CNRS Nantes University UFIP UFIP
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***  PROTEIN BINDING 11-DEC-10 3ASF  ***

elNémo ID: 21080403075964353

Job options:

ID        	=	 21080403075964353
JOBID     	=	 PROTEIN BINDING 11-DEC-10 3ASF
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    PROTEIN BINDING                         11-DEC-10   3ASF              
TITLE     MAMA MSR-1 C2                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MAGNETOSOME PROTEIN MAMA;                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 41-217;                                       
COMPND   5 SYNONYM: MAGNETOSOME PROTEIN MAMA, TPR-LIKE;                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MAGNETOSPIRILLUM GRYPHISWALDENSE;               
SOURCE   3 ORGANISM_TAXID: 431944;                                              
SOURCE   4 STRAIN: MSR-1;                                                       
SOURCE   5 GENE: MAMA, MGI495, MGR_4099;                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET52B                                    
KEYWDS    TETRATRICOPEPTIDE REPEATS (TPR) CONTAINING PROTEIN, TPR PROTEIN,      
KEYWDS   2 PROTEIN-PROTEIN INTERACTIONS, MAMA, CYTOSOL, PROTEIN BINDING         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.ZEYTUNI,G.DAVIDOV,R.ZARIVACH                                        
REVDAT   2   26-JUN-13 3ASF    1       JRNL                                     
REVDAT   1   20-JUL-11 3ASF    0                                                
JRNL        AUTH   N.ZEYTUNI,E.OZYAMAK,K.BEN-HARUSH,G.DAVIDOV,M.LEVIN,Y.GAT,    
JRNL        AUTH 2 T.MOYAL,A.BRIK,A.KOMEILI,R.ZARIVACH                          
JRNL        TITL   SELF-RECOGNITION MECHANISM OF MAMA, A MAGNETOSOME-ASSOCIATED 
JRNL        TITL 2 TPR-CONTAINING PROTEIN, PROMOTES COMPLEX ASSEMBLY            
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 108  E480 2011              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   21784982                                                     
JRNL        DOI    10.1073/PNAS.1103367108                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.39 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0110                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.39                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.20                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 22001                          
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) : 0.248                           
REMARK   3   R VALUE            (WORKING SET) : 0.247                           
REMARK   3   FREE R VALUE                     : 0.270                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1132                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.39                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.45                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1432                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.76                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3710                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 61                           
REMARK   3   BIN FREE R VALUE                    : 0.4690                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2693                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 65                                      
REMARK   3   SOLVENT ATOMS            : 82                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 73.86                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.11000                                              
REMARK   3    B22 (A**2) : 1.80000                                              
REMARK   3    B33 (A**2) : -5.11000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.38000                                             
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): 0.338         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.198         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.448        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.935                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.922                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2852 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3881 ; 1.374 ; 1.977       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   356 ; 5.479 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   141 ;40.529 ;23.759       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   471 ;20.941 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;12.459 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   425 ; 0.097 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2160 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1727 ; 1.136 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2769 ; 2.074 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1125 ; 1.980 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1105 ; 3.407 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 32                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    43        A    49                          
REMARK   3    ORIGIN FOR THE GROUP (A): -28.0315 -30.2605 -24.0604              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9320 T22:   0.1523                                     
REMARK   3      T33:   0.4384 T12:  -0.0591                                     
REMARK   3      T13:   0.0472 T23:  -0.1340                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  19.6903 L22:  18.7597                                     
REMARK   3      L33:  12.8697 L12:  -0.2037                                     
REMARK   3      L13: -15.9167 L23:   0.0421                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.9080 S12:  -0.1654 S13:  -1.9184                       
REMARK   3      S21:  -1.9319 S22:   0.3465 S23:  -0.5409                       
REMARK   3      S31:   1.5130 S32:   0.1217 S33:   1.5616                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    50        A    55                          
REMARK   3    ORIGIN FOR THE GROUP (A): -31.0680 -23.8987 -17.6530              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3620 T22:   0.1628                                     
REMARK   3      T33:   0.6904 T12:   0.1796                                     
REMARK   3      T13:  -0.0797 T23:  -0.2040                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8761 L22:  14.1432                                     
REMARK   3      L33:  49.3862 L12:   7.2734                                     
REMARK   3      L13:   1.7206 L23: -10.1074                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.1849 S12:  -0.6149 S13:  -0.1991                       
REMARK   3      S21:  -2.0507 S22:  -0.5788 S23:  -0.7438                       
REMARK   3      S31:   0.4672 S32:  -1.4291 S33:   1.7637                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    56        A    68                          
REMARK   3    ORIGIN FOR THE GROUP (A): -25.0672 -21.0317 -12.1896              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3339 T22:   0.3655                                     
REMARK   3      T33:   0.2113 T12:  -0.0150                                     
REMARK   3      T13:  -0.0317 T23:  -0.0564                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1015 L22:   3.9470                                     
REMARK   3      L33:   4.0044 L12:  -1.6597                                     
REMARK   3      L13:  -0.8002 L23:  -0.9858                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0801 S12:  -0.0102 S13:  -0.0858                       
REMARK   3      S21:  -0.3030 S22:  -0.0891 S23:   0.1833                       
REMARK   3      S31:   0.3419 S32:   0.0175 S33:   0.0090                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    69        A    79                          
REMARK   3    ORIGIN FOR THE GROUP (A): -25.0161 -18.2814 -27.2572              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5002 T22:   0.3329                                     
REMARK   3      T33:   0.1652 T12:   0.1177                                     
REMARK   3      T13:  -0.0486 T23:  -0.1242                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.2486 L22:   1.6905                                     
REMARK   3      L33:   1.7061 L12:   2.6743                                     
REMARK   3      L13:  -1.6192 L23:  -1.5902                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2233 S12:   0.1467 S13:  -0.1915                       
REMARK   3      S21:  -0.1193 S22:   0.1017 S23:   0.2117                       
REMARK   3      S31:   0.1425 S32:  -0.0816 S33:  -0.3249                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    80        A    88                          
REMARK   3    ORIGIN FOR THE GROUP (A): -28.9832 -14.5046 -19.7116              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3362 T22:   0.3044                                     
REMARK   3      T33:   0.2517 T12:   0.1302                                     
REMARK   3      T13:  -0.0471 T23:  -0.0632                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8630 L22:   5.2805                                     
REMARK   3      L33:   6.8230 L12:   4.2913                                     
REMARK   3      L13:  -1.3369 L23:   0.3102                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0144 S12:   0.0343 S13:   0.1041                       
REMARK   3      S21:   0.0025 S22:  -0.0390 S23:   0.1639                       
REMARK   3      S31:   0.2245 S32:  -0.2471 S33:   0.0535                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    89        A   106                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.2262  -9.2639 -19.3129              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3020 T22:   0.3326                                     
REMARK   3      T33:   0.1718 T12:   0.0681                                     
REMARK   3      T13:   0.0062 T23:  -0.0326                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6921 L22:   6.9281                                     
REMARK   3      L33:   1.3783 L12:  -2.0776                                     
REMARK   3      L13:   1.5045 L23:  -2.0767                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3141 S12:   0.2685 S13:   0.0878                       
REMARK   3      S21:  -0.1997 S22:  -0.4076 S23:  -0.3537                       
REMARK   3      S31:  -0.1280 S32:   0.2615 S33:   0.0935                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   107        A   122                          
REMARK   3    ORIGIN FOR THE GROUP (A): -33.1723  -4.8502 -20.0659              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3291 T22:   0.1939                                     
REMARK   3      T33:   0.2512 T12:   0.1191                                     
REMARK   3      T13:   0.0065 T23:  -0.0303                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5002 L22:   2.3676                                     
REMARK   3      L33:  17.2919 L12:   0.1607                                     
REMARK   3      L13:   1.2036 L23:   4.3750                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0766 S12:   0.3700 S13:   0.2742                       
REMARK   3      S21:   0.3128 S22:  -0.1650 S23:   0.3694                       
REMARK   3      S31:   0.2567 S32:  -0.0240 S33:   0.0883                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   123        A   127                          
REMARK   3    ORIGIN FOR THE GROUP (A): -23.0615  -1.2052 -13.0309              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3355 T22:   0.3117                                     
REMARK   3      T33:   0.2700 T12:   0.1039                                     
REMARK   3      T13:   0.0094 T23:  -0.0131                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.9622 L22:   4.3835                                     
REMARK   3      L33:   3.9749 L12:   3.1912                                     
REMARK   3      L13:  -0.5279 L23:  -2.1884                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0336 S12:  -0.2811 S13:  -0.5371                       
REMARK   3      S21:   0.0680 S22:  -0.3213 S23:  -0.1297                       
REMARK   3      S31:   0.0600 S32:   0.3151 S33:   0.3550                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   128        A   138                          
REMARK   3    ORIGIN FOR THE GROUP (A): -26.8592   4.7261 -15.5693              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3357 T22:   0.3237                                     
REMARK   3      T33:   0.2136 T12:   0.0389                                     
REMARK   3      T13:   0.0169 T23:  -0.0041                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.7734 L22:   1.2164                                     
REMARK   3      L33:   5.3719 L12:   2.6104                                     
REMARK   3      L13:   1.0425 L23:  -0.6356                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0913 S12:   0.2520 S13:  -0.1040                       
REMARK   3      S21:  -0.1870 S22:  -0.0595 S23:   0.0193                       
REMARK   3      S31:   0.1375 S32:   0.2834 S33:  -0.0319                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   139        A   144                          
REMARK   3    ORIGIN FOR THE GROUP (A): -39.8488   1.8372 -14.3913              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3441 T22:   0.3198                                     
REMARK   3      T33:   0.2741 T12:   0.0046                                     
REMARK   3      T13:   0.0120 T23:  -0.0354                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.5525 L22:   8.5074                                     
REMARK   3      L33:  12.5898 L12:   3.3143                                     
REMARK   3      L13:  -7.2959 L23:  -3.1655                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1055 S12:   0.0667 S13:   0.2519                       
REMARK   3      S21:  -0.0844 S22:   0.0676 S23:   0.1871                       
REMARK   3      S31:   0.1997 S32:  -0.4772 S33:   0.0379                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   145        A   159                          
REMARK   3    ORIGIN FOR THE GROUP (A): -32.7142   3.4329  -6.3991              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3247 T22:   0.2615                                     
REMARK   3      T33:   0.2177 T12:   0.0545                                     
REMARK   3      T13:   0.0338 T23:  -0.0073                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4545 L22:   3.4463                                     
REMARK   3      L33:   4.7211 L12:   3.9836                                     
REMARK   3      L13:  -0.1553 L23:  -0.0151                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0464 S12:  -0.0492 S13:  -0.0812                       
REMARK   3      S21:   0.1045 S22:  -0.1045 S23:  -0.0034                       
REMARK   3      S31:   0.1372 S32:   0.1425 S33:   0.0580                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   160        A   176                          
REMARK   3    ORIGIN FOR THE GROUP (A): -32.1974  11.9866  -4.8836              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3642 T22:   0.2964                                     
REMARK   3      T33:   0.2333 T12:  -0.0009                                     
REMARK   3      T13:  -0.0164 T23:  -0.0006                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9401 L22:   2.2718                                     
REMARK   3      L33:   1.6691 L12:   1.1207                                     
REMARK   3      L13:  -1.0444 L23:  -0.1752                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0515 S12:   0.1601 S13:   0.1818                       
REMARK   3      S21:  -0.0745 S22:   0.0017 S23:   0.1188                       
REMARK   3      S31:  -0.3063 S32:  -0.1004 S33:  -0.0532                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   177        A   192                          
REMARK   3    ORIGIN FOR THE GROUP (A): -31.7654   6.8872   3.6337              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3060 T22:   0.3029                                     
REMARK   3      T33:   0.1881 T12:   0.0083                                     
REMARK   3      T13:  -0.0206 T23:   0.0427                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8791 L22:   2.3811                                     
REMARK   3      L33:   2.8167 L12:   0.1184                                     
REMARK   3      L13:   0.0886 L23:   2.1334                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0948 S12:  -0.4878 S13:  -0.0597                       
REMARK   3      S21:  -0.0202 S22:   0.0858 S23:   0.0430                       
REMARK   3      S31:   0.0994 S32:   0.1303 S33:   0.0090                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   193        A   204                          
REMARK   3    ORIGIN FOR THE GROUP (A): -27.3899  18.4133   5.5927              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3397 T22:   0.3288                                     
REMARK   3      T33:   0.2792 T12:   0.0030                                     
REMARK   3      T13:  -0.0698 T23:  -0.0022                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3099 L22:   4.4719                                     
REMARK   3      L33:   8.0118 L12:   2.0333                                     
REMARK   3      L13:  -0.4773 L23:   2.3641                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0159 S12:  -0.1088 S13:   0.0215                       
REMARK   3      S21:  -0.0122 S22:  -0.1117 S23:  -0.0536                       
REMARK   3      S31:  -0.3921 S32:   0.1049 S33:   0.0958                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   205        A   210                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.4888   9.2146  12.5817              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3684 T22:   0.3402                                     
REMARK   3      T33:   0.1483 T12:  -0.0884                                     
REMARK   3      T13:  -0.0628 T23:   0.0391                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3470 L22:  10.0034                                     
REMARK   3      L33:   8.8600 L12:   0.4568                                     
REMARK   3      L13:  -3.2227 L23:   5.9716                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3869 S12:  -0.3065 S13:  -0.1402                       
REMARK   3      S21:   0.7134 S22:  -0.7638 S23:   0.2074                       
REMARK   3      S31:  -0.0399 S32:   0.0278 S33:   0.3769                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   211        A   216                          
REMARK   3    ORIGIN FOR THE GROUP (A): -32.6541   0.3163  14.7730              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3691 T22:   0.2338                                     
REMARK   3      T33:   0.4949 T12:  -0.1841                                     
REMARK   3      T13:  -0.0762 T23:   0.2503                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.7085 L22:  87.4940                                     
REMARK   3      L33:   4.5760 L12:  24.1887                                     
REMARK   3      L13:  -5.5348 L23: -20.0020                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1221 S12:  -0.0236 S13:  -1.2023                       
REMARK   3      S21:   1.4352 S22:  -0.4926 S23:  -4.3216                       
REMARK   3      S31:  -0.2829 S32:   0.0069 S33:   0.6147                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    44        B    55                          
REMARK   3    ORIGIN FOR THE GROUP (A): -23.6205  33.2078 -24.6024              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8072 T22:   0.4627                                     
REMARK   3      T33:   0.8807 T12:   0.0309                                     
REMARK   3      T13:   0.0556 T23:   0.4343                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.3492 L22:   1.4973                                     
REMARK   3      L33:   1.5972 L12:  -3.3325                                     
REMARK   3      L13:  -4.1479 L23:   1.0165                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7197 S12:  -1.6234 S13:  -0.0886                       
REMARK   3      S21:   0.3755 S22:   0.8611 S23:   0.6897                       
REMARK   3      S31:   0.1895 S32:   0.4827 S33:  -0.1414                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    56        B    68                          
REMARK   3    ORIGIN FOR THE GROUP (A): -19.6073  26.0059 -33.4976              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5856 T22:   0.3768                                     
REMARK   3      T33:   0.2112 T12:  -0.2576                                     
REMARK   3      T13:  -0.0374 T23:   0.1486                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.7991 L22:   0.2540                                     
REMARK   3      L33:   0.7217 L12:   1.4930                                     
REMARK   3      L13:  -0.7492 L23:  -0.1117                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1459 S12:  -0.5008 S13:   0.2605                       
REMARK   3      S21:   0.0094 S22:  -0.0962 S23:   0.0415                       
REMARK   3      S31:  -0.3129 S32:  -0.1168 S33:  -0.0496                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    69        B    86                          
REMARK   3    ORIGIN FOR THE GROUP (A): -22.3082  22.4246 -21.2025              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5981 T22:   0.3053                                     
REMARK   3      T33:   0.4488 T12:  -0.2222                                     
REMARK   3      T13:   0.1996 T23:   0.1125                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.6670 L22:   0.9489                                     
REMARK   3      L33:   4.7674 L12:   0.0346                                     
REMARK   3      L13:   1.1871 L23:   0.6298                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0221 S12:   0.4875 S13:   0.4172                       
REMARK   3      S21:   0.4216 S22:   0.1886 S23:   0.5176                       
REMARK   3      S31:  -0.4279 S32:   0.8902 S33:  -0.2107                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    87        B    97                          
REMARK   3    ORIGIN FOR THE GROUP (A): -16.7835  14.9817 -31.1063              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2314 T22:   0.7141                                     
REMARK   3      T33:   0.1871 T12:  -0.2723                                     
REMARK   3      T13:   0.0699 T23:  -0.0867                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.7544 L22:   2.3621                                     
REMARK   3      L33:  12.5842 L12:  -4.7200                                     
REMARK   3      L13:  -3.5398 L23:  -1.1542                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3363 S12:  -0.3919 S13:   0.0436                       
REMARK   3      S21:  -0.3218 S22:   0.2859 S23:   0.0883                       
REMARK   3      S31:   0.3202 S32:   0.6740 S33:  -0.6223                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    98        B   109                          
REMARK   3    ORIGIN FOR THE GROUP (A): -22.7182  12.2945 -22.5559              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3453 T22:   0.4402                                     
REMARK   3      T33:   0.1021 T12:  -0.0167                                     
REMARK   3      T13:  -0.0560 T23:   0.0599                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.9079 L22:   5.9176                                     
REMARK   3      L33:   1.7324 L12:  -1.4918                                     
REMARK   3      L13:  -3.6753 L23:   0.5785                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1363 S12:  -0.0444 S13:  -0.3174                       
REMARK   3      S21:   0.1128 S22:  -0.0235 S23:   0.0846                       
REMARK   3      S31:   0.0509 S32:   0.1191 S33:   0.1599                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   110        B   124                          
REMARK   3    ORIGIN FOR THE GROUP (A): -29.0599  10.7351 -29.1072              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2863 T22:   0.3691                                     
REMARK   3      T33:   0.3445 T12:   0.0096                                     
REMARK   3      T13:  -0.0846 T23:  -0.0704                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7015 L22:   1.4883                                     
REMARK   3      L33:   7.8599 L12:  -0.8702                                     
REMARK   3      L13:  -1.9352 L23:   3.2604                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1026 S12:  -0.0819 S13:  -0.1360                       
REMARK   3      S21:  -0.1431 S22:  -0.0008 S23:   0.2429                       
REMARK   3      S31:  -0.1652 S32:   0.3060 S33:   0.1034                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   125        B   131                          
REMARK   3    ORIGIN FOR THE GROUP (A): -20.5403   1.1705 -33.4689              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2616 T22:   0.4485                                     
REMARK   3      T33:   0.1796 T12:   0.1946                                     
REMARK   3      T13:   0.0897 T23:  -0.0488                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  21.1364 L22:   2.7690                                     
REMARK   3      L33:   4.2306 L12:   7.5525                                     
REMARK   3      L13:   7.5188 L23:   3.0136                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0545 S12:   0.5776 S13:  -1.0268                       
REMARK   3      S21:   0.0181 S22:   0.2278 S23:  -0.3516                       
REMARK   3      S31:   0.0784 S32:   0.4472 S33:  -0.2823                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   132        B   142                          
REMARK   3    ORIGIN FOR THE GROUP (A): -32.9408   4.1018 -31.2506              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3867 T22:   0.3975                                     
REMARK   3      T33:   0.2719 T12:   0.0716                                     
REMARK   3      T13:  -0.0151 T23:  -0.0401                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3498 L22:   5.5533                                     
REMARK   3      L33:   0.2918 L12:  -0.4857                                     
REMARK   3      L13:  -0.7123 L23:  -0.7648                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0984 S12:  -0.2678 S13:   0.1015                       
REMARK   3      S21:   0.0374 S22:  -0.0580 S23:   0.1217                       
REMARK   3      S31:   0.0021 S32:   0.0667 S33:  -0.0404                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   143        B   156                          
REMARK   3    ORIGIN FOR THE GROUP (A): -32.2003   6.3569 -40.7443              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3110 T22:   0.3235                                     
REMARK   3      T33:   0.3363 T12:   0.0498                                     
REMARK   3      T13:  -0.0079 T23:   0.0540                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9166 L22:   3.1937                                     
REMARK   3      L33:   7.1100 L12:  -0.2706                                     
REMARK   3      L13:  -1.8350 L23:   1.7259                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1346 S12:   0.2464 S13:   0.6513                       
REMARK   3      S21:  -0.1539 S22:  -0.0337 S23:  -0.0660                       
REMARK   3      S31:   0.1156 S32:   0.2839 S33:  -0.1009                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   157        B   164                          
REMARK   3    ORIGIN FOR THE GROUP (A): -27.9704  -7.3333 -37.5304              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6090 T22:   0.4885                                     
REMARK   3      T33:   0.2600 T12:   0.2356                                     
REMARK   3      T13:  -0.0585 T23:  -0.0256                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5002 L22:   8.4972                                     
REMARK   3      L33:   4.6092 L12:   2.0056                                     
REMARK   3      L13:   1.4849 L23:   6.2558                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1122 S12:   0.1256 S13:  -0.0621                       
REMARK   3      S21:   0.3184 S22:   0.2263 S23:  -0.5072                       
REMARK   3      S31:   0.2404 S32:   0.1690 S33:  -0.3385                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   165        B   171                          
REMARK   3    ORIGIN FOR THE GROUP (A): -34.5847  -5.0144 -42.1538              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4989 T22:   0.2876                                     
REMARK   3      T33:   0.1855 T12:   0.0801                                     
REMARK   3      T13:  -0.0911 T23:  -0.2043                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.1820 L22:  13.0198                                     
REMARK   3      L33:  22.4117 L12: -11.5415                                     
REMARK   3      L13:  15.5986 L23: -12.5252                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.0968 S12:   0.0989 S13:  -0.6445                       
REMARK   3      S21:  -0.8532 S22:  -0.3814 S23:   0.6935                       
REMARK   3      S31:   1.5187 S32:  -0.2102 S33:  -0.7154                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   172        B   184                          
REMARK   3    ORIGIN FOR THE GROUP (A): -33.5150   3.8968 -50.0976              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3328 T22:   0.3600                                     
REMARK   3      T33:   0.3074 T12:   0.0732                                     
REMARK   3      T13:  -0.0359 T23:   0.0115                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8119 L22:   2.9765                                     
REMARK   3      L33:   5.5960 L12:  -0.8749                                     
REMARK   3      L13:   2.6592 L23:   1.5876                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1678 S12:   0.4634 S13:   0.4302                       
REMARK   3      S21:  -0.2936 S22:  -0.1208 S23:   0.2780                       
REMARK   3      S31:  -0.0173 S32:   0.4162 S33:  -0.0470                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 29                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   185        B   193                          
REMARK   3    ORIGIN FOR THE GROUP (A): -28.6164  -7.4816 -49.4507              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4756 T22:   0.3456                                     
REMARK   3      T33:   0.2491 T12:   0.1597                                     
REMARK   3      T13:  -0.1475 T23:  -0.2647                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0640 L22:  15.5019                                     
REMARK   3      L33:  10.7781 L12:   5.1641                                     
REMARK   3      L13:  -4.8270 L23: -12.7797                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3220 S12:   0.3900 S13:  -0.6473                       
REMARK   3      S21:  -0.2579 S22:  -0.7478 S23:  -0.2231                       
REMARK   3      S31:   0.0580 S32:   0.3412 S33:   0.4258                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 30                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   194        B   202                          
REMARK   3    ORIGIN FOR THE GROUP (A): -32.1920 -14.3200 -50.7759              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.0971 T22:   0.3746                                     
REMARK   3      T33:   0.6083 T12:  -0.4903                                     
REMARK   3      T13:  -0.4499 T23:  -0.2590                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  13.4059 L22:  31.8679                                     
REMARK   3      L33:   5.2269 L12:  20.6516                                     
REMARK   3      L13:   7.7666 L23:  12.1320                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0545 S12:   0.6097 S13:  -0.9748                       
REMARK   3      S21:   0.1805 S22:   0.7956 S23:  -1.4514                       
REMARK   3      S31:   1.1910 S32:  -0.0003 S33:  -0.7411                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 31                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   203        B   207                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.4281  -6.6435 -56.8996              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8686 T22:   1.0575                                     
REMARK   3      T33:   0.3277 T12:  -0.1945                                     
REMARK   3      T13:  -0.3074 T23:   0.2515                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4384 L22:   0.2565                                     
REMARK   3      L33:  27.0174 L12:   0.2912                                     
REMARK   3      L13:  -2.9465 L23:  -1.3057                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4461 S12:   0.4656 S13:   0.1672                       
REMARK   3      S21:  -0.2508 S22:   0.5402 S23:   0.1753                       
REMARK   3      S31:   3.8633 S32:  -1.4585 S33:  -0.0941                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 32                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   208        B   213                          
REMARK   3    ORIGIN FOR THE GROUP (A): -26.2739   0.5700 -60.4202              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3743 T22:   0.8651                                     
REMARK   3      T33:   0.7017 T12:  -0.0283                                     
REMARK   3      T13:   0.1069 T23:   0.1102                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  15.0294 L22:   4.7778                                     
REMARK   3      L33:  31.0533 L12:  -8.4616                                     
REMARK   3      L13: -21.6024 L23:  12.1600                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1251 S12:   0.6612 S13:  -0.1936                       
REMARK   3      S21:  -0.0909 S22:  -0.4057 S23:   0.0104                       
REMARK   3      S31:  -0.2121 S32:  -0.9054 S33:   0.2806                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS                   
REMARK   3  U VALUES: WITH TLS ADDED                                            
REMARK   4                                                                      
REMARK   4 3ASF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-DEC-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB029638.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-JUL-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22523                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.390                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.07900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 15.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.44                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55800                            
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: COOT                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 3AS5                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.69                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFAT, HEPES, NACL, PH 7.5,    
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 286K                     
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       43.56450            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.68850            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       43.56450            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       36.68850            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    39                                                      
REMARK 465     GLY A    40                                                      
REMARK 465     ASN A    41                                                      
REMARK 465     ASP A    42                                                      
REMARK 465     VAL A   217                                                      
REMARK 465     GLU A   218                                                      
REMARK 465     LEU A   219                                                      
REMARK 465     ALA A   220                                                      
REMARK 465     LEU A   221                                                      
REMARK 465     VAL A   222                                                      
REMARK 465     PRO A   223                                                      
REMARK 465     ARG A   224                                                      
REMARK 465     MET B    39                                                      
REMARK 465     GLY B    40                                                      
REMARK 465     ASN B    41                                                      
REMARK 465     ASP B    42                                                      
REMARK 465     ASP B    43                                                      
REMARK 465     ARG B   214                                                      
REMARK 465     SER B   215                                                      
REMARK 465     ALA B   216                                                      
REMARK 465     VAL B   217                                                      
REMARK 465     GLU B   218                                                      
REMARK 465     LEU B   219                                                      
REMARK 465     ALA B   220                                                      
REMARK 465     LEU B   221                                                      
REMARK 465     VAL B   222                                                      
REMARK 465     PRO B   223                                                      
REMARK 465     ARG B   224                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASP B 212    CG   OD1  OD2                                       
REMARK 470     GLU B 213    CG   CD   OE1  OE2                                  
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   O2   SO4 B    12     O    HOH B   239              2.00            
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    ALA A 110       76.86   -154.07                                   
REMARK 500    ALA B  77       42.83   -142.82                                   
REMARK 500    THR B  93       51.01    -92.23                                   
REMARK 500    ASN B 144       71.44   -118.32                                   
REMARK 500    PHE B 164      -60.78     17.12                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 4                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 10                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 24                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 31                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 32                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 33                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 9                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 12                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 28                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 29                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 34                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3AS4   RELATED DB: PDB                                   
REMARK 900 HOMOLOGOUS STRUCTURE                                                 
REMARK 900 RELATED ID: 3AS5   RELATED DB: PDB                                   
REMARK 900 HOMOLOGOUS STRUCTURE                                                 
REMARK 900 RELATED ID: 3AS8   RELATED DB: PDB                                   
REMARK 900 DIFFERENT PACKING                                                    
REMARK 900 RELATED ID: 3ASD   RELATED DB: PDB                                   
REMARK 900 R50E MUTANT OF HOMOLOGOUS STRUCTURE                                  
REMARK 900 RELATED ID: 3ASG   RELATED DB: PDB                                   
REMARK 900 D159K MUTANT OF HOMOLOGOUS STRUCTURE                                 
REMARK 900 RELATED ID: 3ASH   RELATED DB: PDB                                   
REMARK 900 D159K MUTANT OF HOMOLOGOUS STRUCTURE                                 
DBREF  3ASF A   41   217  UNP    Q93DY9   Q93DY9_9PROT    41    217             
DBREF  3ASF B   41   217  UNP    Q93DY9   Q93DY9_9PROT    41    217             
SEQADV 3ASF MET A   39  UNP  Q93DY9              EXPRESSION TAG                 
SEQADV 3ASF GLY A   40  UNP  Q93DY9              EXPRESSION TAG                 
SEQADV 3ASF GLU A  218  UNP  Q93DY9              EXPRESSION TAG                 
SEQADV 3ASF LEU A  219  UNP  Q93DY9              EXPRESSION TAG                 
SEQADV 3ASF ALA A  220  UNP  Q93DY9              EXPRESSION TAG                 
SEQADV 3ASF LEU A  221  UNP  Q93DY9              EXPRESSION TAG                 
SEQADV 3ASF VAL A  222  UNP  Q93DY9              EXPRESSION TAG                 
SEQADV 3ASF PRO A  223  UNP  Q93DY9              EXPRESSION TAG                 
SEQADV 3ASF ARG A  224  UNP  Q93DY9              EXPRESSION TAG                 
SEQADV 3ASF MET B   39  UNP  Q93DY9              EXPRESSION TAG                 
SEQADV 3ASF GLY B   40  UNP  Q93DY9              EXPRESSION TAG                 
SEQADV 3ASF GLU B  218  UNP  Q93DY9              EXPRESSION TAG                 
SEQADV 3ASF LEU B  219  UNP  Q93DY9              EXPRESSION TAG                 
SEQADV 3ASF ALA B  220  UNP  Q93DY9              EXPRESSION TAG                 
SEQADV 3ASF LEU B  221  UNP  Q93DY9              EXPRESSION TAG                 
SEQADV 3ASF VAL B  222  UNP  Q93DY9              EXPRESSION TAG                 
SEQADV 3ASF PRO B  223  UNP  Q93DY9              EXPRESSION TAG                 
SEQADV 3ASF ARG B  224  UNP  Q93DY9              EXPRESSION TAG                 
SEQRES   1 A  186  MET GLY ASN ASP ASP ILE ARG GLN VAL TYR TYR ARG ASP          
SEQRES   2 A  186  LYS GLY ILE SER HIS ALA LYS ALA GLY ARG TYR SER GLU          
SEQRES   3 A  186  ALA VAL VAL MET LEU GLU GLN VAL TYR ASP ALA ASP ALA          
SEQRES   4 A  186  PHE ASP VAL GLU VAL ALA LEU HIS LEU GLY ILE ALA TYR          
SEQRES   5 A  186  VAL LYS THR GLY ALA VAL ASP ARG GLY THR GLU LEU LEU          
SEQRES   6 A  186  GLU ARG SER ILE ALA ASP ALA PRO ASP ASN ILE LYS VAL          
SEQRES   7 A  186  ALA THR VAL LEU GLY LEU THR TYR VAL GLN VAL GLN LYS          
SEQRES   8 A  186  TYR ASP LEU ALA VAL PRO LEU LEU VAL LYS VAL ALA GLU          
SEQRES   9 A  186  ALA ASN PRO VAL ASN PHE ASN VAL ARG PHE ARG LEU GLY          
SEQRES  10 A  186  VAL ALA LEU ASP ASN LEU GLY ARG PHE ASP GLU ALA ILE          
SEQRES  11 A  186  ASP SER PHE LYS ILE ALA LEU GLY LEU ARG PRO ASN GLU          
SEQRES  12 A  186  GLY LYS VAL HIS ARG ALA ILE ALA TYR SER TYR GLU GLN          
SEQRES  13 A  186  MET GLY SER HIS GLU GLU ALA LEU PRO HIS PHE LYS LYS          
SEQRES  14 A  186  ALA ASN GLU LEU ASP GLU ARG SER ALA VAL GLU LEU ALA          
SEQRES  15 A  186  LEU VAL PRO ARG                                              
SEQRES   1 B  186  MET GLY ASN ASP ASP ILE ARG GLN VAL TYR TYR ARG ASP          
SEQRES   2 B  186  LYS GLY ILE SER HIS ALA LYS ALA GLY ARG TYR SER GLU          
SEQRES   3 B  186  ALA VAL VAL MET LEU GLU GLN VAL TYR ASP ALA ASP ALA          
SEQRES   4 B  186  PHE ASP VAL GLU VAL ALA LEU HIS LEU GLY ILE ALA TYR          
SEQRES   5 B  186  VAL LYS THR GLY ALA VAL ASP ARG GLY THR GLU LEU LEU          
SEQRES   6 B  186  GLU ARG SER ILE ALA ASP ALA PRO ASP ASN ILE LYS VAL          
SEQRES   7 B  186  ALA THR VAL LEU GLY LEU THR TYR VAL GLN VAL GLN LYS          
SEQRES   8 B  186  TYR ASP LEU ALA VAL PRO LEU LEU VAL LYS VAL ALA GLU          
SEQRES   9 B  186  ALA ASN PRO VAL ASN PHE ASN VAL ARG PHE ARG LEU GLY          
SEQRES  10 B  186  VAL ALA LEU ASP ASN LEU GLY ARG PHE ASP GLU ALA ILE          
SEQRES  11 B  186  ASP SER PHE LYS ILE ALA LEU GLY LEU ARG PRO ASN GLU          
SEQRES  12 B  186  GLY LYS VAL HIS ARG ALA ILE ALA TYR SER TYR GLU GLN          
SEQRES  13 B  186  MET GLY SER HIS GLU GLU ALA LEU PRO HIS PHE LYS LYS          
SEQRES  14 B  186  ALA ASN GLU LEU ASP GLU ARG SER ALA VAL GLU LEU ALA          
SEQRES  15 B  186  LEU VAL PRO ARG                                              
HET    SO4  A   1       5                                                       
HET    SO4  A   2       5                                                       
HET    SO4  A   4       5                                                       
HET    SO4  A  10       5                                                       
HET    SO4  A  24       5                                                       
HET    SO4  A  31       5                                                       
HET    SO4  A  32       5                                                       
HET    SO4  A  33       5                                                       
HET    SO4  B   9       5                                                       
HET    SO4  B  12       5                                                       
HET    SO4  B  28       5                                                       
HET    SO4  B  29       5                                                       
HET    SO4  B  34       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  SO4    13(O4 S 2-)                                                  
FORMUL  16  HOH   *82(H2 O)                                                     
HELIX    1   1 ASP A   43  ALA A   59  1                                  17    
HELIX    2   2 ARG A   61  GLU A   70  1                                  10    
HELIX    3   3 ASP A   79  THR A   93  1                                  15    
HELIX    4   4 ALA A   95  ALA A  110  1                                  16    
HELIX    5   5 ASN A  113  VAL A  127  1                                  15    
HELIX    6   6 LYS A  129  ASN A  144  1                                  16    
HELIX    7   7 ASN A  147  LEU A  161  1                                  15    
HELIX    8   8 ARG A  163  ARG A  178  1                                  16    
HELIX    9   9 GLU A  181  MET A  195  1                                  15    
HELIX   10  10 SER A  197  ARG A  214  1                                  18    
HELIX   11  11 ILE B   44  ILE B   54  1                                  11    
HELIX   12  12 ILE B   54  ALA B   59  1                                   6    
HELIX   13  13 ARG B   61  GLU B   70  1                                  10    
HELIX   14  14 ASP B   79  THR B   93  1                                  15    
HELIX   15  15 ALA B   95  ALA B  110  1                                  16    
HELIX   16  16 ASN B  113  VAL B  127  1                                  15    
HELIX   17  17 LYS B  129  ASN B  144  1                                  16    
HELIX   18  18 ASN B  147  LEU B  161  1                                  15    
HELIX   19  19 PHE B  164  ARG B  178  1                                  15    
HELIX   20  20 GLU B  181  GLY B  196  1                                  16    
HELIX   21  21 SER B  197  ASP B  212  1                                  16    
SITE     1 AC1  4 ALA A  95  VAL A  96  ASP A  97  ARG A  98                    
SITE     1 AC2  3 ARG A 178  HOH A 239  HOH A 261                               
SITE     1 AC3  2 TYR A  62  HIS A 198                                          
SITE     1 AC4  2 ARG A 153  HOH A 250                                          
SITE     1 AC5  4 ARG A 163  PHE A 164  ASP A 165  GLU A 166                    
SITE     1 AC6  4 GLN A 126  ASN A 149  ARG A 153  HOH A 255                    
SITE     1 AC7  4 LYS A 172  HOH A 227  HOH A 254  HOH A 259                    
SITE     1 AC8  3 LYS A  52  HIS A  56  ARG A  61                               
SITE     1 AC9  3 ASN B 149  ARG B 178  HOH B 237                               
SITE     1 BC1  5 LYS B  52  SER B  55  ALA B  59  ARG B  61                    
SITE     2 BC1  5 HOH B 239                                                     
SITE     1 BC2  2 ARG B 153  HOH B 228                                          
SITE     1 BC3  3 LEU B 122  ASN B 149  ARG B 153                               
SITE     1 BC4  4 VAL B 146  PHE B 148  ARG B 178  HOH B 237                    
CRYST1   87.129   73.377   90.224  90.00  93.70  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011477  0.000000  0.000743        0.00000                         
SCALE2      0.000000  0.013628  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011107        0.00000                         
ATOM      1  N   ASP A  43     -29.722 -33.636 -29.724  1.00199.52           N  
ANISOU    1  N   ASP A  43    32978  19870  22960  -4323   2474  -4927       N  
ATOM      2  CA  ASP A  43     -29.702 -32.178 -29.398  1.00188.74           C  
ANISOU    2  CA  ASP A  43    31184  19309  21219  -3694   1237  -4201       C  
ATOM      3  C   ASP A  43     -30.059 -31.833 -27.942  1.00177.89           C  
ANISOU    3  C   ASP A  43    28851  18168  20568  -3030    773  -3550       C  
ATOM      4  O   ASP A  43     -29.897 -30.681 -27.528  1.00170.54           O  
ANISOU    4  O   ASP A  43    27564  17718  19513  -2532     63  -3014       O  
ATOM      5  CB  ASP A  43     -30.590 -31.394 -30.372  1.00194.91           C  
ANISOU    5  CB  ASP A  43    32226  20988  20840  -4159     27  -4543       C  
ATOM      6  CG  ASP A  43     -29.784 -30.567 -31.358  1.00198.42           C  
ANISOU    6  CG  ASP A  43    33423  21555  20412  -4013     28  -4315       C  
ATOM      7  OD1 ASP A  43     -29.739 -30.935 -32.550  1.00212.61           O  
ANISOU    7  OD1 ASP A  43    36115  23381  21286  -4644    296  -4933       O  
ATOM      8  OD2 ASP A  43     -29.187 -29.552 -30.938  1.00190.06           O  
ANISOU    8  OD2 ASP A  43    32099  20528  19587  -3318   -123  -3581       O  
ATOM      9  N   ILE A  44     -30.534 -32.820 -27.174  1.00177.55           N  
ANISOU    9  N   ILE A  44    28472  17712  21276  -3052   1340  -3633       N  
ATOM     10  CA  ILE A  44     -30.828 -32.642 -25.734  1.00168.58           C  
ANISOU   10  CA  ILE A  44    26582  16730  20740  -2388   1135  -2990       C  
ATOM     11  C   ILE A  44     -29.541 -32.342 -24.929  1.00160.98           C  
ANISOU   11  C   ILE A  44    25347  15801  20017  -1497   1439  -2153       C  
ATOM     12  O   ILE A  44     -29.587 -31.846 -23.801  1.00155.60           O  
ANISOU   12  O   ILE A  44    24104  15552  19464   -942   1028  -1632       O  
ATOM     13  CB  ILE A  44     -31.678 -33.841 -25.159  1.00174.50           C  
ANISOU   13  CB  ILE A  44    27140  16906  22256  -2611   1905  -3251       C  
ATOM     14  CG1 ILE A  44     -33.182 -33.535 -25.233  1.00176.79           C  
ANISOU   14  CG1 ILE A  44    27039  17647  22485  -3188   1002  -3785       C  
ATOM     15  CG2 ILE A  44     -31.314 -34.190 -23.714  1.00171.18           C  
ANISOU   15  CG2 ILE A  44    26303  16252  22483  -1677   2528  -2350       C  
ATOM     16  CD1 ILE A  44     -33.768 -33.509 -26.644  1.00185.11           C  
ANISOU   16  CD1 ILE A  44    28401  19088  22843  -4185    410  -4748       C  
ATOM     17  N   ARG A  45     -28.402 -32.642 -25.548  1.00161.47           N  
ANISOU   17  N   ARG A  45    25778  15463  20108  -1428   2170  -2103       N  
ATOM     18  CA  ARG A  45     -27.080 -32.180 -25.121  1.00155.93           C  
ANISOU   18  CA  ARG A  45    24710  14961  19573   -742   2290  -1471       C  
ATOM     19  C   ARG A  45     -26.998 -30.666 -24.847  1.00146.99           C  
ANISOU   19  C   ARG A  45    23206  14622  18021   -617   1194  -1371       C  
ATOM     20  O   ARG A  45     -26.386 -30.243 -23.865  1.00144.16           O  
ANISOU   20  O   ARG A  45    22184  14747  17841    -81    979   -928       O  
ATOM     21  CB  ARG A  45     -26.061 -32.562 -26.197  1.00162.06           C  
ANISOU   21  CB  ARG A  45    26043  15100  20431   -920   3225  -1644       C  
ATOM     22  CG  ARG A  45     -26.423 -32.077 -27.619  1.00165.14           C  
ANISOU   22  CG  ARG A  45    27289  15450  20004  -1720   2932  -2381       C  
ATOM     23  CD  ARG A  45     -25.255 -32.224 -28.556  1.00171.49           C  
ANISOU   23  CD  ARG A  45    28656  15649  20852  -1788   3915  -2458       C  
ATOM     24  NE  ARG A  45     -24.018 -32.268 -27.788  1.00170.83           N  
ANISOU   24  NE  ARG A  45    27821  15469  21615   -995   4438  -1730       N  
ATOM     25  CZ  ARG A  45     -22.831 -32.597 -28.280  0.44177.27           C  
ANISOU   25  CZ  ARG A  45    28774  15645  22934   -822   5550  -1574       C  
ATOM     26  NH1 ARG A  45     -21.775 -32.623 -27.479  1.00177.38           N  
ANISOU   26  NH1 ARG A  45    27819  15813  23761    -41   5821   -849       N  
ATOM     27  NH2 ARG A  45     -22.691 -32.902 -29.564  0.93185.99           N  
ANISOU   27  NH2 ARG A  45    30937  16027  23702  -1427   6398  -2147       N  
ATOM     28  N   GLN A  46     -27.598 -29.865 -25.732  1.00143.65           N  
ANISOU   28  N   GLN A  46    23206  14351  17023  -1115    586  -1787       N  
ATOM     29  CA  GLN A  46     -27.672 -28.410 -25.573  1.00136.47           C  
ANISOU   29  CA  GLN A  46    22047  13960  15846  -1019   -185  -1687       C  
ATOM     30  C   GLN A  46     -28.813 -28.047 -24.633  1.00130.85           C  
ANISOU   30  C   GLN A  46    20862  13658  15195   -939   -864  -1601       C  
ATOM     31  O   GLN A  46     -28.707 -27.080 -23.884  1.00127.26           O  
ANISOU   31  O   GLN A  46    19974  13567  14811   -710  -1201  -1445       O  
ATOM     32  CB  GLN A  46     -27.877 -27.704 -26.922  1.00139.81           C  
ANISOU   32  CB  GLN A  46    23154  14342  15624  -1386   -406  -1919       C  
ATOM     33  CG  GLN A  46     -26.694 -27.778 -27.886  1.00144.71           C  
ANISOU   33  CG  GLN A  46    24353  14494  16134  -1457    378  -1997       C  
ATOM     34  CD  GLN A  46     -27.122 -27.732 -29.356  1.00153.17           C  
ANISOU   34  CD  GLN A  46    26407  15498  16291  -1912    341  -2298       C  
ATOM     35  OE1 GLN A  46     -27.839 -26.827 -29.780  1.00154.42           O  
ANISOU   35  OE1 GLN A  46    26727  16085  15858  -1917   -355  -2166       O  
ATOM     36  NE2 GLN A  46     -26.673 -28.715 -30.136  1.00160.99           N  
ANISOU   36  NE2 GLN A  46    28069  15978  17119  -2261   1161  -2664       N  
ATOM     37  N   VAL A  47     -29.902 -28.817 -24.673  1.00130.73           N  
ANISOU   37  N   VAL A  47    20917  13522  15229  -1207   -939  -1800       N  
ATOM     38  CA  VAL A  47     -31.056 -28.544 -23.814  1.00126.53           C  
ANISOU   38  CA  VAL A  47    19917  13250  14908  -1145  -1425  -1722       C  
ATOM     39  C   VAL A  47     -30.697 -28.656 -22.338  1.00122.18           C  
ANISOU   39  C   VAL A  47    18900  12840  14681   -616  -1176  -1331       C  
ATOM     40  O   VAL A  47     -31.229 -27.904 -21.530  1.00119.78           O  
ANISOU   40  O   VAL A  47    18255  12838  14415   -480  -1544  -1227       O  
ATOM     41  CB  VAL A  47     -32.290 -29.447 -24.120  1.00131.84           C  
ANISOU   41  CB  VAL A  47    20608  13726  15758  -1617  -1433  -2118       C  
ATOM     42  CG1 VAL A  47     -32.362 -30.643 -23.176  1.00133.29           C  
ANISOU   42  CG1 VAL A  47    20629  13454  16558  -1427   -613  -2011       C  
ATOM     43  CG2 VAL A  47     -33.574 -28.641 -23.996  1.00131.79           C  
ANISOU   43  CG2 VAL A  47    20168  14105  15799  -1716  -2237  -2115       C  
ATOM     44  N   TYR A  48     -29.816 -29.597 -21.991  1.00122.33           N  
ANISOU   44  N   TYR A  48    18917  12672  14891   -279   -495  -1067       N  
ATOM     45  CA  TYR A  48     -29.424 -29.788 -20.597  1.00121.02           C  
ANISOU   45  CA  TYR A  48    18305  12868  14805    347   -325   -553       C  
ATOM     46  C   TYR A  48     -28.719 -28.534 -20.158  1.00116.81           C  
ANISOU   46  C   TYR A  48    17403  13032  13944    455   -880   -574       C  
ATOM     47  O   TYR A  48     -29.170 -27.851 -19.244  1.00115.65           O  
ANISOU   47  O   TYR A  48    17000  13314  13626    510  -1238   -598       O  
ATOM     48  CB  TYR A  48     -28.508 -31.004 -20.407  1.00126.52           C  
ANISOU   48  CB  TYR A  48    18981  13302  15786    862    544    -49       C  
ATOM     49  CG  TYR A  48     -28.249 -31.354 -18.948  1.00131.04           C  
ANISOU   49  CG  TYR A  48    19117  14396  16276   1664    703    681       C  
ATOM     50  CD1 TYR A  48     -29.245 -31.951 -18.170  1.00134.58           C  
ANISOU   50  CD1 TYR A  48    19668  14588  16876   1865   1083    925       C  
ATOM     51  CD2 TYR A  48     -27.015 -31.092 -18.350  1.00134.71           C  
ANISOU   51  CD2 TYR A  48    19031  15686  16464   2226    483   1133       C  
ATOM     52  CE1 TYR A  48     -29.023 -32.276 -16.837  1.00140.98           C  
ANISOU   52  CE1 TYR A  48    20219  15934  17411   2691   1291   1706       C  
ATOM     53  CE2 TYR A  48     -26.783 -31.410 -17.011  1.00141.95           C  
ANISOU   53  CE2 TYR A  48    19544  17356  17034   3018    489   1868       C  
ATOM     54  CZ  TYR A  48     -27.793 -32.004 -16.261  1.00145.03           C  
ANISOU   54  CZ  TYR A  48    20222  17457  17425   3291    921   2206       C  
ATOM     55  OH  TYR A  48     -27.575 -32.331 -14.939  1.00154.30           O  
ANISOU   55  OH  TYR A  48    21136  19417  18071   4167    999   3045       O  
ATOM     56  N   TYR A  49     -27.635 -28.215 -20.857  1.00115.03           N  
ANISOU   56  N   TYR A  49    17181  12823  13703    387   -808   -675       N  
ATOM     57  CA  TYR A  49     -26.827 -27.056 -20.524  1.00113.01           C  
ANISOU   57  CA  TYR A  49    16495  13136  13307    358  -1148   -863       C  
ATOM     58  C   TYR A  49     -27.623 -25.744 -20.456  1.00108.45           C  
ANISOU   58  C   TYR A  49    15980  12615  12611    -13  -1570  -1243       C  
ATOM     59  O   TYR A  49     -27.395 -24.960 -19.544  1.00109.94           O  
ANISOU   59  O   TYR A  49    15748  13341  12680    -38  -1765  -1447       O  
ATOM     60  CB  TYR A  49     -25.609 -26.936 -21.454  1.00115.10           C  
ANISOU   60  CB  TYR A  49    16778  13178  13776    273   -799   -964       C  
ATOM     61  CG  TYR A  49     -24.474 -27.918 -21.167  1.00121.02           C  
ANISOU   61  CG  TYR A  49    17080  14094  14807    788   -344   -503       C  
ATOM     62  CD1 TYR A  49     -24.027 -28.155 -19.862  1.00126.23           C  
ANISOU   62  CD1 TYR A  49    16966  15661  15334   1327   -599    -97       C  
ATOM     63  CD2 TYR A  49     -23.825 -28.585 -22.207  1.00124.20           C  
ANISOU   63  CD2 TYR A  49    17821  13794  15575    789    390   -411       C  
ATOM     64  CE1 TYR A  49     -22.979 -29.049 -19.601  1.00133.75           C  
ANISOU   64  CE1 TYR A  49    17364  16873  16581   1985   -197    551       C  
ATOM     65  CE2 TYR A  49     -22.777 -29.479 -21.956  1.00131.15           C  
ANISOU   65  CE2 TYR A  49    18199  14722  16907   1371    969    147       C  
ATOM     66  CZ  TYR A  49     -22.359 -29.703 -20.652  1.00135.93           C  
ANISOU   66  CZ  TYR A  49    17905  16295  17446   2029    635    704       C  
ATOM     67  OH  TYR A  49     -21.326 -30.582 -20.404  1.00144.69           O  
ANISOU   67  OH  TYR A  49    18387  17555  19033   2778   1187   1469       O  
ATOM     68  N   ARG A  50     -28.558 -25.509 -21.378  1.00121.34           N  
ANISOU   68  N   ARG A  50    17644  10566  17894   1824   2059  -1093       N  
ATOM     69  CA  ARG A  50     -29.331 -24.254 -21.353  1.00114.58           C  
ANISOU   69  CA  ARG A  50    16445  10121  16968   1451    812  -1492       C  
ATOM     70  C   ARG A  50     -30.405 -24.189 -20.248  1.00109.48           C  
ANISOU   70  C   ARG A  50    15098  10148  16349   1439     22  -1864       C  
ATOM     71  O   ARG A  50     -30.459 -23.212 -19.507  1.00106.46           O  
ANISOU   71  O   ARG A  50    14112  10182  16155   1709   -687  -1921       O  
ATOM     72  CB  ARG A  50     -29.915 -23.885 -22.732  1.00117.56           C  
ANISOU   72  CB  ARG A  50    17840  10086  16738    961    518  -1833       C  
ATOM     73  CG  ARG A  50     -31.433 -24.021 -22.856  1.00118.19           C  
ANISOU   73  CG  ARG A  50    18044  10567  16293    523   -258  -2319       C  
ATOM     74  CD  ARG A  50     -32.071 -22.836 -23.568  1.00119.14           C  
ANISOU   74  CD  ARG A  50    18356  10851  16061    522  -1303  -2519       C  
ATOM     75  NE  ARG A  50     -33.394 -22.542 -23.015  1.00119.82           N  
ANISOU   75  NE  ARG A  50    17594  12036  15895    792  -2242  -2788       N  
ATOM     76  CZ  ARG A  50     -34.070 -21.414 -23.218  1.00122.96           C  
ANISOU   76  CZ  ARG A  50    17869  12830  16021   1430  -3256  -2913       C  
ATOM     77  NH1 ARG A  50     -33.568 -20.450 -23.973  1.00123.84           N  
ANISOU   77  NH1 ARG A  50    18941  12077  16034   1595  -3607  -2830       N  
ATOM     78  NH2 ARG A  50     -35.259 -21.249 -22.658  1.00127.65           N  
ANISOU   78  NH2 ARG A  50    17419  14767  16314   1985  -3903  -3067       N  
ATOM     79  N   ASP A  51     -31.250 -25.212 -20.142  1.00109.96           N  
ANISOU   79  N   ASP A  51    15408  10341  16029   1020    173  -2095       N  
ATOM     80  CA  ASP A  51     -32.307 -25.230 -19.132  1.00107.62           C  
ANISOU   80  CA  ASP A  51    14259  11054  15575    863   -459  -2387       C  
ATOM     81  C   ASP A  51     -31.690 -25.124 -17.746  1.00102.11           C  
ANISOU   81  C   ASP A  51    12743  10599  15456   1313   -408  -2150       C  
ATOM     82  O   ASP A  51     -32.060 -24.260 -16.947  1.00100.07           O  
ANISOU   82  O   ASP A  51    11760  10998  15261   1654  -1045  -2361       O  
ATOM     83  CB  ASP A  51     -33.138 -26.520 -19.219  1.00113.76           C  
ANISOU   83  CB  ASP A  51    15592  12003  15627   -140   -237  -2487       C  
ATOM     84  CG  ASP A  51     -33.990 -26.601 -20.485  1.00120.92           C  
ANISOU   84  CG  ASP A  51    17231  13022  15688   -995   -552  -2668       C  
ATOM     85  OD1 ASP A  51     -34.311 -25.539 -21.065  1.00121.15           O  
ANISOU   85  OD1 ASP A  51    16869  13440  15721   -608  -1201  -2794       O  
ATOM     86  OD2 ASP A  51     -34.347 -27.735 -20.890  1.00128.72           O  
ANISOU   86  OD2 ASP A  51    19406  13643  15856  -2157   -222  -2633       O  
ATOM     87  N   LYS A  52     -30.733 -26.012 -17.494  1.00101.06           N  
ANISOU   87  N   LYS A  52    12884   9892  15621   1415    378  -1664       N  
ATOM     88  CA  LYS A  52     -30.064 -26.146 -16.207  1.00 97.87           C  
ANISOU   88  CA  LYS A  52    11747   9751  15685   1701    439  -1237       C  
ATOM     89  C   LYS A  52     -29.252 -24.899 -15.844  1.00 93.44           C  
ANISOU   89  C   LYS A  52    10511   9464  15526   1975      1   -935       C  
ATOM     90  O   LYS A  52     -29.324 -24.402 -14.720  1.00 91.31           O  
ANISOU   90  O   LYS A  52     9683   9682  15328   1898   -522   -946       O  
ATOM     91  CB  LYS A  52     -29.146 -27.376 -16.243  1.00103.81           C  
ANISOU   91  CB  LYS A  52    13064   9813  16564   2086   1414   -620       C  
ATOM     92  CG  LYS A  52     -28.719 -27.916 -14.897  1.00106.07           C  
ANISOU   92  CG  LYS A  52    12813  10361  17127   2270   1434   -124       C  
ATOM     93  CD  LYS A  52     -29.753 -28.862 -14.322  1.00109.58           C  
ANISOU   93  CD  LYS A  52    13890  10746  17000   1532   1311   -492       C  
ATOM     94  CE  LYS A  52     -29.108 -29.801 -13.323  1.00117.13           C  
ANISOU   94  CE  LYS A  52    15017  11408  18079   1871   1621    170       C  
ATOM     95  NZ  LYS A  52     -30.077 -30.785 -12.766  1.00123.17           N  
ANISOU   95  NZ  LYS A  52    16715  12014  18069    848   1474   -123       N  
ATOM     96  N   GLY A  53     -28.474 -24.408 -16.802  1.00 92.94           N  
ANISOU   96  N   GLY A  53    10702   9081  15530   2082    217   -639       N  
ATOM     97  CA  GLY A  53     -27.617 -23.246 -16.593  1.00 91.14           C  
ANISOU   97  CA  GLY A  53    10123   9118  15388   1879   -249   -212       C  
ATOM     98  C   GLY A  53     -28.381 -22.021 -16.145  1.00 87.20           C  
ANISOU   98  C   GLY A  53     9968   8620  14542   1723  -1283   -793       C  
ATOM     99  O   GLY A  53     -27.925 -21.288 -15.274  1.00 88.62           O  
ANISOU   99  O   GLY A  53    10064   8984  14623   1397  -1797   -531       O  
ATOM    100  N   ILE A  54     -29.551 -21.804 -16.741  1.00 84.64           N  
ANISOU  100  N   ILE A  54    10150   8122  13887   2009  -1588  -1522       N  
ATOM    101  CA  ILE A  54     -30.460 -20.726 -16.338  1.00 84.34           C  
ANISOU  101  CA  ILE A  54    10486   8158  13400   2444  -2437  -2108       C  
ATOM    102  C   ILE A  54     -30.932 -20.930 -14.894  1.00 82.71           C  
ANISOU  102  C   ILE A  54     9650   8596  13178   2641  -2527  -2317       C  
ATOM    103  O   ILE A  54     -30.940 -19.996 -14.093  1.00 85.37           O  
ANISOU  103  O   ILE A  54    10436   8821  13178   2859  -3029  -2475       O  
ATOM    104  CB  ILE A  54     -31.671 -20.627 -17.308  1.00 86.82           C  
ANISOU  104  CB  ILE A  54    11064   8601  13322   2905  -2703  -2645       C  
ATOM    105  CG1 ILE A  54     -31.222 -20.071 -18.664  1.00 88.22           C  
ANISOU  105  CG1 ILE A  54    12210   7985  13323   2671  -2842  -2489       C  
ATOM    106  CG2 ILE A  54     -32.790 -19.769 -16.722  1.00 91.68           C  
ANISOU  106  CG2 ILE A  54    11682   9723  13427   3904  -3376  -3193       C  
ATOM    107  CD1 ILE A  54     -32.216 -20.293 -19.790  1.00 91.32           C  
ANISOU  107  CD1 ILE A  54    12803   8543  13350   2781  -3003  -2782       C  
ATOM    108  N   SER A  55     -31.310 -22.166 -14.581  1.00 79.27           N  
ANISOU  108  N   SER A  55     8472   8711  12933   2437  -2027  -2313       N  
ATOM    109  CA  SER A  55     -31.730 -22.562 -13.246  1.00 78.35           C  
ANISOU  109  CA  SER A  55     7729   9302  12737   2364  -2020  -2444       C  
ATOM    110  C   SER A  55     -30.646 -22.305 -12.170  1.00 76.95           C  
ANISOU  110  C   SER A  55     7525   8918  12793   2014  -2118  -1917       C  
ATOM    111  O   SER A  55     -30.966 -21.886 -11.049  1.00 79.16           O  
ANISOU  111  O   SER A  55     7781   9546  12751   2056  -2416  -2165       O  
ATOM    112  CB  SER A  55     -32.134 -24.035 -13.276  1.00 78.61           C  
ANISOU  112  CB  SER A  55     7395   9698  12774   1831  -1493  -2367       C  
ATOM    113  OG  SER A  55     -32.959 -24.376 -12.186  1.00 81.33           O  
ANISOU  113  OG  SER A  55     7131  11020  12749   1607  -1579  -2647       O  
ATOM    114  N   HIS A  56     -29.378 -22.544 -12.520  1.00 68.86           N  
ANISOU  114  N   HIS A  56     8914   9188   8059   -477   -607   -609       N  
ATOM    115  CA  HIS A  56     -28.225 -22.145 -11.683  1.00 65.39           C  
ANISOU  115  CA  HIS A  56     8484   8803   7559   -385   -466   -577       C  
ATOM    116  C   HIS A  56     -28.115 -20.651 -11.496  1.00 62.91           C  
ANISOU  116  C   HIS A  56     8073   8587   7241   -331   -423   -566       C  
ATOM    117  O   HIS A  56     -28.011 -20.165 -10.363  1.00 61.93           O  
ANISOU  117  O   HIS A  56     7881   8514   7136   -322   -337   -534       O  
ATOM    118  CB  HIS A  56     -26.927 -22.634 -12.292  1.00 65.10           C  
ANISOU  118  CB  HIS A  56     8611   8723   7398   -290   -444   -593       C  
ATOM    119  CG  HIS A  56     -26.799 -24.117 -12.278  1.00 67.18           C  
ANISOU  119  CG  HIS A  56     9024   8871   7628   -307   -445   -595       C  
ATOM    120  ND1 HIS A  56     -27.145 -24.877 -11.179  1.00 68.70           N  
ANISOU  120  ND1 HIS A  56     9195   9027   7879   -368   -385   -560       N  
ATOM    121  CD2 HIS A  56     -26.358 -24.983 -13.216  1.00 67.89           C  
ANISOU  121  CD2 HIS A  56     9325   8852   7616   -255   -480   -622       C  
ATOM    122  CE1 HIS A  56     -26.926 -26.150 -11.445  1.00 69.83           C  
ANISOU  122  CE1 HIS A  56     9528   9037   7965   -367   -383   -568       C  
ATOM    123  NE2 HIS A  56     -26.445 -26.242 -12.672  1.00 70.46           N  
ANISOU  123  NE2 HIS A  56     9758   9069   7941   -296   -445   -609       N  
ATOM    124  N   ALA A  57     -28.135 -19.938 -12.619  1.00 61.44           N  
ANISOU  124  N   ALA A  57     7921   8410   7013   -284   -479   -593       N  
ATOM    125  CA  ALA A  57     -28.127 -18.495 -12.631  1.00 59.91           C  
ANISOU  125  CA  ALA A  57     7677   8276   6809   -233   -432   -583       C  
ATOM    126  C   ALA A  57     -29.220 -17.921 -11.735  1.00 60.34           C  
ANISOU  126  C   ALA A  57     7598   8382   6944   -260   -405   -546       C  
ATOM    127  O   ALA A  57     -28.936 -17.072 -10.906  1.00 59.44           O  
ANISOU  127  O   ALA A  57     7470   8297   6817   -233   -312   -528       O  
ATOM    128  CB  ALA A  57     -28.259 -17.991 -14.027  1.00 60.03           C  
ANISOU  128  CB  ALA A  57     7771   8274   6763   -164   -497   -608       C  
ATOM    129  N   LYS A  58     -30.454 -18.405 -11.864  1.00 62.10           N  
ANISOU  129  N   LYS A  58     7727   8614   7253   -312   -482   -528       N  
ATOM    130  CA  LYS A  58     -31.560 -17.892 -11.035  1.00 63.26           C  
ANISOU  130  CA  LYS A  58     7722   8823   7490   -312   -427   -461       C  
ATOM    131  C   LYS A  58     -31.405 -18.217  -9.544  1.00 62.68           C  
ANISOU  131  C   LYS A  58     7630   8738   7445   -329   -295   -414       C  
ATOM    132  O   LYS A  58     -31.887 -17.468  -8.698  1.00 63.37           O  
ANISOU  132  O   LYS A  58     7667   8864   7545   -271   -194   -357       O  
ATOM    133  CB  LYS A  58     -32.917 -18.400 -11.538  1.00 65.80           C  
ANISOU  133  CB  LYS A  58     7894   9175   7930   -380   -546   -438       C  
ATOM    134  CG  LYS A  58     -33.450 -17.708 -12.793  1.00 67.72           C  
ANISOU  134  CG  LYS A  58     8120   9471   8137   -311   -678   -462       C  
ATOM    135  CD  LYS A  58     -34.660 -18.467 -13.363  1.00 72.14           C  
ANISOU  135  CD  LYS A  58     8526  10064   8820   -415   -859   -461       C  
ATOM    136  CE  LYS A  58     -35.389 -17.647 -14.437  1.00 74.58           C  
ANISOU  136  CE  LYS A  58     8780  10465   9091   -309  -1000   -467       C  
ATOM    137  NZ  LYS A  58     -36.390 -18.439 -15.218  1.00 77.56           N  
ANISOU  137  NZ  LYS A  58     9031  10873   9563   -423  -1248   -498       N  
ATOM    138  N   ALA A  59     -30.730 -19.324  -9.241  1.00 61.62           N  
ANISOU  138  N   ALA A  59     7569   8545   7297   -380   -289   -432       N  
ATOM    139  CA  ALA A  59     -30.538 -19.796  -7.870  1.00 61.16           C  
ANISOU  139  CA  ALA A  59     7528   8468   7241   -373   -171   -387       C  
ATOM    140  C   ALA A  59     -29.268 -19.274  -7.175  1.00 59.05           C  
ANISOU  140  C   ALA A  59     7366   8218   6852   -295   -118   -416       C  
ATOM    141  O   ALA A  59     -28.929 -19.714  -6.083  1.00 58.64           O  
ANISOU  141  O   ALA A  59     7362   8154   6763   -263    -46   -392       O  
ATOM    142  CB  ALA A  59     -30.564 -21.331  -7.849  1.00 62.46           C  
ANISOU  142  CB  ALA A  59     7732   8548   7450   -455   -183   -381       C  
ATOM    143  N   GLY A  60     -28.574 -18.343  -7.825  1.00 57.47           N  
ANISOU  143  N   GLY A  60     7200   8044   6590   -267   -158   -466       N  
ATOM    144  CA  GLY A  60     -27.318 -17.777  -7.316  1.00 55.57           C  
ANISOU  144  CA  GLY A  60     7024   7826   6262   -234   -140   -500       C  
ATOM    145  C   GLY A  60     -26.110 -18.694  -7.459  1.00 54.55           C  
ANISOU  145  C   GLY A  60     6934   7702   6089   -228   -167   -518       C  
ATOM    146  O   GLY A  60     -25.094 -18.499  -6.800  1.00 54.33           O  
ANISOU  146  O   GLY A  60     6922   7716   6005   -203   -165   -533       O  
ATOM    147  N   ARG A  61     -26.203 -19.701  -8.318  1.00 53.69           N  
ANISOU  147  N   ARG A  61     6849   7552   5998   -241   -200   -515       N  
ATOM    148  CA  ARG A  61     -25.083 -20.617  -8.496  1.00 52.88           C  
ANISOU  148  CA  ARG A  61     6808   7447   5836   -195   -200   -514       C  
ATOM    149  C   ARG A  61     -24.321 -20.227  -9.730  1.00 51.31           C  
ANISOU  149  C   ARG A  61     6628   7256   5609   -167   -220   -531       C  
ATOM    150  O   ARG A  61     -24.361 -20.909 -10.753  1.00 51.23           O  
ANISOU  150  O   ARG A  61     6702   7186   5575   -144   -245   -535       O  
ATOM    151  CB  ARG A  61     -25.557 -22.054  -8.538  1.00 54.06           C  
ANISOU  151  CB  ARG A  61     7033   7511   5994   -208   -197   -495       C  
ATOM    152  CG  ARG A  61     -26.038 -22.493  -7.169  1.00 57.22           C  
ANISOU  152  CG  ARG A  61     7427   7899   6412   -209   -128   -454       C  
ATOM    153  CD  ARG A  61     -26.875 -23.729  -7.248  1.00 63.49           C  
ANISOU  153  CD  ARG A  61     8280   8580   7263   -272   -109   -428       C  
ATOM    154  NE  ARG A  61     -26.087 -24.850  -7.732  1.00 67.73           N  
ANISOU  154  NE  ARG A  61     8965   9049   7721   -222   -110   -434       N  
ATOM    155  CZ  ARG A  61     -26.578 -26.067  -7.938  1.00 72.21           C  
ANISOU  155  CZ  ARG A  61     9647   9477   8309   -280    -98   -425       C  
ATOM    156  NH1 ARG A  61     -27.865 -26.315  -7.701  1.00 75.16           N  
ANISOU  156  NH1 ARG A  61     9961   9782   8814   -416    -92   -405       N  
ATOM    157  NH2 ARG A  61     -25.786 -27.038  -8.380  1.00 72.82           N  
ANISOU  157  NH2 ARG A  61     9904   9479   8284   -202    -83   -427       N  
ATOM    158  N   TYR A  62     -23.606 -19.117  -9.600  1.00 49.66           N  
ANISOU  158  N   TYR A  62     6360   7108   5397   -168   -202   -540       N  
ATOM    159  CA  TYR A  62     -23.141 -18.358 -10.747  1.00 48.80           C  
ANISOU  159  CA  TYR A  62     6259   6994   5287   -156   -186   -543       C  
ATOM    160  C   TYR A  62     -21.992 -19.020 -11.501  1.00 48.43           C  
ANISOU  160  C   TYR A  62     6243   6957   5200    -75   -148   -507       C  
ATOM    161  O   TYR A  62     -21.952 -18.969 -12.728  1.00 48.11           O  
ANISOU  161  O   TYR A  62     6281   6866   5131    -23   -126   -497       O  
ATOM    162  CB  TYR A  62     -22.746 -16.952 -10.315  1.00 48.49           C  
ANISOU  162  CB  TYR A  62     6160   6989   5274   -208   -162   -558       C  
ATOM    163  CG  TYR A  62     -23.913 -16.147  -9.774  1.00 50.64           C  
ANISOU  163  CG  TYR A  62     6446   7233   5559   -243   -169   -580       C  
ATOM    164  CD1 TYR A  62     -25.022 -15.872 -10.585  1.00 51.41           C  
ANISOU  164  CD1 TYR A  62     6578   7289   5667   -220   -177   -577       C  
ATOM    165  CD2 TYR A  62     -23.909 -15.648  -8.468  1.00 49.75           C  
ANISOU  165  CD2 TYR A  62     6325   7140   5436   -275   -170   -598       C  
ATOM    166  CE1 TYR A  62     -26.102 -15.138 -10.117  1.00 51.69           C  
ANISOU  166  CE1 TYR A  62     6609   7316   5714   -218   -165   -573       C  
ATOM    167  CE2 TYR A  62     -24.994 -14.900  -7.981  1.00 51.99           C  
ANISOU  167  CE2 TYR A  62     6648   7390   5715   -268   -146   -600       C  
ATOM    168  CZ  TYR A  62     -26.091 -14.651  -8.821  1.00 53.81           C  
ANISOU  168  CZ  TYR A  62     6881   7593   5969   -235   -132   -578       C  
ATOM    169  OH  TYR A  62     -27.190 -13.929  -8.403  1.00 52.35           O  
ANISOU  169  OH  TYR A  62     6714   7393   5782   -195    -90   -556       O  
ATOM    170  N   SER A  63     -21.064 -19.629 -10.772  1.00 48.25           N  
ANISOU  170  N   SER A  63     6170   7003   5160    -37   -132   -478       N  
ATOM    171  CA  SER A  63     -19.949 -20.301 -11.421  1.00 49.13           C  
ANISOU  171  CA  SER A  63     6298   7140   5229     74    -72   -418       C  
ATOM    172  C   SER A  63     -20.444 -21.426 -12.331  1.00 49.70           C  
ANISOU  172  C   SER A  63     6560   7097   5225    155    -68   -414       C  
ATOM    173  O   SER A  63     -20.025 -21.523 -13.479  1.00 50.78           O  
ANISOU  173  O   SER A  63     6787   7192   5314    246    -14   -383       O  
ATOM    174  CB  SER A  63     -18.959 -20.836 -10.392  1.00 49.66           C  
ANISOU  174  CB  SER A  63     6269   7320   5279    128    -71   -380       C  
ATOM    175  OG  SER A  63     -18.428 -19.791  -9.610  1.00 48.65           O  
ANISOU  175  OG  SER A  63     5979   7291   5213     39   -110   -399       O  
ATOM    176  N   GLU A  64     -21.353 -22.254 -11.827  1.00 49.80           N  
ANISOU  176  N   GLU A  64     6653   7043   5226    117   -120   -446       N  
ATOM    177  CA  GLU A  64     -21.921 -23.323 -12.620  1.00 50.99           C  
ANISOU  177  CA  GLU A  64     7001   7058   5315    147   -146   -462       C  
ATOM    178  C   GLU A  64     -22.774 -22.815 -13.772  1.00 50.68           C  
ANISOU  178  C   GLU A  64     7031   6944   5279    105   -218   -510       C  
ATOM    179  O   GLU A  64     -22.943 -23.515 -14.776  1.00 51.80           O  
ANISOU  179  O   GLU A  64     7368   6974   5338    159   -253   -529       O  
ATOM    180  CB  GLU A  64     -22.746 -24.247 -11.751  1.00 51.54           C  
ANISOU  180  CB  GLU A  64     7115   7061   5404     77   -177   -478       C  
ATOM    181  CG  GLU A  64     -21.933 -24.877 -10.647  1.00 55.07           C  
ANISOU  181  CG  GLU A  64     7545   7568   5811    161   -105   -426       C  
ATOM    182  CD  GLU A  64     -22.556 -24.588  -9.308  1.00 58.88           C  
ANISOU  182  CD  GLU A  64     7921   8091   6357     79   -113   -433       C  
ATOM    183  OE1 GLU A  64     -22.431 -23.404  -8.831  1.00 59.57           O  
ANISOU  183  OE1 GLU A  64     7858   8284   6490     41   -133   -446       O  
ATOM    184  OE2 GLU A  64     -23.194 -25.532  -8.775  1.00 57.58           O  
ANISOU  184  OE2 GLU A  64     7850   7832   6194     54    -88   -422       O  
ATOM    185  N   ALA A  65     -23.316 -21.609 -13.635  1.00 49.25           N  
ANISOU  185  N   ALA A  65     6721   6819   5173     27   -247   -533       N  
ATOM    186  CA  ALA A  65     -24.110 -21.045 -14.712  1.00 48.97           C  
ANISOU  186  CA  ALA A  65     6746   6734   5125     20   -318   -570       C  
ATOM    187  C   ALA A  65     -23.178 -20.660 -15.863  1.00 49.30           C  
ANISOU  187  C   ALA A  65     6890   6759   5083    153   -241   -539       C  
ATOM    188  O   ALA A  65     -23.544 -20.829 -17.033  1.00 49.83           O  
ANISOU  188  O   ALA A  65     7126   6741   5064    222   -295   -564       O  
ATOM    189  CB  ALA A  65     -24.920 -19.866 -14.242  1.00 47.66           C  
ANISOU  189  CB  ALA A  65     6436   6628   5042    -58   -341   -585       C  
ATOM    190  N   VAL A  66     -21.978 -20.167 -15.532  1.00 48.51           N  
ANISOU  190  N   VAL A  66     6688   6737   5006    192   -117   -479       N  
ATOM    191  CA  VAL A  66     -21.006 -19.794 -16.559  1.00 49.55           C  
ANISOU  191  CA  VAL A  66     6884   6857   5085    319      2   -417       C  
ATOM    192  C   VAL A  66     -20.556 -21.037 -17.298  1.00 51.80           C  
ANISOU  192  C   VAL A  66     7370   7064   5246    471     35   -386       C  
ATOM    193  O   VAL A  66     -20.598 -21.082 -18.524  1.00 53.60           O  
ANISOU  193  O   VAL A  66     7799   7200   5367    593     55   -379       O  
ATOM    194  CB  VAL A  66     -19.754 -19.115 -15.997  1.00 49.26           C  
ANISOU  194  CB  VAL A  66     6651   6930   5133    301    124   -347       C  
ATOM    195  CG1 VAL A  66     -18.704 -18.980 -17.072  1.00 50.33           C  
ANISOU  195  CG1 VAL A  66     6841   7051   5230    446    284   -251       C  
ATOM    196  CG2 VAL A  66     -20.073 -17.755 -15.436  1.00 47.06           C  
ANISOU  196  CG2 VAL A  66     6239   6688   4951    161    109   -380       C  
ATOM    197  N   VAL A  67     -20.151 -22.057 -16.554  1.00 52.83           N  
ANISOU  197  N   VAL A  67     7486   7218   5367    486     43   -365       N  
ATOM    198  CA  VAL A  67     -19.635 -23.283 -17.154  1.00 55.21           C  
ANISOU  198  CA  VAL A  67     8009   7433   5533    654    100   -324       C  
ATOM    199  C   VAL A  67     -20.606 -23.869 -18.178  1.00 57.39           C  
ANISOU  199  C   VAL A  67     8581   7532   5690    676    -14   -403       C  
ATOM    200  O   VAL A  67     -20.202 -24.205 -19.295  1.00 59.01           O  
ANISOU  200  O   VAL A  67     9027   7641   5752    851     46   -373       O  
ATOM    201  CB  VAL A  67     -19.246 -24.324 -16.083  1.00 55.39           C  
ANISOU  201  CB  VAL A  67     7999   7494   5553    669    117   -297       C  
ATOM    202  CG1 VAL A  67     -19.146 -25.722 -16.686  1.00 56.80           C  
ANISOU  202  CG1 VAL A  67     8492   7520   5569    819    144   -285       C  
ATOM    203  CG2 VAL A  67     -17.928 -23.920 -15.407  1.00 53.86           C  
ANISOU  203  CG2 VAL A  67     7556   7481   5425    729    233   -196       C  
ATOM    204  N   MET A  68     -21.881 -23.960 -17.821  1.00 57.99           N  
ANISOU  204  N   MET A  68     8640   7568   5824    503   -183   -500       N  
ATOM    205  CA  MET A  68     -22.876 -24.422 -18.787  1.00 61.08           C  
ANISOU  205  CA  MET A  68     9270   7810   6127    485   -343   -589       C  
ATOM    206  C   MET A  68     -23.195 -23.464 -19.933  1.00 61.85           C  
ANISOU  206  C   MET A  68     9438   7895   6166    553   -388   -612       C  
ATOM    207  O   MET A  68     -23.113 -23.836 -21.098  1.00 63.86           O  
ANISOU  207  O   MET A  68     9981   8028   6254    697   -414   -630       O  
ATOM    208  CB  MET A  68     -24.165 -24.775 -18.093  1.00 61.28           C  
ANISOU  208  CB  MET A  68     9205   7813   6263    268   -507   -667       C  
ATOM    209  CG  MET A  68     -23.935 -25.617 -16.923  1.00 63.93           C  
ANISOU  209  CG  MET A  68     9485   8151   6653    210   -443   -636       C  
ATOM    210  SD  MET A  68     -25.399 -26.537 -16.539  1.00 71.74           S  
ANISOU  210  SD  MET A  68    10507   9019   7731    -14   -611   -717       S  
ATOM    211  CE  MET A  68     -24.775 -27.443 -15.110  1.00 71.33           C  
ANISOU  211  CE  MET A  68    10427   8970   7705     -4   -452   -645       C  
ATOM    212  N   LEU A  69     -23.573 -22.238 -19.605  1.00 62.03           N  
ANISOU  212  N   LEU A  69     8905   8422   6242    643   -750   -306       N  
ATOM    213  CA  LEU A  69     -24.105 -21.330 -20.617  1.00 60.99           C  
ANISOU  213  CA  LEU A  69     8960   8138   6074    741   -650   -590       C  
ATOM    214  C   LEU A  69     -23.078 -20.908 -21.652  1.00 60.91           C  
ANISOU  214  C   LEU A  69     9062   8010   6068    859   -607   -765       C  
ATOM    215  O   LEU A  69     -23.440 -20.594 -22.776  1.00 59.64           O  
ANISOU  215  O   LEU A  69     9015   7695   5950    960   -586   -921       O  
ATOM    216  CB  LEU A  69     -24.745 -20.115 -19.955  1.00 60.31           C  
ANISOU  216  CB  LEU A  69     8887   8242   5783    627   -486   -710       C  
ATOM    217  CG  LEU A  69     -26.253 -20.205 -19.678  1.00 60.84           C  
ANISOU  217  CG  LEU A  69     8920   8298   5897    595   -479   -660       C  
ATOM    218  CD1 LEU A  69     -26.839 -21.600 -19.809  1.00 61.87           C  
ANISOU  218  CD1 LEU A  69     8982   8298   6225    631   -673   -446       C  
ATOM    219  CD2 LEU A  69     -26.579 -19.610 -18.331  1.00 59.50           C  
ANISOU  219  CD2 LEU A  69     8646   8438   5524    396   -342   -675       C  
ATOM    220  N   GLU A  70     -21.807 -20.886 -21.256  1.00 63.11           N  
ANISOU  220  N   GLU A  70     9284   8412   6282    826   -599   -706       N  
ATOM    221  CA  GLU A  70     -20.694 -20.693 -22.175  1.00 64.73           C  
ANISOU  221  CA  GLU A  70     9563   8517   6514    940   -573   -827       C  
ATOM    222  C   GLU A  70     -20.823 -21.616 -23.387  1.00 65.99           C  
ANISOU  222  C   GLU A  70     9768   8390   6913   1087   -641   -900       C  
ATOM    223  O   GLU A  70     -20.525 -21.229 -24.524  1.00 65.86           O  
ANISOU  223  O   GLU A  70     9858   8292   6872   1177   -595  -1095       O  
ATOM    224  CB  GLU A  70     -19.387 -21.019 -21.476  1.00 66.55           C  
ANISOU  224  CB  GLU A  70     9658   8901   6725    884   -602   -646       C  
ATOM    225  CG  GLU A  70     -18.635 -19.837 -20.925  1.00 68.72           C  
ANISOU  225  CG  GLU A  70     9944   9445   6721    757   -496   -723       C  
ATOM    226  CD  GLU A  70     -17.247 -20.227 -20.411  1.00 74.21           C  
ANISOU  226  CD  GLU A  70    10484  10312   7399    702   -548   -506       C  
ATOM    227  OE1 GLU A  70     -16.982 -21.437 -20.141  1.00 77.68           O  
ANISOU  227  OE1 GLU A  70    10753  10703   8060    734   -663   -215       O  
ATOM    228  OE2 GLU A  70     -16.416 -19.306 -20.278  1.00 76.10           O  
ANISOU  228  OE2 GLU A  70    10749  10727   7436    622   -466   -605       O  
ATOM    229  N   GLN A  71     -21.282 -22.832 -23.141  1.00 68.11           N  
ANISOU  229  N   GLN A  71     9935   8526   7414   1086   -739   -752       N  
ATOM    230  CA  GLN A  71     -21.386 -23.805 -24.192  1.00 70.69           C  
ANISOU  230  CA  GLN A  71    10281   8572   8003   1181   -773   -872       C  
ATOM    231  C   GLN A  71     -22.659 -23.669 -25.033  1.00 70.88           C  
ANISOU  231  C   GLN A  71    10417   8532   7982   1171   -790  -1048       C  
ATOM    232  O   GLN A  71     -22.773 -24.298 -26.081  1.00 72.69           O  
ANISOU  232  O   GLN A  71    10680   8593   8345   1203   -799  -1234       O  
ATOM    233  CB  GLN A  71     -21.237 -25.206 -23.612  1.00 73.36           C  
ANISOU  233  CB  GLN A  71    10430   8740   8702   1180   -848   -634       C  
ATOM    234  CG  GLN A  71     -19.892 -25.417 -22.922  1.00 75.12           C  
ANISOU  234  CG  GLN A  71    10490   9040   9012   1193   -840   -396       C  
ATOM    235  CD  GLN A  71     -19.852 -26.693 -22.132  1.00 79.23           C  
ANISOU  235  CD  GLN A  71    10751   9438   9914   1173   -922    -28       C  
ATOM    236  OE1 GLN A  71     -19.601 -26.688 -20.923  1.00 80.74           O  
ANISOU  236  OE1 GLN A  71    10759   9893  10026   1064   -985    334       O  
ATOM    237  NE2 GLN A  71     -20.113 -27.804 -22.806  1.00 82.54           N  
ANISOU  237  NE2 GLN A  71    11125   9472  10761   1253   -915   -113       N  
ATOM    238  N   VAL A  72     -23.607 -22.847 -24.598  1.00 69.84           N  
ANISOU  238  N   VAL A  72    10318   8550   7664   1108   -779   -998       N  
ATOM    239  CA  VAL A  72     -24.873 -22.696 -25.331  1.00 70.08           C  
ANISOU  239  CA  VAL A  72    10409   8551   7666   1090   -806  -1082       C  
ATOM    240  C   VAL A  72     -24.988 -21.349 -26.076  1.00 68.74           C  
ANISOU  240  C   VAL A  72    10324   8501   7290   1116   -718  -1191       C  
ATOM    241  O   VAL A  72     -25.580 -21.269 -27.159  1.00 68.96           O  
ANISOU  241  O   VAL A  72    10383   8534   7284   1111   -746  -1273       O  
ATOM    242  CB  VAL A  72     -26.098 -22.896 -24.391  1.00 70.35           C  
ANISOU  242  CB  VAL A  72    10370   8627   7733   1011   -855   -896       C  
ATOM    243  CG1 VAL A  72     -27.398 -22.705 -25.152  1.00 71.31           C  
ANISOU  243  CG1 VAL A  72    10525   8737   7829    989   -885   -939       C  
ATOM    244  CG2 VAL A  72     -26.061 -24.279 -23.744  1.00 71.50           C  
ANISOU  244  CG2 VAL A  72    10390   8648   8127    980   -957   -727       C  
ATOM    245  N   TYR A  73     -24.429 -20.293 -25.489  1.00 67.66           N  
ANISOU  245  N   TYR A  73    10196   8477   7031   1119   -609  -1173       N  
ATOM    246  CA  TYR A  73     -24.479 -18.985 -26.115  1.00 66.67           C  
ANISOU  246  CA  TYR A  73    10113   8417   6801   1148   -505  -1233       C  
ATOM    247  C   TYR A  73     -23.796 -18.970 -27.480  1.00 68.23           C  
ANISOU  247  C   TYR A  73    10357   8619   6948   1207   -526  -1353       C  
ATOM    248  O   TYR A  73     -22.629 -19.393 -27.637  1.00 68.34           O  
ANISOU  248  O   TYR A  73    10392   8612   6961   1243   -529  -1438       O  
ATOM    249  CB  TYR A  73     -23.888 -17.910 -25.231  1.00 65.11           C  
ANISOU  249  CB  TYR A  73     9908   8304   6526   1117   -359  -1245       C  
ATOM    250  CG  TYR A  73     -23.842 -16.576 -25.900  1.00 62.54           C  
ANISOU  250  CG  TYR A  73     9594   7981   6185   1157   -233  -1289       C  
ATOM    251  CD1 TYR A  73     -25.021 -15.880 -26.203  1.00 61.20           C  
ANISOU  251  CD1 TYR A  73     9371   7774   6108   1167   -168  -1208       C  
ATOM    252  CD2 TYR A  73     -22.623 -16.002 -26.243  1.00 61.04           C  
ANISOU  252  CD2 TYR A  73     9437   7824   5930   1188   -175  -1365       C  
ATOM    253  CE1 TYR A  73     -24.978 -14.633 -26.836  1.00 60.37           C  
ANISOU  253  CE1 TYR A  73     9222   7644   6071   1211    -43  -1176       C  
ATOM    254  CE2 TYR A  73     -22.558 -14.767 -26.881  1.00 61.07           C  
ANISOU  254  CE2 TYR A  73     9420   7815   5967   1223    -59  -1361       C  
ATOM    255  CZ  TYR A  73     -23.733 -14.081 -27.173  1.00 61.78           C  
ANISOU  255  CZ  TYR A  73     9435   7848   6190   1237      8  -1254       C  
ATOM    256  OH  TYR A  73     -23.632 -12.850 -27.797  1.00 62.24           O  
ANISOU  256  OH  TYR A  73     9423   7869   6357   1277    131  -1184       O  
ATOM    257  N   ASP A  74     -24.567 -18.484 -28.457  1.00 69.63           N  
ANISOU  257  N   ASP A  74    10518   8855   7081   1201   -535  -1330       N  
ATOM    258  CA  ASP A  74     -24.119 -18.295 -29.828  1.00 71.06           C  
ANISOU  258  CA  ASP A  74    10704   9143   7151   1211   -551  -1411       C  
ATOM    259  C   ASP A  74     -24.439 -16.859 -30.228  1.00 71.30           C  
ANISOU  259  C   ASP A  74    10668   9269   7152   1228   -467  -1258       C  
ATOM    260  O   ASP A  74     -25.610 -16.494 -30.364  1.00 72.18           O  
ANISOU  260  O   ASP A  74    10697   9409   7318   1199   -476  -1094       O  
ATOM    261  CB  ASP A  74     -24.850 -19.280 -30.743  1.00 72.79           C  
ANISOU  261  CB  ASP A  74    10906   9410   7341   1128   -670  -1488       C  
ATOM    262  CG  ASP A  74     -24.239 -19.367 -32.150  1.00 74.46           C  
ANISOU  262  CG  ASP A  74    11112   9795   7384   1086   -682  -1648       C  
ATOM    263  OD1 ASP A  74     -23.491 -18.450 -32.577  1.00 73.30           O  
ANISOU  263  OD1 ASP A  74    10952   9766   7132   1131   -616  -1614       O  
ATOM    264  OD2 ASP A  74     -24.528 -20.373 -32.832  1.00 76.00           O  
ANISOU  264  OD2 ASP A  74    11301  10023   7550    985   -746  -1827       O  
ATOM    265  N   ALA A  75     -23.400 -16.048 -30.407  1.00 71.44           N  
ANISOU  265  N   ALA A  75    10694   9320   7126   1276   -379  -1280       N  
ATOM    266  CA  ALA A  75     -23.561 -14.647 -30.799  1.00 72.19           C  
ANISOU  266  CA  ALA A  75    10693   9460   7273   1299   -278  -1110       C  
ATOM    267  C   ALA A  75     -24.298 -14.446 -32.140  1.00 74.32           C  
ANISOU  267  C   ALA A  75    10836   9929   7473   1254   -360   -929       C  
ATOM    268  O   ALA A  75     -24.920 -13.394 -32.332  1.00 74.72           O  
ANISOU  268  O   ALA A  75    10741   9982   7664   1269   -288   -676       O  
ATOM    269  CB  ALA A  75     -22.202 -13.932 -30.814  1.00 71.99           C  
ANISOU  269  CB  ALA A  75    10695   9439   7218   1343   -183  -1174       C  
ATOM    270  N   ASP A  76     -24.229 -15.430 -33.050  1.00 76.07           N  
ANISOU  270  N   ASP A  76    11079  10327   7496   1179   -493  -1051       N  
ATOM    271  CA  ASP A  76     -24.943 -15.347 -34.349  1.00 79.13           C  
ANISOU  271  CA  ASP A  76    11320  11015   7729   1065   -591   -891       C  
ATOM    272  C   ASP A  76     -26.302 -16.062 -34.362  1.00 79.64           C  
ANISOU  272  C   ASP A  76    11342  11118   7799    965   -700   -834       C  
ATOM    273  O   ASP A  76     -27.050 -15.961 -35.335  1.00 82.15           O  
ANISOU  273  O   ASP A  76    11506  11724   7981    837   -793   -653       O  
ATOM    274  CB  ASP A  76     -24.084 -15.812 -35.542  1.00 81.41           C  
ANISOU  274  CB  ASP A  76    11612  11581   7739    978   -644  -1081       C  
ATOM    275  CG  ASP A  76     -22.632 -15.320 -35.468  1.00 82.84           C  
ANISOU  275  CG  ASP A  76    11853  11711   7911   1081   -545  -1173       C  
ATOM    276  OD1 ASP A  76     -22.383 -14.105 -35.256  1.00 83.08           O  
ANISOU  276  OD1 ASP A  76    11813  11689   8062   1160   -458   -951       O  
ATOM    277  OD2 ASP A  76     -21.730 -16.176 -35.628  1.00 85.45           O  
ANISOU  277  OD2 ASP A  76    12284  12034   8147   1080   -539  -1475       O  
ATOM    278  N   ALA A  77     -26.622 -16.774 -33.289  1.00 77.85           N  
ANISOU  278  N   ALA A  77    11224  10641   7714   1001   -699   -953       N  
ATOM    279  CA  ALA A  77     -27.978 -17.292 -33.107  1.00 78.10           C  
ANISOU  279  CA  ALA A  77    11202  10669   7802    923   -786   -848       C  
ATOM    280  C   ALA A  77     -28.501 -16.939 -31.710  1.00 75.82           C  
ANISOU  280  C   ALA A  77    10927  10123   7756   1021   -692   -738       C  
ATOM    281  O   ALA A  77     -28.676 -17.806 -30.852  1.00 75.04           O  
ANISOU  281  O   ALA A  77    10911   9873   7725   1017   -722   -854       O  
ATOM    282  CB  ALA A  77     -28.030 -18.782 -33.357  1.00 79.46           C  
ANISOU  282  CB  ALA A  77    11457  10844   7889    809   -898  -1124       C  
ATOM    283  N   PHE A  78     -28.783 -15.652 -31.527  1.00 74.88           N  
ANISOU  283  N   PHE A  78    10694   9970   7787   1092   -563   -506       N  
ATOM    284  CA  PHE A  78     -29.041 -15.054 -30.221  1.00 73.20           C  
ANISOU  284  CA  PHE A  78    10482   9528   7801   1171   -395   -478       C  
ATOM    285  C   PHE A  78     -30.311 -15.491 -29.477  1.00 73.06           C  
ANISOU  285  C   PHE A  78    10422   9439   7897   1142   -412   -390       C  
ATOM    286  O   PHE A  78     -31.424 -15.370 -29.987  1.00 74.66           O  
ANISOU  286  O   PHE A  78    10479   9727   8161   1108   -464   -148       O  
ATOM    287  CB  PHE A  78     -29.032 -13.544 -30.358  1.00 73.55           C  
ANISOU  287  CB  PHE A  78    10381   9512   8050   1243   -212   -283       C  
ATOM    288  CG  PHE A  78     -28.970 -12.839 -29.064  1.00 73.54           C  
ANISOU  288  CG  PHE A  78    10394   9280   8267   1294     18   -381       C  
ATOM    289  CD1 PHE A  78     -27.750 -12.530 -28.497  1.00 73.12           C  
ANISOU  289  CD1 PHE A  78    10453   9156   8170   1305    124   -612       C  
ATOM    290  CD2 PHE A  78     -30.132 -12.483 -28.398  1.00 75.27           C  
ANISOU  290  CD2 PHE A  78    10497   9378   8723   1305    145   -264       C  
ATOM    291  CE1 PHE A  78     -27.685 -11.868 -27.292  1.00 73.39           C  
ANISOU  291  CE1 PHE A  78    10487   9036   8361   1292    353   -755       C  
ATOM    292  CE2 PHE A  78     -30.077 -11.823 -27.191  1.00 75.91           C  
ANISOU  292  CE2 PHE A  78    10578   9278   8986   1311    397   -425       C  
ATOM    293  CZ  PHE A  78     -28.850 -11.511 -26.638  1.00 74.98           C  
ANISOU  293  CZ  PHE A  78    10576   9124   8788   1288    502   -688       C  
ATOM    294  N   ASP A  79     -30.109 -15.991 -28.259  1.00 71.16           N  
ANISOU  294  N   ASP A  79    10283   9079   7674   1143   -372   -555       N  
ATOM    295  CA  ASP A  79     -31.182 -16.336 -27.335  1.00 71.01           C  
ANISOU  295  CA  ASP A  79    10219   9003   7756   1114   -358   -484       C  
ATOM    296  C   ASP A  79     -31.086 -15.429 -26.106  1.00 69.94           C  
ANISOU  296  C   ASP A  79    10058   8763   7751   1139   -110   -554       C  
ATOM    297  O   ASP A  79     -30.142 -15.534 -25.314  1.00 68.61           O  
ANISOU  297  O   ASP A  79     9982   8596   7489   1112    -58   -743       O  
ATOM    298  CB  ASP A  79     -31.079 -17.805 -26.916  1.00 70.91           C  
ANISOU  298  CB  ASP A  79    10303   8993   7645   1049   -527   -595       C  
ATOM    299  CG  ASP A  79     -32.115 -18.195 -25.861  1.00 73.49           C  
ANISOU  299  CG  ASP A  79    10570   9292   8060   1007   -519   -501       C  
ATOM    300  OD1 ASP A  79     -32.644 -17.316 -25.135  1.00 76.48           O  
ANISOU  300  OD1 ASP A  79    10866   9645   8546   1026   -334   -443       O  
ATOM    301  OD2 ASP A  79     -32.403 -19.403 -25.749  1.00 76.18           O  
ANISOU  301  OD2 ASP A  79    10932   9628   8385    946   -682   -495       O  
ATOM    302  N   VAL A  80     -32.086 -14.564 -25.948  1.00 68.54           N  
ANISOU  302  N   VAL A  80     8990   9206   7846    709   -953   -330       N  
ATOM    303  CA  VAL A  80     -32.068 -13.498 -24.937  1.00 66.33           C  
ANISOU  303  CA  VAL A  80     8567   8841   7794    990   -957   -304       C  
ATOM    304  C   VAL A  80     -32.030 -14.031 -23.490  1.00 64.04           C  
ANISOU  304  C   VAL A  80     8249   8496   7587   1080   -792   -440       C  
ATOM    305  O   VAL A  80     -31.331 -13.487 -22.638  1.00 61.63           O  
ANISOU  305  O   VAL A  80     7967   8075   7373   1222   -712   -480       O  
ATOM    306  CB  VAL A  80     -33.251 -12.504 -25.152  1.00 69.03           C  
ANISOU  306  CB  VAL A  80     8666   9279   8282   1101  -1155   -140       C  
ATOM    307  CG1 VAL A  80     -34.610 -13.160 -24.849  1.00 70.64           C  
ANISOU  307  CG1 VAL A  80     8627   9695   8515   1029  -1186   -161       C  
ATOM    308  CG2 VAL A  80     -33.048 -11.230 -24.325  1.00 68.85           C  
ANISOU  308  CG2 VAL A  80     8582   9083   8495   1381  -1107   -132       C  
ATOM    309  N   GLU A  81     -32.762 -15.112 -23.244  1.00 64.09           N  
ANISOU  309  N   GLU A  81     8241   8594   7514    935   -745   -505       N  
ATOM    310  CA  GLU A  81     -32.845 -15.704 -21.926  1.00 63.14           C  
ANISOU  310  CA  GLU A  81     8144   8427   7416    945   -610   -613       C  
ATOM    311  C   GLU A  81     -31.522 -16.393 -21.563  1.00 60.63           C  
ANISOU  311  C   GLU A  81     8062   7929   7044    974   -510   -655       C  
ATOM    312  O   GLU A  81     -31.182 -16.516 -20.375  1.00 61.01           O  
ANISOU  312  O   GLU A  81     8153   7904   7124   1030   -450   -686       O  
ATOM    313  CB  GLU A  81     -34.032 -16.660 -21.853  1.00 65.49           C  
ANISOU  313  CB  GLU A  81     8393   8879   7609    725   -588   -668       C  
ATOM    314  CG  GLU A  81     -34.508 -17.005 -20.434  1.00 69.60           C  
ANISOU  314  CG  GLU A  81     8893   9403   8146    683   -461   -776       C  
ATOM    315  CD  GLU A  81     -35.144 -15.821 -19.683  1.00 75.31           C  
ANISOU  315  CD  GLU A  81     9338  10199   9076    835   -434   -810       C  
ATOM    316  OE1 GLU A  81     -35.260 -14.716 -20.274  1.00 77.53           O  
ANISOU  316  OE1 GLU A  81     9437  10497   9521   1020   -535   -721       O  
ATOM    317  OE2 GLU A  81     -35.532 -15.994 -18.494  1.00 78.01           O  
ANISOU  317  OE2 GLU A  81     9670  10555   9415    753   -292   -931       O  
ATOM    318  N   VAL A  82     -30.756 -16.804 -22.571  1.00 58.26           N  
ANISOU  318  N   VAL A  82     7899   7564   6670    931   -494   -652       N  
ATOM    319  CA  VAL A  82     -29.420 -17.326 -22.317  1.00 55.46           C  
ANISOU  319  CA  VAL A  82     7682   7046   6344   1031   -400   -685       C  
ATOM    320  C   VAL A  82     -28.459 -16.197 -22.056  1.00 53.00           C  
ANISOU  320  C   VAL A  82     7276   6730   6129   1188   -435   -650       C  
ATOM    321  O   VAL A  82     -27.740 -16.210 -21.066  1.00 51.49           O  
ANISOU  321  O   VAL A  82     7078   6491   5995   1291   -422   -639       O  
ATOM    322  CB  VAL A  82     -28.874 -18.195 -23.482  1.00 56.70           C  
ANISOU  322  CB  VAL A  82     8006   7117   6420    928   -291   -750       C  
ATOM    323  CG1 VAL A  82     -27.348 -18.365 -23.378  1.00 56.13           C  
ANISOU  323  CG1 VAL A  82     7956   6907   6462   1107   -194   -783       C  
ATOM    324  CG2 VAL A  82     -29.564 -19.553 -23.485  1.00 57.58           C  
ANISOU  324  CG2 VAL A  82     8302   7156   6419    754   -198   -810       C  
ATOM    325  N   ALA A  83     -28.444 -15.213 -22.944  1.00 51.92           N  
ANISOU  325  N   ALA A  83     7091   6653   5983   1166   -495   -616       N  
ATOM    326  CA  ALA A  83     -27.519 -14.096 -22.785  1.00 50.77           C  
ANISOU  326  CA  ALA A  83     6905   6494   5888   1254   -506   -598       C  
ATOM    327  C   ALA A  83     -27.709 -13.393 -21.455  1.00 49.79           C  
ANISOU  327  C   ALA A  83     6708   6363   5844   1343   -517   -586       C  
ATOM    328  O   ALA A  83     -26.738 -12.971 -20.844  1.00 50.26           O  
ANISOU  328  O   ALA A  83     6765   6415   5914   1377   -491   -597       O  
ATOM    329  CB  ALA A  83     -27.668 -13.123 -23.894  1.00 51.32           C  
ANISOU  329  CB  ALA A  83     6997   6593   5909   1182   -584   -539       C  
ATOM    330  N   LEU A  84     -28.954 -13.280 -21.009  1.00 49.54           N  
ANISOU  330  N   LEU A  84     6607   6357   5856   1345   -536   -582       N  
ATOM    331  CA  LEU A  84     -29.273 -12.503 -19.833  1.00 49.23           C  
ANISOU  331  CA  LEU A  84     6514   6297   5894   1390   -485   -616       C  
ATOM    332  C   LEU A  84     -28.645 -13.169 -18.607  1.00 48.89           C  
ANISOU  332  C   LEU A  84     6541   6250   5785   1337   -434   -652       C  
ATOM    333  O   LEU A  84     -27.996 -12.502 -17.778  1.00 49.09           O  
ANISOU  333  O   LEU A  84     6592   6265   5793   1314   -401   -668       O  
ATOM    334  CB  LEU A  84     -30.789 -12.387 -19.686  1.00 50.19           C  
ANISOU  334  CB  LEU A  84     6493   6471   6106   1401   -478   -637       C  
ATOM    335  CG  LEU A  84     -31.345 -12.057 -18.307  1.00 52.03           C  
ANISOU  335  CG  LEU A  84     6671   6693   6402   1386   -341   -746       C  
ATOM    336  CD1 LEU A  84     -30.968 -10.626 -17.901  1.00 51.28           C  
ANISOU  336  CD1 LEU A  84     6603   6476   6404   1468   -260   -775       C  
ATOM    337  CD2 LEU A  84     -32.854 -12.241 -18.289  1.00 54.42           C  
ANISOU  337  CD2 LEU A  84     6770   7102   6801   1378   -311   -794       C  
ATOM    338  N   HIS A  85     -28.822 -14.482 -18.506  1.00 48.08           N  
ANISOU  338  N   HIS A  85     6498   6148   5622   1284   -439   -648       N  
ATOM    339  CA  HIS A  85     -28.329 -15.187 -17.363  1.00 47.87           C  
ANISOU  339  CA  HIS A  85     6566   6093   5526   1233   -439   -627       C  
ATOM    340  C   HIS A  85     -26.842 -15.434 -17.425  1.00 47.26           C  
ANISOU  340  C   HIS A  85     6505   5991   5459   1322   -500   -551       C  
ATOM    341  O   HIS A  85     -26.152 -15.285 -16.406  1.00 47.26           O  
ANISOU  341  O   HIS A  85     6514   6026   5414   1287   -551   -496       O  
ATOM    342  CB  HIS A  85     -29.123 -16.441 -17.155  1.00 49.06           C  
ANISOU  342  CB  HIS A  85     6822   6213   5605   1130   -417   -639       C  
ATOM    343  CG  HIS A  85     -30.524 -16.153 -16.760  1.00 52.08           C  
ANISOU  343  CG  HIS A  85     7126   6683   5975   1006   -343   -734       C  
ATOM    344  ND1 HIS A  85     -31.477 -15.769 -17.676  1.00 54.25           N  
ANISOU  344  ND1 HIS A  85     7241   7045   6323   1026   -338   -771       N  
ATOM    345  CD2 HIS A  85     -31.117 -16.099 -15.545  1.00 55.58           C  
ANISOU  345  CD2 HIS A  85     7596   7165   6355    852   -261   -807       C  
ATOM    346  CE1 HIS A  85     -32.613 -15.534 -17.043  1.00 58.34           C  
ANISOU  346  CE1 HIS A  85     7641   7658   6868    935   -252   -866       C  
ATOM    347  NE2 HIS A  85     -32.422 -15.725 -15.749  1.00 57.90           N  
ANISOU  347  NE2 HIS A  85     7708   7567   6721    811   -175   -915       N  
ATOM    348  N   LEU A  86     -26.335 -15.742 -18.613  1.00 46.59           N  
ANISOU  348  N   LEU A  86     6402   5875   5425   1408   -487   -555       N  
ATOM    349  CA  LEU A  86     -24.899 -15.907 -18.769  1.00 46.83           C  
ANISOU  349  CA  LEU A  86     6370   5909   5512   1513   -505   -517       C  
ATOM    350  C   LEU A  86     -24.247 -14.578 -18.483  1.00 46.03           C  
ANISOU  350  C   LEU A  86     6170   5928   5389   1472   -531   -520       C  
ATOM    351  O   LEU A  86     -23.139 -14.548 -17.940  1.00 47.23           O  
ANISOU  351  O   LEU A  86     6231   6164   5550   1495   -589   -464       O  
ATOM    352  CB  LEU A  86     -24.501 -16.382 -20.170  1.00 47.13           C  
ANISOU  352  CB  LEU A  86     6410   5893   5603   1565   -412   -583       C  
ATOM    353  CG  LEU A  86     -22.991 -16.420 -20.525  1.00 50.19           C  
ANISOU  353  CG  LEU A  86     6661   6317   6091   1676   -370   -600       C  
ATOM    354  CD1 LEU A  86     -22.119 -17.068 -19.433  1.00 52.35           C  
ANISOU  354  CD1 LEU A  86     6841   6583   6464   1828   -465   -480       C  
ATOM    355  CD2 LEU A  86     -22.711 -17.116 -21.871  1.00 50.65           C  
ANISOU  355  CD2 LEU A  86     6763   6283   6196   1688   -200   -720       C  
ATOM    356  N   GLY A  87     -24.920 -13.486 -18.854  1.00 44.16           N  
ANISOU  356  N   GLY A  87     5950   5699   5126   1405   -496   -572       N  
ATOM    357  CA  GLY A  87     -24.384 -12.143 -18.615  1.00 43.59           C  
ANISOU  357  CA  GLY A  87     5862   5683   5015   1331   -483   -591       C  
ATOM    358  C   GLY A  87     -24.332 -11.829 -17.131  1.00 43.63           C  
ANISOU  358  C   GLY A  87     5893   5734   4950   1225   -492   -582       C  
ATOM    359  O   GLY A  87     -23.344 -11.294 -16.628  1.00 44.10           O  
ANISOU  359  O   GLY A  87     5924   5898   4932   1123   -514   -570       O  
ATOM    360  N   ILE A  88     -25.407 -12.150 -16.423  1.00 44.55           N  
ANISOU  360  N   ILE A  88     6067   5797   5060   1192   -463   -603       N  
ATOM    361  CA  ILE A  88     -25.449 -11.940 -14.977  1.00 45.65           C  
ANISOU  361  CA  ILE A  88     6277   5980   5087   1015   -442   -618       C  
ATOM    362  C   ILE A  88     -24.275 -12.736 -14.371  1.00 47.23           C  
ANISOU  362  C   ILE A  88     6450   6291   5203    979   -601   -479       C  
ATOM    363  O   ILE A  88     -23.520 -12.221 -13.546  1.00 48.46           O  
ANISOU  363  O   ILE A  88     6611   6570   5231    806   -648   -446       O  
ATOM    364  CB  ILE A  88     -26.769 -12.462 -14.365  1.00 45.64           C  
ANISOU  364  CB  ILE A  88     6335   5927   5077    952   -369   -677       C  
ATOM    365  CG1 ILE A  88     -27.947 -11.593 -14.753  1.00 45.58           C  
ANISOU  365  CG1 ILE A  88     6277   5843   5195   1008   -220   -803       C  
ATOM    366  CG2 ILE A  88     -26.666 -12.565 -12.845  1.00 47.64           C  
ANISOU  366  CG2 ILE A  88     6709   6240   5149    697   -360   -679       C  
ATOM    367  CD1 ILE A  88     -29.269 -12.221 -14.438  1.00 47.29           C  
ANISOU  367  CD1 ILE A  88     6463   6065   5438    966   -144   -877       C  
ATOM    368  N   ALA A  89     -24.108 -13.977 -14.824  1.00 42.18           N  
ANISOU  368  N   ALA A  89     5475   5872   4677    450   -277   -304       N  
ATOM    369  CA  ALA A  89     -23.141 -14.877 -14.226  1.00 43.11           C  
ANISOU  369  CA  ALA A  89     5515   6010   4852    389   -360   -205       C  
ATOM    370  C   ALA A  89     -21.714 -14.527 -14.591  1.00 43.63           C  
ANISOU  370  C   ALA A  89     5590   6109   4876    368   -386   -229       C  
ATOM    371  O   ALA A  89     -20.805 -14.837 -13.834  1.00 44.69           O  
ANISOU  371  O   ALA A  89     5684   6268   5028    281   -458   -129       O  
ATOM    372  CB  ALA A  89     -23.459 -16.340 -14.573  1.00 43.42           C  
ANISOU  372  CB  ALA A  89     5393   5944   5158    446   -474   -173       C  
ATOM    373  N   TYR A  90     -21.493 -13.862 -15.718  1.00 44.04           N  
ANISOU  373  N   TYR A  90     5681   6161   4891    451   -325   -321       N  
ATOM    374  CA  TYR A  90     -20.154 -13.345 -15.984  1.00 45.75           C  
ANISOU  374  CA  TYR A  90     5866   6404   5111    428   -300   -274       C  
ATOM    375  C   TYR A  90     -19.846 -12.221 -15.026  1.00 46.48           C  
ANISOU  375  C   TYR A  90     6036   6504   5120    283   -326   -234       C  
ATOM    376  O   TYR A  90     -18.773 -12.186 -14.424  1.00 48.04           O  
ANISOU  376  O   TYR A  90     6178   6690   5384    184   -422   -146       O  
ATOM    377  CB  TYR A  90     -19.993 -12.805 -17.397  1.00 46.78           C  
ANISOU  377  CB  TYR A  90     6019   6553   5202    569   -186   -321       C  
ATOM    378  CG  TYR A  90     -19.552 -13.800 -18.435  1.00 49.48           C  
ANISOU  378  CG  TYR A  90     6302   6901   5598    749   -160   -363       C  
ATOM    379  CD1 TYR A  90     -18.482 -14.675 -18.210  1.00 50.64           C  
ANISOU  379  CD1 TYR A  90     6308   7031   5902    751   -184   -292       C  
ATOM    380  CD2 TYR A  90     -20.198 -13.852 -19.662  1.00 51.43           C  
ANISOU  380  CD2 TYR A  90     6650   7161   5730    942   -126   -486       C  
ATOM    381  CE1 TYR A  90     -18.069 -15.575 -19.189  1.00 54.42           C  
ANISOU  381  CE1 TYR A  90     6749   7502   6424    961   -138   -365       C  
ATOM    382  CE2 TYR A  90     -19.799 -14.737 -20.645  1.00 55.75           C  
ANISOU  382  CE2 TYR A  90     7201   7714   6266   1156   -110   -574       C  
ATOM    383  CZ  TYR A  90     -18.733 -15.593 -20.414  1.00 57.68           C  
ANISOU  383  CZ  TYR A  90     7307   7939   6668   1176    -96   -524       C  
ATOM    384  OH  TYR A  90     -18.375 -16.464 -21.425  1.00 62.19           O  
ANISOU  384  OH  TYR A  90     7906   8507   7216   1434    -61   -650       O  
ATOM    385  N   VAL A  91     -20.779 -11.294 -14.863  1.00 46.30           N  
ANISOU  385  N   VAL A  91     6141   6475   4975    278   -272   -309       N  
ATOM    386  CA  VAL A  91     -20.511 -10.183 -13.956  1.00 47.35           C  
ANISOU  386  CA  VAL A  91     6383   6583   5025    170   -328   -327       C  
ATOM    387  C   VAL A  91     -20.224 -10.662 -12.526  1.00 48.99           C  
ANISOU  387  C   VAL A  91     6648   6824   5139     78   -459   -286       C  
ATOM    388  O   VAL A  91     -19.302 -10.175 -11.881  1.00 50.05           O  
ANISOU  388  O   VAL A  91     6821   6922   5273    -20   -616   -272       O  
ATOM    389  CB  VAL A  91     -21.620  -9.111 -13.981  1.00 47.28           C  
ANISOU  389  CB  VAL A  91     6505   6542   4916    208   -235   -435       C  
ATOM    390  CG1 VAL A  91     -21.316  -8.004 -12.955  1.00 48.43           C  
ANISOU  390  CG1 VAL A  91     6796   6629   4973    121   -330   -508       C  
ATOM    391  CG2 VAL A  91     -21.735  -8.500 -15.382  1.00 45.40           C  
ANISOU  391  CG2 VAL A  91     6218   6269   4760    288   -145   -434       C  
ATOM    392  N   LYS A  92     -20.994 -11.634 -12.042  1.00 49.32           N  
ANISOU  392  N   LYS A  92     6688   6926   5124    115   -418   -242       N  
ATOM    393  CA  LYS A  92     -20.831 -12.100 -10.665  1.00 51.50           C  
ANISOU  393  CA  LYS A  92     7042   7267   5257     56   -513   -157       C  
ATOM    394  C   LYS A  92     -19.469 -12.768 -10.430  1.00 52.20           C  
ANISOU  394  C   LYS A  92     7016   7340   5476    -33   -709    -40       C  
ATOM    395  O   LYS A  92     -18.875 -12.636  -9.357  1.00 54.19           O  
ANISOU  395  O   LYS A  92     7373   7617   5600   -112   -883      1       O  
ATOM    396  CB  LYS A  92     -21.970 -13.042 -10.280  1.00 51.77           C  
ANISOU  396  CB  LYS A  92     7040   7357   5272    123   -392    -56       C  
ATOM    397  CG  LYS A  92     -23.342 -12.399 -10.186  1.00 53.39           C  
ANISOU  397  CG  LYS A  92     7340   7576   5368    212   -194   -121       C  
ATOM    398  CD  LYS A  92     -23.407 -11.368  -9.060  1.00 59.31           C  
ANISOU  398  CD  LYS A  92     8350   8388   5794    223   -168   -206       C  
ATOM    399  CE  LYS A  92     -24.824 -11.206  -8.563  1.00 63.25           C  
ANISOU  399  CE  LYS A  92     8913   8940   6179    347     85   -176       C  
ATOM    400  NZ  LYS A  92     -25.075  -9.845  -8.003  1.00 68.17           N  
ANISOU  400  NZ  LYS A  92     9794   9564   6542    414    152   -370       N  
ATOM    401  N   THR A  93     -18.983 -13.473 -11.448  1.00 51.14           N  
ANISOU  401  N   THR A  93     6679   7159   5593      0   -691      3       N  
ATOM    402  CA  THR A  93     -17.696 -14.177 -11.389  1.00 52.10           C  
ANISOU  402  CA  THR A  93     6635   7243   5918    -56   -837    128       C  
ATOM    403  C   THR A  93     -16.518 -13.330 -11.866  1.00 53.15           C  
ANISOU  403  C   THR A  93     6690   7304   6200   -105   -892    136       C  
ATOM    404  O   THR A  93     -15.427 -13.856 -12.137  1.00 54.06           O  
ANISOU  404  O   THR A  93     6606   7368   6564   -118   -953    254       O  
ATOM    405  CB  THR A  93     -17.730 -15.445 -12.222  1.00 51.13           C  
ANISOU  405  CB  THR A  93     6326   7085   6016     43   -775    162       C  
ATOM    406  OG1 THR A  93     -18.266 -15.127 -13.505  1.00 51.35           O  
ANISOU  406  OG1 THR A  93     6362   7099   6048    172   -613     26       O  
ATOM    407  CG2 THR A  93     -18.613 -16.509 -11.561  1.00 51.41           C  
ANISOU  407  CG2 THR A  93     6348   7137   6047     51   -796    245       C  
ATOM    408  N   GLY A  94     -16.734 -12.017 -11.960  1.00 53.82           N  
ANISOU  408  N   GLY A  94     6899   7363   6186   -127   -866     37       N  
ATOM    409  CA  GLY A  94     -15.646 -11.064 -12.187  1.00 55.67           C  
ANISOU  409  CA  GLY A  94     7044   7491   6615   -205   -961     89       C  
ATOM    410  C   GLY A  94     -15.252 -10.788 -13.631  1.00 55.86           C  
ANISOU  410  C   GLY A  94     6891   7490   6840   -110   -753    157       C  
ATOM    411  O   GLY A  94     -14.327 -10.010 -13.873  1.00 58.13           O  
ANISOU  411  O   GLY A  94     7047   7678   7359   -170   -798    269       O  
ATOM    412  N   ALA A  95     -15.927 -11.415 -14.597  1.00 54.08           N  
ANISOU  412  N   ALA A  95     6660   7346   6539     51   -539    107       N  
ATOM    413  CA  ALA A  95     -15.758 -11.043 -16.018  1.00 54.45           C  
ANISOU  413  CA  ALA A  95     6627   7412   6648    194   -315    150       C  
ATOM    414  C   ALA A  95     -16.749  -9.912 -16.363  1.00 53.52           C  
ANISOU  414  C   ALA A  95     6670   7295   6367    214   -238     52       C  
ATOM    415  O   ALA A  95     -17.711 -10.094 -17.110  1.00 52.31           O  
ANISOU  415  O   ALA A  95     6611   7204   6061    348   -119    -44       O  
ATOM    416  CB  ALA A  95     -15.943 -12.246 -16.929  1.00 53.20           C  
ANISOU  416  CB  ALA A  95     6428   7324   6461    389   -177    107       C  
ATOM    417  N   VAL A  96     -16.494  -8.752 -15.777  1.00 55.19           N  
ANISOU  417  N   VAL A  96     6909   7408   6650     78   -352     72       N  
ATOM    418  CA  VAL A  96     -17.383  -7.605 -15.811  1.00 55.72           C  
ANISOU  418  CA  VAL A  96     7126   7431   6614     71   -329    -29       C  
ATOM    419  C   VAL A  96     -17.578  -7.076 -17.229  1.00 56.70           C  
ANISOU  419  C   VAL A  96     7200   7583   6758    204   -116     57       C  
ATOM    420  O   VAL A  96     -18.723  -6.910 -17.679  1.00 55.70           O  
ANISOU  420  O   VAL A  96     7201   7497   6463    296    -33    -48       O  
ATOM    421  CB  VAL A  96     -16.836  -6.500 -14.899  1.00 57.96           C  
ANISOU  421  CB  VAL A  96     7432   7552   7036    -93   -548    -36       C  
ATOM    422  CG1 VAL A  96     -17.668  -5.279 -14.991  1.00 58.36           C  
ANISOU  422  CG1 VAL A  96     7614   7519   7039    -83   -522   -145       C  
ATOM    423  CG2 VAL A  96     -16.767  -6.987 -13.439  1.00 59.42           C  
ANISOU  423  CG2 VAL A  96     7746   7738   7090   -190   -782   -144       C  
ATOM    424  N   ASP A  97     -16.473  -6.838 -17.939  1.00 59.31           N  
ANISOU  424  N   ASP A  97     7337   7896   7301    229    -22    278       N  
ATOM    425  CA  ASP A  97     -16.551  -6.292 -19.287  1.00 61.35           C  
ANISOU  425  CA  ASP A  97     7557   8208   7544    379    206    421       C  
ATOM    426  C   ASP A  97     -17.336  -7.209 -20.199  1.00 59.89           C  
ANISOU  426  C   ASP A  97     7500   8187   7069    597    346    309       C  
ATOM    427  O   ASP A  97     -18.258  -6.757 -20.886  1.00 60.15           O  
ANISOU  427  O   ASP A  97     7659   8255   6938    694    407    262       O  
ATOM    428  CB  ASP A  97     -15.170  -6.014 -19.877  1.00 65.12           C  
ANISOU  428  CB  ASP A  97     7771   8660   8309    401    344    740       C  
ATOM    429  CG  ASP A  97     -14.544  -4.735 -19.338  1.00 70.44           C  
ANISOU  429  CG  ASP A  97     8297   9115   9351    202    190    895       C  
ATOM    430  OD1 ASP A  97     -15.115  -4.121 -18.403  1.00 72.53           O  
ANISOU  430  OD1 ASP A  97     8705   9249   9605     55    -49    699       O  
ATOM    431  OD2 ASP A  97     -13.468  -4.342 -19.855  1.00 77.61           O  
ANISOU  431  OD2 ASP A  97     8937   9965  10584    207    308   1220       O  
ATOM    432  N   ARG A  98     -16.987  -8.490 -20.178  1.00 58.90           N  
ANISOU  432  N   ARG A  98     7339   8129   6909    671    351    257       N  
ATOM    433  CA  ARG A  98     -17.659  -9.505 -20.966  1.00 57.56           C  
ANISOU  433  CA  ARG A  98     7292   8065   6513    881    406    106       C  
ATOM    434  C   ARG A  98     -19.151  -9.554 -20.652  1.00 53.96           C  
ANISOU  434  C   ARG A  98     7008   7579   5914    850    265   -102       C  
ATOM    435  O   ARG A  98     -19.970  -9.600 -21.548  1.00 53.39           O  
ANISOU  435  O   ARG A  98     7058   7551   5674   1004    287   -185       O  
ATOM    436  CB  ARG A  98     -17.020 -10.859 -20.668  1.00 58.78           C  
ANISOU  436  CB  ARG A  98     7352   8227   6753    916    368     67       C  
ATOM    437  CG  ARG A  98     -17.121 -11.900 -21.756  1.00 62.28           C  
ANISOU  437  CG  ARG A  98     7867   8753   7041   1194    462    -44       C  
ATOM    438  CD  ARG A  98     -15.983 -12.910 -21.581  1.00 70.42           C  
ANISOU  438  CD  ARG A  98     8724   9770   8261   1242    503     14       C  
ATOM    439  NE  ARG A  98     -16.015 -13.948 -22.606  1.00 77.36           N  
ANISOU  439  NE  ARG A  98     9692  10704   8997   1544    585   -138       N  
ATOM    440  CZ  ARG A  98     -15.294 -13.942 -23.726  1.00 83.21           C  
ANISOU  440  CZ  ARG A  98    10433  11555   9627   1818    858    -55       C  
ATOM    441  NH1 ARG A  98     -14.440 -12.954 -23.988  1.00 86.06           N  
ANISOU  441  NH1 ARG A  98    10652  11980  10067   1810   1101    244       N  
ATOM    442  NH2 ARG A  98     -15.423 -14.940 -24.589  1.00 85.97           N  
ANISOU  442  NH2 ARG A  98    10924  11942   9799   2121    889   -267       N  
ATOM    443  N   GLY A  99     -19.503  -9.535 -19.372  1.00 52.02           N  
ANISOU  443  N   GLY A  99     6769   7258   5736    665    120   -170       N  
ATOM    444  CA  GLY A  99     -20.901  -9.644 -18.966  1.00 49.17           C  
ANISOU  444  CA  GLY A  99     6523   6867   5292    647     36   -319       C  
ATOM    445  C   GLY A  99     -21.650  -8.387 -19.342  1.00 48.44           C  
ANISOU  445  C   GLY A  99     6513   6739   5153    655     81   -322       C  
ATOM    446  O   GLY A  99     -22.806  -8.431 -19.739  1.00 47.70           O  
ANISOU  446  O   GLY A  99     6492   6632   4999    733     58   -407       O  
ATOM    447  N   THR A 100     -20.975  -7.259 -19.230  1.00 48.46           N  
ANISOU  447  N   THR A 100     6477   6694   5240    572    120   -211       N  
ATOM    448  CA  THR A 100     -21.599  -6.010 -19.559  1.00 49.22           C  
ANISOU  448  CA  THR A 100     6626   6723   5350    573    152   -194       C  
ATOM    449  C   THR A 100     -22.036  -5.966 -21.019  1.00 49.32           C  
ANISOU  449  C   THR A 100     6681   6811   5246    759    239   -135       C  
ATOM    450  O   THR A 100     -23.164  -5.572 -21.329  1.00 48.19           O  
ANISOU  450  O   THR A 100     6617   6631   5059    807    208   -196       O  
ATOM    451  CB  THR A 100     -20.672  -4.837 -19.200  1.00 50.88           C  
ANISOU  451  CB  THR A 100     6754   6821   5754    444    135    -67       C  
ATOM    452  OG1 THR A 100     -20.794  -4.588 -17.795  1.00 52.00           O  
ANISOU  452  OG1 THR A 100     6961   6864   5930    301     -8   -209       O  
ATOM    453  CG2 THR A 100     -21.057  -3.581 -19.943  1.00 52.78           C  
ANISOU  453  CG2 THR A 100     6998   6989   6067    480    196     31       C  
ATOM    454  N   GLU A 101     -21.150  -6.409 -21.899  1.00 50.76           N  
ANISOU  454  N   GLU A 101     6818   7101   5366    884    346    -15       N  
ATOM    455  CA  GLU A 101     -21.402  -6.348 -23.320  1.00 52.89           C  
ANISOU  455  CA  GLU A 101     7175   7476   5445   1102    439     52       C  
ATOM    456  C   GLU A 101     -22.479  -7.343 -23.697  1.00 51.72           C  
ANISOU  456  C   GLU A 101     7167   7352   5129   1232    299   -168       C  
ATOM    457  O   GLU A 101     -23.299  -7.096 -24.582  1.00 52.31           O  
ANISOU  457  O   GLU A 101     7364   7448   5062   1365    247   -189       O  
ATOM    458  CB  GLU A 101     -20.123  -6.648 -24.067  1.00 55.91           C  
ANISOU  458  CB  GLU A 101     7482   7982   5780   1243    634    235       C  
ATOM    459  CG  GLU A 101     -19.002  -5.729 -23.678  1.00 60.48           C  
ANISOU  459  CG  GLU A 101     7854   8490   6633   1098    741    497       C  
ATOM    460  CD  GLU A 101     -17.763  -5.938 -24.521  1.00 68.11           C  
ANISOU  460  CD  GLU A 101     8696   9580   7602   1266    999    755       C  
ATOM    461  OE1 GLU A 101     -17.629  -7.014 -25.157  1.00 71.28           O  
ANISOU  461  OE1 GLU A 101     9185  10122   7775   1489   1087    663       O  
ATOM    462  OE2 GLU A 101     -16.927  -5.009 -24.553  1.00 71.32           O  
ANISOU  462  OE2 GLU A 101     8904   9925   8269   1188   1117   1059       O  
ATOM    463  N   LEU A 102     -22.497  -8.468 -23.001  1.00 50.16           N  
ANISOU  463  N   LEU A 102     6939   7128   4990   1185    199   -316       N  
ATOM    464  CA  LEU A 102     -23.528  -9.455 -23.257  1.00 50.19           C  
ANISOU  464  CA  LEU A 102     7026   7095   4947   1281     18   -511       C  
ATOM    465  C   LEU A 102     -24.878  -8.877 -22.827  1.00 48.85           C  
ANISOU  465  C   LEU A 102     6865   6813   4883   1184    -87   -553       C  
ATOM    466  O   LEU A 102     -25.906  -9.150 -23.451  1.00 49.61           O  
ANISOU  466  O   LEU A 102     7030   6858   4959   1288   -243   -645       O  
ATOM    467  CB  LEU A 102     -23.207 -10.728 -22.500  1.00 49.73           C  
ANISOU  467  CB  LEU A 102     6883   7001   5008   1227    -57   -602       C  
ATOM    468  CG  LEU A 102     -23.784 -12.066 -22.912  1.00 51.66           C  
ANISOU  468  CG  LEU A 102     7169   7186   5270   1359   -252   -785       C  
ATOM    469  CD1 LEU A 102     -23.763 -12.240 -24.409  1.00 54.08           C  
ANISOU  469  CD1 LEU A 102     7652   7563   5331   1636   -283   -879       C  
ATOM    470  CD2 LEU A 102     -22.937 -13.110 -22.257  1.00 50.62           C  
ANISOU  470  CD2 LEU A 102     6921   7041   5269   1313   -251   -790       C  
ATOM    471  N   LEU A 103     -24.872  -8.056 -21.779  1.00 46.92           N  
ANISOU  471  N   LEU A 103     6552   6511   4763   1004    -15   -492       N  
ATOM    472  CA  LEU A 103     -26.122  -7.458 -21.317  1.00 46.21           C  
ANISOU  472  CA  LEU A 103     6460   6313   4785    944    -58   -527       C  
ATOM    473  C   LEU A 103     -26.570  -6.357 -22.269  1.00 47.82           C  
ANISOU  473  C   LEU A 103     6721   6495   4952   1021    -48   -453       C  
ATOM    474  O   LEU A 103     -27.752  -6.240 -22.572  1.00 47.94           O  
ANISOU  474  O   LEU A 103     6747   6430   5038   1070   -151   -490       O  
ATOM    475  CB  LEU A 103     -26.014  -6.975 -19.882  1.00 44.41           C  
ANISOU  475  CB  LEU A 103     6190   6035   4648    780     14   -529       C  
ATOM    476  CG  LEU A 103     -25.952  -8.140 -18.886  1.00 42.21           C  
ANISOU  476  CG  LEU A 103     5861   5775   4399    720    -18   -572       C  
ATOM    477  CD1 LEU A 103     -25.504  -7.686 -17.501  1.00 41.49           C  
ANISOU  477  CD1 LEU A 103     5791   5680   4292    588     38   -569       C  
ATOM    478  CD2 LEU A 103     -27.275  -8.850 -18.804  1.00 39.69           C  
ANISOU  478  CD2 LEU A 103     5488   5388   4202    766    -85   -608       C  
ATOM    479  N   GLU A 104     -25.607  -5.606 -22.785  1.00 49.30           N  
ANISOU  479  N   GLU A 104     6919   6745   5066   1038     64   -312       N  
ATOM    480  CA  GLU A 104     -25.875  -4.572 -23.772  1.00 52.07           C  
ANISOU  480  CA  GLU A 104     7316   7092   5376   1123     88   -176       C  
ATOM    481  C   GLU A 104     -26.506  -5.146 -25.074  1.00 54.63           C  
ANISOU  481  C   GLU A 104     7772   7492   5493   1337    -39   -211       C  
ATOM    482  O   GLU A 104     -27.442  -4.569 -25.651  1.00 55.29           O  
ANISOU  482  O   GLU A 104     7902   7516   5588   1395   -141   -175       O  
ATOM    483  CB  GLU A 104     -24.578  -3.797 -24.044  1.00 53.06           C  
ANISOU  483  CB  GLU A 104     7380   7268   5510   1102    256     44       C  
ATOM    484  CG  GLU A 104     -24.043  -3.092 -22.791  1.00 52.69           C  
ANISOU  484  CG  GLU A 104     7223   7088   5707    890    281     50       C  
ATOM    485  CD  GLU A 104     -22.727  -2.341 -22.979  1.00 55.88           C  
ANISOU  485  CD  GLU A 104     7504   7479   6246    838    393    294       C  
ATOM    486  OE1 GLU A 104     -21.836  -2.816 -23.723  1.00 58.65           O  
ANISOU  486  OE1 GLU A 104     7816   7972   6494    948    519    450       O  
ATOM    487  OE2 GLU A 104     -22.566  -1.267 -22.354  1.00 56.68           O  
ANISOU  487  OE2 GLU A 104     7533   7406   6595    695    353    336       O  
ATOM    488  N   ARG A 105     -25.987  -6.296 -25.503  1.00 55.83           N  
ANISOU  488  N   ARG A 105     7991   7754   5466   1463    -63   -298       N  
ATOM    489  CA  ARG A 105     -26.510  -7.019 -26.641  1.00 58.60           C  
ANISOU  489  CA  ARG A 105     8512   8157   5594   1689   -244   -408       C  
ATOM    490  C   ARG A 105     -27.932  -7.519 -26.382  1.00 57.93           C  
ANISOU  490  C   ARG A 105     8407   7901   5701   1651   -530   -578       C  
ATOM    491  O   ARG A 105     -28.750  -7.607 -27.311  1.00 60.02           O  
ANISOU  491  O   ARG A 105     8796   8134   5874   1797   -762   -634       O  
ATOM    492  CB  ARG A 105     -25.574  -8.198 -26.982  1.00 60.07           C  
ANISOU  492  CB  ARG A 105     8767   8462   5594   1839   -202   -510       C  
ATOM    493  CG  ARG A 105     -25.987  -9.070 -28.185  1.00 65.78           C  
ANISOU  493  CG  ARG A 105     9723   9231   6039   2123   -423   -696       C  
ATOM    494  CD  ARG A 105     -26.231  -8.242 -29.454  1.00 73.88           C  
ANISOU  494  CD  ARG A 105    10949  10374   6745   2327   -424   -567       C  
ATOM    495  NE  ARG A 105     -26.592  -9.069 -30.616  1.00 81.14           N  
ANISOU  495  NE  ARG A 105    12156  11345   7326   2635   -678   -781       N  
ATOM    496  CZ  ARG A 105     -27.825  -9.472 -30.926  1.00 82.63           C  
ANISOU  496  CZ  ARG A 105    12442  11375   7578   2675  -1100   -980       C  
ATOM    497  NH1 ARG A 105     -28.010 -10.227 -31.995  1.00 86.23           N  
ANISOU  497  NH1 ARG A 105    13194  11868   7700   2977  -1366  -1205       N  
ATOM    498  NH2 ARG A 105     -28.868  -9.138 -30.171  1.00 81.90           N  
ANISOU  498  NH2 ARG A 105    12150  11071   7894   2433  -1265   -958       N  
ATOM    499  N   SER A 106     -28.216  -7.863 -25.130  1.00 55.68           N  
ANISOU  499  N   SER A 106     7960   7504   5691   1467   -521   -634       N  
ATOM    500  CA  SER A 106     -29.532  -8.374 -24.763  1.00 55.87           C  
ANISOU  500  CA  SER A 106     7894   7353   5980   1423   -737   -727       C  
ATOM    501  C   SER A 106     -30.583  -7.261 -24.747  1.00 56.68           C  
ANISOU  501  C   SER A 106     7940   7343   6252   1377   -755   -632       C  
ATOM    502  O   SER A 106     -31.762  -7.509 -25.047  1.00 58.08           O  
ANISOU  502  O   SER A 106     8068   7374   6622   1416   -991   -668       O  
ATOM    503  CB  SER A 106     -29.502  -9.051 -23.392  1.00 54.12           C  
ANISOU  503  CB  SER A 106     7509   7073   5980   1265   -662   -751       C  
ATOM    504  OG  SER A 106     -28.439  -9.977 -23.290  1.00 53.63           O  
ANISOU  504  OG  SER A 106     7469   7101   5808   1286   -629   -807       O  
ATOM    505  N   ILE A 107     -30.165  -6.053 -24.369  1.00 52.54           N  
ANISOU  505  N   ILE A 107     6877   7115   5970   1530   -331   -237       N  
ATOM    506  CA  ILE A 107     -31.079  -4.939 -24.385  1.00 52.42           C  
ANISOU  506  CA  ILE A 107     6860   6884   6174   1348   -264    -77       C  
ATOM    507  C   ILE A 107     -31.354  -4.600 -25.867  1.00 54.17           C  
ANISOU  507  C   ILE A 107     6937   7301   6343   1332   -327     38       C  
ATOM    508  O   ILE A 107     -32.505  -4.488 -26.255  1.00 54.57           O  
ANISOU  508  O   ILE A 107     6974   7244   6514   1389   -339     62       O  
ATOM    509  CB  ILE A 107     -30.631  -3.748 -23.425  1.00 51.84           C  
ANISOU  509  CB  ILE A 107     6871   6677   6149   1171   -199      0       C  
ATOM    510  CG1 ILE A 107     -31.820  -2.868 -23.037  1.00 52.70           C  
ANISOU  510  CG1 ILE A 107     7114   6430   6478   1164   -156     72       C  
ATOM    511  CG2 ILE A 107     -29.544  -2.909 -24.003  1.00 51.65           C  
ANISOU  511  CG2 ILE A 107     6762   6942   5920    931   -211     95       C  
ATOM    512  CD1 ILE A 107     -32.836  -3.522 -22.129  1.00 49.68           C  
ANISOU  512  CD1 ILE A 107     6762   5878   6234   1254    -85    -74       C  
ATOM    513  N   ALA A 108     -30.307  -4.526 -26.693  1.00 55.97           N  
ANISOU  513  N   ALA A 108     7018   7912   6334   1269   -371     69       N  
ATOM    514  CA  ALA A 108     -30.454  -4.435 -28.150  1.00 57.71           C  
ANISOU  514  CA  ALA A 108     7115   8382   6430   1259   -433    161       C  
ATOM    515  C   ALA A 108     -31.482  -5.401 -28.730  1.00 57.97           C  
ANISOU  515  C   ALA A 108     7101   8380   6543   1464   -490     50       C  
ATOM    516  O   ALA A 108     -32.353  -4.988 -29.463  1.00 59.60           O  
ANISOU  516  O   ALA A 108     7276   8575   6794   1488   -530    146       O  
ATOM    517  CB  ALA A 108     -29.146  -4.608 -28.810  1.00 58.90           C  
ANISOU  517  CB  ALA A 108     7044   9081   6251   1175   -453    101       C  
ATOM    518  N   ASP A 109     -31.428  -6.674 -28.374  1.00 58.70           N  
ANISOU  518  N   ASP A 109     7254   8438   6611   1608   -504   -167       N  
ATOM    519  CA  ASP A 109     -32.400  -7.636 -28.893  1.00 60.83           C  
ANISOU  519  CA  ASP A 109     7558   8652   6902   1661   -536   -307       C  
ATOM    520  C   ASP A 109     -33.836  -7.337 -28.449  1.00 62.20           C  
ANISOU  520  C   ASP A 109     7731   8615   7283   1534   -464   -311       C  
ATOM    521  O   ASP A 109     -34.782  -7.748 -29.118  1.00 63.34           O  
ANISOU  521  O   ASP A 109     7761   8890   7411   1493   -485   -418       O  
ATOM    522  CB  ASP A 109     -32.031  -9.061 -28.489  1.00 60.96           C  
ANISOU  522  CB  ASP A 109     7859   8524   6776   1800   -573   -539       C  
ATOM    523  CG  ASP A 109     -32.488 -10.115 -29.512  1.00 64.35           C  
ANISOU  523  CG  ASP A 109     8356   9024   7069   1840   -649   -713       C  
ATOM    524  OD1 ASP A 109     -33.511 -10.797 -29.241  1.00 67.11           O  
ANISOU  524  OD1 ASP A 109     8934   9105   7459   1632   -594   -837       O  
ATOM    525  OD2 ASP A 109     -31.810 -10.285 -30.566  1.00 64.20           O  
ANISOU  525  OD2 ASP A 109     8167   9368   6858   2027   -750   -758       O  
ATOM    526  N   ALA A 110     -33.997  -6.654 -27.314  1.00 63.20           N  
ANISOU  526  N   ALA A 110     7940   8511   7561   1476   -382   -249       N  
ATOM    527  CA  ALA A 110     -35.326  -6.349 -26.756  1.00 66.03           C  
ANISOU  527  CA  ALA A 110     8229   8798   8061   1407   -309   -324       C  
ATOM    528  C   ALA A 110     -35.264  -5.092 -25.891  1.00 66.94           C  
ANISOU  528  C   ALA A 110     8401   8726   8305   1466   -276   -198       C  
ATOM    529  O   ALA A 110     -35.270  -5.179 -24.664  1.00 66.61           O  
ANISOU  529  O   ALA A 110     8486   8487   8333   1377   -176   -264       O  
ATOM    530  CB  ALA A 110     -35.870  -7.536 -25.944  1.00 66.70           C  
ANISOU  530  CB  ALA A 110     8485   8744   8113   1178   -197   -545       C  
ATOM    531  N   PRO A 111     -35.215  -3.909 -26.529  1.00 69.17           N  
ANISOU  531  N   PRO A 111     8679   9027   8575   1610   -368    -14       N  
ATOM    532  CA  PRO A 111     -34.835  -2.698 -25.789  1.00 70.18           C  
ANISOU  532  CA  PRO A 111     9035   8870   8758   1621   -356    122       C  
ATOM    533  C   PRO A 111     -35.885  -2.243 -24.788  1.00 72.10           C  
ANISOU  533  C   PRO A 111     9274   8989   9129   1767   -314    -15       C  
ATOM    534  O   PRO A 111     -35.612  -1.374 -23.962  1.00 72.70           O  
ANISOU  534  O   PRO A 111     9579   8786   9257   1777   -292     38       O  
ATOM    535  CB  PRO A 111     -34.636  -1.648 -26.894  1.00 72.65           C  
ANISOU  535  CB  PRO A 111     9510   9163   8930   1704   -484    357       C  
ATOM    536  CG  PRO A 111     -34.843  -2.382 -28.219  1.00 72.45           C  
ANISOU  536  CG  PRO A 111     9248   9494   8785   1763   -559    341       C  
ATOM    537  CD  PRO A 111     -35.637  -3.600 -27.905  1.00 70.89           C  
ANISOU  537  CD  PRO A 111     8778   9474   8682   1770   -499     65       C  
ATOM    538  N   ASP A 112     -37.069  -2.841 -24.839  1.00 73.78           N  
ANISOU  538  N   ASP A 112     9205   9477   9350   1840   -291   -237       N  
ATOM    539  CA  ASP A 112     -38.107  -2.509 -23.878  1.00 76.06           C  
ANISOU  539  CA  ASP A 112     9366   9843   9688   1960   -230   -450       C  
ATOM    540  C   ASP A 112     -38.416  -3.628 -22.889  1.00 74.72           C  
ANISOU  540  C   ASP A 112     9098   9769   9522   1599    -32   -666       C  
ATOM    541  O   ASP A 112     -39.443  -3.588 -22.194  1.00 77.77           O  
ANISOU  541  O   ASP A 112     9259  10413   9875   1588     58   -915       O  
ATOM    542  CB  ASP A 112     -39.374  -2.065 -24.608  1.00 80.71           C  
ANISOU  542  CB  ASP A 112     9658  10835  10173   2345   -362   -607       C  
ATOM    543  CG  ASP A 112     -39.251  -0.665 -25.187  1.00 84.36           C  
ANISOU  543  CG  ASP A 112    10436  11045  10571   2816   -579   -398       C  
ATOM    544  OD1 ASP A 112     -39.783  -0.439 -26.303  1.00 87.86           O  
ANISOU  544  OD1 ASP A 112    10779  11740  10863   3142   -755   -388       O  
ATOM    545  OD2 ASP A 112     -38.625   0.202 -24.525  1.00 84.57           O  
ANISOU  545  OD2 ASP A 112    10879  10600  10652   2839   -582   -249       O  
ATOM    546  N   ASN A 113     -37.537  -4.622 -22.817  1.00 70.94           N  
ANISOU  546  N   ASN A 113     8826   9109   9018   1319     25   -594       N  
ATOM    547  CA  ASN A 113     -37.674  -5.673 -21.812  1.00 69.38           C  
ANISOU  547  CA  ASN A 113     8779   8830   8749    973    190   -739       C  
ATOM    548  C   ASN A 113     -37.176  -5.178 -20.449  1.00 66.79           C  
ANISOU  548  C   ASN A 113     8657   8232   8488    978    265   -692       C  
ATOM    549  O   ASN A 113     -35.983  -4.909 -20.269  1.00 64.77           O  
ANISOU  549  O   ASN A 113     8610   7737   8262   1072    203   -526       O  
ATOM    550  CB  ASN A 113     -36.931  -6.943 -22.234  1.00 68.42           C  
ANISOU  550  CB  ASN A 113     8948   8548   8500    814    167   -704       C  
ATOM    551  CG  ASN A 113     -36.957  -8.022 -21.160  1.00 69.57           C  
ANISOU  551  CG  ASN A 113     9497   8444   8491    489    302   -804       C  
ATOM    552  OD1 ASN A 113     -36.178  -7.991 -20.205  1.00 69.00           O  
ANISOU  552  OD1 ASN A 113     9710   8100   8405    559    313   -722       O  
ATOM    553  ND2 ASN A 113     -37.857  -8.980 -21.312  1.00 73.09           N  
ANISOU  553  ND2 ASN A 113    10018   8989   8762     93    404   -990       N  
ATOM    554  N   ILE A 114     -38.096  -5.094 -19.498  1.00 65.68           N  
ANISOU  554  N   ILE A 114     8405   8229   8320    844    406   -882       N  
ATOM    555  CA  ILE A 114     -37.811  -4.509 -18.193  1.00 63.22           C  
ANISOU  555  CA  ILE A 114     8235   7726   8057    874    479   -879       C  
ATOM    556  C   ILE A 114     -36.828  -5.343 -17.396  1.00 60.57           C  
ANISOU  556  C   ILE A 114     8318   7068   7626    679    530   -786       C  
ATOM    557  O   ILE A 114     -35.919  -4.791 -16.763  1.00 57.86           O  
ANISOU  557  O   ILE A 114     8126   6522   7333    812    491   -686       O  
ATOM    558  CB  ILE A 114     -39.117  -4.228 -17.379  1.00 66.11           C  
ANISOU  558  CB  ILE A 114     8311   8452   8356    798    626  -1164       C  
ATOM    559  CG1 ILE A 114     -39.930  -3.114 -18.051  1.00 68.25           C  
ANISOU  559  CG1 ILE A 114     8208   9042   8681   1258    492  -1281       C  
ATOM    560  CG2 ILE A 114     -38.822  -3.893 -15.937  1.00 64.35           C  
ANISOU  560  CG2 ILE A 114     8276   8041   8131    748    732  -1187       C  
ATOM    561  CD1 ILE A 114     -39.102  -1.892 -18.496  1.00 65.97           C  
ANISOU  561  CD1 ILE A 114     8171   8351   8543   1687    287  -1036       C  
ATOM    562  N   LYS A 115     -36.997  -6.663 -17.456  1.00 60.98           N  
ANISOU  562  N   LYS A 115     8609   7072   7488    383    595   -838       N  
ATOM    563  CA  LYS A 115     -36.098  -7.569 -16.749  1.00 60.53           C  
ANISOU  563  CA  LYS A 115     9090   6659   7247    322    588   -760       C  
ATOM    564  C   LYS A 115     -34.640  -7.340 -17.145  1.00 57.08           C  
ANISOU  564  C   LYS A 115     8721   6116   6848    711    391   -608       C  
ATOM    565  O   LYS A 115     -33.793  -7.212 -16.269  1.00 56.88           O  
ANISOU  565  O   LYS A 115     8882   5974   6756    845    360   -570       O  
ATOM    566  CB  LYS A 115     -36.498  -9.020 -16.969  1.00 63.66           C  
ANISOU  566  CB  LYS A 115     9909   6905   7372    -25    643   -831       C  
ATOM    567  CG  LYS A 115     -35.807 -10.005 -16.041  1.00 67.53           C  
ANISOU  567  CG  LYS A 115    11148   6944   7565    -58    628   -771       C  
ATOM    568  CD  LYS A 115     -36.200 -11.440 -16.419  1.00 75.61           C  
ANISOU  568  CD  LYS A 115    12784   7680   8263   -417    653   -835       C  
ATOM    569  CE  LYS A 115     -35.780 -12.466 -15.365  1.00 81.02           C  
ANISOU  569  CE  LYS A 115    14429   7812   8542   -506    648   -777       C  
ATOM    570  NZ  LYS A 115     -36.175 -13.860 -15.797  1.00 88.13           N  
ANISOU  570  NZ  LYS A 115    16119   8299   9064   -906    659   -839       N  
ATOM    571  N   VAL A 116     -34.336  -7.250 -18.442  1.00 55.04           N  
ANISOU  571  N   VAL A 116     8259   6002   6650    873    266   -554       N  
ATOM    572  CA  VAL A 116     -32.929  -7.025 -18.817  1.00 52.97           C  
ANISOU  572  CA  VAL A 116     7972   5810   6341   1161    108   -466       C  
ATOM    573  C   VAL A 116     -32.479  -5.633 -18.444  1.00 50.85           C  
ANISOU  573  C   VAL A 116     7479   5625   6215   1188    115   -395       C  
ATOM    574  O   VAL A 116     -31.356  -5.458 -17.950  1.00 50.65           O  
ANISOU  574  O   VAL A 116     7491   5673   6078   1283     59   -395       O  
ATOM    575  CB  VAL A 116     -32.523  -7.406 -20.290  1.00 52.83           C  
ANISOU  575  CB  VAL A 116     7825   5988   6259   1306    -24   -446       C  
ATOM    576  CG1 VAL A 116     -33.644  -7.187 -21.239  1.00 55.36           C  
ANISOU  576  CG1 VAL A 116     7901   6421   6713   1168     12   -446       C  
ATOM    577  CG2 VAL A 116     -31.276  -6.619 -20.736  1.00 51.11           C  
ANISOU  577  CG2 VAL A 116     7356   6057   6004   1461   -124   -375       C  
ATOM    578  N   ALA A 117     -33.359  -4.660 -18.634  1.00 50.14           N  
ANISOU  578  N   ALA A 117     7197   5539   6313   1121    168   -371       N  
ATOM    579  CA  ALA A 117     -33.070  -3.275 -18.227  1.00 50.10           C  
ANISOU  579  CA  ALA A 117     7160   5467   6408   1128    168   -315       C  
ATOM    580  C   ALA A 117     -32.677  -3.168 -16.748  1.00 49.84           C  
ANISOU  580  C   ALA A 117     7278   5320   6336   1073    240   -390       C  
ATOM    581  O   ALA A 117     -31.786  -2.404 -16.391  1.00 49.58           O  
ANISOU  581  O   ALA A 117     7276   5291   6272   1024    212   -366       O  
ATOM    582  CB  ALA A 117     -34.245  -2.366 -18.551  1.00 51.02           C  
ANISOU  582  CB  ALA A 117     7173   5548   6663   1221    171   -328       C  
ATOM    583  N   THR A 118     -33.304  -3.991 -15.907  1.00 51.03           N  
ANISOU  583  N   THR A 118     7549   5405   6432   1017    340   -491       N  
ATOM    584  CA  THR A 118     -33.026  -4.016 -14.461  1.00 51.71           C  
ANISOU  584  CA  THR A 118     7819   5396   6433    971    412   -560       C  
ATOM    585  C   THR A 118     -31.597  -4.509 -14.165  1.00 51.75           C  
ANISOU  585  C   THR A 118     7973   5463   6226   1100    299   -542       C  
ATOM    586  O   THR A 118     -30.800  -3.795 -13.551  1.00 51.99           O  
ANISOU  586  O   THR A 118     7953   5578   6222   1106    274   -573       O  
ATOM    587  CB  THR A 118     -34.094  -4.850 -13.690  1.00 53.24           C  
ANISOU  587  CB  THR A 118     8168   5533   6525    783    568   -663       C  
ATOM    588  OG1 THR A 118     -35.372  -4.224 -13.834  1.00 53.46           O  
ANISOU  588  OG1 THR A 118     7905   5716   6690    717    666   -776       O  
ATOM    589  CG2 THR A 118     -33.763  -4.940 -12.206  1.00 53.42           C  
ANISOU  589  CG2 THR A 118     8439   5457   6399    735    638   -710       C  
ATOM    590  N   VAL A 119     -31.276  -5.711 -14.625  1.00 52.14           N  
ANISOU  590  N   VAL A 119     8206   5516   6087   1235    212   -534       N  
ATOM    591  CA  VAL A 119     -29.923  -6.253 -14.471  1.00 52.80           C  
ANISOU  591  CA  VAL A 119     8395   5775   5890   1533     48   -582       C  
ATOM    592  C   VAL A 119     -28.893  -5.336 -15.098  1.00 51.55           C  
ANISOU  592  C   VAL A 119     7821   6023   5740   1543    -30   -598       C  
ATOM    593  O   VAL A 119     -27.878  -5.023 -14.480  1.00 53.08           O  
ANISOU  593  O   VAL A 119     7907   6504   5755   1616    -89   -699       O  
ATOM    594  CB  VAL A 119     -29.802  -7.651 -15.084  1.00 54.45           C  
ANISOU  594  CB  VAL A 119     8931   5889   5866   1778    -74   -602       C  
ATOM    595  CG1 VAL A 119     -28.360  -8.087 -15.113  1.00 57.38           C  
ANISOU  595  CG1 VAL A 119     9305   6593   5903   2252   -297   -719       C  
ATOM    596  CG2 VAL A 119     -30.631  -8.641 -14.283  1.00 57.40           C  
ANISOU  596  CG2 VAL A 119     9902   5818   6089   1652      9   -592       C  
ATOM    597  N   LEU A 120     -29.157  -4.882 -16.323  1.00 49.66           N  
ANISOU  597  N   LEU A 120     7354   5858   5655   1413    -22   -513       N  
ATOM    598  CA  LEU A 120     -28.208  -3.983 -16.957  1.00 48.97           C  
ANISOU  598  CA  LEU A 120     6954   6149   5501   1270    -62   -510       C  
ATOM    599  C   LEU A 120     -28.042  -2.713 -16.139  1.00 48.80           C  
ANISOU  599  C   LEU A 120     6926   6062   5553    978     22   -516       C  
ATOM    600  O   LEU A 120     -26.917  -2.308 -15.837  1.00 50.07           O  
ANISOU  600  O   LEU A 120     6918   6609   5495    849     -6   -629       O  
ATOM    601  CB  LEU A 120     -28.579  -3.673 -18.398  1.00 48.02           C  
ANISOU  601  CB  LEU A 120     6698   6060   5484   1155    -67   -382       C  
ATOM    602  CG  LEU A 120     -27.530  -2.823 -19.132  1.00 48.99           C  
ANISOU  602  CG  LEU A 120     6573   6608   5430    887    -86   -367       C  
ATOM    603  CD1 LEU A 120     -26.068  -3.300 -18.910  1.00 48.78           C  
ANISOU  603  CD1 LEU A 120     6266   7243   5023   1002   -171   -591       C  
ATOM    604  CD2 LEU A 120     -27.876  -2.720 -20.629  1.00 46.38           C  
ANISOU  604  CD2 LEU A 120     6167   6326   5128    822   -109   -225       C  
ATOM    605  N   GLY A 121     -29.157  -2.106 -15.750  1.00 47.46           N  
ANISOU  605  N   GLY A 121     6928   5465   5639    885    118   -447       N  
ATOM    606  CA  GLY A 121     -29.089  -0.842 -15.016  1.00 48.76           C  
ANISOU  606  CA  GLY A 121     7192   5471   5864    652    180   -473       C  
ATOM    607  C   GLY A 121     -28.318  -0.985 -13.709  1.00 49.98           C  
ANISOU  607  C   GLY A 121     7341   5803   5846    650    186   -635       C  
ATOM    608  O   GLY A 121     -27.459  -0.153 -13.380  1.00 51.27           O  
ANISOU  608  O   GLY A 121     7453   6149   5875    373    191   -720       O  
ATOM    609  N   LEU A 122     -28.632  -2.066 -12.982  1.00 49.76           N  
ANISOU  609  N   LEU A 122     7413   5726   5766    918    185   -684       N  
ATOM    610  CA  LEU A 122     -28.007  -2.395 -11.697  1.00 51.31           C  
ANISOU  610  CA  LEU A 122     7680   6071   5746   1029    162   -823       C  
ATOM    611  C   LEU A 122     -26.540  -2.688 -11.901  1.00 53.52           C  
ANISOU  611  C   LEU A 122     7715   6930   5687   1151     17   -956       C  
ATOM    612  O   LEU A 122     -25.683  -2.238 -11.144  1.00 56.25           O  
ANISOU  612  O   LEU A 122     7922   7616   5833   1068     -8  -1121       O  
ATOM    613  CB  LEU A 122     -28.711  -3.601 -11.055  1.00 50.91           C  
ANISOU  613  CB  LEU A 122     7944   5771   5625   1260    184   -801       C  
ATOM    614  CG  LEU A 122     -29.772  -3.425  -9.945  1.00 50.81           C  
ANISOU  614  CG  LEU A 122     8134   5457   5715   1129    344   -818       C  
ATOM    615  CD1 LEU A 122     -30.360  -2.008  -9.806  1.00 47.85           C  
ANISOU  615  CD1 LEU A 122     7610   4965   5604    915    450   -859       C  
ATOM    616  CD2 LEU A 122     -30.887  -4.430 -10.050  1.00 49.49           C  
ANISOU  616  CD2 LEU A 122     8212   5048   5541   1094    434   -754       C  
ATOM    617  N   THR A 123     -26.253  -3.419 -12.964  1.00 51.17           N  
ANISOU  617  N   THR A 123     6773   6208   6460   1040    242   -333       N  
ATOM    618  CA  THR A 123     -24.889  -3.775 -13.274  1.00 51.57           C  
ANISOU  618  CA  THR A 123     6783   6226   6583   1112    275   -247       C  
ATOM    619  C   THR A 123     -24.051  -2.529 -13.512  1.00 50.21           C  
ANISOU  619  C   THR A 123     6649   6227   6199   1103    200   -242       C  
ATOM    620  O   THR A 123     -22.918  -2.454 -13.053  1.00 51.28           O  
ANISOU  620  O   THR A 123     6717   6447   6317   1112    181    -55       O  
ATOM    621  CB  THR A 123     -24.810  -4.728 -14.501  1.00 53.01           C  
ANISOU  621  CB  THR A 123     6955   6217   6967   1167    381   -455       C  
ATOM    622  OG1 THR A 123     -25.512  -5.939 -14.210  1.00 53.74           O  
ANISOU  622  OG1 THR A 123     6995   6069   7352   1151    445   -452       O  
ATOM    623  CG2 THR A 123     -23.365  -5.045 -14.875  1.00 52.76           C  
ANISOU  623  CG2 THR A 123     6838   6157   7049   1277    477   -405       C  
ATOM    624  N   TYR A 124     -24.572  -1.555 -14.239  1.00 49.31           N  
ANISOU  624  N   TYR A 124     6605   6164   5966   1070    139   -388       N  
ATOM    625  CA  TYR A 124     -23.742  -0.404 -14.537  1.00 49.71           C  
ANISOU  625  CA  TYR A 124     6663   6324   5897   1043     61   -333       C  
ATOM    626  C   TYR A 124     -23.384   0.327 -13.250  1.00 50.51           C  
ANISOU  626  C   TYR A 124     6773   6494   5925    968      1   -250       C  
ATOM    627  O   TYR A 124     -22.282   0.850 -13.137  1.00 51.22           O  
ANISOU  627  O   TYR A 124     6832   6674   5955    921    -57   -141       O  
ATOM    628  CB  TYR A 124     -24.429   0.585 -15.458  1.00 49.61           C  
ANISOU  628  CB  TYR A 124     6673   6330   5845   1005    -21   -400       C  
ATOM    629  CG  TYR A 124     -24.447   0.285 -16.938  1.00 52.24           C  
ANISOU  629  CG  TYR A 124     6977   6771   6097    988    -13   -453       C  
ATOM    630  CD1 TYR A 124     -23.283  -0.021 -17.648  1.00 55.66           C  
ANISOU  630  CD1 TYR A 124     7367   7338   6442   1001     58   -438       C  
ATOM    631  CD2 TYR A 124     -25.641   0.378 -17.649  1.00 53.28           C  
ANISOU  631  CD2 TYR A 124     7094   6940   6210    931    -77   -512       C  
ATOM    632  CE1 TYR A 124     -23.334  -0.264 -19.039  1.00 56.08           C  
ANISOU  632  CE1 TYR A 124     7386   7595   6325    936     95   -549       C  
ATOM    633  CE2 TYR A 124     -25.702   0.148 -18.999  1.00 55.40           C  
ANISOU  633  CE2 TYR A 124     7323   7422   6304    841    -93   -568       C  
ATOM    634  CZ  TYR A 124     -24.558  -0.173 -19.695  1.00 56.84           C  
ANISOU  634  CZ  TYR A 124     7487   7774   6335    833      4   -618       C  
ATOM    635  OH  TYR A 124     -24.676  -0.383 -21.046  1.00 55.88           O  
ANISOU  635  OH  TYR A 124     7318   7960   5950    695     12   -727       O  
ATOM    636  N   VAL A 125     -24.312   0.383 -12.289  1.00 51.73           N  
ANISOU  636  N   VAL A 125     6952   6647   6055    924     25   -325       N  
ATOM    637  CA  VAL A 125     -24.042   1.065 -11.023  1.00 54.29           C  
ANISOU  637  CA  VAL A 125     7286   7112   6228    796      0   -345       C  
ATOM    638  C   VAL A 125     -22.870   0.412 -10.285  1.00 56.52           C  
ANISOU  638  C   VAL A 125     7484   7590   6401    726    -41    -87       C  
ATOM    639  O   VAL A 125     -21.946   1.097  -9.841  1.00 57.86           O  
ANISOU  639  O   VAL A 125     7638   7907   6436    598   -132    -42       O  
ATOM    640  CB  VAL A 125     -25.287   1.152 -10.084  1.00 55.39           C  
ANISOU  640  CB  VAL A 125     7435   7300   6311    750     92   -508       C  
ATOM    641  CG1 VAL A 125     -24.877   1.631  -8.693  1.00 57.28           C  
ANISOU  641  CG1 VAL A 125     7674   7805   6285    558     97   -572       C  
ATOM    642  CG2 VAL A 125     -26.319   2.096 -10.647  1.00 54.01           C  
ANISOU  642  CG2 VAL A 125     7282   6929   6307    818    124   -728       C  
ATOM    643  N   GLN A 126     -22.908  -0.908 -10.178  1.00 58.23           N  
ANISOU  643  N   GLN A 126     7611   7785   6727    797      9    113       N  
ATOM    644  CA  GLN A 126     -21.833  -1.655  -9.540  1.00 61.84           C  
ANISOU  644  CA  GLN A 126     7910   8389   7196    763    -37    473       C  
ATOM    645  C   GLN A 126     -20.465  -1.302 -10.106  1.00 62.09           C  
ANISOU  645  C   GLN A 126     7875   8445   7269    794    -98    583       C  
ATOM    646  O   GLN A 126     -19.503  -1.124  -9.342  1.00 63.99           O  
ANISOU  646  O   GLN A 126     7999   8933   7381    663   -211    831       O  
ATOM    647  CB  GLN A 126     -22.042  -3.144  -9.727  1.00 63.68           C  
ANISOU  647  CB  GLN A 126     8028   8422   7746    896     50    670       C  
ATOM    648  CG  GLN A 126     -23.256  -3.715  -9.028  1.00 67.78           C  
ANISOU  648  CG  GLN A 126     8540   8951   8263    834     95    702       C  
ATOM    649  CD  GLN A 126     -23.283  -5.223  -9.170  1.00 75.06           C  
ANISOU  649  CD  GLN A 126     9310   9603   9606    939    162    957       C  
ATOM    650  OE1 GLN A 126     -22.230  -5.859  -9.318  1.00 78.41           O  
ANISOU  650  OE1 GLN A 126     9576   9913  10303   1037    167   1213       O  
ATOM    651  NE2 GLN A 126     -24.480  -5.809  -9.142  1.00 77.80           N  
ANISOU  651  NE2 GLN A 126     9672   9809  10079    921    225    893       N  
ATOM    652  N   VAL A 127     -20.386  -1.207 -11.438  1.00 60.42           N  
ANISOU  652  N   VAL A 127     7711   8044   7201    934    -30    423       N  
ATOM    653  CA  VAL A 127     -19.123  -0.930 -12.151  1.00 61.05           C  
ANISOU  653  CA  VAL A 127     7695   8173   7325    977    -42    529       C  
ATOM    654  C   VAL A 127     -18.822   0.555 -12.237  1.00 60.14           C  
ANISOU  654  C   VAL A 127     7657   8168   7025    825   -169    447       C  
ATOM    655  O   VAL A 127     -17.805   0.961 -12.807  1.00 60.58           O  
ANISOU  655  O   VAL A 127     7622   8300   7093    817   -199    563       O  
ATOM    656  CB  VAL A 127     -19.133  -1.457 -13.606  1.00 61.19           C  
ANISOU  656  CB  VAL A 127     7707   8037   7505   1146    115    368       C  
ATOM    657  CG1 VAL A 127     -17.761  -1.264 -14.243  1.00 63.40           C  
ANISOU  657  CG1 VAL A 127     7833   8438   7817   1191    151    506       C  
ATOM    658  CG2 VAL A 127     -19.547  -2.921 -13.660  1.00 62.91           C  
ANISOU  658  CG2 VAL A 127     7866   8033   8004   1284    267    340       C  
ATOM    659  N   GLN A 128     -19.721   1.368 -11.693  1.00 64.41           N  
ANISOU  659  N   GLN A 128     7799   9143   7529    802    147    625       N  
ATOM    660  CA  GLN A 128     -19.524   2.825 -11.629  1.00 62.49           C  
ANISOU  660  CA  GLN A 128     7574   9164   7002    580    229    540       C  
ATOM    661  C   GLN A 128     -19.637   3.521 -12.986  1.00 59.96           C  
ANISOU  661  C   GLN A 128     7378   8793   6611    597    305    320       C  
ATOM    662  O   GLN A 128     -19.017   4.572 -13.222  1.00 59.87           O  
ANISOU  662  O   GLN A 128     7327   8989   6433    461    360    306       O  
ATOM    663  CB  GLN A 128     -18.212   3.161 -10.933  1.00 64.69           C  
ANISOU  663  CB  GLN A 128     7627   9830   7121    501    245    696       C  
ATOM    664  CG  GLN A 128     -17.928   2.185  -9.822  1.00 69.49           C  
ANISOU  664  CG  GLN A 128     8040  10543   7821    540    142   1008       C  
ATOM    665  CD  GLN A 128     -16.978   2.725  -8.819  1.00 74.52           C  
ANISOU  665  CD  GLN A 128     8437  11671   8205    336    141   1181       C  
ATOM    666  OE1 GLN A 128     -16.055   3.482  -9.151  1.00 74.99           O  
ANISOU  666  OE1 GLN A 128     8428  11971   8094    273    216   1093       O  
ATOM    667  NE2 GLN A 128     -17.189   2.346  -7.561  1.00 77.31           N  
ANISOU  667  NE2 GLN A 128     8627  12249   8495    183     48   1453       N  
ATOM    668  N   LYS A 129     -20.453   2.912 -13.853  1.00 57.92           N  
ANISOU  668  N   LYS A 129     7245   8286   6474    722    291    182       N  
ATOM    669  CA  LYS A 129     -20.911   3.506 -15.108  1.00 54.78           C  
ANISOU  669  CA  LYS A 129     6945   7891   5977    689    332     29       C  
ATOM    670  C   LYS A 129     -22.260   4.164 -14.817  1.00 50.85           C  
ANISOU  670  C   LYS A 129     6591   7220   5507    537    297     45       C  
ATOM    671  O   LYS A 129     -23.323   3.682 -15.221  1.00 49.61           O  
ANISOU  671  O   LYS A 129     6534   6889   5427    572    259    -28       O  
ATOM    672  CB  LYS A 129     -21.014   2.423 -16.178  1.00 56.87           C  
ANISOU  672  CB  LYS A 129     7212   8074   6322    887    341   -180       C  
ATOM    673  CG  LYS A 129     -19.648   1.949 -16.653  1.00 61.18           C  
ANISOU  673  CG  LYS A 129     7562   8846   6834   1070    407   -281       C  
ATOM    674  CD  LYS A 129     -19.734   0.915 -17.746  1.00 65.40           C  
ANISOU  674  CD  LYS A 129     8062   9325   7460   1268    441   -623       C  
ATOM    675  CE  LYS A 129     -18.359   0.640 -18.312  1.00 69.81           C  
ANISOU  675  CE  LYS A 129     8370  10212   7939   1456    538   -787       C  
ATOM    676  NZ  LYS A 129     -18.361  -0.662 -19.025  1.00 74.27           N  
ANISOU  676  NZ  LYS A 129     8865  10610   8744   1720    572  -1207       N  
ATOM    677  N   TYR A 130     -22.193   5.263 -14.079  1.00 48.11           N  
ANISOU  677  N   TYR A 130     6228   6937   5115    365    312    108       N  
ATOM    678  CA  TYR A 130     -23.369   5.905 -13.535  1.00 45.40           C  
ANISOU  678  CA  TYR A 130     5958   6448   4842    254    295     71       C  
ATOM    679  C   TYR A 130     -24.252   6.530 -14.617  1.00 43.55           C  
ANISOU  679  C   TYR A 130     5810   6077   4658    253    280     54       C  
ATOM    680  O   TYR A 130     -25.475   6.330 -14.613  1.00 42.07           O  
ANISOU  680  O   TYR A 130     5682   5758   4545    276    246     19       O  
ATOM    681  CB  TYR A 130     -22.924   6.915 -12.483  1.00 46.35           C  
ANISOU  681  CB  TYR A 130     5998   6680   4930     75    331     41       C  
ATOM    682  CG  TYR A 130     -22.214   6.268 -11.290  1.00 48.48           C  
ANISOU  682  CG  TYR A 130     6129   7197   5094     31    325    112       C  
ATOM    683  CD1 TYR A 130     -22.837   5.261 -10.558  1.00 47.98           C  
ANISOU  683  CD1 TYR A 130     6033   7151   5046     61    269    194       C  
ATOM    684  CD2 TYR A 130     -20.928   6.682 -10.888  1.00 51.93           C  
ANISOU  684  CD2 TYR A 130     6432   7892   5404    -77    355    155       C  
ATOM    685  CE1 TYR A 130     -22.217   4.667  -9.486  1.00 52.14           C  
ANISOU  685  CE1 TYR A 130     6385   7948   5478     -2    232    367       C  
ATOM    686  CE2 TYR A 130     -20.287   6.092  -9.790  1.00 53.85           C  
ANISOU  686  CE2 TYR A 130     6496   8439   5524   -134    330    286       C  
ATOM    687  CZ  TYR A 130     -20.947   5.079  -9.094  1.00 55.66           C  
ANISOU  687  CZ  TYR A 130     6682   8683   5783    -91    262    417       C  
ATOM    688  OH  TYR A 130     -20.369   4.454  -7.995  1.00 58.77           O  
ANISOU  688  OH  TYR A 130     6852   9417   6059   -170    204    656       O  
ATOM    689  N   ASP A 131     -23.593   7.227 -15.553  1.00 43.60           N  
ANISOU  689  N   ASP A 131     5784   6178   4603    209    293    130       N  
ATOM    690  CA AASP A 131     -24.268   7.876 -16.675  0.44 43.31           C  
ANISOU  690  CA AASP A 131     5767   6098   4591    175    252    230       C  
ATOM    691  CA BASP A 131     -24.222   7.866 -16.711  0.56 43.44           C  
ANISOU  691  CA BASP A 131     5780   6124   4599    175    253    233       C  
ATOM    692  C   ASP A 131     -25.141   6.889 -17.407  1.00 42.54           C  
ANISOU  692  C   ASP A 131     5711   6022   4430    277    223    163       C  
ATOM    693  O   ASP A 131     -26.309   7.159 -17.621  1.00 41.44           O  
ANISOU  693  O   ASP A 131     5602   5769   4371    266    175    205       O  
ATOM    694  CB AASP A 131     -23.252   8.486 -17.639  0.44 45.15           C  
ANISOU  694  CB AASP A 131     5902   6563   4688     77    255    391       C  
ATOM    695  CB BASP A 131     -23.168   8.467 -17.695  0.56 45.34           C  
ANISOU  695  CB BASP A 131     5919   6611   4696     76    257    395       C  
ATOM    696  CG AASP A 131     -22.742   9.812 -17.158  0.44 47.04           C  
ANISOU  696  CG AASP A 131     6111   6686   5075    -97    244    510       C  
ATOM    697  CG BASP A 131     -22.085   7.445 -18.207  0.56 47.66           C  
ANISOU  697  CG BASP A 131     6117   7242   4747    172    315    295       C  
ATOM    698  OD1AASP A 131     -23.598  10.648 -16.797  0.44 47.50           O  
ANISOU  698  OD1AASP A 131     6215   6431   5400   -136    206    523       O  
ATOM    699  OD1BASP A 131     -21.842   6.352 -17.624  0.56 46.63           O  
ANISOU  699  OD1BASP A 131     5996   7079   4639    325    348    129       O  
ATOM    700  OD2AASP A 131     -21.504  10.011 -17.113  0.44 48.25           O  
ANISOU  700  OD2AASP A 131     6178   7049   5105   -195    274    561       O  
ATOM    701  OD2BASP A 131     -21.438   7.772 -19.240  0.56 50.85           O  
ANISOU  701  OD2BASP A 131     6395   7972   4954     90    322    404       O  
ATOM    702  N   LEU A 132     -24.574   5.739 -17.738  1.00 42.59           N  
ANISOU  702  N   LEU A 132     5697   6160   4324    378    250     31       N  
ATOM    703  CA  LEU A 132     -25.266   4.687 -18.481  1.00 42.40           C  
ANISOU  703  CA  LEU A 132     5703   6148   4259    448    228   -124       C  
ATOM    704  C   LEU A 132     -26.365   4.012 -17.661  1.00 40.35           C  
ANISOU  704  C   LEU A 132     5542   5620   4167    468    177   -170       C  
ATOM    705  O   LEU A 132     -27.352   3.506 -18.224  1.00 40.46           O  
ANISOU  705  O   LEU A 132     5593   5611   4169    449    132   -248       O  
ATOM    706  CB  LEU A 132     -24.242   3.656 -18.986  1.00 43.66           C  
ANISOU  706  CB  LEU A 132     5784   6460   4345    576    283   -335       C  
ATOM    707  CG  LEU A 132     -23.696   3.922 -20.393  1.00 48.01           C  
ANISOU  707  CG  LEU A 132     6190   7436   4612    529    328   -398       C  
ATOM    708  CD1 LEU A 132     -23.554   5.389 -20.740  1.00 49.19           C  
ANISOU  708  CD1 LEU A 132     6274   7783   4630    345    303    -75       C  
ATOM    709  CD2 LEU A 132     -22.354   3.216 -20.649  1.00 53.12           C  
ANISOU  709  CD2 LEU A 132     6690   8299   5192    680    417   -617       C  
ATOM    710  N   ALA A 133     -26.199   4.004 -16.343  1.00 38.11           N  
ANISOU  710  N   ALA A 133     5268   5214   3998    466    177   -108       N  
ATOM    711  CA  ALA A 133     -27.221   3.437 -15.467  1.00 37.70           C  
ANISOU  711  CA  ALA A 133     5256   5012   4055    433    122    -91       C  
ATOM    712  C   ALA A 133     -28.530   4.238 -15.481  1.00 36.44           C  
ANISOU  712  C   ALA A 133     5106   4838   3899    357    101    -60       C  
ATOM    713  O   ALA A 133     -29.607   3.661 -15.600  1.00 36.28           O  
ANISOU  713  O   ALA A 133     5111   4773   3898    328     46    -78       O  
ATOM    714  CB  ALA A 133     -26.705   3.303 -14.021  1.00 37.36           C  
ANISOU  714  CB  ALA A 133     5148   4991   4053    399    123      5       C  
ATOM    715  N   VAL A 134     -28.430   5.560 -15.355  1.00 36.19           N  
ANISOU  715  N   VAL A 134     5034   4825   3890    326    139    -16       N  
ATOM    716  CA  VAL A 134     -29.601   6.382 -15.060  1.00 36.19           C  
ANISOU  716  CA  VAL A 134     4994   4762   3993    305    128    -13       C  
ATOM    717  C   VAL A 134     -30.808   6.114 -16.003  1.00 37.27           C  
ANISOU  717  C   VAL A 134     5132   4918   4109    319     61     40       C  
ATOM    718  O   VAL A 134     -31.863   5.713 -15.538  1.00 38.03           O  
ANISOU  718  O   VAL A 134     5202   5028   4218    300     34      9       O  
ATOM    719  CB  VAL A 134     -29.226   7.877 -14.960  1.00 37.02           C  
ANISOU  719  CB  VAL A 134     5048   4774   4244    288    164      3       C  
ATOM    720  CG1 VAL A 134     -30.464   8.737 -14.896  1.00 37.92           C  
ANISOU  720  CG1 VAL A 134     5088   4757   4562    332    147     -6       C  
ATOM    721  CG2 VAL A 134     -28.380   8.121 -13.722  1.00 35.98           C  
ANISOU  721  CG2 VAL A 134     4880   4682   4108    218    232   -124       C  
ATOM    722  N   PRO A 135     -30.645   6.277 -17.327  1.00 38.04           N  
ANISOU  722  N   PRO A 135     5224   5106   4124    317     30    136       N  
ATOM    723  CA  PRO A 135     -31.844   6.125 -18.140  1.00 38.88           C  
ANISOU  723  CA  PRO A 135     5283   5314   4175    292    -41    206       C  
ATOM    724  C   PRO A 135     -32.529   4.786 -17.904  1.00 39.03           C  
ANISOU  724  C   PRO A 135     5355   5347   4126    247    -72     63       C  
ATOM    725  O   PRO A 135     -33.763   4.707 -17.924  1.00 39.95           O  
ANISOU  725  O   PRO A 135     5416   5520   4241    208   -125    102       O  
ATOM    726  CB  PRO A 135     -31.302   6.175 -19.585  1.00 40.36           C  
ANISOU  726  CB  PRO A 135     5424   5741   4167    240    -65    296       C  
ATOM    727  CG  PRO A 135     -29.943   6.813 -19.485  1.00 39.93           C  
ANISOU  727  CG  PRO A 135     5370   5666   4136    248    -11    351       C  
ATOM    728  CD  PRO A 135     -29.423   6.406 -18.155  1.00 38.43           C  
ANISOU  728  CD  PRO A 135     5265   5281   4052    302     52    180       C  
ATOM    729  N   LEU A 136     -31.741   3.742 -17.687  1.00 38.64           N  
ANISOU  729  N   LEU A 136     5389   5231   4058    248    -52    -77       N  
ATOM    730  CA  LEU A 136     -32.294   2.415 -17.521  1.00 39.91           C  
ANISOU  730  CA  LEU A 136     5603   5312   4247    182   -109   -184       C  
ATOM    731  C   LEU A 136     -33.038   2.302 -16.174  1.00 38.69           C  
ANISOU  731  C   LEU A 136     5420   5097   4184    125   -136    -90       C  
ATOM    732  O   LEU A 136     -34.159   1.799 -16.097  1.00 39.33           O  
ANISOU  732  O   LEU A 136     5476   5214   4253     17   -204    -68       O  
ATOM    733  CB  LEU A 136     -31.186   1.371 -17.628  1.00 40.95           C  
ANISOU  733  CB  LEU A 136     5799   5311   4449    238    -93   -341       C  
ATOM    734  CG  LEU A 136     -30.734   1.004 -19.041  1.00 46.49           C  
ANISOU  734  CG  LEU A 136     6486   6153   5023    254    -68   -568       C  
ATOM    735  CD1 LEU A 136     -29.359   0.339 -19.028  1.00 48.06           C  
ANISOU  735  CD1 LEU A 136     6687   6245   5326    393    -12   -737       C  
ATOM    736  CD2 LEU A 136     -31.792   0.127 -19.761  1.00 48.86           C  
ANISOU  736  CD2 LEU A 136     6800   6477   5287    118   -139   -751       C  
ATOM    737  N   LEU A 137     -32.417   2.804 -15.124  1.00 36.92           N  
ANISOU  737  N   LEU A 137     5163   4860   4005    164    -82    -39       N  
ATOM    738  CA  LEU A 137     -33.037   2.751 -13.838  1.00 37.38           C  
ANISOU  738  CA  LEU A 137     5131   5003   4067     79    -93     23       C  
ATOM    739  C   LEU A 137     -34.294   3.637 -13.840  1.00 37.66           C  
ANISOU  739  C   LEU A 137     5054   5177   4079     81    -78      4       C  
ATOM    740  O   LEU A 137     -35.330   3.234 -13.310  1.00 38.85           O  
ANISOU  740  O   LEU A 137     5112   5467   4180    -21   -119     41       O  
ATOM    741  CB  LEU A 137     -32.028   3.111 -12.729  1.00 37.58           C  
ANISOU  741  CB  LEU A 137     5100   5091   4085     83    -31     40       C  
ATOM    742  CG  LEU A 137     -30.847   2.123 -12.491  1.00 39.33           C  
ANISOU  742  CG  LEU A 137     5363   5216   4361     94    -66    134       C  
ATOM    743  CD1 LEU A 137     -29.971   2.582 -11.355  1.00 40.26           C  
ANISOU  743  CD1 LEU A 137     5371   5516   4409     55    -15    185       C  
ATOM    744  CD2 LEU A 137     -31.293   0.694 -12.208  1.00 40.59           C  
ANISOU  744  CD2 LEU A 137     5529   5266   4626     -3   -190    283       C  
ATOM    745  N   VAL A 138     -34.237   4.813 -14.472  1.00 37.14           N  
ANISOU  745  N   VAL A 138     4965   5074   4073    195    -34    -17       N  
ATOM    746  CA  VAL A 138     -35.419   5.666 -14.578  1.00 37.68           C  
ANISOU  746  CA  VAL A 138     4891   5212   4212    254    -35     -7       C  
ATOM    747  C   VAL A 138     -36.524   4.904 -15.299  1.00 39.33           C  
ANISOU  747  C   VAL A 138     5077   5549   4314    173   -128     77       C  
ATOM    748  O   VAL A 138     -37.666   4.883 -14.862  1.00 39.72           O  
ANISOU  748  O   VAL A 138     4986   5762   4343    142   -145     82       O  
ATOM    749  CB  VAL A 138     -35.125   6.986 -15.334  1.00 38.89           C  
ANISOU  749  CB  VAL A 138     5014   5225   4537    383    -20     61       C  
ATOM    750  CG1 VAL A 138     -36.409   7.603 -15.956  1.00 39.85           C  
ANISOU  750  CG1 VAL A 138     4974   5398   4766    465    -77    190       C  
ATOM    751  CG2 VAL A 138     -34.415   8.002 -14.454  1.00 36.75           C  
ANISOU  751  CG2 VAL A 138     4707   4809   4444    439     70    -79       C  
ATOM    752  N   LYS A 139     -36.178   4.265 -16.407  1.00 39.51           N  
ANISOU  752  N   LYS A 139     5394   4753   4863    112    234   -271       N  
ATOM    753  CA  LYS A 139     -37.149   3.473 -17.142  1.00 40.64           C  
ANISOU  753  CA  LYS A 139     5614   4953   4872    119    192   -213       C  
ATOM    754  C   LYS A 139     -37.762   2.387 -16.247  1.00 39.77           C  
ANISOU  754  C   LYS A 139     5486   4926   4698     90    161   -273       C  
ATOM    755  O   LYS A 139     -38.991   2.238 -16.178  1.00 40.19           O  
ANISOU  755  O   LYS A 139     5491   5090   4686     40     96   -272       O  
ATOM    756  CB  LYS A 139     -36.492   2.831 -18.373  1.00 41.71           C  
ANISOU  756  CB  LYS A 139     5909   5030   4906     54    310   -182       C  
ATOM    757  CG  LYS A 139     -37.454   2.381 -19.451  1.00 46.39           C  
ANISOU  757  CG  LYS A 139     6649   5740   5237   -108    256   -162       C  
ATOM    758  CD  LYS A 139     -36.860   1.210 -20.297  1.00 53.17           C  
ANISOU  758  CD  LYS A 139     7808   6463   5929   -272    508   -264       C  
ATOM    759  CE  LYS A 139     -37.411   1.209 -21.719  1.00 60.08           C  
ANISOU  759  CE  LYS A 139     8901   7500   6426   -555    465   -261       C  
ATOM    760  NZ  LYS A 139     -36.720   2.216 -22.622  1.00 64.69           N  
ANISOU  760  NZ  LYS A 139     9542   8048   6987   -473    515   -114       N  
ATOM    761  N   VAL A 140     -36.910   1.620 -15.577  1.00 39.43           N  
ANISOU  761  N   VAL A 140     5444   4859   4677    133    229   -264       N  
ATOM    762  CA  VAL A 140     -37.415   0.524 -14.752  1.00 40.66           C  
ANISOU  762  CA  VAL A 140     5657   5028   4764    130    273   -259       C  
ATOM    763  C   VAL A 140     -38.288   0.980 -13.579  1.00 40.98           C  
ANISOU  763  C   VAL A 140     5609   5187   4773    101    180   -323       C  
ATOM    764  O   VAL A 140     -39.361   0.419 -13.377  1.00 41.76           O  
ANISOU  764  O   VAL A 140     5744   5309   4814     19    219   -357       O  
ATOM    765  CB  VAL A 140     -36.290  -0.331 -14.181  1.00 42.51           C  
ANISOU  765  CB  VAL A 140     5874   5236   5040    294    388    -94       C  
ATOM    766  CG1 VAL A 140     -36.865  -1.355 -13.166  1.00 42.38           C  
ANISOU  766  CG1 VAL A 140     5965   5199   4937    323    467    -24       C  
ATOM    767  CG2 VAL A 140     -35.530  -1.027 -15.314  1.00 43.27           C  
ANISOU  767  CG2 VAL A 140     6112   5117   5210    375    656    -23       C  
ATOM    768  N   ALA A 141     -37.812   1.971 -12.807  1.00 41.60           N  
ANISOU  768  N   ALA A 141     5601   5336   4868    104    114   -371       N  
ATOM    769  CA  ALA A 141     -38.588   2.589 -11.710  1.00 43.36           C  
ANISOU  769  CA  ALA A 141     5834   5602   5039     47    143   -494       C  
ATOM    770  C   ALA A 141     -39.954   3.060 -12.164  1.00 44.64           C  
ANISOU  770  C   ALA A 141     5946   5701   5314    108    228   -507       C  
ATOM    771  O   ALA A 141     -40.925   2.903 -11.437  1.00 46.40           O  
ANISOU  771  O   ALA A 141     6141   5970   5518    103    324   -543       O  
ATOM    772  CB  ALA A 141     -37.840   3.759 -11.108  1.00 45.09           C  
ANISOU  772  CB  ALA A 141     6073   5836   5221    -85    145   -631       C  
ATOM    773  N   GLU A 142     -40.040   3.642 -13.357  1.00 45.42           N  
ANISOU  773  N   GLU A 142     5991   5744   5522    184    205   -420       N  
ATOM    774  CA  GLU A 142     -41.332   3.988 -13.920  1.00 49.11           C  
ANISOU  774  CA  GLU A 142     6285   6298   6074    292    221   -283       C  
ATOM    775  C   GLU A 142     -42.215   2.752 -14.111  1.00 49.78           C  
ANISOU  775  C   GLU A 142     6257   6622   6035    131    130   -254       C  
ATOM    776  O   GLU A 142     -43.405   2.793 -13.798  1.00 52.77           O  
ANISOU  776  O   GLU A 142     6407   7172   6472    154    176   -189       O  
ATOM    777  CB  GLU A 142     -41.169   4.740 -15.247  1.00 50.88           C  
ANISOU  777  CB  GLU A 142     6482   6498   6348    399    169    -97       C  
ATOM    778  CG  GLU A 142     -42.443   4.819 -16.100  1.00 59.41           C  
ANISOU  778  CG  GLU A 142     7280   7879   7412    490     56    183       C  
ATOM    779  CD  GLU A 142     -43.324   6.027 -15.773  1.00 70.13           C  
ANISOU  779  CD  GLU A 142     8437   9172   9036    853    266    412       C  
ATOM    780  OE1 GLU A 142     -42.800   7.169 -15.788  1.00 74.29           O  
ANISOU  780  OE1 GLU A 142     9154   9337   9733   1054    498    453       O  
ATOM    781  OE2 GLU A 142     -44.549   5.848 -15.529  1.00 76.22           O  
ANISOU  781  OE2 GLU A 142     8859  10227   9874    941    267    571       O  
ATOM    782  N   ALA A 143     -41.649   1.667 -14.633  1.00 48.85           N  
ANISOU  782  N   ALA A 143     6305   6490   5763    -55     76   -308       N  
ATOM    783  CA  ALA A 143     -42.452   0.485 -14.944  1.00 50.95           C  
ANISOU  783  CA  ALA A 143     6574   6907   5874   -342     73   -349       C  
ATOM    784  C   ALA A 143     -42.693  -0.304 -13.678  1.00 51.14           C  
ANISOU  784  C   ALA A 143     6685   6845   5901   -394    234   -433       C  
ATOM    785  O   ALA A 143     -43.739  -0.937 -13.527  1.00 53.74           O  
ANISOU  785  O   ALA A 143     6924   7323   6172   -629    289   -469       O  
ATOM    786  CB  ALA A 143     -41.764  -0.384 -15.998  1.00 51.37           C  
ANISOU  786  CB  ALA A 143     6915   6846   5755   -552    119   -420       C  
ATOM    787  N   ASN A 144     -41.730  -0.226 -12.760  1.00 49.33           N  
ANISOU  787  N   ASN A 144     6600   6438   5702   -213    299   -435       N  
ATOM    788  CA  ASN A 144     -41.725  -1.045 -11.552  1.00 50.83           C  
ANISOU  788  CA  ASN A 144     6936   6560   5816   -228    444   -429       C  
ATOM    789  C   ASN A 144     -41.622  -0.208 -10.272  1.00 50.16           C  
ANISOU  789  C   ASN A 144     6809   6544   5703   -114    441   -454       C  
ATOM    790  O   ASN A 144     -40.578  -0.227  -9.622  1.00 48.71           O  
ANISOU  790  O   ASN A 144     6718   6377   5411    -41    387   -391       O  
ATOM    791  CB  ASN A 144     -40.514  -1.953 -11.610  1.00 51.48           C  
ANISOU  791  CB  ASN A 144     7245   6454   5859   -131    531   -312       C  
ATOM    792  CG  ASN A 144     -40.872  -3.395 -11.549  1.00 57.18           C  
ANISOU  792  CG  ASN A 144     8237   6966   6522   -267    810   -285       C  
ATOM    793  OD1 ASN A 144     -40.495  -4.159 -12.453  1.00 61.34           O  
ANISOU  793  OD1 ASN A 144     8990   7254   7060   -333   1000   -297       O  
ATOM    794  ND2 ASN A 144     -41.610  -3.801 -10.500  1.00 60.74           N  
ANISOU  794  ND2 ASN A 144     8739   7441   6899   -346    928   -270       N  
ATOM    795  N   PRO A 145     -42.708   0.507  -9.892  1.00 50.01           N  
ANISOU  795  N   PRO A 145     6501   6756   5744   -104    288   -166       N  
ATOM    796  CA  PRO A 145     -42.621   1.488  -8.786  1.00 49.32           C  
ANISOU  796  CA  PRO A 145     6330   6589   5820     69    333   -179       C  
ATOM    797  C   PRO A 145     -42.417   0.878  -7.410  1.00 48.87           C  
ANISOU  797  C   PRO A 145     6397   6458   5713     31    451   -279       C  
ATOM    798  O   PRO A 145     -42.131   1.603  -6.453  1.00 48.61           O  
ANISOU  798  O   PRO A 145     6337   6377   5753    118    510   -324       O  
ATOM    799  CB  PRO A 145     -43.969   2.213  -8.830  1.00 51.04           C  
ANISOU  799  CB  PRO A 145     6264   6941   6188     97    296   -142       C  
ATOM    800  CG  PRO A 145     -44.648   1.760 -10.081  1.00 52.71           C  
ANISOU  800  CG  PRO A 145     6395   7334   6296    -59    175    -39       C  
ATOM    801  CD  PRO A 145     -44.070   0.434 -10.438  1.00 52.08           C  
ANISOU  801  CD  PRO A 145     6575   7229   5983   -241    221   -117       C  
ATOM    802  N   VAL A 146     -42.567  -0.439  -7.302  1.00 49.38           N  
ANISOU  802  N   VAL A 146     6605   6511   5644   -131    480   -305       N  
ATOM    803  CA  VAL A 146     -42.446  -1.071  -6.001  1.00 49.37           C  
ANISOU  803  CA  VAL A 146     6726   6455   5578   -218    550   -332       C  
ATOM    804  C   VAL A 146     -41.068  -1.726  -5.835  1.00 47.62           C  
ANISOU  804  C   VAL A 146     6718   6033   5342   -164    525   -274       C  
ATOM    805  O   VAL A 146     -40.797  -2.341  -4.821  1.00 47.89           O  
ANISOU  805  O   VAL A 146     6869   6000   5324   -243    533   -224       O  
ATOM    806  CB  VAL A 146     -43.640  -2.023  -5.724  1.00 51.71           C  
ANISOU  806  CB  VAL A 146     7021   6857   5766   -459    592   -365       C  
ATOM    807  CG1 VAL A 146     -43.299  -3.494  -6.069  1.00 52.79           C  
ANISOU  807  CG1 VAL A 146     7405   6827   5824   -599    573   -335       C  
ATOM    808  CG2 VAL A 146     -44.058  -1.893  -4.288  1.00 53.98           C  
ANISOU  808  CG2 VAL A 146     7271   7241   5996   -566    680   -410       C  
ATOM    809  N   ASN A 147     -40.193  -1.567  -6.828  1.00 45.91           N  
ANISOU  809  N   ASN A 147     6526   5740   5175    -39    487   -266       N  
ATOM    810  CA  ASN A 147     -38.840  -2.099  -6.728  1.00 44.14           C  
ANISOU  810  CA  ASN A 147     6434   5341   4993     54    475   -229       C  
ATOM    811  C   ASN A 147     -37.938  -1.101  -6.037  1.00 42.10           C  
ANISOU  811  C   ASN A 147     6124   5104   4765    181    450   -177       C  
ATOM    812  O   ASN A 147     -37.518  -0.100  -6.628  1.00 40.00           O  
ANISOU  812  O   ASN A 147     5774   4892   4533    278    436   -191       O  
ATOM    813  CB  ASN A 147     -38.277  -2.464  -8.094  1.00 44.42           C  
ANISOU  813  CB  ASN A 147     6501   5322   5052     90    489   -299       C  
ATOM    814  CG  ASN A 147     -36.891  -3.071  -8.006  1.00 46.16           C  
ANISOU  814  CG  ASN A 147     6803   5355   5379    221    503   -293       C  
ATOM    815  OD1 ASN A 147     -36.125  -2.784  -7.076  1.00 46.89           O  
ANISOU  815  OD1 ASN A 147     6882   5414   5519    322    457   -189       O  
ATOM    816  ND2 ASN A 147     -36.554  -3.922  -8.977  1.00 48.70           N  
ANISOU  816  ND2 ASN A 147     7188   5566   5748    207    575   -420       N  
ATOM    817  N   PHE A 148     -37.620  -1.413  -4.786  1.00 41.51           N  
ANISOU  817  N   PHE A 148     6113   5000   4658    135    434    -99       N  
ATOM    818  CA  PHE A 148     -36.886  -0.533  -3.895  1.00 39.67           C  
ANISOU  818  CA  PHE A 148     5840   4835   4396    168    416    -59       C  
ATOM    819  C   PHE A 148     -35.414  -0.360  -4.274  1.00 39.03           C  
ANISOU  819  C   PHE A 148     5750   4696   4383    320    362     -2       C  
ATOM    820  O   PHE A 148     -34.868   0.753  -4.245  1.00 38.01           O  
ANISOU  820  O   PHE A 148     5550   4643   4246    366    363    -25       O  
ATOM    821  CB  PHE A 148     -36.993  -1.048  -2.462  1.00 40.37           C  
ANISOU  821  CB  PHE A 148     6001   4968   4367     -4    394     34       C  
ATOM    822  CG  PHE A 148     -36.017  -0.411  -1.520  1.00 40.33           C  
ANISOU  822  CG  PHE A 148     5979   5054   4289    -29    351    103       C  
ATOM    823  CD1 PHE A 148     -36.349   0.760  -0.818  1.00 39.84           C  
ANISOU  823  CD1 PHE A 148     5848   5155   4134   -132    441    -30       C  
ATOM    824  CD2 PHE A 148     -34.751  -0.962  -1.345  1.00 40.32           C  
ANISOU  824  CD2 PHE A 148     6010   4977   4330     44    228    286       C  
ATOM    825  CE1 PHE A 148     -35.425   1.369   0.056  1.00 39.05           C  
ANISOU  825  CE1 PHE A 148     5745   5166   3924   -217    411      7       C  
ATOM    826  CE2 PHE A 148     -33.819  -0.375  -0.469  1.00 40.90           C  
ANISOU  826  CE2 PHE A 148     6046   5189   4305    -19    163    375       C  
ATOM    827  CZ  PHE A 148     -34.160   0.793   0.238  1.00 40.28           C  
ANISOU  827  CZ  PHE A 148     5931   5299   4071   -179    257    229       C  
ATOM    828  N   ASN A 149     -34.756  -1.459  -4.588  1.00 39.44           N  
ANISOU  828  N   ASN A 149     5861   4602   4522    390    326     62       N  
ATOM    829  CA  ASN A 149     -33.325  -1.421  -4.891  1.00 39.42           C  
ANISOU  829  CA  ASN A 149     5801   4564   4614    544    290    104       C  
ATOM    830  C   ASN A 149     -33.016  -0.585  -6.145  1.00 37.67           C  
ANISOU  830  C   ASN A 149     5496   4422   4395    612    347    -24       C  
ATOM    831  O   ASN A 149     -32.106   0.266  -6.154  1.00 37.93           O  
ANISOU  831  O   ASN A 149     5448   4552   4411    658    327     -6       O  
ATOM    832  CB  ASN A 149     -32.847  -2.860  -5.039  1.00 42.15           C  
ANISOU  832  CB  ASN A 149     6201   4684   5130    631    269    162       C  
ATOM    833  CG  ASN A 149     -31.384  -2.961  -5.318  1.00 42.92           C  
ANISOU  833  CG  ASN A 149     6184   4742   5381    818    246    192       C  
ATOM    834  OD1 ASN A 149     -30.573  -2.231  -4.758  1.00 43.37           O  
ANISOU  834  OD1 ASN A 149     6141   4947   5388    839    175    291       O  
ATOM    835  ND2 ASN A 149     -31.031  -3.883  -6.193  1.00 44.46           N  
ANISOU  835  ND2 ASN A 149     6376   4745   5769    938    326     80       N  
ATOM    836  N   VAL A 150     -33.790  -0.803  -7.198  1.00 36.91           N  
ANISOU  836  N   VAL A 150     5421   4313   4286    570    407   -136       N  
ATOM    837  CA  VAL A 150     -33.709   0.035  -8.390  1.00 36.24           C  
ANISOU  837  CA  VAL A 150     5268   4348   4151    557    430   -210       C  
ATOM    838  C   VAL A 150     -33.801   1.526  -8.036  1.00 35.08           C  
ANISOU  838  C   VAL A 150     5059   4304   3964    545    383   -150       C  
ATOM    839  O   VAL A 150     -32.959   2.353  -8.444  1.00 35.37           O  
ANISOU  839  O   VAL A 150     5044   4410   3984    563    368   -136       O  
ATOM    840  CB  VAL A 150     -34.835  -0.302  -9.346  1.00 36.58           C  
ANISOU  840  CB  VAL A 150     5337   4426   4136    439    460   -286       C  
ATOM    841  CG1 VAL A 150     -35.091   0.850 -10.297  1.00 37.00           C  
ANISOU  841  CG1 VAL A 150     5307   4641   4111    376    416   -261       C  
ATOM    842  CG2 VAL A 150     -34.488  -1.549 -10.136  1.00 39.43           C  
ANISOU  842  CG2 VAL A 150     5759   4694   4528    418    550   -422       C  
ATOM    843  N   ARG A 151     -34.802   1.880  -7.238  1.00 34.05           N  
ANISOU  843  N   ARG A 151     4932   4174   3832    499    378   -135       N  
ATOM    844  CA  ARG A 151     -34.962   3.287  -6.901  1.00 33.08           C  
ANISOU  844  CA  ARG A 151     4749   4083   3734    499    368   -129       C  
ATOM    845  C   ARG A 151     -33.789   3.769  -6.096  1.00 32.44           C  
ANISOU  845  C   ARG A 151     4680   4020   3625    506    361   -107       C  
ATOM    846  O   ARG A 151     -33.319   4.888  -6.339  1.00 32.70           O  
ANISOU  846  O   ARG A 151     4683   4064   3675    504    348   -103       O  
ATOM    847  CB  ARG A 151     -36.289   3.592  -6.186  1.00 32.51           C  
ANISOU  847  CB  ARG A 151     4635   4012   3704    457    411   -181       C  
ATOM    848  CG  ARG A 151     -36.433   5.023  -5.778  1.00 31.92           C  
ANISOU  848  CG  ARG A 151     4495   3906   3727    479    440   -226       C  
ATOM    849  CD  ARG A 151     -36.447   5.998  -6.981  1.00 31.98           C  
ANISOU  849  CD  ARG A 151     4438   3866   3845    540    363   -147       C  
ATOM    850  NE  ARG A 151     -37.643   5.860  -7.796  1.00 32.55           N  
ANISOU  850  NE  ARG A 151     4411   3966   3990    552    313    -95       N  
ATOM    851  CZ  ARG A 151     -38.056   6.742  -8.700  1.00 33.16           C  
ANISOU  851  CZ  ARG A 151     4392   4011   4196    587    214     23       C  
ATOM    852  NH1 ARG A 151     -39.170   6.503  -9.367  1.00 36.93           N  
ANISOU  852  NH1 ARG A 151     4750   4564   4717    573    145     98       N  
ATOM    853  NH2 ARG A 151     -37.383   7.857  -8.934  1.00 32.83           N  
ANISOU  853  NH2 ARG A 151     4368   3868   4239    613    165     95       N  
ATOM    854  N   PHE A 152     -33.319   2.943  -5.163  1.00 31.88           N  
ANISOU  854  N   PHE A 152     4649   3955   3506    487    350    -65       N  
ATOM    855  CA  PHE A 152     -32.238   3.347  -4.296  1.00 32.56           C  
ANISOU  855  CA  PHE A 152     4723   4115   3533    449    315    -12       C  
ATOM    856  C   PHE A 152     -30.976   3.504  -5.092  1.00 33.87           C  
ANISOU  856  C   PHE A 152     4825   4319   3722    527    282     20       C  
ATOM    857  O   PHE A 152     -30.244   4.470  -4.866  1.00 34.48           O  
ANISOU  857  O   PHE A 152     4870   4479   3751    471    269     24       O  
ATOM    858  CB  PHE A 152     -32.005   2.341  -3.167  1.00 34.58           C  
ANISOU  858  CB  PHE A 152     5016   4393   3729    389    259    100       C  
ATOM    859  CG  PHE A 152     -30.783   2.626  -2.351  1.00 34.72           C  
ANISOU  859  CG  PHE A 152     4988   4537   3665    329    180    206       C  
ATOM    860  CD1 PHE A 152     -30.763   3.693  -1.481  1.00 36.85           C  
ANISOU  860  CD1 PHE A 152     5267   4934   3799    153    213    141       C  
ATOM    861  CD2 PHE A 152     -29.660   1.825  -2.462  1.00 37.63           C  
ANISOU  861  CD2 PHE A 152     5283   4901   4111    438     81    356       C  
ATOM    862  CE1 PHE A 152     -29.638   3.971  -0.725  1.00 39.21           C  
ANISOU  862  CE1 PHE A 152     5519   5400   3979     38    131    241       C  
ATOM    863  CE2 PHE A 152     -28.533   2.077  -1.726  1.00 39.22           C  
ANISOU  863  CE2 PHE A 152     5398   5264   4239    374    -19    489       C  
ATOM    864  CZ  PHE A 152     -28.514   3.154  -0.845  1.00 40.96           C  
ANISOU  864  CZ  PHE A 152     5644   5658   4261    148     -4    442       C  
ATOM    865  N   ARG A 153     -30.699   2.584  -6.025  1.00 35.11           N  
ANISOU  865  N   ARG A 153     4959   4430   3948    627    291     13       N  
ATOM    866  CA  ARG A 153     -29.462   2.707  -6.840  1.00 36.74           C  
ANISOU  866  CA  ARG A 153     5068   4717   4174    683    299     -2       C  
ATOM    867  C   ARG A 153     -29.518   3.853  -7.828  1.00 36.20           C  
ANISOU  867  C   ARG A 153     4990   4724   4039    604    320    -49       C  
ATOM    868  O   ARG A 153     -28.476   4.406  -8.214  1.00 37.90           O  
ANISOU  868  O   ARG A 153     5130   5059   4210    571    319    -46       O  
ATOM    869  CB  ARG A 153     -29.184   1.448  -7.651  1.00 38.57           C  
ANISOU  869  CB  ARG A 153     5268   4873   4514    792    357    -71       C  
ATOM    870  CG  ARG A 153     -29.072   0.181  -6.847  1.00 42.84           C  
ANISOU  870  CG  ARG A 153     5822   5264   5190    891    318     10       C  
ATOM    871  CD  ARG A 153     -27.925   0.249  -5.866  1.00 47.22           C  
ANISOU  871  CD  ARG A 153     6263   5896   5780    940    215    170       C  
ATOM    872  NE  ARG A 153     -28.080  -0.811  -4.890  1.00 52.39           N  
ANISOU  872  NE  ARG A 153     6962   6407   6535    979    119    337       N  
ATOM    873  CZ  ARG A 153     -27.204  -1.084  -3.933  1.00 55.36           C  
ANISOU  873  CZ  ARG A 153     7238   6829   6964   1012    -21    554       C  
ATOM    874  NH1 ARG A 153     -26.090  -0.364  -3.817  1.00 55.40           N  
ANISOU  874  NH1 ARG A 153     7078   7046   6926   1014    -67    598       N  
ATOM    875  NH2 ARG A 153     -27.456  -2.083  -3.100  1.00 55.46           N  
ANISOU  875  NH2 ARG A 153     7314   6694   7065   1013   -135    753       N  
ATOM    876  N   LEU A 154     -30.720   4.176  -8.289  1.00 34.39           N  
ANISOU  876  N   LEU A 154     4820   4438   3807    559    324    -67       N  
ATOM    877  CA  LEU A 154     -30.899   5.356  -9.131  1.00 34.69           C  
ANISOU  877  CA  LEU A 154     4852   4514   3813    474    292    -34       C  
ATOM    878  C   LEU A 154     -30.499   6.603  -8.335  1.00 34.91           C  
ANISOU  878  C   LEU A 154     4893   4517   3854    426    267      1       C  
ATOM    879  O   LEU A 154     -29.804   7.472  -8.837  1.00 36.60           O  
ANISOU  879  O   LEU A 154     5095   4784   4025    341    240     43       O  
ATOM    880  CB  LEU A 154     -32.341   5.437  -9.634  1.00 33.41           C  
ANISOU  880  CB  LEU A 154     4708   4293   3692    454    265    -12       C  
ATOM    881  CG  LEU A 154     -32.816   6.727 -10.280  1.00 35.04           C  
ANISOU  881  CG  LEU A 154     4896   4475   3941    390    181     97       C  
ATOM    882  CD1 LEU A 154     -31.900   7.087 -11.432  1.00 34.50           C  
ANISOU  882  CD1 LEU A 154     4817   4545   3745    264    144    158       C  
ATOM    883  CD2 LEU A 154     -34.266   6.578 -10.754  1.00 34.28           C  
ANISOU  883  CD2 LEU A 154     4759   4359   3906    390    130    148       C  
ATOM    884  N   GLY A 155     -30.886   6.659  -7.071  1.00 34.71           N  
ANISOU  884  N   GLY A 155     4899   4427   3862    436    289    -32       N  
ATOM    885  CA  GLY A 155     -30.458   7.756  -6.208  1.00 35.77           C  
ANISOU  885  CA  GLY A 155     5058   4547   3983    344    301    -58       C  
ATOM    886  C   GLY A 155     -28.950   7.788  -6.088  1.00 36.81           C  
ANISOU  886  C   GLY A 155     5145   4836   4003    280    272    -18       C  
ATOM    887  O   GLY A 155     -28.329   8.841  -6.204  1.00 37.46           O  
ANISOU  887  O   GLY A 155     5240   4938   4054    167    263    -12       O  
ATOM    888  N   VAL A 156     -28.368   6.615  -5.872  1.00 37.01           N  
ANISOU  888  N   VAL A 156     5104   4961   3995    352    252     19       N  
ATOM    889  CA  VAL A 156     -26.934   6.480  -5.796  1.00 39.22           C  
ANISOU  889  CA  VAL A 156     5271   5415   4214    332    215     73       C  
ATOM    890  C   VAL A 156     -26.255   6.952  -7.086  1.00 40.62           C  
ANISOU  890  C   VAL A 156     5387   5680   4366    298    235     55       C  
ATOM    891  O   VAL A 156     -25.301   7.733  -7.023  1.00 42.31           O  
ANISOU  891  O   VAL A 156     5550   6029   4493    169    217     75       O  
ATOM    892  CB  VAL A 156     -26.527   5.026  -5.457  1.00 39.77           C  
ANISOU  892  CB  VAL A 156     5249   5510   4350    474    179    140       C  
ATOM    893  CG1 VAL A 156     -25.021   4.858  -5.538  1.00 42.21           C  
ANISOU  893  CG1 VAL A 156     5368   6006   4662    503    140    199       C  
ATOM    894  CG2 VAL A 156     -26.999   4.649  -4.031  1.00 40.57           C  
ANISOU  894  CG2 VAL A 156     5412   5590   4410    418    123    218       C  
ATOM    895  N   ALA A 157     -26.743   6.502  -8.241  1.00 40.85           N  
ANISOU  895  N   ALA A 157     5421   5668   4430    358    274     14       N  
ATOM    896  CA  ALA A 157     -26.143   6.890  -9.520  1.00 42.87           C  
ANISOU  896  CA  ALA A 157     5621   6062   4605    259    302     -5       C  
ATOM    897  C   ALA A 157     -26.193   8.404  -9.672  1.00 43.55           C  
ANISOU  897  C   ALA A 157     5794   6124   4628     75    247     70       C  
ATOM    898  O   ALA A 157     -25.227   9.021 -10.059  1.00 45.15           O  
ANISOU  898  O   ALA A 157     5946   6481   4727    -72    244     92       O  
ATOM    899  CB  ALA A 157     -26.875   6.232 -10.680  1.00 42.83           C  
ANISOU  899  CB  ALA A 157     5639   6037   4598    276    348    -65       C  
ATOM    900  N   LEU A 158     -27.346   8.984  -9.371  1.00 42.98           N  
ANISOU  900  N   LEU A 158     5843   5840   4647     86    211    107       N  
ATOM    901  CA  LEU A 158     -27.565  10.419  -9.450  1.00 43.96           C  
ANISOU  901  CA  LEU A 158     6060   5829   4811    -45    159    182       C  
ATOM    902  C   LEU A 158     -26.627  11.231  -8.559  1.00 46.15           C  
ANISOU  902  C   LEU A 158     6359   6135   5038   -177    172    153       C  
ATOM    903  O   LEU A 158     -26.087  12.247  -9.007  1.00 47.83           O  
ANISOU  903  O   LEU A 158     6616   6349   5206   -358    137    219       O  
ATOM    904  CB  LEU A 158     -29.023  10.718  -9.096  1.00 42.63           C  
ANISOU  904  CB  LEU A 158     5960   5405   4832     57    147    184       C  
ATOM    905  CG  LEU A 158     -30.084  11.074 -10.155  1.00 42.23           C  
ANISOU  905  CG  LEU A 158     5919   5239   4886     70     59    318       C  
ATOM    906  CD1 LEU A 158     -29.599  11.130 -11.600  1.00 41.69           C  
ANISOU  906  CD1 LEU A 158     5832   5347   4658    -88    -20    455       C  
ATOM    907  CD2 LEU A 158     -31.322  10.220 -10.040  1.00 37.43           C  
ANISOU  907  CD2 LEU A 158     5269   4586   4364    220     75    277       C  
ATOM    908  N   ASP A 159     -26.436  10.795  -7.310  1.00 47.06           N  
ANISOU  908  N   ASP A 159     6452   6292   5137   -135    211     71       N  
ATOM    909  CA  ASP A 159     -25.537  11.473  -6.343  1.00 50.33           C  
ANISOU  909  CA  ASP A 159     6875   6796   5451   -315    220     33       C  
ATOM    910  C   ASP A 159     -24.114  11.532  -6.911  1.00 52.30           C  
ANISOU  910  C   ASP A 159     7004   7317   5551   -440    188     93       C  
ATOM    911  O   ASP A 159     -23.465  12.585  -6.919  1.00 54.07           O  
ANISOU  911  O   ASP A 159     7273   7574   5696   -666    179    102       O  
ATOM    912  CB  ASP A 159     -25.556  10.746  -4.984  1.00 50.48           C  
ANISOU  912  CB  ASP A 159     6859   6901   5417   -285    233    -15       C  
ATOM    913  CG  ASP A 159     -24.548  11.318  -3.962  1.00 55.05           C  
ANISOU  913  CG  ASP A 159     7423   7664   5829   -528    222    -37       C  
ATOM    914  OD1 ASP A 159     -24.921  12.271  -3.228  1.00 57.31           O  
ANISOU  914  OD1 ASP A 159     7842   7823   6109   -699    290   -163       O  
ATOM    915  OD2 ASP A 159     -23.410  10.778  -3.847  1.00 58.33           O  
ANISOU  915  OD2 ASP A 159     7674   8357   6131   -554    152     55       O  
ATOM    916  N   ASN A 160     -23.655  10.387  -7.403  1.00 49.66           N  
ANISOU  916  N   ASN A 160     6813   6331   5721   -425     43    -92       N  
ATOM    917  CA  ASN A 160     -22.352  10.280  -8.032  1.00 51.72           C  
ANISOU  917  CA  ASN A 160     7021   6600   6027   -487    118   -113       C  
ATOM    918  C   ASN A 160     -22.195  11.192  -9.249  1.00 52.65           C  
ANISOU  918  C   ASN A 160     7227   6735   6040   -532    181    -98       C  
ATOM    919  O   ASN A 160     -21.103  11.687  -9.500  1.00 54.34           O  
ANISOU  919  O   ASN A 160     7429   6939   6278   -600    240    -89       O  
ATOM    920  CB  ASN A 160     -22.048   8.826  -8.366  1.00 52.51           C  
ANISOU  920  CB  ASN A 160     7007   6714   6229   -471    169   -177       C  
ATOM    921  CG  ASN A 160     -21.490   8.080  -7.181  1.00 55.23           C  
ANISOU  921  CG  ASN A 160     7230   7030   6725   -450    127   -142       C  
ATOM    922  OD1 ASN A 160     -20.393   8.384  -6.722  1.00 60.42           O  
ANISOU  922  OD1 ASN A 160     7823   7686   7447   -492    122   -105       O  
ATOM    923  ND2 ASN A 160     -22.239   7.108  -6.667  1.00 56.95           N  
ANISOU  923  ND2 ASN A 160     7405   7231   7000   -393     93   -139       N  
ATOM    924  N   LEU A 161     -23.285  11.437  -9.974  1.00 52.11           N  
ANISOU  924  N   LEU A 161     7239   6703   5855   -499    163    -76       N  
ATOM    925  CA  LEU A 161     -23.274  12.388 -11.085  1.00 52.88           C  
ANISOU  925  CA  LEU A 161     7428   6830   5834   -537    203    -12       C  
ATOM    926  C   LEU A 161     -23.377  13.855 -10.671  1.00 52.66           C  
ANISOU  926  C   LEU A 161     7487   6708   5810   -534    183     89       C  
ATOM    927  O   LEU A 161     -23.472  14.735 -11.540  1.00 54.21           O  
ANISOU  927  O   LEU A 161     7762   6907   5926   -553    212    183       O  
ATOM    928  CB  LEU A 161     -24.396  12.079 -12.068  1.00 53.46           C  
ANISOU  928  CB  LEU A 161     7535   7005   5771   -510    175     -4       C  
ATOM    929  CG  LEU A 161     -24.085  11.108 -13.196  1.00 54.81           C  
ANISOU  929  CG  LEU A 161     7666   7292   5867   -573    250   -105       C  
ATOM    930  CD1 LEU A 161     -23.113  10.058 -12.759  1.00 55.91           C  
ANISOU  930  CD1 LEU A 161     7695   7386   6160   -593    323   -224       C  
ATOM    931  CD2 LEU A 161     -25.372  10.490 -13.612  1.00 54.64           C  
ANISOU  931  CD2 LEU A 161     7641   7365   5754   -542    185   -139       C  
ATOM    932  N   GLY A 162     -23.366  14.122  -9.361  1.00 50.59           N  
ANISOU  932  N   GLY A 162     7213   6365   5642   -517    142     71       N  
ATOM    933  CA  GLY A 162     -23.419  15.490  -8.847  1.00 49.19           C  
ANISOU  933  CA  GLY A 162     7114   6075   5499   -529    147    124       C  
ATOM    934  C   GLY A 162     -24.801  16.084  -8.802  1.00 48.74           C  
ANISOU  934  C   GLY A 162     7123   5969   5426   -438    108    187       C  
ATOM    935  O   GLY A 162     -24.969  17.254  -8.449  1.00 49.33           O  
ANISOU  935  O   GLY A 162     7264   5921   5559   -435    134    228       O  
ATOM    936  N   ARG A 163     -25.797  15.270  -9.143  1.00 47.98           N  
ANISOU  936  N   ARG A 163     6996   5958   5272   -366     54    188       N  
ATOM    937  CA  ARG A 163     -27.193  15.693  -9.124  1.00 48.10           C  
ANISOU  937  CA  ARG A 163     7041   5949   5287   -269      7    254       C  
ATOM    938  C   ARG A 163     -27.809  15.408  -7.753  1.00 46.43           C  
ANISOU  938  C   ARG A 163     6796   5695   5147   -225    -21    175       C  
ATOM    939  O   ARG A 163     -28.718  14.560  -7.594  1.00 44.65           O  
ANISOU  939  O   ARG A 163     6518   5537   4907   -169    -70    147       O  
ATOM    940  CB  ARG A 163     -27.999  15.015 -10.241  1.00 48.83           C  
ANISOU  940  CB  ARG A 163     7104   6179   5267   -233    -42    294       C  
ATOM    941  CG  ARG A 163     -27.477  15.219 -11.655  1.00 52.33           C  
ANISOU  941  CG  ARG A 163     7582   6709   5589   -293    -12    370       C  
ATOM    942  CD  ARG A 163     -27.613  16.660 -12.136  1.00 59.40           C  
ANISOU  942  CD  ARG A 163     8556   7523   6487   -272      3    546       C  
ATOM    943  NE  ARG A 163     -28.993  17.160 -12.130  1.00 64.09           N  
ANISOU  943  NE  ARG A 163     9146   8095   7110   -158    -69    660       N  
ATOM    944  CZ  ARG A 163     -29.368  18.364 -12.579  1.00 69.08           C  
ANISOU  944  CZ  ARG A 163     9825   8645   7777   -108    -67    850       C  
ATOM    945  NH1 ARG A 163     -28.478  19.224 -13.087  1.00 71.04           N  
ANISOU  945  NH1 ARG A 163    10144   8822   8024   -171      7    950       N  
ATOM    946  NH2 ARG A 163     -30.644  18.721 -12.511  1.00 70.08           N  
ANISOU  946  NH2 ARG A 163     9915   8747   7962      9   -133    952       N  
ATOM    947  N   PHE A 164     -27.333  16.161  -6.769  1.00 46.47           N  
ANISOU  947  N   PHE A 164     6835   5597   5223   -265     17    134       N  
ATOM    948  CA  PHE A 164     -27.707  15.944  -5.375  1.00 45.62           C  
ANISOU  948  CA  PHE A 164     6705   5474   5152   -259      5     46       C  
ATOM    949  C   PHE A 164     -29.202  16.092  -5.105  1.00 45.74           C  
ANISOU  949  C   PHE A 164     6720   5462   5197   -154     -6     60       C  
ATOM    950  O   PHE A 164     -29.791  15.263  -4.394  1.00 45.12           O  
ANISOU  950  O   PHE A 164     6589   5444   5108   -131    -35      9       O  
ATOM    951  CB  PHE A 164     -26.870  16.825  -4.452  1.00 45.66           C  
ANISOU  951  CB  PHE A 164     6752   5396   5201   -352     54    -20       C  
ATOM    952  CG  PHE A 164     -25.398  16.658  -4.665  1.00 45.76           C  
ANISOU  952  CG  PHE A 164     6737   5448   5201   -458     59    -31       C  
ATOM    953  CD1 PHE A 164     -24.793  15.428  -4.457  1.00 43.62           C  
ANISOU  953  CD1 PHE A 164     6375   5295   4904   -485     11    -53       C  
ATOM    954  CD2 PHE A 164     -24.614  17.720  -5.105  1.00 47.58           C  
ANISOU  954  CD2 PHE A 164     7020   5586   5471   -528    123    -10       C  
ATOM    955  CE1 PHE A 164     -23.430  15.249  -4.665  1.00 43.89           C  
ANISOU  955  CE1 PHE A 164     6356   5364   4956   -571     21    -58       C  
ATOM    956  CE2 PHE A 164     -23.245  17.558  -5.321  1.00 46.06           C  
ANISOU  956  CE2 PHE A 164     6783   5437   5279   -630    136    -22       C  
ATOM    957  CZ  PHE A 164     -22.651  16.318  -5.103  1.00 46.54           C  
ANISOU  957  CZ  PHE A 164     6739   5626   5319   -648     83    -48       C  
ATOM    958  N   ASP A 165     -29.822  17.120  -5.660  1.00 46.74           N  
ANISOU  958  N   ASP A 165     6889   5492   5376    -89     21    144       N  
ATOM    959  CA  ASP A 165     -31.235  17.313  -5.402  1.00 47.33           C  
ANISOU  959  CA  ASP A 165     6938   5534   5512     19     16    165       C  
ATOM    960  C   ASP A 165     -32.074  16.242  -6.076  1.00 46.48           C  
ANISOU  960  C   ASP A 165     6751   5569   5338     77    -68    207       C  
ATOM    961  O   ASP A 165     -33.127  15.865  -5.558  1.00 46.65           O  
ANISOU  961  O   ASP A 165     6717   5614   5394    139    -82    177       O  
ATOM    962  CB  ASP A 165     -31.710  18.697  -5.833  0.89 49.64           C  
ANISOU  962  CB  ASP A 165     7273   5670   5918     91     68    270       C  
ATOM    963  CG  ASP A 165     -31.624  19.712  -4.716  0.34 51.57           C  
ANISOU  963  CG  ASP A 165     7569   5738   6288     67    179    169       C  
ATOM    964  OD1 ASP A 165     -32.025  19.377  -3.580  0.75 51.94           O  
ANISOU  964  OD1 ASP A 165     7593   5802   6336     56    204     38       O  
ATOM    965  OD2 ASP A 165     -31.167  20.847  -4.978  0.75 54.69           O  
ANISOU  965  OD2 ASP A 165     8027   5976   6777     47    252    215       O  
ATOM    966  N   GLU A 166     -31.611  15.757  -7.227  1.00 45.74           N  
ANISOU  966  N   GLU A 166     6650   5577   5149     44   -112    262       N  
ATOM    967  CA  GLU A 166     -32.296  14.680  -7.933  1.00 44.70           C  
ANISOU  967  CA  GLU A 166     6446   5596   4941     65   -186    266       C  
ATOM    968  C   GLU A 166     -32.158  13.371  -7.159  1.00 41.08           C  
ANISOU  968  C   GLU A 166     5931   5192   4482     24   -189    141       C  
ATOM    969  O   GLU A 166     -33.139  12.603  -7.050  1.00 40.01           O  
ANISOU  969  O   GLU A 166     5725   5121   4354     60   -227    113       O  
ATOM    970  CB  GLU A 166     -31.830  14.556  -9.393  1.00 46.34           C  
ANISOU  970  CB  GLU A 166     6668   5910   5027     18   -213    335       C  
ATOM    971  CG  GLU A 166     -32.743  15.329 -10.355  1.00 53.12           C  
ANISOU  971  CG  GLU A 166     7522   6805   5852     89   -270    501       C  
ATOM    972  CD  GLU A 166     -32.063  15.769 -11.641  1.00 61.02           C  
ANISOU  972  CD  GLU A 166     8578   7874   6730     31   -268    614       C  
ATOM    973  OE1 GLU A 166     -32.331  16.911 -12.062  1.00 66.56           O  
ANISOU  973  OE1 GLU A 166     9313   8511   7463     85   -274    789       O  
ATOM    974  OE2 GLU A 166     -31.279  14.995 -12.247  1.00 65.00           O  
ANISOU  974  OE2 GLU A 166     9088   8491   7117    -66   -251    536       O  
ATOM    975  N   ALA A 167     -30.973  13.145  -6.595  1.00 37.82           N  
ANISOU  975  N   ALA A 167     5541   4752   4078    -49   -151     81       N  
ATOM    976  CA  ALA A 167     -30.726  11.927  -5.808  1.00 35.71           C  
ANISOU  976  CA  ALA A 167     5212   4524   3830    -82   -155      3       C  
ATOM    977  C   ALA A 167     -31.611  11.906  -4.594  1.00 35.47           C  
ANISOU  977  C   ALA A 167     5163   4468   3843    -44   -152    -22       C  
ATOM    978  O   ALA A 167     -32.189  10.882  -4.279  1.00 35.43           O  
ANISOU  978  O   ALA A 167     5094   4512   3855    -33   -169    -48       O  
ATOM    979  CB  ALA A 167     -29.275  11.799  -5.388  1.00 33.96           C  
ANISOU  979  CB  ALA A 167     4995   4285   3621   -161   -128    -23       C  
ATOM    980  N   ILE A 168     -31.711  13.038  -3.903  1.00 36.38           N  
ANISOU  980  N   ILE A 168     5336   4502   3985    -34   -114    -25       N  
ATOM    981  CA  ILE A 168     -32.556  13.148  -2.710  1.00 36.22           C  
ANISOU  981  CA  ILE A 168     5305   4461   3995    -10    -83    -71       C  
ATOM    982  C   ILE A 168     -34.021  12.854  -3.073  1.00 37.35           C  
ANISOU  982  C   ILE A 168     5384   4630   4175     81   -102    -45       C  
ATOM    983  O   ILE A 168     -34.693  12.096  -2.382  1.00 37.43           O  
ANISOU  983  O   ILE A 168     5339   4686   4195     86    -98    -79       O  
ATOM    984  CB  ILE A 168     -32.410  14.534  -2.072  1.00 36.34           C  
ANISOU  984  CB  ILE A 168     5396   4365   4045    -24    -12   -108       C  
ATOM    985  CG1 ILE A 168     -31.009  14.675  -1.478  1.00 34.99           C  
ANISOU  985  CG1 ILE A 168     5265   4202   3826   -142     -4   -156       C  
ATOM    986  CG2 ILE A 168     -33.466  14.746  -1.032  1.00 35.75           C  
ANISOU  986  CG2 ILE A 168     5308   4268   4006      9     46   -171       C  
ATOM    987  CD1 ILE A 168     -30.645  16.106  -1.029  1.00 33.56           C  
ANISOU  987  CD1 ILE A 168     5166   3901   3684   -190     74   -217       C  
ATOM    988  N   ASP A 169     -34.520  13.414  -4.167  1.00 38.89           N  
ANISOU  988  N   ASP A 169     5575   4812   4388    146   -129     28       N  
ATOM    989  CA  ASP A 169     -35.898  13.089  -4.572  1.00 40.49           C  
ANISOU  989  CA  ASP A 169     5690   5071   4624    225   -170     62       C  
ATOM    990  C   ASP A 169     -36.135  11.579  -4.731  1.00 38.21           C  
ANISOU  990  C   ASP A 169     5323   4897   4296    185   -215     16       C  
ATOM    991  O   ASP A 169     -37.191  11.054  -4.311  1.00 38.31           O  
ANISOU  991  O   ASP A 169     5257   4943   4356    214   -215     -7       O  
ATOM    992  CB  ASP A 169     -36.293  13.832  -5.855  1.00 43.44           C  
ANISOU  992  CB  ASP A 169     6055   5453   4997    289   -222    183       C  
ATOM    993  CG  ASP A 169     -36.427  15.333  -5.635  1.00 50.47           C  
ANISOU  993  CG  ASP A 169     6993   6188   5992    358   -160    246       C  
ATOM    994  OD1 ASP A 169     -36.418  16.076  -6.647  1.00 58.41           O  
ANISOU  994  OD1 ASP A 169     8015   7177   7000    399   -194    380       O  
ATOM    995  OD2 ASP A 169     -36.537  15.766  -4.449  1.00 56.75           O  
ANISOU  995  OD2 ASP A 169     7812   6880   6868    363    -69    162       O  
ATOM    996  N   SER A 170     -35.161  10.893  -5.333  1.00 35.31           N  
ANISOU  996  N   SER A 170     4972   4576   3867    114   -237     -1       N  
ATOM    997  CA  SER A 170     -35.270   9.457  -5.554  1.00 33.87           C  
ANISOU  997  CA  SER A 170     4719   4468   3681     69   -256    -59       C  
ATOM    998  C   SER A 170     -35.186   8.685  -4.244  1.00 33.30           C  
ANISOU  998  C   SER A 170     4622   4365   3666     43   -214    -98       C  
ATOM    999  O   SER A 170     -35.993   7.764  -4.022  1.00 33.14           O  
ANISOU  999  O   SER A 170     4524   4375   3691     41   -214   -126       O  
ATOM   1000  CB  SER A 170     -34.243   8.953  -6.575  1.00 33.63           C  
ANISOU 1000  CB  SER A 170     4705   4479   3594      2   -261    -85       C  
ATOM   1001  OG  SER A 170     -34.817   8.988  -7.892  1.00 33.94           O  
ANISOU 1001  OG  SER A 170     4719   4619   3555      0   -314    -72       O  
ATOM   1002  N   PHE A 171     -34.244   9.078  -3.378  1.00 32.30           N  
ANISOU 1002  N   PHE A 171     4553   4188   3531     13   -182    -90       N  
ATOM   1003  CA  PHE A 171     -34.111   8.492  -2.053  1.00 33.09           C  
ANISOU 1003  CA  PHE A 171     4635   4287   3650    -19   -154    -94       C  
ATOM   1004  C   PHE A 171     -35.391   8.613  -1.269  1.00 34.13           C  
ANISOU 1004  C   PHE A 171     4739   4426   3801     16   -123   -106       C  
ATOM   1005  O   PHE A 171     -35.814   7.661  -0.623  1.00 34.06           O  
ANISOU 1005  O   PHE A 171     4674   4443   3821     -3   -106   -101       O  
ATOM   1006  CB  PHE A 171     -32.978   9.155  -1.279  1.00 33.21           C  
ANISOU 1006  CB  PHE A 171     4714   4281   3620    -69   -142    -86       C  
ATOM   1007  CG  PHE A 171     -31.618   8.757  -1.771  1.00 33.56           C  
ANISOU 1007  CG  PHE A 171     4752   4326   3671   -116   -163    -68       C  
ATOM   1008  CD1 PHE A 171     -31.358   7.438  -2.129  1.00 32.21           C  
ANISOU 1008  CD1 PHE A 171     4505   4167   3565   -125   -169    -58       C  
ATOM   1009  CD2 PHE A 171     -30.599   9.694  -1.881  1.00 33.17           C  
ANISOU 1009  CD2 PHE A 171     4762   4253   3588   -153   -160    -69       C  
ATOM   1010  CE1 PHE A 171     -30.091   7.064  -2.593  1.00 33.49           C  
ANISOU 1010  CE1 PHE A 171     4642   4318   3764   -159   -168    -49       C  
ATOM   1011  CE2 PHE A 171     -29.337   9.315  -2.332  1.00 33.13           C  
ANISOU 1011  CE2 PHE A 171     4729   4253   3604   -196   -169    -54       C  
ATOM   1012  CZ  PHE A 171     -29.084   8.003  -2.686  1.00 30.57           C  
ANISOU 1012  CZ  PHE A 171     4321   3941   3351   -193   -170    -44       C  
ATOM   1013  N   LYS A 172     -36.048   9.759  -1.364  1.00 35.07           N  
ANISOU 1013  N   LYS A 172     4886   4512   3926     73   -103   -114       N  
ATOM   1014  CA  LYS A 172     -37.272   9.921  -0.616  1.00 36.33           C  
ANISOU 1014  CA  LYS A 172     5005   4672   4127    113    -51   -138       C  
ATOM   1015  C   LYS A 172     -38.352   9.026  -1.176  1.00 37.05           C  
ANISOU 1015  C   LYS A 172     4987   4815   4273    143    -82   -131       C  
ATOM   1016  O   LYS A 172     -39.185   8.505  -0.422  1.00 37.87           O  
ANISOU 1016  O   LYS A 172     5031   4943   4413    139    -37   -149       O  
ATOM   1017  CB  LYS A 172     -37.692  11.387  -0.560  1.00 37.95           C  
ANISOU 1017  CB  LYS A 172     5250   4798   4370    176     -1   -152       C  
ATOM   1018  CG  LYS A 172     -36.903  12.152   0.536  1.00 39.79           C  
ANISOU 1018  CG  LYS A 172     5579   4985   4553    112     70   -212       C  
ATOM   1019  CD  LYS A 172     -36.876  13.667   0.301  1.00 43.40           C  
ANISOU 1019  CD  LYS A 172     6097   5318   5073    158    124   -229       C  
ATOM   1020  CE  LYS A 172     -36.420  14.429   1.550  1.00 44.46           C  
ANISOU 1020  CE  LYS A 172     6312   5410   5171     79    225   -340       C  
ATOM   1021  NZ  LYS A 172     -36.796  15.861   1.430  1.00 45.44           N  
ANISOU 1021  NZ  LYS A 172     6471   5375   5418    141    319   -379       N  
ATOM   1022  N   ILE A 173     -38.349   8.816  -2.495  1.00 35.59           N  
ANISOU 1022  N   ILE A 173     4772   4663   4085    156   -154   -112       N  
ATOM   1023  CA  ILE A 173     -39.322   7.894  -3.041  1.00 34.96           C  
ANISOU 1023  CA  ILE A 173     4582   4651   4047    155   -190   -130       C  
ATOM   1024  C   ILE A 173     -39.009   6.484  -2.514  1.00 34.60           C  
ANISOU 1024  C   ILE A 173     4507   4608   4031     78   -160   -163       C  
ATOM   1025  O   ILE A 173     -39.915   5.705  -2.256  1.00 35.34           O  
ANISOU 1025  O   ILE A 173     4512   4724   4189     63   -140   -184       O  
ATOM   1026  CB  ILE A 173     -39.378   7.942  -4.574  1.00 34.95           C  
ANISOU 1026  CB  ILE A 173     4556   4720   4001    158   -277   -117       C  
ATOM   1027  CG1 ILE A 173     -39.920   9.289  -5.055  1.00 34.82           C  
ANISOU 1027  CG1 ILE A 173     4541   4702   3985    249   -312    -37       C  
ATOM   1028  CG2 ILE A 173     -40.271   6.851  -5.084  1.00 34.85           C  
ANISOU 1028  CG2 ILE A 173     4426   4793   4020    119   -312   -170       C  
ATOM   1029  CD1 ILE A 173     -39.632   9.564  -6.568  1.00 34.96           C  
ANISOU 1029  CD1 ILE A 173     4571   4804   3908    239   -403     16       C  
ATOM   1030  N   ALA A 174     -37.730   6.169  -2.332  1.00 34.01           N  
ANISOU 1030  N   ALA A 174     4494   4498   3930     31   -151   -152       N  
ATOM   1031  CA  ALA A 174     -37.344   4.848  -1.819  1.00 34.60           C  
ANISOU 1031  CA  ALA A 174     4528   4549   4066    -26   -120   -147       C  
ATOM   1032  C   ALA A 174     -37.739   4.662  -0.363  1.00 36.04           C  
ANISOU 1032  C   ALA A 174     4702   4730   4259    -37    -66   -102       C  
ATOM   1033  O   ALA A 174     -38.205   3.591   0.012  1.00 37.61           O  
ANISOU 1033  O   ALA A 174     4833   4921   4536    -69    -33    -87       O  
ATOM   1034  CB  ALA A 174     -35.890   4.629  -1.969  1.00 33.91           C  
ANISOU 1034  CB  ALA A 174     4484   4427   3971    -59   -126   -127       C  
ATOM   1035  N   LEU A 175     -37.543   5.701   0.448  1.00 36.57           N  
ANISOU 1035  N   LEU A 175     4840   4806   4246    -25    -47    -86       N  
ATOM   1036  CA  LEU A 175     -37.977   5.723   1.831  1.00 37.60           C  
ANISOU 1036  CA  LEU A 175     4976   4967   4341    -51     16    -64       C  
ATOM   1037  C   LEU A 175     -39.483   5.484   1.920  1.00 38.34           C  
ANISOU 1037  C   LEU A 175     4986   5078   4502    -24     64    -94       C  
ATOM   1038  O   LEU A 175     -39.951   4.806   2.810  1.00 39.45           O  
ANISOU 1038  O   LEU A 175     5088   5244   4655    -64    122    -62       O  
ATOM   1039  CB  LEU A 175     -37.639   7.073   2.419  1.00 37.76           C  
ANISOU 1039  CB  LEU A 175     5088   4992   4267    -50     42    -97       C  
ATOM   1040  CG  LEU A 175     -37.340   7.088   3.901  1.00 42.85           C  
ANISOU 1040  CG  LEU A 175     5773   5700   4808   -126     90    -76       C  
ATOM   1041  CD1 LEU A 175     -36.163   6.132   4.308  1.00 42.57           C  
ANISOU 1041  CD1 LEU A 175     5730   5704   4739   -195     33     32       C  
ATOM   1042  CD2 LEU A 175     -37.071   8.560   4.262  1.00 45.96           C  
ANISOU 1042  CD2 LEU A 175     6258   6080   5124   -135    129   -162       C  
ATOM   1043  N   GLY A 176     -40.240   6.046   0.988  1.00 38.03           N  
ANISOU 1043  N   GLY A 176     4908   5034   4508     41     39   -141       N  
ATOM   1044  CA  GLY A 176     -41.674   5.829   0.947  1.00 38.96           C  
ANISOU 1044  CA  GLY A 176     4916   5178   4708     69     70   -168       C  
ATOM   1045  C   GLY A 176     -42.011   4.353   0.830  1.00 39.69           C  
ANISOU 1045  C   GLY A 176     4920   5281   4878      8     72   -161       C  
ATOM   1046  O   GLY A 176     -43.009   3.903   1.388  1.00 40.01           O  
ANISOU 1046  O   GLY A 176     4879   5342   4979     -8    135   -166       O  
ATOM   1047  N   LEU A 177     -41.178   3.590   0.110  1.00 37.80           N  
ANISOU 1047  N   LEU A 177     5079   4662   4621   -168   -243    175       N  
ATOM   1048  CA  LEU A 177     -41.389   2.131  -0.021  1.00 39.86           C  
ANISOU 1048  CA  LEU A 177     5353   4859   4931   -255   -138    247       C  
ATOM   1049  C   LEU A 177     -40.932   1.353   1.213  1.00 41.24           C  
ANISOU 1049  C   LEU A 177     5548   5090   5030   -315      8    395       C  
ATOM   1050  O   LEU A 177     -41.473   0.292   1.525  1.00 43.14           O  
ANISOU 1050  O   LEU A 177     5781   5304   5304   -416    124    429       O  
ATOM   1051  CB  LEU A 177     -40.628   1.540  -1.225  1.00 39.06           C  
ANISOU 1051  CB  LEU A 177     5383   4609   4849   -230   -179    320       C  
ATOM   1052  CG  LEU A 177     -40.950   1.961  -2.666  1.00 39.51           C  
ANISOU 1052  CG  LEU A 177     5483   4573   4955   -181   -317    211       C  
ATOM   1053  CD1 LEU A 177     -39.829   1.506  -3.682  1.00 36.23           C  
ANISOU 1053  CD1 LEU A 177     5214   4040   4512   -162   -331    302       C  
ATOM   1054  CD2 LEU A 177     -42.339   1.492  -3.086  1.00 35.74           C  
ANISOU 1054  CD2 LEU A 177     4902   4085   4591   -223   -335     65       C  
ATOM   1055  N   ARG A 178     -39.888   1.850   1.867  1.00 40.94           N  
ANISOU 1055  N   ARG A 178     5554   5117   4884   -255      1    483       N  
ATOM   1056  CA  ARG A 178     -39.255   1.150   2.990  1.00 42.95           C  
ANISOU 1056  CA  ARG A 178     5860   5419   5037   -273    103    637       C  
ATOM   1057  C   ARG A 178     -38.805   2.160   4.029  1.00 43.50           C  
ANISOU 1057  C   ARG A 178     5883   5649   4994   -223     87    625       C  
ATOM   1058  O   ARG A 178     -37.620   2.472   4.110  1.00 42.94           O  
ANISOU 1058  O   ARG A 178     5861   5596   4857   -143     38    682       O  
ATOM   1059  CB  ARG A 178     -38.023   0.380   2.521  1.00 42.25           C  
ANISOU 1059  CB  ARG A 178     5897   5220   4934   -215     86    771       C  
ATOM   1060  CG  ARG A 178     -38.348  -0.810   1.698  1.00 43.81           C  
ANISOU 1060  CG  ARG A 178     6155   5259   5230   -266    121    802       C  
ATOM   1061  CD  ARG A 178     -37.198  -1.734   1.711  1.00 46.54           C  
ANISOU 1061  CD  ARG A 178     6618   5520   5544   -206    130    943       C  
ATOM   1062  NE  ARG A 178     -37.379  -2.772   0.718  1.00 50.79           N  
ANISOU 1062  NE  ARG A 178     7214   5890   6193   -240    145    949       N  
ATOM   1063  CZ  ARG A 178     -36.425  -3.610   0.342  1.00 51.86           C  
ANISOU 1063  CZ  ARG A 178     7443   5918   6344   -177    132   1029       C  
ATOM   1064  NH1 ARG A 178     -35.213  -3.541   0.891  1.00 51.40           N  
ANISOU 1064  NH1 ARG A 178     7421   5909   6197    -68     95   1104       N  
ATOM   1065  NH2 ARG A 178     -36.702  -4.516  -0.586  1.00 54.31           N  
ANISOU 1065  NH2 ARG A 178     7794   6075   6763   -217    148   1009       N  
ATOM   1066  N   PRO A 179     -39.737   2.663   4.842  1.00 44.96           N  
ANISOU 1066  N   PRO A 179     5960   5963   5159   -274    133    528       N  
ATOM   1067  CA  PRO A 179     -39.372   3.741   5.752  1.00 46.10           C  
ANISOU 1067  CA  PRO A 179     6045   6261   5207   -224    107    482       C  
ATOM   1068  C   PRO A 179     -38.449   3.308   6.878  1.00 48.00           C  
ANISOU 1068  C   PRO A 179     6355   6589   5293   -202    164    630       C  
ATOM   1069  O   PRO A 179     -37.990   4.141   7.641  1.00 47.78           O  
ANISOU 1069  O   PRO A 179     6282   6697   5175   -153    137    593       O  
ATOM   1070  CB  PRO A 179     -40.722   4.198   6.322  1.00 47.25           C  
ANISOU 1070  CB  PRO A 179     6046   6526   5381   -294    157    322       C  
ATOM   1071  CG  PRO A 179     -41.762   3.602   5.364  1.00 48.07           C  
ANISOU 1071  CG  PRO A 179     6115   6518   5628   -357    164    244       C  
ATOM   1072  CD  PRO A 179     -41.162   2.324   4.918  1.00 45.86           C  
ANISOU 1072  CD  PRO A 179     5979   6097   5349   -384    211    422       C  
ATOM   1073  N   ASN A 180     -38.197   2.016   6.998  1.00 50.71           N  
ANISOU 1073  N   ASN A 180     6814   6851   5602   -229    232    789       N  
ATOM   1074  CA  ASN A 180     -37.371   1.550   8.081  1.00 54.33           C  
ANISOU 1074  CA  ASN A 180     7363   7381   5899   -184    263    934       C  
ATOM   1075  C   ASN A 180     -35.941   1.392   7.637  1.00 53.61           C  
ANISOU 1075  C   ASN A 180     7341   7229   5799    -55    162   1005       C  
ATOM   1076  O   ASN A 180     -35.149   0.834   8.361  1.00 55.69           O  
ANISOU 1076  O   ASN A 180     7693   7523   5944     15    155   1126       O  
ATOM   1077  CB  ASN A 180     -37.888   0.210   8.619  1.00 57.22           C  
ANISOU 1077  CB  ASN A 180     7852   7680   6210   -281    393   1076       C  
ATOM   1078  CG  ASN A 180     -38.837   0.373   9.799  1.00 62.09           C  
ANISOU 1078  CG  ASN A 180     8425   8448   6716   -400    522   1042       C  
ATOM   1079  OD1 ASN A 180     -38.965   1.463  10.360  1.00 65.96           O  
ANISOU 1079  OD1 ASN A 180     8792   9114   7155   -382    501    920       O  
ATOM   1080  ND2 ASN A 180     -39.507  -0.722  10.188  1.00 66.76           N  
ANISOU 1080  ND2 ASN A 180     9124   8970   7269   -535    670   1140       N  
ATOM   1081  N   GLU A 181     -35.610   1.871   6.447  1.00 53.52           N  
ANISOU 1081  N   GLU A 181     7295   7135   5905    -23     84    921       N  
ATOM   1082  CA  GLU A 181     -34.317   1.570   5.849  1.00 52.57           C  
ANISOU 1082  CA  GLU A 181     7229   6946   5799     71     15    964       C  
ATOM   1083  C   GLU A 181     -33.283   2.696   6.087  1.00 50.81           C  
ANISOU 1083  C   GLU A 181     6933   6851   5521    145    -57    874       C  
ATOM   1084  O   GLU A 181     -33.130   3.634   5.293  1.00 49.39           O  
ANISOU 1084  O   GLU A 181     6708   6649   5407    130    -99    759       O  
ATOM   1085  CB  GLU A 181     -34.507   1.213   4.370  1.00 51.99           C  
ANISOU 1085  CB  GLU A 181     7185   6698   5868     39     -2    933       C  
ATOM   1086  CG  GLU A 181     -33.350   0.474   3.761  1.00 54.87           C  
ANISOU 1086  CG  GLU A 181     7617   6972   6257    116    -38    986       C  
ATOM   1087  CD  GLU A 181     -33.490  -1.039   3.761  1.00 60.27           C  
ANISOU 1087  CD  GLU A 181     8410   7522   6967    118      5   1116       C  
ATOM   1088  OE1 GLU A 181     -34.622  -1.566   3.901  1.00 63.38           O  
ANISOU 1088  OE1 GLU A 181     8834   7855   7391     21     81   1154       O  
ATOM   1089  OE2 GLU A 181     -32.439  -1.707   3.587  1.00 62.63           O  
ANISOU 1089  OE2 GLU A 181     8760   7768   7266    215    -35   1163       O  
ATOM   1090  N   GLY A 182     -32.572   2.575   7.205  1.00 50.78           N  
ANISOU 1090  N   GLY A 182     6931   6975   5386    222    -71    926       N  
ATOM   1091  CA  GLY A 182     -31.596   3.561   7.656  1.00 49.21           C  
ANISOU 1091  CA  GLY A 182     6645   6926   5124    288   -131    826       C  
ATOM   1092  C   GLY A 182     -30.508   3.993   6.677  1.00 47.48           C  
ANISOU 1092  C   GLY A 182     6390   6667   4983    316   -183    729       C  
ATOM   1093  O   GLY A 182     -30.109   5.164   6.690  1.00 47.37           O  
ANISOU 1093  O   GLY A 182     6295   6735   4966    299   -204    597       O  
ATOM   1094  N   LYS A 183     -30.021   3.069   5.849  1.00 46.10           N  
ANISOU 1094  N   LYS A 183     6275   6365   4873    348   -192    780       N  
ATOM   1095  CA  LYS A 183     -29.134   3.411   4.748  1.00 44.97           C  
ANISOU 1095  CA  LYS A 183     6104   6172   4809    338   -210    675       C  
ATOM   1096  C   LYS A 183     -29.659   4.530   3.815  1.00 42.88           C  
ANISOU 1096  C   LYS A 183     5839   5839   4611    223   -191    574       C  
ATOM   1097  O   LYS A 183     -28.866   5.268   3.233  1.00 43.26           O  
ANISOU 1097  O   LYS A 183     5862   5895   4679    190   -192    462       O  
ATOM   1098  CB  LYS A 183     -28.713   2.174   3.951  1.00 45.01           C  
ANISOU 1098  CB  LYS A 183     6174   6044   4881    382   -214    735       C  
ATOM   1099  CG  LYS A 183     -29.767   1.593   3.030  1.00 45.87           C  
ANISOU 1099  CG  LYS A 183     6371   5976   5081    302   -174    797       C  
ATOM   1100  CD  LYS A 183     -29.165   0.429   2.244  1.00 47.96           C  
ANISOU 1100  CD  LYS A 183     6686   6119   5414    353   -181    826       C  
ATOM   1101  CE  LYS A 183     -30.151  -0.260   1.325  1.00 47.48           C  
ANISOU 1101  CE  LYS A 183     6708   5886   5447    278   -144    874       C  
ATOM   1102  NZ  LYS A 183     -29.396  -1.213   0.485  1.00 48.21           N  
ANISOU 1102  NZ  LYS A 183     6831   5875   5609    328   -153    862       N  
ATOM   1103  N   VAL A 184     -30.972   4.683   3.689  1.00 41.24           N  
ANISOU 1103  N   VAL A 184     5665   5566   4435    163   -176    601       N  
ATOM   1104  CA  VAL A 184     -31.514   5.663   2.754  1.00 38.65           C  
ANISOU 1104  CA  VAL A 184     5367   5150   4166     88   -190    512       C  
ATOM   1105  C   VAL A 184     -31.490   7.064   3.349  1.00 38.89           C  
ANISOU 1105  C   VAL A 184     5340   5277   4157     73   -209    405       C  
ATOM   1106  O   VAL A 184     -31.155   8.030   2.655  1.00 38.88           O  
ANISOU 1106  O   VAL A 184     5378   5218   4177     26   -223    315       O  
ATOM   1107  CB  VAL A 184     -32.946   5.339   2.395  1.00 38.84           C  
ANISOU 1107  CB  VAL A 184     5425   5081   4250     52   -190    543       C  
ATOM   1108  CG1 VAL A 184     -33.535   6.429   1.506  1.00 37.09           C  
ANISOU 1108  CG1 VAL A 184     5247   4771   4075     11   -241    443       C  
ATOM   1109  CG2 VAL A 184     -33.047   3.980   1.726  1.00 37.33           C  
ANISOU 1109  CG2 VAL A 184     5295   4773   4113     50   -166    631       C  
ATOM   1110  N   HIS A 185     -31.874   7.181   4.623  1.00 38.85           N  
ANISOU 1110  N   HIS A 185     5259   5410   4089    104   -203    412       N  
ATOM   1111  CA  HIS A 185     -31.650   8.405   5.404  1.00 38.56           C  
ANISOU 1111  CA  HIS A 185     5147   5498   4005    105   -219    299       C  
ATOM   1112  C   HIS A 185     -30.204   8.808   5.467  1.00 38.84           C  
ANISOU 1112  C   HIS A 185     5144   5605   4008    116   -222    227       C  
ATOM   1113  O   HIS A 185     -29.917   9.973   5.517  1.00 39.66           O  
ANISOU 1113  O   HIS A 185     5221   5731   4114     78   -229    106       O  
ATOM   1114  CB  HIS A 185     -32.118   8.262   6.838  1.00 39.46           C  
ANISOU 1114  CB  HIS A 185     5183   5779   4030    140   -202    321       C  
ATOM   1115  CG  HIS A 185     -33.589   8.407   7.010  1.00 38.65           C  
ANISOU 1115  CG  HIS A 185     5063   5662   3960    104   -186    303       C  
ATOM   1116  ND1 HIS A 185     -34.238   9.614   6.868  1.00 38.58           N  
ANISOU 1116  ND1 HIS A 185     5018   5635   4004     84   -224    167       N  
ATOM   1117  CD2 HIS A 185     -34.540   7.494   7.314  1.00 37.58           C  
ANISOU 1117  CD2 HIS A 185     4933   5526   3817     80   -135    384       C  
ATOM   1118  CE1 HIS A 185     -35.530   9.433   7.084  1.00 39.92           C  
ANISOU 1118  CE1 HIS A 185     5147   5814   4204     64   -206    147       C  
ATOM   1119  NE2 HIS A 185     -35.736   8.157   7.364  1.00 37.90           N  
ANISOU 1119  NE2 HIS A 185     4912   5576   3911     46   -139    275       N  
ATOM   1120  N   ARG A 186     -29.289   7.861   5.482  1.00 39.34           N  
ANISOU 1120  N   ARG A 186     5198   5702   4048    170   -218    282       N  
ATOM   1121  CA  ARG A 186     -27.865   8.212   5.436  1.00 40.57           C  
ANISOU 1121  CA  ARG A 186     5286   5936   4189    178   -219    172       C  
ATOM   1122  C   ARG A 186     -27.473   8.783   4.063  1.00 38.87           C  
ANISOU 1122  C   ARG A 186     5137   5580   4050     70   -183     91       C  
ATOM   1123  O   ARG A 186     -26.687   9.721   3.971  1.00 39.69           O  
ANISOU 1123  O   ARG A 186     5202   5724   4154      5   -157    -47       O  
ATOM   1124  CB  ARG A 186     -27.021   6.992   5.784  1.00 42.04           C  
ANISOU 1124  CB  ARG A 186     5440   6193   4339    291   -245    233       C  
ATOM   1125  CG  ARG A 186     -25.733   7.310   6.454  1.00 47.98           C  
ANISOU 1125  CG  ARG A 186     6064   7127   5040    353   -277    103       C  
ATOM   1126  CD  ARG A 186     -25.064   6.041   6.971  1.00 55.71           C  
ANISOU 1126  CD  ARG A 186     7024   8174   5967    512   -342    175       C  
ATOM   1127  NE  ARG A 186     -25.796   5.403   8.069  1.00 60.39           N  
ANISOU 1127  NE  ARG A 186     7680   8813   6453    599   -377    333       N  
ATOM   1128  CZ  ARG A 186     -25.735   5.796   9.343  1.00 64.45           C  
ANISOU 1128  CZ  ARG A 186     8137   9508   6841    659   -417    308       C  
ATOM   1129  NH1 ARG A 186     -25.000   6.847   9.692  1.00 65.99           N  
ANISOU 1129  NH1 ARG A 186     8196   9857   7020    647   -435    121       N  
ATOM   1130  NH2 ARG A 186     -26.421   5.142  10.278  1.00 66.63           N  
ANISOU 1130  NH2 ARG A 186     8501   9813   6999    716   -429    464       N  
ATOM   1131  N   ALA A 187     -28.059   8.236   2.999  1.00 34.97           N  
ANISOU 1131  N   ALA A 187     4755   4919   3612     38   -173    172       N  
ATOM   1132  CA  ALA A 187     -27.690   8.642   1.648  1.00 33.61           C  
ANISOU 1132  CA  ALA A 187     4678   4611   3481    -65   -135    113       C  
ATOM   1133  C   ALA A 187     -28.200  10.049   1.451  1.00 33.14           C  
ANISOU 1133  C   ALA A 187     4693   4478   3421   -146   -142     44       C  
ATOM   1134  O   ALA A 187     -27.526  10.891   0.843  1.00 33.30           O  
ANISOU 1134  O   ALA A 187     4771   4443   3435   -250    -96    -51       O  
ATOM   1135  CB  ALA A 187     -28.270   7.702   0.617  1.00 31.95           C  
ANISOU 1135  CB  ALA A 187     4570   4251   3316    -66   -137    211       C  
ATOM   1136  N   ILE A 188     -29.385  10.311   1.991  1.00 32.56           N  
ANISOU 1136  N   ILE A 188     4620   4399   3351   -103   -195     83       N  
ATOM   1137  CA  ILE A 188     -30.000  11.623   1.841  1.00 32.80           C  
ANISOU 1137  CA  ILE A 188     4726   4343   3393   -146   -230     11       C  
ATOM   1138  C   ILE A 188     -29.107  12.645   2.549  1.00 34.44           C  
ANISOU 1138  C   ILE A 188     4861   4653   3570   -188   -199   -116       C  
ATOM   1139  O   ILE A 188     -28.858  13.761   2.027  1.00 34.22           O  
ANISOU 1139  O   ILE A 188     4937   4514   3549   -279   -185   -201       O  
ATOM   1140  CB  ILE A 188     -31.389  11.647   2.491  1.00 32.66           C  
ANISOU 1140  CB  ILE A 188     4665   4349   3394    -74   -292     35       C  
ATOM   1141  CG1 ILE A 188     -32.393  10.928   1.609  1.00 31.18           C  
ANISOU 1141  CG1 ILE A 188     4559   4031   3254    -57   -329    114       C  
ATOM   1142  CG2 ILE A 188     -31.880  13.096   2.801  1.00 32.55           C  
ANISOU 1142  CG2 ILE A 188     4670   4303   3392    -81   -342    -79       C  
ATOM   1143  CD1 ILE A 188     -33.683  10.615   2.331  1.00 28.36           C  
ANISOU 1143  CD1 ILE A 188     4114   3739   2923      0   -360    125       C  
ATOM   1144  N   ALA A 189     -28.636  12.239   3.726  1.00 34.14           N  
ANISOU 1144  N   ALA A 189     4660   4818   3492   -123   -192   -131       N  
ATOM   1145  CA  ALA A 189     -27.795  13.079   4.539  1.00 36.37           C  
ANISOU 1145  CA  ALA A 189     4837   5238   3745   -146   -172   -270       C  
ATOM   1146  C   ALA A 189     -26.489  13.412   3.825  1.00 37.98           C  
ANISOU 1146  C   ALA A 189     5055   5414   3961   -256    -98   -375       C  
ATOM   1147  O   ALA A 189     -26.086  14.585   3.828  1.00 39.46           O  
ANISOU 1147  O   ALA A 189     5259   5576   4156   -354    -63   -508       O  
ATOM   1148  CB  ALA A 189     -27.515  12.423   5.911  1.00 35.95           C  
ANISOU 1148  CB  ALA A 189     4618   5420   3622    -34   -195   -256       C  
ATOM   1149  N   TYR A 190     -25.829  12.412   3.230  1.00 38.20           N  
ANISOU 1149  N   TYR A 190     5074   5446   3994   -249    -66   -335       N  
ATOM   1150  CA ATYR A 190     -24.615  12.653   2.447  0.46 39.68           C  
ANISOU 1150  CA ATYR A 190     5263   5615   4196   -372     23   -456       C  
ATOM   1151  CA BTYR A 190     -24.617  12.678   2.468  0.54 39.58           C  
ANISOU 1151  CA BTYR A 190     5250   5604   4184   -373     23   -458       C  
ATOM   1152  C   TYR A 190     -24.902  13.623   1.305  1.00 39.87           C  
ANISOU 1152  C   TYR A 190     5501   5414   4232   -531     77   -472       C  
ATOM   1153  O   TYR A 190     -24.145  14.559   1.071  1.00 41.56           O  
ANISOU 1153  O   TYR A 190     5740   5606   4443   -676    161   -610       O  
ATOM   1154  CB ATYR A 190     -24.019  11.351   1.890  0.46 39.84           C  
ANISOU 1154  CB ATYR A 190     5245   5658   4230   -326     41   -415       C  
ATOM   1155  CB BTYR A 190     -23.937  11.394   1.980  0.54 39.78           C  
ANISOU 1155  CB BTYR A 190     5223   5669   4222   -325     42   -429       C  
ATOM   1156  CG ATYR A 190     -23.390  10.442   2.932  0.46 41.85           C  
ANISOU 1156  CG ATYR A 190     5310   6123   4465   -169    -14   -430       C  
ATOM   1157  CG BTYR A 190     -22.522  11.619   1.484  0.54 42.08           C  
ANISOU 1157  CG BTYR A 190     5437   6022   4528   -440    143   -614       C  
ATOM   1158  CD1ATYR A 190     -22.702  10.967   4.019  0.46 43.06           C  
ANISOU 1158  CD1ATYR A 190     5300   6472   4586   -134    -34   -569       C  
ATOM   1159  CD1BTYR A 190     -21.657  12.496   2.151  0.54 44.83           C  
ANISOU 1159  CD1BTYR A 190     5648   6513   4872   -502    182   -807       C  
ATOM   1160  CD2ATYR A 190     -23.464   9.052   2.811  0.46 43.51           C  
ANISOU 1160  CD2ATYR A 190     5520   6326   4686    -47    -57   -312       C  
ATOM   1161  CD2BTYR A 190     -22.035  10.947   0.368  0.54 43.15           C  
ANISOU 1161  CD2BTYR A 190     5617   6090   4687   -496    208   -623       C  
ATOM   1162  CE1ATYR A 190     -22.128  10.144   4.965  0.46 45.05           C  
ANISOU 1162  CE1ATYR A 190     5403   6913   4799     32   -111   -580       C  
ATOM   1163  CE1BTYR A 190     -20.362  12.708   1.703  0.54 45.97           C  
ANISOU 1163  CE1BTYR A 190     5697   6730   5040   -629    292  -1012       C  
ATOM   1164  CE2ATYR A 190     -22.882   8.218   3.756  0.46 45.73           C  
ANISOU 1164  CE2ATYR A 190     5667   6772   4936    116   -129   -314       C  
ATOM   1165  CE2BTYR A 190     -20.736  11.157  -0.085  0.54 44.87           C  
ANISOU 1165  CE2BTYR A 190     5743   6384   4921   -619    320   -824       C  
ATOM   1166  CZ ATYR A 190     -22.218   8.777   4.830  0.46 46.88           C  
ANISOU 1166  CZ ATYR A 190     5662   7116   5032    162   -163   -445       C  
ATOM   1167  CZ BTYR A 190     -19.908  12.042   0.586  0.54 46.11           C  
ANISOU 1167  CZ BTYR A 190     5756   6683   5078   -691    365  -1022       C  
ATOM   1168  OH ATYR A 190     -21.637   7.965   5.778  0.46 51.60           O  
ANISOU 1168  OH ATYR A 190     6148   7878   5578    348   -259   -447       O  
ATOM   1169  OH BTYR A 190     -18.617  12.251   0.147  0.54 49.15           O  
ANISOU 1169  OH BTYR A 190     6025   7160   5489   -833    493  -1255       O  
ATOM   1170  N   SER A 191     -26.004  13.405   0.596  1.00 39.00           N  
ANISOU 1170  N   SER A 191     5556   5134   4128   -505     25   -334       N  
ATOM   1171  CA  SER A 191     -26.340  14.288  -0.491  1.00 39.75           C  
ANISOU 1171  CA  SER A 191     5889   5003   4211   -625     45   -332       C  
ATOM   1172  C   SER A 191     -26.464  15.711  -0.001  1.00 41.48           C  
ANISOU 1172  C   SER A 191     6156   5174   4429   -680     36   -426       C  
ATOM   1173  O   SER A 191     -25.860  16.612  -0.584  1.00 43.61           O  
ANISOU 1173  O   SER A 191     6560   5329   4678   -840    120   -509       O  
ATOM   1174  CB  SER A 191     -27.623  13.849  -1.198  1.00 38.96           C  
ANISOU 1174  CB  SER A 191     5937   4749   4117   -550    -46   -189       C  
ATOM   1175  OG  SER A 191     -27.406  12.646  -1.929  1.00 37.81           O  
ANISOU 1175  OG  SER A 191     5791   4600   3972   -540    -18   -121       O  
ATOM   1176  N   TYR A 192     -27.237  15.940   1.053  1.00 41.36           N  
ANISOU 1176  N   TYR A 192     6040   5238   4435   -562    -52   -423       N  
ATOM   1177  CA  TYR A 192     -27.352  17.288   1.576  1.00 43.02           C  
ANISOU 1177  CA  TYR A 192     6281   5406   4656   -602    -66   -533       C  
ATOM   1178  C   TYR A 192     -25.985  17.846   1.938  1.00 45.73           C  
ANISOU 1178  C   TYR A 192     6526   5854   4992   -732     46   -698       C  
ATOM   1179  O   TYR A 192     -25.665  18.994   1.632  1.00 47.68           O  
ANISOU 1179  O   TYR A 192     6906   5965   5244   -870    101   -793       O  
ATOM   1180  CB  TYR A 192     -28.228  17.316   2.824  1.00 41.85           C  
ANISOU 1180  CB  TYR A 192     5980   5394   4526   -456   -160   -540       C  
ATOM   1181  CG  TYR A 192     -29.702  17.389   2.541  1.00 39.91           C  
ANISOU 1181  CG  TYR A 192     5839   5013   4310   -358   -273   -462       C  
ATOM   1182  CD1 TYR A 192     -30.228  18.367   1.694  1.00 38.42           C  
ANISOU 1182  CD1 TYR A 192     5884   4574   4139   -390   -330   -474       C  
ATOM   1183  CD2 TYR A 192     -30.573  16.498   3.133  1.00 36.45           C  
ANISOU 1183  CD2 TYR A 192     5272   4698   3879   -234   -327   -390       C  
ATOM   1184  CE1 TYR A 192     -31.587  18.456   1.444  1.00 38.24           C  
ANISOU 1184  CE1 TYR A 192     5936   4442   4152   -274   -460   -437       C  
ATOM   1185  CE2 TYR A 192     -31.934  16.561   2.874  1.00 39.00           C  
ANISOU 1185  CE2 TYR A 192     5655   4919   4243   -151   -426   -360       C  
ATOM   1186  CZ  TYR A 192     -32.441  17.542   2.025  1.00 39.63           C  
ANISOU 1186  CZ  TYR A 192     5940   4766   4351   -158   -504   -393       C  
ATOM   1187  OH  TYR A 192     -33.818  17.607   1.807  1.00 39.59           O  
ANISOU 1187  OH  TYR A 192     5966   4679   4394    -47   -629   -396       O  
ATOM   1188  N   GLU A 193     -25.201  17.028   2.623  1.00 47.20           N  
ANISOU 1188  N   GLU A 193     6089   6150   5694    -61   -551      8       N  
ATOM   1189  CA  GLU A 193     -23.879  17.405   3.088  1.00 50.16           C  
ANISOU 1189  CA  GLU A 193     6352   6631   6074   -155   -541    -14       C  
ATOM   1190  C   GLU A 193     -23.028  17.897   1.899  1.00 52.20           C  
ANISOU 1190  C   GLU A 193     6636   6908   6287   -324   -431    -81       C  
ATOM   1191  O   GLU A 193     -22.398  18.955   1.971  1.00 53.19           O  
ANISOU 1191  O   GLU A 193     6824   7064   6319   -515   -407   -125       O  
ATOM   1192  CB  GLU A 193     -23.238  16.209   3.812  1.00 50.54           C  
ANISOU 1192  CB  GLU A 193     6204   6780   6216    -28   -575      4       C  
ATOM   1193  CG  GLU A 193     -21.889  16.461   4.465  1.00 56.47           C  
ANISOU 1193  CG  GLU A 193     6757   7715   6983    -78   -622    -30       C  
ATOM   1194  CD  GLU A 193     -21.517  15.404   5.505  1.00 62.26           C  
ANISOU 1194  CD  GLU A 193     7372   8510   7773    112   -748     21       C  
ATOM   1195  OE1 GLU A 193     -20.757  14.458   5.167  1.00 65.63           O  
ANISOU 1195  OE1 GLU A 193     7638   9002   8294    274   -742     -7       O  
ATOM   1196  OE2 GLU A 193     -21.977  15.524   6.667  1.00 63.71           O  
ANISOU 1196  OE2 GLU A 193     7656   8658   7892    109   -855     85       O  
ATOM   1197  N   GLN A 194     -23.056  17.155   0.791  1.00 53.42           N  
ANISOU 1197  N   GLN A 194     6791   7034   6473   -304   -342   -103       N  
ATOM   1198  CA  GLN A 194     -22.304  17.538  -0.406  1.00 55.55           C  
ANISOU 1198  CA  GLN A 194     7118   7314   6672   -509   -201   -188       C  
ATOM   1199  C   GLN A 194     -22.764  18.847  -1.046  1.00 56.07           C  
ANISOU 1199  C   GLN A 194     7534   7217   6551   -685   -217   -173       C  
ATOM   1200  O   GLN A 194     -22.034  19.439  -1.826  1.00 58.42           O  
ANISOU 1200  O   GLN A 194     7957   7509   6729   -939    -96   -249       O  
ATOM   1201  CB  GLN A 194     -22.315  16.413  -1.419  1.00 56.26           C  
ANISOU 1201  CB  GLN A 194     7173   7383   6818   -457    -89   -220       C  
ATOM   1202  CG  GLN A 194     -21.251  15.379  -1.179  1.00 59.06           C  
ANISOU 1202  CG  GLN A 194     7221   7895   7322   -341     -6   -300       C  
ATOM   1203  CD  GLN A 194     -21.500  14.115  -1.963  1.00 62.25           C  
ANISOU 1203  CD  GLN A 194     7654   8214   7782   -229     96   -316       C  
ATOM   1204  OE1 GLN A 194     -22.567  13.508  -1.856  1.00 60.94           O  
ANISOU 1204  OE1 GLN A 194     7629   7921   7605   -122     30   -227       O  
ATOM   1205  NE2 GLN A 194     -20.512  13.696  -2.751  1.00 65.98           N  
ANISOU 1205  NE2 GLN A 194     7994   8771   8303   -278    284   -457       N  
ATOM   1206  N   MET A 195     -23.959  19.306  -0.710  1.00 55.12           N  
ANISOU 1206  N   MET A 195     7590   6959   6390   -548   -361    -91       N  
ATOM   1207  CA  MET A 195     -24.403  20.622  -1.121  1.00 56.79           C  
ANISOU 1207  CA  MET A 195     8174   6981   6423   -627   -423    -69       C  
ATOM   1208  C   MET A 195     -24.193  21.691  -0.054  1.00 57.65           C  
ANISOU 1208  C   MET A 195     8376   7058   6471   -679   -461    -73       C  
ATOM   1209  O   MET A 195     -24.649  22.817  -0.221  1.00 59.28           O  
ANISOU 1209  O   MET A 195     8943   7056   6522   -689   -525    -52       O  
ATOM   1210  CB  MET A 195     -25.876  20.588  -1.461  1.00 56.47           C  
ANISOU 1210  CB  MET A 195     8263   6823   6370   -399   -578     -8       C  
ATOM   1211  CG  MET A 195     -26.223  19.895  -2.755  1.00 57.77           C  
ANISOU 1211  CG  MET A 195     8485   6965   6499   -416   -566      0       C  
ATOM   1212  SD  MET A 195     -27.990  20.113  -3.075  1.00 62.35           S  
ANISOU 1212  SD  MET A 195     9184   7472   7034   -148   -807     46       S  
ATOM   1213  CE  MET A 195     -28.701  19.101  -1.771  1.00 54.62           C  
ANISOU 1213  CE  MET A 195     7796   6697   6259     34   -810     14       C  
ATOM   1214  N   GLY A 196     -23.514  21.343   1.040  1.00 57.55           N  
ANISOU 1214  N   GLY A 196     8076   7230   6559   -700   -436   -100       N  
ATOM   1215  CA  GLY A 196     -23.333  22.254   2.169  1.00 57.87           C  
ANISOU 1215  CA  GLY A 196     8193   7261   6533   -775   -469   -109       C  
ATOM   1216  C   GLY A 196     -24.554  22.531   3.047  1.00 57.10           C  
ANISOU 1216  C   GLY A 196     8179   7051   6463   -544   -583    -65       C  
ATOM   1217  O   GLY A 196     -24.526  23.457   3.872  1.00 58.15           O  
ANISOU 1217  O   GLY A 196     8471   7115   6507   -613   -591    -83       O  
ATOM   1218  N   SER A 197     -25.620  21.733   2.903  1.00 55.12           N  
ANISOU 1218  N   SER A 197     7818   6802   6323   -301   -647    -35       N  
ATOM   1219  CA  SER A 197     -26.853  21.949   3.688  1.00 54.04           C  
ANISOU 1219  CA  SER A 197     7700   6613   6217    -95   -724    -46       C  
ATOM   1220  C   SER A 197     -26.826  21.112   4.950  1.00 51.99           C  
ANISOU 1220  C   SER A 197     7193   6508   6053    -83   -712    -50       C  
ATOM   1221  O   SER A 197     -27.656  20.223   5.156  1.00 50.95           O  
ANISOU 1221  O   SER A 197     6918   6441   5997     37   -725    -60       O  
ATOM   1222  CB  SER A 197     -28.093  21.618   2.856  1.00 54.50           C  
ANISOU 1222  CB  SER A 197     7758   6638   6310    115   -800    -51       C  
ATOM   1223  OG  SER A 197     -27.936  22.072   1.520  1.00 56.98           O  
ANISOU 1223  OG  SER A 197     8310   6821   6518     75   -829    -21       O  
ATOM   1224  N   HIS A 198     -25.840  21.399   5.788  1.00 51.41           N  
ANISOU 1224  N   HIS A 198     7099   6496   5938   -246   -692    -47       N  
ATOM   1225  CA  HIS A 198     -25.643  20.663   7.004  1.00 50.05           C  
ANISOU 1225  CA  HIS A 198     6758   6450   5809   -257   -717    -31       C  
ATOM   1226  C   HIS A 198     -26.850  20.717   7.911  1.00 49.63           C  
ANISOU 1226  C   HIS A 198     6752   6352   5753   -162   -718    -72       C  
ATOM   1227  O   HIS A 198     -27.182  19.715   8.536  1.00 48.60           O  
ANISOU 1227  O   HIS A 198     6515   6293   5657   -134   -723    -62       O  
ATOM   1228  CB  HIS A 198     -24.396  21.145   7.701  1.00 51.07           C  
ANISOU 1228  CB  HIS A 198     6865   6676   5862   -461   -730    -33       C  
ATOM   1229  CG  HIS A 198     -23.184  20.949   6.871  1.00 51.99           C  
ANISOU 1229  CG  HIS A 198     6842   6915   5995   -568   -703    -45       C  
ATOM   1230  ND1 HIS A 198     -22.653  19.700   6.641  1.00 52.04           N  
ANISOU 1230  ND1 HIS A 198     6595   7059   6117   -462   -728    -23       N  
ATOM   1231  CD2 HIS A 198     -22.440  21.820   6.152  1.00 52.83           C  
ANISOU 1231  CD2 HIS A 198     7045   7022   6005   -779   -628   -100       C  
ATOM   1232  CE1 HIS A 198     -21.609  19.812   5.841  1.00 53.67           C  
ANISOU 1232  CE1 HIS A 198     6683   7382   6326   -584   -664    -84       C  
ATOM   1233  NE2 HIS A 198     -21.452  21.088   5.537  1.00 54.98           N  
ANISOU 1233  NE2 HIS A 198     7057   7479   6351   -813   -594   -135       N  
ATOM   1234  N   GLU A 199     -27.529  21.856   7.964  1.00 50.30           N  
ANISOU 1234  N   GLU A 199     7020   6308   5781   -113   -699   -135       N  
ATOM   1235  CA  GLU A 199     -28.719  21.933   8.779  1.00 51.00           C  
ANISOU 1235  CA  GLU A 199     7103   6391   5883     -9   -668   -225       C  
ATOM   1236  C   GLU A 199     -29.739  20.864   8.343  1.00 49.60           C  
ANISOU 1236  C   GLU A 199     6734   6313   5797    122   -666   -261       C  
ATOM   1237  O   GLU A 199     -30.332  20.192   9.192  1.00 49.43           O  
ANISOU 1237  O   GLU A 199     6620   6382   5778     80   -612   -321       O  
ATOM   1238  CB  GLU A 199     -29.309  23.341   8.760  1.00 53.47           C  
ANISOU 1238  CB  GLU A 199     7644   6532   6138    103   -654   -309       C  
ATOM   1239  CG  GLU A 199     -30.773  23.353   9.156  1.00 56.94           C  
ANISOU 1239  CG  GLU A 199     7986   7007   6638    308   -619   -454       C  
ATOM   1240  CD  GLU A 199     -31.182  24.606   9.893  1.00 62.63           C  
ANISOU 1240  CD  GLU A 199     8920   7579   7296    383   -559   -569       C  
ATOM   1241  OE1 GLU A 199     -30.890  25.724   9.405  1.00 64.35           O  
ANISOU 1241  OE1 GLU A 199     9437   7578   7433    448   -595   -546       O  
ATOM   1242  OE2 GLU A 199     -31.824  24.458  10.961  1.00 66.50           O  
ANISOU 1242  OE2 GLU A 199     9315   8152   7796    360   -456   -696       O  
ATOM   1243  N   GLU A 200     -29.897  20.663   7.036  1.00 48.63           N  
ANISOU 1243  N   GLU A 200     6582   6180   5715    222   -712   -233       N  
ATOM   1244  CA  GLU A 200     -30.796  19.593   6.552  1.00 48.13           C  
ANISOU 1244  CA  GLU A 200     6343   6236   5708    287   -706   -273       C  
ATOM   1245  C   GLU A 200     -30.275  18.170   6.683  1.00 44.84           C  
ANISOU 1245  C   GLU A 200     5844   5886   5304    161   -664   -205       C  
ATOM   1246  O   GLU A 200     -31.050  17.246   6.875  1.00 44.16           O  
ANISOU 1246  O   GLU A 200     5675   5888   5215    127   -614   -262       O  
ATOM   1247  CB  GLU A 200     -31.286  19.856   5.137  1.00 49.51           C  
ANISOU 1247  CB  GLU A 200     6537   6382   5891    430   -788   -276       C  
ATOM   1248  CG  GLU A 200     -32.486  20.767   5.140  1.00 55.99           C  
ANISOU 1248  CG  GLU A 200     7353   7204   6716    655   -854   -400       C  
ATOM   1249  CD  GLU A 200     -32.655  21.477   3.828  1.00 63.45           C  
ANISOU 1249  CD  GLU A 200     8460   8031   7617    822   -998   -360       C  
ATOM   1250  OE1 GLU A 200     -33.764  21.402   3.241  1.00 65.28           O  
ANISOU 1250  OE1 GLU A 200     8561   8372   7869   1012  -1103   -444       O  
ATOM   1251  OE2 GLU A 200     -31.655  22.094   3.382  1.00 66.96           O  
ANISOU 1251  OE2 GLU A 200     9172   8286   7983    736  -1010   -255       O  
ATOM   1252  N   ALA A 201     -28.969  17.994   6.621  1.00 42.82           N  
ANISOU 1252  N   ALA A 201     5624   5593   5049     89   -681   -102       N  
ATOM   1253  CA  ALA A 201     -28.402  16.671   6.854  1.00 41.91           C  
ANISOU 1253  CA  ALA A 201     5465   5511   4948     44   -667    -39       C  
ATOM   1254  C   ALA A 201     -28.592  16.104   8.244  1.00 42.07           C  
ANISOU 1254  C   ALA A 201     5532   5547   4906    -29   -660    -41       C  
ATOM   1255  O   ALA A 201     -28.908  14.937   8.359  1.00 42.92           O  
ANISOU 1255  O   ALA A 201     5679   5644   4983    -56   -625    -32       O  
ATOM   1256  CB  ALA A 201     -26.957  16.631   6.504  1.00 41.64           C  
ANISOU 1256  CB  ALA A 201     5395   5481   4944     31   -697     33       C  
ATOM   1257  N   LEU A 202     -28.368  16.894   9.294  1.00 42.75           N  
ANISOU 1257  N   LEU A 202     5670   5633   4938    -96   -685    -51       N  
ATOM   1258  CA  LEU A 202     -28.282  16.337  10.669  1.00 42.95           C  
ANISOU 1258  CA  LEU A 202     5798   5656   4863   -205   -702    -28       C  
ATOM   1259  C   LEU A 202     -29.470  15.453  11.058  1.00 43.36           C  
ANISOU 1259  C   LEU A 202     5920   5709   4845   -288   -601   -107       C  
ATOM   1260  O   LEU A 202     -29.241  14.319  11.469  1.00 43.83           O  
ANISOU 1260  O   LEU A 202     6116   5712   4824   -341   -622    -40       O  
ATOM   1261  CB  LEU A 202     -28.037  17.420  11.721  1.00 43.60           C  
ANISOU 1261  CB  LEU A 202     5954   5741   4869   -311   -720    -53       C  
ATOM   1262  CG  LEU A 202     -27.959  17.028  13.210  1.00 44.68           C  
ANISOU 1262  CG  LEU A 202     6250   5869   4858   -469   -749    -32       C  
ATOM   1263  CD1 LEU A 202     -26.868  15.971  13.523  1.00 42.43           C  
ANISOU 1263  CD1 LEU A 202     6012   5580   4528   -437   -914    116       C  
ATOM   1264  CD2 LEU A 202     -27.786  18.300  14.059  1.00 41.36           C  
ANISOU 1264  CD2 LEU A 202     5908   5447   4357   -596   -736    -83       C  
ATOM   1265  N   PRO A 203     -30.726  15.934  10.885  1.00 43.23           N  
ANISOU 1265  N   PRO A 203     5818   5761   4846   -297   -492   -264       N  
ATOM   1266  CA  PRO A 203     -31.913  15.114  11.211  1.00 44.33           C  
ANISOU 1266  CA  PRO A 203     5968   5971   4903   -440   -359   -396       C  
ATOM   1267  C   PRO A 203     -31.915  13.781  10.513  1.00 43.99           C  
ANISOU 1267  C   PRO A 203     5981   5898   4834   -473   -345   -340       C  
ATOM   1268  O   PRO A 203     -32.346  12.780  11.107  1.00 45.30           O  
ANISOU 1268  O   PRO A 203     6319   6038   4852   -671   -254   -377       O  
ATOM   1269  CB  PRO A 203     -33.086  15.909  10.638  1.00 45.53           C  
ANISOU 1269  CB  PRO A 203     5897   6263   5138   -340   -297   -581       C  
ATOM   1270  CG  PRO A 203     -32.591  17.296  10.445  1.00 45.55           C  
ANISOU 1270  CG  PRO A 203     5887   6197   5222   -162   -385   -544       C  
ATOM   1271  CD  PRO A 203     -31.092  17.233  10.302  1.00 43.44           C  
ANISOU 1271  CD  PRO A 203     5737   5809   4957   -161   -497   -341       C  
ATOM   1272  N   HIS A 204     -31.456  13.771   9.257  1.00 42.38           N  
ANISOU 1272  N   HIS A 204     5684   5676   4742   -314   -411   -265       N  
ATOM   1273  CA  HIS A 204     -31.434  12.548   8.463  1.00 42.58           C  
ANISOU 1273  CA  HIS A 204     5781   5652   4743   -338   -377   -224       C  
ATOM   1274  C   HIS A 204     -30.388  11.625   9.009  1.00 44.55           C  
ANISOU 1274  C   HIS A 204     6261   5734   4929   -325   -432    -79       C  
ATOM   1275  O   HIS A 204     -30.586  10.427   9.033  1.00 45.04           O  
ANISOU 1275  O   HIS A 204     6534   5698   4880   -416   -369    -67       O  
ATOM   1276  CB  HIS A 204     -31.224  12.817   6.978  1.00 40.47           C  
ANISOU 1276  CB  HIS A 204     5381   5405   4591   -198   -417   -198       C  
ATOM   1277  CG  HIS A 204     -32.454  13.321   6.313  1.00 39.23           C  
ANISOU 1277  CG  HIS A 204     5049   5406   4451   -199   -394   -341       C  
ATOM   1278  ND1 HIS A 204     -33.546  12.513   6.063  1.00 36.43           N  
ANISOU 1278  ND1 HIS A 204     4656   5173   4013   -355   -299   -466       N  
ATOM   1279  CD2 HIS A 204     -32.794  14.559   5.896  1.00 37.82           C  
ANISOU 1279  CD2 HIS A 204     4732   5293   4343    -55   -472   -391       C  
ATOM   1280  CE1 HIS A 204     -34.504  13.235   5.523  1.00 37.72           C  
ANISOU 1280  CE1 HIS A 204     4595   5518   4216   -282   -340   -597       C  
ATOM   1281  NE2 HIS A 204     -34.069  14.475   5.397  1.00 39.92           N  
ANISOU 1281  NE2 HIS A 204     4837   5738   4590    -69   -456   -542       N  
ATOM   1282  N   PHE A 205     -29.283  12.173   9.489  1.00 40.82           N  
ANISOU 1282  N   PHE A 205     6225   5526   3757   -373   -632    395       N  
ATOM   1283  CA  PHE A 205     -28.311  11.317  10.125  1.00 43.14           C  
ANISOU 1283  CA  PHE A 205     6321   5954   4114   -594   -701    549       C  
ATOM   1284  C   PHE A 205     -28.838  10.730  11.432  1.00 45.33           C  
ANISOU 1284  C   PHE A 205     6556   6313   4353   -758   -748    545       C  
ATOM   1285  O   PHE A 205     -28.593   9.563  11.723  1.00 46.04           O  
ANISOU 1285  O   PHE A 205     6560   6447   4485   -771   -831    656       O  
ATOM   1286  CB  PHE A 205     -27.038  12.081  10.442  1.00 44.96           C  
ANISOU 1286  CB  PHE A 205     6577   6217   4288   -839   -652    591       C  
ATOM   1287  CG  PHE A 205     -26.044  12.025   9.375  1.00 45.83           C  
ANISOU 1287  CG  PHE A 205     6632   6282   4500   -806   -565    609       C  
ATOM   1288  CD1 PHE A 205     -25.483  10.817   9.019  1.00 46.50           C  
ANISOU 1288  CD1 PHE A 205     6448   6451   4767   -713   -670    695       C  
ATOM   1289  CD2 PHE A 205     -25.641  13.186   8.722  1.00 47.46           C  
ANISOU 1289  CD2 PHE A 205     7113   6307   4611   -892   -310    515       C  
ATOM   1290  CE1 PHE A 205     -24.537  10.762   7.999  1.00 49.92           C  
ANISOU 1290  CE1 PHE A 205     6811   6824   5331   -716   -519    658       C  
ATOM   1291  CE2 PHE A 205     -24.677  13.147   7.729  1.00 48.57           C  
ANISOU 1291  CE2 PHE A 205     7253   6359   4840   -944   -119    476       C  
ATOM   1292  CZ  PHE A 205     -24.125  11.937   7.355  1.00 48.86           C  
ANISOU 1292  CZ  PHE A 205     6945   6515   5102   -862   -223    532       C  
ATOM   1293  N   LYS A 206     -29.517  11.545  12.231  1.00 47.79           N  
ANISOU 1293  N   LYS A 206     7007   6591   4557   -891   -653    416       N  
ATOM   1294  CA  LYS A 206     -30.097  11.076  13.476  1.00 51.19           C  
ANISOU 1294  CA  LYS A 206     7507   7035   4907  -1106   -602    369       C  
ATOM   1295  C   LYS A 206     -31.118   9.975  13.228  1.00 52.63           C  
ANISOU 1295  C   LYS A 206     7583   7188   5226  -1013   -514    234       C  
ATOM   1296  O   LYS A 206     -31.047   8.902  13.842  1.00 52.88           O  
ANISOU 1296  O   LYS A 206     7708   7186   5197  -1147   -488    321       O  
ATOM   1297  CB  LYS A 206     -30.718  12.239  14.241  1.00 52.58           C  
ANISOU 1297  CB  LYS A 206     7847   7150   4980  -1271   -438    193       C  
ATOM   1298  CG  LYS A 206     -29.707  12.963  15.153  1.00 55.58           C  
ANISOU 1298  CG  LYS A 206     8396   7577   5143  -1570   -482    302       C  
ATOM   1299  CD  LYS A 206     -30.209  14.364  15.471  1.00 59.21           C  
ANISOU 1299  CD  LYS A 206     9038   7925   5532  -1672   -266    120       C  
ATOM   1300  CE  LYS A 206     -29.551  14.972  16.684  1.00 61.99           C  
ANISOU 1300  CE  LYS A 206     9590   8325   5638  -2073   -246    137       C  
ATOM   1301  NZ  LYS A 206     -29.864  16.434  16.705  1.00 62.93           N  
ANISOU 1301  NZ  LYS A 206     9910   8288   5713  -2142     12    -30       N  
ATOM   1302  N   LYS A 207     -32.035  10.230  12.286  1.00 54.29           N  
ANISOU 1302  N   LYS A 207     7634   7397   5597   -765   -476     -4       N  
ATOM   1303  CA  LYS A 207     -33.031   9.240  11.909  1.00 56.53           C  
ANISOU 1303  CA  LYS A 207     7721   7706   6052   -698   -388   -247       C  
ATOM   1304  C   LYS A 207     -32.291   7.972  11.459  1.00 56.21           C  
ANISOU 1304  C   LYS A 207     7671   7655   6032   -679   -449    -17       C  
ATOM   1305  O   LYS A 207     -32.654   6.878  11.876  1.00 57.56           O  
ANISOU 1305  O   LYS A 207     7880   7767   6223   -841   -286    -77       O  
ATOM   1306  CB  LYS A 207     -33.976   9.793  10.843  1.00 57.58           C  
ANISOU 1306  CB  LYS A 207     7645   7899   6334   -342   -474   -562       C  
ATOM   1307  CG  LYS A 207     -35.474   9.624  11.150  1.00 63.61           C  
ANISOU 1307  CG  LYS A 207     8133   8737   7298   -375   -311  -1076       C  
ATOM   1308  CD  LYS A 207     -36.293  10.907  10.800  1.00 68.53           C  
ANISOU 1308  CD  LYS A 207     8649   9391   7996    -15   -436  -1379       C  
ATOM   1309  CE  LYS A 207     -36.144  12.012  11.895  1.00 70.49           C  
ANISOU 1309  CE  LYS A 207     9144   9512   8126   -204   -275  -1308       C  
ATOM   1310  NZ  LYS A 207     -36.460  13.416  11.442  1.00 71.04           N  
ANISOU 1310  NZ  LYS A 207     9324   9502   8166    211   -415  -1408       N  
ATOM   1311  N   ALA A 208     -31.221   8.110  10.670  1.00 55.25           N  
ANISOU 1311  N   ALA A 208     7547   7545   5899   -511   -620    226       N  
ATOM   1312  CA  ALA A 208     -30.470   6.924  10.244  1.00 56.59           C  
ANISOU 1312  CA  ALA A 208     7682   7688   6129   -463   -659    421       C  
ATOM   1313  C   ALA A 208     -29.967   6.128  11.459  1.00 59.68           C  
ANISOU 1313  C   ALA A 208     8255   8016   6401   -649   -651    617       C  
ATOM   1314  O   ALA A 208     -30.238   4.934  11.568  1.00 61.06           O  
ANISOU 1314  O   ALA A 208     8524   8083   6593   -680   -528    622       O  
ATOM   1315  CB  ALA A 208     -29.313   7.277   9.265  1.00 54.57           C  
ANISOU 1315  CB  ALA A 208     7378   7442   5912   -304   -774    593       C  
ATOM   1316  N   ASN A 209     -29.281   6.799  12.379  1.00 62.12           N  
ANISOU 1316  N   ASN A 209     8683   8368   6549   -770   -777    753       N  
ATOM   1317  CA  ASN A 209     -28.816   6.176  13.615  1.00 67.46           C  
ANISOU 1317  CA  ASN A 209     9633   8984   7014   -890   -862    935       C  
ATOM   1318  C   ASN A 209     -29.874   5.428  14.418  1.00 72.69           C  
ANISOU 1318  C   ASN A 209    10625   9455   7538  -1091   -590    827       C  
ATOM   1319  O   ASN A 209     -29.626   4.319  14.893  1.00 75.04           O  
ANISOU 1319  O   ASN A 209    11239   9581   7691  -1076   -578    992       O  
ATOM   1320  CB  ASN A 209     -28.191   7.224  14.526  1.00 67.57           C  
ANISOU 1320  CB  ASN A 209     9725   9111   6837  -1043  -1032    984       C  
ATOM   1321  CG  ASN A 209     -26.888   7.733  14.002  1.00 65.73           C  
ANISOU 1321  CG  ASN A 209     9209   9048   6715   -932  -1261   1060       C  
ATOM   1322  OD1 ASN A 209     -26.156   7.021  13.299  1.00 62.26           O  
ANISOU 1322  OD1 ASN A 209     8574   8631   6449   -719  -1367   1155       O  
ATOM   1323  ND2 ASN A 209     -26.576   8.979  14.336  1.00 65.21           N  
ANISOU 1323  ND2 ASN A 209     9117   9087   6570  -1112  -1277    968       N  
ATOM   1324  N   GLU A 210     -31.031   6.059  14.596  1.00 76.80           N  
ANISOU 1324  N   GLU A 210    11111   9973   8097  -1278   -339    522       N  
ATOM   1325  CA  GLU A 210     -32.146   5.454  15.313  1.00 84.22           C  
ANISOU 1325  CA  GLU A 210    12306  10728   8966  -1562     46    284       C  
ATOM   1326  C   GLU A 210     -32.609   4.138  14.660  1.00 88.22           C  
ANISOU 1326  C   GLU A 210    12786  11113   9619  -1534    270    173       C  
ATOM   1327  O   GLU A 210     -32.851   3.162  15.354  1.00 91.75           O  
ANISOU 1327  O   GLU A 210    13671  11299   9888  -1745    551    181       O  
ATOM   1328  CB  GLU A 210     -33.298   6.462  15.442  1.00 84.18           C  
ANISOU 1328  CB  GLU A 210    12098  10794   9093  -1714    269   -125       C  
ATOM   1329  CG  GLU A 210     -34.631   5.881  15.933  1.00 90.18           C  
ANISOU 1329  CG  GLU A 210    12936  11405   9923  -2043    771   -560       C  
ATOM   1330  CD  GLU A 210     -35.780   6.897  15.919  1.00 93.78           C  
ANISOU 1330  CD  GLU A 210    13032  11979  10619  -2097    950  -1055       C  
ATOM   1331  OE1 GLU A 210     -35.534   8.101  16.173  1.00 93.18           O  
ANISOU 1331  OE1 GLU A 210    12948  11973  10483  -2024    789   -980       O  
ATOM   1332  OE2 GLU A 210     -36.935   6.484  15.655  1.00 97.15           O  
ANISOU 1332  OE2 GLU A 210    13168  12430  11315  -2209   1266  -1567       O  
ATOM   1333  N   LEU A 211     -32.705   4.104  13.336  1.00117.18           N  
ANISOU 1333  N   LEU A 211    21803  10741  11977  -1811   -319   2295       N  
ATOM   1334  CA  LEU A 211     -33.225   2.920  12.652  1.00121.69           C  
ANISOU 1334  CA  LEU A 211    22451  11401  12385  -1969    121   2183       C  
ATOM   1335  C   LEU A 211     -32.236   1.751  12.631  1.00129.65           C  
ANISOU 1335  C   LEU A 211    23056  11806  14398  -1964    575   2125       C  
ATOM   1336  O   LEU A 211     -32.639   0.596  12.484  1.00130.51           O  
ANISOU 1336  O   LEU A 211    23362  11895  14328  -2066    888   2034       O  
ATOM   1337  CB  LEU A 211     -33.728   3.276  11.252  1.00123.14           C  
ANISOU 1337  CB  LEU A 211    23264  11592  11931  -2487    348   2159       C  
ATOM   1338  CG  LEU A 211     -34.871   4.300  11.261  1.00122.64           C  
ANISOU 1338  CG  LEU A 211    23033  11791  11773  -2532   -369   2628       C  
ATOM   1339  CD1 LEU A 211     -34.994   5.017   9.930  1.00127.59           C  
ANISOU 1339  CD1 LEU A 211    24432  12148  11896  -3298   -780   2833       C  
ATOM   1340  CD2 LEU A 211     -36.197   3.663  11.647  1.00124.57           C  
ANISOU 1340  CD2 LEU A 211    22879  11990  12460  -2520   -757   3142       C  
ATOM   1341  N   ASP A 212     -30.950   2.057  12.793  1.00140.12           N  
ANISOU 1341  N   ASP A 212    23597  12392  17249  -1865    596   2358       N  
ATOM   1342  CA  ASP A 212     -29.935   1.031  13.025  1.00153.84           C  
ANISOU 1342  CA  ASP A 212    24260  13040  21151  -1804    848   2751       C  
ATOM   1343  C   ASP A 212     -30.063   0.490  14.462  1.00157.54           C  
ANISOU 1343  C   ASP A 212    24693  13531  21631  -1912  -1015   3280       C  
ATOM   1344  O   ASP A 212     -29.660  -0.642  14.742  1.00164.31           O  
ANISOU 1344  O   ASP A 212    24818  13687  23923  -1940  -1148   3666       O  
ATOM   1345  CB  ASP A 212     -28.524   1.574  12.750  1.00165.74           C  
ANISOU 1345  CB  ASP A 212    24448  13214  25311  -1737   1317   3259       C  
ATOM   1346  CG  ASP A 212     -28.361   2.131  11.330  1.00168.85           C  
ANISOU 1346  CG  ASP A 212    25505  13236  25413  -1808   3586   2632       C  
ATOM   1347  OD1 ASP A 212     -28.787   1.474  10.356  1.00171.03           O  
ANISOU 1347  OD1 ASP A 212    27122  13276  24586  -2120   5378   2000       O  
ATOM   1348  OD2 ASP A 212     -27.786   3.231  11.189  1.00171.54           O  
ANISOU 1348  OD2 ASP A 212    25427  13300  26447  -1757   3505   2812       O  
ATOM   1349  N   GLU A 213     -30.627   1.302  15.363  1.00157.63           N  
ANISOU 1349  N   GLU A 213    25849  14040  20003  -2116  -2222   3307       N  
ATOM   1350  CA  GLU A 213     -31.061   0.837  16.693  1.00164.13           C  
ANISOU 1350  CA  GLU A 213    27906  14665  19790  -2530  -3464   3557       C  
ATOM   1351  C   GLU A 213     -32.279  -0.070  16.568  1.00158.14           C  
ANISOU 1351  C   GLU A 213    27520  14635  17931  -2239  -2379   3028       C  
ATOM   1352  O   GLU A 213     -32.314  -1.150  17.152  1.00161.49           O  
ANISOU 1352  O   GLU A 213    28111  14761  18487  -2410  -2860   3220       O  
ATOM   1353  CB  GLU A 213     -31.419   2.008  17.613  1.00167.90           C  
ANISOU 1353  CB  GLU A 213    30326  14937  18530  -3006  -4092   3549       C  
ATOM   1354  CG  GLU A 213     -30.498   2.204  18.794  1.00187.55           C  
ANISOU 1354  CG  GLU A 213    34142  16028  21087  -4114  -6518   4454       C  
ATOM   1355  CD  GLU A 213     -29.247   2.971  18.438  1.00197.28           C  
ANISOU 1355  CD  GLU A 213    34050  16630  24277  -4289  -7765   5195       C  
ATOM   1356  OE1 GLU A 213     -28.161   2.359  18.459  1.00213.63           O  
ANISOU 1356  OE1 GLU A 213    34453  17613  29102  -4568  -9279   6278       O  
ATOM   1357  OE2 GLU A 213     -29.347   4.179  18.126  1.00193.16           O  
ANISOU 1357  OE2 GLU A 213    33891  16485  23013  -4126  -7146   4834       O  
ATOM   1358  N   ARG A 214     -33.275   0.391  15.802  1.00152.64           N  
ANISOU 1358  N   ARG A 214    26854  14698  16441  -1916  -1213   2574       N  
ATOM   1359  CA  ARG A 214     -34.515  -0.356  15.534  1.00150.52           C  
ANISOU 1359  CA  ARG A 214    26625  14872  15693  -1762   -512   2401       C  
ATOM   1360  C   ARG A 214     -34.242  -1.759  14.981  1.00150.68           C  
ANISOU 1360  C   ARG A 214    26136  14887  16226  -1794   -326   2330       C  
ATOM   1361  O   ARG A 214     -35.103  -2.642  15.048  1.00149.80           O  
ANISOU 1361  O   ARG A 214    26157  14973  15784  -1785   -149   2309       O  
ATOM   1362  CB  ARG A 214     -35.435   0.433  14.589  1.00148.88           C  
ANISOU 1362  CB  ARG A 214    26177  15016  15375  -1720    -59   2440       C  
ATOM   1363  CG  ARG A 214     -36.878  -0.081  14.539  1.00152.63           C  
ANISOU 1363  CG  ARG A 214    26418  15464  16110  -1705    168   2768       C  
ATOM   1364  CD  ARG A 214     -37.882   1.001  14.138  1.00159.85           C  
ANISOU 1364  CD  ARG A 214    26774  16093  17867  -1716    248   3334       C  
ATOM   1365  NE  ARG A 214     -37.760   2.222  14.940  1.00164.07           N  
ANISOU 1365  NE  ARG A 214    27631  16233  18472  -1421   1051   3225       N  
ATOM   1366  CZ  ARG A 214     -38.263   2.391  16.163  1.00172.82           C  
ANISOU 1366  CZ  ARG A 214    29449  16481  19734  -1209   2400   3181       C  
ATOM   1367  NH1 ARG A 214     -38.937   1.416  16.764  1.00178.78           N  
ANISOU 1367  NH1 ARG A 214    30362  16771  20795  -1131   3105   3256       N  
ATOM   1368  NH2 ARG A 214     -38.087   3.546  16.792  1.00179.03           N  
ANISOU 1368  NH2 ARG A 214    31196  16614  20211  -1204   3309   3015       N  
ATOM   1369  N   SER A 215     -33.037  -1.948  14.443  1.00155.01           N  
ANISOU 1369  N   SER A 215    26068  14917  17913  -1837    -71   2357       N  
ATOM   1370  CA  SER A 215     -32.511  -3.272  14.121  1.00160.25           C  
ANISOU 1370  CA  SER A 215    26235  14986  19665  -1858    601   2363       C  
ATOM   1371  C   SER A 215     -31.794  -3.847  15.350  1.00166.51           C  
ANISOU 1371  C   SER A 215    26342  15113  21810  -1879   -676   2998       C  
ATOM   1372  O   SER A 215     -30.564  -3.968  15.377  1.00177.05           O  
ANISOU 1372  O   SER A 215    26423  15273  25574  -1913   -862   3614       O  
ATOM   1373  CB  SER A 215     -31.566  -3.199  12.915  1.00168.23           C  
ANISOU 1373  CB  SER A 215    26993  15036  21890  -1957   2280   2191       C  
ATOM   1374  OG  SER A 215     -32.229  -2.685  11.769  1.00166.49           O  
ANISOU 1374  OG  SER A 215    28188  15128  19943  -2384   3018   1721       O  
ATOM   1375  N   ALA A 216     -32.583  -4.188  16.369  1.00164.05           N  
ANISOU 1375  N   ALA A 216    26924  15200  20205  -2010  -1602   3031       N  
ATOM   1376  CA  ALA A 216     -32.064  -4.717  17.628  1.00173.01           C  
ANISOU 1376  CA  ALA A 216    28313  15505  21916  -2467  -3315   3726       C  
ATOM   1377  C   ALA A 216     -32.596  -6.125  17.856  1.00171.59           C  
ANISOU 1377  C   ALA A 216    28190  15462  21544  -2406  -3063   3613       C  
ATOM   1378  O   ALA A 216     -33.744  -6.418  17.528  1.00163.33           O  
ANISOU 1378  O   ALA A 216    27646  15273  19140  -2122  -1950   3004       O  
ATOM   1379  CB  ALA A 216     -32.458  -3.813  18.786  1.00176.68           C  
ANISOU 1379  CB  ALA A 216    30852  15774  20503  -3049  -4401   3812       C  
TER    1380      ALA A 216                                                      
ATOM   1381  N   ILE B  44     -22.990  37.705 -16.914  1.00167.78           N  
ANISOU 1381  N   ILE B  44    20363  22684  20701   2236    877   1796       N  
ATOM   1382  CA  ILE B  44     -23.956  37.649 -18.054  1.00164.25           C  
ANISOU 1382  CA  ILE B  44    20264  21224  20918   1798    877   2280       C  
ATOM   1383  C   ILE B  44     -23.296  37.277 -19.378  1.00161.71           C  
ANISOU 1383  C   ILE B  44    20244  20311  20885   1425    742   2445       C  
ATOM   1384  O   ILE B  44     -23.971  36.880 -20.326  1.00158.38           O  
ANISOU 1384  O   ILE B  44    20085  19229  20861   1156    736   2918       O  
ATOM   1385  CB  ILE B  44     -24.778  38.961 -18.182  1.00146.84           C  
ANISOU 1385  CB  ILE B  44    17954  18614  19222   1518    880   1893       C  
ATOM   1386  CG1 ILE B  44     -26.092  38.818 -17.406  1.00148.10           C  
ANISOU 1386  CG1 ILE B  44    18039  18914  19318   1767   1043   2238       C  
ATOM   1387  CG2 ILE B  44     -25.104  39.290 -19.639  1.00142.43           C  
ANISOU 1387  CG2 ILE B  44    17674  17114  19329   1006    803   2094       C  
ATOM   1388  CD1 ILE B  44     -25.941  38.540 -15.892  1.00152.36           C  
ANISOU 1388  CD1 ILE B  44    18246  20498  19144   2366   1159   2112       C  
ATOM   1389  N   ARG B  45     -21.977  37.414 -19.445  1.00164.54           N  
ANISOU 1389  N   ARG B  45    20528  20958  21030   1419    630   2012       N  
ATOM   1390  CA  ARG B  45     -21.242  36.982 -20.630  1.00162.79           C  
ANISOU 1390  CA  ARG B  45    20575  20274  21002   1121    509   2173       C  
ATOM   1391  C   ARG B  45     -21.379  35.478 -20.810  1.00162.25           C  
ANISOU 1391  C   ARG B  45    20723  20156  20768   1276    590   2902       C  
ATOM   1392  O   ARG B  45     -21.445  34.986 -21.938  1.00158.84           O  
ANISOU 1392  O   ARG B  45    20547  19143  20662    977    531   3214       O  
ATOM   1393  CB  ARG B  45     -19.771  37.321 -20.513  1.00164.74           C  
ANISOU 1393  CB  ARG B  45    20669  20919  21005   1146    400   1580       C  
ATOM   1394  CG  ARG B  45     -19.461  38.664 -19.910  1.00169.40           C  
ANISOU 1394  CG  ARG B  45    20886  21798  21678   1131    394    718       C  
ATOM   1395  CD  ARG B  45     -17.972  38.831 -19.867  1.00173.00           C  
ANISOU 1395  CD  ARG B  45    21177  22633  21921   1147    293    142       C  
ATOM   1396  NE  ARG B  45     -17.303  37.530 -19.948  1.00173.30           N  
ANISOU 1396  NE  ARG B  45    21407  22960  21479   1361    247    622       N  
ATOM   1397  CZ  ARG B  45     -16.487  37.156 -20.932  1.00171.23           C  
ANISOU 1397  CZ  ARG B  45    21381  22324  21351   1122    149    753       C  
ATOM   1398  NH1 ARG B  45     -16.198  37.989 -21.928  1.00169.73           N  
ANISOU 1398  NH1 ARG B  45    21262  21500  21725    689     86    468       N  
ATOM   1399  NH2 ARG B  45     -15.945  35.945 -20.910  1.00170.77           N  
ANISOU 1399  NH2 ARG B  45    21463  22538  20881   1346    148   1196       N  
ATOM   1400  N   GLN B  46     -21.401  34.758 -19.687  1.00166.78           N  
ANISOU 1400  N   GLN B  46    21141  21373  20852   1773    759   3158       N  
ATOM   1401  CA  GLN B  46     -21.758  33.340 -19.669  1.00167.58           C  
ANISOU 1401  CA  GLN B  46    21368  21377  20927   1986    966   3926       C  
ATOM   1402  C   GLN B  46     -23.144  33.178 -20.284  1.00164.98           C  
ANISOU 1402  C   GLN B  46    21197  20322  21165   1715   1039   4318       C  
ATOM   1403  O   GLN B  46     -23.408  32.205 -20.992  1.00163.42           O  
ANISOU 1403  O   GLN B  46    21164  19643  21282   1577   1122   4766       O  
ATOM   1404  CB  GLN B  46     -21.771  32.782 -18.238  1.00173.26           C  
ANISOU 1404  CB  GLN B  46    21822  22943  21065   2647   1217   4212       C  
ATOM   1405  CG  GLN B  46     -20.535  33.081 -17.393  1.00178.24           C  
ANISOU 1405  CG  GLN B  46    22172  24541  21007   3020   1140   3731       C  
ATOM   1406  CD  GLN B  46     -19.291  32.342 -17.857  1.00178.61           C  
ANISOU 1406  CD  GLN B  46    22325  24645  20891   3030   1095   3830       C  
ATOM   1407  OE1 GLN B  46     -19.356  31.186 -18.280  1.00177.51           O  
ANISOU 1407  OE1 GLN B  46    22369  24132  20945   3056   1273   4488       O  
ATOM   1408  NE2 GLN B  46     -18.146  33.009 -17.767  1.00180.59           N  
ANISOU 1408  NE2 GLN B  46    22427  25354  20835   3005    880   3135       N  
ATOM   1409  N   VAL B  47     -24.023  34.140 -19.999  1.00164.94           N  
ANISOU 1409  N   VAL B  47    21098  20264  21308   1643   1016   4095       N  
ATOM   1410  CA  VAL B  47     -25.375  34.175 -20.560  1.00162.53           C  
ANISOU 1410  CA  VAL B  47    20901  19330  21519   1386   1058   4387       C  
ATOM   1411  C   VAL B  47     -25.311  34.415 -22.072  1.00157.91           C  
ANISOU 1411  C   VAL B  47    20527  18088  21383    872    849   4290       C  
ATOM   1412  O   VAL B  47     -26.065  33.800 -22.829  1.00156.38           O  
ANISOU 1412  O   VAL B  47    20444  17416  21556    679    878   4638       O  
ATOM   1413  CB  VAL B  47     -26.267  35.253 -19.861  1.00164.17           C  
ANISOU 1413  CB  VAL B  47    20937  19677  21763   1450   1088   4138       C  
ATOM   1414  CG1 VAL B  47     -27.611  35.424 -20.576  1.00162.08           C  
ANISOU 1414  CG1 VAL B  47    20782  18753  22047   1145   1095   4392       C  
ATOM   1415  CG2 VAL B  47     -26.480  34.908 -18.384  1.00168.75           C  
ANISOU 1415  CG2 VAL B  47    21280  20976  21861   2013   1315   4309       C  
ATOM   1416  N   TYR B  48     -24.404  35.294 -22.501  1.00156.07           N  
ANISOU 1416  N   TYR B  48    20299  17874  21126    678    662   3805       N  
ATOM   1417  CA  TYR B  48     -24.222  35.577 -23.924  1.00152.28           C  
ANISOU 1417  CA  TYR B  48    19981  16874  21003    266    489   3753       C  
ATOM   1418  C   TYR B  48     -23.601  34.394 -24.660  1.00150.24           C  
ANISOU 1418  C   TYR B  48    19887  16490  20708    194    446   4005       C  
ATOM   1419  O   TYR B  48     -24.074  34.013 -25.731  1.00148.28           O  
ANISOU 1419  O   TYR B  48    19745  15828  20766    -57    382   4207       O  
ATOM   1420  CB  TYR B  48     -23.387  36.850 -24.150  1.00152.45           C  
ANISOU 1420  CB  TYR B  48    19922  16909  21091    111    380   3208       C  
ATOM   1421  CG  TYR B  48     -23.108  37.140 -25.613  1.00149.89           C  
ANISOU 1421  CG  TYR B  48    19739  16119  21093   -235    247   3240       C  
ATOM   1422  CD1 TYR B  48     -24.148  37.435 -26.497  1.00148.85           C  
ANISOU 1422  CD1 TYR B  48    19653  15570  21332   -436    231   3502       C  
ATOM   1423  CD2 TYR B  48     -21.809  37.111 -26.114  1.00149.15           C  
ANISOU 1423  CD2 TYR B  48    19702  16066  20900   -322    147   3029       C  
ATOM   1424  CE1 TYR B  48     -23.903  37.688 -27.840  1.00147.47           C  
ANISOU 1424  CE1 TYR B  48    19557  15100  21375   -672    125   3581       C  
ATOM   1425  CE2 TYR B  48     -21.549  37.366 -27.459  1.00147.57           C  
ANISOU 1425  CE2 TYR B  48    19607  15500  20961   -588     49   3107       C  
ATOM   1426  CZ  TYR B  48     -22.602  37.650 -28.315  1.00146.84           C  
ANISOU 1426  CZ  TYR B  48    19537  15065  21187   -741     41   3397       C  
ATOM   1427  OH  TYR B  48     -22.360  37.909 -29.643  1.00145.96           O  
ANISOU 1427  OH  TYR B  48    19480  14717  21259   -927    -40   3516       O  
ATOM   1428  N   TYR B  49     -22.557  33.809 -24.078  1.00150.96           N  
ANISOU 1428  N   TYR B  49    19955  16985  20416    435    489   3966       N  
ATOM   1429  CA  TYR B  49     -21.833  32.714 -24.729  1.00149.46           C  
ANISOU 1429  CA  TYR B  49    19900  16677  20208    377    473   4169       C  
ATOM   1430  C   TYR B  49     -22.611  31.398 -24.837  1.00149.65           C  
ANISOU 1430  C   TYR B  49    19948  16438  20473    433    676   4683       C  
ATOM   1431  O   TYR B  49     -22.285  30.567 -25.679  1.00148.48           O  
ANISOU 1431  O   TYR B  49    19890  16017  20508    266    660   4796       O  
ATOM   1432  CB  TYR B  49     -20.454  32.498 -24.092  1.00151.06           C  
ANISOU 1432  CB  TYR B  49    20049  17405  19941    637    477   3991       C  
ATOM   1433  CG  TYR B  49     -19.468  33.617 -24.362  1.00150.75           C  
ANISOU 1433  CG  TYR B  49    19981  17477  19817    471    273   3416       C  
ATOM   1434  CD1 TYR B  49     -19.719  34.577 -25.345  1.00148.85           C  
ANISOU 1434  CD1 TYR B  49    19802  16783  19968    100    136   3211       C  
ATOM   1435  CD2 TYR B  49     -18.269  33.699 -23.655  1.00153.33           C  
ANISOU 1435  CD2 TYR B  49    20177  18374  19706    711    252   3093       C  
ATOM   1436  CE1 TYR B  49     -18.817  35.603 -25.601  1.00149.49           C  
ANISOU 1436  CE1 TYR B  49    19817  16882  20100    -40     33   2723       C  
ATOM   1437  CE2 TYR B  49     -17.355  34.721 -23.906  1.00153.84           C  
ANISOU 1437  CE2 TYR B  49    20165  18490  19797    539    103   2507       C  
ATOM   1438  CZ  TYR B  49     -17.637  35.671 -24.883  1.00151.98           C  
ANISOU 1438  CZ  TYR B  49    19995  17699  20050    154     18   2338       C  
ATOM   1439  OH  TYR B  49     -16.743  36.688 -25.146  1.00152.79           O  
ANISOU 1439  OH  TYR B  49    19984  17765  20305     -8    -48   1799       O  
ATOM   1440  N   ARG B  50     -23.624  31.202 -23.994  1.00151.41           N  
ANISOU 1440  N   ARG B  50    20054  16724  20750    664    894   4963       N  
ATOM   1441  CA  ARG B  50     -24.542  30.077 -24.176  1.00152.05           C  
ANISOU 1441  CA  ARG B  50    20105  16426  21240    662   1131   5409       C  
ATOM   1442  C   ARG B  50     -25.535  30.443 -25.268  1.00149.21           C  
ANISOU 1442  C   ARG B  50    19782  15579  21328    254    968   5296       C  
ATOM   1443  O   ARG B  50     -25.640  29.753 -26.278  1.00148.39           O  
ANISOU 1443  O   ARG B  50    19701  15124  21557      2    933   5314       O  
ATOM   1444  CB  ARG B  50     -25.270  29.706 -22.876  1.00156.13           C  
ANISOU 1444  CB  ARG B  50    20455  17186  21680   1094   1472   5807       C  
ATOM   1445  CG  ARG B  50     -26.546  28.889 -23.100  1.00158.22           C  
ANISOU 1445  CG  ARG B  50    20643  16940  22532   1019   1724   6184       C  
ATOM   1446  CD  ARG B  50     -26.881  28.011 -21.915  1.00164.18           C  
ANISOU 1446  CD  ARG B  50    21220  17880  23279   1520   2192   6752       C  
ATOM   1447  NE  ARG B  50     -28.258  27.526 -21.991  1.00167.03           N  
ANISOU 1447  NE  ARG B  50    21465  17754  24243   1445   2442   7041       N  
ATOM   1448  CZ  ARG B  50     -29.312  28.195 -21.532  1.00167.91           C  
ANISOU 1448  CZ  ARG B  50    21518  17901  24379   1486   2446   7055       C  
ATOM   1449  NH1 ARG B  50     -29.161  29.384 -20.961  1.00166.66           N  
ANISOU 1449  NH1 ARG B  50    21391  18225  23705   1597   2226   6775       N  
ATOM   1450  NH2 ARG B  50     -30.526  27.672 -21.646  1.00170.11           N  
ANISOU 1450  NH2 ARG B  50    21671  17712  25248   1408   2687   7307       N  
ATOM   1451  N   ASP B  51     -26.249  31.544 -25.051  1.00147.87           N  
ANISOU 1451  N   ASP B  51    19581  15448  21155    212    877   5153       N  
ATOM   1452  CA  ASP B  51     -27.177  32.103 -26.031  1.00145.60           C  
ANISOU 1452  CA  ASP B  51    19297  14812  21210   -112    716   5061       C  
ATOM   1453  C   ASP B  51     -26.567  32.118 -27.443  1.00142.54           C  
ANISOU 1453  C   ASP B  51    19000  14258  20900   -427    472   4864       C  
ATOM   1454  O   ASP B  51     -27.266  31.869 -28.427  1.00142.39           O  
ANISOU 1454  O   ASP B  51    18931  13995  21175   -651    391   4879       O  
ATOM   1455  CB  ASP B  51     -27.575  33.526 -25.603  1.00145.60           C  
ANISOU 1455  CB  ASP B  51    19257  14934  21128    -92    644   4867       C  
ATOM   1456  CG  ASP B  51     -28.985  33.914 -26.039  1.00145.96           C  
ANISOU 1456  CG  ASP B  51    19235  14695  21528   -248    632   4975       C  
ATOM   1457  OD1 ASP B  51     -29.926  33.729 -25.236  1.00147.62           O  
ANISOU 1457  OD1 ASP B  51    19354  14907  21826    -82    818   5178       O  
ATOM   1458  OD2 ASP B  51     -29.152  34.417 -27.173  1.00144.71           O  
ANISOU 1458  OD2 ASP B  51    19092  14354  21535   -502    451   4881       O  
ATOM   1459  N   LYS B  52     -25.268  32.401 -27.539  1.00140.08           N  
ANISOU 1459  N   LYS B  52    18783  14134  20305   -422    357   4658       N  
ATOM   1460  CA  LYS B  52     -24.606  32.464 -28.840  1.00137.27           C  
ANISOU 1460  CA  LYS B  52    18507  13666  19981   -678    143   4497       C  
ATOM   1461  C   LYS B  52     -23.805  31.224 -29.230  1.00136.12           C  
ANISOU 1461  C   LYS B  52    18414  13492  19813   -704    164   4535       C  
ATOM   1462  O   LYS B  52     -23.737  30.878 -30.404  1.00135.39           O  
ANISOU 1462  O   LYS B  52    18321  13259  19859   -928     29   4456       O  
ATOM   1463  CB  LYS B  52     -23.740  33.721 -28.965  1.00136.43           C  
ANISOU 1463  CB  LYS B  52    18447  13684  19706   -718     10   4224       C  
ATOM   1464  CG  LYS B  52     -24.304  34.770 -29.924  1.00136.43           C  
ANISOU 1464  CG  LYS B  52    18402  13507  19926   -904   -102   4200       C  
ATOM   1465  CD  LYS B  52     -24.187  34.322 -31.388  1.00136.07           C  
ANISOU 1465  CD  LYS B  52    18375  13380  19943  -1098   -263   4251       C  
ATOM   1466  CE  LYS B  52     -24.809  35.332 -32.343  1.00136.92           C  
ANISOU 1466  CE  LYS B  52    18387  13424  20211  -1188   -338   4332       C  
ATOM   1467  NZ  LYS B  52     -24.696  34.879 -33.756  1.00137.11           N  
ANISOU 1467  NZ  LYS B  52    18370  13528  20197  -1310   -504   4364       N  
ATOM   1468  N   GLY B  53     -23.200  30.559 -28.258  1.00136.27           N  
ANISOU 1468  N   GLY B  53    18441  13688  19646   -448    349   4657       N  
ATOM   1469  CA  GLY B  53     -22.362  29.393 -28.540  1.00135.51           C  
ANISOU 1469  CA  GLY B  53    18380  13549  19557   -439    423   4729       C  
ATOM   1470  C   GLY B  53     -23.059  28.175 -29.133  1.00136.24           C  
ANISOU 1470  C   GLY B  53    18363  13277  20123   -572    572   4872       C  
ATOM   1471  O   GLY B  53     -22.412  27.349 -29.786  1.00135.86           O  
ANISOU 1471  O   GLY B  53    18322  13111  20186   -684    575   4809       O  
ATOM   1472  N   ILE B  54     -24.367  28.047 -28.900  1.00137.37           N  
ANISOU 1472  N   ILE B  54    18370  13232  20591   -568    716   5019       N  
ATOM   1473  CA  ILE B  54     -25.140  26.945 -29.486  1.00138.95           C  
ANISOU 1473  CA  ILE B  54    18384  13054  21353   -729    880   5047       C  
ATOM   1474  C   ILE B  54     -25.224  27.120 -30.989  1.00136.83           C  
ANISOU 1474  C   ILE B  54    18074  12730  21183  -1086    563   4670       C  
ATOM   1475  O   ILE B  54     -25.179  26.146 -31.734  1.00138.21           O  
ANISOU 1475  O   ILE B  54    18105  12711  21696  -1254    614   4505       O  
ATOM   1476  CB  ILE B  54     -26.598  26.775 -28.898  1.00141.90           C  
ANISOU 1476  CB  ILE B  54    18578  13224  22111   -648   1126   5265       C  
ATOM   1477  CG1 ILE B  54     -27.662  27.640 -29.624  1.00141.50           C  
ANISOU 1477  CG1 ILE B  54    18464  13153  22144   -885    862   5042       C  
ATOM   1478  CG2 ILE B  54     -26.620  26.856 -27.363  1.00143.36           C  
ANISOU 1478  CG2 ILE B  54    18784  13605  22079   -228   1413   5665       C  
ATOM   1479  CD1 ILE B  54     -27.590  29.152 -29.415  1.00139.00           C  
ANISOU 1479  CD1 ILE B  54    18305  13121  21385   -839    618   4991       C  
ATOM   1480  N   SER B  55     -25.339  28.375 -31.419  1.00133.56           N  
ANISOU 1480  N   SER B  55    17745  12516  20484  -1170    268   4535       N  
ATOM   1481  CA  SER B  55     -25.499  28.710 -32.820  1.00131.63           C  
ANISOU 1481  CA  SER B  55    17424  12350  20239  -1416    -20   4266       C  
ATOM   1482  C   SER B  55     -24.291  28.217 -33.607  1.00129.21           C  
ANISOU 1482  C   SER B  55    17180  12115  19799  -1519   -139   4076       C  
ATOM   1483  O   SER B  55     -24.459  27.583 -34.652  1.00130.60           O  
ANISOU 1483  O   SER B  55    17177  12284  20161  -1703   -229   3826       O  
ATOM   1484  CB  SER B  55     -25.695  30.218 -32.994  1.00130.41           C  
ANISOU 1484  CB  SER B  55    17346  12384  19820  -1401   -218   4287       C  
ATOM   1485  OG  SER B  55     -26.716  30.704 -32.136  1.00130.84           O  
ANISOU 1485  OG  SER B  55    17359  12370  19983  -1289    -90   4461       O  
ATOM   1486  N   HIS B  56     -23.088  28.477 -33.083  1.00107.13           N  
ANISOU 1486  N   HIS B  56    15447  13312  11943  -2336   -258   1212       N  
ATOM   1487  CA AHIS B  56     -21.894  28.064 -33.807  0.50105.38           C  
ANISOU 1487  CA AHIS B  56    15300  13035  11703  -2385   -294   1334       C  
ATOM   1488  CA BHIS B  56     -21.794  28.028 -33.647  0.50105.39           C  
ANISOU 1488  CA BHIS B  56    15296  13054  11691  -2398   -293   1319       C  
ATOM   1489  C   HIS B  56     -21.844  26.530 -33.964  1.00103.60           C  
ANISOU 1489  C   HIS B  56    15058  12944  11359  -2421   -356   1458       C  
ATOM   1490  O   HIS B  56     -21.017  26.014 -34.724  1.00102.89           O  
ANISOU 1490  O   HIS B  56    15001  12810  11281  -2454   -381   1538       O  
ATOM   1491  CB AHIS B  56     -20.626  28.701 -33.213  0.50106.01           C  
ANISOU 1491  CB AHIS B  56    15387  13081  11811  -2473   -256   1214       C  
ATOM   1492  CB BHIS B  56     -20.652  28.279 -32.635  0.50105.84           C  
ANISOU 1492  CB BHIS B  56    15327  13186  11701  -2511   -266   1188       C  
ATOM   1493  CG AHIS B  56     -20.677  30.204 -33.179  0.50107.32           C  
ANISOU 1493  CG AHIS B  56    15531  13046  12198  -2438   -178   1069       C  
ATOM   1494  CG BHIS B  56     -19.504  29.093 -33.168  0.50106.02           C  
ANISOU 1494  CG BHIS B  56    15415  13023  11842  -2536   -240   1174       C  
ATOM   1495  ND1AHIS B  56     -21.651  30.927 -33.837  0.50107.18           N  
ANISOU 1495  ND1AHIS B  56    15490  12853  12378  -2324   -154   1127       N  
ATOM   1496  ND1BHIS B  56     -18.632  29.772 -32.343  0.50106.91           N  
ANISOU 1496  ND1BHIS B  56    15491  13158  11972  -2625   -188    992       N  
ATOM   1497  CD2AHIS B  56     -19.876  31.118 -32.582  0.50108.61           C  
ANISOU 1497  CD2AHIS B  56    15656  13138  12471  -2507   -110    872       C  
ATOM   1498  CD2BHIS B  56     -19.098  29.354 -34.433  0.50105.27           C  
ANISOU 1498  CD2BHIS B  56    15394  12757  11845  -2496   -256   1318       C  
ATOM   1499  CE1AHIS B  56     -21.457  32.217 -33.634  0.50108.97           C  
ANISOU 1499  CE1AHIS B  56    15656  12866  12882  -2315    -72    985       C  
ATOM   1500  CE1BHIS B  56     -17.737  30.410 -33.076  0.50106.94           C  
ANISOU 1500  CE1BHIS B  56    15561  12960  12111  -2629   -174   1033       C  
ATOM   1501  NE2AHIS B  56     -20.384  32.361 -32.879  0.50109.93           N  
ANISOU 1501  NE2AHIS B  56    15769  13042  12953  -2429    -39    800       N  
ATOM   1502  NE2BHIS B  56     -17.999  30.175 -34.348  0.50105.83           N  
ANISOU 1502  NE2BHIS B  56    15484  12711  12013  -2552   -218   1247       N  
ATOM   1503  N   ALA B  57     -22.805  25.838 -33.319  1.00102.65           N  
ANISOU 1503  N   ALA B  57    14861  12972  11169  -2413   -372   1467       N  
ATOM   1504  CA  ALA B  57     -23.028  24.372 -33.399  1.00100.69           C  
ANISOU 1504  CA  ALA B  57    14544  12809  10903  -2438   -419   1590       C  
ATOM   1505  C   ALA B  57     -24.296  23.914 -34.172  1.00 99.90           C  
ANISOU 1505  C   ALA B  57    14426  12706  10824  -2362   -431   1622       C  
ATOM   1506  O   ALA B  57     -24.286  22.835 -34.775  1.00 99.27           O  
ANISOU 1506  O   ALA B  57    14294  12617  10805  -2382   -451   1675       O  
ATOM   1507  CB  ALA B  57     -23.027  23.759 -31.993  1.00101.01           C  
ANISOU 1507  CB  ALA B  57    14456  13062  10861  -2516   -436   1639       C  
ATOM   1508  N   LYS B  58     -25.377  24.702 -34.132  1.00 99.73           N  
ANISOU 1508  N   LYS B  58    14417  12694  10780  -2282   -411   1570       N  
ATOM   1509  CA  LYS B  58     -26.597  24.409 -34.916  1.00 99.32           C  
ANISOU 1509  CA  LYS B  58    14341  12666  10727  -2209   -422   1608       C  
ATOM   1510  C   LYS B  58     -26.357  24.647 -36.410  1.00 99.14           C  
ANISOU 1510  C   LYS B  58    14350  12590  10726  -2186   -426   1660       C  
ATOM   1511  O   LYS B  58     -26.866  23.917 -37.267  1.00 99.11           O  
ANISOU 1511  O   LYS B  58    14289  12674  10694  -2188   -440   1677       O  
ATOM   1512  CB  LYS B  58     -27.796  25.265 -34.469  1.00100.11           C  
ANISOU 1512  CB  LYS B  58    14423  12790  10823  -2124   -396   1554       C  
ATOM   1513  CG  LYS B  58     -28.026  25.346 -32.958  1.00100.62           C  
ANISOU 1513  CG  LYS B  58    14422  12983  10825  -2163   -377   1451       C  
ATOM   1514  CD  LYS B  58     -29.502  25.547 -32.590  1.00100.87           C  
ANISOU 1514  CD  LYS B  58    14388  13104  10831  -2093   -362   1397       C  
ATOM   1515  CE  LYS B  58     -30.208  24.208 -32.411  1.00100.90           C  
ANISOU 1515  CE  LYS B  58    14319  13265  10751  -2118   -408   1502       C  
ATOM   1516  NZ  LYS B  58     -31.577  24.365 -31.860  1.00102.00           N  
ANISOU 1516  NZ  LYS B  58    14384  13535  10835  -2067   -395   1444       N  
ATOM   1517  N   ALA B  59     -25.589  25.689 -36.706  1.00 99.13           N  
ANISOU 1517  N   ALA B  59    14410  12483  10772  -2180   -408   1678       N  
ATOM   1518  CA  ALA B  59     -25.229  26.024 -38.070  1.00 99.30           C  
ANISOU 1518  CA  ALA B  59    14427  12513  10788  -2178   -417   1776       C  
ATOM   1519  C   ALA B  59     -24.009  25.237 -38.540  1.00 98.58           C  
ANISOU 1519  C   ALA B  59    14338  12450  10664  -2277   -428   1742       C  
ATOM   1520  O   ALA B  59     -23.705  25.225 -39.730  1.00 99.28           O  
ANISOU 1520  O   ALA B  59    14383  12639  10698  -2308   -436   1788       O  
ATOM   1521  CB  ALA B  59     -25.000  27.507 -38.208  1.00100.26           C  
ANISOU 1521  CB  ALA B  59    14572  12489  11033  -2127   -391   1858       C  
ATOM   1522  N   GLY B  60     -23.304  24.592 -37.615  1.00 97.45           N  
ANISOU 1522  N   GLY B  60    14212  12255  10556  -2336   -428   1672       N  
ATOM   1523  CA  GLY B  60     -22.341  23.559 -37.995  1.00 96.92           C  
ANISOU 1523  CA  GLY B  60    14101  12198  10525  -2422   -433   1630       C  
ATOM   1524  C   GLY B  60     -20.859  23.866 -37.891  1.00 96.50           C  
ANISOU 1524  C   GLY B  60    14104  12062  10500  -2482   -428   1629       C  
ATOM   1525  O   GLY B  60     -20.037  23.130 -38.444  1.00 96.35           O  
ANISOU 1525  O   GLY B  60    14033  12048  10528  -2549   -425   1584       O  
ATOM   1526  N   ARG B  61     -20.506  24.927 -37.169  1.00 96.39           N  
ANISOU 1526  N   ARG B  61    14172  11971  10480  -2467   -417   1646       N  
ATOM   1527  CA  ARG B  61     -19.092  25.254 -36.954  1.00 96.17           C  
ANISOU 1527  CA  ARG B  61    14193  11873  10472  -2532   -410   1636       C  
ATOM   1528  C   ARG B  61     -18.549  24.477 -35.736  1.00 95.49           C  
ANISOU 1528  C   ARG B  61    14057  11824  10400  -2596   -420   1631       C  
ATOM   1529  O   ARG B  61     -18.284  25.031 -34.666  1.00 95.24           O  
ANISOU 1529  O   ARG B  61    14033  11827  10326  -2624   -408   1601       O  
ATOM   1530  CB  ARG B  61     -18.888  26.781 -36.871  1.00 97.23           C  
ANISOU 1530  CB  ARG B  61    14397  11903  10642  -2503   -381   1635       C  
ATOM   1531  CG  ARG B  61     -19.491  27.538 -38.075  1.00 97.85           C  
ANISOU 1531  CG  ARG B  61    14464  11962  10750  -2437   -381   1746       C  
ATOM   1532  CD  ARG B  61     -19.336  29.059 -37.990  1.00 98.73           C  
ANISOU 1532  CD  ARG B  61    14593  11899  11019  -2400   -343   1785       C  
ATOM   1533  NE  ARG B  61     -20.423  29.722 -37.261  1.00 98.31           N  
ANISOU 1533  NE  ARG B  61    14505  11763  11083  -2323   -306   1721       N  
ATOM   1534  CZ  ARG B  61     -21.595  30.070 -37.787  1.00 98.19           C  
ANISOU 1534  CZ  ARG B  61    14428  11744  11133  -2232   -308   1835       C  
ATOM   1535  NH1 ARG B  61     -22.503  30.677 -37.033  1.00 97.88           N  
ANISOU 1535  NH1 ARG B  61    14344  11611  11235  -2166   -263   1737       N  
ATOM   1536  NH2 ARG B  61     -21.870  29.812 -39.061  1.00 98.93           N  
ANISOU 1536  NH2 ARG B  61    14477  11968  11143  -2217   -350   2034       N  
ATOM   1537  N   TYR B  62     -18.393  23.172 -35.955  1.00 95.53           N  
ANISOU 1537  N   TYR B  62    13967  11842  10486  -2631   -436   1663       N  
ATOM   1538  CA  TYR B  62     -18.027  22.184 -34.935  1.00 95.21           C  
ANISOU 1538  CA  TYR B  62    13808  11839  10526  -2687   -455   1755       C  
ATOM   1539  C   TYR B  62     -16.588  22.361 -34.440  1.00 94.17           C  
ANISOU 1539  C   TYR B  62    13681  11705  10394  -2762   -458   1795       C  
ATOM   1540  O   TYR B  62     -16.272  22.096 -33.274  1.00 94.32           O  
ANISOU 1540  O   TYR B  62    13605  11842  10387  -2817   -476   1904       O  
ATOM   1541  CB  TYR B  62     -18.258  20.766 -35.493  1.00 96.14           C  
ANISOU 1541  CB  TYR B  62    13781  11896  10851  -2697   -454   1769       C  
ATOM   1542  CG  TYR B  62     -19.686  20.507 -35.993  1.00 98.47           C  
ANISOU 1542  CG  TYR B  62    14048  12223  11140  -2639   -448   1711       C  
ATOM   1543  CD1 TYR B  62     -19.929  19.979 -37.264  1.00100.85           C  
ANISOU 1543  CD1 TYR B  62    14289  12506  11522  -2643   -421   1573       C  
ATOM   1544  CD2 TYR B  62     -20.794  20.803 -35.190  1.00100.23           C  
ANISOU 1544  CD2 TYR B  62    14282  12542  11259  -2593   -463   1767       C  
ATOM   1545  CE1 TYR B  62     -21.242  19.739 -37.707  1.00103.02           C  
ANISOU 1545  CE1 TYR B  62    14518  12853  11770  -2602   -414   1513       C  
ATOM   1546  CE2 TYR B  62     -22.102  20.574 -35.626  1.00101.68           C  
ANISOU 1546  CE2 TYR B  62    14437  12762  11432  -2539   -459   1722       C  
ATOM   1547  CZ  TYR B  62     -22.318  20.044 -36.877  1.00103.16           C  
ANISOU 1547  CZ  TYR B  62    14571  12928  11697  -2543   -437   1605       C  
ATOM   1548  OH  TYR B  62     -23.615  19.828 -37.286  1.00105.08           O  
ANISOU 1548  OH  TYR B  62    14769  13247  11907  -2501   -432   1556       O  
ATOM   1549  N   SER B  63     -15.735  22.808 -35.359  1.00 93.38           N  
ANISOU 1549  N   SER B  63    13667  11514  10300  -2773   -442   1722       N  
ATOM   1550  CA  SER B  63     -14.370  23.240 -35.084  1.00 92.37           C  
ANISOU 1550  CA  SER B  63    13576  11372  10148  -2838   -439   1729       C  
ATOM   1551  C   SER B  63     -14.381  24.438 -34.132  1.00 92.09           C  
ANISOU 1551  C   SER B  63    13604  11414   9969  -2851   -424   1680       C  
ATOM   1552  O   SER B  63     -13.615  24.482 -33.158  1.00 92.19           O  
ANISOU 1552  O   SER B  63    13562  11540   9925  -2928   -428   1708       O  
ATOM   1553  CB  SER B  63     -13.661  23.585 -36.408  1.00 92.78           C  
ANISOU 1553  CB  SER B  63    13700  11336  10215  -2844   -423   1655       C  
ATOM   1554  OG  SER B  63     -14.563  24.107 -37.397  1.00 92.82           O  
ANISOU 1554  OG  SER B  63    13754  11348  10163  -2783   -414   1612       O  
ATOM   1555  N   GLU B  64     -15.275  25.389 -34.405  1.00 91.70           N  
ANISOU 1555  N   GLU B  64    13631  11322   9886  -2784   -401   1595       N  
ATOM   1556  CA  GLU B  64     -15.395  26.599 -33.603  1.00 92.28           C  
ANISOU 1556  CA  GLU B  64    13728  11421   9912  -2794   -361   1473       C  
ATOM   1557  C   GLU B  64     -16.419  26.517 -32.498  1.00 92.77           C  
ANISOU 1557  C   GLU B  64    13697  11656   9892  -2792   -354   1422       C  
ATOM   1558  O   GLU B  64     -16.365  27.290 -31.549  1.00 93.57           O  
ANISOU 1558  O   GLU B  64    13749  11868   9933  -2843   -312   1267       O  
ATOM   1559  CB  GLU B  64     -15.781  27.769 -34.484  1.00 93.24           C  
ANISOU 1559  CB  GLU B  64    13933  11362  10131  -2721   -327   1426       C  
ATOM   1560  CG  GLU B  64     -14.639  28.366 -35.236  1.00 93.61           C  
ANISOU 1560  CG  GLU B  64    14045  11282  10241  -2752   -317   1451       C  
ATOM   1561  CD  GLU B  64     -14.917  29.776 -35.642  1.00 95.72           C  
ANISOU 1561  CD  GLU B  64    14332  11370  10666  -2702   -271   1430       C  
ATOM   1562  OE1 GLU B  64     -14.006  30.615 -35.478  1.00 96.74           O  
ANISOU 1562  OE1 GLU B  64    14475  11395  10886  -2754   -233   1364       O  
ATOM   1563  OE2 GLU B  64     -16.048  30.046 -36.101  1.00 97.24           O  
ANISOU 1563  OE2 GLU B  64    14504  11517  10925  -2613   -269   1491       O  
ATOM   1564  N   ALA B  65     -17.373  25.603 -32.640  1.00 92.63           N  
ANISOU 1564  N   ALA B  65    13633  11683   9876  -2743   -387   1522       N  
ATOM   1565  CA  ALA B  65     -18.487  25.466 -31.690  1.00 93.58           C  
ANISOU 1565  CA  ALA B  65    13656  11988   9911  -2736   -386   1497       C  
ATOM   1566  C   ALA B  65     -18.028  25.359 -30.233  1.00 94.66           C  
ANISOU 1566  C   ALA B  65    13644  12428   9892  -2856   -387   1490       C  
ATOM   1567  O   ALA B  65     -18.563  26.030 -29.340  1.00 96.11           O  
ANISOU 1567  O   ALA B  65    13750  12802   9964  -2888   -347   1320       O  
ATOM   1568  CB  ALA B  65     -19.324  24.272 -32.053  1.00 93.20           C  
ANISOU 1568  CB  ALA B  65    13555  11943   9912  -2690   -427   1644       C  
ATOM   1569  N   VAL B  66     -17.049  24.485 -30.024  1.00 94.04           N  
ANISOU 1569  N   VAL B  66    13489  12425   9815  -2930   -429   1674       N  
ATOM   1570  CA  VAL B  66     -16.326  24.318 -28.783  1.00 95.64           C  
ANISOU 1570  CA  VAL B  66    13518  12961   9858  -3064   -442   1745       C  
ATOM   1571  C   VAL B  66     -16.063  25.656 -28.046  1.00 98.12           C  
ANISOU 1571  C   VAL B  66    13818  13449  10013  -3141   -375   1443       C  
ATOM   1572  O   VAL B  66     -16.598  25.910 -26.964  1.00100.25           O  
ANISOU 1572  O   VAL B  66    13926  14068  10096  -3217   -352   1331       O  
ATOM   1573  CB  VAL B  66     -14.979  23.592 -29.095  1.00 94.84           C  
ANISOU 1573  CB  VAL B  66    13394  12775   9866  -3110   -478   1944       C  
ATOM   1574  CG1 VAL B  66     -14.238  23.213 -27.835  1.00 96.68           C  
ANISOU 1574  CG1 VAL B  66    13396  13395   9943  -3252   -509   2122       C  
ATOM   1575  CG2 VAL B  66     -15.221  22.343 -29.943  1.00 93.10           C  
ANISOU 1575  CG2 VAL B  66    13157  12321   9894  -3038   -515   2143       C  
ATOM   1576  N   VAL B  67     -15.253  26.504 -28.663  1.00 98.54           N  
ANISOU 1576  N   VAL B  67    14012  13265  10161  -3131   -334   1290       N  
ATOM   1577  CA  VAL B  67     -14.735  27.723 -28.061  1.00101.32           C  
ANISOU 1577  CA  VAL B  67    14329  13716  10450  -3219   -258    987       C  
ATOM   1578  C   VAL B  67     -15.670  28.456 -27.086  1.00104.93           C  
ANISOU 1578  C   VAL B  67    14642  14420  10804  -3264   -187    689       C  
ATOM   1579  O   VAL B  67     -15.307  28.638 -25.927  1.00107.53           O  
ANISOU 1579  O   VAL B  67    14770  15170  10914  -3419   -158    541       O  
ATOM   1580  CB  VAL B  67     -14.198  28.680 -29.168  1.00100.58           C  
ANISOU 1580  CB  VAL B  67    14426  13203  10585  -3151   -214    872       C  
ATOM   1581  CG1 VAL B  67     -13.656  29.974 -28.567  1.00102.74           C  
ANISOU 1581  CG1 VAL B  67    14636  13514  10885  -3245   -118    530       C  
ATOM   1582  CG2 VAL B  67     -13.118  27.972 -30.007  1.00 97.91           C  
ANISOU 1582  CG2 VAL B  67    14186  12717  10298  -3144   -273   1112       C  
ATOM   1583  N   MET B  68     -16.852  28.870 -27.534  1.00106.36           N  
ANISOU 1583  N   MET B  68    14891  14388  11132  -3143   -156    588       N  
ATOM   1584  CA  MET B  68     -17.764  29.640 -26.671  1.00110.94           C  
ANISOU 1584  CA  MET B  68    15319  15161  11672  -3178    -72    251       C  
ATOM   1585  C   MET B  68     -18.429  28.839 -25.540  1.00112.86           C  
ANISOU 1585  C   MET B  68    15345  15925  11609  -3268   -109    317       C  
ATOM   1586  O   MET B  68     -18.689  29.381 -24.462  1.00116.16           O  
ANISOU 1586  O   MET B  68    15547  16721  11866  -3389    -37      1       O  
ATOM   1587  CB  MET B  68     -18.844  30.340 -27.497  1.00111.51           C  
ANISOU 1587  CB  MET B  68    15500  14836  12032  -3014    -27    157       C  
ATOM   1588  CG  MET B  68     -18.440  31.684 -28.078  1.00113.87           C  
ANISOU 1588  CG  MET B  68    15859  14737  12667  -2973     63    -57       C  
ATOM   1589  SD  MET B  68     -19.890  32.616 -28.620  1.00117.72           S  
ANISOU 1589  SD  MET B  68    16340  14873  13514  -2809    135   -181       S  
ATOM   1590  CE  MET B  68     -19.124  33.921 -29.588  1.00119.45           C  
ANISOU 1590  CE  MET B  68    16624  14571  14189  -2755    204   -208       C  
ATOM   1591  N   LEU B  69     -18.702  27.560 -25.796  1.00118.85           N  
ANISOU 1591  N   LEU B  69    15744  14960  14452  -3811   1509   2308       N  
ATOM   1592  CA  LEU B  69     -19.417  26.691 -24.848  1.00115.45           C  
ANISOU 1592  CA  LEU B  69    15515  14191  14160  -3463   1613   1989       C  
ATOM   1593  C   LEU B  69     -18.477  25.949 -23.898  1.00114.70           C  
ANISOU 1593  C   LEU B  69    15473  14307  13801  -3384   1623   1624       C  
ATOM   1594  O   LEU B  69     -18.759  25.820 -22.707  1.00113.70           O  
ANISOU 1594  O   LEU B  69    15582  13815  13801  -3262   1733   1429       O  
ATOM   1595  CB  LEU B  69     -20.316  25.701 -25.597  1.00112.67           C  
ANISOU 1595  CB  LEU B  69    15013  13974  13821  -3173   1583   1979       C  
ATOM   1596  CG  LEU B  69     -21.447  26.356 -26.388  1.00112.81           C  
ANISOU 1596  CG  LEU B  69    14986  13758  14115  -3182   1585   2325       C  
ATOM   1597  CD1 LEU B  69     -22.233  25.319 -27.140  1.00110.49           C  
ANISOU 1597  CD1 LEU B  69    14499  13692  13787  -2919   1541   2252       C  
ATOM   1598  CD2 LEU B  69     -22.364  27.172 -25.492  1.00111.64           C  
ANISOU 1598  CD2 LEU B  69    15138  12871  14406  -3151   1720   2381       C  
ATOM   1599  N   GLU B  70     -17.355  25.484 -24.442  1.00116.10           N  
ANISOU 1599  N   GLU B  70    15399  15127  13587  -3449   1503   1543       N  
ATOM   1600  CA  GLU B  70     -16.332  24.751 -23.699  1.00115.99           C  
ANISOU 1600  CA  GLU B  70    15371  15417  13281  -3354   1474   1221       C  
ATOM   1601  C   GLU B  70     -15.551  25.627 -22.722  1.00118.36           C  
ANISOU 1601  C   GLU B  70    15816  15616  13538  -3620   1525   1154       C  
ATOM   1602  O   GLU B  70     -14.570  25.185 -22.125  1.00118.66           O  
ANISOU 1602  O   GLU B  70    15807  15986  13289  -3588   1489    916       O  
ATOM   1603  CB  GLU B  70     -15.381  24.077 -24.681  1.00116.99           C  
ANISOU 1603  CB  GLU B  70    15133  16309  13006  -3331   1320   1134       C  
ATOM   1604  CG  GLU B  70     -14.220  23.332 -24.072  1.00117.36           C  
ANISOU 1604  CG  GLU B  70    15104  16755  12732  -3211   1256    814       C  
ATOM   1605  CD  GLU B  70     -12.944  23.553 -24.847  1.00121.42           C  
ANISOU 1605  CD  GLU B  70    15268  18037  12828  -3437   1137    808       C  
ATOM   1606  OE1 GLU B  70     -12.674  24.714 -25.233  1.00124.80           O  
ANISOU 1606  OE1 GLU B  70    15639  18542  13234  -3844   1150   1082       O  
ATOM   1607  OE2 GLU B  70     -12.210  22.568 -25.074  1.00122.13           O  
ANISOU 1607  OE2 GLU B  70    15123  18655  12625  -3210   1024    535       O  
ATOM   1608  N   GLN B  71     -15.975  26.873 -22.567  1.00120.70           N  
ANISOU 1608  N   GLN B  71    16269  15456  14133  -3873   1594   1345       N  
ATOM   1609  CA  GLN B  71     -15.516  27.676 -21.446  1.00122.92           C  
ANISOU 1609  CA  GLN B  71    16735  15489  14479  -4078   1660   1190       C  
ATOM   1610  C   GLN B  71     -16.726  28.178 -20.660  1.00121.73           C  
ANISOU 1610  C   GLN B  71    16874  14619  14759  -3966   1801   1160       C  
ATOM   1611  O   GLN B  71     -16.675  29.217 -19.996  1.00124.57           O  
ANISOU 1611  O   GLN B  71    17384  14617  15329  -4176   1854   1084       O  
ATOM   1612  CB  GLN B  71     -14.595  28.808 -21.912  1.00127.81           C  
ANISOU 1612  CB  GLN B  71    17230  16278  15051  -4552   1586   1365       C  
ATOM   1613  CG  GLN B  71     -13.176  28.340 -22.288  1.00130.55           C  
ANISOU 1613  CG  GLN B  71    17280  17430  14892  -4681   1471   1274       C  
ATOM   1614  CD  GLN B  71     -12.112  29.419 -22.090  1.00137.49           C  
ANISOU 1614  CD  GLN B  71    18097  18435  15707  -5171   1435   1295       C  
ATOM   1615  OE1 GLN B  71     -11.097  29.193 -21.425  1.00139.26           O  
ANISOU 1615  OE1 GLN B  71    18249  19038  15623  -5229   1412   1008       O  
ATOM   1616  NE2 GLN B  71     -12.346  30.598 -22.659  1.00142.07           N  
ANISOU 1616  NE2 GLN B  71    18695  18685  16598  -5531   1418   1648       N  
ATOM   1617  N   VAL B  72     -17.813  27.409 -20.749  1.00117.54           N  
ANISOU 1617  N   VAL B  72    16392  13905  14359  -3632   1856   1185       N  
ATOM   1618  CA  VAL B  72     -19.072  27.681 -20.036  1.00115.74           C  
ANISOU 1618  CA  VAL B  72    16389  13091  14494  -3464   1999   1141       C  
ATOM   1619  C   VAL B  72     -19.690  26.400 -19.447  1.00111.03           C  
ANISOU 1619  C   VAL B  72    15843  12514  13827  -3101   2073    993       C  
ATOM   1620  O   VAL B  72     -20.409  26.452 -18.444  1.00110.51           O  
ANISOU 1620  O   VAL B  72    15946  12132  13911  -2971   2211    862       O  
ATOM   1621  CB  VAL B  72     -20.091  28.419 -20.948  1.00116.95           C  
ANISOU 1621  CB  VAL B  72    16535  12873  15026  -3498   1993   1460       C  
ATOM   1622  CG1 VAL B  72     -21.457  28.508 -20.304  1.00116.23           C  
ANISOU 1622  CG1 VAL B  72    16617  12268  15275  -3258   2136   1390       C  
ATOM   1623  CG2 VAL B  72     -19.596  29.817 -21.261  1.00122.20           C  
ANISOU 1623  CG2 VAL B  72    17208  13350  15870  -3867   1932   1638       C  
ATOM   1624  N   TYR B  73     -19.403  25.259 -20.076  1.00107.39           N  
ANISOU 1624  N   TYR B  73    15216  12435  13149  -2948   1976   1011       N  
ATOM   1625  CA  TYR B  73     -19.847  23.965 -19.568  1.00103.54           C  
ANISOU 1625  CA  TYR B  73    14763  11949  12627  -2636   2012    901       C  
ATOM   1626  C   TYR B  73     -19.224  23.768 -18.196  1.00103.75           C  
ANISOU 1626  C   TYR B  73    14910  12059  12449  -2602   2070    696       C  
ATOM   1627  O   TYR B  73     -18.097  24.214 -17.946  1.00105.32           O  
ANISOU 1627  O   TYR B  73    15071  12535  12410  -2783   2016    587       O  
ATOM   1628  CB  TYR B  73     -19.468  22.822 -20.530  1.00101.71           C  
ANISOU 1628  CB  TYR B  73    14310  12105  12228  -2488   1859    893       C  
ATOM   1629  CG  TYR B  73     -19.596  21.409 -19.969  1.00 98.61           C  
ANISOU 1629  CG  TYR B  73    13942  11717  11807  -2189   1847    768       C  
ATOM   1630  CD1 TYR B  73     -20.842  20.882 -19.594  1.00 95.93           C  
ANISOU 1630  CD1 TYR B  73    13712  10992  11742  -2017   1950    827       C  
ATOM   1631  CD2 TYR B  73     -18.471  20.590 -19.828  1.00 97.48           C  
ANISOU 1631  CD2 TYR B  73    13695  11959  11383  -2080   1722    614       C  
ATOM   1632  CE1 TYR B  73     -20.959  19.583 -19.078  1.00 93.62           C  
ANISOU 1632  CE1 TYR B  73    13442  10656  11470  -1780   1927    776       C  
ATOM   1633  CE2 TYR B  73     -18.580  19.286 -19.316  1.00 95.67           C  
ANISOU 1633  CE2 TYR B  73    13495  11665  11189  -1796   1685    548       C  
ATOM   1634  CZ  TYR B  73     -19.826  18.793 -18.941  1.00 94.12           C  
ANISOU 1634  CZ  TYR B  73    13425  11040  11294  -1666   1787    651       C  
ATOM   1635  OH  TYR B  73     -19.936  17.511 -18.435  1.00 92.86           O  
ANISOU 1635  OH  TYR B  73    13294  10771  11215  -1423   1741    646       O  
ATOM   1636  N   ASP B  74     -19.981  23.128 -17.310  1.00102.08           N  
ANISOU 1636  N   ASP B  74    14819  11648  12319  -2390   2180    663       N  
ATOM   1637  CA  ASP B  74     -19.554  22.875 -15.946  1.00102.31           C  
ANISOU 1637  CA  ASP B  74    14943  11797  12131  -2329   2246    517       C  
ATOM   1638  C   ASP B  74     -20.139  21.533 -15.560  1.00100.48           C  
ANISOU 1638  C   ASP B  74    14729  11516  11930  -2051   2267    604       C  
ATOM   1639  O   ASP B  74     -21.357  21.419 -15.421  1.00 99.84           O  
ANISOU 1639  O   ASP B  74    14714  11120  12098  -1969   2385    700       O  
ATOM   1640  CB  ASP B  74     -20.090  23.976 -15.027  1.00104.35           C  
ANISOU 1640  CB  ASP B  74    15348  11790  12509  -2442   2412    404       C  
ATOM   1641  CG  ASP B  74     -19.511  23.915 -13.621  1.00105.99           C  
ANISOU 1641  CG  ASP B  74    15609  12245  12415  -2427   2475    208       C  
ATOM   1642  OD1 ASP B  74     -18.747  22.976 -13.311  1.00104.78           O  
ANISOU 1642  OD1 ASP B  74    15395  12445  11972  -2309   2390    219       O  
ATOM   1643  OD2 ASP B  74     -19.827  24.826 -12.823  1.00107.63           O  
ANISOU 1643  OD2 ASP B  74    15902  12311  12678  -2518   2600     26       O  
ATOM   1644  N   ALA B  75     -19.276  20.529 -15.396  1.00 99.96           N  
ANISOU 1644  N   ALA B  75    14592  11752  11635  -1911   2144    583       N  
ATOM   1645  CA  ALA B  75     -19.705  19.160 -15.068  1.00 99.30           C  
ANISOU 1645  CA  ALA B  75    14521  11579  11629  -1653   2122    705       C  
ATOM   1646  C   ALA B  75     -20.630  19.094 -13.841  1.00100.27           C  
ANISOU 1646  C   ALA B  75    14782  11508  11806  -1605   2312    811       C  
ATOM   1647  O   ALA B  75     -21.445  18.173 -13.710  1.00 99.66           O  
ANISOU 1647  O   ALA B  75    14723  11220  11921  -1463   2341    984       O  
ATOM   1648  CB  ALA B  75     -18.490  18.254 -14.873  1.00100.21           C  
ANISOU 1648  CB  ALA B  75    14546  12044  11482  -1497   1951    656       C  
ATOM   1649  N   ASP B  76     -20.511  20.102 -12.976  1.00101.77           N  
ANISOU 1649  N   ASP B  76    15044  11791  11830  -1743   2440    687       N  
ATOM   1650  CA  ASP B  76     -21.214  20.152 -11.698  1.00103.78           C  
ANISOU 1650  CA  ASP B  76    15382  12026  12023  -1706   2625    723       C  
ATOM   1651  C   ASP B  76     -22.364  21.163 -11.649  1.00104.03           C  
ANISOU 1651  C   ASP B  76    15469  11761  12294  -1799   2806    644       C  
ATOM   1652  O   ASP B  76     -22.873  21.476 -10.566  1.00106.42           O  
ANISOU 1652  O   ASP B  76    15807  12127  12500  -1791   2973    576       O  
ATOM   1653  CB  ASP B  76     -20.214  20.428 -10.569  1.00106.36           C  
ANISOU 1653  CB  ASP B  76    15706  12774  11930  -1744   2632    574       C  
ATOM   1654  CG  ASP B  76     -18.995  19.519 -10.635  1.00106.79           C  
ANISOU 1654  CG  ASP B  76    15681  13155  11739  -1626   2435    635       C  
ATOM   1655  OD1 ASP B  76     -19.146  18.306 -10.900  1.00106.11           O  
ANISOU 1655  OD1 ASP B  76    15573  12970  11772  -1432   2341    861       O  
ATOM   1656  OD2 ASP B  76     -17.874  20.023 -10.433  1.00108.24           O  
ANISOU 1656  OD2 ASP B  76    15809  13685  11632  -1726   2362    439       O  
ATOM   1657  N   ALA B  77     -22.780  21.663 -12.810  1.00101.83           N  
ANISOU 1657  N   ALA B  77    15173  11205  12313  -1868   2767    650       N  
ATOM   1658  CA  ALA B  77     -23.959  22.533 -12.897  1.00101.82           C  
ANISOU 1658  CA  ALA B  77    15206  10878  12601  -1902   2911    613       C  
ATOM   1659  C   ALA B  77     -24.754  22.249 -14.176  1.00 98.90           C  
ANISOU 1659  C   ALA B  77    14772  10248  12558  -1856   2853    789       C  
ATOM   1660  O   ALA B  77     -25.224  23.161 -14.856  1.00 99.36           O  
ANISOU 1660  O   ALA B  77    14822  10078  12852  -1926   2861    779       O  
ATOM   1661  CB  ALA B  77     -23.543  24.001 -12.823  1.00103.75           C  
ANISOU 1661  CB  ALA B  77    15496  11052  12869  -2082   2926    374       C  
ATOM   1662  N   PHE B  78     -24.911  20.972 -14.481  1.00 96.27           N  
ANISOU 1662  N   PHE B  78    14380   9947  12249  -1735   2784    949       N  
ATOM   1663  CA  PHE B  78     -25.379  20.531 -15.785  1.00 93.29           C  
ANISOU 1663  CA  PHE B  78    13897   9435  12113  -1697   2679   1055       C  
ATOM   1664  C   PHE B  78     -26.525  21.350 -16.390  1.00 92.98           C  
ANISOU 1664  C   PHE B  78    13825   9133  12367  -1726   2759   1093       C  
ATOM   1665  O   PHE B  78     -27.583  21.511 -15.790  1.00 93.71           O  
ANISOU 1665  O   PHE B  78    13943   9064  12596  -1674   2924   1112       O  
ATOM   1666  CB  PHE B  78     -25.755  19.057 -15.723  1.00 92.73           C  
ANISOU 1666  CB  PHE B  78    13781   9326  12126  -1556   2641   1183       C  
ATOM   1667  CG  PHE B  78     -25.654  18.354 -17.032  0.50 89.76           C  
ANISOU 1667  CG  PHE B  78    13265   8949  11889  -1506   2458   1182       C  
ATOM   1668  CD1 PHE B  78     -24.425  17.908 -17.496  0.80 87.61           C  
ANISOU 1668  CD1 PHE B  78    12926   8924  11437  -1470   2268   1085       C  
ATOM   1669  CD2 PHE B  78     -26.786  18.121 -17.798  1.00 88.01           C  
ANISOU 1669  CD2 PHE B  78    12943   8535  11959  -1483   2470   1239       C  
ATOM   1670  CE1 PHE B  78     -24.325  17.252 -18.709  0.68 86.29           C  
ANISOU 1670  CE1 PHE B  78    12591   8821  11375  -1403   2095   1013       C  
ATOM   1671  CE2 PHE B  78     -26.694  17.463 -19.012  0.60 86.73           C  
ANISOU 1671  CE2 PHE B  78    12617   8435  11900  -1434   2294   1176       C  
ATOM   1672  CZ  PHE B  78     -25.463  17.024 -19.466  0.58 86.00           C  
ANISOU 1672  CZ  PHE B  78    12454   8597  11623  -1389   2107   1048       C  
ATOM   1673  N   ASP B  79     -26.263  21.874 -17.584  1.00 91.79           N  
ANISOU 1673  N   ASP B  79    13592   8996  12286  -1803   2635   1119       N  
ATOM   1674  CA  ASP B  79     -27.259  22.477 -18.457  1.00 91.50           C  
ANISOU 1674  CA  ASP B  79    13476   8763  12523  -1803   2649   1221       C  
ATOM   1675  C   ASP B  79     -27.202  21.612 -19.712  1.00 89.50           C  
ANISOU 1675  C   ASP B  79    13041   8680  12281  -1763   2483   1287       C  
ATOM   1676  O   ASP B  79     -26.136  21.456 -20.311  1.00 89.13           O  
ANISOU 1676  O   ASP B  79    12920   8904  12038  -1823   2332   1251       O  
ATOM   1677  CB  ASP B  79     -26.869  23.940 -18.724  1.00 93.49           C  
ANISOU 1677  CB  ASP B  79    13774   8926  12820  -1953   2628   1225       C  
ATOM   1678  CG  ASP B  79     -27.479  24.521 -20.008  1.00 94.53           C  
ANISOU 1678  CG  ASP B  79    13779   8964  13173  -1972   2551   1419       C  
ATOM   1679  OD1 ASP B  79     -27.436  23.875 -21.080  1.00 94.22           O  
ANISOU 1679  OD1 ASP B  79    13568   9148  13081  -1953   2423   1514       O  
ATOM   1680  OD2 ASP B  79     -27.969  25.673 -19.937  1.00 97.12           O  
ANISOU 1680  OD2 ASP B  79    14163   9008  13728  -1999   2606   1466       O  
ATOM   1681  N   VAL B  80     -28.332  21.022 -20.094  1.00 88.41           N  
ANISOU 1681  N   VAL B  80    12802   8431  12357  -1663   2510   1345       N  
ATOM   1682  CA  VAL B  80     -28.326  19.966 -21.119  1.00 86.55           C  
ANISOU 1682  CA  VAL B  80    12378   8362  12142  -1604   2354   1318       C  
ATOM   1683  C   VAL B  80     -28.039  20.471 -22.542  1.00 86.18           C  
ANISOU 1683  C   VAL B  80    12142   8569  12032  -1668   2203   1364       C  
ATOM   1684  O   VAL B  80     -27.394  19.775 -23.329  1.00 85.78           O  
ANISOU 1684  O   VAL B  80    11931   8818  11844  -1647   2040   1260       O  
ATOM   1685  CB  VAL B  80     -29.614  19.091 -21.068  1.00 86.71           C  
ANISOU 1685  CB  VAL B  80    12323   8200  12422  -1511   2419   1337       C  
ATOM   1686  CG1 VAL B  80     -30.856  19.894 -21.455  1.00 86.87           C  
ANISOU 1686  CG1 VAL B  80    12263   8094  12647  -1505   2511   1444       C  
ATOM   1687  CG2 VAL B  80     -29.463  17.851 -21.942  1.00 86.29           C  
ANISOU 1687  CG2 VAL B  80    12088   8282  12415  -1451   2242   1219       C  
ATOM   1688  N   GLU B  81     -28.500  21.678 -22.860  1.00 86.48           N  
ANISOU 1688  N   GLU B  81    12180   8510  12166  -1735   2248   1524       N  
ATOM   1689  CA  GLU B  81     -28.298  22.230 -24.199  1.00 86.94           C  
ANISOU 1689  CA  GLU B  81    12042   8837  12153  -1812   2108   1665       C  
ATOM   1690  C   GLU B  81     -26.807  22.483 -24.455  1.00 86.22           C  
ANISOU 1690  C   GLU B  81    11932   9067  11758  -1959   1992   1646       C  
ATOM   1691  O   GLU B  81     -26.280  22.093 -25.510  1.00 86.32           O  
ANISOU 1691  O   GLU B  81    11712   9512  11570  -1982   1838   1625       O  
ATOM   1692  CB  GLU B  81     -29.155  23.478 -24.424  1.00 88.95           C  
ANISOU 1692  CB  GLU B  81    12310   8856  12631  -1834   2169   1902       C  
ATOM   1693  CG  GLU B  81     -30.675  23.279 -24.169  1.00 90.61           C  
ANISOU 1693  CG  GLU B  81    12495   8805  13124  -1674   2290   1905       C  
ATOM   1694  CD  GLU B  81     -31.371  22.330 -25.164  1.00 92.45           C  
ANISOU 1694  CD  GLU B  81    12458   9290  13379  -1589   2199   1876       C  
ATOM   1695  OE1 GLU B  81     -31.009  22.322 -26.365  1.00 92.76           O  
ANISOU 1695  OE1 GLU B  81    12278   9703  13261  -1633   2037   1947       O  
ATOM   1696  OE2 GLU B  81     -32.297  21.593 -24.735  1.00 93.21           O  
ANISOU 1696  OE2 GLU B  81    12536   9239  13641  -1493   2289   1772       O  
ATOM   1697  N   VAL B  82     -26.125  23.086 -23.479  1.00 85.82           N  
ANISOU 1697  N   VAL B  82    12094   8863  11650  -2058   2066   1616       N  
ATOM   1698  CA  VAL B  82     -24.678  23.261 -23.573  1.00 85.27           C  
ANISOU 1698  CA  VAL B  82    11999   9118  11281  -2212   1967   1568       C  
ATOM   1699  C   VAL B  82     -24.028  21.909 -23.843  1.00 83.62           C  
ANISOU 1699  C   VAL B  82    11646   9274  10851  -2090   1850   1355       C  
ATOM   1700  O   VAL B  82     -23.324  21.741 -24.842  1.00 84.57           O  
ANISOU 1700  O   VAL B  82    11536   9852  10744  -2141   1703   1337       O  
ATOM   1701  CB  VAL B  82     -24.051  23.906 -22.314  1.00 86.07           C  
ANISOU 1701  CB  VAL B  82    12337   9021  11343  -2319   2065   1481       C  
ATOM   1702  CG1 VAL B  82     -22.534  23.954 -22.439  1.00 85.78           C  
ANISOU 1702  CG1 VAL B  82    12230   9390  10970  -2480   1952   1409       C  
ATOM   1703  CG2 VAL B  82     -24.587  25.311 -22.100  1.00 87.66           C  
ANISOU 1703  CG2 VAL B  82    12665   8832  11809  -2436   2150   1629       C  
ATOM   1704  N   ALA B  83     -24.300  20.941 -22.978  1.00 81.44           N  
ANISOU 1704  N   ALA B  83    11483   8806  10655  -1921   1909   1200       N  
ATOM   1705  CA  ALA B  83     -23.689  19.628 -23.089  1.00 79.98           C  
ANISOU 1705  CA  ALA B  83    11192   8851  10344  -1771   1785    991       C  
ATOM   1706  C   ALA B  83     -24.050  18.915 -24.380  1.00 79.29           C  
ANISOU 1706  C   ALA B  83    10829   8999  10299  -1677   1646    901       C  
ATOM   1707  O   ALA B  83     -23.207  18.233 -24.963  1.00 79.56           O  
ANISOU 1707  O   ALA B  83    10674   9412  10143  -1605   1487    700       O  
ATOM   1708  CB  ALA B  83     -24.066  18.778 -21.906  1.00 80.09           C  
ANISOU 1708  CB  ALA B  83    11385   8543  10501  -1626   1874    937       C  
ATOM   1709  N   LEU B  84     -25.299  19.051 -24.813  1.00 78.46           N  
ANISOU 1709  N   LEU B  84    10672   8705  10432  -1662   1701   1007       N  
ATOM   1710  CA  LEU B  84     -25.742  18.445 -26.063  1.00 78.45           C  
ANISOU 1710  CA  LEU B  84    10377   8970  10460  -1587   1570    897       C  
ATOM   1711  C   LEU B  84     -24.921  18.990 -27.213  1.00 79.63           C  
ANISOU 1711  C   LEU B  84    10274   9698  10283  -1697   1436    928       C  
ATOM   1712  O   LEU B  84     -24.278  18.237 -27.937  1.00 80.10           O  
ANISOU 1712  O   LEU B  84    10088  10192  10153  -1617   1279    675       O  
ATOM   1713  CB  LEU B  84     -27.228  18.719 -26.314  1.00 78.44           C  
ANISOU 1713  CB  LEU B  84    10346   8722  10735  -1578   1660   1046       C  
ATOM   1714  CG  LEU B  84     -27.746  18.713 -27.759  1.00 78.41           C  
ANISOU 1714  CG  LEU B  84    10004   9098  10687  -1570   1541   1042       C  
ATOM   1715  CD1 LEU B  84     -27.646  17.341 -28.376  1.00 77.54           C  
ANISOU 1715  CD1 LEU B  84     9660   9221  10581  -1436   1385    671       C  
ATOM   1716  CD2 LEU B  84     -29.170  19.227 -27.851  1.00 77.11           C  
ANISOU 1716  CD2 LEU B  84     9832   8687  10776  -1564   1645   1247       C  
ATOM   1717  N   HIS B  85     -24.932  20.308 -27.360  1.00 80.61           N  
ANISOU 1717  N   HIS B  85    10444   9832  10352  -1882   1495   1240       N  
ATOM   1718  CA  HIS B  85     -24.279  20.956 -28.490  1.00 82.72           C  
ANISOU 1718  CA  HIS B  85    10454  10657  10319  -2039   1380   1389       C  
ATOM   1719  C   HIS B  85     -22.772  20.907 -28.400  1.00 83.71           C  
ANISOU 1719  C   HIS B  85    10528  11172  10104  -2130   1302   1265       C  
ATOM   1720  O   HIS B  85     -22.077  20.842 -29.418  1.00 85.21           O  
ANISOU 1720  O   HIS B  85    10402  12005   9967  -2190   1169   1227       O  
ATOM   1721  CB  HIS B  85     -24.766  22.379 -28.613  1.00 83.55           C  
ANISOU 1721  CB  HIS B  85    10642  10558  10544  -2218   1453   1813       C  
ATOM   1722  CG  HIS B  85     -26.189  22.471 -29.052  1.00 84.27           C  
ANISOU 1722  CG  HIS B  85    10665  10461  10892  -2114   1485   1954       C  
ATOM   1723  ND1 HIS B  85     -27.220  22.781 -28.189  1.00 82.88           N  
ANISOU 1723  ND1 HIS B  85    10733   9682  11075  -2036   1637   2022       N  
ATOM   1724  CD2 HIS B  85     -26.759  22.263 -30.263  1.00 85.74           C  
ANISOU 1724  CD2 HIS B  85    10528  11049  10999  -2064   1383   2011       C  
ATOM   1725  CE1 HIS B  85     -28.360  22.780 -28.855  1.00 83.84           C  
ANISOU 1725  CE1 HIS B  85    10691   9820  11344  -1943   1625   2132       C  
ATOM   1726  NE2 HIS B  85     -28.109  22.468 -30.115  1.00 85.88           N  
ANISOU 1726  NE2 HIS B  85    10608  10681  11341  -1961   1469   2131       N  
ATOM   1727  N   LEU B  86     -22.272  20.918 -27.172  1.00 83.49           N  
ANISOU 1727  N   LEU B  86    10778  10822  10121  -2134   1386   1190       N  
ATOM   1728  CA  LEU B  86     -20.859  20.774 -26.939  1.00 84.64           C  
ANISOU 1728  CA  LEU B  86    10877  11328   9953  -2190   1314   1037       C  
ATOM   1729  C   LEU B  86     -20.436  19.366 -27.327  1.00 85.15           C  
ANISOU 1729  C   LEU B  86    10726  11733   9894  -1939   1170    656       C  
ATOM   1730  O   LEU B  86     -19.458  19.188 -28.039  1.00 86.95           O  
ANISOU 1730  O   LEU B  86    10674  12576   9784  -1959   1040    513       O  
ATOM   1731  CB  LEU B  86     -20.532  21.075 -25.482  1.00 83.89           C  
ANISOU 1731  CB  LEU B  86    11113  10824   9935  -2230   1435   1029       C  
ATOM   1732  CG  LEU B  86     -19.087  21.449 -25.178  1.00 85.58           C  
ANISOU 1732  CG  LEU B  86    11298  11395   9823  -2393   1388    971       C  
ATOM   1733  CD1 LEU B  86     -19.006  22.376 -23.986  1.00 86.04           C  
ANISOU 1733  CD1 LEU B  86    11655  11052   9985  -2557   1525   1067       C  
ATOM   1734  CD2 LEU B  86     -18.321  20.213 -24.901  1.00 84.75           C  
ANISOU 1734  CD2 LEU B  86    11110  11545   9547  -2155   1287    648       C  
ATOM   1735  N   GLY B  87     -21.191  18.366 -26.888  1.00 78.95           N  
ANISOU 1735  N   GLY B  87     8109  13695   8193  -2665   1187   -490       N  
ATOM   1736  CA  GLY B  87     -20.868  16.981 -27.214  1.00 78.16           C  
ANISOU 1736  CA  GLY B  87     7990  13618   8087  -2718    938   -313       C  
ATOM   1737  C   GLY B  87     -20.821  16.747 -28.713  1.00 77.26           C  
ANISOU 1737  C   GLY B  87     8072  13191   8089  -2833    871   -257       C  
ATOM   1738  O   GLY B  87     -19.988  15.983 -29.210  1.00 76.61           O  
ANISOU 1738  O   GLY B  87     8062  13045   8001  -2861    754   -358       O  
ATOM   1739  N   ILE B  88     -21.725  17.414 -29.429  1.00 77.56           N  
ANISOU 1739  N   ILE B  88     8177  13123   8168  -2813    961    -87       N  
ATOM   1740  CA  ILE B  88     -21.857  17.238 -30.875  1.00 77.74           C  
ANISOU 1740  CA  ILE B  88     8316  13023   8196  -2836    891     -8       C  
ATOM   1741  C   ILE B  88     -20.553  17.714 -31.540  1.00 78.03           C  
ANISOU 1741  C   ILE B  88     8470  12916   8258  -2846   1059   -269       C  
ATOM   1742  O   ILE B  88     -19.970  17.012 -32.360  1.00 77.68           O  
ANISOU 1742  O   ILE B  88     8489  12867   8157  -2845    915   -344       O  
ATOM   1743  CB  ILE B  88     -23.132  17.931 -31.422  1.00 78.81           C  
ANISOU 1743  CB  ILE B  88     8413  13262   8266  -2699    989    290       C  
ATOM   1744  CG1 ILE B  88     -24.384  17.297 -30.811  1.00 80.08           C  
ANISOU 1744  CG1 ILE B  88     8357  13687   8382  -2746    790    575       C  
ATOM   1745  CG2 ILE B  88     -23.211  17.798 -32.926  1.00 80.09           C  
ANISOU 1745  CG2 ILE B  88     8626  13476   8327  -2642    919    343       C  
ATOM   1746  CD1 ILE B  88     -25.713  17.944 -31.240  1.00 81.71           C  
ANISOU 1746  CD1 ILE B  88     8420  14194   8433  -2555    875    910       C  
ATOM   1747  N   ALA B  89     -20.076  18.882 -31.124  1.00 79.84           N  
ANISOU 1747  N   ALA B  89     8716  13035   8585  -2873   1376   -433       N  
ATOM   1748  CA  ALA B  89     -18.756  19.383 -31.506  1.00 81.43           C  
ANISOU 1748  CA  ALA B  89     8937  13134   8868  -2996   1577   -688       C  
ATOM   1749  C   ALA B  89     -17.624  18.338 -31.483  1.00 81.24           C  
ANISOU 1749  C   ALA B  89     8812  13338   8716  -3038   1354   -883       C  
ATOM   1750  O   ALA B  89     -17.012  18.081 -32.523  1.00 81.52           O  
ANISOU 1750  O   ALA B  89     8891  13393   8690  -2985   1349   -858       O  
ATOM   1751  CB  ALA B  89     -18.396  20.563 -30.644  1.00 83.75           C  
ANISOU 1751  CB  ALA B  89     9210  13275   9334  -3150   1885   -980       C  
ATOM   1752  N   TYR B  90     -17.344  17.742 -30.322  1.00 81.73           N  
ANISOU 1752  N   TYR B  90     8727  13642   8682  -3039   1201  -1033       N  
ATOM   1753  CA  TYR B  90     -16.191  16.819 -30.196  1.00 83.32           C  
ANISOU 1753  CA  TYR B  90     8819  14128   8711  -2963   1058  -1177       C  
ATOM   1754  C   TYR B  90     -16.250  15.627 -31.158  1.00 82.93           C  
ANISOU 1754  C   TYR B  90     8958  13964   8586  -2781    840   -996       C  
ATOM   1755  O   TYR B  90     -15.234  15.234 -31.761  1.00 83.80           O  
ANISOU 1755  O   TYR B  90     9068  14208   8562  -2663    827  -1099       O  
ATOM   1756  CB  TYR B  90     -16.005  16.309 -28.762  1.00 84.33           C  
ANISOU 1756  CB  TYR B  90     8738  14627   8675  -2856    958  -1255       C  
ATOM   1757  CG  TYR B  90     -15.780  17.388 -27.730  1.00 88.46           C  
ANISOU 1757  CG  TYR B  90     9031  15397   9182  -3008   1122  -1603       C  
ATOM   1758  CD1 TYR B  90     -16.857  17.978 -27.083  1.00 90.01           C  
ANISOU 1758  CD1 TYR B  90     9262  15487   9451  -3002   1184  -1552       C  
ATOM   1759  CD2 TYR B  90     -14.488  17.811 -27.387  1.00 92.87           C  
ANISOU 1759  CD2 TYR B  90     9305  16358   9623  -3153   1209  -2035       C  
ATOM   1760  CE1 TYR B  90     -16.665  18.969 -26.127  1.00 94.03           C  
ANISOU 1760  CE1 TYR B  90     9604  16194   9926  -3107   1329  -1981       C  
ATOM   1761  CE2 TYR B  90     -14.284  18.807 -26.420  1.00 97.03           C  
ANISOU 1761  CE2 TYR B  90     9607  17117  10142  -3360   1333  -2506       C  
ATOM   1762  CZ  TYR B  90     -15.379  19.380 -25.797  1.00 97.81           C  
ANISOU 1762  CZ  TYR B  90     9821  17016  10324  -3318   1393  -2505       C  
ATOM   1763  OH  TYR B  90     -15.193  20.362 -24.850  1.00102.08           O  
ANISOU 1763  OH  TYR B  90    10188  17754  10843  -3485   1511  -3069       O  
ATOM   1764  N   VAL B  91     -17.446  15.061 -31.289  1.00 82.60           N  
ANISOU 1764  N   VAL B  91     9053  13708   8621  -2765    671   -765       N  
ATOM   1765  CA  VAL B  91     -17.685  13.967 -32.220  1.00 83.71           C  
ANISOU 1765  CA  VAL B  91     9396  13665   8743  -2677    445   -712       C  
ATOM   1766  C   VAL B  91     -17.359  14.350 -33.669  1.00 84.34           C  
ANISOU 1766  C   VAL B  91     9559  13767   8719  -2600    490   -800       C  
ATOM   1767  O   VAL B  91     -16.752  13.568 -34.409  1.00 85.46           O  
ANISOU 1767  O   VAL B  91     9830  13918   8723  -2417    368   -930       O  
ATOM   1768  CB  VAL B  91     -19.132  13.445 -32.119  1.00 84.26           C  
ANISOU 1768  CB  VAL B  91     9508  13553   8954  -2813    267   -496       C  
ATOM   1769  CG1 VAL B  91     -19.271  12.527 -30.902  1.00 85.78           C  
ANISOU 1769  CG1 VAL B  91     9667  13686   9238  -2801    206   -324       C  
ATOM   1770  CG2 VAL B  91     -20.100  14.592 -32.030  1.00 83.35           C  
ANISOU 1770  CG2 VAL B  91     9258  13538   8871  -2906    403   -341       C  
ATOM   1771  N   LYS B  92     -17.755  15.553 -34.064  1.00 84.23           N  
ANISOU 1771  N   LYS B  92     9479  13779   8746  -2663    703   -696       N  
ATOM   1772  CA  LYS B  92     -17.474  16.010 -35.409  1.00 86.46           C  
ANISOU 1772  CA  LYS B  92     9791  14159   8898  -2514    822   -657       C  
ATOM   1773  C   LYS B  92     -15.973  16.306 -35.569  1.00 87.56           C  
ANISOU 1773  C   LYS B  92     9842  14449   8975  -2472   1023   -780       C  
ATOM   1774  O   LYS B  92     -15.365  15.930 -36.565  1.00 89.33           O  
ANISOU 1774  O   LYS B  92    10094  14856   8989  -2247    988   -810       O  
ATOM   1775  CB  LYS B  92     -18.338  17.224 -35.747  1.00 87.25           C  
ANISOU 1775  CB  LYS B  92     9859  14226   9065  -2502   1079   -392       C  
ATOM   1776  CG  LYS B  92     -19.848  16.933 -35.752  1.00 87.85           C  
ANISOU 1776  CG  LYS B  92     9919  14355   9102  -2495    871   -234       C  
ATOM   1777  CD  LYS B  92     -20.249  15.961 -36.867  1.00 90.60           C  
ANISOU 1777  CD  LYS B  92    10286  14917   9217  -2383    539   -330       C  
ATOM   1778  CE  LYS B  92     -21.758  15.900 -37.025  1.00 92.59           C  
ANISOU 1778  CE  LYS B  92    10400  15384   9395  -2423    373   -172       C  
ATOM   1779  NZ  LYS B  92     -22.146  14.814 -37.966  1.00 95.86           N  
ANISOU 1779  NZ  LYS B  92    10797  16012   9613  -2442    -20   -435       N  
ATOM   1780  N   THR B  93     -15.384  16.932 -34.555  1.00 87.47           N  
ANISOU 1780  N   THR B  93     9679  14444   9109  -2687   1213   -888       N  
ATOM   1781  CA  THR B  93     -13.996  17.362 -34.578  1.00 89.62           C  
ANISOU 1781  CA  THR B  93     9750  14946   9354  -2774   1426  -1029       C  
ATOM   1782  C   THR B  93     -13.031  16.317 -33.998  1.00 90.10           C  
ANISOU 1782  C   THR B  93     9689  15357   9188  -2636   1223  -1229       C  
ATOM   1783  O   THR B  93     -12.219  16.629 -33.120  1.00 91.81           O  
ANISOU 1783  O   THR B  93     9631  15862   9391  -2805   1316  -1434       O  
ATOM   1784  CB  THR B  93     -13.848  18.698 -33.821  1.00 91.00           C  
ANISOU 1784  CB  THR B  93     9783  14973   9817  -3147   1756  -1146       C  
ATOM   1785  OG1 THR B  93     -14.906  19.586 -34.207  1.00 90.86           O  
ANISOU 1785  OG1 THR B  93     9953  14565  10004  -3151   1972   -898       O  
ATOM   1786  CG2 THR B  93     -12.496  19.348 -34.118  1.00 95.57           C  
ANISOU 1786  CG2 THR B  93    10104  15753  10453  -3370   2045  -1263       C  
ATOM   1787  N   GLY B  94     -13.127  15.075 -34.477  1.00 89.95           N  
ANISOU 1787  N   GLY B  94     9869  15335   8973  -2303    960  -1194       N  
ATOM   1788  CA  GLY B  94     -12.131  14.026 -34.167  1.00 91.51           C  
ANISOU 1788  CA  GLY B  94    10021  15837   8909  -2000    839  -1301       C  
ATOM   1789  C   GLY B  94     -12.142  13.359 -32.789  1.00 91.13           C  
ANISOU 1789  C   GLY B  94     9920  15865   8838  -1930    734  -1316       C  
ATOM   1790  O   GLY B  94     -11.811  12.170 -32.677  1.00 92.93           O  
ANISOU 1790  O   GLY B  94    10297  16112   8898  -1549    610  -1272       O  
ATOM   1791  N   ALA B  95     -12.495  14.131 -31.752  1.00 89.56           N  
ANISOU 1791  N   ALA B  95     9519  15726   8784  -2227    820  -1361       N  
ATOM   1792  CA  ALA B  95     -12.627  13.650 -30.373  1.00 89.20           C  
ANISOU 1792  CA  ALA B  95     9353  15876   8664  -2120    751  -1326       C  
ATOM   1793  C   ALA B  95     -13.954  12.901 -30.160  1.00 87.30           C  
ANISOU 1793  C   ALA B  95     9408  15145   8617  -2078    600  -1051       C  
ATOM   1794  O   ALA B  95     -14.820  13.320 -29.397  1.00 85.39           O  
ANISOU 1794  O   ALA B  95     9092  14848   8504  -2247    615   -967       O  
ATOM   1795  CB  ALA B  95     -12.510  14.816 -29.418  1.00 89.99           C  
ANISOU 1795  CB  ALA B  95     9108  16289   8794  -2433    892  -1567       C  
ATOM   1796  N   VAL B  96     -14.079  11.781 -30.863  1.00 88.17           N  
ANISOU 1796  N   VAL B  96     9839  14914   8747  -1858    466   -939       N  
ATOM   1797  CA  VAL B  96     -15.245  10.924 -30.823  1.00 88.31           C  
ANISOU 1797  CA  VAL B  96    10129  14415   9008  -1911    323   -721       C  
ATOM   1798  C   VAL B  96     -15.514  10.481 -29.382  1.00 89.72           C  
ANISOU 1798  C   VAL B  96    10174  14707   9205  -1800    378   -436       C  
ATOM   1799  O   VAL B  96     -16.601  10.706 -28.856  1.00 89.12           O  
ANISOU 1799  O   VAL B  96    10030  14520   9309  -2024    363   -244       O  
ATOM   1800  CB  VAL B  96     -15.051   9.695 -31.744  1.00 91.13           C  
ANISOU 1800  CB  VAL B  96    10874  14368   9380  -1674    195   -781       C  
ATOM   1801  CG1 VAL B  96     -16.227   8.744 -31.630  1.00 92.92           C  
ANISOU 1801  CG1 VAL B  96    11362  13992   9948  -1850     65   -609       C  
ATOM   1802  CG2 VAL B  96     -14.846  10.133 -33.200  1.00 90.72           C  
ANISOU 1802  CG2 VAL B  96    10904  14346   9216  -1698    134  -1048       C  
ATOM   1803  N   ASP B  97     -14.509   9.882 -28.748  1.00 92.40           N  
ANISOU 1803  N   ASP B  97    10428  15385   9293  -1381    465   -363       N  
ATOM   1804  CA  ASP B  97     -14.640   9.310 -27.401  1.00 94.88           C  
ANISOU 1804  CA  ASP B  97    10598  15915   9534  -1106    562      1       C  
ATOM   1805  C   ASP B  97     -15.016  10.328 -26.319  1.00 92.67           C  
ANISOU 1805  C   ASP B  97     9900  16170   9138  -1263    615    -22       C  
ATOM   1806  O   ASP B  97     -15.870  10.043 -25.478  1.00 93.76           O  
ANISOU 1806  O   ASP B  97     9978  16276   9367  -1230    652    340       O  
ATOM   1807  CB  ASP B  97     -13.373   8.527 -27.007  1.00 99.54           C  
ANISOU 1807  CB  ASP B  97    11131  16928   9760   -487    680    107       C  
ATOM   1808  CG  ASP B  97     -13.309   7.125 -27.642  1.00104.53           C  
ANISOU 1808  CG  ASP B  97    12294  16850  10573   -165    699    313       C  
ATOM   1809  OD1 ASP B  97     -13.693   6.955 -28.825  1.00105.43           O  
ANISOU 1809  OD1 ASP B  97    12770  16338  10949   -427    559     85       O  
ATOM   1810  OD2 ASP B  97     -12.859   6.186 -26.952  1.00110.31           O  
ANISOU 1810  OD2 ASP B  97    13084  17666  11160    402    875    692       O  
ATOM   1811  N   ARG B  98     -14.384  11.503 -26.346  1.00 79.42           N  
ANISOU 1811  N   ARG B  98    10182  11309   8683   -139   -187    684       N  
ATOM   1812  CA  ARG B  98     -14.728  12.599 -25.435  1.00 77.17           C  
ANISOU 1812  CA  ARG B  98     9885  11110   8325   -164   -351    678       C  
ATOM   1813  C   ARG B  98     -16.179  13.020 -25.617  1.00 73.62           C  
ANISOU 1813  C   ARG B  98     9588  10719   7663   -176   -385    648       C  
ATOM   1814  O   ARG B  98     -16.888  13.271 -24.639  1.00 72.79           O  
ANISOU 1814  O   ARG B  98     9497  10678   7481   -185   -506    643       O  
ATOM   1815  CB  ARG B  98     -13.828  13.804 -25.685  1.00 79.18           C  
ANISOU 1815  CB  ARG B  98    10050  11296   8735   -203   -286    649       C  
ATOM   1816  CG  ARG B  98     -13.781  14.832 -24.557  1.00 82.16           C  
ANISOU 1816  CG  ARG B  98    10328  11736   9152   -255   -438    563       C  
ATOM   1817  CD  ARG B  98     -12.788  15.978 -24.864  1.00 89.65           C  
ANISOU 1817  CD  ARG B  98    11125  12546  10388   -314   -311    486       C  
ATOM   1818  NE  ARG B  98     -11.356  15.631 -24.770  1.00 95.57           N  
ANISOU 1818  NE  ARG B  98    11646  13243  11423   -317   -309    454       N  
ATOM   1819  CZ  ARG B  98     -10.593  15.153 -25.764  1.00 98.69           C  
ANISOU 1819  CZ  ARG B  98    12017  13490  11988   -283    -97    537       C  
ATOM   1820  NH1 ARG B  98     -11.095  14.908 -26.972  1.00 97.84           N  
ANISOU 1820  NH1 ARG B  98    12127  13317  11731   -237    119    639       N  
ATOM   1821  NH2 ARG B  98      -9.307  14.897 -25.540  1.00101.94           N  
ANISOU 1821  NH2 ARG B  98    12172  13841  12719   -287   -108    503       N  
ATOM   1822  N   GLY B  99     -16.614  13.104 -26.874  1.00 71.32           N  
ANISOU 1822  N   GLY B  99     9403  10428   7267   -162   -278    631       N  
ATOM   1823  CA  GLY B  99     -17.978  13.521 -27.204  1.00 67.29           C  
ANISOU 1823  CA  GLY B  99     8995  10003   6569   -148   -334    616       C  
ATOM   1824  C   GLY B  99     -19.019  12.458 -26.905  1.00 64.27           C  
ANISOU 1824  C   GLY B  99     8620   9654   6144   -160   -410    534       C  
ATOM   1825  O   GLY B  99     -20.122  12.781 -26.473  1.00 62.39           O  
ANISOU 1825  O   GLY B  99     8399   9451   5854   -164   -496    527       O  
ATOM   1826  N   THR B 100     -18.674  11.197 -27.160  1.00 63.23           N  
ANISOU 1826  N   THR B 100     8454   9471   6099   -168   -332    465       N  
ATOM   1827  CA  THR B 100     -19.507  10.075 -26.786  1.00 62.30           C  
ANISOU 1827  CA  THR B 100     8297   9307   6068   -185   -325    381       C  
ATOM   1828  C   THR B 100     -19.858  10.204 -25.290  1.00 61.00           C  
ANISOU 1828  C   THR B 100     8107   9115   5954   -163   -394    505       C  
ATOM   1829  O   THR B 100     -21.043  10.240 -24.913  1.00 60.25           O  
ANISOU 1829  O   THR B 100     8026   9020   5845   -173   -430    472       O  
ATOM   1830  CB  THR B 100     -18.799   8.737 -27.056  1.00 63.48           C  
ANISOU 1830  CB  THR B 100     8374   9329   6414   -191   -156    325       C  
ATOM   1831  OG1 THR B 100     -18.578   8.597 -28.450  1.00 64.63           O  
ANISOU 1831  OG1 THR B 100     8566   9523   6466   -217    -70    160       O  
ATOM   1832  CG2 THR B 100     -19.646   7.566 -26.605  1.00 65.11           C  
ANISOU 1832  CG2 THR B 100     8506   9417   6814   -205    -73    250       C  
ATOM   1833  N   GLU B 101     -18.825  10.323 -24.456  1.00 60.48           N  
ANISOU 1833  N   GLU B 101     7997   9048   5934   -126   -415    636       N  
ATOM   1834  CA  GLU B 101     -19.004  10.403 -23.017  1.00 59.91           C  
ANISOU 1834  CA  GLU B 101     7918   9020   5823    -78   -487    747       C  
ATOM   1835  C   GLU B 101     -19.847  11.605 -22.590  1.00 57.99           C  
ANISOU 1835  C   GLU B 101     7749   8845   5438   -117   -577    701       C  
ATOM   1836  O   GLU B 101     -20.642  11.506 -21.644  1.00 57.83           O  
ANISOU 1836  O   GLU B 101     7768   8833   5370    -89   -572    741       O  
ATOM   1837  CB  GLU B 101     -17.657  10.365 -22.286  1.00 61.80           C  
ANISOU 1837  CB  GLU B 101     8063   9327   6091    -16   -553    861       C  
ATOM   1838  CG  GLU B 101     -16.961   8.994 -22.390  1.00 65.38           C  
ANISOU 1838  CG  GLU B 101     8417   9680   6743     64   -426    980       C  
ATOM   1839  CD  GLU B 101     -15.655   8.902 -21.596  0.37 69.67           C  
ANISOU 1839  CD  GLU B 101     8818  10327   7326    164   -529   1132       C  
ATOM   1840  OE1 GLU B 101     -14.936   7.884 -21.753  0.72 72.25           O  
ANISOU 1840  OE1 GLU B 101     9030  10554   7869    244   -412   1260       O  
ATOM   1841  OE2 GLU B 101     -15.345   9.838 -20.820  0.69 71.11           O  
ANISOU 1841  OE2 GLU B 101     8977  10693   7348    163   -727   1101       O  
ATOM   1842  N   LEU B 102     -19.707  12.732 -23.278  1.00 56.03           N  
ANISOU 1842  N   LEU B 102     7518   8618   5154   -167   -606    638       N  
ATOM   1843  CA  LEU B 102     -20.520  13.875 -22.910  1.00 54.58           C  
ANISOU 1843  CA  LEU B 102     7377   8449   4909   -199   -639    606       C  
ATOM   1844  C   LEU B 102     -21.966  13.686 -23.355  1.00 53.05           C  
ANISOU 1844  C   LEU B 102     7221   8225   4710   -195   -618    584       C  
ATOM   1845  O   LEU B 102     -22.901  14.169 -22.702  1.00 53.20           O  
ANISOU 1845  O   LEU B 102     7261   8222   4729   -204   -615    580       O  
ATOM   1846  CB  LEU B 102     -19.976  15.155 -23.509  1.00 55.40           C  
ANISOU 1846  CB  LEU B 102     7461   8532   5054   -231   -610    588       C  
ATOM   1847  CG  LEU B 102     -20.713  16.398 -23.017  1.00 56.37           C  
ANISOU 1847  CG  LEU B 102     7598   8622   5198   -266   -589    556       C  
ATOM   1848  CD1 LEU B 102     -20.466  16.593 -21.529  1.00 56.29           C  
ANISOU 1848  CD1 LEU B 102     7568   8666   5153   -307   -648    460       C  
ATOM   1849  CD2 LEU B 102     -20.224  17.599 -23.777  1.00 59.17           C  
ANISOU 1849  CD2 LEU B 102     7913   8892   5674   -274   -478    580       C  
ATOM   1850  N   LEU B 103     -22.148  12.986 -24.468  1.00 51.68           N  
ANISOU 1850  N   LEU B 103     7034   8057   4544   -186   -603    537       N  
ATOM   1851  CA  LEU B 103     -23.489  12.718 -24.950  1.00 50.69           C  
ANISOU 1851  CA  LEU B 103     6883   7940   4434   -186   -628    456       C  
ATOM   1852  C   LEU B 103     -24.188  11.682 -24.081  1.00 49.91           C  
ANISOU 1852  C   LEU B 103     6743   7734   4487   -197   -560    425       C  
ATOM   1853  O   LEU B 103     -25.397  11.706 -23.971  1.00 49.08           O  
ANISOU 1853  O   LEU B 103     6591   7589   4466   -207   -562    371       O  
ATOM   1854  CB  LEU B 103     -23.478  12.294 -26.411  1.00 51.65           C  
ANISOU 1854  CB  LEU B 103     6989   8158   4475   -176   -654    346       C  
ATOM   1855  CG  LEU B 103     -23.120  13.431 -27.381  1.00 52.95           C  
ANISOU 1855  CG  LEU B 103     7213   8441   4462   -115   -678    437       C  
ATOM   1856  CD1 LEU B 103     -23.092  12.914 -28.804  1.00 55.53           C  
ANISOU 1856  CD1 LEU B 103     7557   8926   4616    -79   -697    320       C  
ATOM   1857  CD2 LEU B 103     -24.037  14.643 -27.278  1.00 52.88           C  
ANISOU 1857  CD2 LEU B 103     7194   8460   4435    -67   -730    547       C  
ATOM   1858  N   GLU B 104     -23.412  10.805 -23.449  1.00 49.57           N  
ANISOU 1858  N   GLU B 104     6697   7627   4510   -174   -472    491       N  
ATOM   1859  CA  GLU B 104     -23.954   9.796 -22.570  1.00 50.68           C  
ANISOU 1859  CA  GLU B 104     6804   7634   4815   -142   -331    539       C  
ATOM   1860  C   GLU B 104     -24.455  10.441 -21.274  1.00 49.96           C  
ANISOU 1860  C   GLU B 104     6788   7552   4641   -105   -315    654       C  
ATOM   1861  O   GLU B 104     -25.458   9.999 -20.673  1.00 50.01           O  
ANISOU 1861  O   GLU B 104     6782   7434   4783    -83   -176    677       O  
ATOM   1862  CB  GLU B 104     -22.901   8.730 -22.300  1.00 52.35           C  
ANISOU 1862  CB  GLU B 104     6983   7785   5120    -82   -219    649       C  
ATOM   1863  CG  GLU B 104     -22.595   7.874 -23.554  1.00 56.72           C  
ANISOU 1863  CG  GLU B 104     7452   8268   5828   -135   -148    481       C  
ATOM   1864  CD  GLU B 104     -21.367   6.956 -23.406  1.00 62.15           C  
ANISOU 1864  CD  GLU B 104     8088   8873   6653    -71    -16    609       C  
ATOM   1865  OE1 GLU B 104     -20.354   7.359 -22.778  1.00 63.75           O  
ANISOU 1865  OE1 GLU B 104     8313   9172   6736      1    -97    797       O  
ATOM   1866  OE2 GLU B 104     -21.417   5.823 -23.932  1.00 64.81           O  
ANISOU 1866  OE2 GLU B 104     8329   9041   7254    -97    174    499       O  
ATOM   1867  N   ARG B 105     -23.757  11.496 -20.865  1.00 49.00           N  
ANISOU 1867  N   ARG B 105     6733   7561   4323   -105   -426    694       N  
ATOM   1868  CA  ARG B 105     -24.146  12.286 -19.700  1.00 49.09           C  
ANISOU 1868  CA  ARG B 105     6824   7615   4213    -92   -415    726       C  
ATOM   1869  C   ARG B 105     -25.421  13.040 -20.019  1.00 48.34           C  
ANISOU 1869  C   ARG B 105     6717   7435   4211   -149   -389    642       C  
ATOM   1870  O   ARG B 105     -26.303  13.113 -19.177  1.00 48.07           O  
ANISOU 1870  O   ARG B 105     6723   7330   4210   -133   -273    663       O  
ATOM   1871  CB  ARG B 105     -23.035  13.255 -19.316  1.00 49.60           C  
ANISOU 1871  CB  ARG B 105     6907   7831   4107   -112   -541    693       C  
ATOM   1872  CG  ARG B 105     -23.361  14.196 -18.199  1.00 52.42           C  
ANISOU 1872  CG  ARG B 105     7336   8253   4327   -130   -529    631       C  
ATOM   1873  CD  ARG B 105     -23.420  13.471 -16.843  1.00 59.29           C  
ANISOU 1873  CD  ARG B 105     8292   9224   5010    -14   -466    748       C  
ATOM   1874  NE  ARG B 105     -24.022  14.305 -15.792  1.00 63.52           N  
ANISOU 1874  NE  ARG B 105     8929   9815   5390    -32   -400    655       N  
ATOM   1875  CZ  ARG B 105     -25.330  14.545 -15.650  1.00 62.71           C  
ANISOU 1875  CZ  ARG B 105     8878   9544   5403    -58   -221    641       C  
ATOM   1876  NH1 ARG B 105     -25.742  15.335 -14.661  1.00 63.19           N  
ANISOU 1876  NH1 ARG B 105     9037   9654   5318    -80   -132    532       N  
ATOM   1877  NH2 ARG B 105     -26.227  14.014 -16.489  1.00 58.48           N  
ANISOU 1877  NH2 ARG B 105     8276   8798   5146    -69   -130    700       N  
ATOM   1878  N   SER B 106     -25.536  13.546 -21.255  1.00 47.41           N  
ANISOU 1878  N   SER B 106     6541   7332   4141   -190   -479    573       N  
ATOM   1879  CA  SER B 106     -26.714  14.296 -21.673  1.00 47.33           C  
ANISOU 1879  CA  SER B 106     6480   7274   4229   -206   -485    539       C  
ATOM   1880  C   SER B 106     -27.950  13.422 -21.687  1.00 47.98           C  
ANISOU 1880  C   SER B 106     6472   7247   4509   -203   -420    485       C  
ATOM   1881  O   SER B 106     -29.005  13.806 -21.175  1.00 49.07           O  
ANISOU 1881  O   SER B 106     6579   7282   4780   -206   -337    488       O  
ATOM   1882  CB  SER B 106     -26.493  14.889 -23.055  1.00 47.96           C  
ANISOU 1882  CB  SER B 106     6516   7446   4260   -193   -596    537       C  
ATOM   1883  OG  SER B 106     -25.262  15.593 -23.088  1.00 48.25           O  
ANISOU 1883  OG  SER B 106     6607   7525   4199   -200   -597    581       O  
ATOM   1884  N   ILE B 107     -27.811  12.231 -22.252  1.00 48.06           N  
ANISOU 1884  N   ILE B 107     6415   7248   4597   -208   -422    411       N  
ATOM   1885  CA  ILE B 107     -28.921  11.316 -22.353  1.00 49.04           C  
ANISOU 1885  CA  ILE B 107     6398   7237   4998   -229   -338    293       C  
ATOM   1886  C   ILE B 107     -29.358  10.874 -20.929  1.00 48.88           C  
ANISOU 1886  C   ILE B 107     6426   7024   5121   -194    -87    408       C  
ATOM   1887  O   ILE B 107     -30.518  10.588 -20.716  1.00 49.33           O  
ANISOU 1887  O   ILE B 107     6371   6916   5456   -209     38    348       O  
ATOM   1888  CB  ILE B 107     -28.618  10.148 -23.384  1.00 50.48           C  
ANISOU 1888  CB  ILE B 107     6472   7437   5270   -265   -367    112       C  
ATOM   1889  CG1 ILE B 107     -29.861   9.753 -24.179  1.00 53.57           C  
ANISOU 1889  CG1 ILE B 107     6643   7815   5896   -318   -435   -145       C  
ATOM   1890  CG2 ILE B 107     -28.050   8.890 -22.709  1.00 52.43           C  
ANISOU 1890  CG2 ILE B 107     6731   7511   5677   -246   -136    176       C  
ATOM   1891  CD1 ILE B 107     -30.573  10.889 -24.906  1.00 54.58           C  
ANISOU 1891  CD1 ILE B 107     6708   8136   5893   -290   -673   -167       C  
ATOM   1892  N   ALA B 108     -28.431  10.880 -19.968  1.00 48.50           N  
ANISOU 1892  N   ALA B 108     6536   7020   4870   -134    -15    577       N  
ATOM   1893  CA  ALA B 108     -28.735  10.629 -18.547  1.00 49.66           C  
ANISOU 1893  CA  ALA B 108     6785   7069   5011    -54    218    735       C  
ATOM   1894  C   ALA B 108     -29.599  11.724 -17.960  1.00 50.26           C  
ANISOU 1894  C   ALA B 108     6914   7117   5064    -76    265    717       C  
ATOM   1895  O   ALA B 108     -30.519  11.455 -17.202  1.00 51.94           O  
ANISOU 1895  O   ALA B 108     7136   7159   5439    -40    509    769       O  
ATOM   1896  CB  ALA B 108     -27.462  10.509 -17.741  1.00 49.64           C  
ANISOU 1896  CB  ALA B 108     6924   7231   4704     39    198    903       C  
ATOM   1897  N   ASP B 109     -29.288  12.969 -18.312  1.00 49.99           N  
ANISOU 1897  N   ASP B 109     6907   7214   4871   -131     84    649       N  
ATOM   1898  CA  ASP B 109     -30.084  14.113 -17.890  1.00 51.02           C  
ANISOU 1898  CA  ASP B 109     7056   7281   5045   -163    154    613       C  
ATOM   1899  C   ASP B 109     -31.450  14.205 -18.557  1.00 51.24           C  
ANISOU 1899  C   ASP B 109     6898   7149   5420   -191    178    553       C  
ATOM   1900  O   ASP B 109     -32.411  14.583 -17.900  1.00 52.60           O  
ANISOU 1900  O   ASP B 109     7062   7165   5758   -191    366    559       O  
ATOM   1901  CB  ASP B 109     -29.363  15.415 -18.158  1.00 50.75           C  
ANISOU 1901  CB  ASP B 109     7058   7375   4850   -211     11    562       C  
ATOM   1902  CG  ASP B 109     -30.156  16.616 -17.653  1.00 55.05           C  
ANISOU 1902  CG  ASP B 109     7608   7806   5500   -248    149    516       C  
ATOM   1903  OD1 ASP B 109     -30.725  17.367 -18.484  1.00 57.31           O  
ANISOU 1903  OD1 ASP B 109     7767   8022   5984   -261    106    521       O  
ATOM   1904  OD2 ASP B 109     -30.248  16.771 -16.408  1.00 60.90           O  
ANISOU 1904  OD2 ASP B 109     8481   8534   6123   -245    322    488       O  
ATOM   1905  N   ALA B 110     -31.518  13.910 -19.858  1.00 52.12           N  
ANISOU 1905  N   ALA B 110     5642   7545   6614    176   -622   -858       N  
ATOM   1906  CA  ALA B 110     -32.789  13.924 -20.616  1.00 52.47           C  
ANISOU 1906  CA  ALA B 110     5738   7391   6807    185   -680   -904       C  
ATOM   1907  C   ALA B 110     -32.955  12.689 -21.499  1.00 52.63           C  
ANISOU 1907  C   ALA B 110     5798   7302   6897    192   -648   -816       C  
ATOM   1908  O   ALA B 110     -32.708  12.735 -22.706  1.00 51.89           O  
ANISOU 1908  O   ALA B 110     5791   7094   6831    184   -714   -818       O  
ATOM   1909  CB  ALA B 110     -32.935  15.187 -21.453  1.00 52.24           C  
ANISOU 1909  CB  ALA B 110     5841   7206   6802    178   -788  -1008       C  
ATOM   1910  N   PRO B 111     -33.402  11.582 -20.899  1.00 54.40           N  
ANISOU 1910  N   PRO B 111     5981   7547   7141    193   -525   -749       N  
ATOM   1911  CA  PRO B 111     -33.496  10.298 -21.591  1.00 55.89           C  
ANISOU 1911  CA  PRO B 111     6240   7598   7395    172   -441   -680       C  
ATOM   1912  C   PRO B 111     -34.327  10.342 -22.890  1.00 57.16           C  
ANISOU 1912  C   PRO B 111     6388   7651   7679    121   -523   -819       C  
ATOM   1913  O   PRO B 111     -34.096   9.535 -23.806  1.00 57.09           O  
ANISOU 1913  O   PRO B 111     6440   7536   7714    101   -497   -797       O  
ATOM   1914  CB  PRO B 111     -34.168   9.405 -20.547  1.00 57.50           C  
ANISOU 1914  CB  PRO B 111     6442   7808   7598    130   -256   -629       C  
ATOM   1915  CG  PRO B 111     -33.785  10.022 -19.240  1.00 56.89           C  
ANISOU 1915  CG  PRO B 111     6301   7929   7383    201   -253   -583       C  
ATOM   1916  CD  PRO B 111     -33.786  11.476 -19.479  1.00 55.11           C  
ANISOU 1916  CD  PRO B 111     5989   7777   7171    199   -426   -732       C  
ATOM   1917  N   ASP B 112     -35.268  11.280 -22.970  1.00 58.28           N  
ANISOU 1917  N   ASP B 112     6445   7847   7851    137   -628   -978       N  
ATOM   1918  CA  ASP B 112     -36.179  11.338 -24.111  1.00 60.29           C  
ANISOU 1918  CA  ASP B 112     6649   8087   8169    155   -720  -1140       C  
ATOM   1919  C   ASP B 112     -35.813  12.394 -25.160  1.00 59.25           C  
ANISOU 1919  C   ASP B 112     6632   7900   7981    278   -898  -1146       C  
ATOM   1920  O   ASP B 112     -36.555  12.606 -26.121  1.00 60.32           O  
ANISOU 1920  O   ASP B 112     6739   8062   8115    369  -1005  -1274       O  
ATOM   1921  CB  ASP B 112     -37.625  11.477 -23.624  1.00 62.92           C  
ANISOU 1921  CB  ASP B 112     6798   8571   8538    142   -711  -1352       C  
ATOM   1922  CG  ASP B 112     -38.084  10.261 -22.812  1.00 67.41           C  
ANISOU 1922  CG  ASP B 112     7294   9162   9155    -50   -478  -1361       C  
ATOM   1923  OD1 ASP B 112     -37.773   9.104 -23.209  1.00 70.51           O  
ANISOU 1923  OD1 ASP B 112     7774   9420   9597   -162   -339  -1291       O  
ATOM   1924  OD2 ASP B 112     -38.755  10.468 -21.775  1.00 71.24           O  
ANISOU 1924  OD2 ASP B 112     7665   9783   9620    -93   -413  -1440       O  
ATOM   1925  N   ASN B 113     -34.649  13.023 -24.983  1.00 57.82           N  
ANISOU 1925  N   ASN B 113     6584   7660   7723    274   -909  -1020       N  
ATOM   1926  CA  ASN B 113     -34.157  14.025 -25.922  1.00 57.14           C  
ANISOU 1926  CA  ASN B 113     6678   7470   7559    329  -1013  -1001       C  
ATOM   1927  C   ASN B 113     -33.673  13.430 -27.250  1.00 56.34           C  
ANISOU 1927  C   ASN B 113     6640   7322   7444    310  -1034   -953       C  
ATOM   1928  O   ASN B 113     -32.575  12.864 -27.369  1.00 55.58           O  
ANISOU 1928  O   ASN B 113     6560   7235   7321    219   -966   -860       O  
ATOM   1929  CB  ASN B 113     -33.074  14.898 -25.288  1.00 56.99           C  
ANISOU 1929  CB  ASN B 113     6766   7429   7456    250   -970   -945       C  
ATOM   1930  CG  ASN B 113     -32.718  16.087 -26.155  1.00 57.88           C  
ANISOU 1930  CG  ASN B 113     7136   7376   7481    259  -1022   -943       C  
ATOM   1931  OD1 ASN B 113     -32.229  15.935 -27.269  1.00 57.67           O  
ANISOU 1931  OD1 ASN B 113     7218   7289   7403    231  -1037   -886       O  
ATOM   1932  ND2 ASN B 113     -32.965  17.279 -25.645  1.00 60.13           N  
ANISOU 1932  ND2 ASN B 113     7547   7564   7732    296  -1031  -1006       N  
ATOM   1933  N   ILE B 114     -34.524  13.601 -28.245  1.00 56.95           N  
ANISOU 1933  N   ILE B 114     6731   7395   7512    431  -1141  -1042       N  
ATOM   1934  CA  ILE B 114     -34.304  13.140 -29.604  1.00 56.58           C  
ANISOU 1934  CA  ILE B 114     6723   7342   7432    445  -1184  -1037       C  
ATOM   1935  C   ILE B 114     -33.027  13.638 -30.256  1.00 56.32           C  
ANISOU 1935  C   ILE B 114     6898   7216   7285    379  -1174   -907       C  
ATOM   1936  O   ILE B 114     -32.345  12.869 -30.925  1.00 56.17           O  
ANISOU 1936  O   ILE B 114     6852   7229   7260    303  -1141   -874       O  
ATOM   1937  CB  ILE B 114     -35.510  13.513 -30.486  1.00 58.29           C  
ANISOU 1937  CB  ILE B 114     6915   7638   7594    654  -1327  -1181       C  
ATOM   1938  CG1 ILE B 114     -36.784  12.842 -29.939  1.00 57.76           C  
ANISOU 1938  CG1 ILE B 114     6566   7750   7629    657  -1309  -1387       C  
ATOM   1939  CG2 ILE B 114     -35.212  13.206 -31.966  1.00 58.00           C  
ANISOU 1939  CG2 ILE B 114     6938   7624   7475    692  -1385  -1171       C  
ATOM   1940  CD1 ILE B 114     -36.600  11.359 -29.593  1.00 56.43           C  
ANISOU 1940  CD1 ILE B 114     6250   7589   7602    422  -1137  -1404       C  
ATOM   1941  N   LYS B 115     -32.711  14.914 -30.082  1.00 56.95           N  
ANISOU 1941  N   LYS B 115     7191   7180   7267    387  -1182   -858       N  
ATOM   1942  CA  LYS B 115     -31.472  15.452 -30.619  1.00 57.95           C  
ANISOU 1942  CA  LYS B 115     7523   7226   7270    243  -1119   -770       C  
ATOM   1943  C   LYS B 115     -30.223  14.764 -30.047  1.00 56.52           C  
ANISOU 1943  C   LYS B 115     7194   7179   7100     45  -1005   -750       C  
ATOM   1944  O   LYS B 115     -29.293  14.442 -30.798  1.00 57.26           O  
ANISOU 1944  O   LYS B 115     7305   7333   7117    -56   -969   -726       O  
ATOM   1945  CB  LYS B 115     -31.404  16.952 -30.415  1.00 59.86           C  
ANISOU 1945  CB  LYS B 115     8061   7270   7411    240  -1092   -751       C  
ATOM   1946  CG  LYS B 115     -32.324  17.717 -31.341  1.00 65.08           C  
ANISOU 1946  CG  LYS B 115     8979   7778   7970    500  -1203   -730       C  
ATOM   1947  CD  LYS B 115     -32.980  18.944 -30.669  1.00 71.37           C  
ANISOU 1947  CD  LYS B 115     9987   8389   8740    656  -1221   -763       C  
ATOM   1948  CE  LYS B 115     -31.975  20.047 -30.325  1.00 75.33           C  
ANISOU 1948  CE  LYS B 115    10809   8647   9162    417  -1049   -724       C  
ATOM   1949  NZ  LYS B 115     -30.904  20.193 -31.375  1.00 78.11           N  
ANISOU 1949  NZ  LYS B 115    11400   8905   9370    202   -935   -626       N  
ATOM   1950  N   VAL B 116     -30.199  14.527 -28.735  1.00 55.32           N  
ANISOU 1950  N   VAL B 116     6887   7115   7014     24   -954   -771       N  
ATOM   1951  CA  VAL B 116     -29.056  13.841 -28.092  1.00 54.42           C  
ANISOU 1951  CA  VAL B 116     6623   7190   6864    -68   -865   -759       C  
ATOM   1952  C   VAL B 116     -28.971  12.414 -28.632  1.00 53.98           C  
ANISOU 1952  C   VAL B 116     6459   7187   6860      5   -868   -724       C  
ATOM   1953  O   VAL B 116     -27.936  11.969 -29.123  1.00 53.97           O  
ANISOU 1953  O   VAL B 116     6429   7298   6778    -35   -839   -721       O  
ATOM   1954  CB  VAL B 116     -29.215  13.768 -26.551  1.00 53.83           C  
ANISOU 1954  CB  VAL B 116     6411   7222   6820    -37   -819   -772       C  
ATOM   1955  CG1 VAL B 116     -28.129  12.900 -25.942  1.00 53.34           C  
ANISOU 1955  CG1 VAL B 116     6196   7394   6675    -23   -750   -747       C  
ATOM   1956  CG2 VAL B 116     -29.210  15.176 -25.917  1.00 55.76           C  
ANISOU 1956  CG2 VAL B 116     6745   7424   7014   -125   -799   -848       C  
ATOM   1957  N   ALA B 117     -30.101  11.720 -28.545  1.00 52.95           N  
ANISOU 1957  N   ALA B 117     6271   6984   6862     99   -886   -732       N  
ATOM   1958  CA  ALA B 117     -30.215  10.367 -29.014  1.00 53.28           C  
ANISOU 1958  CA  ALA B 117     6251   7011   6980    139   -851   -732       C  
ATOM   1959  C   ALA B 117     -29.732  10.217 -30.469  1.00 53.92           C  
ANISOU 1959  C   ALA B 117     6378   7098   7009    120   -902   -757       C  
ATOM   1960  O   ALA B 117     -29.004   9.276 -30.784  1.00 54.39           O  
ANISOU 1960  O   ALA B 117     6402   7204   7057    136   -857   -748       O  
ATOM   1961  CB  ALA B 117     -31.644   9.902 -28.859  1.00 53.27           C  
ANISOU 1961  CB  ALA B 117     6186   6937   7115    162   -840   -807       C  
ATOM   1962  N   THR B 118     -30.113  11.155 -31.336  1.00 54.48           N  
ANISOU 1962  N   THR B 118     6547   7128   7022    116   -993   -785       N  
ATOM   1963  CA  THR B 118     -29.725  11.118 -32.736  1.00 55.12           C  
ANISOU 1963  CA  THR B 118     6689   7235   7017    103  -1038   -800       C  
ATOM   1964  C   THR B 118     -28.230  11.076 -32.845  1.00 55.01           C  
ANISOU 1964  C   THR B 118     6682   7331   6885     -5   -974   -767       C  
ATOM   1965  O   THR B 118     -27.660  10.093 -33.313  1.00 54.75           O  
ANISOU 1965  O   THR B 118     6561   7386   6854      9   -952   -797       O  
ATOM   1966  CB  THR B 118     -30.268  12.358 -33.514  1.00 56.50           C  
ANISOU 1966  CB  THR B 118     7053   7336   7079    159  -1130   -789       C  
ATOM   1967  OG1 THR B 118     -31.671  12.199 -33.709  1.00 58.81           O  
ANISOU 1967  OG1 THR B 118     7268   7634   7441    318  -1220   -882       O  
ATOM   1968  CG2 THR B 118     -29.596  12.536 -34.883  1.00 56.13           C  
ANISOU 1968  CG2 THR B 118     7127   7325   6874    116  -1145   -764       C  
ATOM   1969  N   VAL B 119     -27.591  12.147 -32.400  1.00 55.61           N  
ANISOU 1969  N   VAL B 119     6852   7425   6851   -121   -932   -743       N  
ATOM   1970  CA  VAL B 119     -26.163  12.265 -32.582  1.00 56.87           C  
ANISOU 1970  CA  VAL B 119     6985   7763   6859   -273   -858   -778       C  
ATOM   1971  C   VAL B 119     -25.349  11.155 -31.912  1.00 56.45           C  
ANISOU 1971  C   VAL B 119     6714   7927   6807   -195   -820   -813       C  
ATOM   1972  O   VAL B 119     -24.346  10.720 -32.454  1.00 57.69           O  
ANISOU 1972  O   VAL B 119     6786   8278   6853   -224   -798   -876       O  
ATOM   1973  CB  VAL B 119     -25.666  13.627 -32.145  1.00 58.34           C  
ANISOU 1973  CB  VAL B 119     7306   7933   6926   -471   -776   -801       C  
ATOM   1974  CG1 VAL B 119     -26.013  13.886 -30.690  1.00 57.89           C  
ANISOU 1974  CG1 VAL B 119     7177   7870   6947   -429   -761   -810       C  
ATOM   1975  CG2 VAL B 119     -24.180  13.730 -32.386  1.00 60.16           C  
ANISOU 1975  CG2 VAL B 119     7459   8422   6976   -685   -673   -904       C  
ATOM   1976  N   LEU B 120     -25.783  10.688 -30.750  1.00 55.85           N  
ANISOU 1976  N   LEU B 120     6563   7828   6827    -68   -809   -774       N  
ATOM   1977  CA  LEU B 120     -25.057   9.646 -30.024  1.00 56.03           C  
ANISOU 1977  CA  LEU B 120     6448   8031   6809     86   -767   -771       C  
ATOM   1978  C   LEU B 120     -25.268   8.272 -30.674  1.00 55.91           C  
ANISOU 1978  C   LEU B 120     6440   7914   6886    238   -769   -752       C  
ATOM   1979  O   LEU B 120     -24.355   7.435 -30.715  1.00 56.83           O  
ANISOU 1979  O   LEU B 120     6490   8188   6914    380   -747   -777       O  
ATOM   1980  CB  LEU B 120     -25.505   9.625 -28.554  1.00 56.19           C  
ANISOU 1980  CB  LEU B 120     6439   8040   6871    181   -732   -710       C  
ATOM   1981  CG  LEU B 120     -24.985   8.600 -27.544  1.00 56.67           C  
ANISOU 1981  CG  LEU B 120     6425   8248   6858    418   -680   -654       C  
ATOM   1982  CD1 LEU B 120     -23.501   8.792 -27.278  1.00 58.88           C  
ANISOU 1982  CD1 LEU B 120     6539   8938   6895    461   -681   -761       C  
ATOM   1983  CD2 LEU B 120     -25.783   8.757 -26.257  1.00 55.62           C  
ANISOU 1983  CD2 LEU B 120     6309   8041   6779    460   -640   -577       C  
ATOM   1984  N   GLY B 121     -26.481   8.038 -31.158  1.00 54.58           N  
ANISOU 1984  N   GLY B 121     6348   7506   6884    221   -788   -740       N  
ATOM   1985  CA  GLY B 121     -26.809   6.781 -31.809  1.00 54.49           C  
ANISOU 1985  CA  GLY B 121     6351   7372   6980    303   -758   -772       C  
ATOM   1986  C   GLY B 121     -26.016   6.543 -33.093  1.00 54.90           C  
ANISOU 1986  C   GLY B 121     6367   7546   6944    290   -800   -855       C  
ATOM   1987  O   GLY B 121     -25.589   5.416 -33.350  1.00 55.19           O  
ANISOU 1987  O   GLY B 121     6397   7576   6997    415   -757   -891       O  
ATOM   1988  N   LEU B 122     -25.828   7.597 -33.892  1.00 54.36           N  
ANISOU 1988  N   LEU B 122     6309   7572   6771    146   -867   -885       N  
ATOM   1989  CA  LEU B 122     -25.047   7.511 -35.124  1.00 55.49           C  
ANISOU 1989  CA  LEU B 122     6418   7870   6793     97   -893   -965       C  
ATOM   1990  C   LEU B 122     -23.557   7.322 -34.813  1.00 57.12           C  
ANISOU 1990  C   LEU B 122     6512   8358   6830    127   -854  -1016       C  
ATOM   1991  O   LEU B 122     -22.900   6.456 -35.401  1.00 57.98           O  
ANISOU 1991  O   LEU B 122     6541   8594   6892    227   -854  -1102       O  
ATOM   1992  CB  LEU B 122     -25.304   8.724 -36.026  1.00 55.32           C  
ANISOU 1992  CB  LEU B 122     6507   7842   6668    -60   -943   -954       C  
ATOM   1993  CG  LEU B 122     -26.776   8.920 -36.412  1.00 54.75           C  
ANISOU 1993  CG  LEU B 122     6510   7585   6705     -5  -1014   -942       C  
ATOM   1994  CD1 LEU B 122     -27.042  10.300 -37.032  1.00 55.39           C  
ANISOU 1994  CD1 LEU B 122     6782   7625   6638    -71  -1059   -880       C  
ATOM   1995  CD2 LEU B 122     -27.213   7.815 -37.330  1.00 54.18           C  
ANISOU 1995  CD2 LEU B 122     6344   7524   6716     68  -1041  -1056       C  
ATOM   1996  N   THR B 123     -23.038   8.104 -33.861  1.00 58.07           N  
ANISOU 1996  N   THR B 123     6599   8615   6849     59   -822  -1001       N  
ATOM   1997  CA  THR B 123     -21.688   7.876 -33.324  1.00 59.97           C  
ANISOU 1997  CA  THR B 123     6667   9214   6904    133   -789  -1097       C  
ATOM   1998  C   THR B 123     -21.456   6.426 -32.917  1.00 60.77           C  
ANISOU 1998  C   THR B 123     6721   9333   7035    477   -790  -1083       C  
ATOM   1999  O   THR B 123     -20.430   5.831 -33.255  1.00 62.30           O  
ANISOU 1999  O   THR B 123     6788   9800   7081    618   -799  -1199       O  
ATOM   2000  CB  THR B 123     -21.434   8.733 -32.123  1.00 60.01           C  
ANISOU 2000  CB  THR B 123     6622   9349   6828     55   -750  -1102       C  
ATOM   2001  OG1 THR B 123     -21.786  10.072 -32.448  1.00 61.30           O  
ANISOU 2001  OG1 THR B 123     6916   9386   6986   -246   -722  -1098       O  
ATOM   2002  CG2 THR B 123     -19.979   8.690 -31.738  1.00 62.70           C  
ANISOU 2002  CG2 THR B 123     6725  10180   6918     90   -722  -1278       C  
ATOM   2003  N   TYR B 124     -22.393   5.844 -32.186  1.00 60.39           N  
ANISOU 2003  N   TYR B 124     6797   8990   7156    623   -763   -950       N  
ATOM   2004  CA  TYR B 124     -22.187   4.464 -31.802  1.00 62.52           C  
ANISOU 2004  CA  TYR B 124     7123   9191   7438    952   -720   -909       C  
ATOM   2005  C   TYR B 124     -21.890   3.629 -33.048  1.00 63.86           C  
ANISOU 2005  C   TYR B 124     7295   9338   7628   1014   -732  -1016       C  
ATOM   2006  O   TYR B 124     -20.953   2.828 -33.054  1.00 65.56           O  
ANISOU 2006  O   TYR B 124     7466   9730   7711   1288   -732  -1078       O  
ATOM   2007  CB  TYR B 124     -23.362   3.890 -31.016  1.00 61.93           C  
ANISOU 2007  CB  TYR B 124     7241   8734   7554   1022   -634   -758       C  
ATOM   2008  CG  TYR B 124     -23.368   4.217 -29.535  1.00 62.36           C  
ANISOU 2008  CG  TYR B 124     7299   8864   7529   1120   -601   -645       C  
ATOM   2009  CD1 TYR B 124     -22.187   4.485 -28.843  1.00 63.43           C  
ANISOU 2009  CD1 TYR B 124     7282   9409   7410   1292   -638   -685       C  
ATOM   2010  CD2 TYR B 124     -24.569   4.213 -28.820  1.00 61.90           C  
ANISOU 2010  CD2 TYR B 124     7369   8519   7630   1045   -527   -531       C  
ATOM   2011  CE1 TYR B 124     -22.204   4.758 -27.481  1.00 63.79           C  
ANISOU 2011  CE1 TYR B 124     7310   9568   7358   1402   -611   -600       C  
ATOM   2012  CE2 TYR B 124     -24.604   4.486 -27.472  1.00 61.15           C  
ANISOU 2012  CE2 TYR B 124     7274   8508   7450   1136   -492   -431       C  
ATOM   2013  CZ  TYR B 124     -23.421   4.761 -26.806  1.00 62.09           C  
ANISOU 2013  CZ  TYR B 124     7249   9027   7313   1323   -539   -457       C  
ATOM   2014  OH  TYR B 124     -23.456   5.035 -25.474  1.00 56.72           O  
ANISOU 2014  OH  TYR B 124     6547   8479   6525   1427   -510   -378       O  
ATOM   2015  N   VAL B 125     -22.671   3.845 -34.106  1.00 54.40           N  
ANISOU 2015  N   VAL B 125     6786   8424   5457   1726    833   -174       N  
ATOM   2016  CA  VAL B 125     -22.474   3.117 -35.357  1.00 56.04           C  
ANISOU 2016  CA  VAL B 125     6900   8877   5512   1626    897   -258       C  
ATOM   2017  C   VAL B 125     -21.135   3.508 -35.958  1.00 58.71           C  
ANISOU 2017  C   VAL B 125     7101   9565   5639   1435    905   -272       C  
ATOM   2018  O   VAL B 125     -20.362   2.653 -36.336  1.00 59.52           O  
ANISOU 2018  O   VAL B 125     7006   9918   5689   1451   1018   -600       O  
ATOM   2019  CB  VAL B 125     -23.614   3.379 -36.362  1.00 57.22           C  
ANISOU 2019  CB  VAL B 125     7047   9101   5592   1474    818   -136       C  
ATOM   2020  CG1 VAL B 125     -23.270   2.817 -37.741  1.00 58.43           C  
ANISOU 2020  CG1 VAL B 125     6983   9778   5436   1234    901   -295       C  
ATOM   2021  CG2 VAL B 125     -24.910   2.777 -35.840  1.00 54.05           C  
ANISOU 2021  CG2 VAL B 125     6734   8441   5361   1657    852   -214       C  
ATOM   2022  N   GLN B 126     -20.858   4.807 -35.990  1.00 61.03           N  
ANISOU 2022  N   GLN B 126     7432   9857   5898   1247    735     36       N  
ATOM   2023  CA  GLN B 126     -19.621   5.323 -36.555  1.00 65.17           C  
ANISOU 2023  CA  GLN B 126     7812  10796   6153    953    697    135       C  
ATOM   2024  C   GLN B 126     -18.339   4.762 -35.897  1.00 65.18           C  
ANISOU 2024  C   GLN B 126     7743  10870   6151   1135    872   -182       C  
ATOM   2025  O   GLN B 126     -17.278   4.716 -36.553  1.00 68.50           O  
ANISOU 2025  O   GLN B 126     7931  11815   6281    909    936   -334       O  
ATOM   2026  CB  GLN B 126     -19.655   6.847 -36.537  1.00 67.38           C  
ANISOU 2026  CB  GLN B 126     8136  10863   6601    716    346    622       C  
ATOM   2027  CG  GLN B 126     -18.300   7.540 -36.587  1.00 72.07           C  
ANISOU 2027  CG  GLN B 126     8635  11718   7029    458    259    794       C  
ATOM   2028  CD  GLN B 126     -18.411   8.995 -36.202  1.00 76.86           C  
ANISOU 2028  CD  GLN B 126     9273  11818   8110    351   -173   1204       C  
ATOM   2029  OE1 GLN B 126     -19.449   9.629 -36.433  1.00 80.76           O  
ANISOU 2029  OE1 GLN B 126     9752  11912   9019    285   -530   1476       O  
ATOM   2030  NE2 GLN B 126     -17.349   9.539 -35.610  1.00 77.90           N  
ANISOU 2030  NE2 GLN B 126     9391  11902   8302    348   -202   1202       N  
ATOM   2031  N   VAL B 127     -18.429   4.325 -34.634  1.00 62.40           N  
ANISOU 2031  N   VAL B 127     7522  10099   6088   1469    917   -275       N  
ATOM   2032  CA  VAL B 127     -17.306   3.614 -34.002  1.00 62.72           C  
ANISOU 2032  CA  VAL B 127     7457  10138   6235   1629    983   -496       C  
ATOM   2033  C   VAL B 127     -17.577   2.120 -33.723  1.00 63.48           C  
ANISOU 2033  C   VAL B 127     7452   9998   6669   1854    965   -720       C  
ATOM   2034  O   VAL B 127     -16.876   1.515 -32.920  1.00 64.94           O  
ANISOU 2034  O   VAL B 127     7554   9990   7129   1985    868   -741       O  
ATOM   2035  CB  VAL B 127     -16.823   4.310 -32.708  1.00 61.31           C  
ANISOU 2035  CB  VAL B 127     7401   9775   6119   1691    936   -314       C  
ATOM   2036  CG1 VAL B 127     -16.324   5.707 -33.000  1.00 61.78           C  
ANISOU 2036  CG1 VAL B 127     7477   9956   6037   1478    858   -138       C  
ATOM   2037  CG2 VAL B 127     -17.927   4.347 -31.688  1.00 60.15           C  
ANISOU 2037  CG2 VAL B 127     7375   9394   6085   1779    902   -211       C  
ATOM   2038  N   GLN B 128     -18.591   1.539 -34.366  1.00 63.59           N  
ANISOU 2038  N   GLN B 128     7443   9979   6739   1865    978   -822       N  
ATOM   2039  CA  GLN B 128     -18.890   0.094 -34.271  1.00 65.65           C  
ANISOU 2039  CA  GLN B 128     7543   9939   7462   2043    866  -1039       C  
ATOM   2040  C   GLN B 128     -19.395  -0.417 -32.903  1.00 64.56           C  
ANISOU 2040  C   GLN B 128     7546   9388   7594   2104    665   -630       C  
ATOM   2041  O   GLN B 128     -19.161  -1.572 -32.538  1.00 67.90           O  
ANISOU 2041  O   GLN B 128     7779   9465   8554   2189    398   -631       O  
ATOM   2042  CB  GLN B 128     -17.689  -0.748 -34.726  1.00 70.64           C  
ANISOU 2042  CB  GLN B 128     7750  10627   8463   2153    803  -1598       C  
ATOM   2043  CG  GLN B 128     -17.065  -0.323 -36.039  1.00 75.05           C  
ANISOU 2043  CG  GLN B 128     8016  11897   8603   1953   1021  -2091       C  
ATOM   2044  CD  GLN B 128     -15.722  -0.991 -36.259  1.00 84.47           C  
ANISOU 2044  CD  GLN B 128     8695  13239  10160   2065    975  -2784       C  
ATOM   2045  OE1 GLN B 128     -14.752  -0.338 -36.648  1.00 87.82           O  
ANISOU 2045  OE1 GLN B 128     8953  14245  10167   1867   1118  -2965       O  
ATOM   2046  NE2 GLN B 128     -15.651  -2.299 -35.995  1.00 88.73           N  
ANISOU 2046  NE2 GLN B 128     8919  13219  11573   2366    707  -3183       N  
ATOM   2047  N   LYS B 129     -20.093   0.436 -32.160  1.00 61.30           N  
ANISOU 2047  N   LYS B 129     7372   9065   6854   1997    730   -301       N  
ATOM   2048  CA  LYS B 129     -20.809   0.011 -30.971  1.00 61.20           C  
ANISOU 2048  CA  LYS B 129     7400   8986   6865   1888    587     43       C  
ATOM   2049  C   LYS B 129     -22.244  -0.280 -31.348  1.00 59.19           C  
ANISOU 2049  C   LYS B 129     7211   8704   6574   1861    621     41       C  
ATOM   2050  O   LYS B 129     -23.143   0.464 -30.978  1.00 57.92           O  
ANISOU 2050  O   LYS B 129     7132   8750   6124   1774    730     62       O  
ATOM   2051  CB  LYS B 129     -20.792   1.113 -29.912  1.00 61.11           C  
ANISOU 2051  CB  LYS B 129     7449   9283   6484   1750    679    158       C  
ATOM   2052  CG  LYS B 129     -19.617   1.067 -28.943  1.00 64.86           C  
ANISOU 2052  CG  LYS B 129     7829   9854   6958   1661    563    346       C  
ATOM   2053  CD  LYS B 129     -18.764   2.322 -29.068  1.00 66.08           C  
ANISOU 2053  CD  LYS B 129     8027  10132   6947   1729    728    129       C  
ATOM   2054  CE  LYS B 129     -18.132   2.681 -27.725  1.00 69.95           C  
ANISOU 2054  CE  LYS B 129     8416  10924   7235   1554    690    268       C  
ATOM   2055  NZ  LYS B 129     -17.438   3.997 -27.791  1.00 69.54           N  
ANISOU 2055  NZ  LYS B 129     8385  10947   7086   1614    823     22       N  
ATOM   2056  N   TYR B 130     -22.467  -1.366 -32.074  1.00 59.46           N  
ANISOU 2056  N   TYR B 130     7139   8480   6970   1946    507    -78       N  
ATOM   2057  CA  TYR B 130     -23.770  -1.583 -32.712  1.00 57.73           C  
ANISOU 2057  CA  TYR B 130     6981   8255   6697   1941    580   -157       C  
ATOM   2058  C   TYR B 130     -24.840  -1.880 -31.670  1.00 57.25           C  
ANISOU 2058  C   TYR B 130     6968   8261   6522   1739    467    215       C  
ATOM   2059  O   TYR B 130     -25.980  -1.445 -31.785  1.00 55.42           O  
ANISOU 2059  O   TYR B 130     6819   8208   6029   1693    607    160       O  
ATOM   2060  CB  TYR B 130     -23.682  -2.687 -33.767  1.00 59.72           C  
ANISOU 2060  CB  TYR B 130     7016   8270   7402   2071    487   -516       C  
ATOM   2061  CG  TYR B 130     -22.714  -2.340 -34.881  1.00 63.43           C  
ANISOU 2061  CG  TYR B 130     7309   9000   7791   2144    660  -1019       C  
ATOM   2062  CD1 TYR B 130     -22.981  -1.289 -35.763  1.00 62.96           C  
ANISOU 2062  CD1 TYR B 130     7343   9381   7196   2017    900  -1081       C  
ATOM   2063  CD2 TYR B 130     -21.511  -3.047 -35.050  1.00 69.35           C  
ANISOU 2063  CD2 TYR B 130     7713   9619   9017   2270    520  -1419       C  
ATOM   2064  CE1 TYR B 130     -22.092  -0.957 -36.783  1.00 66.37           C  
ANISOU 2064  CE1 TYR B 130     7541  10280   7394   1903   1026  -1440       C  
ATOM   2065  CE2 TYR B 130     -20.610  -2.718 -36.074  1.00 71.85           C  
ANISOU 2065  CE2 TYR B 130     7758  10414   9128   2243    716  -1983       C  
ATOM   2066  CZ  TYR B 130     -20.911  -1.680 -36.941  1.00 70.93           C  
ANISOU 2066  CZ  TYR B 130     7749  10899   8300   2005    984  -1950       C  
ATOM   2067  OH  TYR B 130     -20.033  -1.341 -37.953  1.00 73.02           O  
ANISOU 2067  OH  TYR B 130     7683  11853   8208   1803   1145  -2399       O  
ATOM   2068  N   ASP B 131     -24.425  -2.625 -30.660  1.00 58.99           N  
ANISOU 2068  N   ASP B 131     7071   8400   6941   1558    166    612       N  
ATOM   2069  CA  ASP B 131     -25.223  -3.002 -29.523  1.00 60.74           C  
ANISOU 2069  CA  ASP B 131     7230   8906   6940   1170    -17   1096       C  
ATOM   2070  C   ASP B 131     -25.876  -1.789 -28.873  1.00 57.43           C  
ANISOU 2070  C   ASP B 131     6833   9142   5846   1016    296    923       C  
ATOM   2071  O   ASP B 131     -27.081  -1.780 -28.599  1.00 57.02           O  
ANISOU 2071  O   ASP B 131     6723   9438   5503    818    361    910       O  
ATOM   2072  CB  ASP B 131     -24.271  -3.689 -28.548  1.00 66.45           C  
ANISOU 2072  CB  ASP B 131     7777   9538   7932    915   -448   1640       C  
ATOM   2073  CG  ASP B 131     -22.779  -3.414 -28.891  1.00 69.22           C  
ANISOU 2073  CG  ASP B 131     8107   9599   8592   1222   -429   1373       C  
ATOM   2074  OD1 ASP B 131     -22.311  -2.239 -28.736  1.00 66.87           O  
ANISOU 2074  OD1 ASP B 131     7913   9659   7836   1291    -99   1129       O  
ATOM   2075  OD2 ASP B 131     -22.088  -4.377 -29.349  1.00 75.16           O  
ANISOU 2075  OD2 ASP B 131     8678   9753  10125   1399   -774   1327       O  
ATOM   2076  N   LEU B 132     -25.053  -0.769 -28.663  1.00 56.15           N  
ANISOU 2076  N   LEU B 132     7096   7729   6508    728   -451    131       N  
ATOM   2077  CA  LEU B 132     -25.421   0.434 -27.974  1.00 54.94           C  
ANISOU 2077  CA  LEU B 132     6989   7663   6221    680   -525     13       C  
ATOM   2078  C   LEU B 132     -26.273   1.343 -28.880  1.00 53.12           C  
ANISOU 2078  C   LEU B 132     6831   7377   5973    687   -409   -106       C  
ATOM   2079  O   LEU B 132     -27.184   2.043 -28.415  1.00 52.09           O  
ANISOU 2079  O   LEU B 132     6767   7306   5719    661   -409   -198       O  
ATOM   2080  CB  LEU B 132     -24.146   1.140 -27.515  1.00 55.66           C  
ANISOU 2080  CB  LEU B 132     6974   7746   6425    642   -660      0       C  
ATOM   2081  CG  LEU B 132     -23.722   1.139 -26.029  1.00 58.68           C  
ANISOU 2081  CG  LEU B 132     7351   8258   6686    597   -880     17       C  
ATOM   2082  CD1 LEU B 132     -24.323   0.011 -25.198  1.00 59.07           C  
ANISOU 2082  CD1 LEU B 132     7480   8420   6543    619   -905    134       C  
ATOM   2083  CD2 LEU B 132     -22.198   1.130 -25.881  1.00 60.58           C  
ANISOU 2083  CD2 LEU B 132     7419   8433   7164    579  -1038     91       C  
ATOM   2084  N   ALA B 133     -25.971   1.319 -30.171  1.00 51.75           N  
ANISOU 2084  N   ALA B 133     6654   7084   5925    729   -302    -93       N  
ATOM   2085  CA  ALA B 133     -26.646   2.173 -31.126  1.00 50.48           C  
ANISOU 2085  CA  ALA B 133     6566   6865   5749    746   -212   -173       C  
ATOM   2086  C   ALA B 133     -28.084   1.746 -31.300  1.00 49.11           C  
ANISOU 2086  C   ALA B 133     6483   6713   5460    756   -198   -196       C  
ATOM   2087  O   ALA B 133     -28.964   2.594 -31.385  1.00 48.80           O  
ANISOU 2087  O   ALA B 133     6481   6678   5381    744   -188   -267       O  
ATOM   2088  CB  ALA B 133     -25.926   2.167 -32.466  1.00 50.60           C  
ANISOU 2088  CB  ALA B 133     6592   6747   5883    803    -89   -134       C  
ATOM   2089  N   VAL B 134     -28.339   0.444 -31.306  1.00 48.55           N  
ANISOU 2089  N   VAL B 134     6426   6639   5383    776   -198   -130       N  
ATOM   2090  CA  VAL B 134     -29.667  -0.021 -31.678  1.00 47.67           C  
ANISOU 2090  CA  VAL B 134     6376   6502   5234    788   -192   -152       C  
ATOM   2091  C   VAL B 134     -30.818   0.657 -30.895  1.00 48.11           C  
ANISOU 2091  C   VAL B 134     6430   6615   5231    754   -209   -202       C  
ATOM   2092  O   VAL B 134     -31.721   1.203 -31.500  1.00 47.95           O  
ANISOU 2092  O   VAL B 134     6442   6545   5229    759   -204   -253       O  
ATOM   2093  CB  VAL B 134     -29.743  -1.557 -31.754  1.00 47.43           C  
ANISOU 2093  CB  VAL B 134     6335   6432   5254    810   -185    -81       C  
ATOM   2094  CG1 VAL B 134     -31.175  -2.039 -31.843  1.00 46.50           C  
ANISOU 2094  CG1 VAL B 134     6237   6280   5149    808   -204   -102       C  
ATOM   2095  CG2 VAL B 134     -28.969  -2.032 -32.970  1.00 45.85           C  
ANISOU 2095  CG2 VAL B 134     6183   6123   5113    854   -124    -79       C  
ATOM   2096  N   PRO B 135     -30.774   0.646 -29.556  1.00 49.13           N  
ANISOU 2096  N   PRO B 135     6531   6841   5291    725   -223   -181       N  
ATOM   2097  CA  PRO B 135     -31.936   1.179 -28.848  1.00 48.99           C  
ANISOU 2097  CA  PRO B 135     6532   6853   5227    705   -182   -227       C  
ATOM   2098  C   PRO B 135     -32.174   2.654 -29.085  1.00 48.92           C  
ANISOU 2098  C   PRO B 135     6532   6820   5232    684   -161   -336       C  
ATOM   2099  O   PRO B 135     -33.311   3.079 -29.090  1.00 49.16           O  
ANISOU 2099  O   PRO B 135     6561   6808   5308    681   -109   -369       O  
ATOM   2100  CB  PRO B 135     -31.603   0.948 -27.373  1.00 50.52           C  
ANISOU 2100  CB  PRO B 135     6743   7164   5287    687   -192   -187       C  
ATOM   2101  CG  PRO B 135     -30.517  -0.043 -27.333  1.00 50.29           C  
ANISOU 2101  CG  PRO B 135     6677   7158   5271    702   -260    -82       C  
ATOM   2102  CD  PRO B 135     -29.950  -0.232 -28.701  1.00 50.11           C  
ANISOU 2102  CD  PRO B 135     6621   7033   5385    725   -263    -84       C  
ATOM   2103  N   LEU B 136     -31.125   3.438 -29.273  1.00 48.67           N  
ANISOU 2103  N   LEU B 136     6488   6795   5209    671   -192   -381       N  
ATOM   2104  CA  LEU B 136     -31.316   4.855 -29.487  1.00 48.69           C  
ANISOU 2104  CA  LEU B 136     6481   6756   5263    653   -158   -476       C  
ATOM   2105  C   LEU B 136     -31.864   5.125 -30.881  1.00 48.62           C  
ANISOU 2105  C   LEU B 136     6480   6643   5347    691   -133   -456       C  
ATOM   2106  O   LEU B 136     -32.834   5.862 -31.047  1.00 49.17           O  
ANISOU 2106  O   LEU B 136     6540   6664   5476    688    -99   -490       O  
ATOM   2107  CB  LEU B 136     -30.016   5.615 -29.293  1.00 48.94           C  
ANISOU 2107  CB  LEU B 136     6470   6795   5327    627   -198   -525       C  
ATOM   2108  CG  LEU B 136     -29.395   5.587 -27.895  1.00 49.28           C  
ANISOU 2108  CG  LEU B 136     6518   6942   5264    581   -283   -569       C  
ATOM   2109  CD1 LEU B 136     -27.890   5.755 -28.025  1.00 46.82           C  
ANISOU 2109  CD1 LEU B 136     6123   6605   5059    568   -372   -557       C  
ATOM   2110  CD2 LEU B 136     -30.006   6.643 -26.952  1.00 47.47           C  
ANISOU 2110  CD2 LEU B 136     6334   6740   4962    537   -250   -713       C  
ATOM   2111  N   LEU B 137     -31.241   4.516 -31.881  1.00 48.53           N  
ANISOU 2111  N   LEU B 137     6498   6592   5348    731   -148   -394       N  
ATOM   2112  CA  LEU B 137     -31.634   4.692 -33.276  1.00 48.32           C  
ANISOU 2112  CA  LEU B 137     6533   6477   5348    778   -143   -370       C  
ATOM   2113  C   LEU B 137     -33.070   4.214 -33.541  1.00 48.32           C  
ANISOU 2113  C   LEU B 137     6555   6443   5359    784   -200   -363       C  
ATOM   2114  O   LEU B 137     -33.812   4.847 -34.300  1.00 48.77           O  
ANISOU 2114  O   LEU B 137     6634   6437   5459    803   -231   -362       O  
ATOM   2115  CB  LEU B 137     -30.621   4.023 -34.189  1.00 48.12           C  
ANISOU 2115  CB  LEU B 137     6569   6411   5301    826   -115   -317       C  
ATOM   2116  CG  LEU B 137     -29.587   4.972 -34.780  1.00 49.24           C  
ANISOU 2116  CG  LEU B 137     6707   6499   5503    853    -27   -300       C  
ATOM   2117  CD1 LEU B 137     -29.331   6.158 -33.923  1.00 51.67           C  
ANISOU 2117  CD1 LEU B 137     6905   6827   5899    804    -18   -354       C  
ATOM   2118  CD2 LEU B 137     -28.288   4.257 -35.098  1.00 50.23           C  
ANISOU 2118  CD2 LEU B 137     6833   6585   5664    885     42   -244       C  
ATOM   2119  N   VAL B 138     -33.487   3.139 -32.883  1.00 47.71           N  
ANISOU 2119  N   VAL B 138     6453   6394   5277    769   -222   -346       N  
ATOM   2120  CA  VAL B 138     -34.896   2.776 -32.906  1.00 47.87           C  
ANISOU 2120  CA  VAL B 138     6444   6359   5384    765   -266   -339       C  
ATOM   2121  C   VAL B 138     -35.765   3.983 -32.475  1.00 49.36           C  
ANISOU 2121  C   VAL B 138     6569   6524   5662    743   -221   -371       C  
ATOM   2122  O   VAL B 138     -36.741   4.350 -33.157  1.00 48.87           O  
ANISOU 2122  O   VAL B 138     6482   6371   5712    754   -280   -360       O  
ATOM   2123  CB  VAL B 138     -35.186   1.567 -31.994  1.00 48.30           C  
ANISOU 2123  CB  VAL B 138     6451   6439   5460    752   -244   -298       C  
ATOM   2124  CG1 VAL B 138     -36.692   1.474 -31.680  1.00 46.84           C  
ANISOU 2124  CG1 VAL B 138     6187   6178   5432    742   -236   -284       C  
ATOM   2125  CG2 VAL B 138     -34.643   0.256 -32.641  1.00 46.00           C  
ANISOU 2125  CG2 VAL B 138     6203   6119   5155    777   -294   -267       C  
ATOM   2126  N   LYS B 139     -35.370   4.601 -31.355  1.00 50.69           N  
ANISOU 2126  N   LYS B 139     6712   6762   5785    712   -126   -413       N  
ATOM   2127  CA  LYS B 139     -36.053   5.755 -30.784  1.00 51.95           C  
ANISOU 2127  CA  LYS B 139     6821   6890   6025    689    -39   -468       C  
ATOM   2128  C   LYS B 139     -36.149   6.953 -31.741  1.00 51.07           C  
ANISOU 2128  C   LYS B 139     6691   6700   6013    702    -57   -479       C  
ATOM   2129  O   LYS B 139     -37.237   7.478 -31.964  1.00 51.60           O  
ANISOU 2129  O   LYS B 139     6693   6674   6237    706    -46   -464       O  
ATOM   2130  CB  LYS B 139     -35.330   6.185 -29.493  1.00 53.41           C  
ANISOU 2130  CB  LYS B 139     7030   7171   6089    653     38   -543       C  
ATOM   2131  CG  LYS B 139     -36.215   6.778 -28.423  1.00 56.94           C  
ANISOU 2131  CG  LYS B 139     7465   7601   6568    631    176   -605       C  
ATOM   2132  CD  LYS B 139     -35.459   7.757 -27.527  1.00 61.72           C  
ANISOU 2132  CD  LYS B 139     8117   8266   7066    591    221   -735       C  
ATOM   2133  CE  LYS B 139     -35.969   7.681 -26.088  1.00 65.05           C  
ANISOU 2133  CE  LYS B 139     8616   8736   7364    577    354   -789       C  
ATOM   2134  NZ  LYS B 139     -35.543   6.397 -25.465  1.00 66.55           N  
ANISOU 2134  NZ  LYS B 139     8877   9042   7365    591    304   -703       N  
ATOM   2135  N   VAL B 140     -35.019   7.389 -32.289  1.00 50.09           N  
ANISOU 2135  N   VAL B 140     6605   6596   5829    715    -72   -486       N  
ATOM   2136  CA  VAL B 140     -34.995   8.528 -33.214  1.00 50.78           C  
ANISOU 2136  CA  VAL B 140     6680   6604   6007    740    -64   -467       C  
ATOM   2137  C   VAL B 140     -35.783   8.262 -34.503  1.00 51.34           C  
ANISOU 2137  C   VAL B 140     6795   6603   6108    789   -172   -377       C  
ATOM   2138  O   VAL B 140     -36.503   9.126 -34.974  1.00 52.43           O  
ANISOU 2138  O   VAL B 140     6890   6659   6372    803   -185   -341       O  
ATOM   2139  CB  VAL B 140     -33.531   8.991 -33.602  1.00 51.00           C  
ANISOU 2139  CB  VAL B 140     6734   6645   5999    755    -26   -467       C  
ATOM   2140  CG1 VAL B 140     -33.532  10.045 -34.767  1.00 50.62           C  
ANISOU 2140  CG1 VAL B 140     6691   6499   6041    804      2   -399       C  
ATOM   2141  CG2 VAL B 140     -32.765   9.507 -32.396  1.00 50.74           C  
ANISOU 2141  CG2 VAL B 140     6641   6659   5978    699     27   -571       C  
ATOM   2142  N   ALA B 141     -35.638   7.081 -35.082  1.00 51.76           N  
ANISOU 2142  N   ALA B 141     6939   6676   6050    814   -262   -345       N  
ATOM   2143  CA  ALA B 141     -36.439   6.712 -36.257  1.00 53.33           C  
ANISOU 2143  CA  ALA B 141     7207   6806   6247    853   -412   -289       C  
ATOM   2144  C   ALA B 141     -37.934   6.894 -35.981  1.00 54.65           C  
ANISOU 2144  C   ALA B 141     7252   6895   6615    829   -482   -274       C  
ATOM   2145  O   ALA B 141     -38.666   7.402 -36.843  1.00 54.76           O  
ANISOU 2145  O   ALA B 141     7267   6829   6711    856   -599   -215       O  
ATOM   2146  CB  ALA B 141     -36.173   5.275 -36.662  1.00 53.10           C  
ANISOU 2146  CB  ALA B 141     7282   6797   6096    868   -491   -298       C  
ATOM   2147  N   GLU B 142     -38.377   6.483 -34.786  1.00 54.81           N  
ANISOU 2147  N   GLU B 142     7170   6929   6727    786   -403   -312       N  
ATOM   2148  CA  GLU B 142     -39.785   6.625 -34.417  1.00 56.75           C  
ANISOU 2148  CA  GLU B 142     7274   7070   7217    767   -413   -287       C  
ATOM   2149  C   GLU B 142     -40.265   8.092 -34.332  1.00 56.50           C  
ANISOU 2149  C   GLU B 142     7145   6962   7358    765   -333   -275       C  
ATOM   2150  O   GLU B 142     -41.329   8.433 -34.848  1.00 56.70           O  
ANISOU 2150  O   GLU B 142     7076   6865   7599    775   -430   -208       O  
ATOM   2151  CB  GLU B 142     -40.095   5.874 -33.132  1.00 57.31           C  
ANISOU 2151  CB  GLU B 142     7277   7162   7335    736   -288   -311       C  
ATOM   2152  CG  GLU B 142     -41.289   6.444 -32.402  1.00 62.35           C  
ANISOU 2152  CG  GLU B 142     7765   7691   8234    719   -165   -297       C  
ATOM   2153  CD  GLU B 142     -42.275   5.394 -32.054  1.00 68.61           C  
ANISOU 2153  CD  GLU B 142     8459   8395   9212    715   -169   -247       C  
ATOM   2154  OE1 GLU B 142     -42.340   4.381 -32.780  1.00 72.38           O  
ANISOU 2154  OE1 GLU B 142     8958   8852   9689    724   -352   -221       O  
ATOM   2155  OE2 GLU B 142     -43.000   5.576 -31.061  1.00 73.48           O  
ANISOU 2155  OE2 GLU B 142     8978   8946   9994    706     24   -236       O  
ATOM   2156  N   ALA B 143     -39.465   8.940 -33.688  1.00 51.27           N  
ANISOU 2156  N   ALA B 143     6178   5882   7418     92    173   -302       N  
ATOM   2157  CA  ALA B 143     -39.794  10.359 -33.564  1.00 52.39           C  
ANISOU 2157  CA  ALA B 143     6206   5901   7799    188    235   -271       C  
ATOM   2158  C   ALA B 143     -39.398  11.191 -34.807  1.00 52.94           C  
ANISOU 2158  C   ALA B 143     6219   5937   7955    336    197    -52       C  
ATOM   2159  O   ALA B 143     -40.001  12.224 -35.076  1.00 54.22           O  
ANISOU 2159  O   ALA B 143     6312   6020   8269    482    241     17       O  
ATOM   2160  CB  ALA B 143     -39.185  10.956 -32.267  1.00 51.94           C  
ANISOU 2160  CB  ALA B 143     6249   5660   7826    105    318   -399       C  
ATOM   2161  N   ASN B 144     -38.387  10.749 -35.550  1.00 51.89           N  
ANISOU 2161  N   ASN B 144     6147   5855   7712    317    134     54       N  
ATOM   2162  CA  ASN B 144     -38.032  11.370 -36.829  1.00 53.22           C  
ANISOU 2162  CA  ASN B 144     6300   6006   7913    432    118    267       C  
ATOM   2163  C   ASN B 144     -38.166  10.393 -38.011  1.00 52.01           C  
ANISOU 2163  C   ASN B 144     6132   6063   7567    477      9    369       C  
ATOM   2164  O   ASN B 144     -37.180   9.945 -38.576  1.00 50.18           O  
ANISOU 2164  O   ASN B 144     5966   5874   7226    446    -13    439       O  
ATOM   2165  CB  ASN B 144     -36.611  11.931 -36.778  1.00 54.12           C  
ANISOU 2165  CB  ASN B 144     6487   5995   8080    346    182    300       C  
ATOM   2166  CG  ASN B 144     -36.475  13.124 -35.859  1.00 57.74           C  
ANISOU 2166  CG  ASN B 144     6981   6223   8731    284    307    215       C  
ATOM   2167  OD1 ASN B 144     -37.431  13.545 -35.198  1.00 61.50           O  
ANISOU 2167  OD1 ASN B 144     7446   6612   9308    337    352    137       O  
ATOM   2168  ND2 ASN B 144     -35.272  13.687 -35.816  1.00 60.21           N  
ANISOU 2168  ND2 ASN B 144     7335   6449   9093    154    382    208       N  
ATOM   2169  N   PRO B 145     -39.398  10.050 -38.388  1.00 53.12           N  
ANISOU 2169  N   PRO B 145     6169   6360   7653    543    -53    354       N  
ATOM   2170  CA  PRO B 145     -39.513   9.036 -39.445  1.00 53.02           C  
ANISOU 2170  CA  PRO B 145     6162   6555   7428    535   -153    409       C  
ATOM   2171  C   PRO B 145     -38.810   9.436 -40.744  1.00 54.23           C  
ANISOU 2171  C   PRO B 145     6368   6702   7534    652   -183    633       C  
ATOM   2172  O   PRO B 145     -38.212   8.604 -41.399  1.00 54.24           O  
ANISOU 2172  O   PRO B 145     6452   6793   7362    606   -220    672       O  
ATOM   2173  CB  PRO B 145     -41.026   8.908 -39.644  1.00 54.47           C  
ANISOU 2173  CB  PRO B 145     6162   6942   7589    583   -213    336       C  
ATOM   2174  CG  PRO B 145     -41.640  10.055 -38.918  1.00 55.55           C  
ANISOU 2174  CG  PRO B 145     6191   6969   7946    701   -146    303       C  
ATOM   2175  CD  PRO B 145     -40.707  10.423 -37.829  1.00 54.21           C  
ANISOU 2175  CD  PRO B 145     6163   6538   7893    598    -31    247       C  
ATOM   2176  N   VAL B 146     -38.830  10.723 -41.070  1.00 56.18           N  
ANISOU 2176  N   VAL B 146     6610   6812   7924    803   -139    779       N  
ATOM   2177  CA  VAL B 146     -38.343  11.206 -42.354  1.00 57.02           C  
ANISOU 2177  CA  VAL B 146     6804   6894   7966    924   -140   1009       C  
ATOM   2178  C   VAL B 146     -36.803  11.322 -42.489  1.00 55.92           C  
ANISOU 2178  C   VAL B 146     6789   6626   7830    798    -31   1065       C  
ATOM   2179  O   VAL B 146     -36.310  11.842 -43.500  1.00 57.42           O  
ANISOU 2179  O   VAL B 146     7079   6759   7976    862     19   1253       O  
ATOM   2180  CB  VAL B 146     -39.136  12.488 -42.725  1.00 60.22           C  
ANISOU 2180  CB  VAL B 146     7209   7196   8474   1176   -127   1154       C  
ATOM   2181  CG1 VAL B 146     -38.367  13.454 -43.625  1.00 62.92           C  
ANISOU 2181  CG1 VAL B 146     7756   7333   8817   1269    -24   1394       C  
ATOM   2182  CG2 VAL B 146     -40.459  12.085 -43.320  1.00 60.78           C  
ANISOU 2182  CG2 VAL B 146     7115   7559   8419   1347   -295   1150       C  
ATOM   2183  N   ASN B 147     -36.045  10.817 -41.510  1.00 52.96           N  
ANISOU 2183  N   ASN B 147     6404   6236   7480    628      5    899       N  
ATOM   2184  CA  ASN B 147     -34.587  10.900 -41.579  1.00 51.81           C  
ANISOU 2184  CA  ASN B 147     6299   6053   7333    516     95    909       C  
ATOM   2185  C   ASN B 147     -33.971   9.624 -42.169  1.00 50.00           C  
ANISOU 2185  C   ASN B 147     6089   6024   6883    508     32    904       C  
ATOM   2186  O   ASN B 147     -33.954   8.566 -41.526  1.00 47.22           O  
ANISOU 2186  O   ASN B 147     5746   5766   6430    477    -31    758       O  
ATOM   2187  CB  ASN B 147     -34.011  11.200 -40.195  1.00 51.85           C  
ANISOU 2187  CB  ASN B 147     6263   5965   7472    375    157    723       C  
ATOM   2188  CG  ASN B 147     -32.488  11.345 -40.201  1.00 53.28           C  
ANISOU 2188  CG  ASN B 147     6411   6180   7652    244    243    687       C  
ATOM   2189  OD1 ASN B 147     -31.744  10.484 -40.699  1.00 51.57           O  
ANISOU 2189  OD1 ASN B 147     6171   6144   7279    259    207    694       O  
ATOM   2190  ND2 ASN B 147     -32.021  12.433 -39.623  1.00 56.24           N  
ANISOU 2190  ND2 ASN B 147     6774   6396   8196    108    367    625       N  
ATOM   2191  N   PHE B 148     -33.446   9.726 -43.389  1.00 50.68           N  
ANISOU 2191  N   PHE B 148     6225   6152   6876    547     73   1064       N  
ATOM   2192  CA  PHE B 148     -32.951   8.538 -44.110  1.00 49.27           C  
ANISOU 2192  CA  PHE B 148     6092   6155   6471    572     28   1072       C  
ATOM   2193  C   PHE B 148     -31.703   7.935 -43.450  1.00 48.07           C  
ANISOU 2193  C   PHE B 148     5895   6083   6285    515     65    929       C  
ATOM   2194  O   PHE B 148     -31.646   6.732 -43.251  1.00 46.15           O  
ANISOU 2194  O   PHE B 148     5715   5944   5876    562     -3    838       O  
ATOM   2195  CB  PHE B 148     -32.722   8.845 -45.597  1.00 50.67           C  
ANISOU 2195  CB  PHE B 148     6349   6360   6541    635     78   1278       C  
ATOM   2196  CG  PHE B 148     -31.879   7.822 -46.330  1.00 50.45           C  
ANISOU 2196  CG  PHE B 148     6371   6495   6302    647     93   1280       C  
ATOM   2197  CD1 PHE B 148     -32.459   6.726 -46.953  1.00 52.18           C  
ANISOU 2197  CD1 PHE B 148     6686   6842   6297    711    -12   1276       C  
ATOM   2198  CD2 PHE B 148     -30.500   7.986 -46.429  1.00 52.02           C  
ANISOU 2198  CD2 PHE B 148     6515   6731   6516    586    230   1267       C  
ATOM   2199  CE1 PHE B 148     -31.652   5.795 -47.658  1.00 54.47           C  
ANISOU 2199  CE1 PHE B 148     7062   7253   6379    744     26   1275       C  
ATOM   2200  CE2 PHE B 148     -29.691   7.065 -47.113  1.00 52.63           C  
ANISOU 2200  CE2 PHE B 148     6624   6973   6397    636    262   1261       C  
ATOM   2201  CZ  PHE B 148     -30.258   5.975 -47.725  1.00 52.84           C  
ANISOU 2201  CZ  PHE B 148     6791   7084   6199    731    164   1274       C  
ATOM   2202  N   ASN B 149     -30.727   8.777 -43.121  1.00 48.18           N  
ANISOU 2202  N   ASN B 149     5812   6055   6438    418    177    901       N  
ATOM   2203  CA  ASN B 149     -29.479   8.325 -42.514  1.00 49.23           C  
ANISOU 2203  CA  ASN B 149     5833   6338   6533    388    195    749       C  
ATOM   2204  C   ASN B 149     -29.675   7.460 -41.255  1.00 47.70           C  
ANISOU 2204  C   ASN B 149     5659   6185   6277    445     74    570       C  
ATOM   2205  O   ASN B 149     -29.128   6.337 -41.153  1.00 48.20           O  
ANISOU 2205  O   ASN B 149     5765   6396   6152    567     19    501       O  
ATOM   2206  CB  ASN B 149     -28.608   9.525 -42.201  1.00 51.40           C  
ANISOU 2206  CB  ASN B 149     5967   6570   6989    209    335    699       C  
ATOM   2207  CG  ASN B 149     -27.189   9.139 -41.805  1.00 53.92           C  
ANISOU 2207  CG  ASN B 149     6093   7142   7252    179    353    532       C  
ATOM   2208  OD1 ASN B 149     -26.537   9.875 -41.053  1.00 57.03           O  
ANISOU 2208  OD1 ASN B 149     6330   7563   7775     12    413    387       O  
ATOM   2209  ND2 ASN B 149     -26.700   8.008 -42.316  1.00 51.51           N  
ANISOU 2209  ND2 ASN B 149     5789   7039   6742    347    304    537       N  
ATOM   2210  N   VAL B 150     -30.484   7.966 -40.329  1.00 46.33           N  
ANISOU 2210  N   VAL B 150     5496   5865   6240    381     50    506       N  
ATOM   2211  CA  VAL B 150     -30.845   7.242 -39.108  1.00 44.49           C  
ANISOU 2211  CA  VAL B 150     5334   5628   5940    413    -36    349       C  
ATOM   2212  C   VAL B 150     -31.399   5.864 -39.436  1.00 43.66           C  
ANISOU 2212  C   VAL B 150     5416   5565   5604    519   -103    362       C  
ATOM   2213  O   VAL B 150     -30.991   4.861 -38.847  1.00 44.72           O  
ANISOU 2213  O   VAL B 150     5670   5758   5563    610   -146    262       O  
ATOM   2214  CB  VAL B 150     -31.862   8.040 -38.281  1.00 43.74           C  
ANISOU 2214  CB  VAL B 150     5238   5355   6023    322    -21    299       C  
ATOM   2215  CG1 VAL B 150     -32.511   7.174 -37.217  1.00 41.68           C  
ANISOU 2215  CG1 VAL B 150     5104   5074   5657    341    -83    162       C  
ATOM   2216  CG2 VAL B 150     -31.181   9.231 -37.669  1.00 44.92           C  
ANISOU 2216  CG2 VAL B 150     5265   5442   6361    197     55    225       C  
ATOM   2217  N   ARG B 151     -32.316   5.800 -40.380  1.00 43.11           N  
ANISOU 2217  N   ARG B 151     5399   5468   5512    512   -106    476       N  
ATOM   2218  CA AARG B 151     -32.888   4.525 -40.810  0.46 42.72           C  
ANISOU 2218  CA AARG B 151     5536   5460   5234    549   -147    466       C  
ATOM   2219  CA BARG B 151     -32.878   4.514 -40.760  0.54 42.52           C  
ANISOU 2219  CA BARG B 151     5512   5433   5209    548   -147    460       C  
ATOM   2220  C   ARG B 151     -31.829   3.641 -41.444  1.00 43.26           C  
ANISOU 2220  C   ARG B 151     5703   5636   5098    670   -135    492       C  
ATOM   2221  O   ARG B 151     -31.790   2.440 -41.214  1.00 43.01           O  
ANISOU 2221  O   ARG B 151     5889   5599   4851    737   -145    417       O  
ATOM   2222  CB AARG B 151     -34.033   4.747 -41.807  0.46 42.67           C  
ANISOU 2222  CB AARG B 151     5507   5471   5233    509   -172    567       C  
ATOM   2223  CB BARG B 151     -34.125   4.682 -41.642  0.54 42.30           C  
ANISOU 2223  CB BARG B 151     5469   5416   5186    500   -174    544       C  
ATOM   2224  CG AARG B 151     -35.411   4.676 -41.193  0.46 41.67           C  
ANISOU 2224  CG AARG B 151     5373   5311   5148    416   -199    466       C  
ATOM   2225  CG BARG B 151     -34.795   3.369 -42.041  0.54 40.59           C  
ANISOU 2225  CG BARG B 151     5441   5254   4726    461   -201    485       C  
ATOM   2226  CD AARG B 151     -35.748   3.255 -40.775  0.46 38.77           C  
ANISOU 2226  CD AARG B 151     5228   4944   4557    342   -190    323       C  
ATOM   2227  CD BARG B 151     -35.242   2.529 -40.847  0.54 36.89           C  
ANISOU 2227  CD BARG B 151     5139   4702   4173    376   -176    306       C  
ATOM   2228  NE AARG B 151     -36.982   3.207 -39.998  0.46 37.10           N  
ANISOU 2228  NE AARG B 151     4994   4707   4394    204   -174    187       N  
ATOM   2229  NE BARG B 151     -36.434   3.055 -40.179  0.54 36.46           N  
ANISOU 2229  NE BARG B 151     4963   4621   4267    254   -175    223       N  
ATOM   2230  CZ AARG B 151     -37.781   4.245 -39.785  0.46 37.30           C  
ANISOU 2230  CZ AARG B 151     4796   4745   4628    190   -186    192       C  
ATOM   2231  CZ BARG B 151     -37.155   2.394 -39.271  0.54 35.93           C  
ANISOU 2231  CZ BARG B 151     5028   4495   4126    121   -125     61       C  
ATOM   2232  NH1AARG B 151     -38.866   4.066 -39.046  0.46 38.99           N  
ANISOU 2232  NH1AARG B 151     4982   4968   4864     61   -148     39       N  
ATOM   2233  NH1BARG B 151     -38.206   2.973 -38.728  0.54 33.98           N  
ANISOU 2233  NH1BARG B 151     4621   4259   4030     22   -108    -17       N  
ATOM   2234  NH2AARG B 151     -37.508   5.452 -40.301  0.46 35.13           N  
ANISOU 2234  NH2AARG B 151     4354   4463   4529    308   -210    342       N  
ATOM   2235  NH2BARG B 151     -36.822   1.163 -38.883  0.54 36.97           N  
ANISOU 2235  NH2BARG B 151     5479   4544   4021     99    -69    -23       N  
ATOM   2236  N   PHE B 152     -30.976   4.248 -42.259  1.00 44.84           N  
ANISOU 2236  N   PHE B 152     5767   5917   5353    701    -88    596       N  
ATOM   2237  CA  PHE B 152     -29.945   3.486 -42.945  1.00 47.06           C  
ANISOU 2237  CA  PHE B 152     6102   6329   5448    833    -55    616       C  
ATOM   2238  C   PHE B 152     -28.925   2.949 -41.932  1.00 47.66           C  
ANISOU 2238  C   PHE B 152     6166   6490   5449    967    -76    475       C  
ATOM   2239  O   PHE B 152     -28.653   1.744 -41.897  1.00 48.21           O  
ANISOU 2239  O   PHE B 152     6444   6588   5284   1136    -91    428       O  
ATOM   2240  CB  PHE B 152     -29.267   4.300 -44.045  1.00 48.65           C  
ANISOU 2240  CB  PHE B 152     6155   6609   5720    806     33    749       C  
ATOM   2241  CG  PHE B 152     -28.105   3.592 -44.681  1.00 53.05           C  
ANISOU 2241  CG  PHE B 152     6718   7335   6101    945     94    745       C  
ATOM   2242  CD1 PHE B 152     -28.256   2.311 -45.203  1.00 55.26           C  
ANISOU 2242  CD1 PHE B 152     7240   7634   6123   1077     76    742       C  
ATOM   2243  CD2 PHE B 152     -26.853   4.202 -44.744  1.00 56.13           C  
ANISOU 2243  CD2 PHE B 152     6872   7876   6577    932    188    720       C  
ATOM   2244  CE1 PHE B 152     -27.177   1.648 -45.775  1.00 59.17           C  
ANISOU 2244  CE1 PHE B 152     7752   8281   6448   1248    146    732       C  
ATOM   2245  CE2 PHE B 152     -25.771   3.552 -45.322  1.00 59.19           C  
ANISOU 2245  CE2 PHE B 152     7220   8465   6803   1082    256    696       C  
ATOM   2246  CZ  PHE B 152     -25.929   2.268 -45.835  1.00 59.81           C  
ANISOU 2246  CZ  PHE B 152     7552   8548   6624   1269    232    710       C  
ATOM   2247  N   ARG B 153     -28.410   3.813 -41.063  1.00 48.11           N  
ANISOU 2247  N   ARG B 153     6011   6584   5682    907    -81    396       N  
ATOM   2248  CA  ARG B 153     -27.485   3.329 -40.033  1.00 48.74           C  
ANISOU 2248  CA  ARG B 153     6056   6798   5665   1061   -139    246       C  
ATOM   2249  C   ARG B 153     -28.113   2.339 -39.075  1.00 46.89           C  
ANISOU 2249  C   ARG B 153     6116   6437   5260   1161   -210    166       C  
ATOM   2250  O   ARG B 153     -27.422   1.574 -38.464  1.00 47.96           O  
ANISOU 2250  O   ARG B 153     6347   6664   5209   1381   -262     81       O  
ATOM   2251  CB  ARG B 153     -26.899   4.464 -39.236  1.00 49.70           C  
ANISOU 2251  CB  ARG B 153     5893   6999   5990    931   -139    143       C  
ATOM   2252  CG  ARG B 153     -26.345   5.547 -40.082  1.00 52.54           C  
ANISOU 2252  CG  ARG B 153     6011   7426   6523    763    -20    207       C  
ATOM   2253  CD  ARG B 153     -25.264   5.052 -40.998  1.00 54.44           C  
ANISOU 2253  CD  ARG B 153     6149   7905   6628    894     35    228       C  
ATOM   2254  NE  ARG B 153     -24.791   6.183 -41.774  1.00 58.57           N  
ANISOU 2254  NE  ARG B 153     6474   8460   7319    674    192    286       N  
ATOM   2255  CZ  ARG B 153     -23.793   6.135 -42.644  1.00 61.11           C  
ANISOU 2255  CZ  ARG B 153     6642   8994   7580    691    305    297       C  
ATOM   2256  NH1 ARG B 153     -23.146   4.996 -42.840  1.00 62.21           N  
ANISOU 2256  NH1 ARG B 153     6781   9352   7501    964    260    250       N  
ATOM   2257  NH2 ARG B 153     -23.441   7.232 -43.308  1.00 62.10           N  
ANISOU 2257  NH2 ARG B 153     6642   9098   7853    440    486    351       N  
ATOM   2258  N   LEU B 154     -29.418   2.340 -38.938  1.00 45.00           N  
ANISOU 2258  N   LEU B 154     6032   5998   5065   1011   -201    189       N  
ATOM   2259  CA  LEU B 154     -30.019   1.401 -37.997  1.00 45.20           C  
ANISOU 2259  CA  LEU B 154     6370   5887   4917   1054   -222     98       C  
ATOM   2260  C   LEU B 154     -30.002   0.027 -38.643  1.00 46.49           C  
ANISOU 2260  C   LEU B 154     6861   6012   4791   1197   -187    129       C  
ATOM   2261  O   LEU B 154     -29.634  -0.960 -38.023  1.00 47.92           O  
ANISOU 2261  O   LEU B 154     7327   6146   4732   1393   -193     66       O  
ATOM   2262  CB  LEU B 154     -31.443   1.827 -37.597  1.00 42.11           C  
ANISOU 2262  CB  LEU B 154     6007   5329   4663    819   -195     75       C  
ATOM   2263  CG  LEU B 154     -32.244   0.779 -36.834  1.00 42.82           C  
ANISOU 2263  CG  LEU B 154     6455   5260   4555    787   -159    -17       C  
ATOM   2264  CD1 LEU B 154     -31.738   0.602 -35.387  1.00 40.67           C  
ANISOU 2264  CD1 LEU B 154     6308   4953   4190    901   -192   -130       C  
ATOM   2265  CD2 LEU B 154     -33.757   1.092 -36.867  1.00 42.41           C  
ANISOU 2265  CD2 LEU B 154     6371   5116   4625    530   -108    -43       C  
ATOM   2266  N   GLY B 155     -30.403  -0.018 -39.906  1.00 47.55           N  
ANISOU 2266  N   GLY B 155     6987   6153   4927   1111   -145    226       N  
ATOM   2267  CA  GLY B 155     -30.324  -1.233 -40.700  1.00 49.38           C  
ANISOU 2267  CA  GLY B 155     7523   6352   4886   1221    -94    249       C  
ATOM   2268  C   GLY B 155     -28.975  -1.901 -40.587  1.00 51.47           C  
ANISOU 2268  C   GLY B 155     7873   6720   4963   1554    -96    230       C  
ATOM   2269  O   GLY B 155     -28.898  -3.100 -40.351  1.00 52.18           O  
ANISOU 2269  O   GLY B 155     8358   6690   4776   1725    -57    187       O  
ATOM   2270  N   VAL B 156     -27.917  -1.122 -40.761  1.00 52.59           N  
ANISOU 2270  N   VAL B 156     7651   7086   5242   1648   -126    251       N  
ATOM   2271  CA  VAL B 156     -26.593  -1.652 -40.631  1.00 56.26           C  
ANISOU 2271  CA  VAL B 156     8094   7736   5545   1985   -141    207       C  
ATOM   2272  C   VAL B 156     -26.402  -2.320 -39.261  1.00 58.00           C  
ANISOU 2272  C   VAL B 156     8548   7899   5588   2209   -213    102       C  
ATOM   2273  O   VAL B 156     -26.004  -3.501 -39.165  1.00 59.59           O  
ANISOU 2273  O   VAL B 156     9100   8053   5489   2528   -196     85       O  
ATOM   2274  CB  VAL B 156     -25.564  -0.551 -40.786  1.00 57.31           C  
ANISOU 2274  CB  VAL B 156     7731   8156   5886   1965   -155    192       C  
ATOM   2275  CG1 VAL B 156     -24.173  -1.093 -40.490  1.00 60.01           C  
ANISOU 2275  CG1 VAL B 156     7968   8775   6055   2338   -194    101       C  
ATOM   2276  CG2 VAL B 156     -25.642   0.038 -42.183  1.00 57.45           C  
ANISOU 2276  CG2 VAL B 156     7594   8209   6023   1784    -56    314       C  
ATOM   2277  N   ALA B 157     -26.683  -1.557 -38.210  1.00 65.46           N  
ANISOU 2277  N   ALA B 157     9821   8683   6366   2083   -152   -261       N  
ATOM   2278  CA  ALA B 157     -26.449  -2.018 -36.851  1.00 65.62           C  
ANISOU 2278  CA  ALA B 157     9729   8707   6496   2195   -290   -289       C  
ATOM   2279  C   ALA B 157     -27.172  -3.337 -36.616  1.00 65.51           C  
ANISOU 2279  C   ALA B 157     9754   8687   6448   2269   -403   -236       C  
ATOM   2280  O   ALA B 157     -26.576  -4.263 -36.105  1.00 66.27           O  
ANISOU 2280  O   ALA B 157     9828   8736   6612   2336   -532   -323       O  
ATOM   2281  CB  ALA B 157     -26.865  -0.971 -35.855  1.00 64.40           C  
ANISOU 2281  CB  ALA B 157     9625   8529   6313   2215   -326   -203       C  
ATOM   2282  N   LEU B 158     -28.435  -3.425 -37.030  1.00 65.86           N  
ANISOU 2282  N   LEU B 158     9875   8752   6395   2259   -381   -136       N  
ATOM   2283  CA  LEU B 158     -29.198  -4.672 -36.981  1.00 67.10           C  
ANISOU 2283  CA  LEU B 158    10073   8910   6508   2274   -424   -120       C  
ATOM   2284  C   LEU B 158     -28.569  -5.878 -37.728  1.00 69.71           C  
ANISOU 2284  C   LEU B 158    10371   9246   6869   2296   -450   -177       C  
ATOM   2285  O   LEU B 158     -28.496  -7.009 -37.193  1.00 69.83           O  
ANISOU 2285  O   LEU B 158    10459   9204   6868   2329   -558   -200       O  
ATOM   2286  CB  LEU B 158     -30.585  -4.423 -37.541  1.00 66.13           C  
ANISOU 2286  CB  LEU B 158     9956   8818   6348   2267   -394    -99       C  
ATOM   2287  CG  LEU B 158     -31.776  -4.222 -36.619  1.00 64.51           C  
ANISOU 2287  CG  LEU B 158     9740   8617   6153   2230   -371   -158       C  
ATOM   2288  CD1 LEU B 158     -31.378  -4.038 -35.159  1.00 58.61           C  
ANISOU 2288  CD1 LEU B 158     9073   7820   5375   2167   -352   -155       C  
ATOM   2289  CD2 LEU B 158     -32.605  -3.071 -37.147  1.00 62.30           C  
ANISOU 2289  CD2 LEU B 158     9396   8337   5936   2293   -429   -213       C  
ATOM   2290  N   ASP B 159     -28.134  -5.633 -38.965  1.00 72.50           N  
ANISOU 2290  N   ASP B 159    10670   9635   7238   2254   -354   -214       N  
ATOM   2291  CA  ASP B 159     -27.517  -6.675 -39.773  1.00 75.49           C  
ANISOU 2291  CA  ASP B 159    10980  10032   7670   2249   -338   -317       C  
ATOM   2292  C   ASP B 159     -26.285  -7.172 -39.025  1.00 77.74           C  
ANISOU 2292  C   ASP B 159    11137  10275   8124   2325   -464   -502       C  
ATOM   2293  O   ASP B 159     -26.084  -8.376 -38.882  1.00 78.42           O  
ANISOU 2293  O   ASP B 159    11221  10316   8259   2412   -619   -574       O  
ATOM   2294  CB  ASP B 159     -27.207  -6.199 -41.214  1.00 76.68           C  
ANISOU 2294  CB  ASP B 159    11167  10198   7769   2113   -154   -364       C  
ATOM   2295  CG  ASP B 159     -25.699  -6.102 -41.536  1.00 80.44           C  
ANISOU 2295  CG  ASP B 159    11481  10688   8391   2001     -7   -630       C  
ATOM   2296  OD1 ASP B 159     -25.179  -6.996 -42.254  1.00 80.38           O  
ANISOU 2296  OD1 ASP B 159    11365  10708   8466   1960     53   -797       O  
ATOM   2297  OD2 ASP B 159     -25.047  -5.117 -41.110  1.00 83.10           O  
ANISOU 2297  OD2 ASP B 159    11775  11014   8785   1936     67   -719       O  
ATOM   2298  N   ASN B 160     -25.495  -6.245 -38.498  1.00 79.43           N  
ANISOU 2298  N   ASN B 160    11266  10476   8435   2313   -449   -604       N  
ATOM   2299  CA  ASN B 160     -24.241  -6.635 -37.887  1.00 82.37           C  
ANISOU 2299  CA  ASN B 160    11472  10788   9034   2420   -625   -873       C  
ATOM   2300  C   ASN B 160     -24.439  -7.507 -36.631  1.00 82.49           C  
ANISOU 2300  C   ASN B 160    11681  10651   9009   2590   -969   -819       C  
ATOM   2301  O   ASN B 160     -23.674  -8.426 -36.371  1.00 84.75           O  
ANISOU 2301  O   ASN B 160    11932  10826   9443   2737  -1243  -1031       O  
ATOM   2302  CB  ASN B 160     -23.374  -5.418 -37.601  1.00 83.72           C  
ANISOU 2302  CB  ASN B 160    11496  10977   9335   2359   -524  -1032       C  
ATOM   2303  CG  ASN B 160     -22.226  -5.753 -36.704  1.00 87.21           C  
ANISOU 2303  CG  ASN B 160    11767  11324  10044   2531   -806  -1339       C  
ATOM   2304  OD1 ASN B 160     -22.423  -6.077 -35.536  1.00 87.11           O  
ANISOU 2304  OD1 ASN B 160    11946  11173   9978   2690  -1116  -1244       O  
ATOM   2305  ND2 ASN B 160     -21.011  -5.708 -37.241  1.00 92.61           N  
ANISOU 2305  ND2 ASN B 160    12114  12051  11022   2486   -714  -1763       N  
ATOM   2306  N   LEU B 161     -25.487  -7.231 -35.876  1.00 80.88           N  
ANISOU 2306  N   LEU B 161    11728  10411   8592   2548   -961   -572       N  
ATOM   2307  CA  LEU B 161     -25.877  -8.098 -34.783  1.00 81.50           C  
ANISOU 2307  CA  LEU B 161    12141  10306   8518   2597  -1199   -501       C  
ATOM   2308  C   LEU B 161     -26.495  -9.397 -35.323  1.00 81.85           C  
ANISOU 2308  C   LEU B 161    12314  10330   8452   2576  -1214   -451       C  
ATOM   2309  O   LEU B 161     -26.957 -10.248 -34.564  1.00 82.30           O  
ANISOU 2309  O   LEU B 161    12738  10213   8316   2548  -1358   -389       O  
ATOM   2310  CB  LEU B 161     -26.845  -7.338 -33.850  1.00 80.31           C  
ANISOU 2310  CB  LEU B 161    12197  10138   8179   2472  -1081   -326       C  
ATOM   2311  CG  LEU B 161     -26.299  -6.334 -32.807  1.00 79.83           C  
ANISOU 2311  CG  LEU B 161    12169  10005   8154   2502  -1165   -352       C  
ATOM   2312  CD1 LEU B 161     -24.845  -5.900 -32.981  1.00 80.42           C  
ANISOU 2312  CD1 LEU B 161    11968  10087   8500   2646  -1300   -572       C  
ATOM   2313  CD2 LEU B 161     -27.178  -5.115 -32.734  1.00 77.76           C  
ANISOU 2313  CD2 LEU B 161    11836   9871   7835   2374   -901   -230       C  
ATOM   2314  N   GLY B 162     -26.499  -9.544 -36.644  1.00 82.14           N  
ANISOU 2314  N   GLY B 162    12106  10521   8580   2556  -1048   -485       N  
ATOM   2315  CA  GLY B 162     -27.068 -10.716 -37.285  1.00 83.04           C  
ANISOU 2315  CA  GLY B 162    12297  10640   8611   2540  -1043   -443       C  
ATOM   2316  C   GLY B 162     -28.559 -10.845 -37.073  1.00 83.09           C  
ANISOU 2316  C   GLY B 162    12502  10665   8401   2400   -888   -266       C  
ATOM   2317  O   GLY B 162     -29.085 -11.956 -37.036  1.00 83.58           O  
ANISOU 2317  O   GLY B 162    12761  10656   8340   2360   -928   -242       O  
ATOM   2318  N   ARG B 163     -29.251  -9.716 -36.915  1.00 83.40           N  
ANISOU 2318  N   ARG B 163    12480  10790   8415   2317   -711   -195       N  
ATOM   2319  CA  ARG B 163     -30.712  -9.747 -36.864  1.00 84.37           C  
ANISOU 2319  CA  ARG B 163    12663  10959   8432   2187   -544   -153       C  
ATOM   2320  C   ARG B 163     -31.315  -9.643 -38.268  1.00 84.56           C  
ANISOU 2320  C   ARG B 163    12487  11117   8522   2211   -445   -150       C  
ATOM   2321  O   ARG B 163     -32.534  -9.595 -38.415  1.00 84.68           O  
ANISOU 2321  O   ARG B 163    12465  11179   8529   2149   -349   -194       O  
ATOM   2322  CB  ARG B 163     -31.267  -8.641 -35.975  1.00 84.45           C  
ANISOU 2322  CB  ARG B 163    12686  10974   8425   2104   -447   -158       C  
ATOM   2323  CG  ARG B 163     -32.564  -9.025 -35.268  1.00 85.64           C  
ANISOU 2323  CG  ARG B 163    12984  11095   8461   1902   -282   -240       C  
ATOM   2324  CD  ARG B 163     -32.268  -9.224 -33.826  1.00 86.68           C  
ANISOU 2324  CD  ARG B 163    13480  11041   8412   1771   -315   -235       C  
ATOM   2325  NE  ARG B 163     -31.778  -7.963 -33.281  1.00 85.86           N  
ANISOU 2325  NE  ARG B 163    13288  10949   8384   1834   -352   -208       N  
ATOM   2326  CZ  ARG B 163     -32.538  -7.076 -32.645  1.00 86.14           C  
ANISOU 2326  CZ  ARG B 163    13273  11023   8431   1704   -180   -288       C  
ATOM   2327  NH1 ARG B 163     -31.991  -5.957 -32.198  1.00 85.03           N  
ANISOU 2327  NH1 ARG B 163    13061  10889   8358   1781   -239   -247       N  
ATOM   2328  NH2 ARG B 163     -33.836  -7.299 -32.445  1.00 86.85           N  
ANISOU 2328  NH2 ARG B 163    13356  11149   8494   1487     62   -461       N  
ATOM   2329  N   PHE B 164     -30.426  -9.587 -39.268  1.00 85.37           N  
ANISOU 2329  N   PHE B 164    12477  11258   8701   2287   -476   -152       N  
ATOM   2330  CA  PHE B 164     -30.711  -9.680 -40.714  1.00 86.22           C  
ANISOU 2330  CA  PHE B 164    12514  11431   8815   2294   -418   -144       C  
ATOM   2331  C   PHE B 164     -32.155  -9.459 -41.183  1.00 87.09           C  
ANISOU 2331  C   PHE B 164    12619  11570   8900   2289   -395   -141       C  
ATOM   2332  O   PHE B 164     -32.415  -8.556 -41.962  1.00 86.88           O  
ANISOU 2332  O   PHE B 164    12608  11531   8872   2320   -421   -132       O  
ATOM   2333  CB  PHE B 164     -30.094 -10.963 -41.304  1.00 86.61           C  
ANISOU 2333  CB  PHE B 164    12545  11476   8884   2317   -454   -190       C  
ATOM   2334  CG  PHE B 164     -28.590 -10.992 -41.234  1.00 86.86           C  
ANISOU 2334  CG  PHE B 164    12479  11484   9039   2353   -504   -319       C  
ATOM   2335  CD1 PHE B 164     -27.839  -9.947 -41.768  1.00 86.91           C  
ANISOU 2335  CD1 PHE B 164    12390  11524   9108   2288   -378   -394       C  
ATOM   2336  CD2 PHE B 164     -27.923 -12.058 -40.623  1.00 87.94           C  
ANISOU 2336  CD2 PHE B 164    12639  11532   9240   2443   -697   -422       C  
ATOM   2337  CE1 PHE B 164     -26.443  -9.959 -41.705  1.00 89.48           C  
ANISOU 2337  CE1 PHE B 164    12542  11841   9613   2291   -382   -627       C  
ATOM   2338  CE2 PHE B 164     -26.521 -12.086 -40.553  1.00 89.98           C  
ANISOU 2338  CE2 PHE B 164    12729  11756   9703   2518   -803   -655       C  
ATOM   2339  CZ  PHE B 164     -25.777 -11.035 -41.097  1.00 90.93           C  
ANISOU 2339  CZ  PHE B 164    12651  11956   9941   2432   -615   -788       C  
ATOM   2340  N   ASP B 165     -33.077 -10.295 -40.720  1.00 96.39           N  
ANISOU 2340  N   ASP B 165    16058  10031  10532    811  -3023  -2147       N  
ATOM   2341  CA  ASP B 165     -34.496 -10.087 -40.973  1.00 99.99           C  
ANISOU 2341  CA  ASP B 165    16194  10384  11412    125  -3358  -1805       C  
ATOM   2342  C   ASP B 165     -34.910  -8.662 -40.587  1.00 93.40           C  
ANISOU 2342  C   ASP B 165    14403  10370  10714    -69  -2379  -1620       C  
ATOM   2343  O   ASP B 165     -35.654  -8.005 -41.311  1.00 93.15           O  
ANISOU 2343  O   ASP B 165    14142  10488  10762    -87  -2336  -1617       O  
ATOM   2344  CB  ASP B 165     -35.319 -11.181 -40.259  1.00109.41           C  
ANISOU 2344  CB  ASP B 165    17437  11063  13068   -793  -4254  -1175       C  
ATOM   2345  CG  ASP B 165     -36.549 -10.645 -39.552  1.00112.28           C  
ANISOU 2345  CG  ASP B 165    16684  12100  13874  -1615  -3879   -337       C  
ATOM   2346  OD1 ASP B 165     -37.648 -10.660 -40.159  1.00119.44           O  
ANISOU 2346  OD1 ASP B 165    17355  12893  15131  -2075  -4447     74       O  
ATOM   2347  OD2 ASP B 165     -36.406 -10.230 -38.376  1.00110.75           O  
ANISOU 2347  OD2 ASP B 165    15870  12610  13600  -1667  -3063    -51       O  
ATOM   2348  N   GLU B 166     -34.394  -8.178 -39.459  1.00 88.61           N  
ANISOU 2348  N   GLU B 166    13397  10205  10064    -87  -1729  -1535       N  
ATOM   2349  CA  GLU B 166     -34.703  -6.838 -38.995  1.00 83.33           C  
ANISOU 2349  CA  GLU B 166    12147  10131   9382    -35  -1071  -1474       C  
ATOM   2350  C   GLU B 166     -33.989  -5.762 -39.770  1.00 77.31           C  
ANISOU 2350  C   GLU B 166    11416   9463   8496    408   -773  -1814       C  
ATOM   2351  O   GLU B 166     -34.570  -4.732 -40.051  1.00 75.52           O  
ANISOU 2351  O   GLU B 166    10938   9463   8290    455   -590  -1825       O  
ATOM   2352  CB  GLU B 166     -34.461  -6.693 -37.492  1.00 83.69           C  
ANISOU 2352  CB  GLU B 166    11980  10491   9326    -45   -732  -1294       C  
ATOM   2353  CG  GLU B 166     -35.721  -6.923 -36.653  1.00 91.25           C  
ANISOU 2353  CG  GLU B 166    12405  11969  10294   -333   -656   -629       C  
ATOM   2354  CD  GLU B 166     -37.012  -6.670 -37.445  1.00 97.34           C  
ANISOU 2354  CD  GLU B 166    12739  13006  11237   -547   -782   -293       C  
ATOM   2355  OE1 GLU B 166     -37.506  -7.618 -38.101  1.00102.91           O  
ANISOU 2355  OE1 GLU B 166    13500  13296  12302  -1105  -1450     32       O  
ATOM   2356  OE2 GLU B 166     -37.536  -5.531 -37.407  1.00 97.50           O  
ANISOU 2356  OE2 GLU B 166    12451  13567  11026   -118   -368   -358       O  
ATOM   2357  N   ALA B 167     -32.737  -5.990 -40.121  1.00 74.78           N  
ANISOU 2357  N   ALA B 167    11332   9054   8025    761   -753  -1953       N  
ATOM   2358  CA  ALA B 167     -32.052  -5.053 -40.979  1.00 72.53           C  
ANISOU 2358  CA  ALA B 167    10874   9020   7662   1107   -516  -1922       C  
ATOM   2359  C   ALA B 167     -32.784  -4.844 -42.321  1.00 73.53           C  
ANISOU 2359  C   ALA B 167    11101   9152   7684   1318   -609  -2014       C  
ATOM   2360  O   ALA B 167     -32.829  -3.706 -42.811  1.00 72.16           O  
ANISOU 2360  O   ALA B 167    10648   9195   7572   1346   -407  -1897       O  
ATOM   2361  CB  ALA B 167     -30.653  -5.487 -41.219  1.00 73.93           C  
ANISOU 2361  CB  ALA B 167    11083   9400   7606   1581   -431  -1786       C  
ATOM   2362  N   ILE B 168     -33.359  -5.915 -42.896  1.00 76.24           N  
ANISOU 2362  N   ILE B 168    11934   9140   7892   1446  -1086  -2201       N  
ATOM   2363  CA  ILE B 168     -34.000  -5.813 -44.209  1.00 77.79           C  
ANISOU 2363  CA  ILE B 168    12393   9230   7930   1761  -1347  -2350       C  
ATOM   2364  C   ILE B 168     -35.160  -4.814 -44.155  1.00 74.41           C  
ANISOU 2364  C   ILE B 168    11495   8935   7841   1258  -1204  -2249       C  
ATOM   2365  O   ILE B 168     -35.205  -3.894 -44.967  1.00 72.90           O  
ANISOU 2365  O   ILE B 168    11181   8962   7555   1513   -980  -2267       O  
ATOM   2366  CB  ILE B 168     -34.377  -7.203 -44.898  1.00 85.05           C  
ANISOU 2366  CB  ILE B 168    14225   9467   8620   2087  -2303  -2624       C  
ATOM   2367  CG1 ILE B 168     -35.553  -7.934 -44.229  1.00 88.53           C  
ANISOU 2367  CG1 ILE B 168    14676   9357   9604   1143  -3035  -2396       C  
ATOM   2368  CG2 ILE B 168     -33.176  -8.124 -45.012  1.00 88.62           C  
ANISOU 2368  CG2 ILE B 168    15312   9854   8504   2961  -2475  -2821       C  
ATOM   2369  CD1 ILE B 168     -36.855  -7.895 -45.012  1.00 92.05           C  
ANISOU 2369  CD1 ILE B 168    15181   9474  10319    816  -3696  -2308       C  
ATOM   2370  N   ASP B 169     -36.047  -4.964 -43.169  1.00 73.55           N  
ANISOU 2370  N   ASP B 169    11070   8829   8045    659  -1290  -2043       N  
ATOM   2371  CA  ASP B 169     -37.182  -4.042 -42.978  1.00 71.99           C  
ANISOU 2371  CA  ASP B 169    10361   8989   8002    437  -1095  -1876       C  
ATOM   2372  C   ASP B 169     -36.765  -2.581 -42.881  1.00 65.91           C  
ANISOU 2372  C   ASP B 169     9443   8491   7108    736   -633  -2016       C  
ATOM   2373  O   ASP B 169     -37.423  -1.698 -43.431  1.00 65.65           O  
ANISOU 2373  O   ASP B 169     9298   8589   7057    860   -597  -2074       O  
ATOM   2374  CB  ASP B 169     -37.960  -4.377 -41.710  1.00 75.57           C  
ANISOU 2374  CB  ASP B 169    10328   9787   8596     40  -1045  -1411       C  
ATOM   2375  CG  ASP B 169     -38.435  -5.790 -41.686  1.00 83.23           C  
ANISOU 2375  CG  ASP B 169    11358  10408   9857   -513  -1731   -995       C  
ATOM   2376  OD1 ASP B 169     -39.476  -6.054 -41.049  1.00 91.23           O  
ANISOU 2376  OD1 ASP B 169    11715  11858  11089   -971  -1825   -265       O  
ATOM   2377  OD2 ASP B 169     -37.765  -6.643 -42.298  1.00 86.26           O  
ANISOU 2377  OD2 ASP B 169    12449  10115  10209   -423  -2267  -1295       O  
ATOM   2378  N   SER B 170     -35.684  -2.334 -42.165  1.00 60.77           N  
ANISOU 2378  N   SER B 170     8848   7827   6414    810   -456  -2027       N  
ATOM   2379  CA  SER B 170     -35.187  -0.991 -42.052  1.00 57.12           C  
ANISOU 2379  CA  SER B 170     8379   7364   5957    950   -404  -2041       C  
ATOM   2380  C   SER B 170     -34.619  -0.545 -43.365  1.00 55.92           C  
ANISOU 2380  C   SER B 170     8222   7204   5821   1072   -403  -1908       C  
ATOM   2381  O   SER B 170     -34.775   0.613 -43.747  1.00 55.98           O  
ANISOU 2381  O   SER B 170     8212   7166   5890   1093   -512  -1841       O  
ATOM   2382  CB  SER B 170     -34.161  -0.859 -40.934  1.00 56.50           C  
ANISOU 2382  CB  SER B 170     8383   7157   5925    904   -471  -1974       C  
ATOM   2383  OG  SER B 170     -34.834  -0.809 -39.689  1.00 56.60           O  
ANISOU 2383  OG  SER B 170     8460   7293   5750   1054   -459  -2089       O  
ATOM   2384  N   PHE B 171     -33.970  -1.468 -44.070  1.00 55.61           N  
ANISOU 2384  N   PHE B 171     8248   7254   5626   1291   -324  -1821       N  
ATOM   2385  CA  PHE B 171     -33.508  -1.186 -45.410  1.00 55.66           C  
ANISOU 2385  CA  PHE B 171     8205   7522   5419   1700   -209  -1580       C  
ATOM   2386  C   PHE B 171     -34.706  -0.932 -46.329  1.00 54.97           C  
ANISOU 2386  C   PHE B 171     8299   7331   5252   1813   -336  -1843       C  
ATOM   2387  O   PHE B 171     -34.722   0.042 -47.078  1.00 55.17           O  
ANISOU 2387  O   PHE B 171     8193   7504   5262   1912   -267  -1633       O  
ATOM   2388  CB  PHE B 171     -32.582  -2.295 -45.907  1.00 59.24           C  
ANISOU 2388  CB  PHE B 171     8820   8240   5445   2325   -108  -1480       C  
ATOM   2389  CG  PHE B 171     -31.226  -2.293 -45.226  1.00 58.80           C  
ANISOU 2389  CG  PHE B 171     8371   8505   5462   2288     80   -999       C  
ATOM   2390  CD1 PHE B 171     -30.617  -1.081 -44.879  1.00 54.88           C  
ANISOU 2390  CD1 PHE B 171     7328   8137   5385   1799     69   -392       C  
ATOM   2391  CD2 PHE B 171     -30.559  -3.493 -44.926  1.00 58.64           C  
ANISOU 2391  CD2 PHE B 171     8584   8564   5132   2717     81  -1104       C  
ATOM   2392  CE1 PHE B 171     -29.362  -1.052 -44.230  1.00 55.47           C  
ANISOU 2392  CE1 PHE B 171     6960   8456   5658   1628     52    197       C  
ATOM   2393  CE2 PHE B 171     -29.302  -3.465 -44.273  1.00 58.57           C  
ANISOU 2393  CE2 PHE B 171     8112   8919   5221   2675    242   -593       C  
ATOM   2394  CZ  PHE B 171     -28.707  -2.236 -43.924  1.00 54.58           C  
ANISOU 2394  CZ  PHE B 171     6931   8582   5224   2076    224    105       C  
ATOM   2395  N   LYS B 172     -35.727  -1.775 -46.225  1.00 51.16           N  
ANISOU 2395  N   LYS B 172     7018   6273   6146    562   -561   -307       N  
ATOM   2396  CA  LYS B 172     -36.977  -1.554 -46.947  1.00 50.90           C  
ANISOU 2396  CA  LYS B 172     6859   6208   6270    492   -592   -283       C  
ATOM   2397  C   LYS B 172     -37.636  -0.192 -46.657  1.00 49.63           C  
ANISOU 2397  C   LYS B 172     6471   6094   6290    429   -444   -271       C  
ATOM   2398  O   LYS B 172     -38.080   0.480 -47.586  1.00 49.80           O  
ANISOU 2398  O   LYS B 172     6381   6136   6403    493   -491   -253       O  
ATOM   2399  CB  LYS B 172     -37.967  -2.685 -46.689  1.00 53.19           C  
ANISOU 2399  CB  LYS B 172     7244   6364   6601    327   -680   -288       C  
ATOM   2400  CG  LYS B 172     -37.747  -3.899 -47.613  1.00 55.99           C  
ANISOU 2400  CG  LYS B 172     7799   6624   6851    431   -933   -323       C  
ATOM   2401  CD  LYS B 172     -38.034  -5.197 -46.874  1.00 59.93           C  
ANISOU 2401  CD  LYS B 172     8530   6927   7311    262  -1036   -307       C  
ATOM   2402  CE  LYS B 172     -39.520  -5.522 -46.768  1.00 62.26           C  
ANISOU 2402  CE  LYS B 172     8730   7140   7785    -18  -1038   -273       C  
ATOM   2403  NZ  LYS B 172     -39.857  -6.706 -47.612  1.00 63.49           N  
ANISOU 2403  NZ  LYS B 172     9060   7113   7950    -23  -1333   -313       N  
ATOM   2404  N   ILE B 173     -37.673   0.239 -45.398  1.00 47.68           N  
ANISOU 2404  N   ILE B 173     6176   5861   6079    339   -293   -296       N  
ATOM   2405  CA  ILE B 173     -38.136   1.597 -45.093  1.00 46.43           C  
ANISOU 2405  CA  ILE B 173     5820   5739   6079    341   -190   -328       C  
ATOM   2406  C   ILE B 173     -37.225   2.651 -45.718  1.00 45.92           C  
ANISOU 2406  C   ILE B 173     5736   5684   6025    462   -211   -285       C  
ATOM   2407  O   ILE B 173     -37.687   3.524 -46.420  1.00 46.41           O  
ANISOU 2407  O   ILE B 173     5705   5720   6209    510   -259   -260       O  
ATOM   2408  CB  ILE B 173     -38.324   1.849 -43.562  1.00 46.34           C  
ANISOU 2408  CB  ILE B 173     5762   5771   6072    251    -31   -396       C  
ATOM   2409  CG1 ILE B 173     -39.593   1.155 -43.049  1.00 46.25           C  
ANISOU 2409  CG1 ILE B 173     5680   5803   6089     78     28   -419       C  
ATOM   2410  CG2 ILE B 173     -38.362   3.337 -43.248  1.00 44.48           C  
ANISOU 2410  CG2 ILE B 173     5372   5552   5973    329     25   -465       C  
ATOM   2411  CD1 ILE B 173     -39.538   0.792 -41.607  1.00 44.21           C  
ANISOU 2411  CD1 ILE B 173     5484   5608   5705    -39    173   -433       C  
ATOM   2412  N   ALA B 174     -35.929   2.564 -45.489  1.00 45.91           N  
ANISOU 2412  N   ALA B 174     5824   5725   5893    501   -190   -271       N  
ATOM   2413  CA  ALA B 174     -35.018   3.565 -46.057  1.00 46.74           C  
ANISOU 2413  CA  ALA B 174     5886   5866   6006    551   -192   -210       C  
ATOM   2414  C   ALA B 174     -35.107   3.603 -47.579  1.00 48.22           C  
ANISOU 2414  C   ALA B 174     6078   6087   6154    614   -289   -107       C  
ATOM   2415  O   ALA B 174     -34.857   4.647 -48.212  1.00 48.68           O  
ANISOU 2415  O   ALA B 174     6094   6140   6261    612   -298    -10       O  
ATOM   2416  CB  ALA B 174     -33.590   3.312 -45.622  1.00 45.94           C  
ANISOU 2416  CB  ALA B 174     5836   5861   5755    578   -160   -237       C  
ATOM   2417  N   LEU B 175     -35.450   2.464 -48.174  1.00 49.45           N  
ANISOU 2417  N   LEU B 175     6310   6267   6211    666   -381   -124       N  
ATOM   2418  CA  LEU B 175     -35.564   2.436 -49.619  1.00 51.50           C  
ANISOU 2418  CA  LEU B 175     6584   6583   6401    759   -487    -51       C  
ATOM   2419  C   LEU B 175     -36.847   3.179 -50.030  1.00 51.69           C  
ANISOU 2419  C   LEU B 175     6528   6500   6610    748   -544    -24       C  
ATOM   2420  O   LEU B 175     -36.844   3.914 -50.998  1.00 52.62           O  
ANISOU 2420  O   LEU B 175     6645   6629   6717    803   -600     78       O  
ATOM   2421  CB  LEU B 175     -35.465   1.009 -50.174  1.00 52.48           C  
ANISOU 2421  CB  LEU B 175     6824   6757   6356    857   -613   -114       C  
ATOM   2422  CG  LEU B 175     -34.666   0.909 -51.480  1.00 56.08           C  
ANISOU 2422  CG  LEU B 175     7308   7402   6597   1009   -678    -68       C  
ATOM   2423  CD1 LEU B 175     -33.450   1.862 -51.505  1.00 57.48           C  
ANISOU 2423  CD1 LEU B 175     7403   7744   6692    980   -541     22       C  
ATOM   2424  CD2 LEU B 175     -34.229  -0.529 -51.738  1.00 57.69           C  
ANISOU 2424  CD2 LEU B 175     7641   7666   6611   1155   -814   -193       C  
ATOM   2425  N   GLY B 176     -37.914   3.013 -49.253  1.00 51.12           N  
ANISOU 2425  N   GLY B 176     6384   6344   6695    678   -528   -120       N  
ATOM   2426  CA  GLY B 176     -39.042   3.938 -49.281  1.00 51.87           C  
ANISOU 2426  CA  GLY B 176     6350   6366   6991    688   -561   -152       C  
ATOM   2427  C   GLY B 176     -38.681   5.432 -49.292  1.00 52.12           C  
ANISOU 2427  C   GLY B 176     6366   6327   7110    721   -550    -84       C  
ATOM   2428  O   GLY B 176     -39.238   6.201 -50.069  1.00 52.97           O  
ANISOU 2428  O   GLY B 176     6465   6361   7300    804   -670    -40       O  
ATOM   2429  N   LEU B 177     -37.746   5.858 -48.454  1.00 51.44           N  
ANISOU 2429  N   LEU B 177     6298   6236   7009    660   -439    -77       N  
ATOM   2430  CA  LEU B 177     -37.417   7.295 -48.390  1.00 52.61           C  
ANISOU 2430  CA  LEU B 177     6449   6266   7272    659   -461    -19       C  
ATOM   2431  C   LEU B 177     -36.543   7.771 -49.560  1.00 54.24           C  
ANISOU 2431  C   LEU B 177     6758   6482   7367    642   -512    189       C  
ATOM   2432  O   LEU B 177     -36.617   8.923 -49.935  1.00 55.03           O  
ANISOU 2432  O   LEU B 177     6905   6436   7567    637   -599    288       O  
ATOM   2433  CB  LEU B 177     -36.747   7.645 -47.061  1.00 51.18           C  
ANISOU 2433  CB  LEU B 177     6241   6072   7132    591   -350   -106       C  
ATOM   2434  CG  LEU B 177     -37.545   7.342 -45.794  1.00 51.40           C  
ANISOU 2434  CG  LEU B 177     6171   6128   7230    599   -273   -298       C  
ATOM   2435  CD1 LEU B 177     -36.614   7.306 -44.573  1.00 50.56           C  
ANISOU 2435  CD1 LEU B 177     6085   6061   7062    546   -162   -369       C  
ATOM   2436  CD2 LEU B 177     -38.654   8.361 -45.596  1.00 51.59           C  
ANISOU 2436  CD2 LEU B 177     6090   6053   7458    692   -352   -413       C  
ATOM   2437  N   ARG B 178     -35.686   6.888 -50.083  1.00 55.30           N  
ANISOU 2437  N   ARG B 178     6932   6798   7280    631   -461    251       N  
ATOM   2438  CA  ARG B 178     -34.796   7.206 -51.207  1.00 58.51           C  
ANISOU 2438  CA  ARG B 178     7397   7315   7516    603   -466    445       C  
ATOM   2439  C   ARG B 178     -34.768   5.986 -52.099  1.00 59.56           C  
ANISOU 2439  C   ARG B 178     7562   7640   7425    718   -501    430       C  
ATOM   2440  O   ARG B 178     -34.028   5.040 -51.824  1.00 58.69           O  
ANISOU 2440  O   ARG B 178     7440   7689   7169    743   -442    344       O  
ATOM   2441  CB  ARG B 178     -33.371   7.526 -50.751  1.00 58.57           C  
ANISOU 2441  CB  ARG B 178     7365   7430   7457    473   -344    491       C  
ATOM   2442  CG  ARG B 178     -33.255   8.739 -49.870  1.00 59.42           C  
ANISOU 2442  CG  ARG B 178     7455   7333   7786    355   -340    489       C  
ATOM   2443  CD  ARG B 178     -31.865   9.312 -49.877  1.00 61.29           C  
ANISOU 2443  CD  ARG B 178     7652   7670   7965    181   -261    601       C  
ATOM   2444  NE  ARG B 178     -31.814  10.466 -48.983  1.00 64.20           N  
ANISOU 2444  NE  ARG B 178     8023   7793   8575     74   -303    570       N  
ATOM   2445  CZ  ARG B 178     -30.714  10.926 -48.382  1.00 65.39           C  
ANISOU 2445  CZ  ARG B 178     8104   7977   8764    -80   -249    559       C  
ATOM   2446  NH1 ARG B 178     -29.540  10.335 -48.569  1.00 65.09           N  
ANISOU 2446  NH1 ARG B 178     7957   8243   8530   -145   -133    572       N  
ATOM   2447  NH2 ARG B 178     -30.791  11.983 -47.577  1.00 65.70           N  
ANISOU 2447  NH2 ARG B 178     8168   7752   9042   -151   -333    502       N  
ATOM   2448  N   PRO B 179     -35.586   5.990 -53.164  1.00 61.85           N  
ANISOU 2448  N   PRO B 179     7907   7905   7686    818   -632    489       N  
ATOM   2449  CA  PRO B 179     -35.731   4.788 -53.970  1.00 63.31           C  
ANISOU 2449  CA  PRO B 179     8131   8241   7683    955   -711    426       C  
ATOM   2450  C   PRO B 179     -34.526   4.403 -54.851  1.00 66.01           C  
ANISOU 2450  C   PRO B 179     8500   8873   7706   1010   -664    505       C  
ATOM   2451  O   PRO B 179     -34.457   3.260 -55.303  1.00 65.73           O  
ANISOU 2451  O   PRO B 179     8496   8973   7503   1155   -737    390       O  
ATOM   2452  CB  PRO B 179     -36.971   5.100 -54.829  1.00 64.55           C  
ANISOU 2452  CB  PRO B 179     8325   8284   7915   1056   -885    453       C  
ATOM   2453  CG  PRO B 179     -37.688   6.156 -54.083  1.00 63.40           C  
ANISOU 2453  CG  PRO B 179     8130   7912   8046    991   -895    442       C  
ATOM   2454  CD  PRO B 179     -36.581   7.003 -53.551  1.00 63.25           C  
ANISOU 2454  CD  PRO B 179     8121   7884   8028    847   -759    559       C  
ATOM   2455  N   ASN B 180     -33.589   5.325 -55.073  1.00 68.77           N  
ANISOU 2455  N   ASN B 180     8828   9329   7971    890   -552    683       N  
ATOM   2456  CA AASN B 180     -32.459   5.066 -55.963  0.50 71.77           C  
ANISOU 2456  CA AASN B 180     9182  10065   8023    924   -476    763       C  
ATOM   2457  CA BASN B 180     -32.457   5.070 -55.964  0.50 71.78           C  
ANISOU 2457  CA BASN B 180     9182  10066   8024    923   -476    764       C  
ATOM   2458  C   ASN B 180     -31.089   5.160 -55.280  1.00 72.34           C  
ANISOU 2458  C   ASN B 180     9121  10327   8036    799   -305    743       C  
ATOM   2459  O   ASN B 180     -30.092   5.525 -55.924  1.00 75.18           O  
ANISOU 2459  O   ASN B 180     9405  10982   8178    718   -193    879       O  
ATOM   2460  CB AASN B 180     -32.496   6.014 -57.175  0.50 75.18           C  
ANISOU 2460  CB AASN B 180     9691  10558   8314    871   -491   1036       C  
ATOM   2461  CB BASN B 180     -32.480   6.031 -57.166  0.50 75.19           C  
ANISOU 2461  CB BASN B 180     9690  10559   8316    867   -488   1038       C  
ATOM   2462  CG AASN B 180     -33.836   6.002 -57.907  0.50 75.99           C  
ANISOU 2462  CG AASN B 180     9924  10481   8465   1026   -693   1045       C  
ATOM   2463  CG BASN B 180     -33.796   5.999 -57.937  0.50 76.05           C  
ANISOU 2463  CG BASN B 180     9932  10503   8461   1025   -689   1049       C  
ATOM   2464  OD1AASN B 180     -34.412   7.057 -58.169  0.50 77.91           O  
ANISOU 2464  OD1AASN B 180    10264  10510   8826    961   -770   1214       O  
ATOM   2465  OD1BASN B 180     -34.351   7.047 -58.263  0.50 78.08           O  
ANISOU 2465  OD1BASN B 180    10290  10558   8818    964   -766   1227       O  
ATOM   2466  ND2AASN B 180     -34.332   4.812 -58.240  0.50 74.71           N  
ANISOU 2466  ND2AASN B 180     9774  10390   8220   1239   -812    848       N  
ATOM   2467  ND2BASN B 180     -34.293   4.800 -58.236  0.50 74.72           N  
ANISOU 2467  ND2BASN B 180     9773  10400   8216   1238   -808    848       N  
ATOM   2468  N   GLU B 181     -31.020   4.850 -53.980  1.00 70.15           N  
ANISOU 2468  N   GLU B 181     8803   9912   7937    773   -282    573       N  
ATOM   2469  CA  GLU B 181     -29.706   4.777 -53.306  1.00 70.17           C  
ANISOU 2469  CA  GLU B 181     8674  10115   7872    706   -158    498       C  
ATOM   2470  C   GLU B 181     -29.137   3.373 -53.495  1.00 69.85           C  
ANISOU 2470  C   GLU B 181     8616  10338   7585    940   -202    291       C  
ATOM   2471  O   GLU B 181     -29.714   2.398 -53.014  1.00 67.99           O  
ANISOU 2471  O   GLU B 181     8487   9944   7402   1077   -319    124       O  
ATOM   2472  CB  GLU B 181     -29.787   5.128 -51.810  1.00 68.13           C  
ANISOU 2472  CB  GLU B 181     8398   9607   7879    598   -131    402       C  
ATOM   2473  CG  GLU B 181     -29.937   6.618 -51.515  1.00 69.01           C  
ANISOU 2473  CG  GLU B 181     8500   9501   8218    378    -99    562       C  
ATOM   2474  CD  GLU B 181     -28.624   7.374 -51.328  1.00 70.94           C  
ANISOU 2474  CD  GLU B 181     8608   9905   8441    176     12    639       C  
ATOM   2475  OE1 GLU B 181     -27.536   6.778 -51.484  1.00 72.74           O  
ANISOU 2475  OE1 GLU B 181     8703  10476   8456    213     89    563       O  
ATOM   2476  OE2 GLU B 181     -28.687   8.586 -51.015  1.00 71.60           O  
ANISOU 2476  OE2 GLU B 181     8708   9763   8730    -17      2    757       O  
ATOM   2477  N   GLY B 182     -28.016   3.270 -54.204  1.00 71.94           N  
ANISOU 2477  N   GLY B 182     8749  11010   7575    982   -122    299       N  
ATOM   2478  CA  GLY B 182     -27.365   1.978 -54.417  1.00 72.27           C  
ANISOU 2478  CA  GLY B 182     8762  11335   7362   1259   -193     58       C  
ATOM   2479  C   GLY B 182     -26.920   1.259 -53.146  1.00 70.32           C  
ANISOU 2479  C   GLY B 182     8523  10999   7193   1346   -247   -175       C  
ATOM   2480  O   GLY B 182     -27.182   0.054 -52.978  1.00 69.22           O  
ANISOU 2480  O   GLY B 182     8530  10772   6998   1575   -419   -369       O  
ATOM   2481  N   LYS B 183     -26.258   1.989 -52.245  1.00 69.50           N  
ANISOU 2481  N   LYS B 183     8291  10895   7219   1162   -129   -157       N  
ATOM   2482  CA  LYS B 183     -25.763   1.365 -51.023  1.00 67.92           C  
ANISOU 2482  CA  LYS B 183     8109  10634   7063   1259   -189   -378       C  
ATOM   2483  C   LYS B 183     -26.866   0.622 -50.293  1.00 64.82           C  
ANISOU 2483  C   LYS B 183     7973   9840   6813   1329   -332   -444       C  
ATOM   2484  O   LYS B 183     -26.613  -0.415 -49.658  1.00 64.65           O  
ANISOU 2484  O   LYS B 183     8070   9773   6721   1508   -462   -635       O  
ATOM   2485  CB  LYS B 183     -25.082   2.370 -50.095  1.00 68.14           C  
ANISOU 2485  CB  LYS B 183     7980  10658   7251   1036    -65   -348       C  
ATOM   2486  CG  LYS B 183     -25.993   3.321 -49.345  1.00 66.75           C  
ANISOU 2486  CG  LYS B 183     7895  10083   7384    811    -32   -210       C  
ATOM   2487  CD  LYS B 183     -25.172   4.480 -48.799  1.00 68.22           C  
ANISOU 2487  CD  LYS B 183     7899  10320   7700    578     73   -163       C  
ATOM   2488  CE  LYS B 183     -26.051   5.492 -48.110  1.00 66.80           C  
ANISOU 2488  CE  LYS B 183     7813   9749   7818    398     73    -58       C  
ATOM   2489  NZ  LYS B 183     -25.267   6.344 -47.171  1.00 67.20           N  
ANISOU 2489  NZ  LYS B 183     7736   9776   8018    235    108   -113       N  
ATOM   2490  N   VAL B 184     -28.092   1.133 -50.396  1.00 62.30           N  
ANISOU 2490  N   VAL B 184     7742   9242   6685   1185   -321   -285       N  
ATOM   2491  CA  VAL B 184     -29.170   0.504 -49.675  1.00 59.43           C  
ANISOU 2491  CA  VAL B 184     7568   8549   6461   1192   -420   -334       C  
ATOM   2492  C   VAL B 184     -29.541  -0.813 -50.325  1.00 60.88           C  
ANISOU 2492  C   VAL B 184     7911   8718   6501   1396   -608   -436       C  
ATOM   2493  O   VAL B 184     -29.806  -1.784 -49.623  1.00 60.32           O  
ANISOU 2493  O   VAL B 184     8014   8462   6439   1455   -731   -543       O  
ATOM   2494  CB  VAL B 184     -30.374   1.421 -49.492  1.00 57.74           C  
ANISOU 2494  CB  VAL B 184     7356   8083   6499   1002   -362   -188       C  
ATOM   2495  CG1 VAL B 184     -31.502   0.682 -48.781  1.00 54.08           C  
ANISOU 2495  CG1 VAL B 184     7038   7358   6150    986   -440   -248       C  
ATOM   2496  CG2 VAL B 184     -29.961   2.648 -48.714  1.00 56.07           C  
ANISOU 2496  CG2 VAL B 184     7027   7838   6438    832   -230   -134       C  
ATOM   2497  N   HIS B 185     -29.534  -0.861 -51.656  1.00 64.63           N  
ANISOU 2497  N   HIS B 185     9972   8399   6184   1864   -995  -2343       N  
ATOM   2498  CA  HIS B 185     -29.765  -2.115 -52.368  1.00 65.27           C  
ANISOU 2498  CA  HIS B 185     9741   8640   6417   1978  -1251  -2505       C  
ATOM   2499  C   HIS B 185     -28.778  -3.227 -52.016  1.00 66.67           C  
ANISOU 2499  C   HIS B 185     9890   8794   6643   1884  -1358  -2560       C  
ATOM   2500  O   HIS B 185     -29.187  -4.352 -51.759  1.00 66.60           O  
ANISOU 2500  O   HIS B 185     9808   8698   6799   1865  -1430  -2684       O  
ATOM   2501  CB  HIS B 185     -29.829  -1.885 -53.873  1.00 65.22           C  
ANISOU 2501  CB  HIS B 185     9634   8870   6275   2147  -1377  -2541       C  
ATOM   2502  CG  HIS B 185     -31.169  -1.414 -54.335  1.00 63.59           C  
ANISOU 2502  CG  HIS B 185     9227   8746   6186   2205  -1420  -2354       C  
ATOM   2503  ND1 HIS B 185     -32.251  -2.258 -54.447  1.00 61.84           N  
ANISOU 2503  ND1 HIS B 185     8791   8552   6152   2089  -1667  -2277       N  
ATOM   2504  CD2 HIS B 185     -31.614  -0.182 -54.673  1.00 60.15           C  
ANISOU 2504  CD2 HIS B 185     8704   8376   5774   2347  -1243  -2080       C  
ATOM   2505  CE1 HIS B 185     -33.301  -1.568 -54.850  1.00 62.88           C  
ANISOU 2505  CE1 HIS B 185     8606   8814   6469   2140  -1687  -1856       C  
ATOM   2506  NE2 HIS B 185     -32.941  -0.307 -54.992  1.00 61.24           N  
ANISOU 2506  NE2 HIS B 185     8468   8614   6186   2347  -1376  -1737       N  
ATOM   2507  N   ARG B 186     -27.493  -2.905 -51.981  1.00 69.37           N  
ANISOU 2507  N   ARG B 186    10242   9214   6900   1819  -1349  -2354       N  
ATOM   2508  CA  ARG B 186     -26.474  -3.864 -51.576  1.00 73.14           C  
ANISOU 2508  CA  ARG B 186    10544   9685   7561   1764  -1376  -2137       C  
ATOM   2509  C   ARG B 186     -26.824  -4.502 -50.237  1.00 73.69           C  
ANISOU 2509  C   ARG B 186    10646   9587   7765   1488  -1465  -2119       C  
ATOM   2510  O   ARG B 186     -26.990  -5.725 -50.129  1.00 73.96           O  
ANISOU 2510  O   ARG B 186    10546   9534   8018   1594  -1440  -2216       O  
ATOM   2511  CB  ARG B 186     -25.122  -3.153 -51.463  1.00 75.51           C  
ANISOU 2511  CB  ARG B 186    10735  10135   7818   1592  -1436  -1640       C  
ATOM   2512  CG  ARG B 186     -23.893  -4.076 -51.497  1.00 80.35           C  
ANISOU 2512  CG  ARG B 186    10938  10814   8776   1709  -1353  -1134       C  
ATOM   2513  CD  ARG B 186     -22.671  -3.365 -52.100  1.00 84.98           C  
ANISOU 2513  CD  ARG B 186    11273  11610   9405   1766  -1310   -578       C  
ATOM   2514  NE  ARG B 186     -22.775  -3.247 -53.556  1.00 86.20           N  
ANISOU 2514  NE  ARG B 186    11540  11751   9458   2282   -969   -876       N  
ATOM   2515  CZ  ARG B 186     -22.895  -2.107 -54.238  1.00 86.67           C  
ANISOU 2515  CZ  ARG B 186    11766  11932   9230   2303  -1012  -1019       C  
ATOM   2516  NH1 ARG B 186     -22.917  -0.928 -53.619  1.00 86.20           N  
ANISOU 2516  NH1 ARG B 186    11837  11966   8948   1869  -1305   -908       N  
ATOM   2517  NH2 ARG B 186     -22.988  -2.147 -55.561  1.00 87.67           N  
ANISOU 2517  NH2 ARG B 186    12050  12027   9233   2722   -719  -1266       N  
ATOM   2518  N   ALA B 187     -26.961  -3.642 -49.233  1.00 74.75           N  
ANISOU 2518  N   ALA B 187    11092   9606   7702   1108  -1513  -2010       N  
ATOM   2519  CA  ALA B 187     -27.077  -4.068 -47.861  1.00 76.44           C  
ANISOU 2519  CA  ALA B 187    11496   9624   7923    725  -1593  -1917       C  
ATOM   2520  C   ALA B 187     -28.274  -4.986 -47.642  1.00 75.65           C  
ANISOU 2520  C   ALA B 187    11317   9368   8056    944  -1475  -2243       C  
ATOM   2521  O   ALA B 187     -28.179  -5.935 -46.845  1.00 75.91           O  
ANISOU 2521  O   ALA B 187    11268   9321   8251    790  -1566  -2180       O  
ATOM   2522  CB  ALA B 187     -27.128  -2.853 -46.938  1.00 78.27           C  
ANISOU 2522  CB  ALA B 187    12414   9604   7720    225  -1536  -1808       C  
ATOM   2523  N   ILE B 188     -29.376  -4.731 -48.355  1.00 75.14           N  
ANISOU 2523  N   ILE B 188    11212   9293   8045   1258  -1322  -2479       N  
ATOM   2524  CA  ILE B 188     -30.577  -5.563 -48.206  1.00 75.96           C  
ANISOU 2524  CA  ILE B 188    11156   9293   8410   1389  -1293  -2633       C  
ATOM   2525  C   ILE B 188     -30.365  -6.957 -48.780  1.00 76.64           C  
ANISOU 2525  C   ILE B 188    10988   9471   8657   1486  -1489  -2782       C  
ATOM   2526  O   ILE B 188     -30.974  -7.937 -48.318  1.00 77.00           O  
ANISOU 2526  O   ILE B 188    10953   9399   8903   1444  -1538  -2869       O  
ATOM   2527  CB  ILE B 188     -31.831  -5.036 -48.956  1.00 76.86           C  
ANISOU 2527  CB  ILE B 188    11117   9453   8632   1624  -1195  -2601       C  
ATOM   2528  CG1 ILE B 188     -31.680  -3.582 -49.396  1.00 78.01           C  
ANISOU 2528  CG1 ILE B 188    11431   9630   8576   1719   -986  -2466       C  
ATOM   2529  CG2 ILE B 188     -33.109  -5.294 -48.119  1.00 77.79           C  
ANISOU 2529  CG2 ILE B 188    11159   9343   9054   1657   -988  -2458       C  
ATOM   2530  CD1 ILE B 188     -32.777  -3.112 -50.333  1.00 80.43           C  
ANISOU 2530  CD1 ILE B 188    11423  10076   9060   1957   -953  -2266       C  
ATOM   2531  N   ALA B 189     -29.542  -7.039 -49.815  1.00 77.65           N  
ANISOU 2531  N   ALA B 189    11085   9739   8679   1629  -1510  -2801       N  
ATOM   2532  CA  ALA B 189     -29.410  -8.289 -50.547  1.00 79.88           C  
ANISOU 2532  CA  ALA B 189    11397   9947   9006   1754  -1496  -2967       C  
ATOM   2533  C   ALA B 189     -28.612  -9.235 -49.659  1.00 80.76           C  
ANISOU 2533  C   ALA B 189    11389   9932   9363   1734  -1384  -2792       C  
ATOM   2534  O   ALA B 189     -28.894 -10.431 -49.602  1.00 81.68           O  
ANISOU 2534  O   ALA B 189    11565   9861   9608   1762  -1327  -2934       O  
ATOM   2535  CB  ALA B 189     -28.738  -8.040 -51.873  1.00 81.10           C  
ANISOU 2535  CB  ALA B 189    11709  10165   8939   1955  -1367  -2992       C  
ATOM   2536  N   TYR B 190     -27.664  -8.655 -48.921  1.00 81.07           N  
ANISOU 2536  N   TYR B 190    11274  10076   9452   1599  -1401  -2406       N  
ATOM   2537  CA  TYR B 190     -26.866  -9.376 -47.943  1.00 82.98           C  
ANISOU 2537  CA  TYR B 190    11284  10281   9960   1458  -1408  -2011       C  
ATOM   2538  C   TYR B 190     -27.679  -9.922 -46.806  1.00 81.70           C  
ANISOU 2538  C   TYR B 190    11188   9971   9882   1221  -1533  -2155       C  
ATOM   2539  O   TYR B 190     -27.598 -11.096 -46.495  1.00 82.77           O  
ANISOU 2539  O   TYR B 190    11181   9987  10282   1293  -1453  -2109       O  
ATOM   2540  CB  TYR B 190     -25.746  -8.500 -47.412  1.00 84.25           C  
ANISOU 2540  CB  TYR B 190    11299  10639  10073   1139  -1586  -1423       C  
ATOM   2541  CG  TYR B 190     -24.582  -8.496 -48.346  1.00 88.01           C  
ANISOU 2541  CG  TYR B 190    11466  11247  10726   1450  -1372   -990       C  
ATOM   2542  CD1 TYR B 190     -24.115  -9.693 -48.895  1.00 91.60           C  
ANISOU 2542  CD1 TYR B 190    11716  11543  11542   1913   -932   -827       C  
ATOM   2543  CD2 TYR B 190     -23.941  -7.309 -48.691  1.00 89.29           C  
ANISOU 2543  CD2 TYR B 190    11603  11617  10704   1316  -1494   -698       C  
ATOM   2544  CE1 TYR B 190     -23.038  -9.713 -49.761  1.00 97.02           C  
ANISOU 2544  CE1 TYR B 190    12165  12247  12450   2308   -521   -331       C  
ATOM   2545  CE2 TYR B 190     -22.852  -7.315 -49.555  1.00 93.97           C  
ANISOU 2545  CE2 TYR B 190    11852  12319  11531   1656  -1223   -197       C  
ATOM   2546  CZ  TYR B 190     -22.407  -8.524 -50.088  1.00 98.00           C  
ANISOU 2546  CZ  TYR B 190    12146  12640  12449   2191   -687      9       C  
ATOM   2547  OH  TYR B 190     -21.337  -8.551 -50.947  1.00102.97           O  
ANISOU 2547  OH  TYR B 190    12487  13273  13364   2634   -210    592       O  
ATOM   2548  N   SER B 191     -28.476  -9.079 -46.187  1.00 80.43           N  
ANISOU 2548  N   SER B 191    11291   9757   9510    982  -1624  -2298       N  
ATOM   2549  CA  SER B 191     -29.335  -9.555 -45.114  1.00 80.59           C  
ANISOU 2549  CA  SER B 191    11431   9575   9615    812  -1628  -2412       C  
ATOM   2550  C   SER B 191     -30.250 -10.732 -45.547  1.00 80.89           C  
ANISOU 2550  C   SER B 191    11301   9524   9907   1065  -1591  -2718       C  
ATOM   2551  O   SER B 191     -30.444 -11.706 -44.790  1.00 80.55           O  
ANISOU 2551  O   SER B 191    11185   9349  10068    985  -1608  -2716       O  
ATOM   2552  CB  SER B 191     -30.122  -8.384 -44.522  1.00 80.23           C  
ANISOU 2552  CB  SER B 191    11821   9351   9312    642  -1479  -2466       C  
ATOM   2553  OG  SER B 191     -29.241  -7.439 -43.930  1.00 81.33           O  
ANISOU 2553  OG  SER B 191    12351   9461   9088    209  -1551  -2189       O  
ATOM   2554  N   TYR B 192     -30.783 -10.630 -46.770  1.00 82.20           N  
ANISOU 2554  N   TYR B 192    11462   9759  10009   1275  -1598  -2932       N  
ATOM   2555  CA  TYR B 192     -31.534 -11.705 -47.434  1.00 84.66           C  
ANISOU 2555  CA  TYR B 192    11779   9982  10403   1327  -1682  -3167       C  
ATOM   2556  C   TYR B 192     -30.739 -13.007 -47.568  1.00 88.78           C  
ANISOU 2556  C   TYR B 192    12378  10330  11022   1420  -1526  -3207       C  
ATOM   2557  O   TYR B 192     -31.250 -14.093 -47.276  1.00 89.81           O  
ANISOU 2557  O   TYR B 192    12557  10273  11291   1345  -1549  -3332       O  
ATOM   2558  CB  TYR B 192     -31.982 -11.246 -48.820  1.00 85.06           C  
ANISOU 2558  CB  TYR B 192    11946  10153  10219   1364  -1805  -3277       C  
ATOM   2559  CG  TYR B 192     -33.326 -10.584 -48.846  1.00 82.68           C  
ANISOU 2559  CG  TYR B 192    11452   9960  10002   1273  -1977  -3133       C  
ATOM   2560  CD1 TYR B 192     -34.420 -11.159 -48.199  1.00 82.10           C  
ANISOU 2560  CD1 TYR B 192    11177   9800  10214   1148  -2080  -3018       C  
ATOM   2561  CD2 TYR B 192     -33.517  -9.403 -49.539  1.00 80.80           C  
ANISOU 2561  CD2 TYR B 192    11158   9906   9636   1349  -1988  -2989       C  
ATOM   2562  CE1 TYR B 192     -35.665 -10.563 -48.225  1.00 82.52           C  
ANISOU 2562  CE1 TYR B 192    10906   9950  10498   1135  -2142  -2647       C  
ATOM   2563  CE2 TYR B 192     -34.753  -8.795 -49.572  1.00 82.08           C  
ANISOU 2563  CE2 TYR B 192    11021  10158  10008   1339  -2044  -2649       C  
ATOM   2564  CZ  TYR B 192     -35.827  -9.378 -48.913  1.00 83.83           C  
ANISOU 2564  CZ  TYR B 192    10970  10291  10588   1248  -2099  -2420       C  
ATOM   2565  OH  TYR B 192     -37.068  -8.766 -48.947  1.00 88.74           O  
ANISOU 2565  OH  TYR B 192    11149  10999  11566   1308  -2060  -1848       O  
ATOM   2566  N   GLU B 193     -29.487 -12.863 -48.006  1.00 93.00           N  
ANISOU 2566  N   GLU B 193    12911  10895  11530   1615  -1292  -3015       N  
ATOM   2567  CA  GLU B 193     -28.563 -13.961 -48.276  1.00 99.75           C  
ANISOU 2567  CA  GLU B 193    13829  11513  12558   1862   -893  -2867       C  
ATOM   2568  C   GLU B 193     -28.182 -14.721 -47.008  1.00102.23           C  
ANISOU 2568  C   GLU B 193    13811  11770  13259   1804   -855  -2539       C  
ATOM   2569  O   GLU B 193     -28.036 -15.951 -47.025  1.00105.53           O  
ANISOU 2569  O   GLU B 193    14329  11888  13876   1970   -533  -2531       O  
ATOM   2570  CB  GLU B 193     -27.321 -13.392 -48.969  1.00101.63           C  
ANISOU 2570  CB  GLU B 193    13986  11837  12790   2137   -591  -2515       C  
ATOM   2571  CG  GLU B 193     -26.208 -14.384 -49.250  1.00108.35           C  
ANISOU 2571  CG  GLU B 193    14813  12397  13956   2541     53  -2110       C  
ATOM   2572  CD  GLU B 193     -25.078 -14.297 -48.235  1.00111.04           C  
ANISOU 2572  CD  GLU B 193    14436  12963  14791   2534     48  -1262       C  
ATOM   2573  OE1 GLU B 193     -24.559 -13.178 -48.018  1.00110.30           O  
ANISOU 2573  OE1 GLU B 193    14024  13228  14656   2330   -270   -893       O  
ATOM   2574  OE2 GLU B 193     -24.702 -15.350 -47.669  1.00114.47           O  
ANISOU 2574  OE2 GLU B 193    14641  13211  15638   2668    333   -890       O  
ATOM   2575  N   GLN B 194     -28.025 -13.981 -45.916  1.00167.19           N  
ANISOU 2575  N   GLN B 194    32518  12204  18801  -4036  -7632  -2246       N  
ATOM   2576  CA  GLN B 194     -27.714 -14.569 -44.627  1.00178.43           C  
ANISOU 2576  CA  GLN B 194    34920  12673  20202  -4438  -9038  -1744       C  
ATOM   2577  C   GLN B 194     -28.928 -15.309 -44.098  1.00181.81           C  
ANISOU 2577  C   GLN B 194    36503  13153  19422  -5337  -9084  -1263       C  
ATOM   2578  O   GLN B 194     -28.800 -16.355 -43.461  1.00191.40           O  
ANISOU 2578  O   GLN B 194    38654  13401  20667  -5803 -10400   -891       O  
ATOM   2579  CB  GLN B 194     -27.290 -13.495 -43.630  1.00178.74           C  
ANISOU 2579  CB  GLN B 194    35319  12746  19848  -4665  -9260  -1430       C  
ATOM   2580  CG  GLN B 194     -26.355 -12.407 -44.170  1.00175.93           C  
ANISOU 2580  CG  GLN B 194    33821  12710  20311  -3908  -8747  -1913       C  
ATOM   2581  CD  GLN B 194     -25.099 -12.938 -44.834  1.00183.09           C  
ANISOU 2581  CD  GLN B 194    33714  12823  23027  -3172  -9318  -2645       C  
ATOM   2582  OE1 GLN B 194     -24.688 -14.076 -44.610  1.00193.87           O  
ANISOU 2582  OE1 GLN B 194    35200  13056  25403  -3103 -10597  -2716       O  
ATOM   2583  NE2 GLN B 194     -24.471 -12.099 -45.647  1.00179.94           N  
ANISOU 2583  NE2 GLN B 194    32270  12915  23181  -2731  -8384  -3323       N  
ATOM   2584  N   MET B 195     -30.106 -14.754 -44.376  1.00176.30           N  
ANISOU 2584  N   MET B 195    35711  13468  17806  -5653  -7746  -1335       N  
ATOM   2585  CA  MET B 195     -31.377 -15.367 -44.000  1.00179.78           C  
ANISOU 2585  CA  MET B 195    36990  14088  17229  -6565  -7405  -1174       C  
ATOM   2586  C   MET B 195     -31.698 -16.585 -44.885  1.00181.02           C  
ANISOU 2586  C   MET B 195    36987  14044  17746  -6299  -7562  -1268       C  
ATOM   2587  O   MET B 195     -32.592 -17.370 -44.566  1.00184.60           O  
ANISOU 2587  O   MET B 195    38233  14432  17473  -7049  -7549  -1110       O  
ATOM   2588  CB  MET B 195     -32.503 -14.327 -44.067  1.00174.40           C  
ANISOU 2588  CB  MET B 195    35867  14357  16037  -6881  -5989  -1498       C  
ATOM   2589  CG  MET B 195     -33.528 -14.419 -42.939  1.00180.88           C  
ANISOU 2589  CG  MET B 195    37687  15274  15761  -8287  -5481  -1598       C  
ATOM   2590  SD  MET B 195     -34.778 -13.113 -43.006  1.00177.54           S  
ANISOU 2590  SD  MET B 195    36225  15692  15541  -8556  -3850  -2413       S  
ATOM   2591  CE  MET B 195     -35.861 -13.732 -44.297  1.00174.31           C  
ANISOU 2591  CE  MET B 195    35019  15507  15704  -8098  -3494  -2640       C  
ATOM   2592  N   GLY B 196     -30.971 -16.728 -45.993  1.00179.28           N  
ANISOU 2592  N   GLY B 196    35769  13743  18606  -5387  -7573  -1647       N  
ATOM   2593  CA  GLY B 196     -31.065 -17.909 -46.854  1.00182.20           C  
ANISOU 2593  CA  GLY B 196    35912  13816  19499  -5159  -7725  -1896       C  
ATOM   2594  C   GLY B 196     -31.965 -17.781 -48.072  1.00176.24           C  
ANISOU 2594  C   GLY B 196    34631  13902  18429  -5100  -6565  -2158       C  
ATOM   2595  O   GLY B 196     -31.949 -18.646 -48.960  1.00178.12           O  
ANISOU 2595  O   GLY B 196    34594  13987  19093  -4943  -6503  -2485       O  
ATOM   2596  N   SER B 197     -32.750 -16.706 -48.113  1.00170.60           N  
ANISOU 2596  N   SER B 197    33774  13941  17104  -5296  -5782  -2055       N  
ATOM   2597  CA  SER B 197     -33.679 -16.462 -49.212  1.00166.74           C  
ANISOU 2597  CA  SER B 197    32890  14031  16433  -5349  -5080  -2168       C  
ATOM   2598  C   SER B 197     -32.912 -15.747 -50.312  1.00164.71           C  
ANISOU 2598  C   SER B 197    32027  14013  16540  -5042  -4783  -2458       C  
ATOM   2599  O   SER B 197     -32.682 -14.536 -50.204  1.00161.74           O  
ANISOU 2599  O   SER B 197    31384  13902  16167  -4955  -4631  -2402       O  
ATOM   2600  CB  SER B 197     -34.839 -15.576 -48.744  1.00164.76           C  
ANISOU 2600  CB  SER B 197    32574  14188  15835  -5723  -4633  -2082       C  
ATOM   2601  OG  SER B 197     -35.060 -15.684 -47.344  1.00167.86           O  
ANISOU 2601  OG  SER B 197    33584  14406  15789  -6267  -4679  -2021       O  
ATOM   2602  N   HIS B 198     -32.507 -16.473 -51.360  1.00167.52           N  
ANISOU 2602  N   HIS B 198    32228  14264  17155  -5051  -4621  -2861       N  
ATOM   2603  CA AHIS B 198     -31.698 -15.924 -52.457  0.25168.83           C  
ANISOU 2603  CA AHIS B 198    32024  14639  17483  -5182  -4120  -3369       C  
ATOM   2604  CA BHIS B 198     -31.720 -15.837 -52.415  0.25168.45           C  
ANISOU 2604  CA BHIS B 198    31979  14612  17411  -5176  -4129  -3332       C  
ATOM   2605  CA CHIS B 198     -31.728 -15.825 -52.405  0.50168.31           C  
ANISOU 2605  CA CHIS B 198    31963  14598  17388  -5174  -4132  -3323       C  
ATOM   2606  C   HIS B 198     -32.551 -15.348 -53.600  1.00167.63           C  
ANISOU 2606  C   HIS B 198    32132  14963  16595  -5798  -3822  -3133       C  
ATOM   2607  O   HIS B 198     -32.089 -14.498 -54.376  1.00169.10           O  
ANISOU 2607  O   HIS B 198    32350  15380  16520  -6230  -3536  -3298       O  
ATOM   2608  CB AHIS B 198     -30.753 -17.008 -52.997  0.25176.11           C  
ANISOU 2608  CB AHIS B 198    32600  15105  19208  -5160  -3930  -4252       C  
ATOM   2609  CB BHIS B 198     -30.539 -16.691 -52.878  0.25175.56           C  
ANISOU 2609  CB BHIS B 198    32452  15060  19192  -5098  -3928  -4258       C  
ATOM   2610  CB CHIS B 198     -30.503 -16.632 -52.827  0.50175.25           C  
ANISOU 2610  CB CHIS B 198    32400  15019  19166  -5075  -3945  -4247       C  
ATOM   2611  CG AHIS B 198     -29.923 -17.670 -51.939  0.25180.65           C  
ANISOU 2611  CG AHIS B 198    32907  14851  20881  -4574  -4721  -4448       C  
ATOM   2612  CG BHIS B 198     -29.403 -15.873 -53.405  0.25178.76           C  
ANISOU 2612  CG BHIS B 198    32385  15586  19949  -5254  -3354  -4968       C  
ATOM   2613  CG CHIS B 198     -29.289 -15.778 -53.007  0.50177.39           C  
ANISOU 2613  CG CHIS B 198    32157  15309  19931  -5039  -3572  -4854       C  
ATOM   2614  ND1AHIS B 198     -28.878 -17.031 -51.308  0.25182.35           N  
ANISOU 2614  ND1AHIS B 198    32726  14753  21805  -4199  -5036  -4646       N  
ATOM   2615  ND1BHIS B 198     -28.416 -15.361 -52.590  0.25179.42           N  
ANISOU 2615  ND1BHIS B 198    32017  15348  20803  -4741  -3669  -5150       N  
ATOM   2616  ND1CHIS B 198     -28.356 -15.594 -52.010  0.50178.49           N  
ANISOU 2616  ND1CHIS B 198    31893  14943  20982  -4445  -4119  -4985       N  
ATOM   2617  CD2AHIS B 198     -29.985 -18.911 -51.401  0.25185.60           C  
ANISOU 2617  CD2AHIS B 198    33703  14741  22073  -4384  -5517  -4400       C  
ATOM   2618  CD2BHIS B 198     -29.125 -15.431 -54.655  0.25182.72           C  
ANISOU 2618  CD2BHIS B 198    32940  16488  19996  -6071  -2474  -5543       C  
ATOM   2619  CD2CHIS B 198     -28.894 -15.001 -54.042  0.50179.25           C  
ANISOU 2619  CD2CHIS B 198    32353  15986  19768  -5683  -2764  -5325       C  
ATOM   2620  CE1AHIS B 198     -28.333 -17.849 -50.425  0.25188.58           C  
ANISOU 2620  CE1AHIS B 198    33472  14561  23618  -3819  -6138  -4678       C  
ATOM   2621  CE1BHIS B 198     -27.565 -14.662 -53.319  0.25182.86           C  
ANISOU 2621  CE1BHIS B 198    32080  16011  21387  -5115  -2905  -5904       C  
ATOM   2622  CE1CHIS B 198     -27.417 -14.769 -52.438  0.50180.48           C  
ANISOU 2622  CE1CHIS B 198    31672  15354  21548  -4573  -3548  -5623       C  
ATOM   2623  NE2AHIS B 198     -28.986 -18.996 -50.462  0.25190.94           N  
ANISOU 2623  NE2AHIS B 198    34158  14558  23833  -3955  -6500  -4505       N  
ATOM   2624  NE2BHIS B 198     -27.973 -14.688 -54.575  0.25185.38           N  
ANISOU 2624  NE2BHIS B 198    32781  16782  20870  -6033  -2129  -6167       N  
ATOM   2625  NE2CHIS B 198     -27.720 -14.394 -53.667  0.50181.16           N  
ANISOU 2625  NE2CHIS B 198    32024  16041  20765  -5396  -2659  -5858       N  
ATOM   2626  N   GLU B 199     -33.779 -15.864 -53.721  1.00165.95           N  
ANISOU 2626  N   GLU B 199    32203  14779  16070  -5974  -4021  -2756       N  
ATOM   2627  CA  GLU B 199     -34.738 -15.390 -54.731  1.00165.48           C  
ANISOU 2627  CA  GLU B 199    32437  14900  15537  -6575  -4182  -2407       C  
ATOM   2628  C   GLU B 199     -35.061 -13.914 -54.486  1.00161.78           C  
ANISOU 2628  C   GLU B 199    31779  14486  15204  -6540  -4595  -2008       C  
ATOM   2629  O   GLU B 199     -35.161 -13.126 -55.431  1.00165.13           O  
ANISOU 2629  O   GLU B 199    32512  14902  15326  -7139  -4939  -1771       O  
ATOM   2630  CB  GLU B 199     -36.033 -16.227 -54.730  1.00166.37           C  
ANISOU 2630  CB  GLU B 199    32697  14907  15609  -6649  -4420  -2159       C  
ATOM   2631  CG  GLU B 199     -37.199 -15.611 -55.558  1.00170.02           C  
ANISOU 2631  CG  GLU B 199    33317  15285  15994  -7164  -5021  -1716       C  
ATOM   2632  CD  GLU B 199     -38.384 -16.562 -55.789  1.00172.98           C  
ANISOU 2632  CD  GLU B 199    33802  15508  16415  -7323  -5215  -1614       C  
ATOM   2633  OE1 GLU B 199     -38.501 -17.591 -55.087  1.00171.67           O  
ANISOU 2633  OE1 GLU B 199    33578  15357  16291  -7013  -4844  -1826       O  
ATOM   2634  OE2 GLU B 199     -39.212 -16.269 -56.680  1.00177.95           O  
ANISOU 2634  OE2 GLU B 199    34654  15901  17057  -7846  -5900  -1278       O  
ATOM   2635  N   GLU B 200     -35.220 -13.544 -53.215  1.00155.48           N  
ANISOU 2635  N   GLU B 200    30572  13656  14845  -6003  -4630  -1962       N  
ATOM   2636  CA  GLU B 200     -35.401 -12.143 -52.848  1.00151.54           C  
ANISOU 2636  CA  GLU B 200    29700  13151  14727  -5897  -4912  -1792       C  
ATOM   2637  C   GLU B 200     -34.128 -11.343 -53.103  1.00148.22           C  
ANISOU 2637  C   GLU B 200    29332  12876  14106  -5897  -4787  -1857       C  
ATOM   2638  O   GLU B 200     -34.193 -10.204 -53.553  1.00149.47           O  
ANISOU 2638  O   GLU B 200    29482  12987  14319  -6150  -5203  -1613       O  
ATOM   2639  CB  GLU B 200     -35.827 -11.998 -51.382  1.00150.14           C  
ANISOU 2639  CB  GLU B 200    29139  12943  14962  -5589  -4695  -1962       C  
ATOM   2640  CG  GLU B 200     -37.343 -11.989 -51.134  1.00154.12           C  
ANISOU 2640  CG  GLU B 200    29229  13252  16077  -5795  -4771  -2134       C  
ATOM   2641  CD  GLU B 200     -37.853 -13.247 -50.435  1.00156.48           C  
ANISOU 2641  CD  GLU B 200    29833  13565  16057  -6002  -4320  -2363       C  
ATOM   2642  OE1 GLU B 200     -37.230 -13.684 -49.437  1.00155.78           O  
ANISOU 2642  OE1 GLU B 200    30182  13532  15472  -6042  -4023  -2415       O  
ATOM   2643  OE2 GLU B 200     -38.893 -13.791 -50.874  1.00159.94           O  
ANISOU 2643  OE2 GLU B 200    30166  13864  16738  -6231  -4405  -2452       O  
ATOM   2644  N   ALA B 201     -32.980 -11.962 -52.839  1.00144.45           N  
ANISOU 2644  N   ALA B 201    28877  12448  13558  -5666  -4333  -2244       N  
ATOM   2645  CA  ALA B 201     -31.686 -11.278 -52.814  1.00141.60           C  
ANISOU 2645  CA  ALA B 201    28353  12169  13279  -5571  -4086  -2532       C  
ATOM   2646  C   ALA B 201     -31.168 -10.838 -54.176  1.00144.58           C  
ANISOU 2646  C   ALA B 201    29081  12704  13146  -6388  -3814  -2761       C  
ATOM   2647  O   ALA B 201     -30.735  -9.695 -54.342  1.00144.01           O  
ANISOU 2647  O   ALA B 201    29056  12742  12917  -6619  -3877  -2666       O  
ATOM   2648  CB  ALA B 201     -30.659 -12.161 -52.136  1.00142.55           C  
ANISOU 2648  CB  ALA B 201    28234  12023  13902  -5102  -3914  -3021       C  
ATOM   2649  N   LEU B 202     -31.225 -11.767 -55.135  1.00147.57           N  
ANISOU 2649  N   LEU B 202    29823  13081  13166  -7003  -3473  -3105       N  
ATOM   2650  CA  LEU B 202     -30.585 -11.655 -56.457  1.00153.55           C  
ANISOU 2650  CA  LEU B 202    31115  13991  13235  -8207  -2867  -3653       C  
ATOM   2651  C   LEU B 202     -30.674 -10.277 -57.156  1.00154.75           C  
ANISOU 2651  C   LEU B 202    31985  14239  12572  -9161  -3288  -3147       C  
ATOM   2652  O   LEU B 202     -29.648  -9.717 -57.546  1.00158.94           O  
ANISOU 2652  O   LEU B 202    32677  14932  12780  -9823  -2669  -3706       O  
ATOM   2653  CB  LEU B 202     -31.127 -12.758 -57.381  1.00159.37           C  
ANISOU 2653  CB  LEU B 202    32354  14696  13501  -8938  -2634  -3856       C  
ATOM   2654  CG  LEU B 202     -30.192 -13.753 -58.082  1.00168.34           C  
ANISOU 2654  CG  LEU B 202    33367  15834  14758  -9587  -1450  -5179       C  
ATOM   2655  CD1 LEU B 202     -30.995 -14.662 -59.030  1.00174.43           C  
ANISOU 2655  CD1 LEU B 202    34833  16608  14832 -10458  -1367  -5150       C  
ATOM   2656  CD2 LEU B 202     -29.052 -13.049 -58.833  1.00177.30           C  
ANISOU 2656  CD2 LEU B 202    34726  17172  15467 -10772   -482  -6111       C  
ATOM   2657  N   PRO B 203     -31.897  -9.739 -57.328  1.00125.96           N  
ANISOU 2657  N   PRO B 203    20159  18045   9654  -4186  -2893   2405       N  
ATOM   2658  CA  PRO B 203     -32.099  -8.462 -58.025  1.00119.70           C  
ANISOU 2658  CA  PRO B 203    17794  18143   9542  -4005  -3052   2568       C  
ATOM   2659  C   PRO B 203     -31.570  -7.209 -57.318  1.00110.89           C  
ANISOU 2659  C   PRO B 203    15501  17329   9302  -2988  -3102   2607       C  
ATOM   2660  O   PRO B 203     -31.109  -6.290 -57.992  1.00107.05           O  
ANISOU 2660  O   PRO B 203    14269  17109   9296  -2482  -3158   2656       O  
ATOM   2661  CB  PRO B 203     -33.625  -8.383 -58.187  1.00123.88           C  
ANISOU 2661  CB  PRO B 203    17730  19647   9690  -5260  -3143   2756       C  
ATOM   2662  CG  PRO B 203     -34.174  -9.286 -57.149  1.00128.85           C  
ANISOU 2662  CG  PRO B 203    19202  20047   9706  -6010  -3060   2689       C  
ATOM   2663  CD  PRO B 203     -33.185 -10.393 -57.027  1.00132.07           C  
ANISOU 2663  CD  PRO B 203    21381  19099   9700  -5636  -2883   2456       C  
ATOM   2664  N   HIS B 204     -31.656  -7.162 -55.987  1.00108.03           N  
ANISOU 2664  N   HIS B 204    15071  16905   9069  -2792  -3068   2582       N  
ATOM   2665  CA  HIS B 204     -31.067  -6.060 -55.198  1.00100.74           C  
ANISOU 2665  CA  HIS B 204    13286  16140   8849  -1910  -3080   2586       C  
ATOM   2666  C   HIS B 204     -29.582  -5.971 -55.475  1.00 98.95           C  
ANISOU 2666  C   HIS B 204    13244  15541   8808  -1019  -3033   2432       C  
ATOM   2667  O   HIS B 204     -29.028  -4.882 -55.605  1.00 94.62           O  
ANISOU 2667  O   HIS B 204    11917  15294   8740   -561  -3063   2450       O  
ATOM   2668  CB  HIS B 204     -31.301  -6.242 -53.693  1.00 99.37           C  
ANISOU 2668  CB  HIS B 204    13221  15852   8682  -1860  -3033   2553       C  
ATOM   2669  CG  HIS B 204     -32.716  -6.017 -53.260  1.00 97.39           C  
ANISOU 2669  CG  HIS B 204    12419  16285   8297  -2582  -3084   2736       C  
ATOM   2670  ND1 HIS B 204     -33.367  -4.813 -53.418  1.00 93.93           N  
ANISOU 2670  ND1 HIS B 204    10850  16652   8186  -2445  -3144   2952       N  
ATOM   2671  CD2 HIS B 204     -33.598  -6.840 -52.648  1.00 99.00           C  
ANISOU 2671  CD2 HIS B 204    13073  16592   7950  -3406  -3063   2749       C  
ATOM   2672  CE1 HIS B 204     -34.593  -4.908 -52.934  1.00 95.96           C  
ANISOU 2672  CE1 HIS B 204    10740  17631   8090  -3044  -3167   3111       C  
ATOM   2673  NE2 HIS B 204     -34.759  -6.129 -52.459  1.00 98.45           N  
ANISOU 2673  NE2 HIS B 204    11948  17574   7881  -3747  -3131   2981       N  
ATOM   2674  N   PHE B 205     -28.952  -7.141 -55.554  1.00103.73           N  
ANISOU 2674  N   PHE B 205    14979  15547   8885   -788  -2935   2290       N  
ATOM   2675  CA  PHE B 205     -27.599  -7.267 -56.058  1.00105.34           C  
ANISOU 2675  CA  PHE B 205    15403  15623   8999     88  -2878   2177       C  
ATOM   2676  C   PHE B 205     -27.497  -6.658 -57.457  1.00104.61           C  
ANISOU 2676  C   PHE B 205    14766  15864   9115    -58  -2960   2239       C  
ATOM   2677  O   PHE B 205     -26.564  -5.910 -57.735  1.00102.47           O  
ANISOU 2677  O   PHE B 205    13849  15955   9129    487  -2980   2203       O  
ATOM   2678  CB  PHE B 205     -27.188  -8.732 -56.118  1.00112.07           C  
ANISOU 2678  CB  PHE B 205    17816  15745   9018    403  -2717   2071       C  
ATOM   2679  CG  PHE B 205     -27.016  -9.381 -54.782  1.00114.58           C  
ANISOU 2679  CG  PHE B 205    18845  15667   9022    811  -2598   1997       C  
ATOM   2680  CD1 PHE B 205     -25.928  -9.069 -53.981  1.00113.48           C  
ANISOU 2680  CD1 PHE B 205    18253  15841   9020   1875  -2559   1934       C  
ATOM   2681  CD2 PHE B 205     -27.912 -10.340 -54.348  1.00119.24           C  
ANISOU 2681  CD2 PHE B 205    20611  15635   9057     68  -2512   1989       C  
ATOM   2682  CE1 PHE B 205     -25.745  -9.682 -52.759  1.00116.39           C  
ANISOU 2682  CE1 PHE B 205    19283  15883   9056   2343  -2442   1878       C  
ATOM   2683  CE2 PHE B 205     -27.742 -10.959 -53.130  1.00122.03           C  
ANISOU 2683  CE2 PHE B 205    21747  15548   9070    463  -2385   1920       C  
ATOM   2684  CZ  PHE B 205     -26.653 -10.630 -52.330  1.00120.92           C  
ANISOU 2684  CZ  PHE B 205    21110  15690   9141   1687  -2351   1871       C  
ATOM   2685  N   LYS B 206     -28.458  -6.969 -58.329  1.00107.57           N  
ANISOU 2685  N   LYS B 206    15393  16207   9272   -887  -3005   2330       N  
ATOM   2686  CA  LYS B 206     -28.489  -6.389 -59.686  1.00107.61           C  
ANISOU 2686  CA  LYS B 206    14877  16549   9460  -1072  -3088   2409       C  
ATOM   2687  C   LYS B 206     -28.693  -4.869 -59.677  1.00102.96           C  
ANISOU 2687  C   LYS B 206    13017  16571   9531   -998  -3177   2535       C  
ATOM   2688  O   LYS B 206     -27.899  -4.122 -60.266  1.00100.47           O  
ANISOU 2688  O   LYS B 206    12255  16434   9481   -602  -3190   2510       O  
ATOM   2689  CB  LYS B 206     -29.575  -7.047 -60.565  1.00112.47           C  
ANISOU 2689  CB  LYS B 206    15981  17154   9597  -2088  -3117   2496       C  
ATOM   2690  CG  LYS B 206     -29.341  -8.511 -60.964  1.00119.91           C  
ANISOU 2690  CG  LYS B 206    18523  17325   9713  -2285  -2987   2370       C  
ATOM   2691  CD  LYS B 206     -30.422  -8.995 -61.941  1.00126.90           C  
ANISOU 2691  CD  LYS B 206    19792  18350  10071  -3534  -3023   2455       C  
ATOM   2692  CE  LYS B 206     -30.528 -10.521 -61.998  1.00136.70           C  
ANISOU 2692  CE  LYS B 206    22972  18696  10271  -4111  -2846   2330       C  
ATOM   2693  NZ  LYS B 206     -31.528 -11.061 -61.026  1.00139.11           N  
ANISOU 2693  NZ  LYS B 206    23759  19001  10095  -5118  -2809   2339       N  
ATOM   2694  N   LYS B 207     -29.769  -4.438 -59.015  1.00103.02           N  
ANISOU 2694  N   LYS B 207    12565  16903   9672  -1379  -3211   2677       N  
ATOM   2695  CA  LYS B 207     -30.177  -3.034 -58.934  1.00101.43           C  
ANISOU 2695  CA  LYS B 207    11432  17199   9907  -1217  -3240   2841       C  
ATOM   2696  C   LYS B 207     -29.019  -2.195 -58.411  1.00 98.76           C  
ANISOU 2696  C   LYS B 207    10871  16708   9943   -571  -3184   2723       C  
ATOM   2697  O   LYS B 207     -28.711  -1.134 -58.959  1.00 97.30           O  
ANISOU 2697  O   LYS B 207    10308  16682   9980   -405  -3173   2772       O  
ATOM   2698  CB  LYS B 207     -31.385  -2.903 -57.996  1.00102.68           C  
ANISOU 2698  CB  LYS B 207    11271  17750   9992  -1500  -3244   2999       C  
ATOM   2699  CG  LYS B 207     -32.623  -2.245 -58.595  1.00106.23           C  
ANISOU 2699  CG  LYS B 207    11028  19027  10305  -1752  -3290   3284       C  
ATOM   2700  CD  LYS B 207     -33.876  -2.973 -58.103  1.00111.86           C  
ANISOU 2700  CD  LYS B 207    11666  20332  10502  -2479  -3323   3400       C  
ATOM   2701  CE  LYS B 207     -35.144  -2.497 -58.793  1.00117.87           C  
ANISOU 2701  CE  LYS B 207    11617  22282  10884  -2754  -3375   3712       C  
ATOM   2702  NZ  LYS B 207     -35.853  -1.451 -58.005  1.00119.66           N  
ANISOU 2702  NZ  LYS B 207    11101  23195  11167  -2126  -3320   3952       N  
ATOM   2703  N   ALA B 208     -28.378  -2.705 -57.358  1.00110.83           N  
ANISOU 2703  N   ALA B 208    11979  15292  14838   -995   2443    582       N  
ATOM   2704  CA  ALA B 208     -27.257  -2.051 -56.701  1.00109.18           C  
ANISOU 2704  CA  ALA B 208    11828  15171  14483   -386   1983   1142       C  
ATOM   2705  C   ALA B 208     -26.176  -1.641 -57.682  1.00108.23           C  
ANISOU 2705  C   ALA B 208    11467  15322  14333   -268   1601   1234       C  
ATOM   2706  O   ALA B 208     -25.758  -0.483 -57.680  1.00106.18           O  
ANISOU 2706  O   ALA B 208    10944  15348  14050   -235   1217   1256       O  
ATOM   2707  CB  ALA B 208     -26.676  -2.950 -55.622  1.00113.42           C  
ANISOU 2707  CB  ALA B 208    12962  15360  14772    229   2498   1533       C  
ATOM   2708  N   ASN B 209     -25.724  -2.572 -58.521  1.00112.03           N  
ANISOU 2708  N   ASN B 209    12119  15610  14834   -288   1890   1217       N  
ATOM   2709  CA  ASN B 209     -24.749  -2.193 -59.540  1.00112.44           C  
ANISOU 2709  CA  ASN B 209    11936  15910  14876   -229   1559   1263       C  
ATOM   2710  C   ASN B 209     -25.333  -1.250 -60.596  1.00111.79           C  
ANISOU 2710  C   ASN B 209    11537  16091  14845   -453   1282   1068       C  
ATOM   2711  O   ASN B 209     -24.707  -0.245 -60.940  1.00110.92           O  
ANISOU 2711  O   ASN B 209    11378  16056  14709   -351   1112   1172       O  
ATOM   2712  CB  ASN B 209     -24.088  -3.390 -60.211  1.00115.72           C  
ANISOU 2712  CB  ASN B 209    12633  16071  15262   -118   1937   1332       C  
ATOM   2713  CG  ASN B 209     -23.005  -2.965 -61.192  1.00115.23           C  
ANISOU 2713  CG  ASN B 209    12298  16305  15179    -56   1576   1364       C  
ATOM   2714  OD1 ASN B 209     -22.419  -1.886 -61.057  1.00114.19           O  
ANISOU 2714  OD1 ASN B 209    11872  16511  15003    -42   1237   1323       O  
ATOM   2715  ND2 ASN B 209     -22.741  -3.804 -62.189  1.00117.88           N  
ANISOU 2715  ND2 ASN B 209    12766  16453  15569   -139   1818   1321       N  
ATOM   2716  N   GLU B 210     -26.524  -1.571 -61.099  1.00115.52           N  
ANISOU 2716  N   GLU B 210    11810  16808  15272   -677   1403    693       N  
ATOM   2717  CA  GLU B 210     -27.191  -0.706 -62.067  1.00118.89           C  
ANISOU 2717  CA  GLU B 210    11891  17877  15405   -420   1160    545       C  
ATOM   2718  C   GLU B 210     -27.282   0.734 -61.551  1.00118.15           C  
ANISOU 2718  C   GLU B 210    11996  17706  15187    -11   1030    914       C  
ATOM   2719  O   GLU B 210     -26.935   1.678 -62.268  1.00119.57           O  
ANISOU 2719  O   GLU B 210    12407  17851  15174    425   1113   1182       O  
ATOM   2720  CB  GLU B 210     -28.578  -1.246 -62.418  1.00125.14           C  
ANISOU 2720  CB  GLU B 210    12123  19482  15941   -660   1289   -208       C  
ATOM   2721  CG  GLU B 210     -29.382  -0.335 -63.343  1.00132.12           C  
ANISOU 2721  CG  GLU B 210    12508  21544  16145     77    996   -371       C  
ATOM   2722  CD  GLU B 210     -30.850  -0.712 -63.410  1.00144.73           C  
ANISOU 2722  CD  GLU B 210    13232  24468  17289   -108   1053  -1385       C  
ATOM   2723  OE1 GLU B 210     -31.223  -1.783 -62.883  1.00147.59           O  
ANISOU 2723  OE1 GLU B 210    13449  24604  18023  -1117   1518  -2099       O  
ATOM   2724  OE2 GLU B 210     -31.635   0.064 -63.998  1.00157.75           O  
ANISOU 2724  OE2 GLU B 210    14362  27470  18106    832    782  -1540       O  
ATOM   2725  N   LEU B 211     -27.743   0.899 -60.312  1.00117.98           N  
ANISOU 2725  N   LEU B 211    12028  17530  15267   -148   1027    921       N  
ATOM   2726  CA  LEU B 211     -27.827   2.224 -59.712  1.00118.96           C  
ANISOU 2726  CA  LEU B 211    12407  17470  15322    108   1071   1185       C  
ATOM   2727  C   LEU B 211     -26.452   2.890 -59.666  1.00119.39           C  
ANISOU 2727  C   LEU B 211    12762  17029  15569    -45   1300   1323       C  
ATOM   2728  O   LEU B 211     -26.316   4.046 -60.070  1.00122.74           O  
ANISOU 2728  O   LEU B 211    13602  17146  15885    172   1733   1464       O  
ATOM   2729  CB  LEU B 211     -28.483   2.174 -58.328  1.00118.11           C  
ANISOU 2729  CB  LEU B 211    12247  17314  15315    -85   1013   1110       C  
ATOM   2730  CG  LEU B 211     -29.985   2.473 -58.251  1.00121.33           C  
ANISOU 2730  CG  LEU B 211    12418  18280  15400    174    950    923       C  
ATOM   2731  CD1 LEU B 211     -30.323   3.727 -59.044  1.00125.37           C  
ANISOU 2731  CD1 LEU B 211    13141  19078  15413   1004   1073   1206       C  
ATOM   2732  CD2 LEU B 211     -30.837   1.300 -58.721  1.00124.82           C  
ANISOU 2732  CD2 LEU B 211    12330  19370  15726   -134    972    287       C  
ATOM   2733  N   ASP B 212     -25.442   2.149 -59.199  1.00118.94           N  
ANISOU 2733  N   ASP B 212    12530  16968  15693   -352   1190   1198       N  
ATOM   2734  CA  ASP B 212     -24.052   2.617 -59.212  1.00122.28           C  
ANISOU 2734  CA  ASP B 212    12906  17371  16183   -609   1392    981       C  
ATOM   2735  C   ASP B 212     -23.551   2.833 -60.650  1.00124.21           C  
ANISOU 2735  C   ASP B 212    13366  17389  16438   -575   1638   1041       C  
ATOM   2736  O   ASP B 212     -23.486   1.886 -61.442  1.00122.51           O  
ANISOU 2736  O   ASP B 212    13046  17307  16192   -420   1401   1159       O  
ATOM   2737  CB  ASP B 212     -23.143   1.640 -58.454  1.00123.12           C  
ANISOU 2737  CB  ASP B 212    12631  17984  16163   -539   1149    828       C  
ATOM   2738  N   GLU B 213     -23.223   4.094 -60.963  1.00129.64           N  
ANISOU 2738  N   GLU B 213    14476  17621  17159   -733   2309    934       N  
ATOM   2739  CA  GLU B 213     -22.692   4.557 -62.268  1.00133.79           C  
ANISOU 2739  CA  GLU B 213    15466  17713  17653   -636   2875   1022       C  
ATOM   2740  C   GLU B 213     -23.263   5.931 -62.618  1.00140.31           C  
ANISOU 2740  C   GLU B 213    17240  17782  18290   -214   3856   1319       C  
ATOM   2741  O   GLU B 213     -24.479   6.113 -62.687  1.00140.12           O  
ANISOU 2741  O   GLU B 213    17433  17907  17896    605   3716   1786       O  
ATOM   2742  CB  GLU B 213     -22.960   3.562 -63.401  1.00130.71           C  
ANISOU 2742  CB  GLU B 213    14911  17652  17098   -143   2365   1347       C  
TER    2743      GLU B 213                                                      
HETATM 2744  S   SO4 A   1     -13.234  -8.761 -18.041  1.00 86.39           S  
HETATM 2745  O1  SO4 A   1     -12.384  -8.064 -19.010  1.00 86.07           O  
HETATM 2746  O2  SO4 A   1     -14.326  -9.475 -18.727  1.00 84.27           O  
HETATM 2747  O3  SO4 A   1     -12.411  -9.772 -17.373  1.00 87.30           O  
HETATM 2748  O4  SO4 A   1     -13.698  -7.777 -17.054  1.00 84.04           O  
HETATM 2749  S   SO4 A   2     -32.774  -5.322  -1.167  1.00 76.30           S  
HETATM 2750  O1  SO4 A   2     -31.890  -6.185  -1.948  1.00 76.53           O  
HETATM 2751  O2  SO4 A   2     -34.053  -5.274  -1.893  1.00 72.07           O  
HETATM 2752  O3  SO4 A   2     -32.948  -5.893   0.183  1.00 75.76           O  
HETATM 2753  O4  SO4 A   2     -32.142  -4.004  -1.038  1.00 71.79           O  
HETATM 2754  S   SO4 A   4     -18.820  23.501   4.230  1.00 93.14           S  
HETATM 2755  O1  SO4 A   4     -17.617  23.800   5.033  1.00 91.97           O  
HETATM 2756  O2  SO4 A   4     -18.525  23.645   2.808  1.00 93.44           O  
HETATM 2757  O3  SO4 A   4     -19.251  22.114   4.432  1.00 93.10           O  
HETATM 2758  O4  SO4 A   4     -19.916  24.395   4.603  1.00 92.26           O  
HETATM 2759  S   SO4 A  10     -24.484  -2.490  -0.813  1.00120.65           S  
HETATM 2760  O1  SO4 A  10     -24.185  -3.671  -1.626  1.00120.02           O  
HETATM 2761  O2  SO4 A  10     -25.006  -2.893   0.496  1.00120.46           O  
HETATM 2762  O3  SO4 A  10     -23.277  -1.675  -0.663  1.00119.97           O  
HETATM 2763  O4  SO4 A  10     -25.504  -1.689  -1.478  1.00121.07           O  
HETATM 2764  S   SO4 A  24     -29.813  18.308  -8.941  0.50 53.14           S  
HETATM 2765  O1  SO4 A  24     -28.665  18.602  -9.787  0.50 52.89           O  
HETATM 2766  O2  SO4 A  24     -31.089  18.716  -9.546  0.50 54.16           O  
HETATM 2767  O3  SO4 A  24     -29.895  16.893  -8.672  0.50 51.27           O  
HETATM 2768  O4  SO4 A  24     -29.550  19.081  -7.727  0.50 54.17           O  
HETATM 2769  S   SO4 A  31     -27.583  -4.735  -6.557  0.50 51.58           S  
HETATM 2770  O1  SO4 A  31     -26.711  -4.589  -7.724  0.50 51.59           O  
HETATM 2771  O2  SO4 A  31     -28.445  -5.907  -6.742  0.50 50.60           O  
HETATM 2772  O3  SO4 A  31     -26.752  -4.900  -5.353  0.50 51.65           O  
HETATM 2773  O4  SO4 A  31     -28.372  -3.516  -6.437  0.50 50.08           O  
HETATM 2774  S   SO4 A  32     -39.675  16.196   3.098  0.50 71.71           S  
HETATM 2775  O1  SO4 A  32     -38.237  16.483   3.141  0.50 68.94           O  
HETATM 2776  O2  SO4 A  32     -40.126  16.047   1.703  0.50 68.44           O  
HETATM 2777  O3  SO4 A  32     -39.947  14.964   3.852  0.50 69.44           O  
HETATM 2778  O4  SO4 A  32     -40.391  17.319   3.727  0.50 69.73           O  
HETATM 2779  S   SO4 A  33     -27.758 -30.360  -9.501  1.00114.45           S  
HETATM 2780  O1  SO4 A  33     -27.802 -29.257 -10.457  1.00114.29           O  
HETATM 2781  O2  SO4 A  33     -28.534 -31.477 -10.053  1.00114.51           O  
HETATM 2782  O3  SO4 A  33     -26.370 -30.777  -9.302  1.00113.76           O  
HETATM 2783  O4  SO4 A  33     -28.319 -29.905  -8.227  1.00113.63           O  
HETATM 2784  S   SO4 B   9     -27.186  11.560 -45.807  0.50 46.54           S  
HETATM 2785  O1  SO4 B   9     -26.653  12.920 -45.992  0.50 44.33           O  
HETATM 2786  O2  SO4 B   9     -28.636  11.713 -45.681  0.50 43.85           O  
HETATM 2787  O3  SO4 B   9     -26.782  10.704 -46.930  0.50 41.92           O  
HETATM 2788  O4  SO4 B   9     -26.680  10.954 -44.572  0.50 43.51           O  
HETATM 2789  S   SO4 B  12     -25.491  31.372 -37.320  0.50 63.12           S  
HETATM 2790  O1  SO4 B  12     -24.692  31.475 -38.540  0.50 61.50           O  
HETATM 2791  O2  SO4 B  12     -26.896  31.646 -37.618  0.50 62.66           O  
HETATM 2792  O3  SO4 B  12     -25.412  30.009 -36.792  0.50 62.81           O  
HETATM 2793  O4  SO4 B  12     -24.996  32.284 -36.290  0.50 61.49           O  
HETATM 2794  S   SO4 B  28     -20.309   6.366 -44.637  0.50 68.70           S  
HETATM 2795  O1  SO4 B  28     -19.466   5.376 -45.310  0.50 67.66           O  
HETATM 2796  O2  SO4 B  28     -21.680   6.245 -45.135  0.50 68.09           O  
HETATM 2797  O3  SO4 B  28     -20.255   6.127 -43.195  0.50 67.13           O  
HETATM 2798  O4  SO4 B  28     -19.856   7.733 -44.916  0.50 67.51           O  
HETATM 2799  S   SO4 B  29     -23.606   9.311 -39.874  0.50 59.93           S  
HETATM 2800  O1  SO4 B  29     -22.994   9.292 -41.209  0.50 58.70           O  
HETATM 2801  O2  SO4 B  29     -24.598   8.243 -39.865  0.50 58.88           O  
HETATM 2802  O3  SO4 B  29     -22.619   9.038 -38.820  0.50 59.88           O  
HETATM 2803  O4  SO4 B  29     -24.181  10.626 -39.566  0.50 57.68           O  
HETATM 2804  S   SO4 B  34     -33.610  13.253 -45.997  0.50 64.77           S  
HETATM 2805  O1  SO4 B  34     -32.782  14.451 -46.221  0.50 63.37           O  
HETATM 2806  O2  SO4 B  34     -33.694  12.493 -47.252  0.50 62.27           O  
HETATM 2807  O3  SO4 B  34     -32.999  12.434 -44.940  0.50 61.51           O  
HETATM 2808  O4  SO4 B  34     -34.957  13.654 -45.579  0.50 63.06           O  
HETATM 2809  O   HOH A   7     -27.953   2.977 -20.856  1.00 30.55           O  
ANISOU 2809  O   HOH A   7     4229   4832   2544    352    116   -496       O  
HETATM 2810  O   HOH A  11     -30.017   5.749 -23.373  1.00 35.32           O  
ANISOU 2810  O   HOH A  11     4009   4770   4642   -409    342   -414       O  
HETATM 2811  O   HOH A  12     -23.172  17.305   8.063  1.00 29.85           O  
ANISOU 2811  O   HOH A  12     3641   4278   3420   -137   -887     96       O  
HETATM 2812  O   HOH A  17     -35.220   6.416 -19.473  1.00 44.71           O  
ANISOU 2812  O   HOH A  17     5751   6378   4859    233   -236    508       O  
HETATM 2813  O   HOH A  18     -33.516   0.254 -23.948  1.00 35.34           O  
ANISOU 2813  O   HOH A  18     5446   3628   4353   1391   -314    400       O  
HETATM 2814  O   HOH A  19     -33.466  17.650   7.065  1.00 39.15           O  
ANISOU 2814  O   HOH A  19     4814   5473   4587    237   -565   -556       O  
HETATM 2815  O   HOH A  23     -28.331 -13.595 -34.030  1.00 35.53           O  
ANISOU 2815  O   HOH A  23     5347   5454   2698   1060   -547      8       O  
HETATM 2816  O   HOH A  28     -34.088   3.038 -25.625  1.00 40.50           O  
ANISOU 2816  O   HOH A  28     5582   5903   3900    647     67   -383       O  
HETATM 2817  O   HOH A  29     -35.108  11.425  -8.859  1.00 27.96           O  
ANISOU 2817  O   HOH A  29     4051   3848   2722     95   -366    143       O  
HETATM 2818  O   HOH A  36     -20.384   0.054 -21.516  1.00 46.05           O  
ANISOU 2818  O   HOH A  36     5883   5799   5812    430    308    626       O  
HETATM 2819  O   HOH A  37     -40.658   9.621   1.743  1.00 41.89           O  
ANISOU 2819  O   HOH A  37     5532   5425   4959    172    161   -230       O  
HETATM 2820  O   HOH A 225     -39.536   3.956  -7.748  1.00 33.41           O  
ANISOU 2820  O   HOH A 225     4938   4490   3265   -369    469   -982       O  
HETATM 2821  O   HOH A 226     -38.838   1.369  -8.373  1.00 30.97           O  
ANISOU 2821  O   HOH A 226     4442   4396   2928   -119    166   -474       O  
HETATM 2822  O   HOH A 227     -35.428  16.208   4.068  1.00 38.83           O  
ANISOU 2822  O   HOH A 227     5774   4636   4342   -149    449   -644       O  
HETATM 2823  O   HOH A 228     -36.450   4.672 -23.562  1.00 47.93           O  
ANISOU 2823  O   HOH A 228     7344   5938   4926   -216    430    324       O  
HETATM 2824  O   HOH A 229     -44.655   5.205   3.098  1.00 38.44           O  
ANISOU 2824  O   HOH A 229     4637   5187   4779     47    320   -205       O  
HETATM 2825  O   HOH A 230     -40.746  -6.523 -20.007  1.00 36.19           O  
ANISOU 2825  O   HOH A 230     4055   5477   4218    169    647  -1465       O  
HETATM 2826  O   HOH A 231     -39.028   7.142 -13.510  1.00 35.75           O  
ANISOU 2826  O   HOH A 231     4038   5386   4157    434      1   -140       O  
HETATM 2827  O   HOH A 232     -41.192   7.200 -12.021  1.00 34.04           O  
ANISOU 2827  O   HOH A 232     4744   3694   4494    485    962   -574       O  
HETATM 2828  O   HOH A 233     -18.531  -2.968 -17.822  1.00 41.50           O  
ANISOU 2828  O   HOH A 233     5355   5289   5123    106   -126    117       O  
HETATM 2829  O   HOH A 234     -26.696   0.950 -22.249  1.00 33.12           O  
ANISOU 2829  O   HOH A 234     4270   5430   2882    423   -381   -379       O  
HETATM 2830  O   HOH A 235     -27.903   0.394 -24.228  1.00 32.44           O  
ANISOU 2830  O   HOH A 235     4775   4494   3054   -211    -86    420       O  
HETATM 2831  O   HOH A 236     -20.323   9.917 -19.419  1.00 41.82           O  
ANISOU 2831  O   HOH A 236     5114   6949   3825   -297    263    855       O  
HETATM 2832  O   HOH A 237     -42.955   5.732  -7.981  1.00 30.87           O  
ANISOU 2832  O   HOH A 237     3521   3991   4216    593    310   -121       O  
HETATM 2833  O   HOH A 238     -25.768  10.062  -1.262  1.00 29.83           O  
ANISOU 2833  O   HOH A 238     4282   4548   2503   -589    252   -115       O  
HETATM 2834  O   HOH A 239     -30.825  -2.051  -1.565  1.00 36.12           O  
ANISOU 2834  O   HOH A 239     5306   4257   4160    476    -90    733       O  
HETATM 2835  O   HOH A 240     -38.253   6.961   7.909  1.00 38.94           O  
ANISOU 2835  O   HOH A 240     4960   5747   4087    -79      0    267       O  
HETATM 2836  O   HOH A 241     -19.983  19.148   1.721  1.00 38.12           O  
ANISOU 2836  O   HOH A 241     4561   5516   4406   -831   -243   -322       O  
HETATM 2837  O   HOH A 242     -39.683  10.000 -10.460  1.00 44.00           O  
ANISOU 2837  O   HOH A 242     5389   5062   6265    790   -143    507       O  
HETATM 2838  O   HOH A 243     -42.023   9.919  -9.240  1.00 49.04           O  
ANISOU 2838  O   HOH A 243     6097   6943   5590    298   -682    193       O  
HETATM 2839  O   HOH A 244     -26.493  24.203   6.558  1.00 39.19           O  
ANISOU 2839  O   HOH A 244     6148   4596   4145   -293   -677   -133       O  
HETATM 2840  O   HOH A 245     -26.337   4.498   2.666  1.00 30.68           O  
ANISOU 2840  O   HOH A 245     4176   4373   3106    278   -197    337       O  
HETATM 2841  O   HOH A 246     -20.507   8.243 -15.302  1.00 51.16           O  
ANISOU 2841  O   HOH A 246     6498   7614   5324     -6    371    277       O  
HETATM 2842  O   HOH A 247     -41.974   5.365 -10.311  1.00 34.50           O  
ANISOU 2842  O   HOH A 247     4723   4141   4244    272    852   -734       O  
HETATM 2843  O   HOH A 248     -40.831   2.672 -18.293  1.00 37.11           O  
ANISOU 2843  O   HOH A 248     4939   5139   4021   -123   -151    -16       O  
HETATM 2844  O   HOH A 249     -43.274  -1.348   1.036  0.69 29.49           O  
ANISOU 2844  O   HOH A 249     3969   3475   3759   -626    271    309       O  
HETATM 2845  O   HOH A 250     -25.800   0.156  -0.110  1.00 47.98           O  
ANISOU 2845  O   HOH A 250     6171   6544   5512    479   -485   1186       O  
HETATM 2846  O   HOH A 251     -35.608  14.468   8.530  1.00 42.27           O  
ANISOU 2846  O   HOH A 251     5060   6262   4739   -402   -175   -892       O  
HETATM 2847  O   HOH A 252     -38.525  -1.404   5.938  1.00 29.88           O  
ANISOU 2847  O   HOH A 252     4461   3798   3093   -362    389   1069       O  
HETATM 2848  O   HOH A 253     -34.788 -14.809 -27.904  1.00 37.03           O  
ANISOU 2848  O   HOH A 253     4709   5773   3587    216  -1429    -25       O  
HETATM 2849  O   HOH A 254     -37.859  12.879   4.314  1.00 43.37           O  
ANISOU 2849  O   HOH A 254     6095   5494   4889    -32    363   -462       O  
HETATM 2850  O   HOH A 255     -26.384  -2.039  -7.884  1.00 36.71           O  
ANISOU 2850  O   HOH A 255     5939   4709   3300   1143    119  -1273       O  
HETATM 2851  O   HOH A 256     -37.567   9.363 -11.828  1.00 37.25           O  
ANISOU 2851  O   HOH A 256     4814   4461   4877    493   -231    629       O  
HETATM 2852  O   HOH A 257     -24.237   1.360  -5.087  1.00 42.18           O  
ANISOU 2852  O   HOH A 257     5619   6988   3417    -60    107   -470       O  
HETATM 2853  O   HOH A 258     -21.724  -8.132  -8.066  1.00 52.82           O  
ANISOU 2853  O   HOH A 258     8044   7393   4632    120   -570   -675       O  
HETATM 2854  O   HOH A 259     -38.087  15.962   6.039  1.00 55.17           O  
ANISOU 2854  O   HOH A 259     7751   6775   6435   -111    714   -833       O  
HETATM 2855  O   HOH A 260     -30.540   3.268 -22.011  1.00 44.13           O  
ANISOU 2855  O   HOH A 260     5886   6812   4069    108    -34   -345       O  
HETATM 2856  O   HOH A 261     -29.816  -4.658  -2.573  1.00 34.80           O  
ANISOU 2856  O   HOH A 261     5119   3497   4607    888   -160    888       O  
HETATM 2857  O   HOH A 262     -23.912  25.109   6.891  1.00 36.42           O  
ANISOU 2857  O   HOH A 262     5898   4378   3560   -918   -571   -155       O  
HETATM 2858  O   HOH B   3     -35.823   7.802 -39.562  1.00 33.48           O  
ANISOU 2858  O   HOH B   3     5046   4200   3474   1021   -524   -114       O  
HETATM 2859  O   HOH B   5     -40.249   5.524 -38.104  1.00 34.66           O  
ANISOU 2859  O   HOH B   5     4781   4162   4226    867  -1019   -196       O  
HETATM 2860  O   HOH B   6     -27.118  -2.014 -26.034  1.00 30.08           O  
ANISOU 2860  O   HOH B   6     4623   4237   2568   1320     53    219       O  
HETATM 2861  O   HOH B   8     -27.953   2.754 -25.813  1.00 37.20           O  
ANISOU 2861  O   HOH B   8     5009   5643   3481    587   -529   -311       O  
HETATM 2862  O   HOH B  10     -30.388   3.689 -24.998  1.00 34.63           O  
ANISOU 2862  O   HOH B  10     4851   5346   2958    578   -308   -464       O  
HETATM 2863  O   HOH B  13     -32.988   7.706 -54.434  1.00 42.34           O  
ANISOU 2863  O   HOH B  13     5472   5737   4875    542   -442    967       O  
HETATM 2864  O   HOH B  15     -32.261   4.810 -26.042  1.00 35.90           O  
ANISOU 2864  O   HOH B  15     4987   5347   3306    589    -93   -567       O  
HETATM 2865  O   HOH B  16     -27.481   5.533 -22.298  1.00 33.18           O  
ANISOU 2865  O   HOH B  16     4084   4555   3967   -215    486    159       O  
HETATM 2866  O   HOH B  20     -29.468 -14.729 -36.555  1.00 46.89           O  
ANISOU 2866  O   HOH B  20     6528   7740   3545    654   -926    210       O  
HETATM 2867  O   HOH B  21     -32.708  11.830 -15.404  1.00 35.35           O  
ANISOU 2867  O   HOH B  21     4459   3834   5138    577     64    130       O  
HETATM 2868  O   HOH B  22     -26.020   4.537 -24.461  1.00 34.90           O  
ANISOU 2868  O   HOH B  22     4116   5033   4110   1240   -298   -142       O  
HETATM 2869  O   HOH B  25     -38.520  13.225 -39.143  1.00 34.34           O  
ANISOU 2869  O   HOH B  25     3931   3491   5624    810    140    704       O  
HETATM 2870  O   HOH B  26     -26.862  -6.407 -44.560  1.00 41.89           O  
ANISOU 2870  O   HOH B  26     7079   5730   3105   1740    226   -477       O  
HETATM 2871  O   HOH B  27     -40.720  14.291 -38.536  1.00 38.56           O  
ANISOU 2871  O   HOH B  27     4307   4000   6342   1139    158    639       O  
HETATM 2872  O   HOH B  35     -33.763   9.985 -53.810  1.00 48.26           O  
ANISOU 2872  O   HOH B  35     6343   5933   6057    361   -579   1130       O  
HETATM 2873  O   HOH B 225     -33.106   3.072 -21.240  1.00 30.97           O  
ANISOU 2873  O   HOH B 225     4260   4937   2570      6   -175   -193       O  
HETATM 2874  O   HOH B 226     -34.247   5.431 -21.987  1.00 35.44           O  
ANISOU 2874  O   HOH B 226     4544   5798   3121     -2   -281    466       O  
HETATM 2875  O   HOH B 227     -32.820   6.877 -23.485  1.00 39.17           O  
ANISOU 2875  O   HOH B 227     4437   5042   5402    164   -177   -508       O  
HETATM 2876  O   HOH B 228     -22.225   4.527 -46.612  1.00 49.18           O  
ANISOU 2876  O   HOH B 228     5236   7871   5576   1018    664    575       O  
HETATM 2877  O   HOH B 229     -30.673   1.196 -23.597  1.00 36.11           O  
ANISOU 2877  O   HOH B 229     5117   5674   2926    641   -301   -166       O  
HETATM 2878  O   HOH B 230     -26.336   7.345 -20.546  1.00 33.68           O  
ANISOU 2878  O   HOH B 230     4439   5365   2992    147    107    437       O  
HETATM 2879  O   HOH B 231     -38.837   2.747 -34.048  1.00 47.23           O  
ANISOU 2879  O   HOH B 231     6200   5975   5768    763   -504   -305       O  
HETATM 2880  O   HOH B 232     -37.987   0.415 -35.051  1.00 37.53           O  
ANISOU 2880  O   HOH B 232     5120   4734   4405    790   -647   -329       O  
HETATM 2881  O   HOH B 233     -30.246  19.403 -15.981  1.00 52.28           O  
ANISOU 2881  O   HOH B 233     7737   6845   5279   -107   -197   1403       O  
HETATM 2882  O   HOH B 234     -33.131  15.350 -15.126  1.00 37.13           O  
ANISOU 2882  O   HOH B 234     5498   5377   3231    -49   -473    877       O  
HETATM 2883  O   HOH B 235     -28.212  12.155 -39.686  1.00 44.13           O  
ANISOU 2883  O   HOH B 235     5810   6135   4820     75  -1219   -780       O  
HETATM 2884  O   HOH B 236     -37.459  11.141 -48.698  1.00 34.54           O  
ANISOU 2884  O   HOH B 236     4295   3431   5395    694   -761    135       O  
HETATM 2885  O   HOH B 237     -30.531  11.644 -43.925  1.00 43.76           O  
ANISOU 2885  O   HOH B 237     5327   5112   6187    246    488   1147       O  
HETATM 2886  O   HOH B 238     -17.287   6.132 -28.644  1.00 54.18           O  
ANISOU 2886  O   HOH B 238     6641   8300   5646  -1576    379    616       O  
HETATM 2887  O   HOH B 239     -27.721  32.673 -39.123  1.00 63.95           O  
HETATM 2888  O   HOH B 240     -24.404  18.684 -12.071  1.00 35.07           O  
ANISOU 2888  O   HOH B 240     5593   4179   3551   -504    248    586       O  
HETATM 2889  O   HOH B 241     -33.899  11.436 -12.569  1.00 38.36           O  
ANISOU 2889  O   HOH B 241     5268   4539   4766    176   -298    801       O  
HETATM 2890  O   HOH B 242      -7.185  16.939 -26.048  1.00 42.28           O  
ANISOU 2890  O   HOH B 242     4130   5853   6079   -433    263    271       O  
CONECT 2744 2745 2746 2747 2748                                                 
CONECT 2745 2744                                                                
CONECT 2746 2744                                                                
CONECT 2747 2744                                                                
CONECT 2748 2744                                                                
CONECT 2749 2750 2751 2752 2753                                                 
CONECT 2750 2749                                                                
CONECT 2751 2749                                                                
CONECT 2752 2749                                                                
CONECT 2753 2749                                                                
CONECT 2754 2755 2756 2757 2758                                                 
CONECT 2755 2754                                                                
CONECT 2756 2754                                                                
CONECT 2757 2754                                                                
CONECT 2758 2754                                                                
CONECT 2759 2760 2761 2762 2763                                                 
CONECT 2760 2759                                                                
CONECT 2761 2759                                                                
CONECT 2762 2759                                                                
CONECT 2763 2759                                                                
CONECT 2764 2765 2766 2767 2768                                                 
CONECT 2765 2764                                                                
CONECT 2766 2764                                                                
CONECT 2767 2764                                                                
CONECT 2768 2764                                                                
CONECT 2769 2770 2771 2772 2773                                                 
CONECT 2770 2769                                                                
CONECT 2771 2769                                                                
CONECT 2772 2769                                                                
CONECT 2773 2769                                                                
CONECT 2774 2775 2776 2777 2778                                                 
CONECT 2775 2774                                                                
CONECT 2776 2774                                                                
CONECT 2777 2774                                                                
CONECT 2778 2774                                                                
CONECT 2779 2780 2781 2782 2783                                                 
CONECT 2780 2779                                                                
CONECT 2781 2779                                                                
CONECT 2782 2779                                                                
CONECT 2783 2779                                                                
CONECT 2784 2785 2786 2787 2788                                                 
CONECT 2785 2784                                                                
CONECT 2786 2784                                                                
CONECT 2787 2784                                                                
CONECT 2788 2784                                                                
CONECT 2789 2790 2791 2792 2793                                                 
CONECT 2790 2789                                                                
CONECT 2791 2789                                                                
CONECT 2792 2789                                                                
CONECT 2793 2789                                                                
CONECT 2794 2795 2796 2797 2798                                                 
CONECT 2795 2794                                                                
CONECT 2796 2794                                                                
CONECT 2797 2794                                                                
CONECT 2798 2794                                                                
CONECT 2799 2800 2801 2802 2803                                                 
CONECT 2800 2799                                                                
CONECT 2801 2799                                                                
CONECT 2802 2799                                                                
CONECT 2803 2799                                                                
CONECT 2804 2805 2806 2807 2808                                                 
CONECT 2805 2804                                                                
CONECT 2806 2804                                                                
CONECT 2807 2804                                                                
CONECT 2808 2804                                                                
MASTER      963    0   13   21    0    0   14    6 2840    2   65   30          
END                                                                             



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