANISOU 4636  N   GLY B 355    39010  20673  40341   6011   4082  -1416       N  
ATOM   4637  CA  GLY B 355      35.441  95.073  69.683  1.00264.86           C  
ANISOU 4637  CA  GLY B 355    39696  20366  40572   6465   4049   -963       C  
ATOM   4638  C   GLY B 355      36.102  94.896  68.336  1.00265.86           C  
ANISOU 4638  C   GLY B 355    40331  20194  40486   6450   4305   -277       C  
ATOM   4639  O   GLY B 355      35.739  95.568  67.367  1.00266.19           O  
ANISOU 4639  O   GLY B 355    40843  19737  40557   6810   4335    157       O  
ATOM   4640  N   ASN B 356      37.060  93.970  68.268  1.00265.01           N  
ANISOU 4640  N   ASN B 356    40141  20408  40143   6054   4488   -177       N  
ATOM   4641  CA  ASN B 356      37.722  93.604  67.021  1.00265.05           C  
ANISOU 4641  CA  ASN B 356    40591  20248  39866   6016   4741    449       C  
ATOM   4642  C   ASN B 356      36.759  93.134  65.930  1.00266.99           C  
ANISOU 4642  C   ASN B 356    41202  20703  39540   6498   4474    885       C  
ATOM   4643  O   ASN B 356      35.654  92.679  66.193  1.00268.79           O  
ANISOU 4643  O   ASN B 356    41232  21404  39489   6776   4062    674       O  
ATOM   4644  CB  ASN B 356      38.716  92.441  67.267  1.00255.67           C  
ANISOU 4644  CB  ASN B 356    39149  19555  38435   5543   4881    387       C  
ATOM   4645  CG  ASN B 356      39.977  92.865  67.981  1.00253.18           C  
ANISOU 4645  CG  ASN B 356    38595  18939  38663   5042   5226    114       C  
ATOM   4646  OD1 ASN B 356      40.234  94.058  68.203  1.00254.59           O  
ANISOU 4646  OD1 ASN B 356    38828  18471  39431   5011   5418     11       O  
ATOM   4647  ND2 ASN B 356      40.783  91.871  68.346  1.00245.63           N  
ANISOU 4647  ND2 ASN B 356    37358  18441  37526   4648   5295    -18       N  
ATOM   4648  N   SER B 357      37.278  93.051  64.699  1.00265.73           N  
ANISOU 4648  N   SER B 357    41544  20273  39147   6555   4719   1489       N  
ATOM   4649  CA  SER B 357      36.643  92.281  63.628  1.00261.23           C  
ANISOU 4649  CA  SER B 357    41300  20030  37923   6922   4485   1900       C  
ATOM   4650  C   SER B 357      36.832  90.772  63.890  1.00255.76           C  
ANISOU 4650  C   SER B 357    40270  20137  36770   6663   4341   1741       C  
ATOM   4651  O   SER B 357      37.846  90.331  64.445  1.00253.94           O  
ANISOU 4651  O   SER B 357    39760  20062  36661   6175   4580   1562       O  
ATOM   4652  CB  SER B 357      37.175  92.663  62.224  1.00262.77           C  
ANISOU 4652  CB  SER B 357    42171  19695  37972   7079   4815   2601       C  
ATOM   4653  OG  SER B 357      36.305  93.556  61.554  1.00265.22           O  
ANISOU 4653  OG  SER B 357    42911  19560  38299   7620   4666   2881       O  
ATOM   4654  N   PHE B 358      35.832  89.994  63.487  1.00256.76           N  
ANISOU 4654  N   PHE B 358    40415  20752  36391   7007   3933   1797       N  
ATOM   4655  CA  PHE B 358      35.802  88.554  63.691  1.00253.27           C  
ANISOU 4655  CA  PHE B 358    39660  21061  35508   6832   3737   1651       C  
ATOM   4656  C   PHE B 358      35.933  88.229  65.203  1.00248.47           C  
ANISOU 4656  C   PHE B 358    38404  20845  35158   6446   3683   1035       C  
ATOM   4657  O   PHE B 358      36.397  87.171  65.632  1.00241.88           O  
ANISOU 4657  O   PHE B 358    37264  20516  34121   6116   3684    877       O  
ATOM   4658  CB  PHE B 358      36.868  87.900  62.802  1.00253.28           C  
ANISOU 4658  CB  PHE B 358    39960  21073  35199   6618   4042   2080       C  
ATOM   4659  CG  PHE B 358      37.001  88.548  61.430  1.00260.29           C  
ANISOU 4659  CG  PHE B 358    41535  21410  35954   6942   4242   2692       C  
ATOM   4660  CD1 PHE B 358      35.974  88.465  60.489  1.00262.70           C  
ANISOU 4660  CD1 PHE B 358    42199  21775  35838   7497   3904   2972       C  
ATOM   4661  CD2 PHE B 358      38.144  89.267  61.087  1.00265.43           C  
ANISOU 4661  CD2 PHE B 358    42472  21465  36911   6704   4771   2984       C  
ATOM   4662  CE1 PHE B 358      36.120  89.022  59.226  1.00269.11           C  
ANISOU 4662  CE1 PHE B 358    43677  22105  36468   7814   4089   3553       C  
ATOM   4663  CE2 PHE B 358      38.282  89.864  59.842  1.00271.69           C  
ANISOU 4663  CE2 PHE B 358    43918  21744  37568   7001   4998   3575       C  
ATOM   4664  CZ  PHE B 358      37.277  89.729  58.905  1.00273.26           C  
ANISOU 4664  CZ  PHE B 358    44505  22040  37280   7564   4655   3870       C  
ATOM   4665  N   GLN B 359      35.399  89.139  65.996  1.00248.36           N  
ANISOU 4665  N   GLN B 359    38194  20611  35559   6548   3597    684       N  
ATOM   4666  CA  GLN B 359      35.518  89.027  67.451  1.00243.26           C  
ANISOU 4666  CA  GLN B 359    36984  20264  35178   6227   3569     92       C  
ATOM   4667  C   GLN B 359      34.759  87.827  67.981  1.00237.99           C  
ANISOU 4667  C   GLN B 359    35917  20382  34127   6245   3222   -179       C  
ATOM   4668  O   GLN B 359      35.273  87.160  68.847  1.00234.39           O  
ANISOU 4668  O   GLN B 359    35086  20321  33651   5872   3272   -477       O  
ATOM   4669  CB  GLN B 359      35.017  90.285  68.122  1.00245.23           C  
ANISOU 4669  CB  GLN B 359    37137  20105  35932   6389   3536   -228       C  
ATOM   4670  CG  GLN B 359      35.054  90.287  69.644  1.00243.16           C  
ANISOU 4670  CG  GLN B 359    36322  20134  35933   6119   3492   -870       C  
ATOM   4671  CD  GLN B 359      34.200  91.374  70.226  1.00248.30           C  
ANISOU 4671  CD  GLN B 359    36869  20503  36971   6403   3354  -1205       C  
ATOM   4672  OE1 GLN B 359      33.628  92.199  69.503  1.00254.46           O  
ANISOU 4672  OE1 GLN B 359    37991  20813  37877   6792   3300   -953       O  
ATOM   4673  NE2 GLN B 359      34.113  91.394  71.532  1.00247.88           N  
ANISOU 4673  NE2 GLN B 359    36355  20725  37100   6230   3296  -1774       N  
ATOM   4674  N   GLY B 360      33.556  87.554  67.469  1.00238.52           N  
ANISOU 4674  N   GLY B 360    36056  20660  33909   6676   2874    -78       N  
ATOM   4675  CA  GLY B 360      32.767  86.448  67.938  1.00237.20           C  
ANISOU 4675  CA  GLY B 360    35498  21196  33431   6704   2556   -328       C  
ATOM   4676  C   GLY B 360      32.900  85.183  67.109  1.00238.70           C  
ANISOU 4676  C   GLY B 360    35806  21780  33109   6680   2462    -11       C  
ATOM   4677  O   GLY B 360      32.141  84.220  67.296  1.00240.24           O  
ANISOU 4677  O   GLY B 360    35720  22526  33032   6756   2170   -156       O  
ATOM   4678  N   GLU B 361      33.882  85.151  66.229  1.00242.33           N  
ANISOU 4678  N   GLU B 361    36658  21965  33452   6558   2723    400       N  
ATOM   4679  CA  GLU B 361      34.156  83.974  65.420  1.00240.41           C  
ANISOU 4679  CA  GLU B 361    36550  22063  32729   6514   2673    696       C  
ATOM   4680  C   GLU B 361      35.596  83.480  65.606  1.00236.70           C  
ANISOU 4680  C   GLU B 361    36032  21639  32265   6006   3030    748       C  
ATOM   4681  O   GLU B 361      36.078  82.599  64.921  1.00229.99           O  
ANISOU 4681  O   GLU B 361    35327  20991  31067   5917   3076   1010       O  
ATOM   4682  CB  GLU B 361      33.850  84.329  63.961  1.00245.56           C  
ANISOU 4682  CB  GLU B 361    37787  22371  33142   6950   2614   1196       C  
ATOM   4683  CG  GLU B 361      32.371  84.685  63.673  1.00248.81           C  
ANISOU 4683  CG  GLU B 361    38246  22787  33504   7500   2192   1151       C  
ATOM   4684  CD  GLU B 361      32.005  86.161  63.832  1.00253.61           C  
ANISOU 4684  CD  GLU B 361    39007  22813  34540   7747   2242   1109       C  
ATOM   4685  OE1 GLU B 361      31.167  86.472  64.706  1.00247.12           O  
ANISOU 4685  OE1 GLU B 361    37814  22110  33969   7848   2037    700       O  
ATOM   4686  OE2 GLU B 361      32.538  87.024  63.086  1.00263.20           O  
ANISOU 4686  OE2 GLU B 361    40711  23438  35852   7849   2498   1486       O  
ATOM   4687  N   THR B 362      36.311  84.089  66.551  1.00239.46           N  
ANISOU 4687  N   THR B 362    36166  21779  33037   5676   3282    473       N  
ATOM   4688  CA  THR B 362      37.686  83.765  66.878  1.00239.51           C  
ANISOU 4688  CA  THR B 362    36065  21788  33148   5189   3609    445       C  
ATOM   4689  C   THR B 362      37.777  82.623  67.896  1.00233.98           C  
ANISOU 4689  C   THR B 362    34859  21741  32298   4887   3468     79       C  
ATOM   4690  O   THR B 362      37.186  82.695  68.988  1.00230.44           O  
ANISOU 4690  O   THR B 362    34033  21537  31984   4877   3296   -344       O  
ATOM   4691  CB  THR B 362      38.418  84.991  67.452  1.00242.82           C  
ANISOU 4691  CB  THR B 362    36466  21655  34137   4982   3919    278       C  
ATOM   4692  OG1 THR B 362      38.060  86.171  66.728  1.00243.50           O  
ANISOU 4692  OG1 THR B 362    36966  21129  34424   5315   3996    545       O  
ATOM   4693  CG2 THR B 362      39.918  84.788  67.346  1.00243.93           C  
ANISOU 4693  CG2 THR B 362    36636  21647  34398   4546   4302    396       C  
ATOM   4694  N   TRP B 363      38.518  81.575  67.536  1.00230.28           N  
ANISOU 4694  N   TRP B 363    34398  21550  31547   4653   3552    251       N  
ATOM   4695  CA  TRP B 363      38.713  80.425  68.402  1.00224.04           C  
ANISOU 4695  CA  TRP B 363    33177  21352  30596   4362   3439    -31       C  
ATOM   4696  C   TRP B 363      40.165  80.338  68.843  1.00227.65           C  
ANISOU 4696  C   TRP B 363    33513  21723  31258   3902   3752   -117       C  
ATOM   4697  O   TRP B 363      41.053  80.743  68.108  1.00232.67           O  
ANISOU 4697  O   TRP B 363    34445  21945  32014   3807   4055    168       O  
ATOM   4698  CB  TRP B 363      38.250  79.140  67.702  1.00214.97           C  
ANISOU 4698  CB  TRP B 363    32071  20657  28950   4492   3206    182       C  
ATOM   4699  CG  TRP B 363      36.767  79.143  67.336  1.00211.55           C  
ANISOU 4699  CG  TRP B 363    31686  20354  28339   4945   2848    206       C  
ATOM   4700  CD1 TRP B 363      36.169  79.826  66.308  1.00215.94           C  
ANISOU 4700  CD1 TRP B 363    32647  20554  28843   5356   2774    496       C  
ATOM   4701  CD2 TRP B 363      35.717  78.432  67.998  1.00204.82           C  
ANISOU 4701  CD2 TRP B 363    30451  20011  27357   5035   2521    -73       C  
ATOM   4702  NE1 TRP B 363      34.816  79.586  66.294  1.00218.01           N  
ANISOU 4702  NE1 TRP B 363    32784  21080  28968   5700   2393    387       N  
ATOM   4703  CE2 TRP B 363      34.515  78.732  67.322  1.00211.63           C  
ANISOU 4703  CE2 TRP B 363    31482  20800  28127   5498   2249     37       C  
ATOM   4704  CE3 TRP B 363      35.671  77.582  69.103  1.00195.97           C  
ANISOU 4704  CE3 TRP B 363    28866  19394  26198   4777   2439   -400       C  
ATOM   4705  CZ2 TRP B 363      33.291  78.200  67.715  1.00209.48           C  
ANISOU 4705  CZ2 TRP B 363    30890  20936  27764   5686   1912   -187       C  
ATOM   4706  CZ3 TRP B 363      34.459  77.056  69.488  1.00195.05           C  
ANISOU 4706  CZ3 TRP B 363    28462  19675  25970   4960   2136   -591       C  
ATOM   4707  CH2 TRP B 363      33.284  77.368  68.800  1.00201.65           C  
ANISOU 4707  CH2 TRP B 363    29437  20423  26757   5402   1880   -494       C  
ATOM   4708  N   ARG B 364      40.395  79.810  70.046  1.00227.31           N  
ANISOU 4708  N   ARG B 364    33034  22074  31259   3627   3680   -511       N  
ATOM   4709  CA  ARG B 364      41.728  79.591  70.564  1.00226.26           C  
ANISOU 4709  CA  ARG B 364    32728  21940  31300   3200   3908   -648       C  
ATOM   4710  C   ARG B 364      42.000  78.086  70.703  1.00220.17           C  
ANISOU 4710  C   ARG B 364    31751  21747  30156   3014   3789   -642       C  
ATOM   4711  O   ARG B 364      41.120  77.322  71.121  1.00216.15           O  
ANISOU 4711  O   ARG B 364    31033  21718  29377   3123   3506   -768       O  
ATOM   4712  CB  ARG B 364      41.919  80.246  71.939  1.00227.55           C  
ANISOU 4712  CB  ARG B 364    32554  22070  31834   3025   3918  -1149       C  
ATOM   4713  CG  ARG B 364      43.345  80.122  72.485  1.00226.26           C  
ANISOU 4713  CG  ARG B 364    32202  21862  31903   2597   4132  -1327       C  
ATOM   4714  CD  ARG B 364      43.591  80.915  73.749  1.00229.51           C  
ANISOU 4714  CD  ARG B 364    32328  22165  32711   2453   4139  -1831       C  
ATOM   4715  NE  ARG B 364      42.847  80.399  74.899  1.00231.49           N  
ANISOU 4715  NE  ARG B 364    32240  22964  32749   2500   3857  -2206       N  
ATOM   4716  CZ  ARG B 364      41.620  80.788  75.290  1.00242.21           C  
ANISOU 4716  CZ  ARG B 364    33544  24419  34065   2790   3669  -2371       C  
ATOM   4717  NH1 ARG B 364      40.902  81.728  74.626  1.00249.83           N  
ANISOU 4717  NH1 ARG B 364    34772  24966  35187   3095   3685  -2206       N  
ATOM   4718  NH2 ARG B 364      41.087  80.221  76.371  1.00244.55           N  
ANISOU 4718  NH2 ARG B 364    33517  25241  34158   2788   3467  -2703       N  
ATOM   4719  N   LEU B 365      43.218  77.675  70.356  1.00218.88           N  
ANISOU 4719  N   LEU B 365    31636  21518  30008   2733   4016   -497       N  
ATOM   4720  CA  LEU B 365      43.636  76.299  70.572  1.00214.50           C  
ANISOU 4720  CA  LEU B 365    30868  21467  29163   2523   3923   -522       C  
ATOM   4721  C   LEU B 365      43.665  75.977  72.065  1.00207.04           C  
ANISOU 4721  C   LEU B 365    29477  20903  28285   2323   3776   -984       C  
ATOM   4722  O   LEU B 365      43.928  76.829  72.907  1.00204.26           O  
ANISOU 4722  O   LEU B 365    28977  20357  28274   2222   3845  -1298       O  
ATOM   4723  CB  LEU B 365      45.005  76.053  69.979  1.00219.00           C  
ANISOU 4723  CB  LEU B 365    31554  21849  29806   2257   4220   -319       C  
ATOM   4724  CG  LEU B 365      44.963  75.940  68.461  1.00222.94           C  
ANISOU 4724  CG  LEU B 365    32492  22143  30070   2460   4340    172       C  
ATOM   4725  CD1 LEU B 365      46.312  76.268  67.850  1.00225.49           C  
ANISOU 4725  CD1 LEU B 365    32991  22064  30620   2229   4753    374       C  
ATOM   4726  CD2 LEU B 365      44.511  74.548  68.039  1.00218.44           C  
ANISOU 4726  CD2 LEU B 365    31905  22080  29012   2555   4094    310       C  
ATOM   4727  N   SER B 366      43.424  74.704  72.383  1.00201.60           N  
ANISOU 4727  N   SER B 366    28583  20758  27259   2270   3572  -1021       N  
ATOM   4728  CA  SER B 366      43.568  74.168  73.729  1.00201.11           C  
ANISOU 4728  CA  SER B 366    28129  21109  27172   2070   3447  -1394       C  
ATOM   4729  C   SER B 366      44.289  72.840  73.713  1.00199.72           C  
ANISOU 4729  C   SER B 366    27832  21291  26761   1843   3420  -1312       C  
ATOM   4730  O   SER B 366      44.056  72.012  72.849  1.00195.91           O  
ANISOU 4730  O   SER B 366    27483  20952  25999   1930   3356  -1017       O  
ATOM   4731  CB  SER B 366      42.234  73.960  74.417  1.00201.50           C  
ANISOU 4731  CB  SER B 366    27992  21520  27046   2279   3190  -1578       C  
ATOM   4732  OG  SER B 366      42.430  73.294  75.657  1.00202.49           O  
ANISOU 4732  OG  SER B 366    27777  22080  27079   2087   3093  -1883       O  
ATOM   4733  N   PHE B 367      45.124  72.614  74.715  1.00201.19           N  
ANISOU 4733  N   PHE B 367    27751  21637  27053   1571   3438  -1598       N  
ATOM   4734  CA  PHE B 367      45.871  71.355  74.841  1.00196.63           C  
ANISOU 4734  CA  PHE B 367    27028  21402  26280   1349   3396  -1558       C  
ATOM   4735  C   PHE B 367      45.798  70.815  76.257  1.00194.55           C  
ANISOU 4735  C   PHE B 367    26424  21584  25911   1238   3217  -1902       C  
ATOM   4736  O   PHE B 367      46.767  70.234  76.751  1.00191.99           O  
ANISOU 4736  O   PHE B 367    25933  21422  25592    999   3219  -2020       O  
ATOM   4737  CB  PHE B 367      47.327  71.554  74.448  1.00198.94           C  
ANISOU 4737  CB  PHE B 367    27375  21384  26829   1096   3645  -1506       C  
ATOM   4738  CG  PHE B 367      47.475  72.078  73.074  1.00205.27           C  
ANISOU 4738  CG  PHE B 367    28533  21746  27715   1198   3870  -1145       C  
ATOM   4739  CD1 PHE B 367      47.301  71.230  71.986  1.00208.30           C  
ANISOU 4739  CD1 PHE B 367    29118  22242  27784   1302   3855   -782       C  
ATOM   4740  CD2 PHE B 367      47.709  73.429  72.857  1.00210.98           C  
ANISOU 4740  CD2 PHE B 367    29409  21938  28815   1219   4091  -1163       C  
ATOM   4741  CE1 PHE B 367      47.401  71.720  70.694  1.00214.62           C  
ANISOU 4741  CE1 PHE B 367    30289  22651  28605   1433   4066   -433       C  
ATOM   4742  CE2 PHE B 367      47.808  73.923  71.571  1.00213.89           C  
ANISOU 4742  CE2 PHE B 367    30144  21891  29231   1337   4320   -790       C  
ATOM   4743  CZ  PHE B 367      47.652  73.072  70.494  1.00215.18           C  
ANISOU 4743  CZ  PHE B 367    30527  22192  29037   1453   4308   -422       C  
ATOM   4744  N   SER B 368      44.639  70.924  76.885  1.00194.35           N  
ANISOU 4744  N   SER B 368    26298  21780  25764   1425   3059  -2048       N  
ATOM   4745  CA  SER B 368      44.497  70.526  78.287  1.00193.71           C  
ANISOU 4745  CA  SER B 368    25921  22114  25563   1351   2920  -2377       C  
ATOM   4746  C   SER B 368      44.602  69.007  78.434  1.00191.02           C  
ANISOU 4746  C   SER B 368    25453  22233  24893   1245   2793  -2250       C  
ATOM   4747  O   SER B 368      45.055  68.499  79.469  1.00191.78           O  
ANISOU 4747  O   SER B 368    25338  22630  24897   1096   2721  -2465       O  
ATOM   4748  CB  SER B 368      43.196  71.087  78.809  1.00195.91           C  
ANISOU 4748  CB  SER B 368    26144  22478  25814   1594   2831  -2540       C  
ATOM   4749  OG  SER B 368      43.075  72.446  78.441  1.00204.40           O  
ANISOU 4749  OG  SER B 368    27382  23075  27204   1717   2945  -2592       O  
ATOM   4750  N   HIS B 369      44.194  68.287  77.393  1.00189.65           N  
ANISOU 4750  N   HIS B 369    25415  22101  24542   1334   2755  -1906       N  
ATOM   4751  CA  HIS B 369      44.333  66.829  77.356  1.00184.51           C  
ANISOU 4751  CA  HIS B 369    24664  21822  23618   1234   2643  -1754       C  
ATOM   4752  C   HIS B 369      45.802  66.370  77.425  1.00179.86           C  
ANISOU 4752  C   HIS B 369    24027  21216  23092    962   2717  -1771       C  
ATOM   4753  O   HIS B 369      46.175  65.491  78.210  1.00180.34           O  
ANISOU 4753  O   HIS B 369    23895  21614  23009    823   2618  -1870       O  
ATOM   4754  CB  HIS B 369      43.667  66.258  76.104  1.00184.14           C  
ANISOU 4754  CB  HIS B 369    24793  21760  23413   1397   2584  -1408       C  
ATOM   4755  CG  HIS B 369      44.268  66.719  74.815  1.00181.24           C  
ANISOU 4755  CG  HIS B 369    24718  20981  23161   1418   2739  -1170       C  
ATOM   4756  ND1 HIS B 369      44.253  68.037  74.408  1.00181.82           N  
ANISOU 4756  ND1 HIS B 369    24988  20625  23470   1527   2886  -1172       N  
ATOM   4757  CD2 HIS B 369      44.881  66.026  73.826  1.00176.45           C  
ANISOU 4757  CD2 HIS B 369    24255  20328  22458   1358   2786   -911       C  
ATOM   4758  CE1 HIS B 369      44.838  68.129  73.224  1.00179.98           C  
ANISOU 4758  CE1 HIS B 369    25018  20099  23266   1530   3034   -901       C  
ATOM   4759  NE2 HIS B 369      45.224  66.923  72.850  1.00178.45           N  
ANISOU 4759  NE2 HIS B 369    24797  20142  22864   1433   2977   -749       N  
ATOM   4760  N   THR B 370      46.620  66.994  76.603  1.00176.41           N  
ANISOU 4760  N   THR B 370    23769  20375  22884    898   2901  -1671       N  
ATOM   4761  CA  THR B 370      48.029  66.691  76.521  1.00173.07           C  
ANISOU 4761  CA  THR B 370    23300  19869  22589    650   3006  -1686       C  
ATOM   4762  C   THR B 370      48.749  67.083  77.811  1.00167.53           C  
ANISOU 4762  C   THR B 370    22363  19224  22065    481   2983  -2080       C  
ATOM   4763  O   THR B 370      49.638  66.364  78.274  1.00155.81           O  
ANISOU 4763  O   THR B 370    20716  17929  20553    297   2928  -2173       O  
ATOM   4764  CB  THR B 370      48.551  67.470  75.315  1.00176.49           C  
ANISOU 4764  CB  THR B 370    23996  19808  23255    656   3255  -1481       C  
ATOM   4765  OG1 THR B 370      47.781  67.084  74.171  1.00172.50           O  
ANISOU 4765  OG1 THR B 370    23725  19295  22522    860   3231  -1136       O  
ATOM   4766  CG2 THR B 370      50.004  67.192  75.062  1.00178.61           C  
ANISOU 4766  CG2 THR B 370    24219  19949  23695    406   3411  -1469       C  
ATOM   4767  N   GLU B 371      48.373  68.224  78.375  1.00171.25           N  
ANISOU 4767  N   GLU B 371    22818  19524  22722    561   3010  -2324       N  
ATOM   4768  CA  GLU B 371      48.970  68.699  79.617  1.00175.60           C  
ANISOU 4768  CA  GLU B 371    23157  20122  23440    438   2963  -2744       C  
ATOM   4769  C   GLU B 371      48.619  67.750  80.767  1.00172.38           C  
ANISOU 4769  C   GLU B 371    22544  20261  22690    445   2738  -2896       C  
ATOM   4770  O   GLU B 371      49.436  67.489  81.651  1.00174.36           O  
ANISOU 4770  O   GLU B 371    22617  20681  22951    300   2652  -3147       O  
ATOM   4771  CB  GLU B 371      48.466  70.095  79.933  1.00182.96           C  
ANISOU 4771  CB  GLU B 371    24131  20765  24620    562   3024  -2971       C  
ATOM   4772  CG  GLU B 371      48.969  71.159  78.969  1.00188.64           C  
ANISOU 4772  CG  GLU B 371    25042  20893  25738    530   3269  -2861       C  
ATOM   4773  CD  GLU B 371      48.122  72.425  78.978  1.00196.63           C  
ANISOU 4773  CD  GLU B 371    26166  21603  26938    729   3321  -2959       C  
ATOM   4774  OE1 GLU B 371      47.414  72.660  79.987  1.00202.70           O  
ANISOU 4774  OE1 GLU B 371    26801  22599  27616    842   3176  -3247       O  
ATOM   4775  OE2 GLU B 371      48.156  73.199  77.993  1.00203.38           O  
ANISOU 4775  OE2 GLU B 371    27252  21992  28029    785   3515  -2748       O  
ATOM   4776  N   LYS B 372      47.390  67.250  80.742  1.00169.72           N  
ANISOU 4776  N   LYS B 372    22236  20189  22060    623   2648  -2738       N  
ATOM   4777  CA  LYS B 372      46.960  66.243  81.698  1.00167.41           C  
ANISOU 4777  CA  LYS B 372    21775  20405  21427    636   2478  -2797       C  
ATOM   4778  C   LYS B 372      47.834  65.010  81.586  1.00161.84           C  
ANISOU 4778  C   LYS B 372    21007  19895  20589    462   2413  -2652       C  
ATOM   4779  O   LYS B 372      48.357  64.516  82.595  1.00155.23           O  
ANISOU 4779  O   LYS B 372    20011  19336  19631    368   2300  -2841       O  
ATOM   4780  CB  LYS B 372      45.492  65.878  81.486  1.00168.59           C  
ANISOU 4780  CB  LYS B 372    21956  20751  21349    843   2426  -2610       C  
ATOM   4781  CG  LYS B 372      44.890  65.046  82.608  1.00167.21           C  
ANISOU 4781  CG  LYS B 372    21600  21071  20858    874   2303  -2696       C  
ATOM   4782  CD  LYS B 372      43.430  64.705  82.341  1.00165.80           C  
ANISOU 4782  CD  LYS B 372    21416  21053  20525   1064   2274  -2519       C  
ATOM   4783  CE  LYS B 372      42.834  63.919  83.510  1.00167.52           C  
ANISOU 4783  CE  LYS B 372    21449  21747  20452   1084   2206  -2597       C  
ATOM   4784  NZ  LYS B 372      41.347  63.756  83.396  1.00171.44           N  
ANISOU 4784  NZ  LYS B 372    21889  22384  20865   1271   2205  -2492       N  
ATOM   4785  N   TYR B 373      48.018  64.529  80.360  1.00162.41           N  
ANISOU 4785  N   TYR B 373    21213  19817  20678    435   2477  -2327       N  
ATOM   4786  CA  TYR B 373      48.870  63.359  80.134  1.00164.44           C  
ANISOU 4786  CA  TYR B 373    21416  20224  20838    279   2425  -2184       C  
ATOM   4787  C   TYR B 373      50.283  63.594  80.651  1.00163.48           C  
ANISOU 4787  C   TYR B 373    21173  20008  20931     79   2443  -2434       C  
ATOM   4788  O   TYR B 373      50.881  62.710  81.274  1.00165.21           O  
ANISOU 4788  O   TYR B 373    21248  20501  21022    -25   2311  -2499       O  
ATOM   4789  CB  TYR B 373      48.988  63.033  78.635  1.00168.51           C  
ANISOU 4789  CB  TYR B 373    22120  20518  21387    289   2528  -1837       C  
ATOM   4790  CG  TYR B 373      49.921  61.867  78.362  1.00169.53           C  
ANISOU 4790  CG  TYR B 373    22189  20776  21448    132   2487  -1713       C  
ATOM   4791  CD1 TYR B 373      51.300  62.049  78.179  1.00171.81           C  
ANISOU 4791  CD1 TYR B 373    22442  20855  21981    -52   2597  -1797       C  
ATOM   4792  CD2 TYR B 373      49.427  60.571  78.343  1.00169.83           C  
ANISOU 4792  CD2 TYR B 373    22180  21142  21206    164   2336  -1531       C  
ATOM   4793  CE1 TYR B 373      52.149  60.963  77.970  1.00172.85           C  
ANISOU 4793  CE1 TYR B 373    22497  21115  22060   -183   2551  -1704       C  
ATOM   4794  CE2 TYR B 373      50.259  59.482  78.131  1.00172.00           C  
ANISOU 4794  CE2 TYR B 373    22394  21531  21427     33   2284  -1429       C  
ATOM   4795  CZ  TYR B 373      51.612  59.672  77.946  1.00174.64           C  
ANISOU 4795  CZ  TYR B 373    22698  21671  21986   -131   2386  -1517       C  
ATOM   4796  OH  TYR B 373      52.381  58.547  77.737  1.00177.34           O  
ANISOU 4796  OH  TYR B 373    22966  22138  22274   -242   2323  -1422       O  
ATOM   4797  N   ILE B 374      50.836  64.770  80.370  1.00164.00           N  
ANISOU 4797  N   ILE B 374    21292  19670  21348     29   2601  -2573       N  
ATOM   4798  CA  ILE B 374      52.201  65.090  80.794  1.00170.79           C  
ANISOU 4798  CA  ILE B 374    22009  20388  22495   -168   2627  -2842       C  
ATOM   4799  C   ILE B 374      52.325  65.133  82.304  1.00170.33           C  
ANISOU 4799  C   ILE B 374    21749  20619  22349   -176   2430  -3229       C  
ATOM   4800  O   ILE B 374      53.263  64.591  82.865  1.00163.31           O  
ANISOU 4800  O   ILE B 374    20701  19887  21463   -304   2311  -3384       O  
ATOM   4801  CB  ILE B 374      52.664  66.454  80.285  1.00178.70           C  
ANISOU 4801  CB  ILE B 374    23089  20867  23940   -219   2851  -2941       C  
ATOM   4802  CG1 ILE B 374      52.767  66.461  78.766  1.00180.96           C  
ANISOU 4802  CG1 ILE B 374    23600  20836  24320   -219   3081  -2557       C  
ATOM   4803  CG2 ILE B 374      54.036  66.805  80.859  1.00183.50           C  
ANISOU 4803  CG2 ILE B 374    23491  21338  24892   -429   2855  -3282       C  
ATOM   4804  CD1 ILE B 374      52.605  67.839  78.171  1.00183.25           C  
ANISOU 4804  CD1 ILE B 374    24063  20630  24932   -163   3310  -2539       C  
ATOM   4805  N   LEU B 375      51.379  65.784  82.962  1.00178.04           N  
ANISOU 4805  N   LEU B 375    22737  21670  23238    -21   2390  -3395       N  
ATOM   4806  CA  LEU B 375      51.372  65.837  84.420  1.00183.44           C  
ANISOU 4806  CA  LEU B 375    23262  22664  23771     12   2208  -3764       C  
ATOM   4807  C   LEU B 375      51.296  64.436  85.009  1.00181.65           C  
ANISOU 4807  C   LEU B 375    22957  22927  23131     15   2029  -3650       C  
ATOM   4808  O   LEU B 375      51.918  64.162  86.042  1.00188.06           O  
ANISOU 4808  O   LEU B 375    23633  23975  23844    -27   1864  -3911       O  
ATOM   4809  CB  LEU B 375      50.182  66.656  84.904  1.00184.14           C  
ANISOU 4809  CB  LEU B 375    23398  22781  23786    209   2224  -3905       C  
ATOM   4810  CG  LEU B 375      50.485  68.129  85.190  1.00184.07           C  
ANISOU 4810  CG  LEU B 375    23368  22408  24161    208   2292  -4274       C  
ATOM   4811  CD1 LEU B 375      51.238  68.242  86.511  1.00185.50           C  
ANISOU 4811  CD1 LEU B 375    23362  22785  24331    153   2112  -4735       C  
ATOM   4812  CD2 LEU B 375      51.275  68.815  84.086  1.00183.29           C  
ANISOU 4812  CD2 LEU B 375    23349  21768  24525     72   2489  -4177       C  
ATOM   4813  N   ASN B 376      50.562  63.542  84.351  1.00174.28           N  
ANISOU 4813  N   ASN B 376    22113  22135  21970     72   2050  -3267       N  
ATOM   4814  CA  ASN B 376      50.452  62.180  84.870  1.00170.72           C  
ANISOU 4814  CA  ASN B 376    21592  22115  21158     69   1898  -3128       C  
ATOM   4815  C   ASN B 376      51.485  61.212  84.332  1.00167.40           C  
ANISOU 4815  C   ASN B 376    21138  21686  20779    -86   1855  -2957       C  
ATOM   4816  O   ASN B 376      51.617  60.094  84.839  1.00171.30           O  
ANISOU 4816  O   ASN B 376    21563  22506  21016   -104   1711  -2875       O  
ATOM   4817  CB  ASN B 376      49.047  61.675  84.672  1.00169.86           C  
ANISOU 4817  CB  ASN B 376    21547  22203  20788    217   1919  -2863       C  
ATOM   4818  CG  ASN B 376      48.048  62.594  85.324  1.00173.15           C  
ANISOU 4818  CG  ASN B 376    21965  22662  21162    380   1959  -3066       C  
ATOM   4819  OD1 ASN B 376      48.141  62.864  86.538  1.00175.73           O  
ANISOU 4819  OD1 ASN B 376    22205  23195  21366    417   1883  -3369       O  
ATOM   4820  ND2 ASN B 376      47.135  63.141  84.529  1.00173.78           N  
ANISOU 4820  ND2 ASN B 376    22146  22535  21347    496   2070  -2928       N  
ATOM   4821  N   ASN B 377      52.246  61.646  83.332  1.00164.56           N  
ANISOU 4821  N   ASN B 377    20827  20948  20750   -195   1991  -2906       N  
ATOM   4822  CA  ASN B 377      53.354  60.853  82.801  1.00163.17           C  
ANISOU 4822  CA  ASN B 377    20600  20727  20670   -349   1977  -2792       C  
ATOM   4823  C   ASN B 377      54.579  61.731  82.619  1.00166.10           C  
ANISOU 4823  C   ASN B 377    20898  20742  21470   -498   2081  -3033       C  
ATOM   4824  O   ASN B 377      54.974  62.014  81.500  1.00167.32           O  
ANISOU 4824  O   ASN B 377    21139  20561  21871   -570   2281  -2874       O  
ATOM   4825  CB  ASN B 377      52.967  60.211  81.457  1.00161.80           C  
ANISOU 4825  CB  ASN B 377    20575  20457  20441   -329   2086  -2382       C  
ATOM   4826  CG  ASN B 377      51.755  59.296  81.568  1.00162.45           C  
ANISOU 4826  CG  ASN B 377    20698  20863  20162   -197   1981  -2150       C  
ATOM   4827  OD1 ASN B 377      51.874  58.083  81.445  1.00169.24           O  
ANISOU 4827  OD1 ASN B 377    21523  21923  20856   -231   1883  -1966       O  
ATOM   4828  ND2 ASN B 377      50.582  59.871  81.795  1.00158.02           N  
ANISOU 4828  ND2 ASN B 377    20194  20337  19509    -48   2006  -2167       N  
ATOM   4829  N   HIS B 378      55.193  62.132  83.725  1.00167.36           N  
ANISOU 4829  N   HIS B 378    20894  20978  21718   -541   1945  -3422       N  
ATOM   4830  CA  HIS B 378      56.143  63.244  83.774  1.00166.01           C  
ANISOU 4830  CA  HIS B 378    20623  20449  22005   -661   2032  -3746       C  
ATOM   4831  C   HIS B 378      57.612  62.886  83.917  1.00162.58           C  
ANISOU 4831  C   HIS B 378    19983  19972  21816   -838   1953  -3929       C  
ATOM   4832  O   HIS B 378      58.476  63.772  83.961  1.00165.70           O  
ANISOU 4832  O   HIS B 378    20254  20056  22649   -960   2025  -4221       O  
ATOM   4833  CB  HIS B 378      55.682  64.167  84.900  1.00170.31           C  
ANISOU 4833  CB  HIS B 378    21121  21061  22526   -557   1930  -4119       C  
ATOM   4834  CG  HIS B 378      55.741  63.527  86.245  1.00172.04           C  
ANISOU 4834  CG  HIS B 378    21220  21737  22407   -489   1640  -4341       C  
ATOM   4835  ND1 HIS B 378      54.662  62.941  86.871  1.00169.75           N  
ANISOU 4835  ND1 HIS B 378    21005  21847  21643   -322   1539  -4222       N  
ATOM   4836  CD2 HIS B 378      56.792  63.339  87.059  1.00177.75           C  
ANISOU 4836  CD2 HIS B 378    21758  22581  23197   -559   1433  -4662       C  
ATOM   4837  CE1 HIS B 378      55.057  62.441  88.025  1.00173.28           C  
ANISOU 4837  CE1 HIS B 378    21344  22638  21855   -288   1298  -4443       C  
ATOM   4838  NE2 HIS B 378      56.345  62.678  88.165  1.00180.69           N  
ANISOU 4838  NE2 HIS B 378    22127  23420  23106   -420   1207  -4723       N  
ATOM   4839  N   GLY B 379      57.936  61.599  83.982  1.00157.81           N  
ANISOU 4839  N   GLY B 379    19325  19658  20977   -857   1804  -3775       N  
ATOM   4840  CA  GLY B 379      59.325  61.205  84.174  1.00161.21           C  
ANISOU 4840  CA  GLY B 379    19540  20072  21639  -1004   1697  -3969       C  
ATOM   4841  C   GLY B 379      60.030  60.797  82.897  1.00166.04           C  
ANISOU 4841  C   GLY B 379    20158  20435  22493  -1141   1908  -3713       C  
ATOM   4842  O   GLY B 379      59.404  60.512  81.876  1.00162.72           O  
ANISOU 4842  O   GLY B 379    19934  19941  21949  -1100   2088  -3335       O  
ATOM   4843  N   ILE B 380      61.358  60.774  82.939  1.00176.69           N  
ANISOU 4843  N   ILE B 380    21283  21653  24196  -1296   1885  -3937       N  
ATOM   4844  CA  ILE B 380      62.119  60.112  81.871  1.00180.35           C  
ANISOU 4844  CA  ILE B 380    21719  21974  24830  -1415   2049  -3708       C  
ATOM   4845  C   ILE B 380      62.015  58.638  82.100  1.00178.72           C  
ANISOU 4845  C   ILE B 380    21508  22163  24232  -1342   1813  -3522       C  
ATOM   4846  O   ILE B 380      61.944  57.876  81.136  1.00181.99           O  
ANISOU 4846  O   ILE B 380    22026  22565  24557  -1347   1933  -3189       O  
ATOM   4847  CB  ILE B 380      63.628  60.427  81.789  1.00186.04           C  
ANISOU 4847  CB  ILE B 380    22162  22434  26089  -1612   2115  -3997       C  
ATOM   4848  CG1 ILE B 380      64.262  60.624  83.171  1.00190.85           C  
ANISOU 4848  CG1 ILE B 380    22506  23205  26803  -1620   1780  -4490       C  
ATOM   4849  CG2 ILE B 380      63.877  61.623  80.893  1.00188.81           C  
ANISOU 4849  CG2 ILE B 380    22560  22275  26902  -1734   2510  -3985       C  
ATOM   4850  CD1 ILE B 380      65.739  60.359  83.166  1.00193.28           C  
ANISOU 4850  CD1 ILE B 380    22501  23406  27529  -1779   1729  -4734       C  
ATOM   4851  N   GLU B 381      61.984  58.253  83.378  1.00175.79           N  
ANISOU 4851  N   GLU B 381    21033  22136  23622  -1260   1478  -3738       N  
ATOM   4852  CA  GLU B 381      61.747  56.875  83.800  1.00171.84           C  
ANISOU 4852  CA  GLU B 381    20550  22030  22708  -1165   1232  -3556       C  
ATOM   4853  C   GLU B 381      60.260  56.647  83.911  1.00164.38           C  
ANISOU 4853  C   GLU B 381    19833  21299  21325  -1010   1233  -3287       C  
ATOM   4854  O   GLU B 381      59.569  57.464  84.500  1.00157.66           O  
ANISOU 4854  O   GLU B 381    19041  20475  20386   -930   1232  -3430       O  
ATOM   4855  CB  GLU B 381      62.402  56.554  85.141  1.00177.80           C  
ANISOU 4855  CB  GLU B 381    21115  23060  23378  -1125    875  -3890       C  
ATOM   4856  CG  GLU B 381      63.918  56.501  85.085  1.00188.16           C  
ANISOU 4856  CG  GLU B 381    22157  24219  25114  -1264    806  -4157       C  
ATOM   4857  CD  GLU B 381      64.559  56.303  86.466  1.00197.72           C  
ANISOU 4857  CD  GLU B 381    23183  25698  26243  -1191    409  -4538       C  
ATOM   4858  OE1 GLU B 381      63.815  56.340  87.478  1.00204.53           O  
ANISOU 4858  OE1 GLU B 381    24151  26849  26710  -1034    222  -4603       O  
ATOM   4859  OE2 GLU B 381      65.806  56.184  86.561  1.00201.54           O  
ANISOU 4859  OE2 GLU B 381    23412  26097  27065  -1281    286  -4797       O  
ATOM   4860  N   LYS B 382      59.787  55.505  83.432  1.00161.43           N  
ANISOU 4860  N   LYS B 382    19560  21087  20689   -963   1215  -2930       N  
ATOM   4861  CA  LYS B 382      58.357  55.214  83.406  1.00158.45           C  
ANISOU 4861  CA  LYS B 382    19369  20884  19948   -829   1236  -2657       C  
ATOM   4862  C   LYS B 382      57.813  54.952  84.824  1.00155.02           C  
ANISOU 4862  C   LYS B 382    18917  20825  19155   -707   1003  -2769       C  
ATOM   4863  O   LYS B 382      56.606  54.971  85.072  1.00153.37           O  
ANISOU 4863  O   LYS B 382    18826  20767  18678   -594   1032  -2634       O  
ATOM   4864  CB  LYS B 382      58.121  54.027  82.461  1.00155.43           C  
ANISOU 4864  CB  LYS B 382    19069  20541  19446   -828   1270  -2279       C  
ATOM   4865  CG  LYS B 382      58.586  54.277  81.014  1.00155.39           C  
ANISOU 4865  CG  LYS B 382    19122  20187  19732   -917   1523  -2150       C  
ATOM   4866  CD  LYS B 382      59.005  52.998  80.275  1.00154.70           C  
ANISOU 4866  CD  LYS B 382    19024  20143  19610   -948   1492  -1919       C  
ATOM   4867  CE  LYS B 382      59.454  53.226  78.814  1.00153.13           C  
ANISOU 4867  CE  LYS B 382    18909  19619  19651  -1013   1768  -1785       C  
ATOM   4868  NZ  LYS B 382      59.569  51.980  77.974  1.00146.79           N  
ANISOU 4868  NZ  LYS B 382    18145  18871  18754  -1000   1749  -1535       N  
ATOM   4869  N   THR B 383      58.707  54.714  85.768  1.00153.72           N  
ANISOU 4869  N   THR B 383    18604  20816  18984   -718    774  -3023       N  
ATOM   4870  CA  THR B 383      58.283  54.369  87.119  1.00157.23           C  
ANISOU 4870  CA  THR B 383    19060  21637  19041   -581    551  -3109       C  
ATOM   4871  C   THR B 383      58.323  55.562  88.052  1.00163.93           C  
ANISOU 4871  C   THR B 383    19865  22493  19924   -527    497  -3519       C  
ATOM   4872  O   THR B 383      57.984  55.454  89.235  1.00169.46           O  
ANISOU 4872  O   THR B 383    20591  23508  20287   -393    326  -3642       O  
ATOM   4873  CB  THR B 383      59.147  53.233  87.641  1.00159.73           C  
ANISOU 4873  CB  THR B 383    19276  22165  19247   -577    290  -3106       C  
ATOM   4874  OG1 THR B 383      60.482  53.459  87.186  1.00162.77           O  
ANISOU 4874  OG1 THR B 383    19488  22305  20050   -710    272  -3317       O  
ATOM   4875  CG2 THR B 383      58.650  51.894  87.101  1.00159.20           C  
ANISOU 4875  CG2 THR B 383    19295  22210  18981   -564    305  -2668       C  
ATOM   4876  N   CYS B 384      58.648  56.715  87.502  1.00169.79           N  
ANISOU 4876  N   CYS B 384    20564  22884  21062   -620    663  -3715       N  
ATOM   4877  CA  CYS B 384      58.663  57.984  88.265  1.00178.02           C  
ANISOU 4877  CA  CYS B 384    21559  23861  22216   -579    634  -4131       C  
ATOM   4878  C   CYS B 384      57.297  58.255  88.881  1.00179.20           C  
ANISOU 4878  C   CYS B 384    21860  24232  21993   -410    667  -4079       C  
ATOM   4879  O   CYS B 384      56.299  58.368  88.168  1.00183.88           O  
ANISOU 4879  O   CYS B 384    22585  24734  22545   -385    876  -3803       O  
ATOM   4880  CB  CYS B 384      59.068  59.190  87.382  1.00180.95           C  
ANISOU 4880  CB  CYS B 384    21887  23751  23111   -715    874  -4270       C  
ATOM   4881  SG  CYS B 384      59.556  60.727  88.235  1.00183.63           S  
ANISOU 4881  SG  CYS B 384    22089  23908  23772   -722    806  -4867       S  
ATOM   4882  N   CYS B 385      57.270  58.319  90.211  1.00178.95           N  
ANISOU 4882  N   CYS B 385    21805  24505  21681   -281    453  -4352       N  
ATOM   4883  CA  CYS B 385      56.050  58.558  91.006  1.00180.34           C  
ANISOU 4883  CA  CYS B 385    22104  24945  21470   -103    478  -4356       C  
ATOM   4884  C   CYS B 385      55.045  57.409  90.955  1.00177.00           C  
ANISOU 4884  C   CYS B 385    21804  24803  20642    -27    533  -3905       C  
ATOM   4885  O   CYS B 385      53.892  57.557  91.387  1.00184.07           O  
ANISOU 4885  O   CYS B 385    22794  25879  21262    101    626  -3835       O  
ATOM   4886  CB  CYS B 385      55.354  59.870  90.604  1.00184.95           C  
ANISOU 4886  CB  CYS B 385    22737  25249  22285    -91    699  -4475       C  
ATOM   4887  SG  CYS B 385      56.216  61.409  90.954  1.00194.38           S  
ANISOU 4887  SG  CYS B 385    23797  26130  23926   -141    651  -5060       S  
ATOM   4888  N   GLU B 386      55.478  56.268  90.434  1.00171.36           N  
ANISOU 4888  N   GLU B 386    21074  24114  19921   -108    482  -3613       N  
ATOM   4889  CA  GLU B 386      54.621  55.088  90.320  1.00168.37           C  
ANISOU 4889  CA  GLU B 386    20788  23960  19225    -60    524  -3183       C  
ATOM   4890  C   GLU B 386      54.739  54.240  91.573  1.00170.27           C  
ANISOU 4890  C   GLU B 386    21048  24603  19041     57    312  -3184       C  
ATOM   4891  O   GLU B 386      55.563  54.513  92.434  1.00169.51           O  
ANISOU 4891  O   GLU B 386    20897  24611  18897    106    104  -3516       O  
ATOM   4892  CB  GLU B 386      55.016  54.211  89.118  1.00167.87           C  
ANISOU 4892  CB  GLU B 386    20705  23716  19361   -193    567  -2864       C  
ATOM   4893  CG  GLU B 386      54.418  54.556  87.761  1.00170.88           C  
ANISOU 4893  CG  GLU B 386    21146  23795  19983   -257    809  -2652       C  
ATOM   4894  CD  GLU B 386      54.634  53.418  86.756  1.00171.99           C  
ANISOU 4894  CD  GLU B 386    21293  23865  20188   -342    821  -2310       C  
ATOM   4895  OE1 GLU B 386      55.251  52.404  87.161  1.00174.42           O  
ANISOU 4895  OE1 GLU B 386    21547  24345  20379   -356    645  -2248       O  
ATOM   4896  OE2 GLU B 386      54.187  53.502  85.570  1.00170.78           O  
ANISOU 4896  OE2 GLU B 386    21208  23490  20190   -376    990  -2106       O  
ATOM   4897  N   SER B 387      53.935  53.171  91.630  1.00173.98           N  
ANISOU 4897  N   SER B 387    21598  25284  19221    103    361  -2800       N  
ATOM   4898  CA  SER B 387      53.847  52.284  92.780  1.00177.76           C  
ANISOU 4898  CA  SER B 387    22138  26143  19257    228    216  -2706       C  
ATOM   4899  C   SER B 387      55.144  51.475  92.980  1.00178.58           C  
ANISOU 4899  C   SER B 387    22184  26289  19378    198    -52  -2734       C  
ATOM   4900  O   SER B 387      55.508  51.121  94.114  1.00184.26           O  
ANISOU 4900  O   SER B 387    22945  27292  19771    329   -258  -2836       O  
ATOM   4901  CB  SER B 387      52.633  51.339  92.648  1.00174.62           C  
ANISOU 4901  CB  SER B 387    21820  25895  18632    255    380  -2259       C  
ATOM   4902  OG  SER B 387      51.927  51.547  91.436  1.00174.22           O  
ANISOU 4902  OG  SER B 387    21750  25588  18855    164    587  -2080       O  
ATOM   4903  N   SER B 388      55.822  51.160  91.888  1.00176.63           N  
ANISOU 4903  N   SER B 388    21848  25771  19492     45    -53  -2640       N  
ATOM   4904  CA  SER B 388      57.091  50.452  91.998  1.00177.95           C  
ANISOU 4904  CA  SER B 388    21928  25946  19737     15   -304  -2696       C  
ATOM   4905  C   SER B 388      58.252  51.357  91.586  1.00183.59           C  
ANISOU 4905  C   SER B 388    22482  26382  20890    -91   -366  -3082       C  
ATOM   4906  O   SER B 388      59.282  50.879  91.082  1.00186.87           O  
ANISOU 4906  O   SER B 388    22779  26659  21563   -184   -472  -3092       O  
ATOM   4907  CB  SER B 388      57.052  49.132  91.226  1.00174.75           C  
ANISOU 4907  CB  SER B 388    21532  25495  19368    -56   -283  -2278       C  
ATOM   4908  OG  SER B 388      56.908  48.039  92.115  1.00174.01           O  
ANISOU 4908  OG  SER B 388    21521  25702  18891     61   -433  -2068       O  
ATOM   4909  N   GLY B 389      58.064  52.645  91.770  1.00188.53           N  
ANISOU 4909  N   GLY B 389    23094  26909  21629    -81   -281  -3392       N  
ATOM   4910  CA  GLY B 389      59.105  53.610  91.399  1.00190.93           C  
ANISOU 4910  CA  GLY B 389    23234  26910  22398   -197   -303  -3770       C  
ATOM   4911  C   GLY B 389      59.393  54.610  92.512  1.00190.88           C  
ANISOU 4911  C   GLY B 389    23180  27001  22343    -95   -467  -4259       C  
ATOM   4912  O   GLY B 389      59.086  54.386  93.643  1.00187.40           O  
ANISOU 4912  O   GLY B 389    22825  26898  21479     77   -630  -4328       O  
ATOM   4913  N   ALA B 390      60.016  55.713  92.142  1.00189.58           N  
ANISOU 4913  N   ALA B 390    22878  26518  22635   -206   -412  -4598       N  
ATOM   4914  CA  ALA B 390      60.464  56.714  93.116  1.00189.53           C  
ANISOU 4914  CA  ALA B 390    22782  26542  22686   -131   -596  -5133       C  
ATOM   4915  C   ALA B 390      59.844  58.081  92.821  1.00187.91           C  
ANISOU 4915  C   ALA B 390    22604  26078  22713   -165   -355  -5304       C  
ATOM   4916  O   ALA B 390      59.625  58.473  91.652  1.00187.46           O  
ANISOU 4916  O   ALA B 390    22555  25676  22992   -309    -68  -5116       O  
ATOM   4917  CB  ALA B 390      61.967  56.819  93.102  1.00192.08           C  
ANISOU 4917  CB  ALA B 390    22859  26698  23422   -232   -808  -5478       C  
ATOM   4918  N   LYS B 391      59.605  58.828  93.885  1.00188.88           N  
ANISOU 4918  N   LYS B 391    22747  26358  22660    -19   -481  -5676       N  
ATOM   4919  CA  LYS B 391      59.007  60.162  93.747  1.00195.09           C  
ANISOU 4919  CA  LYS B 391    23556  26908  23658    -24   -283  -5885       C  
ATOM   4920  C   LYS B 391      60.061  61.183  93.295  1.00195.33           C  
ANISOU 4920  C   LYS B 391    23377  26496  24344   -197   -271  -6267       C  
ATOM   4921  O   LYS B 391      61.215  61.143  93.677  1.00192.53           O  
ANISOU 4921  O   LYS B 391    22834  26125  24193   -238   -518  -6593       O  
ATOM   4922  CB  LYS B 391      58.299  60.611  95.048  1.00202.63           C  
ANISOU 4922  CB  LYS B 391    24615  28193  24182    209   -401  -6159       C  
ATOM   4923  CG  LYS B 391      56.803  60.963  94.901  1.00203.16           C  
ANISOU 4923  CG  LYS B 391    24856  28303  24031    298   -121  -5931       C  
ATOM   4924  CD  LYS B 391      56.550  62.382  94.365  1.00203.79           C  
ANISOU 4924  CD  LYS B 391    24900  27969  24562    231     80  -6155       C  
ATOM   4925  CE  LYS B 391      55.128  62.648  93.852  1.00198.97           C  
ANISOU 4925  CE  LYS B 391    24440  27311  23847    289    379  -5850       C  
ATOM   4926  NZ  LYS B 391      55.089  63.612  92.704  1.00195.96           N  
ANISOU 4926  NZ  LYS B 391    24038  26415  24001    151    619  -5825       N  
ATOM   4927  N   CYS B 392      59.575  62.137  92.498  1.00197.22           N  
ANISOU 4927  N   CYS B 392    23653  26368  24912   -284     25  -6223       N  
ATOM   4928  CA  CYS B 392      60.227  63.397  92.174  1.00202.49           C  
ANISOU 4928  CA  CYS B 392    24166  26582  26186   -421    109  -6594       C  
ATOM   4929  C   CYS B 392      59.545  64.531  92.937  1.00207.34           C  
ANISOU 4929  C   CYS B 392    24833  27200  26745   -280     98  -6951       C  
ATOM   4930  O   CYS B 392      58.532  64.365  93.620  1.00207.55           O  
ANISOU 4930  O   CYS B 392    25018  27569  26269    -81     65  -6888       O  
ATOM   4931  CB  CYS B 392      60.113  63.679  90.668  1.00201.87           C  
ANISOU 4931  CB  CYS B 392    24135  26059  26507   -600    483  -6243       C  
ATOM   4932  SG  CYS B 392      58.410  63.889  90.081  1.00206.42           S  
ANISOU 4932  SG  CYS B 392    24995  26630  26803   -485    779  -5818       S  
ATOM   4933  N   CYS B 393      60.076  65.730  92.767  1.00213.58           N  
ANISOU 4933  N   CYS B 393    25484  27574  28092   -388    158  -7324       N  
ATOM   4934  CA  CYS B 393      59.495  66.922  93.385  1.00220.34           C  
ANISOU 4934  CA  CYS B 393    26372  28351  28994   -269    162  -7697       C  
ATOM   4935  C   CYS B 393      58.938  67.932  92.379  1.00218.35           C  
ANISOU 4935  C   CYS B 393    26201  27612  29150   -358    524  -7548       C  
ATOM   4936  O   CYS B 393      58.862  69.111  92.682  1.00226.37           O  
ANISOU 4936  O   CYS B 393    27170  28381  30459   -334    542  -7930       O  
ATOM   4937  CB  CYS B 393      60.548  67.591  94.246  1.00228.30           C  
ANISOU 4937  CB  CYS B 393    27144  29283  30316   -283   -127  -8357       C  
ATOM   4938  SG  CYS B 393      62.007  68.099  93.302  1.00235.00           S  
ANISOU 4938  SG  CYS B 393    27703  29532  32053   -608    -19  -8516       S  
ATOM   4939  N   ARG B 394      58.583  67.435  91.191  1.00210.75           N  
ANISOU 4939  N   ARG B 394    25363  26514  28198   -448    792  -7000       N  
ATOM   4940  CA  ARG B 394      58.109  68.272  90.099  1.00210.17           C  
ANISOU 4940  CA  ARG B 394    25397  25973  28484   -521   1135  -6785       C  
ATOM   4941  C   ARG B 394      56.777  68.947  90.449  1.00215.36           C  
ANISOU 4941  C   ARG B 394    26218  26695  28912   -317   1206  -6815       C  
ATOM   4942  O   ARG B 394      56.671  70.183  90.494  1.00225.81           O  
ANISOU 4942  O   ARG B 394    27524  27676  30596   -310   1291  -7102       O  
ATOM   4943  CB  ARG B 394      57.954  67.411  88.846  1.00204.46           C  
ANISOU 4943  CB  ARG B 394    24799  25193  27693   -608   1351  -6190       C  
ATOM   4944  CG  ARG B 394      59.261  66.948  88.200  1.00199.87           C  
ANISOU 4944  CG  ARG B 394    24062  24419  27459   -829   1383  -6130       C  
ATOM   4945  CD  ARG B 394      58.965  66.416  86.797  1.00190.97           C  
ANISOU 4945  CD  ARG B 394    23103  23136  26322   -896   1666  -5561       C  
ATOM   4946  NE  ARG B 394      60.110  66.032  85.965  1.00184.30           N  
ANISOU 4946  NE  ARG B 394    22142  22059  25822  -1102   1783  -5443       N  
ATOM   4947  CZ  ARG B 394      60.731  64.850  85.992  1.00180.05           C  
ANISOU 4947  CZ  ARG B 394    21509  21779  25121  -1150   1637  -5336       C  
ATOM   4948  NH1 ARG B 394      60.383  63.879  86.852  1.00178.06           N  
ANISOU 4948  NH1 ARG B 394    21267  22027  24359  -1012   1351  -5320       N  
ATOM   4949  NH2 ARG B 394      61.736  64.647  85.150  1.00178.10           N  
ANISOU 4949  NH2 ARG B 394    21154  21272  25242  -1335   1794  -5242       N  
ATOM   4950  N   LYS B 395      55.775  68.100  90.710  1.00213.53           N  
ANISOU 4950  N   LYS B 395    26131  26899  28102   -154   1172  -6523       N  
ATOM   4951  CA  LYS B 395      54.425  68.527  91.059  1.00215.47           C  
ANISOU 4951  CA  LYS B 395    26515  27281  28070     53   1244  -6508       C  
ATOM   4952  C   LYS B 395      54.444  69.454  92.274  1.00219.46           C  
ANISOU 4952  C   LYS B 395    26940  27854  28591    179   1077  -7097       C  
ATOM   4953  O   LYS B 395      53.674  70.399  92.384  1.00218.24           O  
ANISOU 4953  O   LYS B 395    26846  27552  28522    295   1179  -7246       O  
ATOM   4954  CB  LYS B 395      53.589  67.305  91.402  1.00213.42           C  
ANISOU 4954  CB  LYS B 395    26356  27544  27189    186   1188  -6177       C  
ATOM   4955  CG  LYS B 395      53.436  66.329  90.255  1.00214.75           C  
ANISOU 4955  CG  LYS B 395    26609  27683  27304     91   1326  -5614       C  
ATOM   4956  CD  LYS B 395      52.188  65.488  90.417  1.00219.43           C  
ANISOU 4956  CD  LYS B 395    27316  28664  27392    245   1358  -5279       C  
ATOM   4957  CE  LYS B 395      51.837  64.777  89.123  1.00221.87           C  
ANISOU 4957  CE  LYS B 395    27719  28854  27724    173   1516  -4755       C  
ATOM   4958  NZ  LYS B 395      50.428  64.281  89.198  1.00221.67           N  
ANISOU 4958  NZ  LYS B 395    27785  29110  27328    332   1581  -4484       N  
ATOM   4959  N   GLU B 396      55.334  69.125  93.203  1.00219.02           N  
ANISOU 4959  N   GLU B 396    26747  28039  28431    172    797  -7440       N  
ATOM   4960  CA  GLU B 396      55.511  69.895  94.429  1.00217.19           C  
ANISOU 4960  CA  GLU B 396    26428  27913  28179    303    578  -8051       C  
ATOM   4961  C   GLU B 396      55.963  71.318  94.109  1.00214.21           C  
ANISOU 4961  C   GLU B 396    25941  26964  28482    197    663  -8422       C  
ATOM   4962  O   GLU B 396      55.383  72.284  94.635  1.00216.27           O  
ANISOU 4962  O   GLU B 396    26228  27158  28786    339    667  -8755       O  
ATOM   4963  CB  GLU B 396      56.538  69.188  95.342  1.00220.30           C  
ANISOU 4963  CB  GLU B 396    26692  28643  28366    310    231  -8324       C  
ATOM   4964  CG  GLU B 396      56.109  67.821  95.899  1.00223.31           C  
ANISOU 4964  CG  GLU B 396    27193  29614  28037    450    116  -8013       C  
ATOM   4965  CD  GLU B 396      55.698  66.777  94.849  1.00222.53           C  
ANISOU 4965  CD  GLU B 396    27199  29535  27816    351    326  -7341       C  
ATOM   4966  OE1 GLU B 396      56.304  66.730  93.742  1.00217.59           O  
ANISOU 4966  OE1 GLU B 396    26510  28540  27623    138    455  -7132       O  
ATOM   4967  OE2 GLU B 396      54.751  66.002  95.110  1.00225.59           O  
ANISOU 4967  OE2 GLU B 396    27731  30300  27683    488    376  -7022       O  
ATOM   4968  N   CYS B 397      56.976  71.441  93.253  1.00214.58           N  
ANISOU 4968  N   CYS B 397    25866  26592  29071    -50    748  -8362       N  
ATOM   4969  CA  CYS B 397      57.458  72.759  92.811  1.00218.95           C  
ANISOU 4969  CA  CYS B 397    26313  26533  30341   -188    884  -8648       C  
ATOM   4970  C   CYS B 397      56.360  73.522  92.066  1.00215.40           C  
ANISOU 4970  C   CYS B 397    26056  25772  30011   -123   1194  -8384       C  
ATOM   4971  O   CYS B 397      56.230  74.752  92.225  1.00222.57           O  
ANISOU 4971  O   CYS B 397    26935  26328  31302    -94   1244  -8729       O  
ATOM   4972  CB  CYS B 397      58.668  72.628  91.874  1.00220.32           C  
ANISOU 4972  CB  CYS B 397    26339  26316  31055   -477    999  -8518       C  
ATOM   4973  SG  CYS B 397      60.212  72.058  92.631  1.00219.18           S  
ANISOU 4973  SG  CYS B 397    25888  26357  31033   -590    634  -8945       S  
ATOM   4974  N   LEU B 398      55.585  72.813  91.241  1.00206.37           N  
ANISOU 4974  N   LEU B 398    25103  24737  28570    -93   1385  -7793       N  
ATOM   4975  CA  LEU B 398      54.452  73.445  90.567  1.00206.39           C  
ANISOU 4975  CA  LEU B 398    25297  24500  28621     12   1636  -7532       C  
ATOM   4976  C   LEU B 398      53.472  74.008  91.577  1.00212.40           C  
ANISOU 4976  C   LEU B 398    26095  25489  29115    264   1536  -7859       C  
ATOM   4977  O   LEU B 398      52.986  75.132  91.406  1.00219.95           O  
ANISOU 4977  O   LEU B 398    27101  26088  30380    333   1663  -8002       O  
ATOM   4978  CB  LEU B 398      53.728  72.445  89.688  1.00203.50           C  
ANISOU 4978  CB  LEU B 398    25109  24315  27894     42   1782  -6898       C  
ATOM   4979  CG  LEU B 398      52.470  72.961  88.999  1.00206.41           C  
ANISOU 4979  CG  LEU B 398    25676  24500  28249    188   1998  -6611       C  
ATOM   4980  CD1 LEU B 398      52.732  74.259  88.236  1.00211.98           C  
ANISOU 4980  CD1 LEU B 398    26421  24539  29580    108   2209  -6673       C  
ATOM   4981  CD2 LEU B 398      52.013  71.874  88.041  1.00204.49           C  
ANISOU 4981  CD2 LEU B 398    25572  24409  27713    181   2105  -6011       C  
ATOM   4982  N   LYS B 399      53.203  73.240  92.631  1.00217.47           N  
ANISOU 4982  N   LYS B 399    26719  26717  29191    408   1320  -7977       N  
ATOM   4983  CA  LYS B 399      52.277  73.669  93.680  1.00229.03           C  
ANISOU 4983  CA  LYS B 399    28221  28471  30330    664   1237  -8293       C  
ATOM   4984  C   LYS B 399      52.787  74.905  94.396  1.00241.12           C  
ANISOU 4984  C   LYS B 399    29623  29744  32246    687   1108  -8952       C  
ATOM   4985  O   LYS B 399      52.068  75.896  94.498  1.00243.83           O  
ANISOU 4985  O   LYS B 399    30012  29885  32744    820   1200  -9146       O  
ATOM   4986  CB  LYS B 399      52.031  72.558  94.698  1.00227.89           C  
ANISOU 4986  CB  LYS B 399    28091  29003  29493    805   1047  -8282       C  
ATOM   4987  CG  LYS B 399      51.137  71.445  94.222  1.00222.04           C  
ANISOU 4987  CG  LYS B 399    27482  28567  28315    851   1183  -7688       C  
ATOM   4988  CD  LYS B 399      51.091  70.327  95.256  1.00218.11           C  
ANISOU 4988  CD  LYS B 399    26992  28694  27185    961   1000  -7679       C  
ATOM   4989  CE  LYS B 399      50.494  69.028  94.721  1.00210.39           C  
ANISOU 4989  CE  LYS B 399    26107  27982  25849    942   1111  -7071       C  
ATOM   4990  NZ  LYS B 399      51.044  67.793  95.369  1.00207.70           N  
ANISOU 4990  NZ  LYS B 399    25751  28082  25080    934    917  -6982       N  
ATOM   4991  N   LEU B 400      54.017  74.835  94.902  1.00246.17           N  
ANISOU 4991  N   LEU B 400    30090  30390  33054    569    879  -9316       N  
ATOM   4992  CA  LEU B 400      54.643  75.974  95.600  1.00243.29           C  
ANISOU 4992  CA  LEU B 400    29563  29764  33109    573    713 -10001       C  
ATOM   4993  C   LEU B 400      54.627  77.245  94.751  1.00240.52           C  
ANISOU 4993  C   LEU B 400    29204  28709  33474    461    954 -10042       C  
ATOM   4994  O   LEU B 400      54.312  78.334  95.240  1.00241.94           O  
ANISOU 4994  O   LEU B 400    29358  28691  33876    578    926 -10480       O  
ATOM   4995  CB  LEU B 400      56.090  75.688  95.924  1.00244.17           C  
ANISOU 4995  CB  LEU B 400    29458  29866  33447    404    462 -10307       C  
ATOM   4996  CG  LEU B 400      56.326  74.625  96.990  1.00244.15           C  
ANISOU 4996  CG  LEU B 400    29442  30522  32800    540    142 -10426       C  
ATOM   4997  CD1 LEU B 400      57.815  74.287  97.011  1.00248.08           C  
ANISOU 4997  CD1 LEU B 400    29713  30927  33619    342    -78 -10635       C  
ATOM   4998  CD2 LEU B 400      55.842  75.078  98.348  1.00243.76           C  
ANISOU 4998  CD2 LEU B 400    29419  30821  32375    825    -78 -10959       C  
ATOM   4999  N   MET B 401      54.974  77.097  93.476  1.00235.44           N  
ANISOU 4999  N   MET B 401    28593  27681  33182    244   1197  -9579       N  
ATOM   5000  CA  MET B 401      55.001  78.236  92.567  1.00235.22           C  
ANISOU 5000  CA  MET B 401    28591  26958  33823    132   1462  -9533       C  
ATOM   5001  C   MET B 401      53.600  78.817  92.374  1.00234.47           C  
ANISOU 5001  C   MET B 401    28700  26799  33590    356   1628  -9375       C  
ATOM   5002  O   MET B 401      53.395  80.044  92.458  1.00239.13           O  
ANISOU 5002  O   MET B 401    29278  26975  34603    409   1687  -9689       O  
ATOM   5003  CB  MET B 401      55.589  77.814  91.236  1.00233.56           C  
ANISOU 5003  CB  MET B 401    28417  26427  33897   -112   1708  -9008       C  
ATOM   5004  CG  MET B 401      55.961  78.970  90.326  1.00236.79           C  
ANISOU 5004  CG  MET B 401    28827  26074  35066   -275   1986  -8987       C  
ATOM   5005  SD  MET B 401      57.191  80.042  91.074  1.00243.16           S  
ANISOU 5005  SD  MET B 401    29312  26480  36598   -435   1824  -9761       S  
ATOM   5006  CE  MET B 401      57.974  80.711  89.591  1.00243.83           C  
ANISOU 5006  CE  MET B 401    29397  25733  37513   -744   2249  -9429       C  
ATOM   5007  N   LYS B 402      52.644  77.918  92.130  1.00231.03           N  
ANISOU 5007  N   LYS B 402    28431  26766  32584    489   1691  -8905       N  
ATOM   5008  CA  LYS B 402      51.234  78.282  92.029  1.00232.58           C  
ANISOU 5008  CA  LYS B 402    28793  27005  32571    728   1815  -8751       C  
ATOM   5009  C   LYS B 402      50.782  79.095  93.222  1.00244.78           C  
ANISOU 5009  C   LYS B 402    30273  28672  34058    941   1665  -9345       C  
ATOM   5010  O   LYS B 402      50.113  80.119  93.064  1.00256.83           O  
ANISOU 5010  O   LYS B 402    31861  29866  35854   1065   1780  -9458       O  
ATOM   5011  CB  LYS B 402      50.313  77.052  91.857  1.00225.54           C  
ANISOU 5011  CB  LYS B 402    28029  26634  31031    845   1846  -8254       C  
ATOM   5012  CG  LYS B 402      49.667  76.909  90.480  1.00224.11           C  
ANISOU 5012  CG  LYS B 402    28030  26199  30922    837   2096  -7647       C  
ATOM   5013  CD  LYS B 402      49.192  75.483  90.171  1.00220.76           C  
ANISOU 5013  CD  LYS B 402    27678  26241  29958    856   2097  -7150       C  
ATOM   5014  CE  LYS B 402      48.054  74.969  91.055  1.00220.98           C  
ANISOU 5014  CE  LYS B 402    27710  26835  29415   1092   2016  -7188       C  
ATOM   5015  NZ  LYS B 402      46.770  75.721  90.992  1.00223.08           N  
ANISOU 5015  NZ  LYS B 402    28054  27005  29702   1325   2126  -7206       N  
ATOM   5016  N   TYR B 403      51.141  78.632  94.415  1.00246.66           N  
ANISOU 5016  N   TYR B 403    30399  29392  33929   1003   1403  -9726       N  
ATOM   5017  CA  TYR B 403      50.700  79.259  95.667  1.00246.86           C  
ANISOU 5017  CA  TYR B 403    30376  29643  33773   1240   1239 -10309       C  
ATOM   5018  C   TYR B 403      51.314  80.632  95.815  1.00249.42           C  
ANISOU 5018  C   TYR B 403    30577  29411  34779   1180   1190 -10860       C  
ATOM   5019  O   TYR B 403      50.598  81.601  96.079  1.00251.60           O  
ANISOU 5019  O   TYR B 403    30886  29508  35200   1358   1239 -11135       O  
ATOM   5020  CB  TYR B 403      51.110  78.413  96.875  1.00242.96           C  
ANISOU 5020  CB  TYR B 403    29811  29778  32722   1317    954 -10582       C  
ATOM   5021  CG  TYR B 403      50.702  78.956  98.247  1.00240.74           C  
ANISOU 5021  CG  TYR B 403    29504  29808  32157   1588    771 -11199       C  
ATOM   5022  CD1 TYR B 403      49.377  78.887  98.683  1.00239.66           C  
ANISOU 5022  CD1 TYR B 403    29488  30031  31541   1857    879 -11125       C  
ATOM   5023  CD2 TYR B 403      51.644  79.495  99.124  1.00238.98           C  
ANISOU 5023  CD2 TYR B 403    29127  29545  32129   1587    486 -11868       C  
ATOM   5024  CE1 TYR B 403      49.010  79.355  99.943  1.00243.26           C  
ANISOU 5024  CE1 TYR B 403    29930  30795  31699   2120    735 -11688       C  
ATOM   5025  CE2 TYR B 403      51.273  79.961 100.381  1.00242.32           C  
ANISOU 5025  CE2 TYR B 403    29545  30279  32244   1859    308 -12445       C  
ATOM   5026  CZ  TYR B 403      49.971  79.892 100.787  1.00244.68           C  
ANISOU 5026  CZ  TYR B 403    29984  30935  32048   2126    444 -12350       C  
ATOM   5027  OH  TYR B 403      49.657  80.369 102.041  1.00251.42           O  
ANISOU 5027  OH  TYR B 403    30837  32101  32590   2403    281 -12945       O  
ATOM   5028  N   LEU B 404      52.637  80.698  95.665  1.00247.16           N  
ANISOU 5028  N   LEU B 404    30132  28849  34926    932   1093 -11035       N  
ATOM   5029  CA  LEU B 404      53.358  81.962  95.673  1.00252.10           C  
ANISOU 5029  CA  LEU B 404    30607  28868  36309    817   1069 -11526       C  
ATOM   5030  C   LEU B 404      52.612  82.989  94.818  1.00255.29           C  
ANISOU 5030  C   LEU B 404    31142  28701  37154    852   1363 -11328       C  
ATOM   5031  O   LEU B 404      52.269  84.084  95.295  1.00264.98           O  
ANISOU 5031  O   LEU B 404    32340  29683  38657    990   1327 -11787       O  
ATOM   5032  CB  LEU B 404      54.756  81.725  95.118  1.00250.81           C  
ANISOU 5032  CB  LEU B 404    30280  28400  36617    490   1062 -11471       C  
ATOM   5033  CG  LEU B 404      55.672  82.927  94.897  1.00255.32           C  
ANISOU 5033  CG  LEU B 404    30662  28256  38090    288   1098 -11881       C  
ATOM   5034  CD1 LEU B 404      56.013  83.588  96.221  1.00261.43           C  
ANISOU 5034  CD1 LEU B 404    31244  29125  38961    410    754 -12725       C  
ATOM   5035  CD2 LEU B 404      56.941  82.462  94.190  1.00254.29           C  
ANISOU 5035  CD2 LEU B 404    30381  27884  38351    -40   1162 -11679       C  
ATOM   5036  N   LEU B 405      52.333  82.610  93.569  1.00252.56           N  
ANISOU 5036  N   LEU B 405    30954  28159  36845    753   1638 -10649       N  
ATOM   5037  CA  LEU B 405      51.639  83.515  92.661  1.00254.54           C  
ANISOU 5037  CA  LEU B 405    31363  27865  37484    803   1912 -10394       C  
ATOM   5038  C   LEU B 405      50.214  83.859  93.124  1.00256.02           C  
ANISOU 5038  C   LEU B 405    31670  28282  37324   1139   1908 -10475       C  
ATOM   5039  O   LEU B 405      49.785  85.009  92.996  1.00263.09           O  
ANISOU 5039  O   LEU B 405    32605  28722  38635   1240   2000 -10661       O  
ATOM   5040  CB  LEU B 405      51.565  82.960  91.251  1.00254.67           C  
ANISOU 5040  CB  LEU B 405    31554  27694  37512    675   2181  -9643       C  
ATOM   5041  CG  LEU B 405      51.048  84.002  90.248  1.00258.55           C  
ANISOU 5041  CG  LEU B 405    32222  27531  38485    715   2458  -9392       C  
ATOM   5042  CD1 LEU B 405      52.165  84.955  89.833  1.00261.32           C  
ANISOU 5042  CD1 LEU B 405    32470  27160  39656    462   2586  -9581       C  
ATOM   5043  CD2 LEU B 405      50.404  83.311  89.050  1.00258.14           C  
ANISOU 5043  CD2 LEU B 405    32411  27523  38147    750   2666  -8642       C  
ATOM   5044  N   GLU B 406      49.487  82.868  93.646  1.00254.68           N  
ANISOU 5044  N   GLU B 406    31548  28795  36421   1309   1817 -10331       N  
ATOM   5045  CA  GLU B 406      48.137  83.114  94.130  1.00256.34           C  
ANISOU 5045  CA  GLU B 406    31839  29269  36289   1624   1832 -10416       C  
ATOM   5046  C   GLU B 406      48.106  84.169  95.222  1.00265.36           C  
ANISOU 5046  C   GLU B 406    32868  30338  37614   1783   1679 -11157       C  
ATOM   5047  O   GLU B 406      47.317  85.117  95.136  1.00272.75           O  
ANISOU 5047  O   GLU B 406    33860  30981  38789   1960   1775 -11284       O  
ATOM   5048  CB  GLU B 406      47.300  81.855  94.466  1.00248.29           C  
ANISOU 5048  CB  GLU B 406    30881  28975  34481   1771   1810 -10099       C  
ATOM   5049  CG  GLU B 406      46.841  80.987  93.279  1.00241.81           C  
ANISOU 5049  CG  GLU B 406    30203  28183  33489   1707   1993  -9349       C  
ATOM   5050  CD  GLU B 406      46.308  81.726  92.033  1.00242.19           C  
ANISOU 5050  CD  GLU B 406    30399  27650  33972   1732   2217  -9000       C  
ATOM   5051  OE1 GLU B 406      45.692  82.816  92.162  1.00241.41           O  
ANISOU 5051  OE1 GLU B 406    30321  27256  34147   1909   2260  -9259       O  
ATOM   5052  OE2 GLU B 406      46.529  81.197  90.893  1.00242.05           O  
ANISOU 5052  OE2 GLU B 406    30488  27463  34016   1584   2345  -8456       O  
ATOM   5053  N   GLN B 407      48.989  84.024  96.207  1.00262.69           N  
ANISOU 5053  N   GLN B 407    32374  30243  37192   1727   1428 -11654       N  
ATOM   5054  CA  GLN B 407      49.090  84.968  97.321  1.00260.59           C  
ANISOU 5054  CA  GLN B 407    31990  29945  37077   1879   1233 -12427       C  
ATOM   5055  C   GLN B 407      49.498  86.359  96.842  1.00263.14           C  
ANISOU 5055  C   GLN B 407    32252  29451  38276   1773   1310 -12698       C  
ATOM   5056  O   GLN B 407      48.835  87.368  97.161  1.00260.11           O  
ANISOU 5056  O   GLN B 407    31882  28848  38098   1976   1329 -13046       O  
ATOM   5057  CB  GLN B 407      50.189  84.462  98.284  1.00258.01           C  
ANISOU 5057  CB  GLN B 407    31505  29977  36550   1797    920 -12859       C  
ATOM   5058  CG  GLN B 407      49.936  83.143  98.993  1.00253.14           C  
ANISOU 5058  CG  GLN B 407    30941  30173  35066   1918    796 -12700       C  
ATOM   5059  CD  GLN B 407      48.795  83.296  99.952  1.00254.29           C  
ANISOU 5059  CD  GLN B 407    31162  30766  34688   2268    779 -12963       C  
ATOM   5060  OE1 GLN B 407      47.663  82.973  99.622  1.00254.66           O  
ANISOU 5060  OE1 GLN B 407    31335  30997  34424   2401    992 -12544       O  
ATOM   5061  NE2 GLN B 407      49.066  83.869 101.115  1.00256.36           N  
ANISOU 5061  NE2 GLN B 407    31336  31170  34897   2428    535 -13686       N  
ATOM   5062  N   LEU B 408      50.592  86.406  96.078  1.00266.45           N  
ANISOU 5062  N   LEU B 408    32600  29411  39226   1457   1371 -12537       N  
ATOM   5063  CA  LEU B 408      51.077  87.675  95.525  1.00271.95           C  
ANISOU 5063  CA  LEU B 408    33239  29277  40811   1313   1491 -12725       C  
ATOM   5064  C   LEU B 408      50.011  88.367  94.674  1.00275.57           C  
ANISOU 5064  C   LEU B 408    33902  29323  41480   1451   1767 -12358       C  
ATOM   5065  O   LEU B 408      50.051  89.588  94.509  1.00280.74           O  
ANISOU 5065  O   LEU B 408    34536  29349  42782   1453   1841 -12623       O  
ATOM   5066  CB  LEU B 408      52.319  87.455  94.664  1.00270.21           C  
ANISOU 5066  CB  LEU B 408    32935  28657  41075    943   1597 -12456       C  
ATOM   5067  CG  LEU B 408      53.647  87.612  95.394  1.00271.50           C  
ANISOU 5067  CG  LEU B 408    32810  28758  41588    759   1338 -13071       C  
ATOM   5068  CD1 LEU B 408      54.763  86.947  94.629  1.00269.26           C  
ANISOU 5068  CD1 LEU B 408    32439  28329  41537    424   1431 -12715       C  
ATOM   5069  CD2 LEU B 408      53.966  89.072  95.601  1.00277.01           C  
ANISOU 5069  CD2 LEU B 408    33371  28786  43091    726   1324 -13646       C  
ATOM   5070  N   LYS B 409      49.070  87.582  94.137  1.00274.13           N  
ANISOU 5070  N   LYS B 409    33908  29478  40768   1574   1905 -11759       N  
ATOM   5071  CA  LYS B 409      47.966  88.122  93.331  1.00271.62           C  
ANISOU 5071  CA  LYS B 409    33790  28843  40570   1748   2130 -11388       C  
ATOM   5072  C   LYS B 409      46.801  88.608  94.189  1.00267.78           C  
ANISOU 5072  C   LYS B 409    33307  28613  39823   2103   2045 -11768       C  
ATOM   5073  O   LYS B 409      46.141  89.595  93.849  1.00273.15           O  
ANISOU 5073  O   LYS B 409    34071  28844  40871   2256   2158 -11799       O  
ATOM   5074  CB  LYS B 409      47.381  87.079  92.359  1.00271.64           C  
ANISOU 5074  CB  LYS B 409    33979  29099  40133   1751   2293 -10607       C  
ATOM   5075  CG  LYS B 409      47.812  87.238  90.908  1.00272.87           C  
ANISOU 5075  CG  LYS B 409    34282  28660  40735   1549   2544 -10046       C  
ATOM   5076  CD  LYS B 409      47.245  86.112  90.039  1.00267.65           C  
ANISOU 5076  CD  LYS B 409    33795  28326  39574   1575   2654  -9335       C  
ATOM   5077  CE  LYS B 409      45.767  86.304  89.697  1.00266.28           C  
ANISOU 5077  CE  LYS B 409    33787  28204  39182   1889   2726  -9082       C  
ATOM   5078  NZ  LYS B 409      45.490  87.503  88.841  1.00269.60           N  
ANISOU 5078  NZ  LYS B 409    34370  27884  40181   1964   2904  -8949       N  
ATOM   5079  N   LYS B 410      46.527  87.904  95.285  1.00259.57           N  
ANISOU 5079  N   LYS B 410    32188  28296  38140   2245   1860 -12037       N  
ATOM   5080  CA  LYS B 410      45.462  88.321  96.176  1.00258.92           C  
ANISOU 5080  CA  LYS B 410    32095  28505  37777   2585   1800 -12427       C  
ATOM   5081  C   LYS B 410      45.821  89.590  96.933  1.00266.75           C  
ANISOU 5081  C   LYS B 410    32961  29129  39261   2654   1662 -13194       C  
ATOM   5082  O   LYS B 410      44.925  90.352  97.296  1.00269.86           O  
ANISOU 5082  O   LYS B 410    33372  29455  39706   2924   1682 -13482       O  
ATOM   5083  CB  LYS B 410      44.941  87.134  97.007  1.00251.09           C  
ANISOU 5083  CB  LYS B 410    31094  28392  35915   2731   1711 -12380       C  
ATOM   5084  CG  LYS B 410      43.755  86.428  96.310  1.00242.56           C  
ANISOU 5084  CG  LYS B 410    30148  27561  34450   2854   1907 -11733       C  
ATOM   5085  CD  LYS B 410      43.951  85.017  95.715  1.00234.37           C  
ANISOU 5085  CD  LYS B 410    29171  26873  33003   2677   1958 -11097       C  
ATOM   5086  CE  LYS B 410      43.500  84.900  94.257  1.00229.70           C  
ANISOU 5086  CE  LYS B 410    28728  25925  32620   2620   2163 -10422       C  
ATOM   5087  NZ  LYS B 410      43.076  83.505  93.925  1.00225.09           N  
ANISOU 5087  NZ  LYS B 410    28195  25853  31474   2595   2212  -9870       N  
ATOM   5088  N   GLU B 411      47.116  89.838  97.107  1.00269.28           N  
ANISOU 5088  N   GLU B 411    33144  29176  39993   2408   1527 -13522       N  
ATOM   5089  CA  GLU B 411      47.547  91.054  97.802  1.00276.11           C  
ANISOU 5089  CA  GLU B 411    33865  29646  41399   2450   1373 -14288       C  
ATOM   5090  C   GLU B 411      47.756  92.251  96.868  1.00280.14           C  
ANISOU 5090  C   GLU B 411    34402  29217  42820   2324   1556 -14221       C  
ATOM   5091  O   GLU B 411      47.607  93.409  97.281  1.00287.27           O  
ANISOU 5091  O   GLU B 411    35241  29726  44180   2452   1501 -14759       O  
ATOM   5092  CB  GLU B 411      48.835  90.810  98.608  1.00277.90           C  
ANISOU 5092  CB  GLU B 411    33887  30045  41655   2276   1088 -14799       C  
ATOM   5093  CG  GLU B 411      49.311  92.067  99.359  1.00285.00           C  
ANISOU 5093  CG  GLU B 411    34612  30533  43142   2320    892 -15654       C  
ATOM   5094  CD  GLU B 411      50.269  91.832 100.504  1.00287.29           C  
ANISOU 5094  CD  GLU B 411    34703  31182  43272   2292    526 -16317       C  
ATOM   5095  OE1 GLU B 411      50.765  90.704 100.651  1.00286.13           O  
ANISOU 5095  OE1 GLU B 411    34540  31534  42640   2190    422 -16098       O  
ATOM   5096  OE2 GLU B 411      50.529  92.801 101.253  1.00290.02           O  
ANISOU 5096  OE2 GLU B 411    34907  31290  43996   2384    326 -17078       O  
ATOM   5097  N   PHE B 412      48.116  91.987  95.618  1.00279.20           N  
ANISOU 5097  N   PHE B 412    34386  28727  42969   2083   1781 -13569       N  
ATOM   5098  CA  PHE B 412      48.428  93.074  94.686  1.00283.59           C  
ANISOU 5098  CA  PHE B 412    34991  28370  44388   1941   1988 -13448       C  
ATOM   5099  C   PHE B 412      47.627  93.003  93.390  1.00282.00           C  
ANISOU 5099  C   PHE B 412    35059  27914  44174   2001   2284 -12663       C  
ATOM   5100  O   PHE B 412      47.668  92.061  92.627  1.00285.39           O  
ANISOU 5100  O   PHE B 412    35605  28550  44280   1889   2405 -12039       O  
ATOM   5101  CB  PHE B 412      49.917  93.101  94.377  1.00285.62           C  
ANISOU 5101  CB  PHE B 412    35094  28233  45194   1553   1997 -13504       C  
ATOM   5102  CG  PHE B 412      50.772  93.370  95.579  1.00290.40           C  
ANISOU 5102  CG  PHE B 412    35416  28955  45966   1496   1681 -14337       C  
ATOM   5103  CD1 PHE B 412      50.792  94.634  96.159  1.00297.98           C  
ANISOU 5103  CD1 PHE B 412    36257  29464  47495   1589   1577 -15015       C  
ATOM   5104  CD2 PHE B 412      51.546  92.365  96.145  1.00287.14           C  
ANISOU 5104  CD2 PHE B 412    34858  29100  45143   1370   1465 -14464       C  
ATOM   5105  CE1 PHE B 412      51.583  94.897  97.270  1.00301.14           C  
ANISOU 5105  CE1 PHE B 412    36392  29972  48055   1555   1252 -15825       C  
ATOM   5106  CE2 PHE B 412      52.334  92.617  97.262  1.00290.33           C  
ANISOU 5106  CE2 PHE B 412    35005  29622  45683   1347   1134 -15256       C  
ATOM   5107  CZ  PHE B 412      52.361  93.887  97.818  1.00297.49           C  
ANISOU 5107  CZ  PHE B 412    35789  30078  47163   1438   1023 -15947       C  
ATOM   5108  N   GLN B 413      47.000  94.141  93.134  1.00280.69           N  
ANISOU 5108  N   GLN B 413    34983  27203  44464   2174   2385 -12755       N  
ATOM   5109  CA  GLN B 413      46.144  94.424  91.954  1.00276.34           C  
ANISOU 5109  CA  GLN B 413    34700  26272  44023   2304   2635 -12121       C  
ATOM   5110  C   GLN B 413      46.999  94.600  90.734  1.00277.65           C  
ANISOU 5110  C   GLN B 413    34981  25789  44723   2005   2885 -11624       C  
ATOM   5111  O   GLN B 413      46.492  94.513  89.601  1.00274.71           O  
ANISOU 5111  O   GLN B 413    34865  25194  44319   2064   3097 -10963       O  
ATOM   5112  CB  GLN B 413      45.421  95.769  92.196  1.00279.42           C  
ANISOU 5112  CB  GLN B 413    35115  26179  44870   2569   2634 -12507       C  
ATOM   5113  CG  GLN B 413      44.956  96.619  90.992  1.00280.56           C  
ANISOU 5113  CG  GLN B 413    35510  25563  45526   2650   2883 -12033       C  
ATOM   5114  CD  GLN B 413      43.489  96.461  90.674  1.00278.70           C  
ANISOU 5114  CD  GLN B 413    35453  25583  44857   3017   2909 -11695       C  
ATOM   5115  OE1 GLN B 413      42.655  96.466  91.571  1.00280.83           O  
ANISOU 5115  OE1 GLN B 413    35620  26300  44780   3292   2753 -12095       O  
ATOM   5116  NE2 GLN B 413      43.162  96.342  89.393  1.00277.88           N  
ANISOU 5116  NE2 GLN B 413    35612  25187  44781   3038   3108 -10971       N  
ATOM   5117  N   GLU B 414      48.299  94.776  90.943  1.00280.91           N  
ANISOU 5117  N   GLU B 414    35205  25933  45594   1689   2862 -11923       N  
ATOM   5118  CA  GLU B 414      49.222  95.036  89.836  1.00281.85           C  
ANISOU 5118  CA  GLU B 414    35400  25380  46308   1377   3140 -11505       C  
ATOM   5119  C   GLU B 414      49.494  93.756  89.052  1.00275.00           C  
ANISOU 5119  C   GLU B 414    34645  24889  44954   1220   3258 -10835       C  
ATOM   5120  O   GLU B 414      50.131  93.769  87.995  1.00269.21           O  
ANISOU 5120  O   GLU B 414    34025  23700  44562    993   3528 -10358       O  
ATOM   5121  CB  GLU B 414      50.506  95.683  90.347  1.00287.52           C  
ANISOU 5121  CB  GLU B 414    35834  25666  47742   1088   3081 -12093       C  
ATOM   5122  CG  GLU B 414      50.307  97.098  90.871  1.00296.94           C  
ANISOU 5122  CG  GLU B 414    36946  26294  49583   1214   3021 -12691       C  
ATOM   5123  CD  GLU B 414      49.729  97.169  92.278  1.00302.62           C  
ANISOU 5123  CD  GLU B 414    37502  27560  49917   1491   2665 -13420       C  
ATOM   5124  OE1 GLU B 414      50.080  98.131  93.014  1.00312.44           O  
ANISOU 5124  OE1 GLU B 414    38549  28451  51712   1489   2521 -14132       O  
ATOM   5125  OE2 GLU B 414      48.928  96.288  92.661  1.00300.21           O  
ANISOU 5125  OE2 GLU B 414    37261  28022  48780   1713   2538 -13301       O  
ATOM   5126  N   LEU B 415      48.966  92.645  89.558  1.00272.04           N  
ANISOU 5126  N   LEU B 415    34248  25345  43769   1357   3070 -10787       N  
ATOM   5127  CA  LEU B 415      49.292  91.321  88.982  1.00266.46           C  
ANISOU 5127  CA  LEU B 415    33602  25067  42572   1201   3130 -10240       C  
ATOM   5128  C   LEU B 415      48.023  90.628  88.522  1.00262.02           C  
ANISOU 5128  C   LEU B 415    33267  24932  41354   1469   3157  -9723       C  
ATOM   5129  O   LEU B 415      47.952  89.410  88.472  1.00260.27           O  
ANISOU 5129  O   LEU B 415    33054  25296  40540   1442   3099  -9430       O  
ATOM   5130  CB  LEU B 415      50.001  90.510  90.060  1.00265.77           C  
ANISOU 5130  CB  LEU B 415    33245  25586  42150   1077   2859 -10678       C  
ATOM   5131  CG  LEU B 415      51.260  91.191  90.634  1.00269.96           C  
ANISOU 5131  CG  LEU B 415    33501  25731  43340    830   2768 -11288       C  
ATOM   5132  CD1 LEU B 415      51.771  90.463  91.873  1.00269.83           C  
ANISOU 5132  CD1 LEU B 415    33232  26376  42915    805   2426 -11807       C  
ATOM   5133  CD2 LEU B 415      52.344  91.303  89.573  1.00268.87           C  
ANISOU 5133  CD2 LEU B 415    33369  25003  43785    483   3045 -10925       C  
ATOM   5134  N   ASP B 416      47.064  91.415  88.050  1.00262.24           N  
ANISOU 5134  N   ASP B 416    33488  24602  41549   1715   3261  -9563       N  
ATOM   5135  CA  ASP B 416      45.814  90.832  87.508  1.00257.93           C  
ANISOU 5135  CA  ASP B 416    33150  24399  40453   1985   3283  -9067       C  
ATOM   5136  C   ASP B 416      46.009  90.272  86.111  1.00257.52           C  
ANISOU 5136  C   ASP B 416    33339  24174  40331   1871   3501  -8309       C  
ATOM   5137  O   ASP B 416      45.152  89.543  85.616  1.00249.51           O  
ANISOU 5137  O   ASP B 416    32471  23514  38815   2044   3492  -7876       O  
ATOM   5138  CB  ASP B 416      44.693  91.876  87.520  1.00256.99           C  
ANISOU 5138  CB  ASP B 416    33136  23968  40538   2321   3288  -9194       C  
ATOM   5139  CG  ASP B 416      44.425  92.437  88.920  1.00256.34           C  
ANISOU 5139  CG  ASP B 416    32822  24081  40491   2469   3077  -9971       C  
ATOM   5140  OD1 ASP B 416      45.046  91.949  89.894  1.00253.50           O  
ANISOU 5140  OD1 ASP B 416    32239  24156  39921   2335   2911 -10389       O  
ATOM   5141  OD2 ASP B 416      43.606  93.375  89.045  1.00255.71           O  
ANISOU 5141  OD2 ASP B 416    32791  23719  40646   2736   3071 -10172       O  
ATOM   5142  N   ALA B 417      47.133  90.604  85.470  1.00263.63           N  
ANISOU 5142  N   ALA B 417    34147  24405  41612   1583   3701  -8159       N  
ATOM   5143  CA  ALA B 417      47.478  90.067  84.149  1.00262.73           C  
ANISOU 5143  CA  ALA B 417    34266  24122  41438   1453   3936  -7460       C  
ATOM   5144  C   ALA B 417      47.945  88.627  84.254  1.00259.72           C  
ANISOU 5144  C   ALA B 417    33776  24387  40520   1283   3847  -7302       C  
ATOM   5145  O   ALA B 417      47.834  87.851  83.296  1.00261.30           O  
ANISOU 5145  O   ALA B 417    34167  24712  40401   1275   3958  -6723       O  
ATOM   5146  CB  ALA B 417      48.589  90.897  83.519  1.00267.41           C  
ANISOU 5146  CB  ALA B 417    34900  23929  42772   1184   4214  -7387       C  
ATOM   5147  N   PHE B 418      48.485  88.275  85.415  1.00261.27           N  
ANISOU 5147  N   PHE B 418    33671  24980  40617   1158   3636  -7827       N  
ATOM   5148  CA  PHE B 418      49.101  86.967  85.612  1.00259.10           C  
ANISOU 5148  CA  PHE B 418    33268  25268  39909    974   3539  -7736       C  
ATOM   5149  C   PHE B 418      48.092  85.911  86.041  1.00256.87           C  
ANISOU 5149  C   PHE B 418    32991  25751  38854   1191   3344  -7632       C  
ATOM   5150  O   PHE B 418      47.225  86.156  86.857  1.00260.79           O  
ANISOU 5150  O   PHE B 418    33428  26510  39149   1427   3188  -7955       O  
ATOM   5151  CB  PHE B 418      50.240  87.044  86.614  1.00259.56           C  
ANISOU 5151  CB  PHE B 418    33010  25380  40229    741   3391  -8327       C  
ATOM   5152  CG  PHE B 418      51.328  87.994  86.205  1.00262.95           C  
ANISOU 5152  CG  PHE B 418    33379  25058  41469    483   3593  -8446       C  
ATOM   5153  CD1 PHE B 418      52.373  87.576  85.387  1.00260.78           C  
ANISOU 5153  CD1 PHE B 418    33107  24569  41408    190   3801  -8104       C  
ATOM   5154  CD2 PHE B 418      51.303  89.325  86.618  1.00268.70           C  
ANISOU 5154  CD2 PHE B 418    34043  25267  42783    531   3596  -8898       C  
ATOM   5155  CE1 PHE B 418      53.383  88.458  85.010  1.00263.31           C  
ANISOU 5155  CE1 PHE B 418    33350  24176  42517    -62   4027  -8207       C  
ATOM   5156  CE2 PHE B 418      52.306  90.215  86.245  1.00271.63           C  
ANISOU 5156  CE2 PHE B 418    34340  24907  43959    277   3802  -9009       C  
ATOM   5157  CZ  PHE B 418      53.344  89.779  85.433  1.00268.76           C  
ANISOU 5157  CZ  PHE B 418    33969  24338  43808    -25   4031  -8651       C  
ATOM   5158  N   CYS B 419      48.249  84.705  85.467  1.00247.43           N  
ANISOU 5158  N   CYS B 419    31860  24904  37246   1098   3372  -7174       N  
ATOM   5159  CA  CYS B 419      47.446  83.519  85.795  1.00235.39           C  
ANISOU 5159  CA  CYS B 419    30322  24104  35009   1246   3210  -7018       C  
ATOM   5160  C   CYS B 419      48.380  82.326  86.054  1.00235.42           C  
ANISOU 5160  C   CYS B 419    30181  24531  34736   1007   3121  -6985       C  
ATOM   5161  O   CYS B 419      49.586  82.421  85.843  1.00234.05           O  
ANISOU 5161  O   CYS B 419    29929  24075  34923    744   3198  -7037       O  
ATOM   5162  CB  CYS B 419      46.404  83.219  84.688  1.00224.66           C  
ANISOU 5162  CB  CYS B 419    29227  22733  33398   1445   3315  -6428       C  
ATOM   5163  SG  CYS B 419      46.981  82.761  83.023  1.00207.69           S  
ANISOU 5163  SG  CYS B 419    27333  20253  31323   1286   3560  -5727       S  
ATOM   5164  N   SER B 420      47.846  81.208  86.524  1.00235.65           N  
ANISOU 5164  N   SER B 420    30160  25221  34155   1097   2965  -6905       N  
ATOM   5165  CA  SER B 420      48.715  80.077  86.822  1.00230.62           C  
ANISOU 5165  CA  SER B 420    29389  24979  33255    893   2861  -6883       C  
ATOM   5166  C   SER B 420      49.220  79.354  85.577  1.00218.48           C  
ANISOU 5166  C   SER B 420    27983  23316  31713    727   3022  -6324       C  
ATOM   5167  O   SER B 420      50.188  78.608  85.680  1.00210.50           O  
ANISOU 5167  O   SER B 420    26853  22476  30649    517   2973  -6324       O  
ATOM   5168  CB  SER B 420      48.031  79.123  87.798  1.00233.87           C  
ANISOU 5168  CB  SER B 420    29708  26118  33032   1039   2656  -6986       C  
ATOM   5169  OG  SER B 420      46.665  78.971  87.471  1.00239.11           O  
ANISOU 5169  OG  SER B 420    30504  26943  33404   1283   2698  -6706       O  
ATOM   5170  N   TYR B 421      48.645  79.610  84.407  1.00212.83           N  
ANISOU 5170  N   TYR B 421    27508  22281  31073    824   3208  -5876       N  
ATOM   5171  CA  TYR B 421      49.113  78.992  83.193  1.00207.91           C  
ANISOU 5171  CA  TYR B 421    27036  21524  30434    692   3372  -5361       C  
ATOM   5172  C   TYR B 421      50.515  79.461  82.794  1.00209.18           C  
ANISOU 5172  C   TYR B 421    27149  21196  31131    407   3554  -5413       C  
ATOM   5173  O   TYR B 421      51.230  78.782  82.056  1.00205.00           O  
ANISOU 5173  O   TYR B 421    26659  20649  30580    236   3671  -5097       O  
ATOM   5174  CB  TYR B 421      48.134  79.169  82.015  1.00206.47           C  
ANISOU 5174  CB  TYR B 421    27152  21125  30169    902   3509  -4873       C  
ATOM   5175  CG  TYR B 421      48.501  78.235  80.868  1.00202.62           C  
ANISOU 5175  CG  TYR B 421    26818  20672  29493    805   3626  -4348       C  
ATOM   5176  CD1 TYR B 421      48.070  76.909  80.848  1.00198.15           C  
ANISOU 5176  CD1 TYR B 421    26230  20659  28397    850   3482  -4129       C  
ATOM   5177  CD2 TYR B 421      49.358  78.652  79.844  1.00201.18           C  
ANISOU 5177  CD2 TYR B 421    26790  19969  29680    651   3893  -4092       C  
ATOM   5178  CE1 TYR B 421      48.465  76.043  79.834  1.00193.06           C  
ANISOU 5178  CE1 TYR B 421    25714  20046  27594    760   3574  -3695       C  
ATOM   5179  CE2 TYR B 421      49.737  77.790  78.828  1.00196.53           C  
ANISOU 5179  CE2 TYR B 421    26339  19430  28901    570   4009  -3643       C  
ATOM   5180  CZ  TYR B 421      49.284  76.489  78.828  1.00192.47           C  
ANISOU 5180  CZ  TYR B 421    25800  19473  27856    631   3834  -3460       C  
ATOM   5181  OH  TYR B 421      49.665  75.645  77.831  1.00191.36           O  
ANISOU 5181  OH  TYR B 421    25793  19377  27536    560   3936  -3050       O  
ATOM   5182  N   HIS B 422      50.894  80.637  83.274  1.00215.94           N  
ANISOU 5182  N   HIS B 422    27907  21643  32495    357   3589  -5824       N  
ATOM   5183  CA  HIS B 422      52.231  81.167  83.050  1.00223.30           C  
ANISOU 5183  CA  HIS B 422    28732  22094  34018     71   3757  -5959       C  
ATOM   5184  C   HIS B 422      53.236  80.335  83.828  1.00228.65           C  
ANISOU 5184  C   HIS B 422    29120  23156  34598   -136   3572  -6253       C  
ATOM   5185  O   HIS B 422      54.308  79.965  83.326  1.00237.52           O  
ANISOU 5185  O   HIS B 422    30174  24138  35934   -380   3702  -6119       O  
ATOM   5186  CB  HIS B 422      52.316  82.578  83.622  1.00225.94           C  
ANISOU 5186  CB  HIS B 422    28975  21962  34909     83   3769  -6435       C  
ATOM   5187  CG  HIS B 422      51.561  83.595  82.838  1.00224.10           C  
ANISOU 5187  CG  HIS B 422    29013  21204  34929    257   3977  -6184       C  
ATOM   5188  ND1 HIS B 422      50.616  84.422  83.407  1.00222.86           N  
ANISOU 5188  ND1 HIS B 422    28879  20983  34813    502   3867  -6466       N  
ATOM   5189  CD2 HIS B 422      51.627  83.935  81.528  1.00222.13           C  
ANISOU 5189  CD2 HIS B 422    29036  20460  34903    238   4290  -5677       C  
ATOM   5190  CE1 HIS B 422      50.125  85.223  82.478  1.00223.89           C  
ANISOU 5190  CE1 HIS B 422    29279  20593  35197    628   4085  -6140       C  
ATOM   5191  NE2 HIS B 422      50.724  84.948  81.330  1.00222.22           N  
ANISOU 5191  NE2 HIS B 422    29234  20113  35084    475   4345  -5650       N  
ATOM   5192  N   VAL B 423      52.874  80.055  85.078  1.00229.22           N  
ANISOU 5192  N   VAL B 423    29027  23722  34344    -22   3267  -6663       N  
ATOM   5193  CA  VAL B 423      53.637  79.161  85.942  1.00228.52           C  
ANISOU 5193  CA  VAL B 423    28693  24100  34031   -147   3028  -6937       C  
ATOM   5194  C   VAL B 423      53.764  77.766  85.324  1.00222.61           C  
ANISOU 5194  C   VAL B 423    28014  23715  32853   -209   3045  -6455       C  
ATOM   5195  O   VAL B 423      54.857  77.194  85.270  1.00216.87           O  
ANISOU 5195  O   VAL B 423    27137  23030  32233   -425   3029  -6475       O  
ATOM   5196  CB  VAL B 423      52.987  79.086  87.342  1.00228.92           C  
ANISOU 5196  CB  VAL B 423    28633  24654  33692     55   2721  -7385       C  
ATOM   5197  CG1 VAL B 423      53.608  77.985  88.193  1.00229.10           C  
ANISOU 5197  CG1 VAL B 423    28467  25238  33342    -17   2459  -7569       C  
ATOM   5198  CG2 VAL B 423      53.092  80.437  88.037  1.00232.72           C  
ANISOU 5198  CG2 VAL B 423    29002  24776  34645     90   2672  -7954       C  
ATOM   5199  N   LYS B 424      52.641  77.234  84.858  1.00219.84           N  
ANISOU 5199  N   LYS B 424    27872  23611  32043    -14   3069  -6045       N  
ATOM   5200  CA  LYS B 424      52.587  75.913  84.230  1.00213.94           C  
ANISOU 5200  CA  LYS B 424    27209  23202  30874    -41   3076  -5580       C  
ATOM   5201  C   LYS B 424      53.463  75.836  82.986  1.00207.40           C  
ANISOU 5201  C   LYS B 424    26468  21974  30358   -241   3340  -5224       C  
ATOM   5202  O   LYS B 424      54.208  74.865  82.800  1.00203.61           O  
ANISOU 5202  O   LYS B 424    25905  21699  29758   -393   3316  -5093       O  
ATOM   5203  CB  LYS B 424      51.140  75.629  83.859  1.00216.90           C  
ANISOU 5203  CB  LYS B 424    27792  23790  30828    218   3076  -5242       C  
ATOM   5204  CG  LYS B 424      50.845  74.188  83.534  1.00216.87           C  
ANISOU 5204  CG  LYS B 424    27834  24252  30315    238   3001  -4863       C  
ATOM   5205  CD  LYS B 424      49.347  73.924  83.482  1.00218.98           C  
ANISOU 5205  CD  LYS B 424    28225  24793  30182    504   2942  -4660       C  
ATOM   5206  CE  LYS B 424      49.038  72.428  83.344  1.00218.75           C  
ANISOU 5206  CE  LYS B 424    28193  25260  29659    514   2837  -4346       C  
ATOM   5207  NZ  LYS B 424      47.591  72.102  83.218  1.00219.58           N  
ANISOU 5207  NZ  LYS B 424    28389  25618  29423    755   2788  -4138       N  
ATOM   5208  N   THR B 425      53.379  76.857  82.135  1.00205.82           N  
ANISOU 5208  N   THR B 425    26444  21201  30556   -231   3604  -5063       N  
ATOM   5209  CA  THR B 425      54.162  76.913  80.896  1.00203.37           C  
ANISOU 5209  CA  THR B 425    26257  20464  30551   -402   3916  -4699       C  
ATOM   5210  C   THR B 425      55.656  76.978  81.204  1.00203.99           C  
ANISOU 5210  C   THR B 425    26059  20367  31080   -706   3961  -4999       C  
ATOM   5211  O   THR B 425      56.462  76.205  80.657  1.00207.64           O  
ANISOU 5211  O   THR B 425    26480  20881  31529   -873   4059  -4786       O  
ATOM   5212  CB  THR B 425      53.743  78.096  80.012  1.00204.93           C  
ANISOU 5212  CB  THR B 425    26717  20055  31089   -308   4197  -4477       C  
ATOM   5213  OG1 THR B 425      52.326  78.112  79.915  1.00202.28           O  
ANISOU 5213  OG1 THR B 425    26584  19902  30370     -3   4094  -4300       O  
ATOM   5214  CG2 THR B 425      54.305  77.957  78.599  1.00204.78           C  
ANISOU 5214  CG2 THR B 425    26911  19688  31208   -417   4539  -3976       C  
ATOM   5215  N   ALA B 426      56.011  77.905  82.082  1.00205.01           N  
ANISOU 5215  N   ALA B 426    25987  20285  31622   -767   3879  -5518       N  
ATOM   5216  CA  ALA B 426      57.385  78.031  82.530  1.00207.76           C  
ANISOU 5216  CA  ALA B 426    26021  20479  32437  -1039   3862  -5901       C  
ATOM   5217  C   ALA B 426      57.928  76.703  83.075  1.00204.71           C  
ANISOU 5217  C   ALA B 426    25435  20668  31675  -1112   3604  -5984       C  
ATOM   5218  O   ALA B 426      59.050  76.304  82.752  1.00202.51           O  
ANISOU 5218  O   ALA B 426    24999  20295  31647  -1339   3696  -5964       O  
ATOM   5219  CB  ALA B 426      57.482  79.075  83.620  1.00213.78           C  
ANISOU 5219  CB  ALA B 426    26580  21071  33572  -1032   3697  -6523       C  
ATOM   5220  N   ILE B 427      57.137  76.022  83.901  1.00205.41           N  
ANISOU 5220  N   ILE B 427    25527  21340  31177   -917   3294  -6073       N  
ATOM   5221  CA  ILE B 427      57.610  74.777  84.498  1.00206.27           C  
ANISOU 5221  CA  ILE B 427    25465  21990  30916   -963   3033  -6151       C  
ATOM   5222  C   ILE B 427      57.691  73.639  83.485  1.00194.93           C  
ANISOU 5222  C   ILE B 427    24162  20709  29193  -1009   3163  -5604       C  
ATOM   5223  O   ILE B 427      58.495  72.726  83.643  1.00182.87           O  
ANISOU 5223  O   ILE B 427    22470  19427  27582  -1132   3048  -5629       O  
ATOM   5224  CB  ILE B 427      56.869  74.373  85.781  1.00213.23           C  
ANISOU 5224  CB  ILE B 427    26296  23446  31275   -756   2678  -6431       C  
ATOM   5225  CG1 ILE B 427      57.779  73.456  86.620  1.00214.85           C  
ANISOU 5225  CG1 ILE B 427    26253  24057  31320   -848   2391  -6697       C  
ATOM   5226  CG2 ILE B 427      55.537  73.718  85.469  1.00212.74           C  
ANISOU 5226  CG2 ILE B 427    26480  23725  30627   -536   2683  -6004       C  
ATOM   5227  CD1 ILE B 427      57.313  73.253  88.046  1.00216.85           C  
ANISOU 5227  CD1 ILE B 427    26430  24815  31145   -661   2043  -7082       C  
ATOM   5228  N   PHE B 428      56.870  73.699  82.441  1.00191.66           N  
ANISOU 5228  N   PHE B 428    24043  20143  28634   -897   3386  -5127       N  
ATOM   5229  CA  PHE B 428      57.032  72.787  81.315  1.00186.28           C  
ANISOU 5229  CA  PHE B 428    23507  19505  27765   -945   3551  -4622       C  
ATOM   5230  C   PHE B 428      58.381  73.005  80.670  1.00184.73           C  
ANISOU 5230  C   PHE B 428    23197  18896  28093  -1210   3807  -4611       C  
ATOM   5231  O   PHE B 428      59.106  72.041  80.389  1.00177.90           O  
ANISOU 5231  O   PHE B 428    22239  18211  27144  -1332   3803  -4486       O  
ATOM   5232  CB  PHE B 428      55.952  72.902  80.244  1.00189.04           C  
ANISOU 5232  CB  PHE B 428    24206  19725  27893   -759   3738  -4134       C  
ATOM   5233  CG  PHE B 428      54.636  72.293  80.622  1.00189.19           C  
ANISOU 5233  CG  PHE B 428    24327  20218  27337   -512   3508  -4026       C  
ATOM   5234  CD1 PHE B 428      54.562  71.062  81.254  1.00185.27           C  
ANISOU 5234  CD1 PHE B 428    23705  20281  26405   -497   3251  -4050       C  
ATOM   5235  CD2 PHE B 428      53.455  72.946  80.291  1.00193.22           C  
ANISOU 5235  CD2 PHE B 428    25060  20591  27764   -289   3567  -3876       C  
ATOM   5236  CE1 PHE B 428      53.343  70.507  81.580  1.00185.19           C  
ANISOU 5236  CE1 PHE B 428    23774  20680  25910   -285   3081  -3935       C  
ATOM   5237  CE2 PHE B 428      52.227  72.395  80.608  1.00191.97           C  
ANISOU 5237  CE2 PHE B 428    24964  20852  27124    -68   3377  -3782       C  
ATOM   5238  CZ  PHE B 428      52.170  71.169  81.255  1.00188.08           C  
ANISOU 5238  CZ  PHE B 428    24330  20910  26219    -75   3147  -3809       C  
ATOM   5239  N   HIS B 429      58.724  74.269  80.445  1.00193.71           N  
ANISOU 5239  N   HIS B 429    24331  19470  29797  -1301   4041  -4749       N  
ATOM   5240  CA  HIS B 429      60.018  74.599  79.858  1.00203.24           C  
ANISOU 5240  CA  HIS B 429    25405  20229  31585  -1572   4333  -4760       C  
ATOM   5241  C   HIS B 429      61.171  74.124  80.751  1.00209.39           C  
ANISOU 5241  C   HIS B 429    25780  21216  32560  -1764   4102  -5210       C  
ATOM   5242  O   HIS B 429      62.192  73.633  80.253  1.00215.70           O  
ANISOU 5242  O   HIS B 429    26446  21936  33573  -1958   4250  -5121       O  
ATOM   5243  CB  HIS B 429      60.141  76.111  79.577  1.00208.95           C  
ANISOU 5243  CB  HIS B 429    26177  20280  32930  -1638   4620  -4862       C  
ATOM   5244  CG  HIS B 429      59.420  76.588  78.344  1.00211.89           C  
ANISOU 5244  CG  HIS B 429    26956  20301  33249  -1507   4959  -4332       C  
ATOM   5245  ND1 HIS B 429      59.992  76.550  77.090  1.00214.41           N  
ANISOU 5245  ND1 HIS B 429    27433  20277  33754  -1624   5366  -3911       N  
ATOM   5246  CD2 HIS B 429      58.216  77.198  78.184  1.00214.38           C  
ANISOU 5246  CD2 HIS B 429    27552  20521  33381  -1260   4958  -4178       C  
ATOM   5247  CE1 HIS B 429      59.149  77.056  76.205  1.00216.76           C  
ANISOU 5247  CE1 HIS B 429    28117  20313  33927  -1437   5580  -3499       C  
ATOM   5248  NE2 HIS B 429      58.064  77.460  76.842  1.00217.05           N  
ANISOU 5248  NE2 HIS B 429    28224  20486  33756  -1215   5328  -3657       N  
ATOM   5249  N   MET B 430      61.006  74.253  82.064  1.00213.37           N  
ANISOU 5249  N   MET B 430    26093  21997  32977  -1691   3735  -5696       N  
ATOM   5250  CA  MET B 430      62.033  73.802  82.997  1.00218.60           C  
ANISOU 5250  CA  MET B 430    26389  22895  33774  -1825   3453  -6151       C  
ATOM   5251  C   MET B 430      62.189  72.285  82.996  1.00211.50           C  
ANISOU 5251  C   MET B 430    25466  22526  32366  -1800   3271  -5936       C  
ATOM   5252  O   MET B 430      63.305  71.760  82.997  1.00211.51           O  
ANISOU 5252  O   MET B 430    25224  22552  32587  -1974   3238  -6052       O  
ATOM   5253  CB  MET B 430      61.675  74.216  84.423  1.00226.68           C  
ANISOU 5253  CB  MET B 430    27275  24162  34691  -1692   3073  -6696       C  
ATOM   5254  CG  MET B 430      62.399  75.475  84.883  1.00238.12           C  
ANISOU 5254  CG  MET B 430    28477  25134  36861  -1838   3096  -7229       C  
ATOM   5255  SD  MET B 430      64.117  75.097  85.306  1.00246.20           S  
ANISOU 5255  SD  MET B 430    29039  26143  38362  -2105   2942  -7660       S  
ATOM   5256  CE  MET B 430      64.998  75.432  83.781  1.00245.20           C  
ANISOU 5256  CE  MET B 430    28904  25364  38894  -2397   3511  -7281       C  
ATOM   5257  N   TRP B 431      61.067  71.578  82.993  1.00206.31           N  
ANISOU 5257  N   TRP B 431    25049  22280  31059  -1582   3153  -5628       N  
ATOM   5258  CA  TRP B 431      61.088  70.116  82.940  1.00205.19           C  
ANISOU 5258  CA  TRP B 431    24916  22621  30426  -1544   2993  -5381       C  
ATOM   5259  C   TRP B 431      61.711  69.631  81.653  1.00203.38           C  
ANISOU 5259  C   TRP B 431    24746  22179  30350  -1689   3300  -4981       C  
ATOM   5260  O   TRP B 431      62.316  68.574  81.622  1.00198.12           O  
ANISOU 5260  O   TRP B 431    23960  21770  29545  -1753   3194  -4918       O  
ATOM   5261  CB  TRP B 431      59.704  69.530  83.077  1.00203.48           C  
ANISOU 5261  CB  TRP B 431    24943  22815  29554  -1296   2860  -5106       C  
ATOM   5262  CG  TRP B 431      59.124  69.707  84.414  1.00202.33           C  
ANISOU 5262  CG  TRP B 431    24729  23000  29147  -1141   2546  -5474       C  
ATOM   5263  CD1 TRP B 431      59.790  69.851  85.590  1.00204.81           C  
ANISOU 5263  CD1 TRP B 431    24786  23459  29573  -1176   2271  -5991       C  
ATOM   5264  CD2 TRP B 431      57.742  69.712  84.734  1.00200.68           C  
ANISOU 5264  CD2 TRP B 431    24710  23047  28490   -906   2469  -5360       C  
ATOM   5265  NE1 TRP B 431      58.905  69.962  86.625  1.00204.06           N  
ANISOU 5265  NE1 TRP B 431    24737  23700  29095   -970   2043  -6198       N  
ATOM   5266  CE2 TRP B 431      57.635  69.874  86.126  1.00201.63           C  
ANISOU 5266  CE2 TRP B 431    24690  23464  28452   -810   2175  -5814       C  
ATOM   5267  CE3 TRP B 431      56.575  69.590  83.976  1.00199.88           C  
ANISOU 5267  CE3 TRP B 431    24878  22958  28109   -757   2616  -4930       C  
ATOM   5268  CZ2 TRP B 431      56.405  69.927  86.780  1.00201.55           C  
ANISOU 5268  CZ2 TRP B 431    24799  23759  28021   -581   2064  -5838       C  
ATOM   5269  CZ3 TRP B 431      55.348  69.638  84.623  1.00198.92           C  
ANISOU 5269  CZ3 TRP B 431    24846  23130  27605   -536   2484  -4967       C  
ATOM   5270  CH2 TRP B 431      55.275  69.802  86.014  1.00199.97           C  
ANISOU 5270  CH2 TRP B 431    24832  23554  27592   -456   2230  -5411       C  
ATOM   5271  N   THR B 432      61.570  70.414  80.589  1.00205.30           N  
ANISOU 5271  N   THR B 432    25185  21943  30873  -1726   3685  -4710       N  
ATOM   5272  CA  THR B 432      62.217  70.086  79.325  1.00205.74           C  
ANISOU 5272  CA  THR B 432    25316  21753  31102  -1860   4031  -4342       C  
ATOM   5273  C   THR B 432      63.715  70.392  79.397  1.00212.36           C  
ANISOU 5273  C   THR B 432    25815  22287  32583  -2136   4156  -4651       C  
ATOM   5274  O   THR B 432      64.533  69.740  78.731  1.00213.31           O  
ANISOU 5274  O   THR B 432    25859  22381  32807  -2269   4320  -4481       O  
ATOM   5275  CB  THR B 432      61.627  70.914  78.182  1.00205.12           C  
ANISOU 5275  CB  THR B 432    25578  21232  31126  -1796   4421  -3955       C  
ATOM   5276  OG1 THR B 432      60.204  70.922  78.291  1.00199.25           O  
ANISOU 5276  OG1 THR B 432    25096  20708  29901  -1532   4272  -3786       O  
ATOM   5277  CG2 THR B 432      62.012  70.322  76.850  1.00204.41           C  
ANISOU 5277  CG2 THR B 432    25653  21029  30982  -1851   4740  -3493       C  
ATOM   5278  N   GLN B 433      64.065  71.392  80.202  1.00217.62           N  
ANISOU 5278  N   GLN B 433    26264  22718  33701  -2219   4077  -5125       N  
ATOM   5279  CA  GLN B 433      65.466  71.773  80.400  1.00219.43           C  
ANISOU 5279  CA  GLN B 433    26116  22643  34612  -2484   4154  -5502       C  
ATOM   5280  C   GLN B 433      66.223  70.807  81.282  1.00212.51           C  
ANISOU 5280  C   GLN B 433    24909  22199  33633  -2527   3763  -5838       C  
ATOM   5281  O   GLN B 433      67.335  70.420  80.956  1.00208.10           O  
ANISOU 5281  O   GLN B 433    24112  21542  33412  -2714   3870  -5885       O  
ATOM   5282  CB  GLN B 433      65.620  73.188  80.916  1.00229.10           C  
ANISOU 5282  CB  GLN B 433    27204  23428  36415  -2563   4198  -5920       C  
ATOM   5283  CG  GLN B 433      66.072  74.147  79.835  1.00236.39           C  
ANISOU 5283  CG  GLN B 433    28195  23665  37955  -2745   4740  -5710       C  
ATOM   5284  CD  GLN B 433      66.382  75.500  80.418  1.00248.62           C  
ANISOU 5284  CD  GLN B 433    29542  24750  40169  -2858   4762  -6184       C  
ATOM   5285  OE1 GLN B 433      67.365  75.644  81.139  1.00257.09           O  
ANISOU 5285  OE1 GLN B 433    30204  25769  41708  -3028   4590  -6699       O  
ATOM   5286  NE2 GLN B 433      65.538  76.502  80.132  1.00256.09           N  
ANISOU 5286  NE2 GLN B 433    30766  25355  41180  -2752   4948  -6037       N  
ATOM   5287  N   ASP B 434      65.607  70.422  82.402  1.00209.54           N  
ANISOU 5287  N   ASP B 434    24525  22302  32786  -2339   3316  -6065       N  
ATOM   5288  CA  ASP B 434      66.172  69.415  83.299  1.00208.37           C  
ANISOU 5288  CA  ASP B 434    24128  22625  32416  -2320   2901  -6336       C  
ATOM   5289  C   ASP B 434      65.309  68.142  83.235  1.00202.03           C  
ANISOU 5289  C   ASP B 434    23571  22354  30837  -2121   2738  -5933       C  
ATOM   5290  O   ASP B 434      64.443  67.941  84.082  1.00191.42           O  
ANISOU 5290  O   ASP B 434    22331  21386  29011  -1922   2448  -6009       O  
ATOM   5291  CB  ASP B 434      66.235  69.984  84.711  1.00214.05           C  
ANISOU 5291  CB  ASP B 434    24641  23471  33217  -2255   2513  -6946       C  
ATOM   5292  CG  ASP B 434      67.010  71.288  84.783  1.00221.59           C  
ANISOU 5292  CG  ASP B 434    25345  23870  34977  -2449   2662  -7371       C  
ATOM   5293  OD1 ASP B 434      66.794  72.035  85.761  1.00224.17           O  
ANISOU 5293  OD1 ASP B 434    25586  24200  35386  -2370   2420  -7829       O  
ATOM   5294  OD2 ASP B 434      67.814  71.576  83.865  1.00226.64           O  
ANISOU 5294  OD2 ASP B 434    25876  24064  36172  -2676   3032  -7250       O  
ATOM   5295  N   PRO B 435      65.558  67.278  82.235  1.00206.50           N  
ANISOU 5295  N   PRO B 435    24219  22942  31299  -2177   2936  -5516       N  
ATOM   5296  CA  PRO B 435      64.746  66.099  81.986  1.00207.08           C  
ANISOU 5296  CA  PRO B 435    24528  23438  30712  -2009   2832  -5102       C  
ATOM   5297  C   PRO B 435      64.974  65.019  83.015  1.00206.06           C  
ANISOU 5297  C   PRO B 435    24236  23826  30232  -1930   2389  -5293       C  
ATOM   5298  O   PRO B 435      64.028  64.275  83.360  1.00210.13           O  
ANISOU 5298  O   PRO B 435    24932  24751  30157  -1743   2194  -5092       O  
ATOM   5299  CB  PRO B 435      65.192  65.662  80.588  1.00206.88           C  
ANISOU 5299  CB  PRO B 435    24592  23194  30817  -2120   3198  -4691       C  
ATOM   5300  CG  PRO B 435      65.892  66.848  80.009  1.00207.31           C  
ANISOU 5300  CG  PRO B 435    24561  22664  31543  -2314   3577  -4796       C  
ATOM   5301  CD  PRO B 435      66.591  67.399  81.197  1.00209.78           C  
ANISOU 5301  CD  PRO B 435    24521  22952  32234  -2401   3311  -5395       C  
ATOM   5302  N   GLN B 436      66.206  64.947  83.520  1.00201.19           N  
ANISOU 5302  N   GLN B 436    23275  23181  29987  -2062   2231  -5680       N  
ATOM   5303  CA  GLN B 436      66.584  63.887  84.475  1.00195.38           C  
ANISOU 5303  CA  GLN B 436    22374  22914  28945  -1979   1795  -5865       C  
ATOM   5304  C   GLN B 436      65.766  63.937  85.761  1.00195.23           C  
ANISOU 5304  C   GLN B 436    22434  23276  28465  -1768   1434  -6079       C  
ATOM   5305  O   GLN B 436      65.586  65.008  86.370  1.00200.12           O  
ANISOU 5305  O   GLN B 436    23014  23758  29265  -1746   1387  -6428       O  
ATOM   5306  CB  GLN B 436      68.083  63.910  84.756  1.00196.35           C  
ANISOU 5306  CB  GLN B 436    22093  22899  29610  -2149   1682  -6279       C  
ATOM   5307  CG  GLN B 436      68.878  63.117  83.744  1.00193.90           C  
ANISOU 5307  CG  GLN B 436    21694  22488  29489  -2285   1894  -6015       C  
ATOM   5308  CD  GLN B 436      68.689  61.609  83.897  1.00192.08           C  
ANISOU 5308  CD  GLN B 436    21543  22732  28706  -2146   1634  -5762       C  
ATOM   5309  OE1 GLN B 436      68.419  61.100  84.985  1.00190.29           O  
ANISOU 5309  OE1 GLN B 436    21311  22909  28081  -1984   1224  -5916       O  
ATOM   5310  NE2 GLN B 436      68.833  60.882  82.797  1.00193.32           N  
ANISOU 5310  NE2 GLN B 436    21785  22831  28835  -2201   1883  -5368       N  
ATOM   5311  N   ASP B 437      65.267  62.762  86.153  1.00189.11           N  
ANISOU 5311  N   ASP B 437    21777  22971  27101  -1610   1197  -5862       N  
ATOM   5312  CA  ASP B 437      64.478  62.610  87.375  1.00187.43           C  
ANISOU 5312  CA  ASP B 437    21661  23178  26374  -1394    877  -6004       C  
ATOM   5313  C   ASP B 437      65.350  62.887  88.583  1.00188.15           C  
ANISOU 5313  C   ASP B 437    21483  23380  26624  -1375    511  -6585       C  
ATOM   5314  O   ASP B 437      64.872  63.351  89.620  1.00185.53           O  
ANISOU 5314  O   ASP B 437    21190  23241  26059  -1223    301  -6874       O  
ATOM   5315  CB  ASP B 437      63.916  61.187  87.464  1.00187.17           C  
ANISOU 5315  CB  ASP B 437    21785  23587  25741  -1259    732  -5618       C  
ATOM   5316  CG  ASP B 437      62.910  60.870  86.360  1.00188.70           C  
ANISOU 5316  CG  ASP B 437    22250  23718  25726  -1241   1036  -5074       C  
ATOM   5317  OD1 ASP B 437      62.364  61.801  85.727  1.00191.39           O  
ANISOU 5317  OD1 ASP B 437    22718  23753  26246  -1269   1318  -4987       O  
ATOM   5318  OD2 ASP B 437      62.649  59.676  86.123  1.00188.76           O  
ANISOU 5318  OD2 ASP B 437    22347  23977  25392  -1188    978  -4735       O  
ATOM   5319  N   SER B 438      66.639  62.598  88.433  1.00193.16           N  
ANISOU 5319  N   SER B 438    21837  23895  27658  -1517    433  -6772       N  
ATOM   5320  CA  SER B 438      67.623  62.876  89.481  1.00202.63           C  
ANISOU 5320  CA  SER B 438    22732  25155  29101  -1510     66  -7366       C  
ATOM   5321  C   SER B 438      67.732  64.369  89.751  1.00209.61           C  
ANISOU 5321  C   SER B 438    23499  25687  30456  -1581    136  -7813       C  
ATOM   5322  O   SER B 438      68.086  64.770  90.871  1.00212.87           O  
ANISOU 5322  O   SER B 438    23750  26227  30902  -1491   -215  -8341       O  
ATOM   5323  CB  SER B 438      68.990  62.300  89.099  1.00204.79           C  
ANISOU 5323  CB  SER B 438    22699  25315  29797  -1666     13  -7460       C  
ATOM   5324  OG  SER B 438      69.508  62.916  87.931  1.00207.34           O  
ANISOU 5324  OG  SER B 438    22907  25122  30747  -1915    440  -7378       O  
ATOM   5325  N   GLN B 439      67.433  65.175  88.728  1.00210.74           N  
ANISOU 5325  N   GLN B 439    23732  25384  30955  -1727    579  -7605       N  
ATOM   5326  CA  GLN B 439      67.461  66.639  88.849  1.00209.10           C  
ANISOU 5326  CA  GLN B 439    23439  24769  31241  -1807    705  -7972       C  
ATOM   5327  C   GLN B 439      66.185  67.133  89.501  1.00205.83           C  
ANISOU 5327  C   GLN B 439    23284  24544  30375  -1592    631  -7997       C  
ATOM   5328  O   GLN B 439      66.027  68.343  89.686  1.00205.16           O  
ANISOU 5328  O   GLN B 439    23169  24156  30626  -1616    711  -8297       O  
ATOM   5329  CB  GLN B 439      67.585  67.349  87.481  1.00206.48           C  
ANISOU 5329  CB  GLN B 439    23142  23859  31452  -2029   1236  -7699       C  
ATOM   5330  CG  GLN B 439      68.834  67.067  86.663  1.00202.77           C  
ANISOU 5330  CG  GLN B 439    22414  23101  31525  -2271   1434  -7659       C  
ATOM   5331  CD  GLN B 439      68.764  67.702  85.276  1.00199.58           C  
ANISOU 5331  CD  GLN B 439    22139  22172  31520  -2446   2005  -7290       C  
ATOM   5332  OE1 GLN B 439      68.110  67.186  84.369  1.00196.82           O  
ANISOU 5332  OE1 GLN B 439    22084  21871  30828  -2399   2254  -6740       O  
ATOM   5333  NE2 GLN B 439      69.429  68.837  85.114  1.00200.68           N  
ANISOU 5333  NE2 GLN B 439    22063  21798  32387  -2640   2210  -7596       N  
ATOM   5334  N   TRP B 440      65.299  66.207  89.865  1.00201.21           N  
ANISOU 5334  N   TRP B 440    22937  24447  29065  -1386    485  -7698       N  
ATOM   5335  CA  TRP B 440      64.079  66.543  90.577  1.00200.20           C  
ANISOU 5335  CA  TRP B 440    23036  24567  28462  -1165    405  -7725       C  
ATOM   5336  C   TRP B 440      63.882  65.580  91.757  1.00200.29           C  
ANISOU 5336  C   TRP B 440    23091  25186  27822   -942      0  -7808       C  
ATOM   5337  O   TRP B 440      62.791  65.059  91.970  1.00199.89           O  
ANISOU 5337  O   TRP B 440    23289  25470  27187   -770      9  -7498       O  
ATOM   5338  CB  TRP B 440      62.853  66.526  89.638  1.00196.97           C  
ANISOU 5338  CB  TRP B 440    22941  24080  27819  -1128    761  -7166       C  
ATOM   5339  CG  TRP B 440      62.986  67.480  88.492  1.00198.58           C  
ANISOU 5339  CG  TRP B 440    23156  23695  28600  -1309   1162  -7049       C  
ATOM   5340  CD1 TRP B 440      63.385  67.179  87.227  1.00196.36           C  
ANISOU 5340  CD1 TRP B 440    22897  23137  28573  -1477   1466  -6667       C  
ATOM   5341  CD2 TRP B 440      62.751  68.891  88.512  1.00202.31           C  
ANISOU 5341  CD2 TRP B 440    23628  23771  29467  -1330   1309  -7312       C  
ATOM   5342  NE1 TRP B 440      63.399  68.308  86.447  1.00198.39           N  
ANISOU 5342  NE1 TRP B 440    23189  22855  29334  -1597   1811  -6645       N  
ATOM   5343  CE2 TRP B 440      63.023  69.378  87.215  1.00202.54           C  
ANISOU 5343  CE2 TRP B 440    23695  23281  29978  -1517   1718  -7037       C  
ATOM   5344  CE3 TRP B 440      62.325  69.790  89.496  1.00204.85           C  
ANISOU 5344  CE3 TRP B 440    23934  24122  29774  -1198   1143  -7752       C  
ATOM   5345  CZ2 TRP B 440      62.897  70.729  86.878  1.00204.92           C  
ANISOU 5345  CZ2 TRP B 440    24020  23072  30768  -1582   1964  -7168       C  
ATOM   5346  CZ3 TRP B 440      62.183  71.132  89.157  1.00207.87           C  
ANISOU 5346  CZ3 TRP B 440    24325  23999  30656  -1264   1374  -7907       C  
ATOM   5347  CH2 TRP B 440      62.485  71.589  87.860  1.00208.63           C  
ANISOU 5347  CH2 TRP B 440    24457  23559  31251  -1460   1780  -7609       C  
ATOM   5348  N   ASP B 441      64.952  65.355  92.523  1.00202.28           N  
ANISOU 5348  N   ASP B 441    23096  25568  28192   -939   -353  -8231       N  
ATOM   5349  CA  ASP B 441      64.830  64.547  93.722  1.00203.24           C  
ANISOU 5349  CA  ASP B 441    23275  26247  27697   -702   -756  -8348       C  
ATOM   5350  C   ASP B 441      64.256  65.424  94.830  1.00211.08           C  
ANISOU 5350  C   ASP B 441    24334  27388  28477   -507   -927  -8781       C  
ATOM   5351  O   ASP B 441      64.646  66.582  94.978  1.00220.25           O  
ANISOU 5351  O   ASP B 441    25329  28223  30131   -578   -935  -9248       O  
ATOM   5352  CB  ASP B 441      66.145  63.943  94.163  1.00200.27           C  
ANISOU 5352  CB  ASP B 441    22633  25985  27475   -727  -1110  -8638       C  
ATOM   5353  CG  ASP B 441      65.949  62.877  95.226  1.00197.78           C  
ANISOU 5353  CG  ASP B 441    22446  26259  26443   -467  -1487  -8597       C  
ATOM   5354  OD1 ASP B 441      65.770  63.216  96.437  1.00198.53           O  
ANISOU 5354  OD1 ASP B 441    22579  26632  26218   -251  -1788  -8994       O  
ATOM   5355  OD2 ASP B 441      65.927  61.691  94.825  1.00194.26           O  
ANISOU 5355  OD2 ASP B 441    22084  25990  25734   -470  -1461  -8145       O  
ATOM   5356  N   PRO B 442      63.299  64.882  95.598  1.00211.23           N  
ANISOU 5356  N   PRO B 442    24598  27886  27771   -259  -1040  -8624       N  
ATOM   5357  CA  PRO B 442      62.749  65.505  96.795  1.00217.29           C  
ANISOU 5357  CA  PRO B 442    25452  28906  28201    -23  -1235  -9026       C  
ATOM   5358  C   PRO B 442      63.773  66.173  97.708  1.00227.12           C  
ANISOU 5358  C   PRO B 442    26449  30115  29730     19  -1616  -9758       C  
ATOM   5359  O   PRO B 442      63.547  67.283  98.182  1.00232.79           O  
ANISOU 5359  O   PRO B 442    27139  30703  30605     83  -1644 -10195       O  
ATOM   5360  CB  PRO B 442      62.102  64.326  97.504  1.00213.55           C  
ANISOU 5360  CB  PRO B 442    25208  29017  26914    208  -1379  -8716       C  
ATOM   5361  CG  PRO B 442      61.582  63.491  96.387  1.00206.72           C  
ANISOU 5361  CG  PRO B 442    24468  28090  25982     83  -1060  -8034       C  
ATOM   5362  CD  PRO B 442      62.575  63.628  95.278  1.00204.94           C  
ANISOU 5362  CD  PRO B 442    24026  27402  26437   -195   -932  -8002       C  
ATOM   5363  N   ARG B 443      64.890  65.502  97.941  1.00230.80           N  
ANISOU 5363  N   ARG B 443    26726  30686  30280     -6  -1921  -9907       N  
ATOM   5364  CA  ARG B 443      65.957  66.063  98.788  1.00239.27           C  
ANISOU 5364  CA  ARG B 443    27524  31725  31660     38  -2334 -10632       C  
ATOM   5365  C   ARG B 443      66.555  67.343  98.229  1.00243.65           C  
ANISOU 5365  C   ARG B 443    27800  31674  33100   -206  -2180 -11022       C  
ATOM   5366  O   ARG B 443      67.157  68.108  98.975  1.00249.10           O  
ANISOU 5366  O   ARG B 443    28283  32288  34075   -156  -2479 -11684       O  
ATOM   5367  CB  ARG B 443      67.030  65.013  99.047  1.00243.44           C  
ANISOU 5367  CB  ARG B 443    27893  32471  32129     61  -2687 -10670       C  
ATOM   5368  CG  ARG B 443      66.511  63.994 100.054  1.00246.48           C  
ANISOU 5368  CG  ARG B 443    28553  33490  31605    383  -2961 -10494       C  
ATOM   5369  CD  ARG B 443      67.406  62.804 100.254  1.00252.35           C  
ANISOU 5369  CD  ARG B 443    29205  34473  32201    435  -3285 -10409       C  
ATOM   5370  NE  ARG B 443      67.000  61.700  99.394  1.00253.10           N  
ANISOU 5370  NE  ARG B 443    29456  34617  32094    341  -3004  -9684       N  
ATOM   5371  CZ  ARG B 443      66.990  60.388  99.734  1.00256.97           C  
ANISOU 5371  CZ  ARG B 443    30095  35499  32041    496  -3186  -9340       C  
ATOM   5372  NH1 ARG B 443      67.319  59.990 100.968  1.00261.18           N  
ANISOU 5372  NH1 ARG B 443    30684  36448  32105    782  -3651  -9622       N  
ATOM   5373  NH2 ARG B 443      66.592  59.488  98.838  1.00255.40           N  
ANISOU 5373  NH2 ARG B 443    30015  35273  31754    380  -2897  -8705       N  
ATOM   5374  N   ASN B 444      66.367  67.571  96.933  1.00244.34           N  
ANISOU 5374  N   ASN B 444    27895  31330  33611   -458  -1716 -10611       N  
ATOM   5375  CA  ASN B 444      66.821  68.808  96.298  1.00250.19           C  
ANISOU 5375  CA  ASN B 444    28416  31450  35195   -700  -1484 -10887       C  
ATOM   5376  C   ASN B 444      65.648  69.737  96.046  1.00250.62           C  
ANISOU 5376  C   ASN B 444    28697  31307  35217   -665  -1162 -10764       C  
ATOM   5377  O   ASN B 444      65.663  70.465  95.059  1.00253.29           O  
ANISOU 5377  O   ASN B 444    28993  31120  36124   -881   -787 -10627       O  
ATOM   5378  CB  ASN B 444      67.464  68.528  94.920  1.00251.16           C  
ANISOU 5378  CB  ASN B 444    28403  31163  35863  -1009  -1133 -10498       C  
ATOM   5379  CG  ASN B 444      68.247  67.237  94.866  1.00253.61           C  
ANISOU 5379  CG  ASN B 444    28603  31740  36017  -1023  -1333 -10325       C  
ATOM   5380  OD1 ASN B 444      68.693  66.713  95.896  1.00261.83           O  
ANISOU 5380  OD1 ASN B 444    29561  33170  36750   -844  -1796 -10644       O  
ATOM   5381  ND2 ASN B 444      68.408  66.703  93.647  1.00248.25           N  
ANISOU 5381  ND2 ASN B 444    27939  30853  35532  -1219   -986  -9813       N  
ATOM   5382  N   LEU B 445      64.638  69.698  96.922  1.00248.42           N  
ANISOU 5382  N   LEU B 445    28664  31446  34275   -384  -1294 -10799       N  
ATOM   5383  CA  LEU B 445      63.436  70.501  96.704  1.00241.74           C  
ANISOU 5383  CA  LEU B 445    28039  30455  33356   -320   -996 -10664       C  
ATOM   5384  C   LEU B 445      63.763  71.985  96.604  1.00244.97           C  
ANISOU 5384  C   LEU B 445    28263  30311  34503   -444   -913 -11153       C  
ATOM   5385  O   LEU B 445      63.546  72.600  95.558  1.00241.71           O  
ANISOU 5385  O   LEU B 445    27878  29407  34552   -626   -519 -10895       O  
ATOM   5386  CB  LEU B 445      62.414  70.281  97.819  1.00236.60           C  
ANISOU 5386  CB  LEU B 445    27629  30354  31912     12  -1178 -10733       C  
ATOM   5387  CG  LEU B 445      61.090  71.050  97.742  1.00229.38           C  
ANISOU 5387  CG  LEU B 445    26934  29365  30855    125   -905 -10628       C  
ATOM   5388  CD1 LEU B 445      60.260  70.625  96.540  1.00222.50           C  
ANISOU 5388  CD1 LEU B 445    26258  28370  29911     27   -486  -9900       C  
ATOM   5389  CD2 LEU B 445      60.303  70.810  99.007  1.00227.08           C  
ANISOU 5389  CD2 LEU B 445    26825  29649  29804    458  -1123 -10800       C  
ATOM   5390  N   SER B 446      64.316  72.530  97.685  1.00247.89           N  
ANISOU 5390  N   SER B 446    28448  30754  34986   -338  -1295 -11859       N  
ATOM   5391  CA  SER B 446      64.637  73.942  97.832  1.00251.57           C  
ANISOU 5391  CA  SER B 446    28716  30736  36131   -420  -1298 -12437       C  
ATOM   5392  C   SER B 446      65.394  74.509  96.628  1.00252.86           C  
ANISOU 5392  C   SER B 446    28662  30203  37210   -780   -962 -12331       C  
ATOM   5393  O   SER B 446      65.077  75.584  96.096  1.00256.56           O  
ANISOU 5393  O   SER B 446    29145  30164  38170   -888   -661 -12354       O  
ATOM   5394  CB  SER B 446      65.509  74.149  99.085  1.00255.18           C  
ANISOU 5394  CB  SER B 446    28924  31388  36642   -293  -1838 -13226       C  
ATOM   5395  OG  SER B 446      64.954  73.506 100.220  1.00254.50           O  
ANISOU 5395  OG  SER B 446    29050  31980  35669     51  -2162 -13307       O  
ATOM   5396  N   SER B 447      66.430  73.784  96.227  1.00251.71           N  
ANISOU 5396  N   SER B 447    28308  30031  37298   -958  -1013 -12228       N  
ATOM   5397  CA  SER B 447      67.251  74.206  95.098  1.00254.07           C  
ANISOU 5397  CA  SER B 447    28383  29703  38446  -1304   -676 -12116       C  
ATOM   5398  C   SER B 447      66.444  74.146  93.813  1.00253.59           C  
ANISOU 5398  C   SER B 447    28609  29406  38337  -1403   -139 -11372       C  
ATOM   5399  O   SER B 447      66.482  75.093  93.013  1.00255.26           O  
ANISOU 5399  O   SER B 447    28791  29024  39170  -1592    227 -11311       O  
ATOM   5400  CB  SER B 447      68.519  73.366  95.007  1.00252.65           C  
ANISOU 5400  CB  SER B 447    27908  29600  38485  -1445   -861 -12182       C  
ATOM   5401  OG  SER B 447      68.250  72.035  95.399  1.00249.05           O  
ANISOU 5401  OG  SER B 447    27628  29774  37225  -1247  -1093 -11884       O  
ATOM   5402  N   CYS B 448      65.704  73.049  93.628  1.00252.58           N  
ANISOU 5402  N   CYS B 448    28763  29732  37474  -1264   -100 -10818       N  
ATOM   5403  CA  CYS B 448      64.867  72.881  92.441  1.00250.33           C  
ANISOU 5403  CA  CYS B 448    28765  29289  37057  -1317    354 -10117       C  
ATOM   5404  C   CYS B 448      63.909  74.044  92.328  1.00246.78           C  
ANISOU 5404  C   CYS B 448    28492  28539  36731  -1245    572 -10148       C  
ATOM   5405  O   CYS B 448      63.829  74.703  91.270  1.00245.22           O  
ANISOU 5405  O   CYS B 448    28356  27813  37004  -1407    976  -9881       O  
ATOM   5406  CB  CYS B 448      64.025  71.596  92.521  1.00252.67           C  
ANISOU 5406  CB  CYS B 448    29337  30174  36491  -1124    288  -9619       C  
ATOM   5407  SG  CYS B 448      64.875  70.050  92.135  1.00258.94           S  
ANISOU 5407  SG  CYS B 448    30035  31246  37104  -1221    194  -9285       S  
ATOM   5408  N   PHE B 449      63.184  74.307  93.415  1.00243.17           N  
ANISOU 5408  N   PHE B 449    28128  28415  35849   -989    313 -10471       N  
ATOM   5409  CA  PHE B 449      62.241  75.431  93.464  1.00242.57           C  
ANISOU 5409  CA  PHE B 449    28203  28091  35870   -882    471 -10575       C  
ATOM   5410  C   PHE B 449      62.943  76.744  93.135  1.00245.48           C  
ANISOU 5410  C   PHE B 449    28355  27761  37155  -1092    619 -10949       C  
ATOM   5411  O   PHE B 449      62.332  77.650  92.542  1.00244.45           O  
ANISOU 5411  O   PHE B 449    28364  27201  37313  -1110    927 -10803       O  
ATOM   5412  CB  PHE B 449      61.633  75.535  94.864  1.00244.33           C  
ANISOU 5412  CB  PHE B 449    28481  28790  35561   -581    116 -11018       C  
ATOM   5413  CG  PHE B 449      60.584  76.609  95.002  1.00247.71           C  
ANISOU 5413  CG  PHE B 449    29067  29030  36022   -432    256 -11142       C  
ATOM   5414  CD1 PHE B 449      59.406  76.545  94.268  1.00245.13           C  
ANISOU 5414  CD1 PHE B 449    29024  28683  35429   -355    575 -10582       C  
ATOM   5415  CD2 PHE B 449      60.760  77.677  95.880  1.00251.89           C  
ANISOU 5415  CD2 PHE B 449    29450  29405  36851   -352     48 -11843       C  
ATOM   5416  CE1 PHE B 449      58.428  77.519  94.390  1.00244.11           C  
ANISOU 5416  CE1 PHE B 449    29030  28381  35340   -201    694 -10698       C  
ATOM   5417  CE2 PHE B 449      59.786  78.659  96.017  1.00251.80           C  
ANISOU 5417  CE2 PHE B 449    29579  29216  36877   -201    173 -11970       C  
ATOM   5418  CZ  PHE B 449      58.611  78.575  95.269  1.00248.77           C  
ANISOU 5418  CZ  PHE B 449    29478  28815  36228   -123    501 -11387       C  
ATOM   5419  N   ASP B 450      64.209  76.866  93.534  1.00248.48           N  
ANISOU 5419  N   ASP B 450    28387  28010  38013  -1243    395 -11441       N  
ATOM   5420  CA  ASP B 450      64.938  78.090  93.245  1.00252.67           C  
ANISOU 5420  CA  ASP B 450    28671  27852  39480  -1468    541 -11819       C  
ATOM   5421  C   ASP B 450      65.221  78.159  91.759  1.00253.14           C  
ANISOU 5421  C   ASP B 450    28773  27393  40016  -1738   1052 -11259       C  
ATOM   5422  O   ASP B 450      65.045  79.212  91.142  1.00259.35           O  
ANISOU 5422  O   ASP B 450    29606  27593  41341  -1846   1382 -11205       O  
ATOM   5423  CB  ASP B 450      66.219  78.167  94.052  1.00252.95           C  
ANISOU 5423  CB  ASP B 450    28292  27886  39929  -1558    155 -12509       C  
ATOM   5424  CG  ASP B 450      66.720  79.584  94.146  1.00255.71           C  
ANISOU 5424  CG  ASP B 450    28389  27596  41172  -1710    205 -13067       C  
ATOM   5425  OD1 ASP B 450      67.781  79.852  93.564  1.00254.45           O  
ANISOU 5425  OD1 ASP B 450    27938  26957  41785  -2009    372 -13148       O  
ATOM   5426  OD2 ASP B 450      66.025  80.436  94.762  1.00259.40           O  
ANISOU 5426  OD2 ASP B 450    28950  28017  41591  -1534    107 -13408       O  
ATOM   5427  N   LYS B 451      65.632  77.027  91.187  1.00247.49           N  
ANISOU 5427  N   LYS B 451    28061  26897  39075  -1830   1120 -10830       N  
ATOM   5428  CA  LYS B 451      65.978  76.961  89.770  1.00243.40           C  
ANISOU 5428  CA  LYS B 451    27589  25945  38946  -2072   1602 -10292       C  
ATOM   5429  C   LYS B 451      64.820  77.511  88.953  1.00245.06           C  
ANISOU 5429  C   LYS B 451    28174  25895  39039  -1993   1985  -9804       C  
ATOM   5430  O   LYS B 451      64.963  78.536  88.268  1.00248.78           O  
ANISOU 5430  O   LYS B 451    28645  25731  40146  -2146   2333  -9762       O  
ATOM   5431  CB  LYS B 451      66.335  75.524  89.347  1.00234.51           C  
ANISOU 5431  CB  LYS B 451    26480  25210  37411  -2106   1584  -9870       C  
ATOM   5432  CG  LYS B 451      67.042  75.424  88.001  1.00232.03           C  
ANISOU 5432  CG  LYS B 451    26118  24454  37587  -2382   2037  -9455       C  
ATOM   5433  CD  LYS B 451      67.908  74.166  87.868  1.00226.92           C  
ANISOU 5433  CD  LYS B 451    25296  24120  36803  -2467   1916  -9338       C  
ATOM   5434  CE  LYS B 451      68.843  74.240  86.659  1.00224.76           C  
ANISOU 5434  CE  LYS B 451    24883  23350  37163  -2766   2364  -9081       C  
ATOM   5435  NZ  LYS B 451      69.803  73.110  86.611  1.00221.30           N  
ANISOU 5435  NZ  LYS B 451    24210  23180  36692  -2854   2224  -9070       N  
ATOM   5436  N   LEU B 452      63.668  76.853  89.084  1.00244.31           N  
ANISOU 5436  N   LEU B 452    28387  26288  38149  -1741   1903  -9463       N  
ATOM   5437  CA  LEU B 452      62.422  77.328  88.499  1.00244.40           C  
ANISOU 5437  CA  LEU B 452    28748  26151  37960  -1599   2171  -9064       C  
ATOM   5438  C   LEU B 452      62.250  78.825  88.742  1.00248.21           C  
ANISOU 5438  C   LEU B 452    29190  26124  38993  -1598   2246  -9457       C  
ATOM   5439  O   LEU B 452      62.080  79.600  87.785  1.00249.35           O  
ANISOU 5439  O   LEU B 452    29472  25708  39560  -1688   2634  -9175       O  
ATOM   5440  CB  LEU B 452      61.251  76.586  89.150  1.00242.96           C  
ANISOU 5440  CB  LEU B 452    28784  26625  36905  -1298   1929  -8933       C  
ATOM   5441  CG  LEU B 452      59.829  77.029  88.818  1.00242.97           C  
ANISOU 5441  CG  LEU B 452    29110  26585  36621  -1091   2106  -8625       C  
ATOM   5442  CD1 LEU B 452      59.537  76.794  87.338  1.00240.41           C  
ANISOU 5442  CD1 LEU B 452    29027  25996  36322  -1164   2503  -7933       C  
ATOM   5443  CD2 LEU B 452      58.867  76.270  89.719  1.00242.49           C  
ANISOU 5443  CD2 LEU B 452    29164  27209  35759   -817   1824  -8632       C  
ATOM   5444  N   LEU B 453      62.323  79.217  90.019  1.00250.85           N  
ANISOU 5444  N   LEU B 453    29344  26647  39321  -1486   1872 -10111       N  
ATOM   5445  CA  LEU B 453      62.145  80.620  90.394  1.00256.54           C  
ANISOU 5445  CA  LEU B 453    30006  26918  40548  -1460   1886 -10567       C  
ATOM   5446  C   LEU B 453      63.046  81.482  89.537  1.00261.74           C  
ANISOU 5446  C   LEU B 453    30507  26799  42140  -1768   2232 -10567       C  
ATOM   5447  O   LEU B 453      62.586  82.397  88.847  1.00263.68           O  
ANISOU 5447  O   LEU B 453    30925  26521  42740  -1786   2565 -10356       O  
ATOM   5448  CB  LEU B 453      62.451  80.866  91.873  1.00260.60           C  
ANISOU 5448  CB  LEU B 453    30275  27714  41025  -1342   1408 -11355       C  
ATOM   5449  CG  LEU B 453      61.359  81.636  92.598  1.00262.83           C  
ANISOU 5449  CG  LEU B 453    30711  28075  41077  -1067   1293 -11643       C  
ATOM   5450  CD1 LEU B 453      60.192  80.719  92.881  1.00258.89           C  
ANISOU 5450  CD1 LEU B 453    30496  28246  39621   -785   1203 -11285       C  
ATOM   5451  CD2 LEU B 453      61.891  82.248  93.883  1.00266.80           C  
ANISOU 5451  CD2 LEU B 453    30934  28621  41815  -1006    887 -12509       C  
ATOM   5452  N   ALA B 454      64.334  81.145  89.549  1.00263.66           N  
ANISOU 5452  N   ALA B 454    30426  26969  42782  -2006   2169 -10776       N  
ATOM   5453  CA  ALA B 454      65.322  81.872  88.754  1.00265.67           C  
ANISOU 5453  CA  ALA B 454    30479  26496  43966  -2332   2522 -10786       C  
ATOM   5454  C   ALA B 454      64.841  81.982  87.324  1.00265.42           C  
ANISOU 5454  C   ALA B 454    30782  26095  43968  -2391   3062 -10027       C  
ATOM   5455  O   ALA B 454      64.697  83.091  86.805  1.00265.18           O  
ANISOU 5455  O   ALA B 454    30833  25436  44486  -2464   3380  -9972       O  
ATOM   5456  CB  ALA B 454      66.688  81.193  88.801  1.00265.17           C  
ANISOU 5456  CB  ALA B 454    30047  26507  44198  -2564   2415 -10972       C  
ATOM   5457  N   PHE B 455      64.548  80.827  86.718  1.00264.28           N  
ANISOU 5457  N   PHE B 455    30850  26354  43211  -2332   3144  -9450       N  
ATOM   5458  CA  PHE B 455      64.087  80.769  85.340  1.00262.29           C  
ANISOU 5458  CA  PHE B 455    30939  25836  42882  -2353   3615  -8713       C  
ATOM   5459  C   PHE B 455      62.968  81.772  85.113  1.00261.67           C  
ANISOU 5459  C   PHE B 455    31165  25444  42812  -2175   3777  -8572       C  
ATOM   5460  O   PHE B 455      63.039  82.588  84.174  1.00264.51           O  
ANISOU 5460  O   PHE B 455    31657  25169  43674  -2287   4202  -8292       O  
ATOM   5461  CB  PHE B 455      63.636  79.355  84.950  1.00257.55           C  
ANISOU 5461  CB  PHE B 455    30552  25828  41475  -2227   3565  -8191       C  
ATOM   5462  CG  PHE B 455      63.158  79.238  83.525  1.00256.50           C  
ANISOU 5462  CG  PHE B 455    30781  25460  41215  -2219   4011  -7454       C  
ATOM   5463  CD1 PHE B 455      64.020  79.499  82.458  1.00255.68           C  
ANISOU 5463  CD1 PHE B 455    30647  24831  41669  -2472   4455  -7186       C  
ATOM   5464  CD2 PHE B 455      61.852  78.859  83.245  1.00255.51           C  
ANISOU 5464  CD2 PHE B 455    31023  25644  40412  -1950   3991  -7035       C  
ATOM   5465  CE1 PHE B 455      63.584  79.393  81.151  1.00253.28           C  
ANISOU 5465  CE1 PHE B 455    30707  24329  41199  -2434   4857  -6513       C  
ATOM   5466  CE2 PHE B 455      61.409  78.746  81.937  1.00253.52           C  
ANISOU 5466  CE2 PHE B 455    31111  25192  40023  -1914   4360  -6385       C  
ATOM   5467  CZ  PHE B 455      62.277  79.010  80.883  1.00252.99           C  
ANISOU 5467  CZ  PHE B 455    31045  24614  40464  -2146   4790  -6117       C  
ATOM   5468  N   PHE B 456      61.967  81.728  85.995  1.00256.50           N  
ANISOU 5468  N   PHE B 456    30614  25221  41622  -1893   3444  -8779       N  
ATOM   5469  CA  PHE B 456      60.776  82.557  85.826  1.00253.56           C  
ANISOU 5469  CA  PHE B 456    30536  24638  41167  -1677   3556  -8639       C  
ATOM   5470  C   PHE B 456      61.167  84.024  85.764  1.00260.92           C  
ANISOU 5470  C   PHE B 456    31359  24810  42967  -1811   3749  -8957       C  
ATOM   5471  O   PHE B 456      60.693  84.777  84.899  1.00258.41           O  
ANISOU 5471  O   PHE B 456    31298  23986  42900  -1784   4097  -8596       O  
ATOM   5472  CB  PHE B 456      59.818  82.330  86.996  1.00249.87           C  
ANISOU 5472  CB  PHE B 456    30101  24759  40077  -1377   3144  -8958       C  
ATOM   5473  CG  PHE B 456      58.413  82.759  86.718  1.00249.80           C  
ANISOU 5473  CG  PHE B 456    30427  24724  39761  -1108   3244  -8674       C  
ATOM   5474  CD1 PHE B 456      57.489  81.858  86.201  1.00244.93           C  
ANISOU 5474  CD1 PHE B 456    30087  24516  38458   -932   3284  -8117       C  
ATOM   5475  CD2 PHE B 456      58.008  84.073  86.951  1.00256.32           C  
ANISOU 5475  CD2 PHE B 456    31278  25093  41017  -1024   3292  -8974       C  
ATOM   5476  CE1 PHE B 456      56.187  82.250  85.932  1.00245.60           C  
ANISOU 5476  CE1 PHE B 456    30452  24574  38288   -675   3358  -7874       C  
ATOM   5477  CE2 PHE B 456      56.714  84.468  86.669  1.00256.92           C  
ANISOU 5477  CE2 PHE B 456    31651  25134  40831   -761   3377  -8713       C  
ATOM   5478  CZ  PHE B 456      55.801  83.557  86.164  1.00250.99           C  
ANISOU 5478  CZ  PHE B 456    31159  24810  39394   -584   3405  -8168       C  
ATOM   5479  N   LEU B 457      62.046  84.424  86.678  1.00271.83           N  
ANISOU 5479  N   LEU B 457    32359  26099  44824  -1949   3513  -9639       N  
ATOM   5480  CA  LEU B 457      62.481  85.818  86.740  1.00283.66           C  
ANISOU 5480  CA  LEU B 457    33697  26866  47212  -2093   3657 -10030       C  
ATOM   5481  C   LEU B 457      63.105  86.216  85.429  1.00281.59           C  
ANISOU 5481  C   LEU B 457    33496  25922  47571  -2359   4199  -9566       C  
ATOM   5482  O   LEU B 457      62.814  87.290  84.908  1.00285.57           O  
ANISOU 5482  O   LEU B 457    34155  25797  48549  -2370   4502  -9439       O  
ATOM   5483  CB  LEU B 457      63.451  86.022  87.895  1.00294.25           C  
ANISOU 5483  CB  LEU B 457    34579  28260  48962  -2216   3286 -10850       C  
ATOM   5484  CG  LEU B 457      62.710  86.012  89.241  1.00297.46           C  
ANISOU 5484  CG  LEU B 457    34974  29206  48838  -1909   2790 -11375       C  
ATOM   5485  CD1 LEU B 457      63.566  85.404  90.350  1.00300.01           C  
ANISOU 5485  CD1 LEU B 457    34935  29996  49057  -1943   2322 -11976       C  
ATOM   5486  CD2 LEU B 457      62.223  87.439  89.587  1.00302.63           C  
ANISOU 5486  CD2 LEU B 457    35648  29359  49977  -1815   2807 -11771       C  
ATOM   5487  N   GLU B 458      63.920  85.328  84.868  1.00272.19           N  
ANISOU 5487  N   GLU B 458    32210  24861  46347  -2555   4338  -9281       N  
ATOM   5488  CA  GLU B 458      64.575  85.600  83.596  1.00267.46           C  
ANISOU 5488  CA  GLU B 458    31671  23660  46292  -2811   4889  -8814       C  
ATOM   5489  C   GLU B 458      63.530  85.812  82.523  1.00263.26           C  
ANISOU 5489  C   GLU B 458    31650  22935  45440  -2630   5239  -8105       C  
ATOM   5490  O   GLU B 458      63.664  86.725  81.690  1.00266.07           O  
ANISOU 5490  O   GLU B 458    32143  22585  46363  -2741   5683  -7842       O  
ATOM   5491  CB  GLU B 458      65.457  84.409  83.196  1.00262.78           C  
ANISOU 5491  CB  GLU B 458    30928  23382  45531  -2986   4943  -8592       C  
ATOM   5492  CG  GLU B 458      66.333  84.623  81.969  1.00264.37           C  
ANISOU 5492  CG  GLU B 458    31121  22994  46332  -3280   5521  -8184       C  
ATOM   5493  CD  GLU B 458      67.393  85.683  82.164  1.00270.59           C  
ANISOU 5493  CD  GLU B 458    31518  23093  48199  -3588   5689  -8662       C  
ATOM   5494  OE1 GLU B 458      67.609  86.152  83.303  1.00273.04           O  
ANISOU 5494  OE1 GLU B 458    31506  23422  48814  -3593   5299  -9380       O  
ATOM   5495  OE2 GLU B 458      68.032  86.068  81.166  1.00273.49           O  
ANISOU 5495  OE2 GLU B 458    31895  22879  49138  -3828   6226  -8328       O  
ATOM   5496  N   CYS B 459      62.476  84.993  82.558  1.00255.85           N  
ANISOU 5496  N   CYS B 459    30993  22607  43610  -2340   5033  -7805       N  
ATOM   5497  CA  CYS B 459      61.395  85.123  81.590  1.00251.50           C  
ANISOU 5497  CA  CYS B 459    30922  21942  42693  -2124   5290  -7164       C  
ATOM   5498  C   CYS B 459      60.773  86.508  81.690  1.00253.63           C  
ANISOU 5498  C   CYS B 459    31321  21667  43377  -2008   5376  -7314       C  
ATOM   5499  O   CYS B 459      60.405  87.103  80.682  1.00255.16           O  
ANISOU 5499  O   CYS B 459    31840  21372  43738  -1960   5754  -6833       O  
ATOM   5500  CB  CYS B 459      60.391  83.987  81.734  1.00245.06           C  
ANISOU 5500  CB  CYS B 459    30314  21891  40904  -1844   5008  -6904       C  
ATOM   5501  SG  CYS B 459      61.167  82.363  81.557  1.00244.96           S  
ANISOU 5501  SG  CYS B 459    30156  22457  40460  -1986   4924  -6709       S  
ATOM   5502  N   LEU B 460      60.685  87.020  82.916  1.00254.38           N  
ANISOU 5502  N   LEU B 460    31166  21845  43640  -1952   5019  -7994       N  
ATOM   5503  CA  LEU B 460      60.168  88.361  83.140  1.00258.16           C  
ANISOU 5503  CA  LEU B 460    31715  21800  44573  -1847   5063  -8238       C  
ATOM   5504  C   LEU B 460      61.186  89.400  82.697  1.00260.37           C  
ANISOU 5504  C   LEU B 460    31835  21221  45872  -2159   5433  -8341       C  
ATOM   5505  O   LEU B 460      60.817  90.422  82.132  1.00262.06           O  
ANISOU 5505  O   LEU B 460    32271  20809  46490  -2115   5726  -8134       O  
ATOM   5506  CB  LEU B 460      59.831  88.610  84.611  1.00262.60           C  
ANISOU 5506  CB  LEU B 460    32043  22704  45028  -1693   4572  -8985       C  
ATOM   5507  CG  LEU B 460      58.679  87.842  85.247  1.00261.14           C  
ANISOU 5507  CG  LEU B 460    32004  23303  43913  -1355   4211  -8980       C  
ATOM   5508  CD1 LEU B 460      58.629  88.135  86.742  1.00264.67           C  
ANISOU 5508  CD1 LEU B 460    32174  24040  44348  -1250   3765  -9784       C  
ATOM   5509  CD2 LEU B 460      57.344  88.225  84.611  1.00261.37           C  
ANISOU 5509  CD2 LEU B 460    32447  23212  43649  -1065   4366  -8519       C  
ATOM   5510  N   ARG B 461      62.465  89.125  82.940  1.00258.07           N  
ANISOU 5510  N   ARG B 461    31154  20890  46011  -2471   5427  -8650       N  
ATOM   5511  CA  ARG B 461      63.515  90.094  82.634  1.00261.62           C  
ANISOU 5511  CA  ARG B 461    31369  20527  47505  -2800   5766  -8829       C  
ATOM   5512  C   ARG B 461      63.671  90.260  81.136  1.00263.12           C  
ANISOU 5512  C   ARG B 461    31874  20193  47908  -2917   6387  -8057       C  
ATOM   5513  O   ARG B 461      63.862  91.373  80.634  1.00267.06           O  
ANISOU 5513  O   ARG B 461    32438  19902  49131  -3035   6766  -7966       O  
ATOM   5514  CB  ARG B 461      64.811  89.600  83.259  1.00260.55           C  
ANISOU 5514  CB  ARG B 461    30720  20569  47707  -3082   5573  -9341       C  
ATOM   5515  CG  ARG B 461      65.878  90.646  83.397  1.00266.65           C  
ANISOU 5515  CG  ARG B 461    31111  20589  49613  -3407   5753  -9804       C  
ATOM   5516  CD  ARG B 461      67.170  89.994  83.826  1.00265.63           C  
ANISOU 5516  CD  ARG B 461    30488  20671  49766  -3680   5590 -10210       C  
ATOM   5517  NE  ARG B 461      67.726  89.106  82.805  1.00261.91           N  
ANISOU 5517  NE  ARG B 461    30087  20290  49134  -3842   5951  -9611       N  
ATOM   5518  CZ  ARG B 461      68.334  89.505  81.683  1.00264.67           C  
ANISOU 5518  CZ  ARG B 461    30484  19992  50084  -4099   6564  -9172       C  
ATOM   5519  NH1 ARG B 461      68.485  90.789  81.384  1.00271.85           N  
ANISOU 5519  NH1 ARG B 461    31387  20070  51833  -4242   6914  -9221       N  
ATOM   5520  NH2 ARG B 461      68.816  88.596  80.838  1.00260.64           N  
ANISOU 5520  NH2 ARG B 461    30034  19660  49337  -4214   6849  -8671       N  
ATOM   5521  N   THR B 462      63.572  89.139  80.426  1.00261.18           N  
ANISOU 5521  N   THR B 462    31838  20390  47009  -2868   6490  -7498       N  
ATOM   5522  CA  THR B 462      63.680  89.150  78.974  1.00264.91           C  
ANISOU 5522  CA  THR B 462    32652  20464  47536  -2935   7062  -6733       C  
ATOM   5523  C   THR B 462      62.333  89.492  78.357  1.00268.93           C  
ANISOU 5523  C   THR B 462    33702  20901  47575  -2587   7154  -6219       C  
ATOM   5524  O   THR B 462      62.254  89.784  77.165  1.00270.19           O  
ANISOU 5524  O   THR B 462    34219  20626  47816  -2580   7626  -5596       O  
ATOM   5525  CB  THR B 462      64.143  87.789  78.450  1.00259.81           C  
ANISOU 5525  CB  THR B 462    32007  20327  46382  -3010   7121  -6373       C  
ATOM   5526  OG1 THR B 462      63.338  86.750  79.026  1.00256.77           O  
ANISOU 5526  OG1 THR B 462    31693  20784  45082  -2743   6638  -6417       O  
ATOM   5527  CG2 THR B 462      65.573  87.558  78.820  1.00260.35           C  
ANISOU 5527  CG2 THR B 462    31558  20327  47034  -3373   7136  -6795       C  
ATOM   5528  N   GLU B 463      61.286  89.460  79.184  1.00273.31           N  
ANISOU 5528  N   GLU B 463    34312  21888  47644  -2288   6701  -6495       N  
ATOM   5529  CA  GLU B 463      59.912  89.620  78.725  1.00275.55           C  
ANISOU 5529  CA  GLU B 463    35063  22239  47392  -1919   6691  -6066       C  
ATOM   5530  C   GLU B 463      59.633  88.587  77.628  1.00271.04           C  
ANISOU 5530  C   GLU B 463    34836  22002  46144  -1817   6872  -5340       C  
ATOM   5531  O   GLU B 463      59.117  88.919  76.563  1.00269.92           O  
ANISOU 5531  O   GLU B 463    35121  21527  45906  -1668   7188  -4754       O  
ATOM   5532  CB  GLU B 463      59.658  91.065  78.244  1.00285.78           C  
ANISOU 5532  CB  GLU B 463    36577  22679  49326  -1882   7018  -5938       C  
ATOM   5533  CG  GLU B 463      60.103  92.133  79.249  1.00294.19           C  
ANISOU 5533  CG  GLU B 463    37270  23317  51191  -2030   6883  -6677       C  
ATOM   5534  CD  GLU B 463      59.751  93.570  78.896  1.00303.64           C  
ANISOU 5534  CD  GLU B 463    38674  23678  53017  -1964   7154  -6600       C  
ATOM   5535  OE1 GLU B 463      60.528  94.450  79.309  1.00308.71           O  
ANISOU 5535  OE1 GLU B 463    39010  23756  54530  -2213   7246  -7056       O  
ATOM   5536  OE2 GLU B 463      58.683  93.820  78.270  1.00308.05           O  
ANISOU 5536  OE2 GLU B 463    39680  24150  53213  -1652   7238  -6126       O  
ATOM   5537  N   LYS B 464      59.998  87.355  77.909  1.00268.35           N  
ANISOU 5537  N   LYS B 464    34308  22302  45349  -1889   6658  -5403       N  
ATOM   5538  CA  LYS B 464      59.895  86.295  76.927  1.00266.51           C  
ANISOU 5538  CA  LYS B 464    34339  22397  44525  -1830   6812  -4788       C  
ATOM   5539  C   LYS B 464      59.560  84.968  77.591  1.00263.15           C  
ANISOU 5539  C   LYS B 464    33783  22850  43351  -1718   6360  -4932       C  
ATOM   5540  O   LYS B 464      60.421  84.309  78.177  1.00267.20           O  
ANISOU 5540  O   LYS B 464    33937  23666  43919  -1923   6197  -5261       O  
ATOM   5541  CB  LYS B 464      61.203  86.204  76.143  1.00268.95           C  
ANISOU 5541  CB  LYS B 464    34547  22328  45312  -2166   7267  -4570       C  
ATOM   5542  CG  LYS B 464      61.129  85.347  74.893  1.00267.53           C  
ANISOU 5542  CG  LYS B 464    34714  22317  44617  -2096   7542  -3869       C  
ATOM   5543  CD  LYS B 464      60.486  86.086  73.729  1.00270.93           C  
ANISOU 5543  CD  LYS B 464    35666  22237  45038  -1905   7931  -3266       C  
ATOM   5544  CE  LYS B 464      59.853  85.127  72.726  1.00267.20           C  
ANISOU 5544  CE  LYS B 464    35606  22156  43761  -1663   7975  -2642       C  
ATOM   5545  NZ  LYS B 464      60.826  84.165  72.122  1.00265.42           N  
ANISOU 5545  NZ  LYS B 464    35297  22113  43436  -1874   8207  -2416       N  
ATOM   5546  N   LEU B 465      58.284  84.616  77.522  1.00258.61           N  
ANISOU 5546  N   LEU B 465    33492  22659  42108  -1384   6152  -4696       N  
ATOM   5547  CA  LEU B 465      57.822  83.299  77.933  1.00250.85           C  
ANISOU 5547  CA  LEU B 465    32464  22478  40366  -1253   5791  -4689       C  
ATOM   5548  C   LEU B 465      57.021  82.714  76.794  1.00244.21           C  
ANISOU 5548  C   LEU B 465    32046  21788  38953  -1030   5921  -4022       C  
ATOM   5549  O   LEU B 465      55.818  83.004  76.661  1.00241.66           O  
ANISOU 5549  O   LEU B 465    31987  21506  38327   -728   5821  -3859       O  
ATOM   5550  CB  LEU B 465      56.977  83.406  79.192  1.00253.50           C  
ANISOU 5550  CB  LEU B 465    32665  23206  40448  -1053   5348  -5167       C  
ATOM   5551  CG  LEU B 465      56.270  82.136  79.671  1.00253.91           C  
ANISOU 5551  CG  LEU B 465    32705  24069  39697   -874   4985  -5137       C  
ATOM   5552  CD1 LEU B 465      57.199  80.920  79.738  1.00252.38           C  
ANISOU 5552  CD1 LEU B 465    32302  24277  39314  -1080   4915  -5128       C  
ATOM   5553  CD2 LEU B 465      55.623  82.419  81.022  1.00257.41           C  
ANISOU 5553  CD2 LEU B 465    32972  24820  40009   -716   4607  -5683       C  
ATOM   5554  N   ASP B 466      57.693  81.916  75.965  1.00240.77           N  
ANISOU 5554  N   ASP B 466    31667  21422  38389  -1167   6137  -3658       N  
ATOM   5555  CA  ASP B 466      57.095  81.266  74.795  1.00239.03           C  
ANISOU 5555  CA  ASP B 466    31843  21348  37629   -973   6269  -3030       C  
ATOM   5556  C   ASP B 466      56.022  80.268  75.176  1.00235.43           C  
ANISOU 5556  C   ASP B 466    31430  21592  36427   -719   5859  -3004       C  
ATOM   5557  O   ASP B 466      56.166  79.585  76.154  1.00237.71           O  
ANISOU 5557  O   ASP B 466    31418  22360  36538   -784   5543  -3364       O  
ATOM   5558  CB  ASP B 466      58.130  80.456  74.023  1.00237.33           C  
ANISOU 5558  CB  ASP B 466    31604  21168  37402  -1187   6531  -2751       C  
ATOM   5559  CG  ASP B 466      59.091  81.315  73.299  1.00241.65           C  
ANISOU 5559  CG  ASP B 466    32197  21015  38603  -1410   7039  -2599       C  
ATOM   5560  OD1 ASP B 466      58.608  82.126  72.482  1.00245.21           O  
ANISOU 5560  OD1 ASP B 466    33022  21006  39141  -1258   7315  -2230       O  
ATOM   5561  OD2 ASP B 466      60.314  81.185  73.556  1.00240.90           O  
ANISOU 5561  OD2 ASP B 466    31762  20824  38944  -1727   7161  -2847       O  
ATOM   5562  N   HIS B 467      54.956  80.180  74.385  1.00230.74           N  
ANISOU 5562  N   HIS B 467    31214  21043  35411   -423   5868  -2571       N  
ATOM   5563  CA  HIS B 467      53.946  79.162  74.644  1.00221.00           C  
ANISOU 5563  CA  HIS B 467    30009  20459  33502   -197   5508  -2515       C  
ATOM   5564  C   HIS B 467      54.566  77.803  74.353  1.00222.06           C  
ANISOU 5564  C   HIS B 467    30056  21005  33311   -334   5485  -2355       C  
ATOM   5565  O   HIS B 467      55.275  77.650  73.358  1.00220.80           O  
ANISOU 5565  O   HIS B 467    30041  20606  33246   -445   5802  -2022       O  
ATOM   5566  CB  HIS B 467      52.681  79.304  73.823  1.00211.90           C  
ANISOU 5566  CB  HIS B 467    29251  19274  31984    155   5495  -2106       C  
ATOM   5567  CG  HIS B 467      51.590  78.420  74.312  1.00199.07           C  
ANISOU 5567  CG  HIS B 467    27573  18279  29784    371   5105  -2160       C  
ATOM   5568  ND1 HIS B 467      50.991  77.467  73.525  1.00191.62           N  
ANISOU 5568  ND1 HIS B 467    26836  17652  28316    546   5029  -1769       N  
ATOM   5569  CD2 HIS B 467      51.038  78.304  75.540  1.00194.21           C  
ANISOU 5569  CD2 HIS B 467    26700  18041  29047    426   4783  -2575       C  
ATOM   5570  CE1 HIS B 467      50.081  76.829  74.237  1.00188.78           C  
ANISOU 5570  CE1 HIS B 467    26337  17812  27576    691   4683  -1932       C  
ATOM   5571  NE2 HIS B 467      50.094  77.316  75.465  1.00189.90           N  
ANISOU 5571  NE2 HIS B 467    26206  18009  27938    623   4545  -2407       N  
ATOM   5572  N   TYR B 468      54.284  76.821  75.212  1.00221.94           N  
ANISOU 5572  N   TYR B 468    29815  21602  32910   -315   5124  -2581       N  
ATOM   5573  CA  TYR B 468      54.943  75.512  75.151  1.00219.41           C  
ANISOU 5573  CA  TYR B 468    29349  21686  32328   -463   5055  -2514       C  
ATOM   5574  C   TYR B 468      54.551  74.702  73.926  1.00219.76           C  
ANISOU 5574  C   TYR B 468    29702  21861  31936   -318   5146  -1982       C  
ATOM   5575  O   TYR B 468      55.287  73.816  73.489  1.00226.84           O  
ANISOU 5575  O   TYR B 468    30554  22906  32728   -455   5225  -1834       O  
ATOM   5576  CB  TYR B 468      54.634  74.695  76.404  1.00212.57           C  
ANISOU 5576  CB  TYR B 468    28199  21427  31138   -446   4644  -2863       C  
ATOM   5577  CG  TYR B 468      55.556  73.499  76.552  1.00207.15           C  
ANISOU 5577  CG  TYR B 468    27299  21083  30322   -642   4567  -2894       C  
ATOM   5578  CD1 TYR B 468      56.914  73.667  76.861  1.00207.35           C  
ANISOU 5578  CD1 TYR B 468    27060  20918  30804   -927   4673  -3162       C  
ATOM   5579  CD2 TYR B 468      55.092  72.204  76.360  1.00199.77           C  
ANISOU 5579  CD2 TYR B 468    26415  20639  28849   -542   4387  -2663       C  
ATOM   5580  CE1 TYR B 468      57.760  72.574  76.990  1.00202.65           C  
ANISOU 5580  CE1 TYR B 468    26261  20629  30106  -1087   4588  -3198       C  
ATOM   5581  CE2 TYR B 468      55.933  71.108  76.488  1.00195.21           C  
ANISOU 5581  CE2 TYR B 468    25648  20353  28168   -708   4310  -2687       C  
ATOM   5582  CZ  TYR B 468      57.262  71.293  76.808  1.00196.85           C  
ANISOU 5582  CZ  TYR B 468    25600  20381  28811   -972   4406  -2954       C  
ATOM   5583  OH  TYR B 468      58.092  70.201  76.913  1.00193.76           O  
ANISOU 5583  OH  TYR B 468    25017  20273  28328  -1118   4318  -2979       O  
ATOM   5584  N   PHE B 469      53.377  74.990  73.384  1.00216.30           N  
ANISOU 5584  N   PHE B 469    29567  21377  31239    -25   5113  -1719       N  
ATOM   5585  CA  PHE B 469      52.865  74.289  72.225  1.00210.44           C  
ANISOU 5585  CA  PHE B 469    29137  20759  30061    162   5149  -1246       C  
ATOM   5586  C   PHE B 469      52.936  75.148  70.983  1.00215.08           C  
ANISOU 5586  C   PHE B 469    30111  20790  30819    258   5516   -859       C  
ATOM   5587  O   PHE B 469      52.987  74.628  69.849  1.00219.00           O  
ANISOU 5587  O   PHE B 469    30880  21285  31044    345   5662   -452       O  
ATOM   5588  CB  PHE B 469      51.427  73.914  72.426  1.00202.89           C  
ANISOU 5588  CB  PHE B 469    28253  20175  28659    459   4820  -1210       C  
ATOM   5589  CG  PHE B 469      51.232  72.943  73.518  1.00198.22           C  
ANISOU 5589  CG  PHE B 469    27339  20156  27817    399   4486  -1498       C  
ATOM   5590  CD1 PHE B 469      51.315  73.348  74.837  1.00197.43           C  
ANISOU 5590  CD1 PHE B 469    26946  20149  27917    305   4339  -1956       C  
ATOM   5591  CD2 PHE B 469      51.002  71.609  73.232  1.00198.38           C  
ANISOU 5591  CD2 PHE B 469    27355  20618  27401    441   4324  -1315       C  
ATOM   5592  CE1 PHE B 469      51.147  72.443  75.862  1.00195.97           C  
ANISOU 5592  CE1 PHE B 469    26493  20500  27465    266   4048  -2198       C  
ATOM   5593  CE2 PHE B 469      50.820  70.694  74.256  1.00197.51           C  
ANISOU 5593  CE2 PHE B 469    26961  21021  27063    387   4034  -1553       C  
ATOM   5594  CZ  PHE B 469      50.895  71.109  75.572  1.00196.22           C  
ANISOU 5594  CZ  PHE B 469    26529  20956  27067    303   3905  -1980       C  
ATOM   5595  N   ILE B 470      52.930  76.464  71.181  1.00215.98           N  
ANISOU 5595  N   ILE B 470    30269  20421  31372    258   5669   -978       N  
ATOM   5596  CA  ILE B 470      53.013  77.437  70.092  1.00217.61           C  
ANISOU 5596  CA  ILE B 470    30853  20028  31801    348   6045   -614       C  
ATOM   5597  C   ILE B 470      54.222  78.346  70.324  1.00217.79           C  
ANISOU 5597  C   ILE B 470    30713  19528  32506     35   6386   -801       C  
ATOM   5598  O   ILE B 470      54.074  79.401  70.913  1.00221.64           O  
ANISOU 5598  O   ILE B 470    31124  19694  33395     27   6387  -1058       O  
ATOM   5599  CB  ILE B 470      51.717  78.228  69.893  1.00220.82           C  
ANISOU 5599  CB  ILE B 470    31537  20264  32100    701   5929   -496       C  
ATOM   5600  CG1 ILE B 470      50.492  77.295  69.929  1.00214.11           C  
ANISOU 5600  CG1 ILE B 470    30725  19982  30643    981   5528   -434       C  
ATOM   5601  CG2 ILE B 470      51.780  78.983  68.558  1.00226.26           C  
ANISOU 5601  CG2 ILE B 470    32697  20394  32878    842   6309     -6       C  
ATOM   5602  CD1 ILE B 470      49.267  77.937  70.528  1.00212.63           C  
ANISOU 5602  CD1 ILE B 470    30527  19817  30445   1236   5267   -627       C  
ATOM   5603  N   PRO B 471      55.403  77.951  69.848  1.00216.51           N  
ANISOU 5603  N   PRO B 471    30490  19269  32504   -216   6680   -685       N  
ATOM   5604  CA  PRO B 471      56.642  78.690  70.128  1.00222.51           C  
ANISOU 5604  CA  PRO B 471    31015  19567  33961   -553   6995   -910       C  
ATOM   5605  C   PRO B 471      56.679  80.124  69.653  1.00230.44           C  
ANISOU 5605  C   PRO B 471    32256  19843  35455   -531   7360   -755       C  
ATOM   5606  O   PRO B 471      57.353  80.912  70.305  1.00236.51           O  
ANISOU 5606  O   PRO B 471    32753  20262  36848   -768   7467  -1108       O  
ATOM   5607  CB  PRO B 471      57.724  77.847  69.433  1.00223.98           C  
ANISOU 5607  CB  PRO B 471    31165  19826  34111   -758   7264   -700       C  
ATOM   5608  CG  PRO B 471      57.045  76.580  68.987  1.00219.22           C  
ANISOU 5608  CG  PRO B 471    30727  19790  32773   -537   7013   -447       C  
ATOM   5609  CD  PRO B 471      55.616  76.929  68.810  1.00216.56           C  
ANISOU 5609  CD  PRO B 471    30702  19495  32084   -170   6799   -281       C  
ATOM   5610  N   LYS B 472      55.998  80.451  68.550  1.00233.30           N  
ANISOU 5610  N   LYS B 472    33111  19973  35557   -250   7538   -251       N  
ATOM   5611  CA  LYS B 472      55.949  81.827  68.044  1.00238.38           C  
ANISOU 5611  CA  LYS B 472    34035  19899  36636   -190   7888    -46       C  
ATOM   5612  C   LYS B 472      55.077  82.741  68.922  1.00236.49           C  
ANISOU 5612  C   LYS B 472    33722  19531  36602    -40   7607   -380       C  
ATOM   5613  O   LYS B 472      55.184  83.967  68.859  1.00244.32           O  
ANISOU 5613  O   LYS B 472    34810  19902  38116    -62   7851   -378       O  
ATOM   5614  CB  LYS B 472      55.453  81.893  66.579  1.00243.56           C  
ANISOU 5614  CB  LYS B 472    35284  20356  36900    111   8142    615       C  
ATOM   5615  CG  LYS B 472      53.980  81.540  66.291  1.00247.14           C  
ANISOU 5615  CG  LYS B 472    36039  21170  36691    556   7755    809       C  
ATOM   5616  CD  LYS B 472      53.547  82.036  64.895  1.00254.74           C  
ANISOU 5616  CD  LYS B 472    37614  21745  37428    870   8040   1423       C  
ATOM   5617  CE  LYS B 472      52.641  81.039  64.127  1.00256.33           C  
ANISOU 5617  CE  LYS B 472    38121  22439  36831   1228   7769   1741       C  
ATOM   5618  NZ  LYS B 472      52.438  81.357  62.670  1.00260.10           N  
ANISOU 5618  NZ  LYS B 472    39211  22587  37028   1521   8071   2355       N  
ATOM   5619  N   PHE B 473      54.183  82.132  69.699  1.00226.80           N  
ANISOU 5619  N   PHE B 473    32337  18880  34956    125   7111   -646       N  
ATOM   5620  CA  PHE B 473      53.321  82.879  70.584  1.00222.79           C  
ANISOU 5620  CA  PHE B 473    31731  18332  34584    281   6827   -994       C  
ATOM   5621  C   PHE B 473      54.056  83.211  71.870  1.00220.97           C  
ANISOU 5621  C   PHE B 473    31015  18073  34868    -21   6734  -1612       C  
ATOM   5622  O   PHE B 473      54.257  82.347  72.720  1.00213.67           O  
ANISOU 5622  O   PHE B 473    29751  17687  33747   -141   6445  -1952       O  
ATOM   5623  CB  PHE B 473      52.036  82.125  70.888  1.00217.74           C  
ANISOU 5623  CB  PHE B 473    31116  18308  33307    588   6370  -1024       C  
ATOM   5624  CG  PHE B 473      50.976  82.971  71.534  1.00217.71           C  
ANISOU 5624  CG  PHE B 473    31109  18212  33397    828   6134  -1274       C  
ATOM   5625  CD1 PHE B 473      50.477  84.090  70.881  1.00221.65           C  
ANISOU 5625  CD1 PHE B 473    31959  18145  34110   1050   6313  -1017       C  
ATOM   5626  CD2 PHE B 473      50.469  82.651  72.796  1.00212.84           C  
ANISOU 5626  CD2 PHE B 473    30149  18073  32647    847   5742  -1760       C  
ATOM   5627  CE1 PHE B 473      49.498  84.878  71.471  1.00221.59           C  
ANISOU 5627  CE1 PHE B 473    31938  18043  34212   1284   6092  -1262       C  
ATOM   5628  CE2 PHE B 473      49.499  83.434  73.382  1.00211.13           C  
ANISOU 5628  CE2 PHE B 473    29923  17777  32521   1076   5549  -2002       C  
ATOM   5629  CZ  PHE B 473      49.008  84.536  72.721  1.00216.16           C  
ANISOU 5629  CZ  PHE B 473    30888  17849  33393   1295   5713  -1765       C  
ATOM   5630  N   ASN B 474      54.416  84.486  72.041  1.00227.06           N  
ANISOU 5630  N   ASN B 474    31760  18211  36301   -125   6956  -1774       N  
ATOM   5631  CA  ASN B 474      54.972  84.969  73.306  1.00229.42           C  
ANISOU 5631  CA  ASN B 474    31610  18439  37117   -361   6818  -2420       C  
ATOM   5632  C   ASN B 474      53.904  85.399  74.296  1.00232.54           C  
ANISOU 5632  C   ASN B 474    31914  19022  37418   -127   6427  -2814       C  
ATOM   5633  O   ASN B 474      52.976  86.112  73.918  1.00233.99           O  
ANISOU 5633  O   ASN B 474    32394  18936  37573    154   6443  -2617       O  
ATOM   5634  CB  ASN B 474      55.918  86.147  73.104  1.00232.58           C  
ANISOU 5634  CB  ASN B 474    31968  18048  38352   -610   7232  -2478       C  
ATOM   5635  CG  ASN B 474      56.423  86.707  74.420  1.00231.28           C  
ANISOU 5635  CG  ASN B 474    31339  17794  38740   -822   7044  -3193       C  
ATOM   5636  OD1 ASN B 474      56.561  85.988  75.419  1.00230.08           O  
ANISOU 5636  OD1 ASN B 474    30840  18200  38379   -896   6684  -3630       O  
ATOM   5637  ND2 ASN B 474      56.672  87.996  74.438  1.00230.47           N  
ANISOU 5637  ND2 ASN B 474    31241  16988  39335   -901   7274  -3319       N  
ATOM   5638  N   LEU B 475      54.066  84.984  75.548  1.00234.52           N  
ANISOU 5638  N   LEU B 475    31761  19719  37625   -235   6091  -3367       N  
ATOM   5639  CA  LEU B 475      53.062  85.219  76.577  1.00235.57           C  
ANISOU 5639  CA  LEU B 475    31780  20143  37580    -12   5712  -3768       C  
ATOM   5640  C   LEU B 475      53.393  86.432  77.407  1.00239.46           C  
ANISOU 5640  C   LEU B 475    32054  20186  38741   -115   5712  -4297       C  
ATOM   5641  O   LEU B 475      52.513  86.959  78.116  1.00236.89           O  
ANISOU 5641  O   LEU B 475    31699  19926  38381    103   5476  -4605       O  
ATOM   5642  CB  LEU B 475      52.929  84.056  77.558  1.00233.61           C  
ANISOU 5642  CB  LEU B 475    31243  20688  36829    -23   5324  -4079       C  
ATOM   5643  CG  LEU B 475      52.056  82.893  77.129  1.00231.21           C  
ANISOU 5643  CG  LEU B 475    31115  20960  35773    193   5160  -3702       C  
ATOM   5644  CD1 LEU B 475      52.369  82.461  75.703  1.00231.68           C  
ANISOU 5644  CD1 LEU B 475    31479  20846  35699    169   5459  -3084       C  
ATOM   5645  CD2 LEU B 475      52.241  81.758  78.126  1.00226.75           C  
ANISOU 5645  CD2 LEU B 475    30231  21092  34830    100   4844  -4017       C  
ATOM   5646  N   PHE B 476      54.662  86.858  77.345  1.00242.44           N  
ANISOU 5646  N   PHE B 476    32256  20116  39743   -449   5970  -4433       N  
ATOM   5647  CA  PHE B 476      55.113  88.035  78.111  1.00245.98           C  
ANISOU 5647  CA  PHE B 476    32461  20075  40922   -585   5979  -4975       C  
ATOM   5648  C   PHE B 476      55.399  89.200  77.173  1.00252.78           C  
ANISOU 5648  C   PHE B 476    33567  20058  42418   -644   6431  -4661       C  
ATOM   5649  O   PHE B 476      56.285  90.021  77.452  1.00260.94           O  
ANISOU 5649  O   PHE B 476    34378  20560  44208   -902   6600  -4983       O  
ATOM   5650  CB  PHE B 476      56.353  87.705  78.965  1.00243.96           C  
ANISOU 5650  CB  PHE B 476    31738  19969  40985   -926   5871  -5498       C  
ATOM   5651  CG  PHE B 476      56.067  86.918  80.228  1.00238.98           C  
ANISOU 5651  CG  PHE B 476    30830  20098  39871   -848   5382  -5981       C  
ATOM   5652  CD1 PHE B 476      54.769  86.717  80.722  1.00236.08           C  
ANISOU 5652  CD1 PHE B 476    30577  20187  38934   -513   5079  -6036       C  
ATOM   5653  CD2 PHE B 476      57.123  86.410  80.959  1.00237.18           C  
ANISOU 5653  CD2 PHE B 476    30213  20114  39787  -1106   5229  -6401       C  
ATOM   5654  CE1 PHE B 476      54.554  85.996  81.891  1.00232.48           C  
ANISOU 5654  CE1 PHE B 476    29878  20416  38038   -449   4676  -6460       C  
ATOM   5655  CE2 PHE B 476      56.913  85.695  82.130  1.00233.37           C  
ANISOU 5655  CE2 PHE B 476    29501  20317  38848  -1023   4789  -6830       C  
ATOM   5656  CZ  PHE B 476      55.630  85.486  82.594  1.00230.78           C  
ANISOU 5656  CZ  PHE B 476    29313  20436  37934   -698   4530  -6845       C  
ATOM   5657  N   SER B 477      54.671  89.290  76.062  1.00252.05           N  
ANISOU 5657  N   SER B 477    33932  19791  42045   -404   6629  -4038       N  
ATOM   5658  CA  SER B 477      54.807  90.428  75.185  1.00256.51           C  
ANISOU 5658  CA  SER B 477    34785  19521  43154   -404   7051  -3701       C  
ATOM   5659  C   SER B 477      54.234  91.691  75.847  1.00260.84           C  
ANISOU 5659  C   SER B 477    35296  19651  44160   -260   6928  -4097       C  
ATOM   5660  O   SER B 477      53.551  91.649  76.878  1.00258.54           O  
ANISOU 5660  O   SER B 477    34816  19762  43655    -98   6518  -4569       O  
ATOM   5661  CB  SER B 477      54.183  90.168  73.809  1.00253.83           C  
ANISOU 5661  CB  SER B 477    34974  19124  42342   -150   7271  -2925       C  
ATOM   5662  OG  SER B 477      52.782  90.061  73.886  1.00252.68           O  
ANISOU 5662  OG  SER B 477    35036  19315  41655    257   6948  -2850       O  
ATOM   5663  N   GLN B 478      54.570  92.825  75.247  1.00266.37           N  
ANISOU 5663  N   GLN B 478    36173  19515  45520   -330   7315  -3904       N  
ATOM   5664  CA  GLN B 478      54.069  94.112  75.712  1.00270.32           C  
ANISOU 5664  CA  GLN B 478    36681  19498  46530   -192   7257  -4217       C  
ATOM   5665  C   GLN B 478      52.587  94.228  75.365  1.00272.49           C  
ANISOU 5665  C   GLN B 478    37338  19916  46278    284   7075  -3913       C  
ATOM   5666  O   GLN B 478      51.832  94.921  76.055  1.00273.58           O  
ANISOU 5666  O   GLN B 478    37418  19976  46552    494   6830  -4290       O  
ATOM   5667  CB  GLN B 478      54.888  95.268  75.107  1.00273.41           C  
ANISOU 5667  CB  GLN B 478    37162  18907  47813   -416   7758  -4050       C  
ATOM   5668  CG  GLN B 478      54.618  96.660  75.684  1.00275.48           C  
ANISOU 5668  CG  GLN B 478    37352  18543  48775   -353   7717  -4468       C  
ATOM   5669  CD  GLN B 478      55.133  96.864  77.102  1.00274.23           C  
ANISOU 5669  CD  GLN B 478    36637  18514  49042   -566   7407  -5358       C  
ATOM   5670  OE1 GLN B 478      55.661  95.945  77.738  1.00271.63           O  
ANISOU 5670  OE1 GLN B 478    35968  18786  48453   -746   7183  -5687       O  
ATOM   5671  NE2 GLN B 478      54.990  98.088  77.605  1.00276.05           N  
ANISOU 5671  NE2 GLN B 478    36782  18166  49937   -533   7380  -5762       N  
ATOM   5672  N   GLU B 479      52.170  93.522  74.308  1.00273.79           N  
ANISOU 5672  N   GLU B 479    37877  20310  45839    463   7178  -3260       N  
ATOM   5673  CA  GLU B 479      50.788  93.556  73.855  1.00273.88           C  
ANISOU 5673  CA  GLU B 479    38257  20464  45341    925   7001  -2933       C  
ATOM   5674  C   GLU B 479      49.839  92.974  74.890  1.00267.05           C  
ANISOU 5674  C   GLU B 479    37151  20344  43969   1134   6483  -3378       C  
ATOM   5675  O   GLU B 479      48.701  93.430  75.033  1.00270.51           O  
ANISOU 5675  O   GLU B 479    37720  20782  44278   1486   6276  -3427       O  
ATOM   5676  CB  GLU B 479      50.593  92.778  72.549  1.00273.65           C  
ANISOU 5676  CB  GLU B 479    38643  20608  44721   1070   7170  -2194       C  
ATOM   5677  CG  GLU B 479      51.264  93.392  71.330  1.00280.93           C  
ANISOU 5677  CG  GLU B 479    39936  20788  46014    978   7713  -1618       C  
ATOM   5678  CD  GLU B 479      52.674  92.876  71.096  1.00282.37           C  
ANISOU 5678  CD  GLU B 479    39938  20939  46410    540   8048  -1552       C  
ATOM   5679  OE1 GLU B 479      53.573  93.198  71.911  1.00284.16           O  
ANISOU 5679  OE1 GLU B 479    39742  20985  47237    189   8094  -2057       O  
ATOM   5680  OE2 GLU B 479      52.897  92.074  70.153  1.00283.03           O  
ANISOU 5680  OE2 GLU B 479    40263  21230  46043    547   8233  -1043       O  
ATOM   5681  N   LEU B 480      50.319  91.966  75.611  1.00258.24           N  
ANISOU 5681  N   LEU B 480    35681  19857  42578    919   6289  -3697       N  
ATOM   5682  CA  LEU B 480      49.502  91.227  76.572  1.00253.18           C  
ANISOU 5682  CA  LEU B 480    34816  19991  41388   1088   5837  -4064       C  
ATOM   5683  C   LEU B 480      49.749  91.693  78.013  1.00255.89           C  
ANISOU 5683  C   LEU B 480    34735  20397  42093    966   5612  -4849       C  
ATOM   5684  O   LEU B 480      48.810  91.837  78.795  1.00254.65           O  
ANISOU 5684  O   LEU B 480    34484  20534  41737   1212   5312  -5194       O  
ATOM   5685  CB  LEU B 480      49.814  89.740  76.441  1.00247.53           C  
ANISOU 5685  CB  LEU B 480    34015  19959  40073    964   5751  -3882       C  
ATOM   5686  CG  LEU B 480      49.801  89.154  75.018  1.00245.44           C  
ANISOU 5686  CG  LEU B 480    34138  19666  39450   1034   5985  -3147       C  
ATOM   5687  CD1 LEU B 480      50.236  87.686  75.055  1.00240.78           C  
ANISOU 5687  CD1 LEU B 480    33391  19747  38347    871   5879  -3075       C  
ATOM   5688  CD2 LEU B 480      48.443  89.319  74.345  1.00243.13           C  
ANISOU 5688  CD2 LEU B 480    34219  19377  38780   1477   5882  -2770       C  
ATOM   5689  N   ILE B 481      51.014  91.906  78.367  1.00260.98           N  
ANISOU 5689  N   ILE B 481    35113  20782  43263    594   5752  -5147       N  
ATOM   5690  CA  ILE B 481      51.359  92.376  79.705  1.00267.53           C  
ANISOU 5690  CA  ILE B 481    35541  21638  44468    473   5528  -5921       C  
ATOM   5691  C   ILE B 481      52.285  93.584  79.675  1.00276.27           C  
ANISOU 5691  C   ILE B 481    36552  21904  46514    225   5797  -6142       C  
ATOM   5692  O   ILE B 481      53.267  93.603  78.932  1.00279.96           O  
ANISOU 5692  O   ILE B 481    37059  21974  47337    -51   6146  -5840       O  
ATOM   5693  CB  ILE B 481      51.998  91.261  80.546  1.00264.27           C  
ANISOU 5693  CB  ILE B 481    34770  21917  43722    263   5288  -6268       C  
ATOM   5694  CG1 ILE B 481      51.074  90.034  80.537  1.00257.65           C  
ANISOU 5694  CG1 ILE B 481    34032  21881  41981    496   5051  -6013       C  
ATOM   5695  CG2 ILE B 481      52.263  91.765  81.964  1.00267.66           C  
ANISOU 5695  CG2 ILE B 481    34815  22410  44472    198   5013  -7092       C  
ATOM   5696  CD1 ILE B 481      51.489  88.904  81.449  1.00253.53           C  
ANISOU 5696  CD1 ILE B 481    33193  22093  41045    359   4775  -6340       C  
ATOM   5697  N   ASP B 482      51.972  94.586  80.489  1.00279.86           N  
ANISOU 5697  N   ASP B 482    36866  22080  47386    322   5645  -6680       N  
ATOM   5698  CA  ASP B 482      52.781  95.806  80.550  1.00286.86           C  
ANISOU 5698  CA  ASP B 482    37633  22132  49228     98   5871  -6957       C  
ATOM   5699  C   ASP B 482      54.075  95.552  81.308  1.00286.25           C  
ANISOU 5699  C   ASP B 482    37101  22147  49512   -289   5803  -7489       C  
ATOM   5700  O   ASP B 482      54.081  94.826  82.307  1.00282.78           O  
ANISOU 5700  O   ASP B 482    36385  22398  48661   -283   5435  -7940       O  
ATOM   5701  CB  ASP B 482      51.991  96.936  81.217  1.00293.43           C  
ANISOU 5701  CB  ASP B 482    38449  22657  50383    350   5694  -7408       C  
ATOM   5702  CG  ASP B 482      52.758  98.266  81.238  1.00303.84           C  
ANISOU 5702  CG  ASP B 482    39658  23040  52746    132   5933  -7687       C  
ATOM   5703  OD1 ASP B 482      53.689  98.465  80.412  1.00309.32           O  
ANISOU 5703  OD1 ASP B 482    40416  23187  53922   -155   6336  -7329       O  
ATOM   5704  OD2 ASP B 482      52.432  99.122  82.094  1.00306.39           O  
ANISOU 5704  OD2 ASP B 482    39821  23164  53430    248   5727  -8280       O  
ATOM   5705  N   ARG B 483      55.157  96.165  80.817  1.00289.15           N  
ANISOU 5705  N   ARG B 483    37399  21803  50661   -614   6166  -7422       N  
ATOM   5706  CA  ARG B 483      56.476  96.125  81.438  1.00289.49           C  
ANISOU 5706  CA  ARG B 483    36987  21768  51235  -1003   6143  -7941       C  
ATOM   5707  C   ARG B 483      56.403  96.347  82.928  1.00290.15           C  
ANISOU 5707  C   ARG B 483    36695  22160  51388   -949   5672  -8829       C  
ATOM   5708  O   ARG B 483      56.940  95.551  83.701  1.00286.86           O  
ANISOU 5708  O   ARG B 483    35960  22317  50717  -1073   5391  -9223       O  
ATOM   5709  CB  ARG B 483      57.341  97.245  80.896  1.00295.83           C  
ANISOU 5709  CB  ARG B 483    37756  21573  53072  -1283   6576  -7897       C  
ATOM   5710  CG  ARG B 483      58.308  96.790  79.842  1.00295.48           C  
ANISOU 5710  CG  ARG B 483    37775  21305  53188  -1585   7028  -7342       C  
ATOM   5711  CD  ARG B 483      59.127  97.939  79.325  1.00304.24           C  
ANISOU 5711  CD  ARG B 483    38846  21397  55352  -1865   7496  -7289       C  
ATOM   5712  NE  ARG B 483      60.491  97.508  79.008  1.00306.88           N  
ANISOU 5712  NE  ARG B 483    38908  21612  56077  -2286   7781  -7241       N  
ATOM   5713  CZ  ARG B 483      61.593  98.249  79.176  1.00314.94           C  
ANISOU 5713  CZ  ARG B 483    39577  21974  58110  -2654   8005  -7602       C  
ATOM   5714  NH1 ARG B 483      61.545  99.494  79.667  1.00320.71           N  
ANISOU 5714  NH1 ARG B 483    40180  22063  59611  -2671   7978  -8058       N  
ATOM   5715  NH2 ARG B 483      62.767  97.717  78.852  1.00316.20           N  
ANISOU 5715  NH2 ARG B 483    39487  22117  58537  -3012   8256  -7526       N  
ATOM   5716  N   LYS B 484      55.695  97.413  83.307  1.00293.16           N  
ANISOU 5716  N   LYS B 484    37139  22172  52074   -733   5583  -9125       N  
ATOM   5717  CA  LYS B 484      55.556  97.841  84.707  1.00292.00           C  
ANISOU 5717  CA  LYS B 484    36670  22217  52059   -642   5160 -10006       C  
ATOM   5718  C   LYS B 484      55.079  96.692  85.598  1.00285.46           C  
ANISOU 5718  C   LYS B 484    35730  22428  50302   -461   4725 -10252       C  
ATOM   5719  O   LYS B 484      55.520  96.561  86.745  1.00286.74           O  
ANISOU 5719  O   LYS B 484    35539  22925  50483   -524   4386 -10955       O  
ATOM   5720  CB  LYS B 484      54.570  99.025  84.860  1.00292.38           C  
ANISOU 5720  CB  LYS B 484    36890  21813  52385   -342   5129 -10171       C  
ATOM   5721  CG  LYS B 484      54.821 100.274  84.010  1.00295.36           C  
ANISOU 5721  CG  LYS B 484    37439  21119  53663   -447   5550  -9906       C  
ATOM   5722  CD  LYS B 484      56.200 100.913  84.182  1.00299.75           C  
ANISOU 5722  CD  LYS B 484    37641  21026  55222   -873   5715 -10312       C  
ATOM   5723  CE  LYS B 484      56.726 101.526  82.883  1.00302.99           C  
ANISOU 5723  CE  LYS B 484    38284  20540  56297  -1089   6299  -9668       C  
ATOM   5724  NZ  LYS B 484      58.215 101.539  82.829  1.00305.93           N  
ANISOU 5724  NZ  LYS B 484    38300  20551  57388  -1569   6518  -9853       N  
ATOM   5725  N   SER B 485      54.167  95.879  85.065  1.00277.76           N  
ANISOU 5725  N   SER B 485    35064  21947  48525   -225   4735  -9673       N  
ATOM   5726  CA  SER B 485      53.656  94.725  85.792  1.00269.95           C  
ANISOU 5726  CA  SER B 485    34003  21923  46642    -56   4380  -9800       C  
ATOM   5727  C   SER B 485      54.770  93.709  86.026  1.00270.35           C  
ANISOU 5727  C   SER B 485    33790  22380  46548   -354   4301  -9889       C  
ATOM   5728  O   SER B 485      55.017  93.285  87.153  1.00267.12           O  
ANISOU 5728  O   SER B 485    33100  22492  45901   -356   3946 -10456       O  
ATOM   5729  CB  SER B 485      52.503  94.081  85.021  1.00260.99           C  
ANISOU 5729  CB  SER B 485    33244  21141  44778    225   4450  -9114       C  
ATOM   5730  OG  SER B 485      51.644  95.057  84.462  1.00261.91           O  
ANISOU 5730  OG  SER B 485    33645  20727  45142    463   4608  -8883       O  
ATOM   5731  N   LYS B 486      55.443  93.335  84.949  1.00275.08           N  
ANISOU 5731  N   LYS B 486    34493  22733  47289   -588   4636  -9326       N  
ATOM   5732  CA  LYS B 486      56.536  92.370  84.994  1.00275.59           C  
ANISOU 5732  CA  LYS B 486    34323  23118  47268   -877   4612  -9335       C  
ATOM   5733  C   LYS B 486      57.660  92.803  85.938  1.00274.03           C  
ANISOU 5733  C   LYS B 486    33672  22740  47706  -1131   4433 -10103       C  
ATOM   5734  O   LYS B 486      58.233  91.979  86.659  1.00270.00           O  
ANISOU 5734  O   LYS B 486    32893  22776  46919  -1223   4149 -10433       O  
ATOM   5735  CB  LYS B 486      57.077  92.138  83.581  1.00281.77           C  
ANISOU 5735  CB  LYS B 486    35310  23517  48233  -1083   5076  -8609       C  
ATOM   5736  CG  LYS B 486      56.060  91.466  82.660  1.00283.13           C  
ANISOU 5736  CG  LYS B 486    35908  23993  47673   -831   5189  -7866       C  
ATOM   5737  CD  LYS B 486      56.643  91.093  81.304  1.00285.48           C  
ANISOU 5737  CD  LYS B 486    36413  24010  48045  -1016   5622  -7170       C  
ATOM   5738  CE  LYS B 486      56.724  92.295  80.369  1.00292.87           C  
ANISOU 5738  CE  LYS B 486    37590  24029  49656  -1059   6063  -6846       C  
ATOM   5739  NZ  LYS B 486      55.419  92.655  79.766  1.00293.61           N  
ANISOU 5739  NZ  LYS B 486    38123  24023  49411   -690   6113  -6406       N  
ATOM   5740  N   GLU B 487      57.956  94.101  85.929  1.00276.57           N  
ANISOU 5740  N   GLU B 487    33912  22282  48887  -1230   4586 -10392       N  
ATOM   5741  CA  GLU B 487      58.991  94.677  86.787  1.00280.98           C  
ANISOU 5741  CA  GLU B 487    34027  22563  50167  -1465   4416 -11167       C  
ATOM   5742  C   GLU B 487      58.550  94.628  88.248  1.00282.87           C  
ANISOU 5742  C   GLU B 487    34075  23372  50029  -1229   3880 -11919       C  
ATOM   5743  O   GLU B 487      59.323  94.240  89.125  1.00282.49           O  
ANISOU 5743  O   GLU B 487    33677  23657  49996  -1348   3566 -12478       O  
ATOM   5744  CB  GLU B 487      59.297  96.122  86.368  1.00286.28           C  
ANISOU 5744  CB  GLU B 487    34686  22212  51873  -1610   4733 -11259       C  
ATOM   5745  CG  GLU B 487      59.950  96.269  84.989  1.00285.55           C  
ANISOU 5745  CG  GLU B 487    34741  21478  52277  -1889   5305 -10580       C  
ATOM   5746  CD  GLU B 487      59.982  97.708  84.478  1.00290.60           C  
ANISOU 5746  CD  GLU B 487    35477  21098  53839  -1963   5662 -10532       C  
ATOM   5747  OE1 GLU B 487      59.835  98.659  85.269  1.00292.80           O  
ANISOU 5747  OE1 GLU B 487    35586  21069  54594  -1896   5456 -11164       O  
ATOM   5748  OE2 GLU B 487      60.122  97.885  83.258  1.00290.82           O  
ANISOU 5748  OE2 GLU B 487    35778  20625  54093  -2070   6160  -9838       O  
ATOM   5749  N   PHE B 488      57.309  95.046  88.498  1.00286.09           N  
ANISOU 5749  N   PHE B 488    34716  23880  50104   -881   3781 -11937       N  
ATOM   5750  CA  PHE B 488      56.723  94.976  89.828  1.00288.65           C  
ANISOU 5750  CA  PHE B 488    34920  24787  49967   -608   3319 -12580       C  
ATOM   5751  C   PHE B 488      56.826  93.552  90.392  1.00283.94           C  
ANISOU 5751  C   PHE B 488    34240  25130  48514   -567   3029 -12584       C  
ATOM   5752  O   PHE B 488      57.272  93.343  91.525  1.00288.40           O  
ANISOU 5752  O   PHE B 488    34522  26084  48969   -560   2651 -13242       O  
ATOM   5753  CB  PHE B 488      55.269  95.435  89.812  1.00288.38           C  
ANISOU 5753  CB  PHE B 488    35189  24788  49592   -226   3323 -12434       C  
ATOM   5754  CG  PHE B 488      54.579  95.286  91.138  1.00287.88           C  
ANISOU 5754  CG  PHE B 488    35030  25378  48970     78   2898 -13035       C  
ATOM   5755  CD1 PHE B 488      54.763  96.227  92.148  1.00292.76           C  
ANISOU 5755  CD1 PHE B 488    35412  25774  50047    133   2653 -13872       C  
ATOM   5756  CD2 PHE B 488      53.756  94.193  91.384  1.00282.32           C  
ANISOU 5756  CD2 PHE B 488    34471  25510  47286    310   2752 -12774       C  
ATOM   5757  CE1 PHE B 488      54.131  96.083  93.369  1.00292.93           C  
ANISOU 5757  CE1 PHE B 488    35368  26419  49513    432   2282 -14424       C  
ATOM   5758  CE2 PHE B 488      53.116  94.043  92.598  1.00282.59           C  
ANISOU 5758  CE2 PHE B 488    34432  26152  46787    593   2407 -13297       C  
ATOM   5759  CZ  PHE B 488      53.302  94.992  93.595  1.00288.21           C  
ANISOU 5759  CZ  PHE B 488    34930  26658  47918    664   2175 -14122       C  
ATOM   5760  N   LEU B 489      56.431  92.585  89.576  1.00277.53           N  
ANISOU 5760  N   LEU B 489    33681  24655  47113   -535   3205 -11846       N  
ATOM   5761  CA  LEU B 489      56.487  91.191  89.959  1.00274.63           C  
ANISOU 5761  CA  LEU B 489    33271  25127  45948   -503   2980 -11742       C  
ATOM   5762  C   LEU B 489      57.908  90.719  90.228  1.00273.69           C  
ANISOU 5762  C   LEU B 489    32814  25061  46113   -818   2869 -12024       C  
ATOM   5763  O   LEU B 489      58.147  89.991  91.192  1.00271.30           O  
ANISOU 5763  O   LEU B 489    32334  25389  45359   -762   2502 -12403       O  
ATOM   5764  CB  LEU B 489      55.864  90.326  88.881  1.00273.66           C  
ANISOU 5764  CB  LEU B 489    33477  25232  45269   -439   3225 -10880       C  
ATOM   5765  CG  LEU B 489      55.747  88.853  89.257  1.00271.60           C  
ANISOU 5765  CG  LEU B 489    33204  25843  44147   -373   3000 -10727       C  
ATOM   5766  CD1 LEU B 489      54.977  88.665  90.562  1.00272.22           C  
ANISOU 5766  CD1 LEU B 489    33228  26556  43645    -77   2620 -11211       C  
ATOM   5767  CD2 LEU B 489      55.092  88.102  88.110  1.00267.07           C  
ANISOU 5767  CD2 LEU B 489    32955  25412  43105   -307   3251  -9892       C  
ATOM   5768  N   SER B 490      58.845  91.135  89.378  1.00274.95           N  
ANISOU 5768  N   SER B 490    32888  24556  47022  -1138   3191 -11836       N  
ATOM   5769  CA  SER B 490      60.253  90.795  89.571  1.00275.54           C  
ANISOU 5769  CA  SER B 490    32598  24592  47500  -1457   3115 -12129       C  
ATOM   5770  C   SER B 490      60.736  91.306  90.913  1.00276.00           C  
ANISOU 5770  C   SER B 490    32296  24709  47862  -1442   2689 -13077       C  
ATOM   5771  O   SER B 490      61.487  90.627  91.617  1.00270.16           O  
ANISOU 5771  O   SER B 490    31283  24402  46962  -1515   2371 -13453       O  
ATOM   5772  CB  SER B 490      61.130  91.430  88.490  1.00280.73           C  
ANISOU 5772  CB  SER B 490    33199  24405  49060  -1800   3579 -11850       C  
ATOM   5773  OG  SER B 490      60.633  91.140  87.202  1.00280.37           O  
ANISOU 5773  OG  SER B 490    33532  24223  48771  -1781   3994 -10986       O  
ATOM   5774  N   LYS B 491      60.285  92.508  91.259  1.00282.11           N  
ANISOU 5774  N   LYS B 491    33079  25044  49064  -1324   2669 -13468       N  
ATOM   5775  CA  LYS B 491      60.631  93.143  92.528  1.00291.94           C  
ANISOU 5775  CA  LYS B 491    34008  26292  50623  -1270   2260 -14414       C  
ATOM   5776  C   LYS B 491      60.108  92.331  93.706  1.00295.97           C  
ANISOU 5776  C   LYS B 491    34526  27738  50189   -962   1787 -14753       C  
ATOM   5777  O   LYS B 491      60.888  91.917  94.569  1.00301.09           O  
ANISOU 5777  O   LYS B 491    34885  28740  50772  -1009   1418 -15288       O  
ATOM   5778  CB  LYS B 491      60.081  94.585  92.596  1.00293.91           C  
ANISOU 5778  CB  LYS B 491    34318  25886  51466  -1163   2357 -14709       C  
ATOM   5779  CG  LYS B 491      60.339  95.365  93.891  1.00294.44           C  
ANISOU 5779  CG  LYS B 491    34080  25905  51887  -1074   1935 -15726       C  
ATOM   5780  CD  LYS B 491      59.570  96.683  93.906  1.00293.71           C  
ANISOU 5780  CD  LYS B 491    34115  25235  52246   -909   2042 -15929       C  
ATOM   5781  CE  LYS B 491      59.673  97.421  95.251  1.00297.89           C  
ANISOU 5781  CE  LYS B 491    34375  25791  53016   -759   1592 -16967       C  
ATOM   5782  NZ  LYS B 491      59.457  98.900  95.176  1.00304.24           N  
ANISOU 5782  NZ  LYS B 491    35158  25753  54684   -749   1724 -17295       N  
ATOM   5783  N   LYS B 492      58.795  92.109  93.748  1.00296.24           N  
ANISOU 5783  N   LYS B 492    34890  28166  49501   -639   1801 -14444       N  
ATOM   5784  CA  LYS B 492      58.179  91.355  94.846  1.00293.97           C  
ANISOU 5784  CA  LYS B 492    34646  28761  48287   -329   1415 -14707       C  
ATOM   5785  C   LYS B 492      58.765  89.943  95.006  1.00289.25           C  
ANISOU 5785  C   LYS B 492    33971  28817  47111   -413   1245 -14517       C  
ATOM   5786  O   LYS B 492      59.147  89.534  96.113  1.00288.97           O  
ANISOU 5786  O   LYS B 492    33754  29289  46751   -319    832 -15061       O  
ATOM   5787  CB  LYS B 492      56.660  91.293  94.668  1.00290.70           C  
ANISOU 5787  CB  LYS B 492    34590  28613  47250     -5   1543 -14295       C  
ATOM   5788  CG  LYS B 492      55.964  92.634  94.890  1.00294.65           C  
ANISOU 5788  CG  LYS B 492    35145  28636  48171    176   1581 -14656       C  
ATOM   5789  CD  LYS B 492      55.913  93.032  96.371  1.00296.95           C  
ANISOU 5789  CD  LYS B 492    35251  29245  48329    396   1152 -15565       C  
ATOM   5790  CE  LYS B 492      55.668  94.522  96.589  1.00301.61           C  
ANISOU 5790  CE  LYS B 492    35787  29179  49631    478   1168 -16080       C  
ATOM   5791  NZ  LYS B 492      55.884  94.942  98.002  1.00305.94           N  
ANISOU 5791  NZ  LYS B 492    36108  29970  50164    646    731 -17045       N  
ATOM   5792  N   ILE B 493      58.847  89.226  93.890  1.00287.01           N  
ANISOU 5792  N   ILE B 493    33835  28501  46712   -575   1558 -13751       N  
ATOM   5793  CA  ILE B 493      59.457  87.903  93.860  1.00288.17           C  
ANISOU 5793  CA  ILE B 493    33912  29169  46407   -684   1449 -13503       C  
ATOM   5794  C   ILE B 493      60.873  87.906  94.396  1.00285.90           C  
ANISOU 5794  C   ILE B 493    33223  28790  46612   -910   1194 -14082       C  
ATOM   5795  O   ILE B 493      61.210  87.077  95.246  1.00283.30           O  
ANISOU 5795  O   ILE B 493    32774  29080  45787   -826    822 -14359       O  
ATOM   5796  CB  ILE B 493      59.461  87.262  92.461  1.00294.33           C  
ANISOU 5796  CB  ILE B 493    34889  29807  47136   -855   1858 -12629       C  
ATOM   5797  CG1 ILE B 493      58.026  86.871  92.077  1.00295.25           C  
ANISOU 5797  CG1 ILE B 493    35389  30251  46541   -584   1998 -12057       C  
ATOM   5798  CG2 ILE B 493      60.339  86.002  92.450  1.00293.49           C  
ANISOU 5798  CG2 ILE B 493    34637  30133  46742  -1013   1733 -12479       C  
ATOM   5799  CD1 ILE B 493      57.860  86.342  90.662  1.00292.56           C  
ANISOU 5799  CD1 ILE B 493    35288  29750  46120   -697   2389 -11205       C  
ATOM   5800  N   GLU B 494      61.699  88.820  93.894  1.00284.04           N  
ANISOU 5800  N   GLU B 494    32779  27781  47358  -1193   1395 -14253       N  
ATOM   5801  CA  GLU B 494      63.093  88.930  94.348  1.00284.60           C  
ANISOU 5801  CA  GLU B 494    32416  27677  48043  -1435   1167 -14844       C  
ATOM   5802  C   GLU B 494      63.158  89.168  95.843  1.00288.44           C  
ANISOU 5802  C   GLU B 494    32707  28535  48351  -1216    617 -15729       C  
ATOM   5803  O   GLU B 494      63.963  88.547  96.547  1.00293.07           O  
ANISOU 5803  O   GLU B 494    33045  29514  48793  -1237    243 -16123       O  
ATOM   5804  CB  GLU B 494      63.761  90.136  93.680  1.00285.54           C  
ANISOU 5804  CB  GLU B 494    32346  26825  49318  -1738   1490 -14967       C  
ATOM   5805  CG  GLU B 494      64.339  89.854  92.317  1.00281.82           C  
ANISOU 5805  CG  GLU B 494    31904  25938  49237  -2057   1982 -14278       C  
ATOM   5806  CD  GLU B 494      65.744  89.270  92.413  1.00281.25           C  
ANISOU 5806  CD  GLU B 494    31429  25917  49514  -2336   1852 -14518       C  
ATOM   5807  OE1 GLU B 494      66.655  89.854  91.805  1.00283.46           O  
ANISOU 5807  OE1 GLU B 494    31469  25511  50722  -