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***  trial2  ***

elNémo ID: 220127225908127749

Job options:

ID        	=	 220127225908127749
JOBID     	=	 trial2
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER trial2

HEADER    TRANSPORT PROTEIN                       13-MAY-12   4F5S              
TITLE     CRYSTAL STRUCTURE OF BOVINE SERUM ALBUMIN                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERUM ALBUMIN;                                             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: MATURE FORM OF BSA, UNP RESIDUES 25-607;                   
COMPND   5 SYNONYM: BSA                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   3 ORGANISM_COMMON: BOVINE;                                             
SOURCE   4 ORGANISM_TAXID: 9913                                                 
KEYWDS    BOVINE SERUM ALBUMIN, TRANSPORT PROTEIN                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.BUJACZ,G.BUJACZ                                                     
REVDAT   2   27-JUN-18 4F5S    1       SEQADV                                   
REVDAT   1   03-OCT-12 4F5S    0                                                
JRNL        AUTH   A.BUJACZ                                                     
JRNL        TITL   STRUCTURES OF BOVINE, EQUINE AND LEPORINE SERUM ALBUMIN.     
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  68  1278 2012              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   22993082                                                     
JRNL        DOI    10.1107/S0907444912027047                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.47 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.47                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 42357                          
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) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1369                            
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) : 2.47                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.54                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2658                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 81.48                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2700                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 78                           
REMARK   3   BIN FREE R VALUE                    : 0.3370                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9306                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 327                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 66.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 72.55                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.58000                                              
REMARK   3    B22 (A**2) : -1.60000                                             
REMARK   3    B33 (A**2) : -1.28000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -2.82000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.815         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.315         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.150         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.565        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.939                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9576 ; 0.021 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12956 ; 2.006 ; 1.978       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1174 ; 7.082 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   448 ;39.571 ;24.866       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1767 ;20.832 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    49 ;23.254 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1429 ; 0.131 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7163 ; 0.009 ; 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):  5869 ; 0.727 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9504 ; 1.362 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3707 ; 2.402 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3447 ; 3.604 ; 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  : 26                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   106                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.2665  20.3761  81.6855              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2651 T22:   0.1429                                     
REMARK   3      T33:   0.1533 T12:  -0.0041                                     
REMARK   3      T13:  -0.0265 T23:   0.0200                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3426 L22:   3.3702                                     
REMARK   3      L33:   5.3166 L12:   0.8133                                     
REMARK   3      L13:   0.7937 L23:   1.0363                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0688 S12:   0.1133 S13:  -0.1149                       
REMARK   3      S21:  -0.6805 S22:   0.0782 S23:  -0.2178                       
REMARK   3      S31:  -0.0304 S32:   0.3657 S33:  -0.0093                       
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   107        A   147                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.5065  28.9378  95.9671              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0489 T22:   0.3649                                     
REMARK   3      T33:   0.2029 T12:  -0.0802                                     
REMARK   3      T13:   0.0443 T23:  -0.0570                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9897 L22:  11.3249                                     
REMARK   3      L33:   4.0184 L12:   1.6843                                     
REMARK   3      L13:  -1.5664 L23:  -2.8180                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0243 S12:   0.0529 S13:   0.1152                       
REMARK   3      S21:  -0.1914 S22:  -0.0657 S23:  -1.3559                       
REMARK   3      S31:  -0.1704 S32:   1.0282 S33:   0.0413                       
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   148        A   198                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.0569  34.5816 102.6005              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2765 T22:   0.2505                                     
REMARK   3      T33:   0.1528 T12:  -0.1984                                     
REMARK   3      T13:   0.0663 T23:  -0.0919                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3816 L22:   6.2739                                     
REMARK   3      L33:   0.9813 L12:   3.1315                                     
REMARK   3      L13:  -0.2196 L23:  -1.1486                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0691 S12:  -0.3321 S13:   0.5873                       
REMARK   3      S21:   0.0485 S22:  -0.0716 S23:  -0.0502                       
REMARK   3      S31:  -0.4378 S32:   0.3386 S33:   0.0025                       
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   199        A   250                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.6445  24.6711 102.2385              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0575 T22:   0.1330                                     
REMARK   3      T33:   0.2381 T12:  -0.0188                                     
REMARK   3      T13:  -0.0556 T23:   0.0213                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9957 L22:   3.4473                                     
REMARK   3      L33:   4.2361 L12:  -1.1090                                     
REMARK   3      L13:  -1.1011 L23:   0.8853                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0388 S12:  -0.0380 S13:  -0.1263                       
REMARK   3      S21:  -0.0360 S22:  -0.0474 S23:   0.5979                       
REMARK   3      S31:  -0.1521 S32:  -0.2514 S33:   0.0086                       
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   251        A   295                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.5445  39.1107 100.1785              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2510 T22:   0.1146                                     
REMARK   3      T33:   0.3470 T12:   0.0046                                     
REMARK   3      T13:  -0.0915 T23:   0.0336                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3528 L22:   3.7793                                     
REMARK   3      L33:   6.8888 L12:  -1.0218                                     
REMARK   3      L13:  -3.1808 L23:   2.3918                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1656 S12:   0.0464 S13:   0.6469                       
REMARK   3      S21:  -0.2729 S22:  -0.0475 S23:   0.0796                       
REMARK   3      S31:  -0.7582 S32:   0.1365 S33:  -0.1180                       
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   296        A   336                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.0431  24.2316 114.9774              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2164 T22:   0.4365                                     
REMARK   3      T33:   0.3319 T12:   0.0123                                     
REMARK   3      T13:   0.1496 T23:   0.0082                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9583 L22:   5.5621                                     
REMARK   3      L33:   2.7929 L12:   2.7274                                     
REMARK   3      L13:   0.7768 L23:  -1.3468                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1456 S12:  -0.2003 S13:   0.1330                       
REMARK   3      S21:   0.5994 S22:  -0.0493 S23:   0.4413                       
REMARK   3      S31:   0.0530 S32:  -0.7546 S33:  -0.0963                       
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   337        A   366                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.9112  16.4922 118.6317              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2602 T22:   0.3246                                     
REMARK   3      T33:   0.2677 T12:   0.0508                                     
REMARK   3      T13:   0.0201 T23:  -0.0164                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6638 L22:   8.3106                                     
REMARK   3      L33:   3.6449 L12:   4.9335                                     
REMARK   3      L13:  -2.0937 L23:  -1.3772                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1953 S12:  -0.4322 S13:  -0.2392                       
REMARK   3      S21:   1.0661 S22:  -0.1767 S23:   0.2393                       
REMARK   3      S31:   0.2898 S32:  -0.3563 S33:  -0.0187                       
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   367        A   398                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.0249  19.9527 128.3245              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6893 T22:   0.5268                                     
REMARK   3      T33:   0.4582 T12:   0.0883                                     
REMARK   3      T13:   0.0953 T23:   0.0642                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  42.0993 L22:   0.6462                                     
REMARK   3      L33:   0.9779 L12:   5.0770                                     
REMARK   3      L13:   6.1421 L23:   0.7873                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0580 S12:  -1.9423 S13:   0.9859                       
REMARK   3      S21:   0.1057 S22:  -0.1876 S23:   0.2146                       
REMARK   3      S31:   0.2043 S32:  -0.2944 S33:   0.2456                       
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   399        A   417                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.7373  12.6974 122.6999              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0442 T22:   0.5378                                     
REMARK   3      T33:   0.1328 T12:   0.1493                                     
REMARK   3      T13:   0.0292 T23:   0.0777                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1732 L22:   7.6163                                     
REMARK   3      L33:   4.8134 L12:  -1.4276                                     
REMARK   3      L13:  -3.9080 L23:   5.0146                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3060 S12:  -1.3350 S13:   0.1216                       
REMARK   3      S21:   0.0007 S22:   0.0458 S23:   0.6353                       
REMARK   3      S31:   0.1312 S32:   0.6273 S33:   0.2602                       
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   418        A   468                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.1753  19.2459 116.1267              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0592 T22:   0.0437                                     
REMARK   3      T33:   0.1002 T12:  -0.0066                                     
REMARK   3      T13:   0.0082 T23:   0.0175                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4725 L22:   4.1610                                     
REMARK   3      L33:   3.4647 L12:  -1.5977                                     
REMARK   3      L13:  -1.0816 L23:   2.0514                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1406 S12:  -0.3221 S13:   0.2675                       
REMARK   3      S21:   0.2170 S22:  -0.0204 S23:   0.0458                       
REMARK   3      S31:  -0.1311 S32:  -0.1300 S33:  -0.1202                       
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   469        A   497                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.1130   5.7987 118.5337              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1846 T22:   0.3441                                     
REMARK   3      T33:   0.3753 T12:  -0.0547                                     
REMARK   3      T13:  -0.0296 T23:   0.2528                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8518 L22:   2.9481                                     
REMARK   3      L33:   1.3097 L12:  -0.6158                                     
REMARK   3      L13:  -1.8187 L23:   1.4077                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2943 S12:  -0.7784 S13:  -0.7345                       
REMARK   3      S21:   0.4221 S22:  -0.1484 S23:   0.4638                       
REMARK   3      S31:   0.3184 S32:   0.2137 S33:   0.4427                       
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   498        A   537                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.7151   9.6356 117.8791              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0891 T22:   0.0824                                     
REMARK   3      T33:   0.1262 T12:   0.0196                                     
REMARK   3      T13:   0.0451 T23:  -0.0198                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6785 L22:   6.6087                                     
REMARK   3      L33:   2.7581 L12:  -0.0474                                     
REMARK   3      L13:  -0.9242 L23:   0.5352                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3521 S12:  -0.2549 S13:   0.1863                       
REMARK   3      S21:  -0.4435 S22:   0.2823 S23:  -0.7532                       
REMARK   3      S31:   0.2755 S32:   0.1545 S33:   0.0697                       
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   538        A   583                          
REMARK   3    ORIGIN FOR THE GROUP (A):  37.7657  10.9143 126.6820              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1336 T22:   0.1945                                     
REMARK   3      T33:   0.2399 T12:   0.1171                                     
REMARK   3      T13:  -0.1101 T23:  -0.1011                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0684 L22:   5.8740                                     
REMARK   3      L33:   4.0020 L12:  -0.4803                                     
REMARK   3      L13:  -1.2417 L23:   1.1805                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1556 S12:  -0.4364 S13:   0.7516                       
REMARK   3      S21:   0.3746 S22:   0.3436 S23:  -0.4250                       
REMARK   3      S31:  -0.2588 S32:   0.0194 S33:  -0.1880                       
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 :   B     1        B   106                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.4331  27.7289  70.2657              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2573 T22:   0.1585                                     
REMARK   3      T33:   0.1848 T12:  -0.0195                                     
REMARK   3      T13:  -0.0279 T23:  -0.0537                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8155 L22:   3.0488                                     
REMARK   3      L33:   6.3003 L12:   1.0818                                     
REMARK   3      L13:   1.1633 L23:  -1.1262                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0460 S12:  -0.1127 S13:   0.1630                       
REMARK   3      S21:  -0.1762 S22:   0.0825 S23:   0.3719                       
REMARK   3      S31:  -0.1486 S32:  -0.4591 S33:  -0.0365                       
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 :   B   107        B   147                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.8587  19.2637  89.4880              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1742 T22:   0.3627                                     
REMARK   3      T33:   0.1985 T12:  -0.0029                                     
REMARK   3      T13:   0.0180 T23:  -0.0094                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1120 L22:   8.2595                                     
REMARK   3      L33:   2.8170 L12:   2.4416                                     
REMARK   3      L13:  -0.6464 L23:  -0.4400                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0970 S12:  -0.5134 S13:  -0.2487                       
REMARK   3      S21:   0.5812 S22:  -0.1481 S23:   0.9212                       
REMARK   3      S31:   0.2344 S32:  -0.5284 S33:   0.0511                       
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 :   B   148        B   198                          
REMARK   3    ORIGIN FOR THE GROUP (A):  52.6958  13.4720  91.7239              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2826 T22:   0.3070                                     
REMARK   3      T33:   0.3196 T12:  -0.0161                                     
REMARK   3      T13:   0.0277 T23:   0.1197                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8752 L22:   3.9976                                     
REMARK   3      L33:   2.8468 L12:   2.0075                                     
REMARK   3      L13:  -0.3663 L23:  -0.9873                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1934 S12:  -0.4179 S13:  -0.4210                       
REMARK   3      S21:   0.3655 S22:  -0.1381 S23:   0.1405                       
REMARK   3      S31:   0.5033 S32:  -0.1361 S33:  -0.0553                       
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   199        B   250                          
REMARK   3    ORIGIN FOR THE GROUP (A):  71.6333  23.3945  79.0243              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2561 T22:   0.4273                                     
REMARK   3      T33:   0.2926 T12:   0.0432                                     
REMARK   3      T13:   0.0976 T23:  -0.0641                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2236 L22:   1.0766                                     
REMARK   3      L33:   0.9096 L12:   1.0745                                     
REMARK   3      L13:   0.3505 L23:   0.0346                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1609 S12:  -0.1282 S13:  -0.0116                       
REMARK   3      S21:  -0.2507 S22:  -0.1248 S23:  -0.1874                       
REMARK   3      S31:   0.1235 S32:   0.3260 S33:   0.2857                       
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   251        B   295                          
REMARK   3    ORIGIN FOR THE GROUP (A):  67.7529   9.0161  78.6553              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5649 T22:   0.2719                                     
REMARK   3      T33:   0.2680 T12:   0.1294                                     
REMARK   3      T13:   0.0811 T23:   0.0245                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.7148 L22:   2.5852                                     
REMARK   3      L33:   1.6398 L12:  -1.1499                                     
REMARK   3      L13:   1.4708 L23:   0.5289                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0619 S12:  -0.2758 S13:  -0.8847                       
REMARK   3      S21:   0.4145 S22:  -0.0318 S23:  -0.1230                       
REMARK   3      S31:   0.8921 S32:   0.2072 S33:  -0.0301                       
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   296        B   336                          
REMARK   3    ORIGIN FOR THE GROUP (A):  90.6454  23.2099  82.3752              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3645 T22:   0.4813                                     
REMARK   3      T33:   0.3961 T12:   0.0934                                     
REMARK   3      T13:   0.0393 T23:   0.0069                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6384 L22:   4.2213                                     
REMARK   3      L33:   1.7409 L12:   3.5171                                     
REMARK   3      L13:  -0.6231 L23:   0.3367                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1941 S12:  -0.2202 S13:  -0.1187                       
REMARK   3      S21:  -0.4220 S22:   0.2044 S23:  -0.6067                       
REMARK   3      S31:   0.0457 S32:   0.4063 S33:  -0.0103                       
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   337        B   366                          
REMARK   3    ORIGIN FOR THE GROUP (A):  87.1945  31.3768  88.5082              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3000 T22:   0.7193                                     
REMARK   3      T33:   0.4070 T12:   0.0219                                     
REMARK   3      T13:  -0.0301 T23:  -0.0330                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8807 L22:   7.5487                                     
REMARK   3      L33:   1.8935 L12:   3.5371                                     
REMARK   3      L13:  -0.4410 L23:  -0.0510                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1318 S12:  -0.6106 S13:   0.3957                       
REMARK   3      S21:   0.2225 S22:  -0.0384 S23:  -0.6540                       
REMARK   3      S31:  -0.2206 S32:   0.9969 S33:   0.1703                       
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   367        B   398                          
REMARK   3    ORIGIN FOR THE GROUP (A):  81.6212  27.8570 103.6209              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7358 T22:   1.0057                                     
REMARK   3      T33:   0.7885 T12:  -0.0147                                     
REMARK   3      T13:  -0.0931 T23:  -0.0121                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.8781 L22:   0.1796                                     
REMARK   3      L33:   3.2583 L12:  -1.2206                                     
REMARK   3      L13:  -5.3124 L23:   0.7255                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3716 S12:  -0.6769 S13:  -0.6584                       
REMARK   3      S21:   0.0537 S22:   0.0202 S23:  -0.0015                       
REMARK   3      S31:  -0.0040 S32:   0.5853 S33:   0.3514                       
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   399        B   417                          
REMARK   3    ORIGIN FOR THE GROUP (A):  61.8415  35.5590 109.5775              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1718 T22:   0.2810                                     
REMARK   3      T33:   0.0503 T12:   0.1770                                     
REMARK   3      T13:  -0.0013 T23:  -0.0141                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8056 L22:  19.4626                                     
REMARK   3      L33:   2.8271 L12:   2.2687                                     
REMARK   3      L13:  -0.9275 L23:  -2.2344                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0878 S12:  -0.4436 S13:   0.0758                       
REMARK   3      S21:   0.3930 S22:   0.1365 S23:  -0.3311                       
REMARK   3      S31:   0.4328 S32:   0.6793 S33:  -0.0487                       
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   418        B   468                          
REMARK   3    ORIGIN FOR THE GROUP (A):  64.2324  28.6609 100.5357              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1546 T22:   0.1756                                     
REMARK   3      T33:   0.1415 T12:   0.0166                                     
REMARK   3      T13:   0.0010 T23:  -0.0113                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9477 L22:   3.5393                                     
REMARK   3      L33:   3.6619 L12:  -0.5805                                     
REMARK   3      L13:  -0.9004 L23:   0.1956                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1195 S12:  -0.0793 S13:  -0.5254                       
REMARK   3      S21:  -0.0441 S22:   0.0371 S23:  -0.2656                       
REMARK   3      S31:   0.2792 S32:   0.3884 S33:   0.0824                       
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   469        B   497                          
REMARK   3    ORIGIN FOR THE GROUP (A):  70.0376  42.1340  99.9601              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4972 T22:   0.5596                                     
REMARK   3      T33:   0.6791 T12:  -0.2789                                     
REMARK   3      T13:  -0.3290 T23:  -0.0907                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0658 L22:   2.4286                                     
REMARK   3      L33:   0.1633 L12:   0.5104                                     
REMARK   3      L13:  -0.5467 L23:  -0.3096                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1503 S12:  -0.1976 S13:   0.5202                       
REMARK   3      S21:   0.6604 S22:   0.0847 S23:  -1.0761                       
REMARK   3      S31:  -0.1239 S32:   0.1861 S33:   0.0656                       
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   498        B   537                          
REMARK   3    ORIGIN FOR THE GROUP (A):  48.6499  38.5950 112.5902              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1180 T22:   0.1455                                     
REMARK   3      T33:   0.1257 T12:   0.0725                                     
REMARK   3      T13:  -0.0099 T23:  -0.0351                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8191 L22:   5.7808                                     
REMARK   3      L33:   2.5868 L12:   3.5961                                     
REMARK   3      L13:  -1.6915 L23:  -0.1001                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1732 S12:   0.0631 S13:   0.1275                       
REMARK   3      S21:  -0.0606 S22:   0.1413 S23:   0.2378                       
REMARK   3      S31:   0.1174 S32:  -0.1464 S33:   0.0320                       
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   538        B   583                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.1777  36.7615 123.5898              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0934 T22:   0.1489                                     
REMARK   3      T33:   0.0876 T12:   0.1048                                     
REMARK   3      T13:  -0.0190 T23:  -0.0026                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.8212 L22:   3.8436                                     
REMARK   3      L33:   4.0501 L12:   1.1742                                     
REMARK   3      L13:   0.6839 L23:   0.0680                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0318 S12:  -0.2558 S13:  -0.6289                       
REMARK   3      S21:   0.2349 S22:  -0.0331 S23:  -0.1037                       
REMARK   3      S31:   0.2671 S32:   0.3034 S33:   0.0649                       
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   : 1.00                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4F5S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAY-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000072490.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-MAY-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.2                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9184                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR SI    
REMARK 200                                   -111                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43883                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.470                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.2                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.09100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 11.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.47                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.57                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 84.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.750                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1AO6                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% MMEPEG 5000, 0.25M AMMONIUM          
REMARK 280  CHLORIDE, 0.1M MES 6.5, VAPOR DIFFUSION, HANGING DROP,              
REMARK 280  TEMPERATURE 293K, PH 6.5                                            
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      108.90000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       22.49450            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      108.90000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       22.49450            
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 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    ARG A  81      -71.31    -58.07                                   
REMARK 500    ARG A  81      -71.50    -57.67                                   
REMARK 500    GLU A  82        0.91    -65.89                                   
REMARK 500    ASP A 111        4.68     83.82                                   
REMARK 500    ASP A 129       97.61   -162.27                                   
REMARK 500    ASN A 300       54.83   -118.68                                   
REMARK 500    ALA A 309      -44.25   -131.80                                   
REMARK 500    ASP A 311      109.91    -54.79                                   
REMARK 500    LYS A 312        9.40    -63.51                                   
REMARK 500    ASP A 364       69.51   -113.39                                   
REMARK 500    GLU A 494       33.48    -97.43                                   
REMARK 500    PHE A 506       20.21   -140.67                                   
REMARK 500    PRO A 516      157.78    -43.52                                   
REMARK 500    LYS A 535       68.19   -116.75                                   
REMARK 500    LEU B  42      -38.94    -34.95                                   
REMARK 500    VAL B  77      105.09    -58.29                                   
REMARK 500    ASP B 129       81.50   -158.34                                   
REMARK 500    CYS B 168        6.30    -62.08                                   
REMARK 500    GLU B 182      -39.95    -38.82                                   
REMARK 500    LYS B 204      -15.81   -143.18                                   
REMARK 500    PHE B 205       21.55   -142.61                                   
REMARK 500    PHE B 222       69.24   -112.46                                   
REMARK 500    ILE B 270      -60.13   -123.92                                   
REMARK 500    ALA B 309      -65.33   -131.28                                   
REMARK 500    ALA B 321      102.56   -160.74                                   
REMARK 500    LYS B 535       69.68   -117.53                                   
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 PGE A 601                 
DBREF  4F5S A    1   583  UNP    P02769   ALBU_BOVIN      25    607             
DBREF  4F5S B    1   583  UNP    P02769   ALBU_BOVIN      25    607             
SEQADV 4F5S THR A  190  UNP  P02769    ALA   214 VARIANT                        
SEQADV 4F5S THR B  190  UNP  P02769    ALA   214 VARIANT                        
SEQRES   1 A  583  ASP THR HIS LYS SER GLU ILE ALA HIS ARG PHE LYS ASP          
SEQRES   2 A  583  LEU GLY GLU GLU HIS PHE LYS GLY LEU VAL LEU ILE ALA          
SEQRES   3 A  583  PHE SER GLN TYR LEU GLN GLN CYS PRO PHE ASP GLU HIS          
SEQRES   4 A  583  VAL LYS LEU VAL ASN GLU LEU THR GLU PHE ALA LYS THR          
SEQRES   5 A  583  CYS VAL ALA ASP GLU SER HIS ALA GLY CYS GLU LYS SER          
SEQRES   6 A  583  LEU HIS THR LEU PHE GLY ASP GLU LEU CYS LYS VAL ALA          
SEQRES   7 A  583  SER LEU ARG GLU THR TYR GLY ASP MET ALA ASP CYS CYS          
SEQRES   8 A  583  GLU LYS GLN GLU PRO GLU ARG ASN GLU CYS PHE LEU SER          
SEQRES   9 A  583  HIS LYS ASP ASP SER PRO ASP LEU PRO LYS LEU LYS PRO          
SEQRES  10 A  583  ASP PRO ASN THR LEU CYS ASP GLU PHE LYS ALA ASP GLU          
SEQRES  11 A  583  LYS LYS PHE TRP GLY LYS TYR LEU TYR GLU ILE ALA ARG          
SEQRES  12 A  583  ARG HIS PRO TYR PHE TYR ALA PRO GLU LEU LEU TYR TYR          
SEQRES  13 A  583  ALA ASN LYS TYR ASN GLY VAL PHE GLN GLU CYS CYS GLN          
SEQRES  14 A  583  ALA GLU ASP LYS GLY ALA CYS LEU LEU PRO LYS ILE GLU          
SEQRES  15 A  583  THR MET ARG GLU LYS VAL LEU THR SER SER ALA ARG GLN          
SEQRES  16 A  583  ARG LEU ARG CYS ALA SER ILE GLN LYS PHE GLY GLU ARG          
SEQRES  17 A  583  ALA LEU LYS ALA TRP SER VAL ALA ARG LEU SER GLN LYS          
SEQRES  18 A  583  PHE PRO LYS ALA GLU PHE VAL GLU VAL THR LYS LEU VAL          
SEQRES  19 A  583  THR ASP LEU THR LYS VAL HIS LYS GLU CYS CYS HIS GLY          
SEQRES  20 A  583  ASP LEU LEU GLU CYS ALA ASP ASP ARG ALA ASP LEU ALA          
SEQRES  21 A  583  LYS TYR ILE CYS ASP ASN GLN ASP THR ILE SER SER LYS          
SEQRES  22 A  583  LEU LYS GLU CYS CYS ASP LYS PRO LEU LEU GLU LYS SER          
SEQRES  23 A  583  HIS CYS ILE ALA GLU VAL GLU LYS ASP ALA ILE PRO GLU          
SEQRES  24 A  583  ASN LEU PRO PRO LEU THR ALA ASP PHE ALA GLU ASP LYS          
SEQRES  25 A  583  ASP VAL CYS LYS ASN TYR GLN GLU ALA LYS ASP ALA PHE          
SEQRES  26 A  583  LEU GLY SER PHE LEU TYR GLU TYR SER ARG ARG HIS PRO          
SEQRES  27 A  583  GLU TYR ALA VAL SER VAL LEU LEU ARG LEU ALA LYS GLU          
SEQRES  28 A  583  TYR GLU ALA THR LEU GLU GLU CYS CYS ALA LYS ASP ASP          
SEQRES  29 A  583  PRO HIS ALA CYS TYR SER THR VAL PHE ASP LYS LEU LYS          
SEQRES  30 A  583  HIS LEU VAL ASP GLU PRO GLN ASN LEU ILE LYS GLN ASN          
SEQRES  31 A  583  CYS ASP GLN PHE GLU LYS LEU GLY GLU TYR GLY PHE GLN          
SEQRES  32 A  583  ASN ALA LEU ILE VAL ARG TYR THR ARG LYS VAL PRO GLN          
SEQRES  33 A  583  VAL SER THR PRO THR LEU VAL GLU VAL SER ARG SER LEU          
SEQRES  34 A  583  GLY LYS VAL GLY THR ARG CYS CYS THR LYS PRO GLU SER          
SEQRES  35 A  583  GLU ARG MET PRO CYS THR GLU ASP TYR LEU SER LEU ILE          
SEQRES  36 A  583  LEU ASN ARG LEU CYS VAL LEU HIS GLU LYS THR PRO VAL          
SEQRES  37 A  583  SER GLU LYS VAL THR LYS CYS CYS THR GLU SER LEU VAL          
SEQRES  38 A  583  ASN ARG ARG PRO CYS PHE SER ALA LEU THR PRO ASP GLU          
SEQRES  39 A  583  THR TYR VAL PRO LYS ALA PHE ASP GLU LYS LEU PHE THR          
SEQRES  40 A  583  PHE HIS ALA ASP ILE CYS THR LEU PRO ASP THR GLU LYS          
SEQRES  41 A  583  GLN ILE LYS LYS GLN THR ALA LEU VAL GLU LEU LEU LYS          
SEQRES  42 A  583  HIS LYS PRO LYS ALA THR GLU GLU GLN LEU LYS THR VAL          
SEQRES  43 A  583  MET GLU ASN PHE VAL ALA PHE VAL ASP LYS CYS CYS ALA          
SEQRES  44 A  583  ALA ASP ASP LYS GLU ALA CYS PHE ALA VAL GLU GLY PRO          
SEQRES  45 A  583  LYS LEU VAL VAL SER THR GLN THR ALA LEU ALA                  
SEQRES   1 B  583  ASP THR HIS LYS SER GLU ILE ALA HIS ARG PHE LYS ASP          
SEQRES   2 B  583  LEU GLY GLU GLU HIS PHE LYS GLY LEU VAL LEU ILE ALA          
SEQRES   3 B  583  PHE SER GLN TYR LEU GLN GLN CYS PRO PHE ASP GLU HIS          
SEQRES   4 B  583  VAL LYS LEU VAL ASN GLU LEU THR GLU PHE ALA LYS THR          
SEQRES   5 B  583  CYS VAL ALA ASP GLU SER HIS ALA GLY CYS GLU LYS SER          
SEQRES   6 B  583  LEU HIS THR LEU PHE GLY ASP GLU LEU CYS LYS VAL ALA          
SEQRES   7 B  583  SER LEU ARG GLU THR TYR GLY ASP MET ALA ASP CYS CYS          
SEQRES   8 B  583  GLU LYS GLN GLU PRO GLU ARG ASN GLU CYS PHE LEU SER          
SEQRES   9 B  583  HIS LYS ASP ASP SER PRO ASP LEU PRO LYS LEU LYS PRO          
SEQRES  10 B  583  ASP PRO ASN THR LEU CYS ASP GLU PHE LYS ALA ASP GLU          
SEQRES  11 B  583  LYS LYS PHE TRP GLY LYS TYR LEU TYR GLU ILE ALA ARG          
SEQRES  12 B  583  ARG HIS PRO TYR PHE TYR ALA PRO GLU LEU LEU TYR TYR          
SEQRES  13 B  583  ALA ASN LYS TYR ASN GLY VAL PHE GLN GLU CYS CYS GLN          
SEQRES  14 B  583  ALA GLU ASP LYS GLY ALA CYS LEU LEU PRO LYS ILE GLU          
SEQRES  15 B  583  THR MET ARG GLU LYS VAL LEU THR SER SER ALA ARG GLN          
SEQRES  16 B  583  ARG LEU ARG CYS ALA SER ILE GLN LYS PHE GLY GLU ARG          
SEQRES  17 B  583  ALA LEU LYS ALA TRP SER VAL ALA ARG LEU SER GLN LYS          
SEQRES  18 B  583  PHE PRO LYS ALA GLU PHE VAL GLU VAL THR LYS LEU VAL          
SEQRES  19 B  583  THR ASP LEU THR LYS VAL HIS LYS GLU CYS CYS HIS GLY          
SEQRES  20 B  583  ASP LEU LEU GLU CYS ALA ASP ASP ARG ALA ASP LEU ALA          
SEQRES  21 B  583  LYS TYR ILE CYS ASP ASN GLN ASP THR ILE SER SER LYS          
SEQRES  22 B  583  LEU LYS GLU CYS CYS ASP LYS PRO LEU LEU GLU LYS SER          
SEQRES  23 B  583  HIS CYS ILE ALA GLU VAL GLU LYS ASP ALA ILE PRO GLU          
SEQRES  24 B  583  ASN LEU PRO PRO LEU THR ALA ASP PHE ALA GLU ASP LYS          
SEQRES  25 B  583  ASP VAL CYS LYS ASN TYR GLN GLU ALA LYS ASP ALA PHE          
SEQRES  26 B  583  LEU GLY SER PHE LEU TYR GLU TYR SER ARG ARG HIS PRO          
SEQRES  27 B  583  GLU TYR ALA VAL SER VAL LEU LEU ARG LEU ALA LYS GLU          
SEQRES  28 B  583  TYR GLU ALA THR LEU GLU GLU CYS CYS ALA LYS ASP ASP          
SEQRES  29 B  583  PRO HIS ALA CYS TYR SER THR VAL PHE ASP LYS LEU LYS          
SEQRES  30 B  583  HIS LEU VAL ASP GLU PRO GLN ASN LEU ILE LYS GLN ASN          
SEQRES  31 B  583  CYS ASP GLN PHE GLU LYS LEU GLY GLU TYR GLY PHE GLN          
SEQRES  32 B  583  ASN ALA LEU ILE VAL ARG TYR THR ARG LYS VAL PRO GLN          
SEQRES  33 B  583  VAL SER THR PRO THR LEU VAL GLU VAL SER ARG SER LEU          
SEQRES  34 B  583  GLY LYS VAL GLY THR ARG CYS CYS THR LYS PRO GLU SER          
SEQRES  35 B  583  GLU ARG MET PRO CYS THR GLU ASP TYR LEU SER LEU ILE          
SEQRES  36 B  583  LEU ASN ARG LEU CYS VAL LEU HIS GLU LYS THR PRO VAL          
SEQRES  37 B  583  SER GLU LYS VAL THR LYS CYS CYS THR GLU SER LEU VAL          
SEQRES  38 B  583  ASN ARG ARG PRO CYS PHE SER ALA LEU THR PRO ASP GLU          
SEQRES  39 B  583  THR TYR VAL PRO LYS ALA PHE ASP GLU LYS LEU PHE THR          
SEQRES  40 B  583  PHE HIS ALA ASP ILE CYS THR LEU PRO ASP THR GLU LYS          
SEQRES  41 B  583  GLN ILE LYS LYS GLN THR ALA LEU VAL GLU LEU LEU LYS          
SEQRES  42 B  583  HIS LYS PRO LYS ALA THR GLU GLU GLN LEU LYS THR VAL          
SEQRES  43 B  583  MET GLU ASN PHE VAL ALA PHE VAL ASP LYS CYS CYS ALA          
SEQRES  44 B  583  ALA ASP ASP LYS GLU ALA CYS PHE ALA VAL GLU GLY PRO          
SEQRES  45 B  583  LYS LEU VAL VAL SER THR GLN THR ALA LEU ALA                  
HET    PGE  A 601      10                                                       
HETNAM     PGE TRIETHYLENE GLYCOL                                               
FORMUL   3  PGE    C6 H14 O4                                                    
FORMUL   4  HOH   *327(H2 O)                                                    
HELIX    1   1 SER A    5  GLY A   15  1                                  11    
HELIX    2   2 GLY A   15  LEU A   31  1                                  17    
HELIX    3   3 PRO A   35  ASP A   56  1                                  22    
HELIX    4   4 SER A   65  LYS A   76  1                                  12    
HELIX    5   5 SER A   79  GLY A   85  1                                   7    
HELIX    6   6 ASP A   86  LYS A   93  5                                   8    
HELIX    7   7 PRO A   96  SER A  104  1                                   9    
HELIX    8   8 ASP A  118  ASP A  129  1                                  12    
HELIX    9   9 ASP A  129  HIS A  145  1                                  17    
HELIX   10  10 TYR A  149  CYS A  168  1                                  20    
HELIX   11  11 ASP A  172  GLY A  206  1                                  35    
HELIX   12  12 GLY A  206  PHE A  222  1                                  17    
HELIX   13  13 GLU A  226  HIS A  246  1                                  21    
HELIX   14  14 ASP A  248  ASP A  265  1                                  18    
HELIX   15  15 ASN A  266  SER A  271  1                                   6    
HELIX   16  16 GLU A  276  LYS A  280  5                                   5    
HELIX   17  17 PRO A  281  VAL A  292  1                                  12    
HELIX   18  18 LEU A  304  ALA A  309  1                                   6    
HELIX   19  19 ASP A  313  ALA A  321  1                                   9    
HELIX   20  20 ALA A  321  HIS A  337  1                                  17    
HELIX   21  21 ALA A  341  LYS A  362  1                                  22    
HELIX   22  22 ASP A  364  SER A  370  1                                   7    
HELIX   23  23 THR A  371  VAL A  380  1                                  10    
HELIX   24  24 PRO A  383  VAL A  414  1                                  32    
HELIX   25  25 SER A  418  CYS A  437  1                                  20    
HELIX   26  26 PRO A  440  THR A  466  1                                  27    
HELIX   27  27 SER A  469  SER A  479  1                                  11    
HELIX   28  28 ASN A  482  ALA A  489  1                                   8    
HELIX   29  29 ASP A  502  THR A  507  5                                   6    
HELIX   30  30 HIS A  509  THR A  514  5                                   6    
HELIX   31  31 PRO A  516  LYS A  535  1                                  20    
HELIX   32  32 THR A  539  ALA A  560  1                                  22    
HELIX   33  33 ASP A  562  ALA A  583  1                                  22    
HELIX   34  34 SER B    5  LEU B   31  1                                  27    
HELIX   35  35 PRO B   35  ASP B   56  1                                  22    
HELIX   36  36 SER B   65  CYS B   75  1                                  11    
HELIX   37  37 SER B   79  GLY B   85  1                                   7    
HELIX   38  38 ASP B   86  CYS B   91  1                                   6    
HELIX   39  39 PRO B   96  SER B  104  1                                   9    
HELIX   40  40 ASP B  118  ASP B  129  1                                  12    
HELIX   41  41 ASP B  129  ARG B  143  1                                  15    
HELIX   42  42 TYR B  149  CYS B  168  1                                  20    
HELIX   43  43 ASP B  172  PHE B  222  1                                  51    
HELIX   44  44 GLU B  226  HIS B  246  1                                  21    
HELIX   45  45 ASP B  248  CYS B  264  1                                  17    
HELIX   46  46 ASN B  266  ILE B  270  5                                   5    
HELIX   47  47 SER B  271  LYS B  275  5                                   5    
HELIX   48  48 GLU B  276  LYS B  280  5                                   5    
HELIX   49  49 PRO B  281  GLU B  291  1                                  11    
HELIX   50  50 LEU B  304  ALA B  309  1                                   6    
HELIX   51  51 ASP B  313  ALA B  321  1                                   9    
HELIX   52  52 ALA B  321  HIS B  337  1                                  17    
HELIX   53  53 ALA B  341  CYS B  360  1                                  20    
HELIX   54  54 ASP B  364  THR B  371  1                                   8    
HELIX   55  55 THR B  371  ASP B  381  1                                  11    
HELIX   56  56 PRO B  383  VAL B  414  1                                  32    
HELIX   57  57 SER B  418  CYS B  437  1                                  20    
HELIX   58  58 GLU B  443  THR B  466  1                                  24    
HELIX   59  59 GLU B  470  SER B  479  1                                  10    
HELIX   60  60 ASN B  482  ALA B  489  1                                   8    
HELIX   61  61 ASP B  502  THR B  507  5                                   6    
HELIX   62  62 HIS B  509  LEU B  515  5                                   7    
HELIX   63  63 PRO B  516  LYS B  535  1                                  20    
HELIX   64  64 THR B  539  ALA B  560  1                                  22    
HELIX   65  65 ASP B  562  LEU B  582  1                                  21    
SSBOND   1 CYS A   53    CYS A   62                          1555   1555  2.07  
SSBOND   2 CYS A   75    CYS A   91                          1555   1555  2.13  
SSBOND   3 CYS A   90    CYS A  101                          1555   1555  2.05  
SSBOND   4 CYS A  123    CYS A  168                          1555   1555  2.08  
SSBOND   5 CYS A  167    CYS A  176                          1555   1555  2.05  
SSBOND   6 CYS A  199    CYS A  245                          1555   1555  2.08  
SSBOND   7 CYS A  244    CYS A  252                          1555   1555  1.98  
SSBOND   8 CYS A  264    CYS A  278                          1555   1555  2.01  
SSBOND   9 CYS A  277    CYS A  288                          1555   1555  2.01  
SSBOND  10 CYS A  315    CYS A  360                          1555   1555  2.04  
SSBOND  11 CYS A  359    CYS A  368                          1555   1555  2.05  
SSBOND  12 CYS A  391    CYS A  437                          1555   1555  2.09  
SSBOND  13 CYS A  436    CYS A  447                          1555   1555  2.06  
SSBOND  14 CYS A  460    CYS A  476                          1555   1555  2.07  
SSBOND  15 CYS A  475    CYS A  486                          1555   1555  2.15  
SSBOND  16 CYS A  513    CYS A  558                          1555   1555  2.05  
SSBOND  17 CYS A  557    CYS A  566                          1555   1555  2.13  
SSBOND  18 CYS B   53    CYS B   62                          1555   1555  2.08  
SSBOND  19 CYS B   75    CYS B   91                          1555   1555  2.09  
SSBOND  20 CYS B   90    CYS B  101                          1555   1555  2.06  
SSBOND  21 CYS B  123    CYS B  168                          1555   1555  2.07  
SSBOND  22 CYS B  167    CYS B  176                          1555   1555  2.10  
SSBOND  23 CYS B  199    CYS B  245                          1555   1555  2.10  
SSBOND  24 CYS B  244    CYS B  252                          1555   1555  2.04  
SSBOND  25 CYS B  264    CYS B  278                          1555   1555  2.06  
SSBOND  26 CYS B  277    CYS B  288                          1555   1555  2.11  
SSBOND  27 CYS B  315    CYS B  360                          1555   1555  2.08  
SSBOND  28 CYS B  359    CYS B  368                          1555   1555  2.05  
SSBOND  29 CYS B  391    CYS B  437                          1555   1555  2.07  
SSBOND  30 CYS B  436    CYS B  447                          1555   1555  1.98  
SSBOND  31 CYS B  460    CYS B  476                          1555   1555  2.04  
SSBOND  32 CYS B  475    CYS B  486                          1555   1555  2.08  
SSBOND  33 CYS B  513    CYS B  558                          1555   1555  2.03  
SSBOND  34 CYS B  557    CYS B  566                          1555   1555  2.14  
CISPEP   1 GLU A   95    PRO A   96          0        -1.36                     
CISPEP   2 GLU B   95    PRO B   96          0        -2.79                     
SITE     1 AC1  4 PHE A 506  VAL A 546  PHE A 550  THR A 578                    
CRYST1  217.800   44.989  143.057  90.00 114.13  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      0.004591  0.000000  0.002057        0.00000                         
SCALE2      0.000000  0.022228  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007660        0.00000                         
ATOM      1  N   ASP A   1     -15.623  24.749  73.372  1.00118.56           N  
ANISOU    1  N   ASP A   1    14274  16038  14737   1755  -5555  -1168       N  
ATOM      2  CA  ASP A   1     -15.370  25.428  74.669  1.00117.08           C  
ANISOU    2  CA  ASP A   1    13858  15951  14676   1941  -5294  -1216       C  
ATOM      3  C   ASP A   1     -13.903  25.174  75.098  1.00112.71           C  
ANISOU    3  C   ASP A   1    13665  15114  14046   1705  -4868  -1036       C  
ATOM      4  O   ASP A   1     -13.585  24.957  76.290  1.00110.24           O  
ANISOU    4  O   ASP A   1    13103  14944  13841   1602  -4530  -1039       O  
ATOM      5  CB  ASP A   1     -16.376  24.925  75.715  1.00118.59           C  
ANISOU    5  CB  ASP A   1    13316  16664  15077   1870  -5188  -1388       C  
ATOM      6  CG  ASP A   1     -17.009  26.061  76.526  1.00121.01           C  
ANISOU    6  CG  ASP A   1    13271  17185  15522   2313  -5263  -1564       C  
ATOM      7  OD1 ASP A   1     -16.267  26.830  77.200  1.00116.55           O  
ANISOU    7  OD1 ASP A   1    12908  16432  14945   2478  -5063  -1515       O  
ATOM      8  OD2 ASP A   1     -18.266  26.170  76.489  1.00125.13           O  
ANISOU    8  OD2 ASP A   1    13304  18079  16161   2497  -5526  -1762       O  
ATOM      9  N   THR A   2     -13.008  25.247  74.112  1.00111.20           N  
ANISOU    9  N   THR A   2    14067  14524  13659   1630  -4896   -888       N  
ATOM     10  CA  THR A   2     -11.626  24.800  74.300  1.00107.19           C  
ANISOU   10  CA  THR A   2    13879  13778  13071   1368  -4516   -727       C  
ATOM     11  C   THR A   2     -10.523  25.925  74.259  1.00105.12           C  
ANISOU   11  C   THR A   2    14083  13170  12687   1525  -4423   -632       C  
ATOM     12  O   THR A   2     -10.040  26.305  73.182  1.00106.09           O  
ANISOU   12  O   THR A   2    14720  12975  12614   1536  -4553   -552       O  
ATOM     13  CB  THR A   2     -11.342  23.495  73.419  1.00106.44           C  
ANISOU   13  CB  THR A   2    14001  13582  12861   1004  -4470   -637       C  
ATOM     14  OG1 THR A   2     -10.025  22.984  73.671  1.00102.94           O  
ANISOU   14  OG1 THR A   2    13804  12950  12359    782  -4093   -506       O  
ATOM     15  CG2 THR A   2     -11.556  23.759  71.916  1.00108.74           C  
ANISOU   15  CG2 THR A   2    14719  13633  12964   1070  -4822   -612       C  
ATOM     16  N   HIS A   3     -10.070  26.341  75.445  1.00102.15           N  
ANISOU   16  N   HIS A   3    13545  12857  12408   1583  -4167   -633       N  
ATOM     17  CA  HIS A   3      -8.946  27.260  75.608  1.00 98.74           C  
ANISOU   17  CA  HIS A   3    13502  12143  11872   1648  -4019   -540       C  
ATOM     18  C   HIS A   3      -7.685  26.424  75.542  1.00 94.37           C  
ANISOU   18  C   HIS A   3    13146  11455  11255   1311  -3681   -403       C  
ATOM     19  O   HIS A   3      -7.196  25.934  76.541  1.00 92.82           O  
ANISOU   19  O   HIS A   3    12724  11378  11166   1174  -3386   -379       O  
ATOM     20  CB  HIS A   3      -9.005  27.880  76.992  1.00 98.74           C  
ANISOU   20  CB  HIS A   3    13208  12299  12010   1808  -3871   -603       C  
ATOM     21  CG  HIS A   3      -9.754  29.171  77.057  1.00102.40           C  
ANISOU   21  CG  HIS A   3    13685  12752  12470   2215  -4159   -714       C  
ATOM     22  ND1 HIS A   3     -10.339  29.627  78.216  1.00103.60           N  
ANISOU   22  ND1 HIS A   3    13452  13139  12772   2428  -4115   -837       N  
ATOM     23  CD2 HIS A   3     -10.008  30.106  76.113  1.00106.09           C  
ANISOU   23  CD2 HIS A   3    14539  12985  12786   2466  -4501   -728       C  
ATOM     24  CE1 HIS A   3     -10.929  30.783  77.981  1.00107.20           C  
ANISOU   24  CE1 HIS A   3    14037  13513  13179   2820  -4420   -930       C  
ATOM     25  NE2 HIS A   3     -10.744  31.095  76.712  1.00108.39           N  
ANISOU   25  NE2 HIS A   3    14668  13371  13146   2851  -4673   -863       N  
ATOM     26  N   LYS A   4      -7.173  26.266  74.339  1.00 92.44           N  
ANISOU   26  N   LYS A   4    13337  10959  10826   1193  -3736   -323       N  
ATOM     27  CA  LYS A   4      -6.331  25.150  73.979  1.00 87.69           C  
ANISOU   27  CA  LYS A   4    12865  10285  10168    889  -3489   -234       C  
ATOM     28  C   LYS A   4      -4.946  24.874  74.548  1.00 82.52           C  
ANISOU   28  C   LYS A   4    12278   9561   9514    716  -3100   -145       C  
ATOM     29  O   LYS A   4      -4.629  23.727  74.761  1.00 81.73           O  
ANISOU   29  O   LYS A   4    12049   9538   9464    524  -2906   -120       O  
ATOM     30  CB  LYS A   4      -6.311  24.973  72.459  1.00 89.64           C  
ANISOU   30  CB  LYS A   4    13549  10303  10206    812  -3670   -195       C  
ATOM     31  CG  LYS A   4      -6.256  26.240  71.668  1.00 91.49           C  
ANISOU   31  CG  LYS A   4    14229  10277  10257    984  -3901   -182       C  
ATOM     32  CD  LYS A   4      -5.656  25.985  70.308  1.00 91.54           C  
ANISOU   32  CD  LYS A   4    14762  10002  10015    805  -3904   -107       C  
ATOM     33  CE  LYS A   4      -6.454  24.963  69.542  1.00 91.53           C  
ANISOU   33  CE  LYS A   4    14717  10062   9997    709  -4094   -136       C  
ATOM     34  NZ  LYS A   4      -5.669  24.389  68.438  1.00 90.74           N  
ANISOU   34  NZ  LYS A   4    15076   9723   9678    474  -3968    -62       N  
ATOM     35  N   SER A   5      -4.087  25.856  74.740  1.00 78.29           N  
ANISOU   35  N   SER A   5    11965   8873   8907    768  -2994    -97       N  
ATOM     36  CA  SER A   5      -2.664  25.468  74.908  1.00 72.75           C  
ANISOU   36  CA  SER A   5    11381   8093   8167    565  -2647    -13       C  
ATOM     37  C   SER A   5      -2.098  25.822  76.250  1.00 69.55           C  
ANISOU   37  C   SER A   5    10746   7792   7889    585  -2439     -1       C  
ATOM     38  O   SER A   5      -1.642  26.946  76.449  1.00 69.40           O  
ANISOU   38  O   SER A   5    10902   7663   7802    653  -2432     20       O  
ATOM     39  CB  SER A   5      -1.784  26.091  73.820  1.00 73.26           C  
ANISOU   39  CB  SER A   5    11959   7882   7995    486  -2620     48       C  
ATOM     40  OG  SER A   5      -0.402  26.118  74.169  1.00 67.99           O  
ANISOU   40  OG  SER A   5    11350   7180   7303    335  -2295    106       O  
ATOM     41  N   GLU A   6      -2.103  24.862  77.163  1.00 66.64           N  
ANISOU   41  N   GLU A   6    10027   7613   7680    506  -2278    -11       N  
ATOM     42  CA  GLU A   6      -1.686  25.107  78.517  1.00 63.88           C  
ANISOU   42  CA  GLU A   6     9445   7372   7453    521  -2106     -5       C  
ATOM     43  C   GLU A   6      -0.322  25.767  78.695  1.00 61.32           C  
ANISOU   43  C   GLU A   6     9321   6921   7056    456  -1914     66       C  
ATOM     44  O   GLU A   6      -0.208  26.645  79.547  1.00 59.89           O  
ANISOU   44  O   GLU A   6     9086   6757   6911    536  -1898     63       O  
ATOM     45  CB  GLU A   6      -1.764  23.843  79.347  1.00 64.27           C  
ANISOU   45  CB  GLU A   6     9180   7600   7641    404  -1957    -14       C  
ATOM     46  CG  GLU A   6      -3.109  23.682  80.152  1.00 69.38           C  
ANISOU   46  CG  GLU A   6     9460   8478   8423    479  -2074   -106       C  
ATOM     47  CD  GLU A   6      -3.451  24.884  81.031  1.00 73.87           C  
ANISOU   47  CD  GLU A   6     9906   9111   9051    669  -2120   -155       C  
ATOM     48  OE1 GLU A   6      -2.755  25.100  82.088  1.00 74.97           O  
ANISOU   48  OE1 GLU A   6     9979   9265   9241    640  -1936   -122       O  
ATOM     49  OE2 GLU A   6      -4.400  25.604  80.640  1.00 73.15           O  
ANISOU   49  OE2 GLU A   6     9805   9044   8946    857  -2355   -230       O  
ATOM     50  N   ILE A   7       0.700  25.428  77.910  1.00 59.67           N  
ANISOU   50  N   ILE A   7     9344   6594   6736    307  -1769    119       N  
ATOM     51  CA  ILE A   7       1.939  26.190  78.085  1.00 59.14           C  
ANISOU   51  CA  ILE A   7     9433   6444   6592    225  -1598    169       C  
ATOM     52  C   ILE A   7       1.695  27.689  77.852  1.00 60.04           C  
ANISOU   52  C   ILE A   7     9826   6410   6575    318  -1766    170       C  
ATOM     53  O   ILE A   7       2.061  28.524  78.680  1.00 60.10           O  
ANISOU   53  O   ILE A   7     9820   6419   6597    338  -1720    184       O  
ATOM     54  CB  ILE A   7       3.203  25.592  77.379  1.00 58.87           C  
ANISOU   54  CB  ILE A   7     9544   6356   6467     42  -1365    205       C  
ATOM     55  CG1 ILE A   7       4.464  26.179  77.965  1.00 57.34           C  
ANISOU   55  CG1 ILE A   7     9339   6184   6264    -60  -1161    240       C  
ATOM     56  CG2 ILE A   7       3.222  25.845  75.898  1.00 62.48           C  
ANISOU   56  CG2 ILE A   7    10398   6630   6711    -20  -1434    209       C  
ATOM     57  CD1 ILE A   7       5.708  25.335  77.683  1.00 60.77           C  
ANISOU   57  CD1 ILE A   7     9728   6671   6692   -198   -898    246       C  
ATOM     58  N   ALA A   8       0.970  28.010  76.797  1.00 61.66           N  
ANISOU   58  N   ALA A   8    10293   6482   6652    395  -1993    149       N  
ATOM     59  CA  ALA A   8       0.673  29.398  76.450  1.00 63.27           C  
ANISOU   59  CA  ALA A   8    10842   6499   6698    510  -2201    145       C  
ATOM     60  C   ALA A   8      -0.231  30.141  77.448  1.00 64.12           C  
ANISOU   60  C   ALA A   8    10764   6682   6917    762  -2372     87       C  
ATOM     61  O   ALA A   8       0.031  31.286  77.721  1.00 65.98           O  
ANISOU   61  O   ALA A   8    11230   6787   7052    814  -2413    100       O  
ATOM     62  CB  ALA A   8       0.143  29.490  75.046  1.00 65.69           C  
ANISOU   62  CB  ALA A   8    11505   6628   6827    538  -2426    136       C  
ATOM     63  N   HIS A   9      -1.254  29.524  78.019  1.00 64.02           N  
ANISOU   63  N   HIS A   9    10352   6879   7095    903  -2455     17       N  
ATOM     64  CA  HIS A   9      -2.014  30.155  79.123  1.00 65.23           C  
ANISOU   64  CA  HIS A   9    10268   7149   7367   1130  -2547    -56       C  
ATOM     65  C   HIS A   9      -1.122  30.601  80.310  1.00 64.16           C  
ANISOU   65  C   HIS A   9    10079   7029   7268   1053  -2322    -14       C  
ATOM     66  O   HIS A   9      -1.174  31.764  80.778  1.00 65.15           O  
ANISOU   66  O   HIS A   9    10365   7057   7330   1193  -2401    -31       O  
ATOM     67  CB  HIS A   9      -3.112  29.222  79.612  1.00 65.74           C  
ANISOU   67  CB  HIS A   9     9860   7488   7630   1206  -2592   -143       C  
ATOM     68  CG  HIS A   9      -3.962  29.789  80.707  1.00 71.93           C  
ANISOU   68  CG  HIS A   9    10365   8431   8535   1436  -2660   -243       C  
ATOM     69  ND1 HIS A   9      -4.206  29.113  81.889  1.00 73.61           N  
ANISOU   69  ND1 HIS A   9    10157   8890   8921   1380  -2487   -284       N  
ATOM     70  CD2 HIS A   9      -4.618  30.974  80.811  1.00 77.99           C  
ANISOU   70  CD2 HIS A   9    11237   9136   9258   1731  -2875   -320       C  
ATOM     71  CE1 HIS A   9      -4.961  29.862  82.678  1.00 75.30           C  
ANISOU   71  CE1 HIS A   9    10208   9206   9196   1616  -2566   -385       C  
ATOM     72  NE2 HIS A   9      -5.227  30.994  82.045  1.00 79.56           N  
ANISOU   72  NE2 HIS A   9    11052   9563   9613   1852  -2806   -414       N  
ATOM     73  N   ARG A  10      -0.276  29.693  80.761  1.00 61.75           N  
ANISOU   73  N   ARG A  10     9587   6829   7048    836  -2062     40       N  
ATOM     74  CA  ARG A  10       0.669  29.986  81.837  1.00 60.50           C  
ANISOU   74  CA  ARG A  10     9369   6694   6923    733  -1859     87       C  
ATOM     75  C   ARG A  10       1.776  31.015  81.512  1.00 61.01           C  
ANISOU   75  C   ARG A  10     9824   6556   6800    605  -1802    157       C  
ATOM     76  O   ARG A  10       2.119  31.837  82.345  1.00 61.73           O  
ANISOU   76  O   ARG A  10     9972   6614   6870    611  -1767    170       O  
ATOM     77  CB  ARG A  10       1.338  28.689  82.337  1.00 58.13           C  
ANISOU   77  CB  ARG A  10     8787   6548   6754    550  -1626    122       C  
ATOM     78  CG  ARG A  10       0.415  27.685  82.936  1.00 55.21           C  
ANISOU   78  CG  ARG A  10     8055   6374   6548    603  -1637     64       C  
ATOM     79  CD  ARG A  10      -0.644  28.285  83.779  1.00 56.13           C  
ANISOU   79  CD  ARG A  10     8003   6588   6736    794  -1748    -19       C  
ATOM     80  NE  ARG A  10      -1.625  27.238  84.019  1.00 60.06           N  
ANISOU   80  NE  ARG A  10     8177   7286   7357    794  -1768    -86       N  
ATOM     81  CZ  ARG A  10      -2.799  27.402  84.610  1.00 59.66           C  
ANISOU   81  CZ  ARG A  10     7879   7400   7390    940  -1856   -192       C  
ATOM     82  NH1 ARG A  10      -3.157  28.577  85.062  1.00 56.78           N  
ANISOU   82  NH1 ARG A  10     7555   7011   7006   1144  -1939   -247       N  
ATOM     83  NH2 ARG A  10      -3.610  26.349  84.775  1.00 62.80           N  
ANISOU   83  NH2 ARG A  10     7985   7995   7880    866  -1849   -250       N  
ATOM     84  N   PHE A  11       2.362  30.962  80.326  1.00 62.05           N  
ANISOU   84  N   PHE A  11    10239   6558   6780    459  -1777    199       N  
ATOM     85  CA  PHE A  11       3.451  31.877  80.047  1.00 62.95           C  
ANISOU   85  CA  PHE A  11    10706   6511   6701    275  -1688    258       C  
ATOM     86  C   PHE A  11       2.939  33.334  80.063  1.00 64.95           C  
ANISOU   86  C   PHE A  11    11324   6558   6796    427  -1912    243       C  
ATOM     87  O   PHE A  11       3.574  34.191  80.634  1.00 64.88           O  
ANISOU   87  O   PHE A  11    11475   6474   6701    335  -1852    277       O  
ATOM     88  CB  PHE A  11       4.106  31.554  78.713  1.00 63.86           C  
ANISOU   88  CB  PHE A  11    11076   6530   6658     77  -1605    289       C  
ATOM     89  CG  PHE A  11       5.267  32.407  78.436  1.00 65.29           C  
ANISOU   89  CG  PHE A  11    11584   6589   6635   -171  -1474    340       C  
ATOM     90  CD1 PHE A  11       5.131  33.551  77.654  1.00 67.72           C  
ANISOU   90  CD1 PHE A  11    12422   6634   6677   -197  -1634    354       C  
ATOM     91  CD2 PHE A  11       6.505  32.124  79.021  1.00 64.78           C  
ANISOU   91  CD2 PHE A  11    11310   6673   6630   -389  -1203    369       C  
ATOM     92  CE1 PHE A  11       6.228  34.416  77.419  1.00 68.46           C  
ANISOU   92  CE1 PHE A  11    12862   6607   6542   -489  -1502    401       C  
ATOM     93  CE2 PHE A  11       7.620  32.963  78.768  1.00 67.77           C  
ANISOU   93  CE2 PHE A  11    11971   6972   6807   -670  -1069    407       C  
ATOM     94  CZ  PHE A  11       7.470  34.123  77.967  1.00 67.93           C  
ANISOU   94  CZ  PHE A  11    12548   6723   6540   -741  -1210    425       C  
ATOM     95  N   LYS A  12       1.772  33.565  79.461  1.00 66.30           N  
ANISOU   95  N   LYS A  12    11620   6642   6929    670  -2184    186       N  
ATOM     96  CA  LYS A  12       1.062  34.858  79.463  1.00 69.53           C  
ANISOU   96  CA  LYS A  12    12361   6854   7205    913  -2454    146       C  
ATOM     97  C   LYS A  12       0.750  35.386  80.852  1.00 68.43           C  
ANISOU   97  C   LYS A  12    12025   6797   7178   1085  -2453    103       C  
ATOM     98  O   LYS A  12       0.897  36.583  81.121  1.00 69.62           O  
ANISOU   98  O   LYS A  12    12529   6752   7169   1143  -2540    109       O  
ATOM     99  CB  LYS A  12      -0.279  34.781  78.709  1.00 70.80           C  
ANISOU   99  CB  LYS A  12    12542   6985   7372   1205  -2769     66       C  
ATOM    100  CG  LYS A  12      -0.148  34.921  77.246  1.00 77.18           C  
ANISOU  100  CG  LYS A  12    13806   7566   7953   1111  -2898    102       C  
ATOM    101  CD  LYS A  12      -1.497  34.712  76.473  1.00 84.28           C  
ANISOU  101  CD  LYS A  12    14687   8461   8875   1395  -3239     22       C  
ATOM    102  CE  LYS A  12      -1.620  33.270  75.955  1.00 85.58           C  
ANISOU  102  CE  LYS A  12    14539   8812   9168   1257  -3143     24       C  
ATOM    103  NZ  LYS A  12      -3.016  32.681  75.947  1.00 87.55           N  
ANISOU  103  NZ  LYS A  12    14414   9258   9594   1509  -3375    -78       N  
ATOM    104  N   ASP A  13       0.275  34.488  81.708  1.00 66.68           N  
ANISOU  104  N   ASP A  13    11277   6849   7209   1162  -2359     54       N  
ATOM    105  CA  ASP A  13      -0.289  34.875  82.992  1.00 65.91           C  
ANISOU  105  CA  ASP A  13    10957   6858   7228   1364  -2371    -15       C  
ATOM    106  C   ASP A  13       0.806  35.191  83.990  1.00 63.48           C  
ANISOU  106  C   ASP A  13    10677   6540   6904   1155  -2153     55       C  
ATOM    107  O   ASP A  13       0.688  36.090  84.766  1.00 63.71           O  
ANISOU  107  O   ASP A  13    10829   6494   6884   1274  -2195     29       O  
ATOM    108  CB  ASP A  13      -1.235  33.791  83.513  1.00 64.96           C  
ANISOU  108  CB  ASP A  13    10292   7037   7353   1477  -2343   -100       C  
ATOM    109  CG  ASP A  13      -2.593  33.795  82.803  1.00 70.03           C  
ANISOU  109  CG  ASP A  13    10868   7720   8019   1763  -2620   -208       C  
ATOM    110  OD1 ASP A  13      -3.444  33.006  83.230  1.00 75.72           O  
ANISOU  110  OD1 ASP A  13    11146   8702   8923   1839  -2607   -292       O  
ATOM    111  OD2 ASP A  13      -2.835  34.536  81.810  1.00 73.61           O  
ANISOU  111  OD2 ASP A  13    11706   7956   8305   1897  -2860   -215       O  
ATOM    112  N   LEU A  14       1.892  34.451  83.944  1.00 62.03           N  
ANISOU  112  N   LEU A  14    10389   6430   6752    850  -1930    139       N  
ATOM    113  CA  LEU A  14       2.959  34.693  84.880  1.00 61.00           C  
ANISOU  113  CA  LEU A  14    10246   6316   6615    645  -1745    202       C  
ATOM    114  C   LEU A  14       3.926  35.727  84.346  1.00 61.39           C  
ANISOU  114  C   LEU A  14    10772   6138   6415    440  -1741    272       C  
ATOM    115  O   LEU A  14       4.524  36.456  85.112  1.00 62.87           O  
ANISOU  115  O   LEU A  14    11091   6266   6529    334  -1688    306       O  
ATOM    116  CB  LEU A  14       3.679  33.393  85.155  1.00 58.43           C  
ANISOU  116  CB  LEU A  14     9554   6197   6450    443  -1524    243       C  
ATOM    117  CG  LEU A  14       2.896  32.270  85.839  1.00 59.79           C  
ANISOU  117  CG  LEU A  14     9281   6589   6846    561  -1490    187       C  
ATOM    118  CD1 LEU A  14       3.703  30.994  85.706  1.00 59.97           C  
ANISOU  118  CD1 LEU A  14     9083   6739   6965    363  -1313    235       C  
ATOM    119  CD2 LEU A  14       2.536  32.512  87.309  1.00 56.42           C  
ANISOU  119  CD2 LEU A  14     8676   6250   6511    654  -1460    150       C  
ATOM    120  N   GLY A  15       4.067  35.796  83.031  1.00 62.37           N  
ANISOU  120  N   GLY A  15    11179   6131   6388    359  -1799    293       N  
ATOM    121  CA  GLY A  15       5.107  36.596  82.396  1.00 63.62           C  
ANISOU  121  CA  GLY A  15    11783   6101   6288     74  -1745    361       C  
ATOM    122  C   GLY A  15       6.377  35.792  82.465  1.00 62.41           C  
ANISOU  122  C   GLY A  15    11368   6136   6209   -248  -1460    412       C  
ATOM    123  O   GLY A  15       6.430  34.835  83.232  1.00 60.97           O  
ANISOU  123  O   GLY A  15    10725   6179   6261   -211  -1345    401       O  
ATOM    124  N   GLU A  16       7.394  36.222  81.732  1.00 64.36           N  
ANISOU  124  N   GLU A  16    11916   6291   6246   -559  -1352    459       N  
ATOM    125  CA  GLU A  16       8.570  35.431  81.417  1.00 66.34           C  
ANISOU  125  CA  GLU A  16    11940   6726   6538   -845  -1087    481       C  
ATOM    126  C   GLU A  16       9.501  35.170  82.550  1.00 66.50           C  
ANISOU  126  C   GLU A  16    11606   6958   6701   -991   -912    502       C  
ATOM    127  O   GLU A  16      10.031  34.047  82.660  1.00 65.91           O  
ANISOU  127  O   GLU A  16    11130   7108   6805  -1030   -747    490       O  
ATOM    128  CB  GLU A  16       9.410  36.104  80.357  1.00 69.38           C  
ANISOU  128  CB  GLU A  16    12758   6972   6629  -1172  -1002    509       C  
ATOM    129  CG  GLU A  16      10.421  35.138  79.750  1.00 72.89           C  
ANISOU  129  CG  GLU A  16    12950   7624   7120  -1400   -729    497       C  
ATOM    130  CD  GLU A  16      11.655  35.819  79.163  1.00 81.67           C  
ANISOU  130  CD  GLU A  16    14342   8716   7974  -1830   -541    515       C  
ATOM    131  OE1 GLU A  16      12.249  36.693  79.860  1.00 86.54           O  
ANISOU  131  OE1 GLU A  16    15059   9323   8501  -2031   -519    548       O  
ATOM    132  OE2 GLU A  16      12.045  35.459  78.028  1.00 80.19           O  
ANISOU  132  OE2 GLU A  16    14267   8534   7666  -1990   -403    492       O  
ATOM    133  N   GLU A  17       9.695  36.179  83.403  1.00 68.59           N  
ANISOU  133  N   GLU A  17    12036   7140   6883  -1057   -966    530       N  
ATOM    134  CA  GLU A  17      10.637  36.045  84.493  1.00 68.82           C  
ANISOU  134  CA  GLU A  17    11772   7355   7020  -1225   -828    555       C  
ATOM    135  C   GLU A  17      10.128  35.033  85.457  1.00 66.59           C  
ANISOU  135  C   GLU A  17    11032   7246   7025   -980   -834    531       C  
ATOM    136  O   GLU A  17      10.853  34.179  85.904  1.00 67.11           O  
ANISOU  136  O   GLU A  17    10727   7523   7247  -1059   -696    534       O  
ATOM    137  CB  GLU A  17      10.946  37.382  85.173  1.00 70.09           C  
ANISOU  137  CB  GLU A  17    12267   7365   6998  -1377   -897    593       C  
ATOM    138  CG  GLU A  17      11.603  38.457  84.243  1.00 76.12           C  
ANISOU  138  CG  GLU A  17    13555   7943   7424  -1712   -876    625       C  
ATOM    139  CD  GLU A  17      12.579  37.884  83.185  1.00 81.70           C  
ANISOU  139  CD  GLU A  17    14157   8803   8082  -2003   -654    616       C  
ATOM    140  OE1 GLU A  17      13.556  37.153  83.528  1.00 81.91           O  
ANISOU  140  OE1 GLU A  17    13740   9118   8263  -2162   -458    606       O  
ATOM    141  OE2 GLU A  17      12.353  38.171  81.987  1.00 86.23           O  
ANISOU  141  OE2 GLU A  17    15107   9204   8453  -2059   -683    610       O  
ATOM    142  N   HIS A  18       8.852  35.095  85.767  1.00 66.40           N  
ANISOU  142  N   HIS A  18    11031   7136   7062   -676   -999    497       N  
ATOM    143  CA  HIS A  18       8.318  34.115  86.695  1.00 63.34           C  
ANISOU  143  CA  HIS A  18    10228   6915   6922   -484   -989    469       C  
ATOM    144  C   HIS A  18       8.183  32.768  86.066  1.00 62.24           C  
ANISOU  144  C   HIS A  18     9814   6910   6923   -428   -919    445       C  
ATOM    145  O   HIS A  18       8.427  31.759  86.735  1.00 61.70           O  
ANISOU  145  O   HIS A  18     9399   7010   7032   -416   -832    443       O  
ATOM    146  CB  HIS A  18       7.039  34.607  87.329  1.00 62.26           C  
ANISOU  146  CB  HIS A  18    10157   6691   6808   -204  -1154    421       C  
ATOM    147  CG  HIS A  18       7.307  35.714  88.264  1.00 62.99           C  
ANISOU  147  CG  HIS A  18    10460   6680   6794   -258  -1188    443       C  
ATOM    148  ND1 HIS A  18       6.323  36.411  88.918  1.00 64.84           N  
ANISOU  148  ND1 HIS A  18    10820   6813   7005    -15  -1321    392       N  
ATOM    149  CD2 HIS A  18       8.483  36.255  88.650  1.00 63.17           C  
ANISOU  149  CD2 HIS A  18    10597   6689   6716   -540  -1107    505       C  
ATOM    150  CE1 HIS A  18       6.885  37.326  89.687  1.00 66.35           C  
ANISOU  150  CE1 HIS A  18    11229   6904   7075   -142  -1318    428       C  
ATOM    151  NE2 HIS A  18       8.196  37.249  89.544  1.00 65.56           N  
ANISOU  151  NE2 HIS A  18    11125   6859   6927   -477  -1197    501       N  
ATOM    152  N   PHE A  19       7.837  32.743  84.780  1.00 62.04           N  
ANISOU  152  N   PHE A  19     9983   6790   6798   -402   -966    428       N  
ATOM    153  CA  PHE A  19       7.820  31.467  84.074  1.00 60.30           C  
ANISOU  153  CA  PHE A  19     9556   6678   6679   -381   -890    408       C  
ATOM    154  C   PHE A  19       9.197  30.814  84.196  1.00 59.72           C  
ANISOU  154  C   PHE A  19     9265   6764   6662   -583   -676    428       C  
ATOM    155  O   PHE A  19       9.296  29.701  84.616  1.00 57.02           O  
ANISOU  155  O   PHE A  19     8615   6562   6488   -521   -612    415       O  
ATOM    156  CB  PHE A  19       7.386  31.662  82.633  1.00 60.90           C  
ANISOU  156  CB  PHE A  19     9937   6605   6598   -365   -972    393       C  
ATOM    157  CG  PHE A  19       7.376  30.409  81.820  1.00 59.40           C  
ANISOU  157  CG  PHE A  19     9600   6494   6475   -358   -896    371       C  
ATOM    158  CD1 PHE A  19       8.530  30.012  81.109  1.00 58.48           C  
ANISOU  158  CD1 PHE A  19     9497   6430   6293   -565   -696    378       C  
ATOM    159  CD2 PHE A  19       6.209  29.646  81.720  1.00 53.34           C  
ANISOU  159  CD2 PHE A  19     8695   5754   5819   -156  -1021    332       C  
ATOM    160  CE1 PHE A  19       8.533  28.863  80.343  1.00 55.01           C  
ANISOU  160  CE1 PHE A  19     8964   6041   5895   -541   -621    350       C  
ATOM    161  CE2 PHE A  19       6.182  28.519  80.953  1.00 51.65           C  
ANISOU  161  CE2 PHE A  19     8403   5582   5638   -165   -966    315       C  
ATOM    162  CZ  PHE A  19       7.364  28.099  80.267  1.00 55.26           C  
ANISOU  162  CZ  PHE A  19     8902   6066   6027   -345   -763    324       C  
ATOM    163  N   LYS A  20      10.265  31.542  83.874  1.00 62.03           N  
ANISOU  163  N   LYS A  20     9724   7040   6806   -829   -574    453       N  
ATOM    164  CA  LYS A  20      11.615  30.964  83.906  1.00 62.18           C  
ANISOU  164  CA  LYS A  20     9495   7251   6878  -1014   -368    449       C  
ATOM    165  C   LYS A  20      12.034  30.527  85.303  1.00 61.53           C  
ANISOU  165  C   LYS A  20     9070   7328   6983   -978   -351    461       C  
ATOM    166  O   LYS A  20      12.503  29.376  85.514  1.00 60.70           O  
ANISOU  166  O   LYS A  20     8648   7382   7032   -920   -265    437       O  
ATOM    167  CB  LYS A  20      12.622  31.959  83.356  1.00 65.09           C  
ANISOU  167  CB  LYS A  20    10103   7596   7033  -1327   -262    463       C  
ATOM    168  CG  LYS A  20      12.734  31.964  81.822  1.00 65.92           C  
ANISOU  168  CG  LYS A  20    10468   7620   6958  -1441   -177    438       C  
ATOM    169  CD  LYS A  20      13.678  33.020  81.400  1.00 69.61           C  
ANISOU  169  CD  LYS A  20    11202   8061   7188  -1795    -68    451       C  
ATOM    170  CE  LYS A  20      15.115  32.486  81.313  1.00 75.52           C  
ANISOU  170  CE  LYS A  20    11613   9095   7985  -2020    198    405       C  
ATOM    171  NZ  LYS A  20      15.586  32.126  79.894  1.00 73.66           N  
ANISOU  171  NZ  LYS A  20    11485   8893   7610  -2168    396    347       N  
ATOM    172  N   GLY A  21      11.823  31.421  86.267  1.00 60.41           N  
ANISOU  172  N   GLY A  21     9024   7118   6811   -992   -451    495       N  
ATOM    173  CA  GLY A  21      11.995  31.073  87.677  1.00 58.20           C  
ANISOU  173  CA  GLY A  21     8483   6944   6687   -940   -473    511       C  
ATOM    174  C   GLY A  21      11.347  29.761  88.084  1.00 56.07           C  
ANISOU  174  C   GLY A  21     7952   6743   6608   -717   -498    486       C  
ATOM    175  O   GLY A  21      12.012  28.914  88.690  1.00 57.30           O  
ANISOU  175  O   GLY A  21     7841   7039   6893   -717   -445    485       O  
ATOM    176  N   LEU A  22      10.082  29.557  87.725  1.00 53.52           N  
ANISOU  176  N   LEU A  22     7712   6328   6294   -538   -586    461       N  
ATOM    177  CA  LEU A  22       9.336  28.408  88.249  1.00 51.96           C  
ANISOU  177  CA  LEU A  22     7301   6191   6251   -372   -618    437       C  
ATOM    178  C   LEU A  22       9.755  27.119  87.552  1.00 51.03           C  
ANISOU  178  C   LEU A  22     7036   6152   6200   -357   -531    417       C  
ATOM    179  O   LEU A  22       9.742  26.090  88.130  1.00 48.47           O  
ANISOU  179  O   LEU A  22     6531   5895   5991   -291   -523    410       O  
ATOM    180  CB  LEU A  22       7.826  28.617  88.135  1.00 51.17           C  
ANISOU  180  CB  LEU A  22     7294   6008   6140   -205   -741    401       C  
ATOM    181  CG  LEU A  22       7.234  29.629  89.092  1.00 52.29           C  
ANISOU  181  CG  LEU A  22     7525   6091   6250   -144   -826    395       C  
ATOM    182  CD1 LEU A  22       5.849  30.062  88.622  1.00 54.73           C  
ANISOU  182  CD1 LEU A  22     7949   6326   6520     41   -957    337       C  
ATOM    183  CD2 LEU A  22       7.177  29.070  90.485  1.00 49.47           C  
ANISOU  183  CD2 LEU A  22     6960   5826   6010   -130   -800    397       C  
ATOM    184  N   VAL A  23      10.142  27.240  86.294  1.00 53.27           N  
ANISOU  184  N   VAL A  23     7445   6408   6386   -426   -465    404       N  
ATOM    185  CA  VAL A  23      10.641  26.168  85.497  1.00 54.09           C  
ANISOU  185  CA  VAL A  23     7459   6573   6519   -415   -362    373       C  
ATOM    186  C   VAL A  23      11.998  25.714  86.019  1.00 54.92           C  
ANISOU  186  C   VAL A  23     7330   6833   6704   -474   -248    368       C  
ATOM    187  O   VAL A  23      12.258  24.531  86.153  1.00 54.46           O  
ANISOU  187  O   VAL A  23     7105   6839   6746   -371   -216    342       O  
ATOM    188  CB  VAL A  23      10.630  26.586  84.038  1.00 55.24           C  
ANISOU  188  CB  VAL A  23     7849   6632   6506   -490   -320    356       C  
ATOM    189  CG1 VAL A  23      11.396  25.573  83.125  1.00 58.65           C  
ANISOU  189  CG1 VAL A  23     8208   7137   6938   -504   -164    311       C  
ATOM    190  CG2 VAL A  23       9.196  26.695  83.578  1.00 55.36           C  
ANISOU  190  CG2 VAL A  23     8040   6513   6482   -369   -478    350       C  
ATOM    191  N   LEU A  24      12.845  26.656  86.398  1.00 57.29           N  
ANISOU  191  N   LEU A  24     7620   7191   6957   -634   -209    389       N  
ATOM    192  CA  LEU A  24      14.163  26.273  86.951  1.00 58.32           C  
ANISOU  192  CA  LEU A  24     7481   7505   7174   -688   -126    373       C  
ATOM    193  C   LEU A  24      14.005  25.554  88.296  1.00 57.37           C  
ANISOU  193  C   LEU A  24     7184   7412   7204   -551   -231    393       C  
ATOM    194  O   LEU A  24      14.736  24.647  88.581  1.00 57.79           O  
ANISOU  194  O   LEU A  24     7025   7575   7357   -472   -206    364       O  
ATOM    195  CB  LEU A  24      15.051  27.502  87.103  1.00 58.24           C  
ANISOU  195  CB  LEU A  24     7505   7559   7064   -936    -77    393       C  
ATOM    196  CG  LEU A  24      16.330  27.245  87.921  1.00 61.71           C  
ANISOU  196  CG  LEU A  24     7627   8211   7607   -996    -41    377       C  
ATOM    197  CD1 LEU A  24      17.436  26.388  87.154  1.00 61.47           C  
ANISOU  197  CD1 LEU A  24     7338   8389   7630   -977    125    288       C  
ATOM    198  CD2 LEU A  24      16.906  28.545  88.629  1.00 58.02           C  
ANISOU  198  CD2 LEU A  24     7214   7776   7053  -1250    -75    423       C  
ATOM    199  N   ILE A  25      13.073  26.018  89.135  1.00 56.91           N  
ANISOU  199  N   ILE A  25     7233   7247   7143   -524   -351    435       N  
ATOM    200  CA  ILE A  25      12.712  25.318  90.376  1.00 55.25           C  
ANISOU  200  CA  ILE A  25     6920   7033   7041   -416   -444    452       C  
ATOM    201  C   ILE A  25      12.202  23.930  90.049  1.00 55.59           C  
ANISOU  201  C   ILE A  25     6922   7052   7149   -262   -447    421       C  
ATOM    202  O   ILE A  25      12.686  22.948  90.574  1.00 56.94           O  
ANISOU  202  O   ILE A  25     6968   7266   7400   -182   -467    413       O  
ATOM    203  CB  ILE A  25      11.658  26.089  91.184  1.00 53.56           C  
ANISOU  203  CB  ILE A  25     6846   6714   6790   -417   -536    482       C  
ATOM    204  CG1 ILE A  25      12.232  27.432  91.656  1.00 54.14           C  
ANISOU  204  CG1 ILE A  25     7006   6783   6780   -573   -549    517       C  
ATOM    205  CG2 ILE A  25      11.194  25.286  92.361  1.00 52.29           C  
ANISOU  205  CG2 ILE A  25     6610   6545   6712   -335   -603    489       C  
ATOM    206  CD1 ILE A  25      11.225  28.490  91.994  1.00 49.01           C  
ANISOU  206  CD1 ILE A  25     6574   6004   6043   -559   -618    526       C  
ATOM    207  N   ALA A  26      11.230  23.808  89.173  1.00 55.68           N  
ANISOU  207  N   ALA A  26     7062   6982   7112   -218   -447    402       N  
ATOM    208  CA  ALA A  26      10.757  22.466  88.872  1.00 55.91           C  
ANISOU  208  CA  ALA A  26     7080   6981   7183   -106   -456    374       C  
ATOM    209  C   ALA A  26      11.880  21.529  88.394  1.00 56.54           C  
ANISOU  209  C   ALA A  26     7059   7125   7297    -43   -376    339       C  
ATOM    210  O   ALA A  26      11.989  20.404  88.850  1.00 57.43           O  
ANISOU  210  O   ALA A  26     7128   7225   7467     60   -414    328       O  
ATOM    211  CB  ALA A  26       9.550  22.510  87.911  1.00 55.53           C  
ANISOU  211  CB  ALA A  26     7181   6850   7070    -87   -484    354       C  
ATOM    212  N   PHE A  27      12.790  21.987  87.556  1.00 58.04           N  
ANISOU  212  N   PHE A  27     7217   7390   7445   -101   -264    312       N  
ATOM    213  CA  PHE A  27      13.859  21.045  87.147  1.00 60.02           C  
ANISOU  213  CA  PHE A  27     7333   7732   7739     -4   -174    252       C  
ATOM    214  C   PHE A  27      14.788  20.742  88.294  1.00 60.44           C  
ANISOU  214  C   PHE A  27     7177   7892   7897     56   -227    252       C  
ATOM    215  O   PHE A  27      15.362  19.630  88.366  1.00 61.84           O  
ANISOU  215  O   PHE A  27     7261   8100   8137    225   -233    204       O  
ATOM    216  CB  PHE A  27      14.678  21.563  85.954  1.00 61.56           C  
ANISOU  216  CB  PHE A  27     7515   8020   7855   -100     -5    201       C  
ATOM    217  CG  PHE A  27      14.044  21.278  84.648  1.00 63.25           C  
ANISOU  217  CG  PHE A  27     7938   8126   7968    -88     53    175       C  
ATOM    218  CD1 PHE A  27      13.733  22.287  83.788  1.00 66.43           C  
ANISOU  218  CD1 PHE A  27     8528   8475   8239   -243     97    188       C  
ATOM    219  CD2 PHE A  27      13.691  19.982  84.308  1.00 70.25           C  
ANISOU  219  CD2 PHE A  27     8882   8937   8873     73     37    141       C  
ATOM    220  CE1 PHE A  27      13.092  22.023  82.556  1.00 70.05           C  
ANISOU  220  CE1 PHE A  27     9213   8813   8588   -234    122    167       C  
ATOM    221  CE2 PHE A  27      13.053  19.690  83.077  1.00 70.95           C  
ANISOU  221  CE2 PHE A  27     9192   8912   8854     70     73    119       C  
ATOM    222  CZ  PHE A  27      12.761  20.719  82.206  1.00 70.75           C  
ANISOU  222  CZ  PHE A  27     9334   8844   8704    -82    112    133       C  
ATOM    223  N   SER A  28      14.942  21.747  89.166  1.00 58.45           N  
ANISOU  223  N   SER A  28     6876   7680   7651    -73   -280    302       N  
ATOM    224  CA  SER A  28      15.852  21.663  90.287  1.00 59.26           C  
ANISOU  224  CA  SER A  28     6790   7888   7839    -52   -355    310       C  
ATOM    225  C   SER A  28      15.431  20.657  91.299  1.00 58.72           C  
ANISOU  225  C   SER A  28     6762   7720   7831     92   -498    332       C  
ATOM    226  O   SER A  28      16.262  19.969  91.845  1.00 60.44           O  
ANISOU  226  O   SER A  28     6845   8000   8121    213   -565    308       O  
ATOM    227  CB  SER A  28      16.093  23.029  90.928  1.00 58.29           C  
ANISOU  227  CB  SER A  28     6657   7811   7679   -256   -380    361       C  
ATOM    228  OG  SER A  28      17.210  23.613  90.222  1.00 61.56           O  
ANISOU  228  OG  SER A  28     6925   8400   8063   -387   -252    316       O  
ATOM    229  N   GLN A  29      14.131  20.546  91.514  1.00 56.85           N  
ANISOU  229  N   GLN A  29     6717   7331   7552     77   -547    370       N  
ATOM    230  CA  GLN A  29      13.579  19.593  92.442  1.00 56.67           C  
ANISOU  230  CA  GLN A  29     6786   7199   7548    156   -663    391       C  
ATOM    231  C   GLN A  29      13.490  18.172  91.854  1.00 57.31           C  
ANISOU  231  C   GLN A  29     6944   7205   7627    314   -665    347       C  
ATOM    232  O   GLN A  29      13.509  17.231  92.559  1.00 58.11           O  
ANISOU  232  O   GLN A  29     7118   7225   7736    402   -766    352       O  
ATOM    233  CB  GLN A  29      12.202  20.109  92.897  1.00 55.37           C  
ANISOU  233  CB  GLN A  29     6766   6942   7329     46   -688    430       C  
ATOM    234  CG  GLN A  29      12.269  21.542  93.460  1.00 53.97           C  
ANISOU  234  CG  GLN A  29     6566   6807   7132    -85   -689    467       C  
ATOM    235  CD  GLN A  29      10.980  22.044  94.081  1.00 50.35           C  
ANISOU  235  CD  GLN A  29     6228   6274   6627   -148   -715    484       C  
ATOM    236  OE1 GLN A  29       9.915  21.861  93.556  1.00 53.58           O  
ANISOU  236  OE1 GLN A  29     6703   6644   7010   -132   -692    459       O  
ATOM    237  NE2 GLN A  29      11.100  22.731  95.180  1.00 50.89           N  
ANISOU  237  NE2 GLN A  29     6314   6339   6682   -221   -760    517       N  
ATOM    238  N   TYR A  30      13.392  18.029  90.547  1.00 58.80           N  
ANISOU  238  N   TYR A  30     7161   7399   7782    342   -558    303       N  
ATOM    239  CA  TYR A  30      13.281  16.699  89.927  1.00 59.28           C  
ANISOU  239  CA  TYR A  30     7341   7366   7817    486   -557    258       C  
ATOM    240  C   TYR A  30      14.637  16.125  89.818  1.00 60.68           C  
ANISOU  240  C   TYR A  30     7376   7630   8052    671   -542    195       C  
ATOM    241  O   TYR A  30      14.798  14.925  90.059  1.00 62.67           O  
ANISOU  241  O   TYR A  30     7728   7783   8301    843   -625    169       O  
ATOM    242  CB  TYR A  30      12.633  16.775  88.547  1.00 59.13           C  
ANISOU  242  CB  TYR A  30     7433   7309   7724    440   -457    233       C  
ATOM    243  CG  TYR A  30      11.134  16.888  88.670  1.00 61.16           C  
ANISOU  243  CG  TYR A  30     7840   7469   7929    318   -517    274       C  
ATOM    244  CD1 TYR A  30      10.295  15.894  88.160  1.00 62.78           C  
ANISOU  244  CD1 TYR A  30     8228   7557   8069    327   -546    258       C  
ATOM    245  CD2 TYR A  30      10.553  17.934  89.408  1.00 60.71           C  
ANISOU  245  CD2 TYR A  30     7736   7446   7885    195   -553    318       C  
ATOM    246  CE1 TYR A  30       8.894  15.985  88.286  1.00 65.87           C  
ANISOU  246  CE1 TYR A  30     8704   7905   8419    198   -603    279       C  
ATOM    247  CE2 TYR A  30       9.147  18.022  89.565  1.00 63.38           C  
ANISOU  247  CE2 TYR A  30     8162   7735   8186    106   -603    331       C  
ATOM    248  CZ  TYR A  30       8.334  17.047  88.991  1.00 65.40           C  
ANISOU  248  CZ  TYR A  30     8549   7911   8388    101   -626    308       C  
ATOM    249  OH  TYR A  30       6.972  17.124  89.124  1.00 68.45           O  
ANISOU  249  OH  TYR A  30     8968   8294   8744     -1   -673    304       O  
ATOM    250  N   LEU A  31      15.637  16.947  89.514  1.00 60.25           N  
ANISOU  250  N   LEU A  31     7091   7760   8039    639   -446    163       N  
ATOM    251  CA  LEU A  31      16.969  16.372  89.364  1.00 62.73           C  
ANISOU  251  CA  LEU A  31     7206   8207   8420    836   -420     74       C  
ATOM    252  C   LEU A  31      17.996  17.096  90.195  1.00 63.67           C  
ANISOU  252  C   LEU A  31     7050   8518   8625    792   -466     76       C  
ATOM    253  O   LEU A  31      18.544  18.111  89.777  1.00 64.34           O  
ANISOU  253  O   LEU A  31     6961   8778   8708    633   -342     58       O  
ATOM    254  CB  LEU A  31      17.379  16.358  87.896  1.00 64.47           C  
ANISOU  254  CB  LEU A  31     7381   8515   8598    863   -217    -15       C  
ATOM    255  CG  LEU A  31      16.280  15.968  86.901  1.00 62.68           C  
ANISOU  255  CG  LEU A  31     7445   8107   8262    830   -162     -5       C  
ATOM    256  CD1 LEU A  31      16.560  16.551  85.547  1.00 65.91           C  
ANISOU  256  CD1 LEU A  31     7835   8607   8599    732     45    -60       C  
ATOM    257  CD2 LEU A  31      16.194  14.473  86.846  1.00 62.18           C  
ANISOU  257  CD2 LEU A  31     7547   7896   8183   1067   -233    -49       C  
ATOM    258  N   GLN A  32      18.292  16.554  91.365  1.00 63.98           N  
ANISOU  258  N   GLN A  32     7069   8519   8721    916   -654     95       N  
ATOM    259  CA  GLN A  32      18.887  17.382  92.378  1.00 64.59           C  
ANISOU  259  CA  GLN A  32     6967   8721   8853    804   -746    135       C  
ATOM    260  C   GLN A  32      20.385  17.273  92.312  1.00 68.46           C  
ANISOU  260  C   GLN A  32     7105   9464   9441    943   -743     35       C  
ATOM    261  O   GLN A  32      21.159  18.035  92.942  1.00 70.39           O  
ANISOU  261  O   GLN A  32     7119   9888   9737    830   -797     43       O  
ATOM    262  CB  GLN A  32      18.380  16.965  93.744  1.00 63.64           C  
ANISOU  262  CB  GLN A  32     7034   8423   8724    828   -962    213       C  
ATOM    263  CG  GLN A  32      16.908  16.951  93.855  1.00 60.96           C  
ANISOU  263  CG  GLN A  32     6997   7873   8292    699   -953    286       C  
ATOM    264  CD  GLN A  32      16.492  16.117  94.997  1.00 63.36           C  
ANISOU  264  CD  GLN A  32     7518   7993   8564    760  -1138    331       C  
ATOM    265  OE1 GLN A  32      15.731  15.129  94.850  1.00 64.86           O  
ANISOU  265  OE1 GLN A  32     7954   8004   8685    819  -1162    331       O  
ATOM    266  NE2 GLN A  32      16.976  16.482  96.163  1.00 59.78           N  
ANISOU  266  NE2 GLN A  32     7010   7569   8136    721  -1276    371       N  
ATOM    267  N   GLN A  33      20.849  16.346  91.531  1.00 70.02           N  
ANISOU  267  N   GLN A  33     7239   9702   9662   1187   -677    -72       N  
ATOM    268  CA  GLN A  33      22.258  16.239  91.518  1.00 73.61           C  
ANISOU  268  CA  GLN A  33     7315  10432  10220   1342   -676   -187       C  
ATOM    269  C   GLN A  33      22.816  16.998  90.359  1.00 74.65           C  
ANISOU  269  C   GLN A  33     7213  10815  10338   1180   -402   -268       C  
ATOM    270  O   GLN A  33      23.997  17.312  90.317  1.00 77.88           O  
ANISOU  270  O   GLN A  33     7237  11530  10822   1182   -348   -364       O  
ATOM    271  CB  GLN A  33      22.619  14.789  91.521  1.00 76.04           C  
ANISOU  271  CB  GLN A  33     7664  10660  10567   1747   -790   -278       C  
ATOM    272  CG  GLN A  33      22.010  14.088  92.724  1.00 74.46           C  
ANISOU  272  CG  GLN A  33     7773  10178  10341   1848  -1070   -183       C  
ATOM    273  CD  GLN A  33      22.371  12.633  92.704  1.00 78.80           C  
ANISOU  273  CD  GLN A  33     8437  10605  10898   2258  -1206   -273       C  
ATOM    274  OE1 GLN A  33      23.528  12.294  92.509  1.00 83.62           O  
ANISOU  274  OE1 GLN A  33     8742  11426  11604   2529  -1222   -408       O  
ATOM    275  NE2 GLN A  33      21.387  11.758  92.856  1.00 77.97           N  
ANISOU  275  NE2 GLN A  33     8776  10167  10681   2309  -1298   -212       N  
ATOM    276  N   CYS A  34      21.944  17.355  89.434  1.00 73.23           N  
ANISOU  276  N   CYS A  34     7268  10509  10045   1008   -232   -230       N  
ATOM    277  CA  CYS A  34      22.389  18.016  88.211  1.00 75.37           C  
ANISOU  277  CA  CYS A  34     7407  10972  10259    837     42   -306       C  
ATOM    278  C   CYS A  34      23.094  19.389  88.349  1.00 76.11           C  
ANISOU  278  C   CYS A  34     7259  11316  10343    506    127   -298       C  
ATOM    279  O   CYS A  34      22.693  20.223  89.158  1.00 74.54           O  
ANISOU  279  O   CYS A  34     7157  11042  10123    298      8   -183       O  
ATOM    280  CB  CYS A  34      21.250  18.048  87.204  1.00 73.47           C  
ANISOU  280  CB  CYS A  34     7525  10507   9884    740    161   -262       C  
ATOM    281  SG  CYS A  34      21.354  16.605  86.161  1.00 78.47           S  
ANISOU  281  SG  CYS A  34     8244  11075  10498   1069    264   -389       S  
ATOM    282  N   PRO A  35      24.173  19.616  87.575  1.00 78.94           N  
ANISOU  282  N   PRO A  35     7308  11979  10705    443    340   -431       N  
ATOM    283  CA  PRO A  35      24.717  20.965  87.617  1.00 80.04           C  
ANISOU  283  CA  PRO A  35     7294  12327  10791     55    434   -414       C  
ATOM    284  C   PRO A  35      23.703  22.068  87.212  1.00 77.81           C  
ANISOU  284  C   PRO A  35     7407  11825  10334   -281    496   -287       C  
ATOM    285  O   PRO A  35      22.756  21.827  86.457  1.00 75.54           O  
ANISOU  285  O   PRO A  35     7440  11305   9957   -236    554   -256       O  
ATOM    286  CB  PRO A  35      25.871  20.904  86.627  1.00 83.42           C  
ANISOU  286  CB  PRO A  35     7377  13102  11217     27    705   -593       C  
ATOM    287  CG  PRO A  35      26.288  19.467  86.641  1.00 84.60           C  
ANISOU  287  CG  PRO A  35     7343  13301  11501    499    650   -717       C  
ATOM    288  CD  PRO A  35      25.079  18.661  86.916  1.00 81.68           C  
ANISOU  288  CD  PRO A  35     7386  12529  11119    730    468   -611       C  
ATOM    289  N   PHE A  36      23.913  23.259  87.756  1.00 77.92           N  
ANISOU  289  N   PHE A  36     7406  11905  10297   -599    458   -218       N  
ATOM    290  CA  PHE A  36      23.178  24.466  87.401  1.00 76.38           C  
ANISOU  290  CA  PHE A  36     7567  11534   9920   -924    508   -118       C  
ATOM    291  C   PHE A  36      23.089  24.755  85.883  1.00 77.98           C  
ANISOU  291  C   PHE A  36     7944  11727   9958  -1082    766   -173       C  
ATOM    292  O   PHE A  36      21.981  24.944  85.357  1.00 76.14           O  
ANISOU  292  O   PHE A  36     8101  11217   9613  -1092    753   -102       O  
ATOM    293  CB  PHE A  36      23.800  25.664  88.154  1.00 77.20           C  
ANISOU  293  CB  PHE A  36     7576  11777   9981  -1258    455    -71       C  
ATOM    294  CG  PHE A  36      23.131  26.963  87.860  1.00 75.44           C  
ANISOU  294  CG  PHE A  36     7754  11356   9552  -1581    484     26       C  
ATOM    295  CD1 PHE A  36      21.770  27.131  88.117  1.00 70.22           C  
ANISOU  295  CD1 PHE A  36     7482  10355   8845  -1485    344    136       C  
ATOM    296  CD2 PHE A  36      23.858  28.025  87.306  1.00 75.57           C  
ANISOU  296  CD2 PHE A  36     7775  11532   9407  -1985    650     -3       C  
ATOM    297  CE1 PHE A  36      21.133  28.343  87.829  1.00 71.09           C  
ANISOU  297  CE1 PHE A  36     7983  10269   8760  -1731    346    213       C  
ATOM    298  CE2 PHE A  36      23.241  29.231  87.022  1.00 73.15           C  
ANISOU  298  CE2 PHE A  36     7910  11002   8882  -2268    652     87       C  
ATOM    299  CZ  PHE A  36      21.873  29.401  87.272  1.00 72.11           C  
ANISOU  299  CZ  PHE A  36     8172  10514   8713  -2116    490    193       C  
ATOM    300  N   ASP A  37      24.244  24.773  85.198  1.00 81.37           N  
ANISOU  300  N   ASP A  37     8081  12469  10368  -1205    994   -306       N  
ATOM    301  CA  ASP A  37      24.351  25.071  83.756  1.00 83.05           C  
ANISOU  301  CA  ASP A  37     8447  12709  10398  -1403   1273   -376       C  
ATOM    302  C   ASP A  37      23.416  24.215  82.892  1.00 81.17           C  
ANISOU  302  C   ASP A  37     8499  12218  10125  -1148   1302   -379       C  
ATOM    303  O   ASP A  37      22.822  24.697  81.922  1.00 80.77           O  
ANISOU  303  O   ASP A  37     8815  11988   9884  -1319   1400   -348       O  
ATOM    304  CB  ASP A  37      25.816  24.902  83.274  1.00 87.48           C  
ANISOU  304  CB  ASP A  37     8549  13705  10986  -1496   1528   -557       C  
ATOM    305  CG  ASP A  37      26.707  26.142  83.570  1.00 93.26           C  
ANISOU  305  CG  ASP A  37     9112  14693  11628  -1961   1601   -562       C  
ATOM    306  OD1 ASP A  37      27.937  26.122  83.252  1.00100.86           O  
ANISOU  306  OD1 ASP A  37     9649  16063  12610  -2096   1814   -718       O  
ATOM    307  OD2 ASP A  37      26.195  27.161  84.104  1.00 94.77           O  
ANISOU  307  OD2 ASP A  37     9598  14692  11717  -2208   1455   -418       O  
ATOM    308  N   GLU A  38      23.280  22.942  83.238  1.00 80.05           N  
ANISOU  308  N   GLU A  38     8224  12042  10148   -749   1198   -415       N  
ATOM    309  CA  GLU A  38      22.416  22.054  82.469  1.00 79.06           C  
ANISOU  309  CA  GLU A  38     8376  11678   9984   -521   1210   -420       C  
ATOM    310  C   GLU A  38      20.961  22.429  82.639  1.00 75.53           C  
ANISOU  310  C   GLU A  38     8349  10883   9467   -561   1022   -267       C  
ATOM    311  O   GLU A  38      20.181  22.297  81.718  1.00 74.81           O  
ANISOU  311  O   GLU A  38     8571  10596   9256   -559   1064   -253       O  
ATOM    312  CB  GLU A  38      22.605  20.604  82.876  1.00 79.01           C  
ANISOU  312  CB  GLU A  38     8182  11689  10148    -98   1119   -491       C  
ATOM    313  CG  GLU A  38      24.064  20.223  83.229  1.00 85.38           C  
ANISOU  313  CG  GLU A  38     8480  12866  11094     32   1193   -638       C  
ATOM    314  CD  GLU A  38      25.130  20.791  82.285  1.00 89.70           C  
ANISOU  314  CD  GLU A  38     8795  13737  11550   -213   1515   -777       C  
ATOM    315  OE1 GLU A  38      25.015  20.582  81.041  1.00 92.57           O  
ANISOU  315  OE1 GLU A  38     9337  14056  11777   -240   1742   -849       O  
ATOM    316  OE2 GLU A  38      26.099  21.422  82.799  1.00 91.08           O  
ANISOU  316  OE2 GLU A  38     8608  14220  11780   -395   1544   -821       O  
ATOM    317  N   HIS A  39      20.596  22.882  83.833  1.00 73.89           N  
ANISOU  317  N   HIS A  39     8135  10609   9330   -587    811   -162       N  
ATOM    318  CA  HIS A  39      19.223  23.278  84.081  1.00 71.49           C  
ANISOU  318  CA  HIS A  39     8178  10015   8970   -608    640    -38       C  
ATOM    319  C   HIS A  39      18.880  24.587  83.324  1.00 70.75           C  
ANISOU  319  C   HIS A  39     8387   9824   8671   -915    711      7       C  
ATOM    320  O   HIS A  39      17.751  24.829  82.894  1.00 67.87           O  
ANISOU  320  O   HIS A  39     8353   9222   8212   -909    630     67       O  
ATOM    321  CB  HIS A  39      18.957  23.370  85.601  1.00 69.28           C  
ANISOU  321  CB  HIS A  39     7814   9697   8812   -543    415     45       C  
ATOM    322  CG  HIS A  39      18.642  22.052  86.239  1.00 71.83           C  
ANISOU  322  CG  HIS A  39     8065   9952   9274   -234    281     40       C  
ATOM    323  ND1 HIS A  39      19.395  21.519  87.267  1.00 72.68           N  
ANISOU  323  ND1 HIS A  39     7905  10188   9521    -95    183     17       N  
ATOM    324  CD2 HIS A  39      17.667  21.141  85.976  1.00 72.73           C  
ANISOU  324  CD2 HIS A  39     8372   9874   9388    -52    219     52       C  
ATOM    325  CE1 HIS A  39      18.897  20.340  87.606  1.00 74.09           C  
ANISOU  325  CE1 HIS A  39     8151  10232   9766    160     67     19       C  
ATOM    326  NE2 HIS A  39      17.859  20.078  86.831  1.00 71.79           N  
ANISOU  326  NE2 HIS A  39     8131   9754   9391    176     97     38       N  
ATOM    327  N   VAL A  40      19.872  25.437  83.177  1.00 73.18           N  
ANISOU  327  N   VAL A  40     8588  10319   8899  -1189    849    -26       N  
ATOM    328  CA  VAL A  40      19.615  26.697  82.551  1.00 74.51           C  
ANISOU  328  CA  VAL A  40     9095  10370   8846  -1497    897     21       C  
ATOM    329  C   VAL A  40      19.316  26.451  81.088  1.00 76.11           C  
ANISOU  329  C   VAL A  40     9552  10471   8897  -1515   1044    -28       C  
ATOM    330  O   VAL A  40      18.427  27.116  80.523  1.00 75.88           O  
ANISOU  330  O   VAL A  40     9936  10195   8701  -1605    972     36       O  
ATOM    331  CB  VAL A  40      20.780  27.630  82.724  1.00 77.49           C  
ANISOU  331  CB  VAL A  40     9323  10974   9145  -1838   1020     -6       C  
ATOM    332  CG1 VAL A  40      20.494  28.995  82.050  1.00 77.82           C  
ANISOU  332  CG1 VAL A  40     9816  10845   8908  -2188   1057     49       C  
ATOM    333  CG2 VAL A  40      21.110  27.752  84.239  1.00 75.43           C  
ANISOU  333  CG2 VAL A  40     8797  10817   9047  -1799    848     40       C  
ATOM    334  N   LYS A  41      20.020  25.486  80.483  1.00 77.73           N  
ANISOU  334  N   LYS A  41     9531  10850   9152  -1404   1233   -145       N  
ATOM    335  CA  LYS A  41      19.664  25.056  79.135  1.00 78.30           C  
ANISOU  335  CA  LYS A  41     9862  10802   9086  -1377   1362   -194       C  
ATOM    336  C   LYS A  41      18.236  24.475  79.084  1.00 75.28           C  
ANISOU  336  C   LYS A  41     9745  10123   8735  -1129   1145   -120       C  
ATOM    337  O   LYS A  41      17.428  24.822  78.213  1.00 74.88           O  
ANISOU  337  O   LYS A  41    10082   9854   8517  -1201   1110    -83       O  
ATOM    338  CB  LYS A  41      20.673  24.056  78.573  1.00 80.79           C  
ANISOU  338  CB  LYS A  41     9882  11359   9456  -1260   1606   -349       C  
ATOM    339  CG  LYS A  41      22.020  24.641  78.286  1.00 83.94           C  
ANISOU  339  CG  LYS A  41    10037  12076   9779  -1550   1872   -453       C  
ATOM    340  CD  LYS A  41      23.066  23.547  78.230  1.00 87.54           C  
ANISOU  340  CD  LYS A  41    10041  12835  10384  -1321   2049   -619       C  
ATOM    341  CE  LYS A  41      24.460  24.104  78.486  1.00 92.45           C  
ANISOU  341  CE  LYS A  41    10239  13863  11026  -1567   2237   -722       C  
ATOM    342  NZ  LYS A  41      24.663  24.489  79.925  1.00 92.04           N  
ANISOU  342  NZ  LYS A  41     9929  13902  11140  -1567   2007   -644       N  
ATOM    343  N   LEU A  42      17.896  23.602  80.004  1.00 72.99           N  
ANISOU  343  N   LEU A  42     9264   9824   8645   -853    989   -100       N  
ATOM    344  CA  LEU A  42      16.574  23.032  79.854  1.00 71.82           C  
ANISOU  344  CA  LEU A  42     9355   9429   8503   -673    815    -46       C  
ATOM    345  C   LEU A  42      15.510  24.136  79.960  1.00 70.72           C  
ANISOU  345  C   LEU A  42     9512   9092   8266   -796    638     58       C  
ATOM    346  O   LEU A  42      14.579  24.158  79.148  1.00 70.66           O  
ANISOU  346  O   LEU A  42     9809   8893   8147   -783    567     79       O  
ATOM    347  CB  LEU A  42      16.315  21.812  80.774  1.00 69.70           C  
ANISOU  347  CB  LEU A  42     8892   9160   8432   -383    682    -44       C  
ATOM    348  CG  LEU A  42      17.397  20.721  80.895  1.00 72.26           C  
ANISOU  348  CG  LEU A  42     8919   9667   8869   -194    801   -151       C  
ATOM    349  CD1 LEU A  42      16.783  19.495  81.486  1.00 69.38           C  
ANISOU  349  CD1 LEU A  42     8564   9181   8616     73    638   -134       C  
ATOM    350  CD2 LEU A  42      18.195  20.324  79.598  1.00 73.23           C  
ANISOU  350  CD2 LEU A  42     9044   9891   8888   -200   1065   -278       C  
ATOM    351  N   VAL A  43      15.639  25.033  80.952  1.00 70.36           N  
ANISOU  351  N   VAL A  43     9388   9087   8258   -896    552    116       N  
ATOM    352  CA  VAL A  43      14.733  26.199  81.083  1.00 69.49           C  
ANISOU  352  CA  VAL A  43     9571   8791   8040   -992    390    198       C  
ATOM    353  C   VAL A  43      14.643  27.076  79.792  1.00 71.51           C  
ANISOU  353  C   VAL A  43    10218   8913   8040  -1201    454    196       C  
ATOM    354  O   VAL A  43      13.534  27.313  79.308  1.00 70.88           O  
ANISOU  354  O   VAL A  43    10436   8622   7874  -1133    301    230       O  
ATOM    355  CB  VAL A  43      15.046  27.124  82.342  1.00 69.74           C  
ANISOU  355  CB  VAL A  43     9499   8882   8118  -1096    311    252       C  
ATOM    356  CG1 VAL A  43      14.213  28.447  82.312  1.00 67.13           C  
ANISOU  356  CG1 VAL A  43     9537   8340   7629  -1192    164    318       C  
ATOM    357  CG2 VAL A  43      14.843  26.387  83.678  1.00 65.86           C  
ANISOU  357  CG2 VAL A  43     8728   8452   7843   -892    193    272       C  
ATOM    358  N   ASN A  44      15.774  27.554  79.255  1.00 73.80           N  
ANISOU  358  N   ASN A  44    10513   9328   8200  -1459    668    152       N  
ATOM    359  CA  ASN A  44      15.761  28.398  78.049  1.00 76.33           C  
ANISOU  359  CA  ASN A  44    11255   9506   8240  -1702    740    151       C  
ATOM    360  C   ASN A  44      15.022  27.722  76.894  1.00 77.10           C  
ANISOU  360  C   ASN A  44    11594   9442   8257  -1577    723    127       C  
ATOM    361  O   ASN A  44      14.078  28.308  76.347  1.00 77.87           O  
ANISOU  361  O   ASN A  44    12091   9292   8204  -1582    554    176       O  
ATOM    362  CB  ASN A  44      17.181  28.797  77.600  1.00 79.05           C  
ANISOU  362  CB  ASN A  44    11520  10061   8456  -2031   1029     83       C  
ATOM    363  CG  ASN A  44      17.811  29.873  78.492  1.00 80.96           C  
ANISOU  363  CG  ASN A  44    11694  10397   8670  -2273   1016    123       C  
ATOM    364  OD1 ASN A  44      17.120  30.626  79.176  1.00 79.51           O  
ANISOU  364  OD1 ASN A  44    11694  10041   8473  -2245    795    210       O  
ATOM    365  ND2 ASN A  44      19.143  29.951  78.468  1.00 84.89           N  
ANISOU  365  ND2 ASN A  44    11924  11183   9150  -2519   1258     48       N  
ATOM    366  N   GLU A  45      15.420  26.495  76.543  1.00 77.21           N  
ANISOU  366  N   GLU A  45    11386   9584   8368  -1447    873     50       N  
ATOM    367  CA  GLU A  45      14.709  25.706  75.515  1.00 77.66           C  
ANISOU  367  CA  GLU A  45    11666   9484   8357  -1318    847     26       C  
ATOM    368  C   GLU A  45      13.182  25.698  75.658  1.00 74.76           C  
ANISOU  368  C   GLU A  45    11495   8889   8022  -1136    534    102       C  
ATOM    369  O   GLU A  45      12.451  26.026  74.716  1.00 75.79           O  
ANISOU  369  O   GLU A  45    12009   8812   7975  -1174    429    121       O  
ATOM    370  CB  GLU A  45      15.240  24.260  75.424  1.00 78.16           C  
ANISOU  370  CB  GLU A  45    11440   9699   8559  -1131   1003    -64       C  
ATOM    371  CG  GLU A  45      14.184  23.236  74.993  1.00 79.58           C  
ANISOU  371  CG  GLU A  45    11769   9704   8764   -910    859    -57       C  
ATOM    372  CD  GLU A  45      14.774  21.922  74.487  1.00 85.28           C  
ANISOU  372  CD  GLU A  45    12374  10510   9517   -772   1047   -160       C  
ATOM    373  OE1 GLU A  45      14.696  21.676  73.247  1.00 87.74           O  
ANISOU  373  OE1 GLU A  45    12979  10712   9646   -831   1149   -204       O  
ATOM    374  OE2 GLU A  45      15.310  21.139  75.323  1.00 84.26           O  
ANISOU  374  OE2 GLU A  45    11893  10539   9582   -593   1083   -199       O  
ATOM    375  N   LEU A  46      12.717  25.299  76.828  1.00 72.28           N  
ANISOU  375  N   LEU A  46    10910   8627   7928   -942    386    134       N  
ATOM    376  CA  LEU A  46      11.283  25.131  77.101  1.00 70.27           C  
ANISOU  376  CA  LEU A  46    10735   8225   7738   -762    116    181       C  
ATOM    377  C   LEU A  46      10.625  26.488  77.000  1.00 70.03           C  
ANISOU  377  C   LEU A  46    11003   8034   7571   -837    -59    235       C  
ATOM    378  O   LEU A  46       9.471  26.615  76.544  1.00 69.73           O  
ANISOU  378  O   LEU A  46    11185   7834   7476   -739   -269    251       O  
ATOM    379  CB  LEU A  46      11.074  24.550  78.492  1.00 67.86           C  
ANISOU  379  CB  LEU A  46    10080   8033   7673   -597     36    198       C  
ATOM    380  CG  LEU A  46       9.765  23.783  78.567  1.00 69.40           C  
ANISOU  380  CG  LEU A  46    10285   8140   7943   -423   -156    208       C  
ATOM    381  CD1 LEU A  46       9.811  22.579  77.586  1.00 71.32           C  
ANISOU  381  CD1 LEU A  46    10609   8347   8141   -380    -75    159       C  
ATOM    382  CD2 LEU A  46       9.429  23.325  80.009  1.00 64.87           C  
ANISOU  382  CD2 LEU A  46     9419   7658   7572   -301   -242    228       C  
ATOM    383  N   THR A  47      11.402  27.500  77.392  1.00 69.70           N  
ANISOU  383  N   THR A  47    10981   8039   7464  -1012     22    254       N  
ATOM    384  CA  THR A  47      10.989  28.862  77.332  1.00 69.89           C  
ANISOU  384  CA  THR A  47    11337   7893   7325  -1100   -126    300       C  
ATOM    385  C   THR A  47      10.877  29.315  75.878  1.00 72.17           C  
ANISOU  385  C   THR A  47    12095   7989   7338  -1241   -126    293       C  
ATOM    386  O   THR A  47       9.837  29.855  75.521  1.00 72.47           O  
ANISOU  386  O   THR A  47    12441   7818   7277  -1141   -370    319       O  
ATOM    387  CB  THR A  47      11.909  29.750  78.178  1.00 71.08           C  
ANISOU  387  CB  THR A  47    11405   8140   7463  -1284    -36    324       C  
ATOM    388  OG1 THR A  47      11.623  29.520  79.570  1.00 69.52           O  
ANISOU  388  OG1 THR A  47    10881   8041   7491  -1114   -131    345       O  
ATOM    389  CG2 THR A  47      11.712  31.238  77.861  1.00 70.60           C  
ANISOU  389  CG2 THR A  47    11811   7863   7149  -1442   -150    366       C  
ATOM    390  N   GLU A  48      11.871  29.087  75.018  1.00 73.61           N  
ANISOU  390  N   GLU A  48    12348   8234   7387  -1455    130    250       N  
ATOM    391  CA  GLU A  48      11.620  29.358  73.574  1.00 77.09           C  
ANISOU  391  CA  GLU A  48    13277   8463   7550  -1577    117    241       C  
ATOM    392  C   GLU A  48      10.273  28.777  73.118  1.00 75.75           C  
ANISOU  392  C   GLU A  48    13230   8134   7418  -1322   -141    250       C  
ATOM    393  O   GLU A  48       9.410  29.495  72.589  1.00 76.53           O  
ANISOU  393  O   GLU A  48    13725   7997   7356  -1288   -386    282       O  
ATOM    394  CB  GLU A  48      12.734  28.858  72.651  1.00 78.98           C  
ANISOU  394  CB  GLU A  48    13529   8816   7664  -1795    453    169       C  
ATOM    395  CG  GLU A  48      13.923  29.866  72.540  1.00 85.83           C  
ANISOU  395  CG  GLU A  48    14518   9758   8333  -2173    681    157       C  
ATOM    396  CD  GLU A  48      15.228  29.382  73.216  1.00 89.53           C  
ANISOU  396  CD  GLU A  48    14456  10585   8974  -2256    974     89       C  
ATOM    397  OE1 GLU A  48      16.130  30.207  73.497  1.00 92.02           O  
ANISOU  397  OE1 GLU A  48    14747  11019   9196  -2546   1116     85       O  
ATOM    398  OE2 GLU A  48      15.364  28.165  73.462  1.00 92.22           O  
ANISOU  398  OE2 GLU A  48    14412  11091   9537  -2031   1050     36       O  
ATOM    399  N   PHE A  49      10.083  27.492  73.410  1.00 73.56           N  
ANISOU  399  N   PHE A  49    12603   7991   7357  -1139   -108    219       N  
ATOM    400  CA  PHE A  49       8.934  26.762  72.942  1.00 72.75           C  
ANISOU  400  CA  PHE A  49    12574   7780   7286   -952   -312    216       C  
ATOM    401  C   PHE A  49       7.652  27.350  73.496  1.00 71.49           C  
ANISOU  401  C   PHE A  49    12439   7527   7196   -768   -648    255       C  
ATOM    402  O   PHE A  49       6.618  27.351  72.843  1.00 72.20           O  
ANISOU  402  O   PHE A  49    12752   7469   7212   -669   -885    257       O  
ATOM    403  CB  PHE A  49       9.057  25.282  73.323  1.00 71.54           C  
ANISOU  403  CB  PHE A  49    12048   7790   7343   -818   -204    177       C  
ATOM    404  CG  PHE A  49       7.915  24.449  72.843  1.00 69.74           C  
ANISOU  404  CG  PHE A  49    11898   7464   7135   -675   -401    172       C  
ATOM    405  CD1 PHE A  49       7.815  24.081  71.508  1.00 70.08           C  
ANISOU  405  CD1 PHE A  49    12279   7364   6984   -745   -384    148       C  
ATOM    406  CD2 PHE A  49       6.927  24.040  73.727  1.00 68.93           C  
ANISOU  406  CD2 PHE A  49    11542   7419   7230   -496   -601    187       C  
ATOM    407  CE1 PHE A  49       6.761  23.342  71.050  1.00 68.35           C  
ANISOU  407  CE1 PHE A  49    12146   7055   6769   -642   -586    145       C  
ATOM    408  CE2 PHE A  49       5.863  23.265  73.274  1.00 66.77           C  
ANISOU  408  CE2 PHE A  49    11324   7080   6964   -408   -785    176       C  
ATOM    409  CZ  PHE A  49       5.791  22.924  71.929  1.00 70.25           C  
ANISOU  409  CZ  PHE A  49    12106   7374   7213   -481   -787    158       C  
ATOM    410  N   ALA A  50       7.713  27.809  74.729  1.00 70.40           N  
ANISOU  410  N   ALA A  50    12050   7493   7207   -709   -671    276       N  
ATOM    411  CA  ALA A  50       6.622  28.592  75.253  1.00 70.27           C  
ANISOU  411  CA  ALA A  50    12088   7390   7223   -541   -957    297       C  
ATOM    412  C   ALA A  50       6.290  29.823  74.354  1.00 72.94           C  
ANISOU  412  C   ALA A  50    12961   7467   7285   -593  -1138    316       C  
ATOM    413  O   ALA A  50       5.126  30.025  74.052  1.00 73.52           O  
ANISOU  413  O   ALA A  50    13173   7423   7337   -406  -1425    305       O  
ATOM    414  CB  ALA A  50       6.927  29.006  76.644  1.00 68.53           C  
ANISOU  414  CB  ALA A  50    11590   7296   7151   -513   -914    314       C  
ATOM    415  N   LYS A  51       7.283  30.619  73.916  1.00 74.61           N  
ANISOU  415  N   LYS A  51    13482   7590   7277   -848   -985    337       N  
ATOM    416  CA  LYS A  51       6.989  31.844  73.166  1.00 77.49           C  
ANISOU  416  CA  LYS A  51    14419   7672   7351   -911  -1172    361       C  
ATOM    417  C   LYS A  51       6.336  31.449  71.846  1.00 79.80           C  
ANISOU  417  C   LYS A  51    15026   7798   7496   -871  -1319    346       C  
ATOM    418  O   LYS A  51       5.379  32.124  71.375  1.00 81.98           O  
ANISOU  418  O   LYS A  51    15663   7849   7638   -725  -1646    352       O  
ATOM    419  CB  LYS A  51       8.259  32.682  72.868  1.00 79.95           C  
ANISOU  419  CB  LYS A  51    15034   7926   7415  -1273   -943    384       C  
ATOM    420  CG  LYS A  51       8.945  33.420  74.082  1.00 78.93           C  
ANISOU  420  CG  LYS A  51    14736   7904   7350  -1374   -845    409       C  
ATOM    421  CD  LYS A  51      10.474  33.585  73.790  1.00 80.10           C  
ANISOU  421  CD  LYS A  51    14924   8164   7347  -1788   -491    404       C  
ATOM    422  CE  LYS A  51      11.352  33.913  75.045  1.00 78.42           C  
ANISOU  422  CE  LYS A  51    14377   8158   7262  -1914   -340    417       C  
ATOM    423  NZ  LYS A  51      11.791  35.364  75.084  1.00 79.30           N  
ANISOU  423  NZ  LYS A  51    14943   8097   7091  -2193   -368    459       N  
ATOM    424  N   THR A  52       6.844  30.356  71.246  1.00 78.40           N  
ANISOU  424  N   THR A  52    14730   7722   7336   -983  -1094    319       N  
ATOM    425  CA  THR A  52       6.375  29.932  69.941  1.00 78.31           C  
ANISOU  425  CA  THR A  52    15053   7547   7155   -995  -1196    306       C  
ATOM    426  C   THR A  52       4.898  29.509  70.037  1.00 77.32           C  
ANISOU  426  C   THR A  52    14796   7402   7180   -686  -1549    294       C  
ATOM    427  O   THR A  52       4.170  29.587  69.042  1.00 79.24           O  
ANISOU  427  O   THR A  52    15398   7450   7260   -640  -1789    292       O  
ATOM    428  CB  THR A  52       7.247  28.776  69.383  1.00 78.39           C  
ANISOU  428  CB  THR A  52    14935   7685   7166  -1154   -860    266       C  
ATOM    429  OG1 THR A  52       8.479  29.291  68.875  1.00 77.97           O  
ANISOU  429  OG1 THR A  52    15126   7613   6885  -1472   -565    257       O  
ATOM    430  CG2 THR A  52       6.563  28.080  68.275  1.00 78.16           C  
ANISOU  430  CG2 THR A  52    15150   7517   7030  -1106   -994    249       C  
ATOM    431  N   CYS A  53       4.454  29.078  71.217  1.00 73.32           N  
ANISOU  431  N   CYS A  53    13785   7103   6971   -494  -1587    281       N  
ATOM    432  CA  CYS A  53       3.082  28.590  71.358  1.00 72.68           C  
ANISOU  432  CA  CYS A  53    13509   7064   7042   -242  -1882    253       C  
ATOM    433  C   CYS A  53       2.129  29.719  71.649  1.00 72.51           C  
ANISOU  433  C   CYS A  53    13614   6938   7000    -27  -2218    246       C  
ATOM    434  O   CYS A  53       0.927  29.628  71.343  1.00 72.00           O  
ANISOU  434  O   CYS A  53    13545   6845   6964    173  -2531    210       O  
ATOM    435  CB  CYS A  53       2.927  27.541  72.460  1.00 71.04           C  
ANISOU  435  CB  CYS A  53    12726   7127   7140   -152  -1773    231       C  
ATOM    436  SG  CYS A  53       3.687  25.966  72.203  1.00 71.87           S  
ANISOU  436  SG  CYS A  53    12645   7352   7310   -290  -1474    218       S  
ATOM    437  N   VAL A  54       2.682  30.763  72.262  1.00 72.06           N  
ANISOU  437  N   VAL A  54    13654   6834   6890    -64  -2153    271       N  
ATOM    438  CA  VAL A  54       2.036  32.077  72.372  1.00 74.04           C  
ANISOU  438  CA  VAL A  54    14200   6903   7030    116  -2451    266       C  
ATOM    439  C   VAL A  54       1.906  32.681  70.963  1.00 76.75           C  
ANISOU  439  C   VAL A  54    15192   6927   7041     50  -2648    284       C  
ATOM    440  O   VAL A  54       0.805  33.047  70.545  1.00 78.35           O  
ANISOU  440  O   VAL A  54    15575   7000   7193    295  -3022    252       O  
ATOM    441  CB  VAL A  54       2.790  33.030  73.372  1.00 74.28           C  
ANISOU  441  CB  VAL A  54    14239   6934   7049     44  -2309    295       C  
ATOM    442  CG1 VAL A  54       2.629  34.447  72.978  1.00 78.29           C  
ANISOU  442  CG1 VAL A  54    15325   7137   7284     84  -2539    311       C  
ATOM    443  CG2 VAL A  54       2.304  32.868  74.823  1.00 72.55           C  
ANISOU  443  CG2 VAL A  54    13496   6946   7125    258  -2316    260       C  
ATOM    444  N   ALA A  55       2.985  32.718  70.193  1.00 77.68           N  
ANISOU  444  N   ALA A  55    15652   6931   6931   -277  -2408    324       N  
ATOM    445  CA  ALA A  55       2.854  33.222  68.821  1.00 81.93           C  
ANISOU  445  CA  ALA A  55    16851   7152   7126   -372  -2586    342       C  
ATOM    446  C   ALA A  55       1.891  32.399  67.949  1.00 84.16           C  
ANISOU  446  C   ALA A  55    17148   7404   7424   -233  -2822    312       C  
ATOM    447  O   ALA A  55       0.989  32.971  67.318  1.00 87.15           O  
ANISOU  447  O   ALA A  55    17899   7561   7654    -55  -3215    302       O  
ATOM    448  CB  ALA A  55       4.211  33.409  68.142  1.00 82.18           C  
ANISOU  448  CB  ALA A  55    17249   7088   6886   -791  -2245    377       C  
ATOM    449  N   ASP A  56       2.056  31.073  67.932  1.00 82.66           N  
ANISOU  449  N   ASP A  56    16571   7428   7407   -300  -2612    294       N  
ATOM    450  CA  ASP A  56       1.211  30.198  67.110  1.00 84.29           C  
ANISOU  450  CA  ASP A  56    16796   7613   7617   -220  -2813    269       C  
ATOM    451  C   ASP A  56       0.657  29.025  67.918  1.00 82.04           C  
ANISOU  451  C   ASP A  56    15858   7636   7676    -78  -2782    230       C  
ATOM    452  O   ASP A  56       1.417  28.132  68.268  1.00 78.95           O  
ANISOU  452  O   ASP A  56    15180   7414   7403   -218  -2444    232       O  
ATOM    453  CB  ASP A  56       2.014  29.615  65.928  1.00 85.56           C  
ANISOU  453  CB  ASP A  56    17313   7655   7542   -518  -2575    284       C  
ATOM    454  CG  ASP A  56       1.196  28.625  65.105  1.00 89.57           C  
ANISOU  454  CG  ASP A  56    17852   8136   8045   -461  -2766    262       C  
ATOM    455  OD1 ASP A  56      -0.054  28.801  65.079  1.00 91.31           O  
ANISOU  455  OD1 ASP A  56    18036   8329   8329   -216  -3183    241       O  
ATOM    456  OD2 ASP A  56       1.786  27.678  64.489  1.00 93.59           O  
ANISOU  456  OD2 ASP A  56    18417   8658   8484   -654  -2509    255       O  
ATOM    457  N   GLU A  57      -0.651  28.996  68.172  1.00 82.51           N  
ANISOU  457  N   GLU A  57    15702   7769   7880    188  -3133    187       N  
ATOM    458  CA  GLU A  57      -1.186  28.011  69.133  1.00 81.02           C  
ANISOU  458  CA  GLU A  57    14881   7891   8011    290  -3086    146       C  
ATOM    459  C   GLU A  57      -1.382  26.572  68.608  1.00 79.47           C  
ANISOU  459  C   GLU A  57    14562   7778   7856    173  -3028    135       C  
ATOM    460  O   GLU A  57      -1.203  25.573  69.341  1.00 78.69           O  
ANISOU  460  O   GLU A  57    14049   7893   7955    123  -2816    125       O  
ATOM    461  CB  GLU A  57      -2.424  28.554  69.841  1.00 81.98           C  
ANISOU  461  CB  GLU A  57    14721   8130   8298    599  -3413     84       C  
ATOM    462  CG  GLU A  57      -2.030  29.136  71.193  1.00 83.11           C  
ANISOU  462  CG  GLU A  57    14582   8402   8595    672  -3241     83       C  
ATOM    463  CD  GLU A  57      -3.137  29.962  71.879  1.00 86.81           C  
ANISOU  463  CD  GLU A  57    14860   8946   9179   1005  -3544      9       C  
ATOM    464  OE1 GLU A  57      -3.954  30.619  71.179  1.00 92.13           O  
ANISOU  464  OE1 GLU A  57    15805   9469   9730   1204  -3916    -29       O  
ATOM    465  OE2 GLU A  57      -3.181  29.944  73.120  1.00 82.68           O  
ANISOU  465  OE2 GLU A  57    13922   8631   8861   1080  -3412    -20       O  
ATOM    466  N   SER A  58      -1.737  26.512  67.343  1.00 80.21           N  
ANISOU  466  N   SER A  58    15068   7672   7735    127  -3233    139       N  
ATOM    467  CA  SER A  58      -1.806  25.335  66.499  1.00 79.44           C  
ANISOU  467  CA  SER A  58    15071   7548   7567    -22  -3200    138       C  
ATOM    468  C   SER A  58      -0.505  24.640  66.247  1.00 77.69           C  
ANISOU  468  C   SER A  58    14959   7296   7263   -256  -2770    164       C  
ATOM    469  O   SER A  58      -0.521  23.621  65.653  1.00 78.50           O  
ANISOU  469  O   SER A  58    15135   7378   7314   -360  -2717    156       O  
ATOM    470  CB  SER A  58      -2.226  25.799  65.101  1.00 81.73           C  
ANISOU  470  CB  SER A  58    15942   7548   7563    -40  -3503    149       C  
ATOM    471  OG  SER A  58      -3.570  26.161  65.062  1.00 82.89           O  
ANISOU  471  OG  SER A  58    15998   7724   7771    190  -3962    106       O  
ATOM    472  N   HIS A  59       0.625  25.226  66.568  1.00 77.34           N  
ANISOU  472  N   HIS A  59    14978   7234   7174   -345  -2479    188       N  
ATOM    473  CA  HIS A  59       1.884  24.615  66.226  1.00 78.14           C  
ANISOU  473  CA  HIS A  59    15176   7328   7185   -552  -2074    190       C  
ATOM    474  C   HIS A  59       2.051  23.323  67.051  1.00 76.59           C  
ANISOU  474  C   HIS A  59    14495   7367   7240   -523  -1875    166       C  
ATOM    475  O   HIS A  59       1.573  23.230  68.183  1.00 76.01           O  
ANISOU  475  O   HIS A  59    13988   7480   7411   -390  -1946    161       O  
ATOM    476  CB  HIS A  59       3.005  25.643  66.411  1.00 79.24           C  
ANISOU  476  CB  HIS A  59    15464   7426   7217   -672  -1835    211       C  
ATOM    477  CG  HIS A  59       4.374  25.115  66.129  1.00 83.78           C  
ANISOU  477  CG  HIS A  59    16068   8050   7713   -879  -1395    190       C  
ATOM    478  ND1 HIS A  59       5.150  24.498  67.094  1.00 85.11           N  
ANISOU  478  ND1 HIS A  59    15775   8460   8104   -865  -1102    169       N  
ATOM    479  CD2 HIS A  59       5.108  25.099  64.990  1.00 88.85           C  
ANISOU  479  CD2 HIS A  59    17138   8544   8076  -1093  -1197    174       C  
ATOM    480  CE1 HIS A  59       6.291  24.102  66.555  1.00 87.14           C  
ANISOU  480  CE1 HIS A  59    16137   8734   8239  -1033   -752    131       C  
ATOM    481  NE2 HIS A  59       6.294  24.456  65.278  1.00 90.04           N  
ANISOU  481  NE2 HIS A  59    17036   8875   8300  -1185   -782    131       N  
ATOM    482  N   ALA A  60       2.669  22.306  66.460  1.00 76.77           N  
ANISOU  482  N   ALA A  60    14626   7362   7180   -642  -1643    145       N  
ATOM    483  CA  ALA A  60       2.778  20.962  67.031  1.00 75.50           C  
ANISOU  483  CA  ALA A  60    14132   7356   7197   -611  -1495    119       C  
ATOM    484  C   ALA A  60       3.228  20.940  68.501  1.00 73.14           C  
ANISOU  484  C   ALA A  60    13344   7285   7161   -525  -1334    121       C  
ATOM    485  O   ALA A  60       4.116  21.680  68.890  1.00 74.03           O  
ANISOU  485  O   ALA A  60    13402   7444   7281   -554  -1147    129       O  
ATOM    486  CB  ALA A  60       3.722  20.105  66.158  1.00 76.15           C  
ANISOU  486  CB  ALA A  60    14469   7351   7113   -732  -1199     83       C  
ATOM    487  N   GLY A  61       2.604  20.126  69.328  1.00 70.92           N  
ANISOU  487  N   GLY A  61    12727   7142   7078   -445  -1416    114       N  
ATOM    488  CA  GLY A  61       3.049  20.015  70.725  1.00 68.78           C  
ANISOU  488  CA  GLY A  61    12035   7065   7035   -375  -1266    116       C  
ATOM    489  C   GLY A  61       2.535  21.048  71.738  1.00 67.99           C  
ANISOU  489  C   GLY A  61    11682   7072   7078   -280  -1413    135       C  
ATOM    490  O   GLY A  61       2.563  20.824  72.951  1.00 66.24           O  
ANISOU  490  O   GLY A  61    11109   7011   7049   -223  -1355    136       O  
ATOM    491  N   CYS A  62       2.068  22.185  71.237  1.00 68.47           N  
ANISOU  491  N   CYS A  62    11960   7027   7027   -254  -1610    147       N  
ATOM    492  CA  CYS A  62       1.525  23.230  72.045  1.00 67.31           C  
ANISOU  492  CA  CYS A  62    11648   6946   6980   -133  -1771    152       C  
ATOM    493  C   CYS A  62       0.283  22.846  72.793  1.00 66.38           C  
ANISOU  493  C   CYS A  62    11189   6987   7046    -17  -1979    120       C  
ATOM    494  O   CYS A  62      -0.057  23.532  73.753  1.00 65.16           O  
ANISOU  494  O   CYS A  62    10804   6938   7016     97  -2042    110       O  
ATOM    495  CB  CYS A  62       1.233  24.439  71.167  1.00 70.63           C  
ANISOU  495  CB  CYS A  62    12465   7171   7200   -110  -1978    163       C  
ATOM    496  SG  CYS A  62       2.737  25.186  70.541  1.00 75.61           S  
ANISOU  496  SG  CYS A  62    13479   7646   7602   -298  -1702    197       S  
ATOM    497  N   GLU A  63      -0.384  21.748  72.403  1.00 67.23           N  
ANISOU  497  N   GLU A  63    11260   7123   7162    -63  -2070     98       N  
ATOM    498  CA  GLU A  63      -1.500  21.181  73.230  1.00 68.42           C  
ANISOU  498  CA  GLU A  63    11031   7476   7491    -18  -2211     57       C  
ATOM    499  C   GLU A  63      -1.140  20.076  74.235  1.00 67.32           C  
ANISOU  499  C   GLU A  63    10616   7473   7491    -96  -1995     59       C  
ATOM    500  O   GLU A  63      -2.016  19.652  74.992  1.00 69.17           O  
ANISOU  500  O   GLU A  63    10552   7877   7852   -100  -2082     24       O  
ATOM    501  CB  GLU A  63      -2.643  20.652  72.386  1.00 70.40           C  
ANISOU  501  CB  GLU A  63    11356   7716   7677    -52  -2483     22       C  
ATOM    502  CG  GLU A  63      -2.425  19.195  71.907  1.00 73.06           C  
ANISOU  502  CG  GLU A  63    11811   8002   7946   -226  -2374     32       C  
ATOM    503  CD  GLU A  63      -1.191  18.996  71.000  1.00 73.76           C  
ANISOU  503  CD  GLU A  63    12294   7876   7856   -300  -2156     69       C  
ATOM    504  OE1 GLU A  63      -1.144  17.945  70.361  1.00 78.63           O  
ANISOU  504  OE1 GLU A  63    13095   8408   8374   -410  -2122     66       O  
ATOM    505  OE2 GLU A  63      -0.266  19.842  70.924  1.00 72.27           O  
ANISOU  505  OE2 GLU A  63    12235   7611   7614   -264  -2006     93       O  
ATOM    506  N   LYS A  64       0.100  19.576  74.238  1.00 66.17           N  
ANISOU  506  N   LYS A  64    10571   7259   7312   -159  -1727     90       N  
ATOM    507  CA  LYS A  64       0.498  18.486  75.185  1.00 64.27           C  
ANISOU  507  CA  LYS A  64    10121   7113   7185   -204  -1551     92       C  
ATOM    508  C   LYS A  64       0.487  19.072  76.555  1.00 62.78           C  
ANISOU  508  C   LYS A  64     9618   7076   7161   -135  -1513     94       C  
ATOM    509  O   LYS A  64       0.748  20.273  76.653  1.00 63.22           O  
ANISOU  509  O   LYS A  64     9686   7119   7214    -59  -1520    106       O  
ATOM    510  CB  LYS A  64       1.897  18.006  74.887  1.00 63.08           C  
ANISOU  510  CB  LYS A  64    10130   6868   6970   -225  -1290    107       C  
ATOM    511  CG  LYS A  64       1.919  17.034  73.686  1.00 65.93           C  
ANISOU  511  CG  LYS A  64    10801   7080   7168   -300  -1286     92       C  
ATOM    512  CD  LYS A  64       3.330  16.776  73.158  1.00 67.10           C  
ANISOU  512  CD  LYS A  64    11131   7140   7225   -291  -1016     82       C  
ATOM    513  CE  LYS A  64       3.316  15.729  72.032  1.00 65.20           C  
ANISOU  513  CE  LYS A  64    11216   6742   6814   -349  -1000     56       C  
ATOM    514  NZ  LYS A  64       4.137  16.298  70.865  1.00 70.23           N  
ANISOU  514  NZ  LYS A  64    12151   7262   7271   -378   -855     40       N  
ATOM    515  N   SER A  65       0.196  18.265  77.593  1.00 61.45           N  
ANISOU  515  N   SER A  65     9215   7028   7107   -177  -1475     84       N  
ATOM    516  CA ASER A  65       0.165  18.745  78.977  0.50 59.90           C  
ANISOU  516  CA ASER A  65     8735   6972   7054   -128  -1428     83       C  
ATOM    517  CA BSER A  65       0.158  18.758  78.972  0.50 58.67           C  
ANISOU  517  CA BSER A  65     8579   6816   6897   -127  -1430     83       C  
ATOM    518  C   SER A  65       1.499  19.324  79.413  1.00 58.36           C  
ANISOU  518  C   SER A  65     8552   6741   6882    -75  -1242    123       C  
ATOM    519  O   SER A  65       2.564  19.037  78.843  1.00 56.95           O  
ANISOU  519  O   SER A  65     8538   6468   6634    -89  -1101    142       O  
ATOM    520  CB ASER A  65      -0.198  17.601  79.930  0.50 59.83           C  
ANISOU  520  CB ASER A  65     8558   7058   7116   -227  -1388     71       C  
ATOM    521  CB BSER A  65      -0.301  17.653  79.949  0.50 58.48           C  
ANISOU  521  CB BSER A  65     8373   6898   6950   -227  -1402     68       C  
ATOM    522  OG ASER A  65      -1.580  17.605  80.252  0.50 62.97           O  
ANISOU  522  OG ASER A  65     8756   7607   7560   -277  -1543     18       O  
ATOM    523  OG BSER A  65       0.744  16.789  80.392  0.50 52.34           O  
ANISOU  523  OG BSER A  65     7656   6056   6176   -253  -1227    100       O  
ATOM    524  N   LEU A  66       1.464  20.100  80.472  1.00 59.31           N  
ANISOU  524  N   LEU A  66     8483   6955   7097    -21  -1232    125       N  
ATOM    525  CA  LEU A  66       2.704  20.533  81.066  1.00 60.18           C  
ANISOU  525  CA  LEU A  66     8569   7058   7239     -4  -1068    163       C  
ATOM    526  C   LEU A  66       3.629  19.406  81.589  1.00 58.77           C  
ANISOU  526  C   LEU A  66     8340   6887   7105    -38   -911    179       C  
ATOM    527  O   LEU A  66       4.835  19.616  81.642  1.00 59.39           O  
ANISOU  527  O   LEU A  66     8431   6951   7181    -24   -774    198       O  
ATOM    528  CB  LEU A  66       2.426  21.617  82.116  1.00 60.96           C  
ANISOU  528  CB  LEU A  66     8511   7237   7413     56  -1106    162       C  
ATOM    529  CG  LEU A  66       2.185  23.005  81.444  1.00 67.19           C  
ANISOU  529  CG  LEU A  66     9464   7950   8115    128  -1219    157       C  
ATOM    530  CD1 LEU A  66       1.592  24.095  82.418  1.00 65.28           C  
ANISOU  530  CD1 LEU A  66     9099   7773   7931    231  -1302    134       C  
ATOM    531  CD2 LEU A  66       3.502  23.557  80.758  1.00 67.17           C  
ANISOU  531  CD2 LEU A  66     9687   7834   8001     67  -1092    199       C  
ATOM    532  N   HIS A  67       3.101  18.243  81.954  1.00 57.77           N  
ANISOU  532  N   HIS A  67     8167   6780   7004    -85   -939    166       N  
ATOM    533  CA  HIS A  67       3.955  17.136  82.474  1.00 59.36           C  
ANISOU  533  CA  HIS A  67     8376   6951   7228    -85   -827    178       C  
ATOM    534  C   HIS A  67       4.692  16.493  81.326  1.00 59.83           C  
ANISOU  534  C   HIS A  67     8641   6900   7193    -58   -748    165       C  
ATOM    535  O   HIS A  67       5.885  16.159  81.432  1.00 59.21           O  
ANISOU  535  O   HIS A  67     8565   6805   7127     14   -617    163       O  
ATOM    536  CB  HIS A  67       3.149  15.959  83.119  1.00 60.80           C  
ANISOU  536  CB  HIS A  67     8541   7143   7416   -176   -888    167       C  
ATOM    537  CG  HIS A  67       2.345  16.318  84.334  1.00 63.23           C  
ANISOU  537  CG  HIS A  67     8648   7575   7802   -233   -935    161       C  
ATOM    538  ND1 HIS A  67       0.988  16.042  84.431  1.00 63.00           N  
ANISOU  538  ND1 HIS A  67     8547   7629   7760   -350  -1036    122       N  
ATOM    539  CD2 HIS A  67       2.702  16.900  85.514  1.00 66.27           C  
ANISOU  539  CD2 HIS A  67     8887   8026   8267   -203   -886    179       C  
ATOM    540  CE1 HIS A  67       0.540  16.448  85.611  1.00 64.54           C  
ANISOU  540  CE1 HIS A  67     8553   7945   8026   -382  -1025    108       C  
ATOM    541  NE2 HIS A  67       1.552  16.982  86.287  1.00 68.27           N  
ANISOU  541  NE2 HIS A  67     8998   8393   8549   -292   -940    147       N  
ATOM    542  N   THR A  68       3.935  16.279  80.242  1.00 60.01           N  
ANISOU  542  N   THR A  68     8830   6854   7116   -109   -837    147       N  
ATOM    543  CA  THR A  68       4.444  15.601  79.087  1.00 60.09           C  
ANISOU  543  CA  THR A  68     9081   6742   7009    -97   -770    127       C  
ATOM    544  C   THR A  68       5.602  16.376  78.564  1.00 60.97           C  
ANISOU  544  C   THR A  68     9225   6851   7091    -42   -619    123       C  
ATOM    545  O   THR A  68       6.643  15.797  78.307  1.00 61.46           O  
ANISOU  545  O   THR A  68     9340   6885   7127     21   -466     95       O  
ATOM    546  CB  THR A  68       3.401  15.561  78.012  1.00 61.74           C  
ANISOU  546  CB  THR A  68     9467   6884   7109   -177   -916    115       C  
ATOM    547  OG1 THR A  68       2.173  15.078  78.563  1.00 61.59           O  
ANISOU  547  OG1 THR A  68     9348   6926   7127   -268  -1069    111       O  
ATOM    548  CG2 THR A  68       3.854  14.754  76.835  1.00 56.05           C  
ANISOU  548  CG2 THR A  68     9037   6015   6243   -180   -847     92       C  
ATOM    549  N   LEU A  69       5.418  17.687  78.382  1.00 61.19           N  
ANISOU  549  N   LEU A  69     9231   6909   7108    -67   -662    140       N  
ATOM    550  CA  LEU A  69       6.530  18.520  77.948  1.00 61.99           C  
ANISOU  550  CA  LEU A  69     9378   7017   7158    -72   -509    137       C  
ATOM    551  C   LEU A  69       7.647  18.585  78.978  1.00 61.65           C  
ANISOU  551  C   LEU A  69     9104   7091   7230    -27   -367    140       C  
ATOM    552  O   LEU A  69       8.803  18.388  78.601  1.00 62.14           O  
ANISOU  552  O   LEU A  69     9168   7181   7262    -10   -188    105       O  
ATOM    553  CB  LEU A  69       6.103  19.941  77.583  1.00 62.71           C  
ANISOU  553  CB  LEU A  69     9562   7081   7183   -120   -605    159       C  
ATOM    554  CG  LEU A  69       5.020  20.122  76.545  1.00 63.05           C  
ANISOU  554  CG  LEU A  69     9839   7010   7106   -145   -789    155       C  
ATOM    555  CD1 LEU A  69       4.376  21.502  76.774  1.00 64.09           C  
ANISOU  555  CD1 LEU A  69     9978   7140   7235   -121   -952    175       C  
ATOM    556  CD2 LEU A  69       5.617  19.944  75.155  1.00 63.60           C  
ANISOU  556  CD2 LEU A  69    10212   6958   6994   -211   -679    134       C  
ATOM    557  N   PHE A  70       7.339  18.886  80.250  1.00 60.15           N  
ANISOU  557  N   PHE A  70     8712   6980   7164    -10   -443    171       N  
ATOM    558  CA  PHE A  70       8.410  18.789  81.282  1.00 60.78           C  
ANISOU  558  CA  PHE A  70     8583   7161   7350     35   -339    175       C  
ATOM    559  C   PHE A  70       9.083  17.413  81.174  1.00 61.01           C  
ANISOU  559  C   PHE A  70     8621   7171   7390    130   -253    134       C  
ATOM    560  O   PHE A  70      10.296  17.322  80.959  1.00 61.95           O  
ANISOU  560  O   PHE A  70     8675   7352   7511    182   -103     94       O  
ATOM    561  CB  PHE A  70       7.892  18.930  82.715  1.00 59.69           C  
ANISOU  561  CB  PHE A  70     8274   7080   7327     42   -440    210       C  
ATOM    562  CG  PHE A  70       7.915  20.318  83.232  1.00 64.52           C  
ANISOU  562  CG  PHE A  70     8814   7744   7957     -4   -462    240       C  
ATOM    563  CD1 PHE A  70       9.082  20.864  83.749  1.00 64.86           C  
ANISOU  563  CD1 PHE A  70     8742   7866   8036    -26   -365    252       C  
ATOM    564  CD2 PHE A  70       6.745  21.103  83.235  1.00 68.62           C  
ANISOU  564  CD2 PHE A  70     9383   8236   8453    -20   -595    249       C  
ATOM    565  CE1 PHE A  70       9.082  22.175  84.254  1.00 66.03           C  
ANISOU  565  CE1 PHE A  70     8875   8038   8176    -90   -396    283       C  
ATOM    566  CE2 PHE A  70       6.755  22.428  83.717  1.00 67.24           C  
ANISOU  566  CE2 PHE A  70     9195   8079   8275    -39   -626    270       C  
ATOM    567  CZ  PHE A  70       7.910  22.957  84.227  1.00 67.89           C  
ANISOU  567  CZ  PHE A  70     9210   8211   8372    -88   -525    293       C  
ATOM    568  N   GLY A  71       8.277  16.362  81.315  1.00 59.38           N  
ANISOU  568  N   GLY A  71     8501   6883   7177    151   -353    134       N  
ATOM    569  CA  GLY A  71       8.758  15.000  81.208  1.00 61.02           C  
ANISOU  569  CA  GLY A  71     8798   7022   7365    255   -309     96       C  
ATOM    570  C   GLY A  71       9.539  14.635  79.977  1.00 62.52           C  
ANISOU  570  C   GLY A  71     9129   7169   7458    321   -164     33       C  
ATOM    571  O   GLY A  71      10.521  13.932  80.071  1.00 64.44           O  
ANISOU  571  O   GLY A  71     9336   7427   7722    465    -67    -19       O  
ATOM    572  N   ASP A  72       9.125  15.095  78.808  1.00 63.41           N  
ANISOU  572  N   ASP A  72     9413   7226   7454    228   -149     27       N  
ATOM    573  CA  ASP A  72       9.899  14.813  77.569  1.00 65.46           C  
ANISOU  573  CA  ASP A  72     9835   7444   7593    267     22    -42       C  
ATOM    574  C   ASP A  72      11.321  15.256  77.661  1.00 65.69           C  
ANISOU  574  C   ASP A  72     9665   7627   7669    326    225    -94       C  
ATOM    575  O   ASP A  72      12.221  14.539  77.248  1.00 66.26           O  
ANISOU  575  O   ASP A  72     9744   7718   7713    454    377   -178       O  
ATOM    576  CB  ASP A  72       9.248  15.483  76.374  1.00 65.67           C  
ANISOU  576  CB  ASP A  72    10094   7385   7472    127     -9    -30       C  
ATOM    577  CG  ASP A  72       7.904  14.823  76.008  1.00 68.87           C  
ANISOU  577  CG  ASP A  72    10713   7647   7807     73   -205     -4       C  
ATOM    578  OD1 ASP A  72       7.537  13.732  76.570  1.00 72.65           O  
ANISOU  578  OD1 ASP A  72    11201   8080   8324    120   -284     -3       O  
ATOM    579  OD2 ASP A  72       7.217  15.368  75.131  1.00 72.49           O  
ANISOU  579  OD2 ASP A  72    11354   8034   8156    -30   -292     11       O  
ATOM    580  N   GLU A  73      11.506  16.430  78.265  1.00 65.14           N  
ANISOU  580  N   GLU A  73     9404   7676   7669    234    219    -51       N  
ATOM    581  CA  GLU A  73      12.814  17.023  78.418  1.00 66.99           C  
ANISOU  581  CA  GLU A  73     9421   8089   7944    226    397    -95       C  
ATOM    582  C   GLU A  73      13.670  16.323  79.474  1.00 66.94           C  
ANISOU  582  C   GLU A  73     9147   8199   8089    405    410   -130       C  
ATOM    583  O   GLU A  73      14.888  16.240  79.321  1.00 67.76           O  
ANISOU  583  O   GLU A  73     9074   8454   8216    477    581   -214       O  
ATOM    584  CB  GLU A  73      12.705  18.538  78.682  1.00 67.26           C  
ANISOU  584  CB  GLU A  73     9402   8183   7969     42    368    -33       C  
ATOM    585  CG  GLU A  73      12.071  19.405  77.511  1.00 72.41           C  
ANISOU  585  CG  GLU A  73    10360   8714   8440   -127    356    -10       C  
ATOM    586  CD  GLU A  73      12.487  18.982  76.064  1.00 79.38           C  
ANISOU  586  CD  GLU A  73    11467   9540   9153   -157    532    -86       C  
ATOM    587  OE1 GLU A  73      13.701  18.750  75.818  1.00 83.47           O  
ANISOU  587  OE1 GLU A  73    11852  10196   9665   -139    763   -171       O  
ATOM    588  OE2 GLU A  73      11.597  18.894  75.170  1.00 81.39           O  
ANISOU  588  OE2 GLU A  73    12025   9622   9277   -200    438    -69       O  
ATOM    589  N   LEU A  74      13.049  15.793  80.535  1.00 65.86           N  
ANISOU  589  N   LEU A  74     8982   7997   8045    478    228    -75       N  
ATOM    590  CA  LEU A  74      13.849  15.059  81.528  1.00 66.72           C  
ANISOU  590  CA  LEU A  74     8898   8177   8274    664    205   -106       C  
ATOM    591  C   LEU A  74      14.386  13.787  80.867  1.00 69.15           C  
ANISOU  591  C   LEU A  74     9317   8426   8533    876    288   -205       C  
ATOM    592  O   LEU A  74      15.508  13.349  81.123  1.00 71.09           O  
ANISOU  592  O   LEU A  74     9377   8786   8847   1068    359   -287       O  
ATOM    593  CB  LEU A  74      13.076  14.740  82.806  1.00 64.86           C  
ANISOU  593  CB  LEU A  74     8668   7862   8113    670     -1    -28       C  
ATOM    594  CG  LEU A  74      12.477  15.806  83.783  1.00 63.25           C  
ANISOU  594  CG  LEU A  74     8358   7704   7970    512   -106     61       C  
ATOM    595  CD1 LEU A  74      11.804  15.187  84.996  1.00 57.22           C  
ANISOU  595  CD1 LEU A  74     7628   6858   7255    533   -271    112       C  
ATOM    596  CD2 LEU A  74      13.498  16.776  84.301  1.00 64.14           C  
ANISOU  596  CD2 LEU A  74     8217   7995   8157    475    -41     61       C  
ATOM    597  N   CYS A  75      13.599  13.206  79.982  1.00 69.40           N  
ANISOU  597  N   CYS A  75     9652   8279   8437    852    272   -208       N  
ATOM    598  CA  CYS A  75      13.996  11.954  79.379  1.00 72.16           C  
ANISOU  598  CA  CYS A  75    10175   8529   8716   1057    335   -299       C  
ATOM    599  C   CYS A  75      15.190  12.076  78.458  1.00 75.05           C  
ANISOU  599  C   CYS A  75    10436   9037   9045   1149    588   -424       C  
ATOM    600  O   CYS A  75      15.948  11.124  78.311  1.00 76.47           O  
ANISOU  600  O   CYS A  75    10617   9216   9222   1405    660   -531       O  
ATOM    601  CB  CYS A  75      12.800  11.306  78.702  1.00 71.31           C  
ANISOU  601  CB  CYS A  75    10442   8187   8464    972    237   -264       C  
ATOM    602  SG  CYS A  75      11.809  10.615  80.027  1.00 73.53           S  
ANISOU  602  SG  CYS A  75    10801   8338   8797    947    -24   -173       S  
ATOM    603  N   LYS A  76      15.388  13.264  77.882  1.00 75.89           N  
ANISOU  603  N   LYS A  76    10451   9271   9112    944    727   -420       N  
ATOM    604  CA  LYS A  76      16.525  13.476  76.977  1.00 79.05           C  
ANISOU  604  CA  LYS A  76    10744   9837   9454    967   1006   -548       C  
ATOM    605  C   LYS A  76      17.863  13.780  77.704  1.00 80.50           C  
ANISOU  605  C   LYS A  76    10481  10315   9789   1067   1108   -624       C  
ATOM    606  O   LYS A  76      18.864  14.068  77.057  1.00 82.67           O  
ANISOU  606  O   LYS A  76    10590  10792  10029   1050   1357   -742       O  
ATOM    607  CB  LYS A  76      16.198  14.580  75.965  1.00 78.58           C  
ANISOU  607  CB  LYS A  76    10844   9769   9245    670   1117   -517       C  
ATOM    608  CG  LYS A  76      14.823  14.490  75.364  1.00 77.67           C  
ANISOU  608  CG  LYS A  76    11119   9392   8999    553    962   -430       C  
ATOM    609  CD  LYS A  76      14.811  14.766  73.852  1.00 81.52           C  
ANISOU  609  CD  LYS A  76    11900   9804   9268    408   1130   -478       C  
ATOM    610  CE  LYS A  76      15.377  16.167  73.421  1.00 84.04           C  
ANISOU  610  CE  LYS A  76    12152  10270   9509    155   1299   -484       C  
ATOM    611  NZ  LYS A  76      15.005  17.317  74.326  1.00 83.00           N  
ANISOU  611  NZ  LYS A  76    11875  10190   9470      6   1139   -370       N  
ATOM    612  N   VAL A  77      17.886  13.728  79.032  1.00 79.15           N  
ANISOU  612  N   VAL A  77    10115  10183   9775   1151    919   -564       N  
ATOM    613  CA  VAL A  77      19.113  14.077  79.774  1.00 80.86           C  
ANISOU  613  CA  VAL A  77     9901  10686  10137   1225    974   -628       C  
ATOM    614  C   VAL A  77      20.128  12.967  79.669  1.00 84.52           C  
ANISOU  614  C   VAL A  77    10217  11245  10652   1583   1054   -790       C  
ATOM    615  O   VAL A  77      19.900  11.864  80.182  1.00 85.71           O  
ANISOU  615  O   VAL A  77    10503  11226  10837   1848    878   -790       O  
ATOM    616  CB  VAL A  77      18.862  14.383  81.287  1.00 78.35           C  
ANISOU  616  CB  VAL A  77     9440  10369   9960   1205    729   -515       C  
ATOM    617  CG1 VAL A  77      20.178  14.711  81.991  1.00 79.95           C  
ANISOU  617  CG1 VAL A  77     9201  10873  10303   1278    767   -588       C  
ATOM    618  CG2 VAL A  77      17.900  15.527  81.458  1.00 74.20           C  
ANISOU  618  CG2 VAL A  77     9036   9765   9389    891    653   -375       C  
ATOM    619  N   ALA A  78      21.257  13.260  79.029  1.00 88.01           N  
ANISOU  619  N   ALA A  78    10388  11963  11090   1591   1316   -936       N  
ATOM    620  CA  ALA A  78      22.243  12.229  78.658  1.00 91.84           C  
ANISOU  620  CA  ALA A  78    10730  12565  11601   1958   1446  -1130       C  
ATOM    621  C   ALA A  78      22.621  11.352  79.835  1.00 92.89           C  
ANISOU  621  C   ALA A  78    10713  12688  11893   2322   1203  -1153       C  
ATOM    622  O   ALA A  78      22.998  10.186  79.664  1.00 95.89           O  
ANISOU  622  O   ALA A  78    11163  13001  12270   2703   1192  -1276       O  
ATOM    623  CB  ALA A  78      23.498  12.869  78.053  1.00 95.08           C  
ANISOU  623  CB  ALA A  78    10743  13366  12016   1870   1766  -1293       C  
ATOM    624  N   SER A  79      22.508  11.912  81.034  1.00 91.10           N  
ANISOU  624  N   SER A  79    10323  12504  11786   2212    996  -1034       N  
ATOM    625  CA  SER A  79      23.083  11.289  82.226  1.00 92.50           C  
ANISOU  625  CA  SER A  79    10300  12729  12118   2524    765  -1062       C  
ATOM    626  C   SER A  79      22.114  10.813  83.314  1.00 90.27           C  
ANISOU  626  C   SER A  79    10322  12132  11845   2555    436   -903       C  
ATOM    627  O   SER A  79      22.543  10.548  84.438  1.00 91.53           O  
ANISOU  627  O   SER A  79    10331  12326  12119   2731    222   -895       O  
ATOM    628  CB  SER A  79      24.027  12.257  82.917  1.00 92.87           C  
ANISOU  628  CB  SER A  79     9846  13134  12308   2401    777  -1083       C  
ATOM    629  OG  SER A  79      25.327  12.063  82.373  1.00 97.24           O  
ANISOU  629  OG  SER A  79    10006  14023  12916   2604    987  -1300       O  
ATOM    630  N   LEU A  80      20.837  10.667  82.965  1.00 88.15           N  
ANISOU  630  N   LEU A  80    10480  11567  11445   2382    396   -788       N  
ATOM    631  CA  LEU A  80      19.773  10.167  83.873  1.00 86.16           C  
ANISOU  631  CA  LEU A  80    10553  11017  11166   2355    124   -646       C  
ATOM    632  C   LEU A  80      20.123   8.803  84.554  1.00 88.44           C  
ANISOU  632  C   LEU A  80    10987  11145  11472   2746    -87   -701       C  
ATOM    633  O   LEU A  80      20.185   8.720  85.795  1.00 88.01           O  
ANISOU  633  O   LEU A  80    10892  11056  11491   2796   -313   -638       O  
ATOM    634  CB  LEU A  80      18.459  10.086  83.072  1.00 83.91           C  
ANISOU  634  CB  LEU A  80    10670  10489  10724   2135    160   -565       C  
ATOM    635  CG  LEU A  80      17.149  10.332  83.811  1.00 81.19           C  
ANISOU  635  CG  LEU A  80    10535   9962  10351   1885    -24   -400       C  
ATOM    636  CD1 LEU A  80      17.201  11.650  84.599  1.00 77.46           C  
ANISOU  636  CD1 LEU A  80     9776   9672   9984   1660    -46   -318       C  
ATOM    637  CD2 LEU A  80      16.011  10.340  82.809  1.00 77.40           C  
ANISOU  637  CD2 LEU A  80    10364   9317   9726   1682     35   -356       C  
ATOM    638  N   ARG A  81      20.361   7.750  83.764  1.00 90.58           N  
ANISOU  638  N   ARG A  81    11463  11297  11655   3027    -25   -820       N  
ATOM    639  CA AARG A  81      20.718   6.444  84.323  0.50 92.74           C  
ANISOU  639  CA AARG A  81    11937  11385  11916   3428   -235   -884       C  
ATOM    640  CA BARG A  81      20.720   6.451  84.316  0.50 92.57           C  
ANISOU  640  CA BARG A  81    11913  11365  11894   3427   -232   -884       C  
ATOM    641  C   ARG A  81      21.981   6.524  85.188  1.00 95.64           C  
ANISOU  641  C   ARG A  81    11881  11999  12457   3711   -341   -973       C  
ATOM    642  O   ARG A  81      21.901   6.420  86.423  1.00 95.15           O  
ANISOU  642  O   ARG A  81    11857  11851  12446   3733   -605   -887       O  
ATOM    643  CB AARG A  81      20.884   5.380  83.222  0.50 95.23           C  
ANISOU  643  CB AARG A  81    12536  11550  12098   3710   -122  -1022       C  
ATOM    644  CB BARG A  81      20.879   5.416  83.190  0.50 94.89           C  
ANISOU  644  CB BARG A  81    12485  11514  12055   3699   -112  -1022       C  
ATOM    645  CG AARG A  81      21.120   3.957  83.747  0.50 95.31           C  
ANISOU  645  CG AARG A  81    12877  11289  12048   4134   -366  -1083       C  
ATOM    646  CG BARG A  81      21.531   4.114  83.609  0.50 95.05           C  
ANISOU  646  CG BARG A  81    12675  11379  12061   4201   -301  -1136       C  
ATOM    647  CD AARG A  81      21.391   2.981  82.622  0.50 94.67           C  
ANISOU  647  CD AARG A  81    13065  11075  11831   4439   -234  -1239       C  
ATOM    648  CD BARG A  81      20.773   2.938  83.087  0.50 90.30           C  
ANISOU  648  CD BARG A  81    12695  10373  11240   4283   -365  -1130       C  
ATOM    649  NE AARG A  81      22.221   1.856  83.052  0.50 94.83           N  
ANISOU  649  NE AARG A  81    13188  10987  11855   4983   -417  -1376       N  
ATOM    650  NE BARG A  81      19.722   2.523  84.005  0.50 83.11           N  
ANISOU  650  NE BARG A  81    12201   9142  10235   4089   -637   -959       N  
ATOM    651  CZ AARG A  81      23.492   1.692  82.700  0.50 96.69           C  
ANISOU  651  CZ AARG A  81    13064  11482  12191   5404   -298  -1592       C  
ATOM    652  CZ BARG A  81      18.428   2.519  83.714  0.50 78.97           C  
ANISOU  652  CZ BARG A  81    12030   8407   9566   3713   -636   -829       C  
ATOM    653  NH1AARG A  81      24.077   2.576  81.910  0.50 95.20           N  
ANISOU  653  NH1AARG A  81    12398  11679  12093   5293     28  -1691       N  
ATOM    654  NH1BARG A  81      17.998   2.921  82.535  0.50 75.26           N  
ANISOU  654  NH1BARG A  81    11578   7988   9031   3503   -410   -837       N  
ATOM    655  NH2AARG A  81      24.174   0.644  83.137  0.50 99.55           N  
ANISOU  655  NH2AARG A  81    13553  11720  12551   5934   -508  -1718       N  
ATOM    656  NH2BARG A  81      17.557   2.106  84.614  0.50 79.82           N  
ANISOU  656  NH2BARG A  81    12479   8262   9587   3535   -869   -696       N  
ATOM    657  N   GLU A  82      23.139   6.715  84.550  1.00 99.24           N  
ANISOU  657  N   GLU A  82    11934  12774  12999   3911   -139  -1151       N  
ATOM    658  CA  GLU A  82      24.430   6.616  85.247  1.00103.48           C  
ANISOU  658  CA  GLU A  82    12040  13574  13704   4248   -249  -1278       C  
ATOM    659  C   GLU A  82      24.603   7.713  86.288  1.00102.24           C  
ANISOU  659  C   GLU A  82    11537  13626  13683   3979   -357  -1169       C  
ATOM    660  O   GLU A  82      25.640   7.791  86.951  1.00104.66           O  
ANISOU  660  O   GLU A  82    11450  14180  14136   4191   -472  -1255       O  
ATOM    661  CB  GLU A  82      25.601   6.613  84.261  1.00107.19           C  
ANISOU  661  CB  GLU A  82    12106  14390  14231   4488     33  -1515       C  
ATOM    662  CG  GLU A  82      25.775   7.919  83.479  1.00107.24           C  
ANISOU  662  CG  GLU A  82    11767  14727  14254   4075    373  -1523       C  
ATOM    663  CD  GLU A  82      26.750   7.774  82.318  1.00111.64           C  
ANISOU  663  CD  GLU A  82    12037  15576  14806   4270    706  -1765       C  
ATOM    664  OE1 GLU A  82      27.850   7.194  82.522  1.00116.16           O  
ANISOU  664  OE1 GLU A  82    12281  16364  15492   4711    667  -1960       O  
ATOM    665  OE2 GLU A  82      26.407   8.235  81.200  1.00109.31           O  
ANISOU  665  OE2 GLU A  82    11851  15296  14385   3988   1002  -1769       O  
ATOM    666  N   THR A  83      23.578   8.554  86.413  1.00 98.67           N  
ANISOU  666  N   THR A  83    11241  13075  13175   3522   -327   -987       N  
ATOM    667  CA  THR A  83      23.516   9.564  87.476  1.00 97.33           C  
ANISOU  667  CA  THR A  83    10868  13018  13095   3243   -452   -859       C  
ATOM    668  C   THR A  83      22.385   9.348  88.484  1.00 94.27           C  
ANISOU  668  C   THR A  83    10890  12292  12636   3096   -703   -676       C  
ATOM    669  O   THR A  83      22.573   9.661  89.660  1.00 93.78           O  
ANISOU  669  O   THR A  83    10724  12262  12648   3057   -905   -607       O  
ATOM    670  CB  THR A  83      23.469  11.016  86.906  1.00 95.88           C  
ANISOU  670  CB  THR A  83    10429  13082  12919   2816   -193   -821       C  
ATOM    671  OG1 THR A  83      24.677  11.265  86.157  1.00100.50           O  
ANISOU  671  OG1 THR A  83    10580  14034  13572   2917     38  -1002       O  
ATOM    672  CG2 THR A  83      23.352  12.041  88.034  1.00 93.49           C  
ANISOU  672  CG2 THR A  83     9983  12855  12685   2535   -335   -686       C  
ATOM    673  N   TYR A  84      21.238   8.806  88.025  1.00 92.69           N  
ANISOU  673  N   TYR A  84    11147  11784  12286   3003   -686   -607       N  
ATOM    674  CA  TYR A  84      19.999   8.642  88.854  1.00 89.42           C  
ANISOU  674  CA  TYR A  84    11122  11073  11780   2787   -870   -442       C  
ATOM    675  C   TYR A  84      19.401   7.211  88.935  1.00 89.91           C  
ANISOU  675  C   TYR A  84    11704  10765  11694   2963  -1031   -435       C  
ATOM    676  O   TYR A  84      18.282   7.039  89.453  1.00 87.75           O  
ANISOU  676  O   TYR A  84    11765  10260  11316   2730  -1136   -311       O  
ATOM    677  CB  TYR A  84      18.901   9.633  88.413  1.00 85.83           C  
ANISOU  677  CB  TYR A  84    10719  10620  11273   2360   -715   -332       C  
ATOM    678  CG  TYR A  84      19.262  11.100  88.575  1.00 84.75           C  
ANISOU  678  CG  TYR A  84    10198  10765  11237   2122   -609   -300       C  
ATOM    679  CD1 TYR A  84      18.907  11.818  89.723  1.00 83.32           C  
ANISOU  679  CD1 TYR A  84     9979  10584  11093   1915   -740   -184       C  
ATOM    680  CD2 TYR A  84      19.939  11.775  87.568  1.00 86.57           C  
ANISOU  680  CD2 TYR A  84    10145  11246  11501   2079   -370   -388       C  
ATOM    681  CE1 TYR A  84      19.251  13.184  89.867  1.00 83.99           C  
ANISOU  681  CE1 TYR A  84     9762  10904  11248   1688   -652   -155       C  
ATOM    682  CE2 TYR A  84      20.287  13.128  87.697  1.00 86.94           C  
ANISOU  682  CE2 TYR A  84     9893  11532  11609   1825   -277   -358       C  
ATOM    683  CZ  TYR A  84      19.958  13.832  88.837  1.00 84.10           C  
ANISOU  683  CZ  TYR A  84     9510  11159  11286   1638   -424   -241       C  
ATOM    684  OH  TYR A  84      20.315  15.170  88.901  1.00 80.01           O  
ANISOU  684  OH  TYR A  84     8745  10853  10801   1381   -332   -215       O  
ATOM    685  N   GLY A  85      20.136   6.213  88.419  1.00 92.44           N  
ANISOU  685  N   GLY A  85    12096  11035  11991   3359  -1042   -575       N  
ATOM    686  CA  GLY A  85      19.699   4.811  88.392  1.00 92.99           C  
ANISOU  686  CA  GLY A  85    12704  10734  11892   3556  -1194   -587       C  
ATOM    687  C   GLY A  85      18.265   4.586  87.947  1.00 90.64           C  
ANISOU  687  C   GLY A  85    12835  10184  11421   3223  -1145   -480       C  
ATOM    688  O   GLY A  85      17.836   5.162  86.941  1.00 88.77           O  
ANISOU  688  O   GLY A  85    12511  10048  11169   3011   -921   -478       O  
ATOM    689  N   ASP A  86      17.533   3.758  88.718  1.00 90.85           N  
ANISOU  689  N   ASP A  86    13327   9888  11303   3159  -1366   -396       N  
ATOM    690  CA  ASP A  86      16.123   3.324  88.462  1.00 88.72           C  
ANISOU  690  CA  ASP A  86    13508   9359  10841   2832  -1367   -301       C  
ATOM    691  C   ASP A  86      15.184   4.448  87.947  1.00 84.68           C  
ANISOU  691  C   ASP A  86    12789   9019  10366   2410  -1173   -222       C  
ATOM    692  O   ASP A  86      14.172   4.169  87.314  1.00 83.68           O  
ANISOU  692  O   ASP A  86    12932   8757  10106   2188  -1124   -187       O  
ATOM    693  CB  ASP A  86      15.518   2.551  89.680  1.00 88.65           C  
ANISOU  693  CB  ASP A  86    13945   9050  10689   2728  -1627   -208       C  
ATOM    694  CG  ASP A  86      14.906   3.492  90.783  1.00 88.69           C  
ANISOU  694  CG  ASP A  86    13771   9167  10759   2368  -1663    -81       C  
ATOM    695  OD1 ASP A  86      15.603   3.754  91.787  1.00 87.82           O  
ANISOU  695  OD1 ASP A  86    13498   9126  10744   2495  -1797    -70       O  
ATOM    696  OD2 ASP A  86      13.724   3.975  90.658  1.00 87.62           O  
ANISOU  696  OD2 ASP A  86    13658   9056  10577   1967  -1563      1       O  
ATOM    697  N   MET A  87      15.555   5.701  88.183  1.00 82.39           N  
ANISOU  697  N   MET A  87    12036   9022  10248   2317  -1080   -203       N  
ATOM    698  CA  MET A  87      14.801   6.852  87.643  1.00 79.91           C  
ANISOU  698  CA  MET A  87    11524   8870   9968   1979   -910   -144       C  
ATOM    699  C   MET A  87      14.578   6.877  86.091  1.00 79.11           C  
ANISOU  699  C   MET A  87    11474   8784   9800   1949   -716   -202       C  
ATOM    700  O   MET A  87      13.514   7.295  85.612  1.00 76.80           O  
ANISOU  700  O   MET A  87    11261   8471   9447   1662   -662   -141       O  
ATOM    701  CB  MET A  87      15.418   8.159  88.170  1.00 78.80           C  
ANISOU  701  CB  MET A  87    10924   9015  10001   1920   -858   -125       C  
ATOM    702  CG  MET A  87      14.811   9.468  87.603  1.00 79.75           C  
ANISOU  702  CG  MET A  87    10846   9301  10154   1618   -693    -76       C  
ATOM    703  SD  MET A  87      15.140  10.928  88.651  1.00 77.70           S  
ANISOU  703  SD  MET A  87    10212   9272  10038   1458   -708    -10       S  
ATOM    704  CE  MET A  87      13.913  12.074  88.002  1.00 75.83           C  
ANISOU  704  CE  MET A  87     9975   9077   9760   1118   -587     58       C  
ATOM    705  N   ALA A  88      15.564   6.411  85.325  1.00 81.12           N  
ANISOU  705  N   ALA A  88    11693   9073  10057   2251   -621   -327       N  
ATOM    706  CA  ALA A  88      15.552   6.464  83.852  1.00 80.77           C  
ANISOU  706  CA  ALA A  88    11693   9056   9941   2244   -415   -399       C  
ATOM    707  C   ALA A  88      14.656   5.385  83.190  1.00 81.42           C  
ANISOU  707  C   ALA A  88    12283   8834   9820   2200   -464   -392       C  
ATOM    708  O   ALA A  88      14.547   5.317  81.970  1.00 81.85           O  
ANISOU  708  O   ALA A  88    12452   8864   9783   2181   -318   -445       O  
ATOM    709  CB  ALA A  88      16.967   6.354  83.349  1.00 84.19           C  
ANISOU  709  CB  ALA A  88    11882   9662  10445   2582   -274   -554       C  
ATOM    710  N   ASP A  89      14.048   4.530  84.017  1.00 80.82           N  
ANISOU  710  N   ASP A  89    12535   8519   9655   2164   -673   -329       N  
ATOM    711  CA  ASP A  89      12.973   3.636  83.615  1.00 79.94           C  
ANISOU  711  CA  ASP A  89    12907   8129   9338   1997   -751   -291       C  
ATOM    712  C   ASP A  89      11.604   4.331  83.713  1.00 76.86           C  
ANISOU  712  C   ASP A  89    12484   7785   8933   1556   -768   -175       C  
ATOM    713  O   ASP A  89      10.609   3.799  83.219  1.00 76.47           O  
ANISOU  713  O   ASP A  89    12757   7572   8726   1349   -810   -145       O  
ATOM    714  CB  ASP A  89      12.981   2.412  84.524  1.00 81.79           C  
ANISOU  714  CB  ASP A  89    13532   8087   9460   2129   -971   -281       C  
ATOM    715  CG  ASP A  89      14.353   1.792  84.645  1.00 86.24           C  
ANISOU  715  CG  ASP A  89    14085   8620  10063   2618  -1005   -401       C  
ATOM    716  OD1 ASP A  89      15.059   1.621  83.625  1.00 87.94           O  
ANISOU  716  OD1 ASP A  89    14255   8883  10274   2873   -855   -523       O  
ATOM    717  OD2 ASP A  89      14.747   1.467  85.775  1.00 92.24           O  
ANISOU  717  OD2 ASP A  89    14880   9313  10854   2762  -1186   -385       O  
ATOM    718  N   CYS A  90      11.545   5.491  84.382  1.00 73.89           N  
ANISOU  718  N   CYS A  90    11727   7633   8713   1420   -748   -116       N  
ATOM    719  CA  CYS A  90      10.369   6.349  84.312  1.00 71.31           C  
ANISOU  719  CA  CYS A  90    11293   7404   8399   1069   -734    -37       C  
ATOM    720  C   CYS A  90      10.134   6.761  82.866  1.00 70.63           C  
ANISOU  720  C   CYS A  90    11205   7363   8266   1006   -601    -70       C  
ATOM    721  O   CYS A  90       9.002   6.930  82.441  1.00 69.01           O  
ANISOU  721  O   CYS A  90    11095   7136   7992    754   -635    -28       O  
ATOM    722  CB  CYS A  90      10.540   7.612  85.141  1.00 69.18           C  
ANISOU  722  CB  CYS A  90    10624   7362   8298    997   -712     10       C  
ATOM    723  SG  CYS A  90      10.723   7.449  86.942  1.00 72.67           S  
ANISOU  723  SG  CYS A  90    11032   7781   8799   1008   -868     65       S  
ATOM    724  N   CYS A  91      11.226   6.890  82.117  1.00 71.47           N  
ANISOU  724  N   CYS A  91    11210   7541   8404   1237   -455   -156       N  
ATOM    725  CA  CYS A  91      11.176   7.243  80.727  1.00 71.74           C  
ANISOU  725  CA  CYS A  91    11286   7603   8370   1191   -312   -198       C  
ATOM    726  C   CYS A  91      10.544   6.183  79.835  1.00 72.74           C  
ANISOU  726  C   CYS A  91    11853   7488   8298   1152   -350   -220       C  
ATOM    727  O   CYS A  91      10.390   6.426  78.639  1.00 73.30           O  
ANISOU  727  O   CYS A  91    12016   7550   8282   1088   -250   -249       O  
ATOM    728  CB  CYS A  91      12.584   7.591  80.223  1.00 73.47           C  
ANISOU  728  CB  CYS A  91    11279   7979   8657   1431   -116   -302       C  
ATOM    729  SG  CYS A  91      13.158   9.204  80.878  1.00 76.18           S  
ANISOU  729  SG  CYS A  91    11113   8636   9196   1345    -40   -267       S  
ATOM    730  N   GLU A  92      10.193   5.025  80.400  1.00 73.05           N  
ANISOU  730  N   GLU A  92    12199   7316   8241   1171   -500   -204       N  
ATOM    731  CA  GLU A  92       9.618   3.905  79.649  1.00 74.55           C  
ANISOU  731  CA  GLU A  92    12866   7246   8215   1119   -559   -223       C  
ATOM    732  C   GLU A  92       8.133   3.893  79.823  1.00 72.33           C  
ANISOU  732  C   GLU A  92    12707   6918   7858    739   -701   -132       C  
ATOM    733  O   GLU A  92       7.438   3.085  79.207  1.00 73.55           O  
ANISOU  733  O   GLU A  92    13239   6881   7826    599   -772   -131       O  
ATOM    734  CB  GLU A  92      10.097   2.533  80.164  1.00 77.32           C  
ANISOU  734  CB  GLU A  92    13568   7351   8461   1350   -660   -266       C  
ATOM    735  CG  GLU A  92      11.573   2.342  80.378  1.00 81.99           C  
ANISOU  735  CG  GLU A  92    14018   7990   9144   1781   -582   -368       C  
ATOM    736  CD  GLU A  92      12.389   2.671  79.153  1.00 87.32           C  
ANISOU  736  CD  GLU A  92    14571   8777   9828   1970   -354   -479       C  
ATOM    737  OE1 GLU A  92      13.057   1.747  78.609  1.00 89.51           O  
ANISOU  737  OE1 GLU A  92    15109   8903   9997   2271   -305   -593       O  
ATOM    738  OE2 GLU A  92      12.379   3.869  78.753  1.00 87.73           O  
ANISOU  738  OE2 GLU A  92    14282   9066   9984   1820   -220   -461       O  
ATOM    739  N   LYS A  93       7.652   4.781  80.673  1.00 69.15           N  
ANISOU  739  N   LYS A  93    11979   6701   7595    570   -743    -64       N  
ATOM    740  CA  LYS A  93       6.252   4.829  81.019  1.00 67.30           C  
ANISOU  740  CA  LYS A  93    11773   6484   7316    221   -868      4       C  
ATOM    741  C   LYS A  93       5.513   5.923  80.235  1.00 66.14           C  
ANISOU  741  C   LYS A  93    11409   6505   7215     48   -843     21       C  
ATOM    742  O   LYS A  93       6.112   6.855  79.679  1.00 63.62           O  
ANISOU  742  O   LYS A  93    10882   6308   6984    172   -728      0       O  
ATOM    743  CB  LYS A  93       6.110   5.101  82.521  1.00 67.05           C  
ANISOU  743  CB  LYS A  93    11536   6547   7391    150   -929     55       C  
ATOM    744  CG  LYS A  93       6.818   4.096  83.483  1.00 66.89           C  
ANISOU  744  CG  LYS A  93    11744   6350   7323    319   -997     49       C  
ATOM    745  CD  LYS A  93       6.796   4.639  84.928  1.00 65.26           C  
ANISOU  745  CD  LYS A  93    11289   6268   7239    255  -1038    100       C  
ATOM    746  CE  LYS A  93       7.157   3.535  85.955  1.00 65.10           C  
ANISOU  746  CE  LYS A  93    11594   6027   7115    332  -1162    109       C  
ATOM    747  NZ  LYS A  93       6.220   2.388  85.720  1.00 66.87           N  
ANISOU  747  NZ  LYS A  93    12284   6024   7101     85  -1256    120       N  
ATOM    748  N   GLN A  94       4.196   5.791  80.218  1.00 66.12           N  
ANISOU  748  N   GLN A  94    11467   6513   7142   -249   -964     53       N  
ATOM    749  CA  GLN A  94       3.311   6.807  79.684  1.00 65.54           C  
ANISOU  749  CA  GLN A  94    11174   6609   7120   -410  -1000     67       C  
ATOM    750  C   GLN A  94       2.866   7.786  80.771  1.00 64.52           C  
ANISOU  750  C   GLN A  94    10656   6702   7156   -488  -1020     98       C  
ATOM    751  O   GLN A  94       3.019   7.524  81.985  1.00 63.04           O  
ANISOU  751  O   GLN A  94    10410   6527   7015   -496  -1021    118       O  
ATOM    752  CB  GLN A  94       2.052   6.186  79.097  1.00 66.45           C  
ANISOU  752  CB  GLN A  94    11505   6662   7082   -690  -1140     69       C  
ATOM    753  CG  GLN A  94       2.230   5.140  78.050  1.00 69.70           C  
ANISOU  753  CG  GLN A  94    12362   6830   7292   -679  -1153     42       C  
ATOM    754  CD  GLN A  94       0.924   4.403  77.891  1.00 75.53           C  
ANISOU  754  CD  GLN A  94    13299   7522   7878  -1022  -1317     53       C  
ATOM    755  OE1 GLN A  94      -0.122   4.910  78.361  1.00 73.91           O  
ANISOU  755  OE1 GLN A  94    12812   7523   7747  -1245  -1406     67       O  
ATOM    756  NE2 GLN A  94       0.955   3.205  77.250  1.00 71.37           N  
ANISOU  756  NE2 GLN A  94    13251   6736   7132  -1074  -1357     37       N  
ATOM    757  N   GLU A  95       2.296   8.907  80.301  1.00 63.87           N  
ANISOU  757  N   GLU A  95    10348   6776   7143   -538  -1047     99       N  
ATOM    758  CA  GLU A  95       1.675   9.874  81.184  1.00 64.00           C  
ANISOU  758  CA  GLU A  95    10021   7002   7296   -610  -1080    113       C  
ATOM    759  C   GLU A  95       0.360   9.292  81.701  1.00 64.54           C  
ANISOU  759  C   GLU A  95    10078   7134   7311   -886  -1193    105       C  
ATOM    760  O   GLU A  95      -0.299   8.610  80.937  1.00 66.17           O  
ANISOU  760  O   GLU A  95    10482   7271   7389  -1039  -1282     90       O  
ATOM    761  CB  GLU A  95       1.517  11.212  80.454  1.00 63.52           C  
ANISOU  761  CB  GLU A  95     9785   7051   7298   -543  -1092    106       C  
ATOM    762  CG  GLU A  95       2.823  12.042  80.421  1.00 64.41           C  
ANISOU  762  CG  GLU A  95     9816   7169   7488   -330   -952    116       C  
ATOM    763  CD  GLU A  95       3.478  12.164  81.813  1.00 72.09           C  
ANISOU  763  CD  GLU A  95    10607   8206   8576   -258   -880    137       C  
ATOM    764  OE1 GLU A  95       4.556  12.814  81.931  1.00 73.88           O  
ANISOU  764  OE1 GLU A  95    10733   8465   8872   -112   -774    142       O  
ATOM    765  OE2 GLU A  95       2.912  11.606  82.809  1.00 71.82           O  
ANISOU  765  OE2 GLU A  95    10542   8194   8551   -371   -933    146       O  
ATOM    766  N   PRO A  96      -0.004   9.502  83.000  1.00 64.28           N  
ANISOU  766  N   PRO A  96     9833   7233   7357   -974  -1181    110       N  
ATOM    767  CA  PRO A  96       0.655  10.212  84.141  1.00 62.03           C  
ANISOU  767  CA  PRO A  96     9336   7026   7205   -843  -1094    131       C  
ATOM    768  C   PRO A  96       1.591   9.343  85.024  1.00 61.33           C  
ANISOU  768  C   PRO A  96     9437   6784   7082   -779  -1044    160       C  
ATOM    769  O   PRO A  96       2.170   9.866  85.968  1.00 59.17           O  
ANISOU  769  O   PRO A  96     9012   6564   6906   -681   -993    179       O  
ATOM    770  CB  PRO A  96      -0.538  10.649  85.006  1.00 62.30           C  
ANISOU  770  CB  PRO A  96     9109   7272   7291  -1036  -1128    104       C  
ATOM    771  CG  PRO A  96      -1.509   9.521  84.894  1.00 64.12           C  
ANISOU  771  CG  PRO A  96     9503   7480   7380  -1322  -1201     81       C  
ATOM    772  CD  PRO A  96      -1.317   8.951  83.429  1.00 65.41           C  
ANISOU  772  CD  PRO A  96     9945   7474   7432  -1283  -1263     84       C  
ATOM    773  N   GLU A  97       1.700   8.043  84.736  1.00 62.55           N  
ANISOU  773  N   GLU A  97     9940   6739   7085   -834  -1081    160       N  
ATOM    774  CA  GLU A  97       2.612   7.145  85.435  1.00 63.62           C  
ANISOU  774  CA  GLU A  97    10318   6689   7164   -724  -1073    178       C  
ATOM    775  C   GLU A  97       4.073   7.601  85.375  1.00 62.68           C  
ANISOU  775  C   GLU A  97    10107   6552   7157   -386   -995    178       C  
ATOM    776  O   GLU A  97       4.822   7.486  86.341  1.00 61.59           O  
ANISOU  776  O   GLU A  97     9959   6379   7063   -267   -993    194       O  
ATOM    777  CB  GLU A  97       2.525   5.739  84.871  1.00 66.33           C  
ANISOU  777  CB  GLU A  97    11105   6791   7307   -793  -1136    168       C  
ATOM    778  CG  GLU A  97       1.207   5.010  85.166  1.00 70.87           C  
ANISOU  778  CG  GLU A  97    11842   7357   7731  -1182  -1219    170       C  
ATOM    779  CD  GLU A  97       0.180   5.095  83.989  1.00 77.13           C  
ANISOU  779  CD  GLU A  97    12609   8231   8467  -1371  -1272    143       C  
ATOM    780  OE1 GLU A  97      -0.894   4.423  84.116  1.00 81.16           O  
ANISOU  780  OE1 GLU A  97    13248   8750   8839  -1718  -1345    134       O  
ATOM    781  OE2 GLU A  97       0.448   5.783  82.959  1.00 72.08           O  
ANISOU  781  OE2 GLU A  97    11847   7639   7901  -1199  -1249    129       O  
ATOM    782  N   ARG A  98       4.476   8.168  84.249  1.00 62.36           N  
ANISOU  782  N   ARG A  98     9988   6551   7156   -248   -932    154       N  
ATOM    783  CA  ARG A  98       5.831   8.624  84.154  1.00 61.34           C  
ANISOU  783  CA  ARG A  98     9737   6446   7123     25   -836    139       C  
ATOM    784  C   ARG A  98       6.083   9.796  85.104  1.00 60.09           C  
ANISOU  784  C   ARG A  98     9240   6469   7122     43   -805    168       C  
ATOM    785  O   ARG A  98       7.109   9.854  85.750  1.00 61.41           O  
ANISOU  785  O   ARG A  98     9326   6647   7361    207   -778    169       O  
ATOM    786  CB  ARG A  98       6.137   8.964  82.724  1.00 62.28           C  
ANISOU  786  CB  ARG A  98     9881   6567   7215    111   -756    103       C  
ATOM    787  CG  ARG A  98       7.556   9.384  82.488  1.00 62.14           C  
ANISOU  787  CG  ARG A  98     9732   6602   7276    358   -625     67       C  
ATOM    788  CD  ARG A  98       7.749   9.677  81.027  1.00 57.70           C  
ANISOU  788  CD  ARG A  98     9245   6031   6646    389   -527     26       C  
ATOM    789  NE  ARG A  98       7.148  10.944  80.743  1.00 60.42           N  
ANISOU  789  NE  ARG A  98     9414   6506   7036    250   -533     57       N  
ATOM    790  CZ  ARG A  98       7.401  11.666  79.657  1.00 63.16           C  
ANISOU  790  CZ  ARG A  98     9770   6884   7345    254   -446     35       C  
ATOM    791  NH1 ARG A  98       8.296  11.208  78.768  1.00 59.18           N  
ANISOU  791  NH1 ARG A  98     9409   6313   6763    383   -312    -27       N  
ATOM    792  NH2 ARG A  98       6.778  12.858  79.500  1.00 59.78           N  
ANISOU  792  NH2 ARG A  98     9221   6547   6945    138   -492     68       N  
ATOM    793  N   ASN A  99       5.134  10.697  85.251  1.00 58.29           N  
ANISOU  793  N   ASN A  99     8826   6380   6940   -119   -825    186       N  
ATOM    794  CA  ASN A  99       5.300  11.749  86.212  1.00 57.45           C  
ANISOU  794  CA  ASN A  99     8456   6416   6956   -109   -803    210       C  
ATOM    795  C   ASN A  99       5.278  11.303  87.683  1.00 58.29           C  
ANISOU  795  C   ASN A  99     8580   6498   7068   -169   -847    237       C  
ATOM    796  O   ASN A  99       6.125  11.745  88.486  1.00 58.82           O  
ANISOU  796  O   ASN A  99     8528   6603   7217    -62   -828    256       O  
ATOM    797  CB  ASN A  99       4.324  12.921  85.921  1.00 57.62           C  
ANISOU  797  CB  ASN A  99     8288   6585   7021   -214   -817    206       C  
ATOM    798  CG  ASN A  99       4.682  14.185  86.697  1.00 57.78           C  
ANISOU  798  CG  ASN A  99     8074   6728   7152   -162   -780    226       C  
ATOM    799  OD1 ASN A  99       5.805  14.693  86.602  1.00 58.71           O  
ANISOU  799  OD1 ASN A  99     8132   6856   7318    -34   -714    236       O  
ATOM    800  ND2 ASN A  99       3.750  14.643  87.554  1.00 60.39           N  
ANISOU  800  ND2 ASN A  99     8274   7157   7513   -276   -814    224       N  
ATOM    801  N   GLU A 100       4.373  10.397  88.054  1.00 59.76           N  
ANISOU  801  N   GLU A 100     8943   6614   7149   -358   -909    237       N  
ATOM    802  CA  GLU A 100       4.370   9.836  89.423  1.00 60.56           C  
ANISOU  802  CA  GLU A 100     9149   6651   7209   -445   -950    262       C  
ATOM    803  C   GLU A 100       5.710   9.296  89.840  1.00 59.92           C  
ANISOU  803  C   GLU A 100     9201   6431   7133   -219   -981    277       C  
ATOM    804  O   GLU A 100       6.108   9.373  90.999  1.00 59.78           O  
ANISOU  804  O   GLU A 100     9170   6402   7141   -201  -1015    304       O  
ATOM    805  CB  GLU A 100       3.377   8.679  89.571  1.00 62.45           C  
ANISOU  805  CB  GLU A 100     9660   6787   7282   -700  -1008    255       C  
ATOM    806  CG  GLU A 100       1.971   9.045  89.216  1.00 67.19           C  
ANISOU  806  CG  GLU A 100    10108   7552   7869   -945   -997    223       C  
ATOM    807  CD  GLU A 100       1.385  10.123  90.128  1.00 74.27           C  
ANISOU  807  CD  GLU A 100    10690   8663   8864  -1033   -946    212       C  
ATOM    808  OE1 GLU A 100       2.107  10.663  91.024  1.00 78.09           O  
ANISOU  808  OE1 GLU A 100    11091   9155   9423   -916   -916    240       O  
ATOM    809  OE2 GLU A 100       0.184  10.442  89.933  1.00 76.78           O  
ANISOU  809  OE2 GLU A 100    10839   9151   9182  -1211   -942    165       O  
ATOM    810  N   CYS A 101       6.367   8.722  88.869  1.00 60.01           N  
ANISOU  810  N   CYS A 101     9351   6338   7113    -41   -977    249       N  
ATOM    811  CA  CYS A 101       7.586   7.976  89.057  1.00 61.84           C  
ANISOU  811  CA  CYS A 101     9737   6429   7332    216  -1021    234       C  
ATOM    812  C   CYS A 101       8.731   8.932  89.346  1.00 59.95           C  
ANISOU  812  C   CYS A 101     9182   6339   7256    419   -973    231       C  
ATOM    813  O   CYS A 101       9.421   8.728  90.271  1.00 60.80           O  
ANISOU  813  O   CYS A 101     9302   6408   7391    531  -1047    243       O  
ATOM    814  CB  CYS A 101       7.798   7.174  87.767  1.00 63.80           C  
ANISOU  814  CB  CYS A 101    10205   6547   7488    338  -1001    185       C  
ATOM    815  SG  CYS A 101       9.234   6.210  87.615  1.00 70.85           S  
ANISOU  815  SG  CYS A 101    11285   7279   8357    717  -1037    128       S  
ATOM    816  N   PHE A 102       8.874  10.007  88.571  1.00 59.15           N  
ANISOU  816  N   PHE A 102     8820   6407   7248    435   -862    216       N  
ATOM    817  CA  PHE A 102       9.807  11.112  88.848  1.00 58.03           C  
ANISOU  817  CA  PHE A 102     8368   6436   7244    537   -804    218       C  
ATOM    818  C   PHE A 102       9.698  11.733  90.253  1.00 57.81           C  
ANISOU  818  C   PHE A 102     8219   6471   7274    439   -863    271       C  
ATOM    819  O   PHE A 102      10.694  11.734  91.002  1.00 58.60           O  
ANISOU  819  O   PHE A 102     8242   6588   7435    574   -915    275       O  
ATOM    820  CB  PHE A 102       9.671  12.226  87.816  1.00 55.75           C  
ANISOU  820  CB  PHE A 102     7902   6285   6995    482   -686    205       C  
ATOM    821  CG  PHE A 102      10.083  11.845  86.432  1.00 56.87           C  
ANISOU  821  CG  PHE A 102     8130   6393   7086    592   -598    147       C  
ATOM    822  CD1 PHE A 102      11.340  11.361  86.167  1.00 55.75           C  
ANISOU  822  CD1 PHE A 102     7961   6255   6966    823   -546     86       C  
ATOM    823  CD2 PHE A 102       9.217  12.038  85.371  1.00 60.08           C  
ANISOU  823  CD2 PHE A 102     8632   6777   7419    471   -565    142       C  
ATOM    824  CE1 PHE A 102      11.713  10.997  84.906  1.00 59.11           C  
ANISOU  824  CE1 PHE A 102     8477   6652   7331    925   -440     18       C  
ATOM    825  CE2 PHE A 102       9.591  11.683  84.105  1.00 60.56           C  
ANISOU  825  CE2 PHE A 102     8811   6789   7411    557   -480     88       C  
ATOM    826  CZ  PHE A 102      10.868  11.151  83.883  1.00 62.75           C  
ANISOU  826  CZ  PHE A 102     9076   7065   7702    785   -401     23       C  
ATOM    827  N   LEU A 103       8.519  12.273  90.600  1.00 56.62           N  
ANISOU  827  N   LEU A 103     8043   6365   7105    218   -859    302       N  
ATOM    828  CA  LEU A 103       8.181  12.613  92.050  1.00 56.10           C  
ANISOU  828  CA  LEU A 103     7947   6320   7049     94   -910    344       C  
ATOM    829  C   LEU A 103       8.678  11.655  93.063  1.00 56.89           C  
ANISOU  829  C   LEU A 103     8243   6277   7096    146  -1022    363       C  
ATOM    830  O   LEU A 103       9.449  12.030  93.953  1.00 59.10           O  
ANISOU  830  O   LEU A 103     8438   6584   7432    217  -1073    387       O  
ATOM    831  CB  LEU A 103       6.689  12.685  92.342  1.00 54.01           C  
ANISOU  831  CB  LEU A 103     7721   6079   6719   -150   -898    345       C  
ATOM    832  CG  LEU A 103       5.949  13.629  91.455  1.00 54.42           C  
ANISOU  832  CG  LEU A 103     7602   6264   6811   -203   -830    321       C  
ATOM    833  CD1 LEU A 103       4.522  13.895  91.990  1.00 55.12           C  
ANISOU  833  CD1 LEU A 103     7638   6439   6867   -415   -821    303       C  
ATOM    834  CD2 LEU A 103       6.816  14.895  91.320  1.00 55.75           C  
ANISOU  834  CD2 LEU A 103     7566   6533   7082    -81   -784    332       C  
ATOM    835  N   SER A 104       8.250  10.415  92.968  1.00 58.11           N  
ANISOU  835  N   SER A 104     8693   6262   7123    102  -1080    355       N  
ATOM    836  CA  SER A 104       8.665   9.447  94.022  1.00 60.99           C  
ANISOU  836  CA  SER A 104     9330   6443   7399    143  -1218    378       C  
ATOM    837  C   SER A 104      10.161   9.287  94.209  1.00 60.83           C  
ANISOU  837  C   SER A 104     9261   6395   7456    455  -1307    364       C  
ATOM    838  O   SER A 104      10.540   8.710  95.162  1.00 62.98           O  
ANISOU  838  O   SER A 104     9728   6532   7671    507  -1447    386       O  
ATOM    839  CB  SER A 104       8.062   8.087  93.841  1.00 60.03           C  
ANISOU  839  CB  SER A 104     9604   6108   7098     48  -1281    370       C  
ATOM    840  OG  SER A 104       8.640   7.626  92.676  1.00 63.55           O  
ANISOU  840  OG  SER A 104    10087   6505   7555    269  -1269    325       O  
ATOM    841  N   HIS A 105      10.984   9.808  93.312  1.00 61.07           N  
ANISOU  841  N   HIS A 105     9032   6563   7607    648  -1230    322       N  
ATOM    842  CA  HIS A 105      12.457   9.861  93.525  1.00 62.03           C  
ANISOU  842  CA  HIS A 105     8991   6745   7832    931  -1296    291       C  
ATOM    843  C   HIS A 105      12.984  11.213  94.018  1.00 60.88           C  
ANISOU  843  C   HIS A 105     8497   6815   7820    887  -1258    315       C  
ATOM    844  O   HIS A 105      14.209  11.398  94.049  1.00 61.14           O  
ANISOU  844  O   HIS A 105     8321   6957   7950   1088  -1292    278       O  
ATOM    845  CB  HIS A 105      13.243   9.516  92.253  1.00 62.26           C  
ANISOU  845  CB  HIS A 105     8937   6819   7901   1180  -1219    206       C  
ATOM    846  CG  HIS A 105      13.109   8.101  91.849  1.00 63.82           C  
ANISOU  846  CG  HIS A 105     9502   6782   7967   1312  -1291    169       C  
ATOM    847  ND1 HIS A 105      12.278   7.699  90.824  1.00 64.69           N  
ANISOU  847  ND1 HIS A 105     9793   6809   7976   1205  -1202    155       N  
ATOM    848  CD2 HIS A 105      13.674   6.980  92.340  1.00 66.75           C  
ANISOU  848  CD2 HIS A 105    10135   6960   8268   1542  -1463    143       C  
ATOM    849  CE1 HIS A 105      12.348   6.395  90.685  1.00 67.00           C  
ANISOU  849  CE1 HIS A 105    10452   6866   8138   1346  -1301    123       C  
ATOM    850  NE2 HIS A 105      13.194   5.930  91.590  1.00 69.64           N  
ANISOU  850  NE2 HIS A 105    10853   7121   8486   1567  -1463    113       N  
ATOM    851  N   LYS A 106      12.087  12.139  94.364  1.00 58.69           N  
ANISOU  851  N   LYS A 106     8154   6605   7539    633  -1190    365       N  
ATOM    852  CA  LYS A 106      12.514  13.334  95.092  1.00 59.65           C  
ANISOU  852  CA  LYS A 106     8047   6872   7746    569  -1189    398       C  
ATOM    853  C   LYS A 106      13.275  12.894  96.376  1.00 61.69           C  
ANISOU  853  C   LYS A 106     8389   7051   8000    663  -1377    423       C  
ATOM    854  O   LYS A 106      12.821  11.997  97.071  1.00 62.39           O  
ANISOU  854  O   LYS A 106     8778   6951   7979    627  -1485    447       O  
ATOM    855  CB  LYS A 106      11.330  14.254  95.420  1.00 56.99           C  
ANISOU  855  CB  LYS A 106     7697   6577   7380    315  -1108    437       C  
ATOM    856  CG  LYS A 106      10.922  15.192  94.278  1.00 56.23           C  
ANISOU  856  CG  LYS A 106     7436   6607   7322    258   -961    415       C  
ATOM    857  CD  LYS A 106       9.869  16.244  94.757  1.00 55.66           C  
ANISOU  857  CD  LYS A 106     7327   6589   7232     66   -911    440       C  
ATOM    858  CE  LYS A 106       9.292  17.062  93.576  1.00 55.08           C  
ANISOU  858  CE  LYS A 106     7160   6598   7170     32   -807    414       C  
ATOM    859  NZ  LYS A 106       8.252  18.116  94.043  1.00 56.41           N  
ANISOU  859  NZ  LYS A 106     7290   6819   7323    -97   -777    419       N  
ATOM    860  N   ASP A 107      14.438  13.483  96.665  1.00 57.38           N  
ANISOU  860  N   ASP A 107     7804   7015   6984    771    262   -811       N  
ATOM    861  CA  ASP A 107      15.256  12.993  97.781  1.00 58.52           C  
ANISOU  861  CA  ASP A 107     7763   7186   7288   1065    345   -705       C  
ATOM    862  C   ASP A 107      15.141  14.010  98.896  1.00 56.54           C  
ANISOU  862  C   ASP A 107     7311   7146   7026   1054    187   -543       C  
ATOM    863  O   ASP A 107      15.577  15.133  98.750  1.00 55.09           O  
ANISOU  863  O   ASP A 107     6994   7180   6757    976    150   -559       O  
ATOM    864  CB  ASP A 107      16.716  12.810  97.364  1.00 60.22           C  
ANISOU  864  CB  ASP A 107     7861   7462   7559   1266    570   -781       C  
ATOM    865  CG  ASP A 107      17.558  12.056  98.406  1.00 65.76           C  
ANISOU  865  CG  ASP A 107     8353   8129   8503   1583    598   -617       C  
ATOM    866  OD1 ASP A 107      17.316  12.127  99.660  1.00 65.80           O  
ANISOU  866  OD1 ASP A 107     8273   8197   8532   1634    388   -425       O  
ATOM    867  OD2 ASP A 107      18.517  11.374  97.945  1.00 71.77           O  
ANISOU  867  OD2 ASP A 107     9054   8775   9441   1793    858   -662       O  
ATOM    868  N   ASP A 108      14.541  13.607 100.013  1.00 56.21           N  
ANISOU  868  N   ASP A 108     7302   7002   7053   1116    132   -391       N  
ATOM    869  CA  ASP A 108      14.361  14.505 101.092  1.00 55.65           C  
ANISOU  869  CA  ASP A 108     7173   7063   6907   1087     46   -265       C  
ATOM    870  C   ASP A 108      15.640  14.754 101.916  1.00 56.45           C  
ANISOU  870  C   ASP A 108     7147   7356   6945   1234    -52   -193       C  
ATOM    871  O   ASP A 108      15.681  15.721 102.687  1.00 55.71           O  
ANISOU  871  O   ASP A 108     7064   7395   6710   1149   -150   -141       O  
ATOM    872  CB  ASP A 108      13.241  14.027 102.000  1.00 56.70           C  
ANISOU  872  CB  ASP A 108     7449   6989   7107   1086     92   -118       C  
ATOM    873  CG  ASP A 108      11.899  14.393 101.488  1.00 57.18           C  
ANISOU  873  CG  ASP A 108     7513   6924   7289    878    119   -108       C  
ATOM    874  OD1 ASP A 108      11.610  15.601 101.457  1.00 56.60           O  
ANISOU  874  OD1 ASP A 108     7366   6962   7179    759    109    -98       O  
ATOM    875  OD2 ASP A 108      11.109  13.473 101.152  1.00 60.08           O  
ANISOU  875  OD2 ASP A 108     7941   7056   7832    825    137    -85       O  
ATOM    876  N   SER A 109      16.666  13.920 101.737  1.00 58.17           N  
ANISOU  876  N   SER A 109     7246   7561   7293   1434    -32   -179       N  
ATOM    877  CA  SER A 109      17.975  14.101 102.399  1.00 59.57           C  
ANISOU  877  CA  SER A 109     7197   7917   7519   1565   -197    -55       C  
ATOM    878  C   SER A 109      19.095  13.961 101.388  1.00 61.81           C  
ANISOU  878  C   SER A 109     7208   8254   8022   1672    -56   -133       C  
ATOM    879  O   SER A 109      19.804  12.988 101.414  1.00 65.38           O  
ANISOU  879  O   SER A 109     7529   8595   8717   1916     17    -40       O  
ATOM    880  CB  SER A 109      18.158  13.023 103.437  1.00 61.46           C  
ANISOU  880  CB  SER A 109     7501   8024   7825   1779   -298    162       C  
ATOM    881  OG  SER A 109      18.972  13.478 104.486  1.00 63.21           O  
ANISOU  881  OG  SER A 109     7625   8427   7966   1789   -611    343       O  
ATOM    882  N   PRO A 110      19.269  14.941 100.490  1.00 61.49           N  
ANISOU  882  N   PRO A 110     7084   8354   7925   1503     32   -283       N  
ATOM    883  CA  PRO A 110      20.139  14.814  99.288  1.00 63.22           C  
ANISOU  883  CA  PRO A 110     7142   8564   8313   1576    315   -393       C  
ATOM    884  C   PRO A 110      21.659  14.696  99.394  1.00 67.89           C  
ANISOU  884  C   PRO A 110     7298   9240   9256   1775    360   -259       C  
ATOM    885  O   PRO A 110      22.337  14.541  98.354  1.00 69.91           O  
ANISOU  885  O   PRO A 110     7440   9433   9688   1857    721   -350       O  
ATOM    886  CB  PRO A 110      19.862  16.089  98.508  1.00 60.68           C  
ANISOU  886  CB  PRO A 110     6873   8388   7794   1307    352   -529       C  
ATOM    887  CG  PRO A 110      18.650  16.729  99.159  1.00 58.01           C  
ANISOU  887  CG  PRO A 110     6736   8073   7233   1116    127   -505       C  
ATOM    888  CD  PRO A 110      18.470  16.188 100.503  1.00 57.19           C  
ANISOU  888  CD  PRO A 110     6664   7921   7145   1232    -59   -351       C  
ATOM    889  N   ASP A 111      22.242  14.835 100.572  1.00 70.79           N  
ANISOU  889  N   ASP A 111     7417   9740   9742   1830     12    -32       N  
ATOM    890  CA  ASP A 111      23.750  14.686 100.658  1.00 76.10           C  
ANISOU  890  CA  ASP A 111     7555  10481  10878   2018     -6    168       C  
ATOM    891  C   ASP A 111      24.604  15.942 100.319  1.00 76.19           C  
ANISOU  891  C   ASP A 111     7207  10725  11016   1827    -43    164       C  
ATOM    892  O   ASP A 111      25.838  15.931 100.392  1.00 80.48           O  
ANISOU  892  O   ASP A 111     7231  11330  12019   1942    -79    360       O  
ATOM    893  CB  ASP A 111      24.203  13.362  99.944  1.00 79.50           C  
ANISOU  893  CB  ASP A 111     7901  10629  11677   2360    439    176       C  
ATOM    894  CG  ASP A 111      25.484  13.527  99.027  1.00 87.00           C  
ANISOU  894  CG  ASP A 111     8393  11575  13086   2487    835    197       C  
ATOM    895  OD1 ASP A 111      26.456  12.739  99.222  1.00 88.77           O  
ANISOU  895  OD1 ASP A 111     8203  11671  13853   2806    940    435       O  
ATOM    896  OD2 ASP A 111      25.517  14.430  98.108  1.00 87.90           O  
ANISOU  896  OD2 ASP A 111     8553  11786  13058   2282   1077      6       O  
ATOM    897  N   LEU A 112      23.927  17.059 100.078  1.00 72.40           N  
ANISOU  897  N   LEU A 112     6973  10362  10174   1526    -81    -15       N  
ATOM    898  CA  LEU A 112      24.530  18.224  99.465  1.00 71.39           C  
ANISOU  898  CA  LEU A 112     6613  10388  10125   1326     12    -71       C  
ATOM    899  C   LEU A 112      25.536  18.948 100.312  1.00 74.63           C  
ANISOU  899  C   LEU A 112     6599  10990  10768   1200   -395    125       C  
ATOM    900  O   LEU A 112      25.359  19.023 101.516  1.00 73.99           O  
ANISOU  900  O   LEU A 112     6624  10969  10520   1120   -862    235       O  
ATOM    901  CB  LEU A 112      23.443  19.096  98.828  1.00 66.82           C  
ANISOU  901  CB  LEU A 112     6446   9817   9127   1074    131   -293       C  
ATOM    902  CG  LEU A 112      22.979  18.352  97.561  1.00 64.64           C  
ANISOU  902  CG  LEU A 112     6442   9349   8767   1181    578   -456       C  
ATOM    903  CD1 LEU A 112      21.881  19.178  96.895  1.00 60.13           C  
ANISOU  903  CD1 LEU A 112     6252   8782   7814    923    607   -609       C  
ATOM    904  CD2 LEU A 112      24.183  18.014  96.594  1.00 61.12           C  
ANISOU  904  CD2 LEU A 112     5708   8843   8673   1344   1038   -452       C  
ATOM    905  N   PRO A 113      26.649  19.404  99.664  1.00 78.78           N  
ANISOU  905  N   PRO A 113     6647  11583  11701   1178   -202    188       N  
ATOM    906  CA  PRO A 113      27.736  20.222 100.205  1.00 83.04           C  
ANISOU  906  CA  PRO A 113     6686  12295  12571    992   -560    377       C  
ATOM    907  C   PRO A 113      27.193  21.446 100.861  1.00 81.44           C  
ANISOU  907  C   PRO A 113     6793  12213  11939    611   -946    269       C  
ATOM    908  O   PRO A 113      26.264  22.066 100.328  1.00 78.08           O  
ANISOU  908  O   PRO A 113     6783  11752  11131    472   -715     42       O  
ATOM    909  CB  PRO A 113      28.514  20.630  98.947  1.00 85.00           C  
ANISOU  909  CB  PRO A 113     6578  12527  13191    993    -24    346       C  
ATOM    910  CG  PRO A 113      28.400  19.440  98.054  1.00 85.54           C  
ANISOU  910  CG  PRO A 113     6758  12380  13364   1346    559    280       C  
ATOM    911  CD  PRO A 113      27.092  18.722  98.426  1.00 80.43           C  
ANISOU  911  CD  PRO A 113     6718  11634  12209   1422    427    139       C  
ATOM    912  N   LYS A 114      27.762  21.776 102.009  1.00 84.75           N  
ANISOU  912  N   LYS A 114     7036  12741  12423    439  -1540    446       N  
ATOM    913  CA  LYS A 114      27.345  22.934 102.771  1.00 84.64           C  
ANISOU  913  CA  LYS A 114     7381  12790  11988     55  -1912    333       C  
ATOM    914  C   LYS A 114      27.965  24.248 102.258  1.00 86.22           C  
ANISOU  914  C   LYS A 114     7316  13064  12380   -265  -1861    275       C  
ATOM    915  O   LYS A 114      29.212  24.458 102.309  1.00 91.01           O  
ANISOU  915  O   LYS A 114     7320  13759  13501   -365  -2080    479       O  
ATOM    916  CB  LYS A 114      27.687  22.727 104.252  1.00 88.95           C  
ANISOU  916  CB  LYS A 114     7986  13391  12419    -53  -2611    532       C  
ATOM    917  CG  LYS A 114      26.541  23.063 105.177  1.00 86.67           C  
ANISOU  917  CG  LYS A 114     8460  13028  11443   -218  -2776    367       C  
ATOM    918  CD  LYS A 114      25.363  22.107 104.921  1.00 82.93           C  
ANISOU  918  CD  LYS A 114     8357  12413  10741     98  -2366    278       C  
ATOM    919  CE  LYS A 114      24.265  22.283 105.979  1.00 82.54           C  
ANISOU  919  CE  LYS A 114     9015  12253  10093    -22  -2485    183       C  
ATOM    920  NZ  LYS A 114      24.779  22.312 107.392  1.00 83.46           N  
ANISOU  920  NZ  LYS A 114     9334  12413   9966   -207  -3110    351       N  
ATOM    921  N   LEU A 115      27.079  25.113 101.761  1.00 82.21           N  
ANISOU  921  N   LEU A 115     7227  12496  11514   -422  -1572     32       N  
ATOM    922  CA  LEU A 115      27.432  26.450 101.311  1.00 83.29           C  
ANISOU  922  CA  LEU A 115     7256  12652  11737   -745  -1491    -45       C  
ATOM    923  C   LEU A 115      27.986  27.262 102.476  1.00 87.07           C  
ANISOU  923  C   LEU A 115     7724  13179  12180  -1126  -2103      3       C  
ATOM    924  O   LEU A 115      27.259  27.583 103.426  1.00 86.13           O  
ANISOU  924  O   LEU A 115     8160  12990  11573  -1280  -2370   -114       O  
ATOM    925  CB  LEU A 115      26.204  27.165 100.734  1.00 78.29           C  
ANISOU  925  CB  LEU A 115     7148  11906  10691   -816  -1136   -271       C  
ATOM    926  CG  LEU A 115      25.581  26.669  99.432  1.00 75.04           C  
ANISOU  926  CG  LEU A 115     6845  11432  10234   -571   -591   -339       C  
ATOM    927  CD1 LEU A 115      24.255  27.397  99.198  1.00 70.38           C  
ANISOU  927  CD1 LEU A 115     6773  10723   9245   -674   -445   -488       C  
ATOM    928  CD2 LEU A 115      26.535  26.817  98.240  1.00 77.05           C  
ANISOU  928  CD2 LEU A 115     6681  11722  10872   -554   -200   -274       C  
ATOM    929  N   LYS A 116      29.280  27.544 102.406  1.00 91.82           N  
ANISOU  929  N   LYS A 116     7705  13872  13311  -1283  -2311    186       N  
ATOM    930  CA  LYS A 116      29.941  28.420 103.349  1.00 96.27           C  
ANISOU  930  CA  LYS A 116     8208  14469  13901  -1731  -2933    236       C  
ATOM    931  C   LYS A 116      30.090  29.753 102.621  1.00 96.51           C  
ANISOU  931  C   LYS A 116     8187  14437  14045  -2040  -2644    103       C  
ATOM    932  O   LYS A 116      31.118  30.007 101.965  1.00100.26           O  
ANISOU  932  O   LYS A 116     8012  14962  15120  -2115  -2514    260       O  
ATOM    933  CB  LYS A 116      31.308  27.856 103.730  1.00102.67           C  
ANISOU  933  CB  LYS A 116     8262  15405  15343  -1731  -3410    591       C  
ATOM    934  CG  LYS A 116      32.079  28.715 104.729  1.00107.71           C  
ANISOU  934  CG  LYS A 116     8808  16080  16036  -2263  -4195    681       C  
ATOM    935  CD  LYS A 116      33.587  28.547 104.552  1.00114.06           C  
ANISOU  935  CD  LYS A 116     8594  16989  17754  -2322  -4478   1064       C  
ATOM    936  CE  LYS A 116      34.020  28.865 103.129  1.00112.96           C  
ANISOU  936  CE  LYS A 116     7904  16820  18195  -2202  -3707   1072       C  
ATOM    937  NZ  LYS A 116      35.488  28.952 103.023  1.00118.48           N  
ANISOU  937  NZ  LYS A 116     7595  17577  19843  -2346  -3954   1445       N  
ATOM    938  N   PRO A 117      29.058  30.607 102.709  1.00 92.97           N  
ANISOU  938  N   PRO A 117     8405  13847  13071  -2202  -2485   -162       N  
ATOM    939  CA  PRO A 117      29.088  31.768 101.835  1.00 92.50           C  
ANISOU  939  CA  PRO A 117     8313  13697  13135  -2413  -2103   -260       C  
ATOM    940  C   PRO A 117      30.124  32.809 102.302  1.00 98.30           C  
ANISOU  940  C   PRO A 117     8775  14414  14161  -2921  -2534   -212       C  
ATOM    941  O   PRO A 117      30.157  33.205 103.475  1.00100.89           O  
ANISOU  941  O   PRO A 117     9439  14687  14208  -3248  -3101   -287       O  
ATOM    942  CB  PRO A 117      27.633  32.297 101.890  1.00 87.46           C  
ANISOU  942  CB  PRO A 117     8441  12875  11915  -2397  -1837   -505       C  
ATOM    943  CG  PRO A 117      26.813  31.216 102.590  1.00 84.34           C  
ANISOU  943  CG  PRO A 117     8405  12492  11148  -2105  -1953   -526       C  
ATOM    944  CD  PRO A 117      27.824  30.573 103.515  1.00 90.03           C  
ANISOU  944  CD  PRO A 117     8807  13355  12045  -2174  -2554   -350       C  
ATOM    945  N   ASP A 118      30.994  33.195 101.377  1.00100.52           N  
ANISOU  945  N   ASP A 118     8462  14725  15006  -3000  -2256    -79       N  
ATOM    946  CA  ASP A 118      31.998  34.211 101.628  1.00106.23           C  
ANISOU  946  CA  ASP A 118     8836  15409  16118  -3500  -2593    -10       C  
ATOM    947  C   ASP A 118      31.621  35.498 100.882  1.00104.17           C  
ANISOU  947  C   ASP A 118     8853  14956  15770  -3722  -2123   -172       C  
ATOM    948  O   ASP A 118      31.430  35.479  99.661  1.00101.70           O  
ANISOU  948  O   ASP A 118     8434  14632  15577  -3482  -1463   -137       O  
ATOM    949  CB  ASP A 118      33.392  33.698 101.247  1.00111.81           C  
ANISOU  949  CB  ASP A 118     8554  16260  17668  -3454  -2647    330       C  
ATOM    950  CG  ASP A 118      34.241  34.756 100.631  1.00116.75           C  
ANISOU  950  CG  ASP A 118     8715  16807  18839  -3815  -2459    416       C  
ATOM    951  OD1 ASP A 118      34.084  34.973  99.413  1.00116.36           O  
ANISOU  951  OD1 ASP A 118     8621  16697  18892  -3641  -1699    402       O  
ATOM    952  OD2 ASP A 118      35.052  35.374 101.352  1.00123.71           O  
ANISOU  952  OD2 ASP A 118     9309  17671  20025  -4297  -3080    507       O  
ATOM    953  N   PRO A 119      31.537  36.624 101.619  1.00105.89           N  
ANISOU  953  N   PRO A 119     9473  14993  15765  -4198  -2467   -341       N  
ATOM    954  CA  PRO A 119      30.876  37.844 101.133  1.00103.33           C  
ANISOU  954  CA  PRO A 119     9618  14415  15227  -4370  -2043   -527       C  
ATOM    955  C   PRO A 119      31.567  38.535  99.934  1.00105.01           C  
ANISOU  955  C   PRO A 119     9336  14584  15980  -4491  -1573   -380       C  
ATOM    956  O   PRO A 119      30.857  39.078  99.071  1.00100.74           O  
ANISOU  956  O   PRO A 119     9109  13900  15269  -4377  -1012   -438       O  
ATOM    957  CB  PRO A 119      30.837  38.752 102.376  1.00106.91           C  
ANISOU  957  CB  PRO A 119    10597  14656  15369  -4882  -2586   -738       C  
ATOM    958  CG  PRO A 119      31.383  37.919 103.525  1.00110.91           C  
ANISOU  958  CG  PRO A 119    10986  15338  15816  -4965  -3341   -658       C  
ATOM    959  CD  PRO A 119      32.215  36.848 102.909  1.00111.44           C  
ANISOU  959  CD  PRO A 119    10174  15695  16473  -4647  -3303   -334       C  
ATOM    960  N   ASN A 120      32.914  38.503  99.890  1.00110.61           N  
ANISOU  960  N   ASN A 120     9275  15399  17351  -4717  -1800   -158       N  
ATOM    961  CA  ASN A 120      33.710  39.062  98.770  1.00113.44           C  
ANISOU  961  CA  ASN A 120     9078  15711  18312  -4830  -1298     29       C  
ATOM    962  C   ASN A 120      33.518  38.383  97.403  1.00110.79           C  
ANISOU  962  C   ASN A 120     8581  15465  18050  -4331   -500    155       C  
ATOM    963  O   ASN A 120      33.016  39.030  96.461  1.00109.26           O  
ANISOU  963  O   ASN A 120     8708  15127  17680  -4301     69    118       O  
ATOM    964  CB  ASN A 120      35.210  39.045  99.082  1.00121.10           C  
ANISOU  964  CB  ASN A 120     9155  16769  20087  -5154  -1718    291       C  
ATOM    965  CG  ASN A 120      35.605  40.053 100.158  1.00125.00           C  
ANISOU  965  CG  ASN A 120     9786  17108  20600  -5818  -2459    187       C  
ATOM    966  OD1 ASN A 120      35.133  41.191 100.184  1.00121.50           O  
ANISOU  966  OD1 ASN A 120     9900  16405  19861  -6131  -2353    -30       O  
ATOM    967  ND2 ASN A 120      36.492  39.633 101.045  1.00130.45           N  
ANISOU  967  ND2 ASN A 120     9980  17932  21653  -6049  -3233    357       N  
ATOM    968  N   THR A 121      33.858  37.091  97.290  1.00110.37           N  
ANISOU  968  N   THR A 121     8118  15614  18206  -3946   -455    301       N  
ATOM    969  CA  THR A 121      33.511  36.324  96.081  1.00106.84           C  
ANISOU  969  CA  THR A 121     7723  15211  17661  -3466    285    349       C  
ATOM    970  C   THR A 121      31.986  36.343  95.871  1.00 99.32           C  
ANISOU  970  C   THR A 121     7642  14191  15906  -3259    447    118       C  
ATOM    971  O   THR A 121      31.517  36.262  94.742  1.00 96.75           O  
ANISOU  971  O   THR A 121     7569  13821  15372  -3043   1036    125       O  
ATOM    972  CB  THR A 121      33.951  34.846  96.179  1.00108.13           C  
ANISOU  972  CB  THR A 121     7442  15545  18097  -3061    267    493       C  
ATOM    973  OG1 THR A 121      34.374  34.398  94.886  1.00109.66           O  
ANISOU  973  OG1 THR A 121     7360  15715  18592  -2779   1077    629       O  
ATOM    974  CG2 THR A 121      32.786  33.956  96.650  1.00 99.76           C  
ANISOU  974  CG2 THR A 121     6981  14548  16374  -2729     63    310       C  
ATOM    975  N   LEU A 122      31.221  36.462  96.949  1.00 96.14           N  
ANISOU  975  N   LEU A 122     7702  13760  15069  -3343    -71    -64       N  
ATOM    976  CA  LEU A 122      29.752  36.450  96.812  1.00 90.26           C  
ANISOU  976  CA  LEU A 122     7687  12927  13682  -3132     86   -237       C  
ATOM    977  C   LEU A 122      29.194  37.788  96.345  1.00 88.79           C  
ANISOU  977  C   LEU A 122     7902  12506  13328  -3358    346   -297       C  
ATOM    978  O   LEU A 122      28.339  37.805  95.479  1.00 84.57           O  
ANISOU  978  O   LEU A 122     7712  11910  12511  -3148    734   -286       O  
ATOM    979  CB  LEU A 122      29.066  35.979  98.097  1.00 88.10           C  
ANISOU  979  CB  LEU A 122     7780  12672  13023  -3074   -428   -387       C  
ATOM    980  CG  LEU A 122      27.593  35.579  98.113  1.00 84.90           C  
ANISOU  980  CG  LEU A 122     7976  12204  12077  -2778   -298   -513       C  
ATOM    981  CD1 LEU A 122      27.195  34.532  97.021  1.00 85.05           C  
ANISOU  981  CD1 LEU A 122     7960  12328  12028  -2359    118   -435       C  
ATOM    982  CD2 LEU A 122      27.265  35.006  99.496  1.00 86.67           C  
ANISOU  982  CD2 LEU A 122     8439  12457  12035  -2752   -793   -614       C  
ATOM    983  N   CYS A 123      29.680  38.901  96.910  1.00 92.43           N  
ANISOU  983  N   CYS A 123     8329  12815  13976  -3800    105   -342       N  
ATOM    984  CA  CYS A 123      29.320  40.233  96.409  1.00 92.96           C  
ANISOU  984  CA  CYS A 123     8711  12612  13996  -4031    402   -361       C  
ATOM    985  C   CYS A 123      29.883  40.443  95.002  1.00 94.97           C  
ANISOU  985  C   CYS A 123     8654  12878  14552  -4000    975   -146       C  
ATOM    986  O   CYS A 123      29.327  41.237  94.232  1.00 94.08           O  
ANISOU  986  O   CYS A 123     8881  12577  14289  -4024   1345    -96       O  
ATOM    987  CB  CYS A 123      29.841  41.351  97.312  1.00 97.41           C  
ANISOU  987  CB  CYS A 123     9310  12969  14731  -4557     32   -470       C  
ATOM    988  SG  CYS A 123      28.704  42.103  98.525  1.00 97.38           S  
ANISOU  988  SG  CYS A 123    10146  12647  14206  -4718   -242   -772       S  
ATOM    989  N   ASP A 124      30.995  39.750  94.697  1.00 97.84           N  
ANISOU  989  N   ASP A 124     8382  13432  15361  -3948   1066      6       N  
ATOM    990  CA  ASP A 124      31.565  39.680  93.344  1.00 99.79           C  
ANISOU  990  CA  ASP A 124     8354  13694  15867  -3846   1725    212       C  
ATOM    991  C   ASP A 124      30.583  39.174  92.303  1.00 95.35           C  
ANISOU  991  C   ASP A 124     8295  13145  14789  -3469   2168    218       C  
ATOM    992  O   ASP A 124      30.477  39.743  91.219  1.00 96.18           O  
ANISOU  992  O   ASP A 124     8615  13128  14803  -3504   2661    338       O  
ATOM    993  CB  ASP A 124      32.881  38.863  93.306  1.00104.11           C  
ANISOU  993  CB  ASP A 124     8104  14412  17042  -3784   1793    381       C  
ATOM    994  CG  ASP A 124      34.096  39.714  93.661  1.00110.51           C  
ANISOU  994  CG  ASP A 124     8300  15142  18548  -4252   1620    514       C  
ATOM    995  OD1 ASP A 124      33.990  40.945  93.504  1.00109.34           O  
ANISOU  995  OD1 ASP A 124     8381  14781  18381  -4595   1702    493       O  
ATOM    996  OD2 ASP A 124      35.150  39.179  94.095  1.00116.68           O  
ANISOU  996  OD2 ASP A 124     8350  16046  19937  -4295   1385    664       O  
ATOM    997  N   GLU A 125      29.851  38.121  92.645  1.00 91.34           N  
ANISOU  997  N   GLU A 125     8008  12769  13930  -3143   1956    106       N  
ATOM    998  CA  GLU A 125      28.974  37.464  91.684  1.00 88.61           C  
ANISOU  998  CA  GLU A 125     8104  12446  13120  -2814   2289    113       C  
ATOM    999  C   GLU A 125      27.634  38.106  91.427  1.00 84.54           C  
ANISOU  999  C   GLU A 125     8218  11778  12126  -2811   2249     90       C  
ATOM   1000  O   GLU A 125      27.019  37.804  90.397  1.00 84.07           O  
ANISOU 1000  O   GLU A 125     8521  11705  11716  -2637   2531    163       O  
ATOM   1001  CB  GLU A 125      28.740  36.010  92.052  1.00 86.84           C  
ANISOU 1001  CB  GLU A 125     7840  12391  12763  -2472   2117     25       C  
ATOM   1002  CG  GLU A 125      29.988  35.160  91.988  1.00 93.46           C  
ANISOU 1002  CG  GLU A 125     8069  13350  14093  -2356   2301    114       C  
ATOM   1003  CD  GLU A 125      29.996  34.182  93.126  1.00 95.78           C  
ANISOU 1003  CD  GLU A 125     8156  13777  14457  -2190   1802     41       C  
ATOM   1004  OE1 GLU A 125      31.090  33.957  93.715  1.00 99.97           O  
ANISOU 1004  OE1 GLU A 125     8063  14386  15535  -2256   1607    147       O  
ATOM   1005  OE2 GLU A 125      28.882  33.680  93.445  1.00 92.65           O  
ANISOU 1005  OE2 GLU A 125     8218  13394  13591  -2011   1580    -89       O  
ATOM   1006  N   PHE A 126      27.155  38.942  92.348  1.00 82.85           N  
ANISOU 1006  N   PHE A 126     8159  11425  11894  -2998   1898     -1       N  
ATOM   1007  CA  PHE A 126      25.891  39.688  92.152  1.00 79.71           C  
ANISOU 1007  CA  PHE A 126     8286  10819  11180  -2985   1901     26       C  
ATOM   1008  C   PHE A 126      26.107  40.945  91.276  1.00 84.06           C  
ANISOU 1008  C   PHE A 126     8940  11159  11838  -3218   2248    205       C  
ATOM   1009  O   PHE A 126      25.279  41.283  90.417  1.00 83.73           O  
ANISOU 1009  O   PHE A 126     9278  11001  11536  -3131   2425    364       O  
ATOM   1010  CB  PHE A 126      25.241  39.958  93.513  1.00 77.79           C  
ANISOU 1010  CB  PHE A 126     8223  10461  10875  -3036   1496   -153       C  
ATOM   1011  CG  PHE A 126      24.440  41.223  93.602  1.00 74.40           C  
ANISOU 1011  CG  PHE A 126     8164   9701  10402  -3169   1556   -124       C  
ATOM   1012  CD1 PHE A 126      23.089  41.208  93.368  1.00 68.33           C  
ANISOU 1012  CD1 PHE A 126     7754   8811   9399  -2937   1587    -45       C  
ATOM   1013  CD2 PHE A 126      25.043  42.416  93.984  1.00 75.53           C  
ANISOU 1013  CD2 PHE A 126     8273   9624  10800  -3533   1567   -167       C  
ATOM   1014  CE1 PHE A 126      22.360  42.352  93.468  1.00 69.44           C  
ANISOU 1014  CE1 PHE A 126     8183   8608   9593  -3017   1681     20       C  
ATOM   1015  CE2 PHE A 126      24.310  43.575  94.090  1.00 74.79           C  
ANISOU 1015  CE2 PHE A 126     8545   9169  10704  -3634   1676   -145       C  
ATOM   1016  CZ  PHE A 126      22.970  43.546  93.824  1.00 72.62           C  
ANISOU 1016  CZ  PHE A 126     8596   8766  10229  -3352   1756    -38       C  
ATOM   1017  N   LYS A 127      27.236  41.618  91.442  1.00 87.99           N  
ANISOU 1017  N   LYS A 127     9089  11602  12742  -3529   2331    220       N  
ATOM   1018  CA  LYS A 127      27.553  42.653  90.483  1.00 92.13           C  
ANISOU 1018  CA  LYS A 127     9683  11937  13386  -3732   2741    422       C  
ATOM   1019  C   LYS A 127      27.713  42.100  89.047  1.00 93.46           C  
ANISOU 1019  C   LYS A 127     9940  12212  13357  -3551   3229    616       C  
ATOM   1020  O   LYS A 127      27.055  42.595  88.114  1.00 94.06           O  
ANISOU 1020  O   LYS A 127    10456  12149  13134  -3523   3452    800       O  
ATOM   1021  CB  LYS A 127      28.744  43.531  90.926  1.00 96.62           C  
ANISOU 1021  CB  LYS A 127     9837  12388  14487  -4151   2743    415       C  
ATOM   1022  CG  LYS A 127      28.332  44.985  91.175  1.00 98.19           C  
ANISOU 1022  CG  LYS A 127    10352  12220  14737  -4435   2719    420       C  
ATOM   1023  CD  LYS A 127      28.182  45.729  89.828  1.00101.96           C  
ANISOU 1023  CD  LYS A 127    11077  12516  15147  -4457   3236    710       C  
ATOM   1024  CE  LYS A 127      27.817  47.221  89.967  1.00102.54           C  
ANISOU 1024  CE  LYS A 127    11451  12168  15340  -4723   3284    767       C  
ATOM   1025  NZ  LYS A 127      28.732  47.989  90.839  1.00104.01           N  
ANISOU 1025  NZ  LYS A 127    11351  12181  15986  -5172   3122    616       N  
ATOM   1026  N   ALA A 128      28.557  41.079  88.873  1.00 94.46           N  
ANISOU 1026  N   ALA A 128     9701  12556  13635  -3427   3400    588       N  
ATOM   1027  CA  ALA A 128      28.774  40.465  87.560  1.00 95.52           C  
ANISOU 1027  CA  ALA A 128     9996  12750  13546  -3257   3942    722       C  
ATOM   1028  C   ALA A 128      27.461  40.228  86.785  1.00 92.61           C  
ANISOU 1028  C   ALA A 128    10326  12350  12513  -3063   3913    782       C  
ATOM   1029  O   ALA A 128      27.353  40.646  85.638  1.00 94.84           O  
ANISOU 1029  O   ALA A 128    10993  12520  12523  -3120   4288    980       O  
ATOM   1030  CB  ALA A 128      29.584  39.176  87.691  1.00 96.47           C  
ANISOU 1030  CB  ALA A 128     9687  13074  13894  -3051   4072    637       C  
ATOM   1031  N   ASP A 129      26.461  39.603  87.429  1.00 88.21           N  
ANISOU 1031  N   ASP A 129     9931  11874  11712  -2865   3442    640       N  
ATOM   1032  CA  ASP A 129      25.163  39.293  86.795  1.00 85.71           C  
ANISOU 1032  CA  ASP A 129    10185  11531  10850  -2701   3300    718       C  
ATOM   1033  C   ASP A 129      24.047  38.981  87.839  1.00 80.57           C  
ANISOU 1033  C   ASP A 129     9574  10897  10143  -2554   2750    589       C  
ATOM   1034  O   ASP A 129      23.885  37.862  88.323  1.00 76.92           O  
ANISOU 1034  O   ASP A 129     9020  10588   9618  -2359   2559    424       O  
ATOM   1035  CB  ASP A 129      25.331  38.179  85.745  1.00 87.14           C  
ANISOU 1035  CB  ASP A 129    10628  11821  10661  -2541   3624    717       C  
ATOM   1036  CG  ASP A 129      23.995  37.672  85.141  1.00 88.27           C  
ANISOU 1036  CG  ASP A 129    11359  11954  10228  -2415   3352    780       C  
ATOM   1037  OD1 ASP A 129      22.860  37.804  85.721  1.00 86.89           O  
ANISOU 1037  OD1 ASP A 129    11259  11742  10014  -2355   2860    796       O  
ATOM   1038  OD2 ASP A 129      24.105  37.068  84.051  1.00 92.15           O  
ANISOU 1038  OD2 ASP A 129    12251  12456  10308  -2383   3656    814       O  
ATOM   1039  N   GLU A 130      23.259  40.007  88.119  1.00 80.06           N  
ANISOU 1039  N   GLU A 130     9671  10630  10120  -2640   2564    695       N  
ATOM   1040  CA  GLU A 130      22.184  39.948  89.083  1.00 76.85           C  
ANISOU 1040  CA  GLU A 130     9317  10154   9728  -2517   2172    614       C  
ATOM   1041  C   GLU A 130      21.117  38.894  88.756  1.00 73.73           C  
ANISOU 1041  C   GLU A 130     9156   9853   9003  -2275   1951    648       C  
ATOM   1042  O   GLU A 130      20.518  38.320  89.673  1.00 70.41           O  
ANISOU 1042  O   GLU A 130     8662   9465   8627  -2128   1684    511       O  
ATOM   1043  CB  GLU A 130      21.585  41.368  89.293  1.00 77.97           C  
ANISOU 1043  CB  GLU A 130     9604   9978  10043  -2646   2153    763       C  
ATOM   1044  CG  GLU A 130      22.614  42.313  90.038  1.00 84.31           C  
ANISOU 1044  CG  GLU A 130    10161  10657  11217  -2926   2266    628       C  
ATOM   1045  CD  GLU A 130      22.508  43.854  89.805  1.00 89.38           C  
ANISOU 1045  CD  GLU A 130    10963  10945  12053  -3138   2447    809       C  
ATOM   1046  OE1 GLU A 130      23.579  44.514  89.764  1.00 91.38           O  
ANISOU 1046  OE1 GLU A 130    11037  11135  12548  -3415   2649    789       O  
ATOM   1047  OE2 GLU A 130      21.382  44.412  89.694  1.00 90.85           O  
ANISOU 1047  OE2 GLU A 130    11415  10887  12216  -3033   2395    988       O  
ATOM   1048  N   LYS A 131      20.880  38.607  87.484  1.00 75.25           N  
ANISOU 1048  N   LYS A 131     9664  10075   8851  -2259   2052    825       N  
ATOM   1049  CA  LYS A 131      19.755  37.707  87.178  1.00 74.02           C  
ANISOU 1049  CA  LYS A 131     9759   9964   8401  -2097   1749    877       C  
ATOM   1050  C   LYS A 131      20.148  36.226  87.301  1.00 72.27           C  
ANISOU 1050  C   LYS A 131     9473   9953   8034  -1953   1765    630       C  
ATOM   1051  O   LYS A 131      19.327  35.378  87.658  1.00 70.09           O  
ANISOU 1051  O   LYS A 131     9235   9714   7683  -1808   1472    568       O  
ATOM   1052  CB  LYS A 131      19.033  38.061  85.854  1.00 77.18           C  
ANISOU 1052  CB  LYS A 131    10615  10260   8450  -2175   1677   1209       C  
ATOM   1053  CG  LYS A 131      17.489  37.850  85.904  1.00 77.75           C  
ANISOU 1053  CG  LYS A 131    10806  10243   8493  -2072   1191   1399       C  
ATOM   1054  CD  LYS A 131      16.896  38.047  87.352  1.00 75.38           C  
ANISOU 1054  CD  LYS A 131    10136   9844   8660  -1930   1032   1298       C  
ATOM   1055  CE  LYS A 131      15.378  38.159  87.378  1.00 74.83           C  
ANISOU 1055  CE  LYS A 131    10089   9604   8738  -1831    662   1581       C  
ATOM   1056  NZ  LYS A 131      14.926  38.605  88.733  1.00 70.88           N  
ANISOU 1056  NZ  LYS A 131     9299   8928   8703  -1706    697   1497       N  
ATOM   1057  N   LYS A 132      21.431  35.953  87.097  1.00 73.41           N  
ANISOU 1057  N   LYS A 132     9460  10201   8231  -1986   2137    504       N  
ATOM   1058  CA  LYS A 132      21.975  34.625  87.319  1.00 72.41           C  
ANISOU 1058  CA  LYS A 132     9190  10228   8094  -1822   2224    285       C  
ATOM   1059  C   LYS A 132      22.294  34.347  88.801  1.00 68.93           C  
ANISOU 1059  C   LYS A 132     8280   9870   8041  -1731   2014    105       C  
ATOM   1060  O   LYS A 132      22.139  33.241  89.300  1.00 66.51           O  
ANISOU 1060  O   LYS A 132     7903   9650   7719  -1551   1866    -33       O  
ATOM   1061  CB  LYS A 132      23.215  34.440  86.466  1.00 75.90           C  
ANISOU 1061  CB  LYS A 132     9622  10702   8515  -1865   2774    272       C  
ATOM   1062  CG  LYS A 132      24.198  33.478  87.038  1.00 77.90           C  
ANISOU 1062  CG  LYS A 132     9453  11071   9073  -1707   2945     86       C  
ATOM   1063  CD  LYS A 132      25.092  32.991  85.928  1.00 87.15           C  
ANISOU 1063  CD  LYS A 132    10771  12212  10129  -1677   3568     86       C  
ATOM   1064  CE  LYS A 132      26.534  33.016  86.395  1.00 91.97           C  
ANISOU 1064  CE  LYS A 132    10722  12872  11349  -1657   3899     73       C  
ATOM   1065  NZ  LYS A 132      27.425  32.526  85.322  1.00 98.90           N  
ANISOU 1065  NZ  LYS A 132    11711  13671  12197  -1591   4636     88       N  
ATOM   1066  N   PHE A 133      22.767  35.353  89.499  1.00 68.81           N  
ANISOU 1066  N   PHE A 133     7990   9807   8348  -1882   1991    112       N  
ATOM   1067  CA  PHE A 133      22.947  35.233  90.928  1.00 67.54           C  
ANISOU 1067  CA  PHE A 133     7518   9692   8452  -1859   1711    -40       C  
ATOM   1068  C   PHE A 133      21.583  34.794  91.539  1.00 63.98           C  
ANISOU 1068  C   PHE A 133     7287   9190   7832  -1702   1379    -75       C  
ATOM   1069  O   PHE A 133      21.504  33.962  92.424  1.00 61.14           O  
ANISOU 1069  O   PHE A 133     6816   8908   7505  -1566   1183   -204       O  
ATOM   1070  CB  PHE A 133      23.438  36.582  91.449  1.00 68.94           C  
ANISOU 1070  CB  PHE A 133     7536   9749   8908  -2121   1706    -20       C  
ATOM   1071  CG  PHE A 133      23.647  36.655  92.939  1.00 67.70           C  
ANISOU 1071  CG  PHE A 133     7182   9596   8945  -2187   1383   -181       C  
ATOM   1072  CD1 PHE A 133      24.911  36.450  93.480  1.00 67.74           C  
ANISOU 1072  CD1 PHE A 133     6764   9726   9248  -2295   1314   -246       C  
ATOM   1073  CD2 PHE A 133      22.580  36.999  93.788  1.00 64.28           C  
ANISOU 1073  CD2 PHE A 133     7008   9008   8408  -2163   1158   -241       C  
ATOM   1074  CE1 PHE A 133      25.128  36.586  94.843  1.00 71.57           C  
ANISOU 1074  CE1 PHE A 133     7152  10203   9840  -2420    938   -375       C  
ATOM   1075  CE2 PHE A 133      22.750  37.085  95.146  1.00 64.11           C  
ANISOU 1075  CE2 PHE A 133     6946   8955   8457  -2253    894   -402       C  
ATOM   1076  CZ  PHE A 133      24.023  36.900  95.698  1.00 69.95           C  
ANISOU 1076  CZ  PHE A 133     7336   9837   9406  -2406    736   -477       C  
ATOM   1077  N   TRP A 134      20.525  35.319  90.941  1.00 64.46           N  
ANISOU 1077  N   TRP A 134     7651   9108   7735  -1717   1342     88       N  
ATOM   1078  CA  TRP A 134      19.161  35.118  91.333  1.00 61.87           C  
ANISOU 1078  CA  TRP A 134     7480   8677   7353  -1592   1088    140       C  
ATOM   1079  C   TRP A 134      18.771  33.664  91.084  1.00 61.31           C  
ANISOU 1079  C   TRP A 134     7489   8726   7078  -1415    970     80       C  
ATOM   1080  O   TRP A 134      18.221  33.026  91.957  1.00 60.39           O  
ANISOU 1080  O   TRP A 134     7317   8608   7020  -1283    790     -3       O  
ATOM   1081  CB  TRP A 134      18.311  36.092  90.518  1.00 62.39           C  
ANISOU 1081  CB  TRP A 134     7773   8551   7381  -1671   1084    413       C  
ATOM   1082  CG  TRP A 134      16.888  36.100  90.894  1.00 60.38           C  
ANISOU 1082  CG  TRP A 134     7584   8136   7222  -1551    855    544       C  
ATOM   1083  CD1 TRP A 134      16.334  36.762  91.920  1.00 60.35           C  
ANISOU 1083  CD1 TRP A 134     7511   7928   7492  -1515    854    539       C  
ATOM   1084  CD2 TRP A 134      15.816  35.450  90.200  1.00 58.91           C  
ANISOU 1084  CD2 TRP A 134     7548   7939   6896  -1470    618    728       C  
ATOM   1085  NE1 TRP A 134      14.980  36.547  91.952  1.00 58.77           N  
ANISOU 1085  NE1 TRP A 134     7338   7587   7406  -1376    688    726       N  
ATOM   1086  CE2 TRP A 134      14.633  35.740  90.904  1.00 58.84           C  
ANISOU 1086  CE2 TRP A 134     7449   7725   7184  -1363    487    858       C  
ATOM   1087  CE3 TRP A 134      15.743  34.665  89.034  1.00 59.93           C  
ANISOU 1087  CE3 TRP A 134     7913   8183   6674  -1505    508    797       C  
ATOM   1088  CZ2 TRP A 134      13.370  35.250  90.510  1.00 59.50           C  
ANISOU 1088  CZ2 TRP A 134     7556   7733   7317  -1288    199   1094       C  
ATOM   1089  CZ3 TRP A 134      14.475  34.159  88.630  1.00 57.83           C  
ANISOU 1089  CZ3 TRP A 134     7762   7848   6364  -1471    156    997       C  
ATOM   1090  CH2 TRP A 134      13.316  34.467  89.370  1.00 61.10           C  
ANISOU 1090  CH2 TRP A 134     7969   8075   7170  -1365    -16   1164       C  
ATOM   1091  N   GLY A 135      19.042  33.152  89.884  1.00 63.39           N  
ANISOU 1091  N   GLY A 135     7944   9059   7082  -1429   1106    119       N  
ATOM   1092  CA  GLY A 135      18.772  31.759  89.530  1.00 62.22           C  
ANISOU 1092  CA  GLY A 135     7951   8980   6710  -1299   1039     30       C  
ATOM   1093  C   GLY A 135      19.554  30.767  90.358  1.00 61.84           C  
ANISOU 1093  C   GLY A 135     7633   9051   6813  -1143   1105   -185       C  
ATOM   1094  O   GLY A 135      18.993  29.796  90.893  1.00 59.00           O  
ANISOU 1094  O   GLY A 135     7279   8694   6444   -999    916   -261       O  
ATOM   1095  N   LYS A 136      20.860  31.000  90.488  1.00 64.25           N  
ANISOU 1095  N   LYS A 136     7666   9438   7307  -1173   1359   -248       N  
ATOM   1096  CA  LYS A 136      21.677  30.131  91.342  1.00 64.49           C  
ANISOU 1096  CA  LYS A 136     7362   9574   7568  -1023   1361   -384       C  
ATOM   1097  C   LYS A 136      21.077  29.969  92.746  1.00 60.65           C  
ANISOU 1097  C   LYS A 136     6774   9085   7187   -953    996   -434       C  
ATOM   1098  O   LYS A 136      21.207  28.924  93.350  1.00 60.88           O  
ANISOU 1098  O   LYS A 136     6698   9165   7270   -784    902   -510       O  
ATOM   1099  CB  LYS A 136      23.112  30.618  91.458  1.00 67.28           C  
ANISOU 1099  CB  LYS A 136     7321  10000   8244  -1108   1585   -376       C  
ATOM   1100  CG  LYS A 136      24.062  29.454  91.666  1.00 72.29           C  
ANISOU 1100  CG  LYS A 136     7649  10716   9103   -910   1725   -440       C  
ATOM   1101  CD  LYS A 136      25.018  29.299  90.446  1.00 80.80           C  
ANISOU 1101  CD  LYS A 136     8696  11765  10239   -894   2293   -406       C  
ATOM   1102  CE  LYS A 136      25.783  27.950  90.447  1.00 85.88           C  
ANISOU 1102  CE  LYS A 136     9110  12411  11110   -623   2546   -458       C  
ATOM   1103  NZ  LYS A 136      26.968  27.919  89.459  1.00 93.69           N  
ANISOU 1103  NZ  LYS A 136     9935  13336  12329   -594   3215   -402       N  
ATOM   1104  N   TYR A 137      20.444  31.002  93.274  1.00 58.27           N  
ANISOU 1104  N   TYR A 137     6536   8689   6915  -1075    842   -382       N  
ATOM   1105  CA  TYR A 137      19.892  30.878  94.563  1.00 55.75           C  
ANISOU 1105  CA  TYR A 137     6210   8324   6648  -1017    603   -438       C  
ATOM   1106  C   TYR A 137      18.631  30.007  94.506  1.00 55.31           C  
ANISOU 1106  C   TYR A 137     6358   8196   6460   -857    494   -406       C  
ATOM   1107  O   TYR A 137      18.479  29.078  95.313  1.00 55.33           O  
ANISOU 1107  O   TYR A 137     6331   8221   6471   -715    376   -474       O  
ATOM   1108  CB  TYR A 137      19.559  32.240  95.115  1.00 56.42           C  
ANISOU 1108  CB  TYR A 137     6366   8259   6812  -1186    571   -409       C  
ATOM   1109  CG  TYR A 137      18.809  32.177  96.432  1.00 54.40           C  
ANISOU 1109  CG  TYR A 137     6232   7886   6551  -1128    420   -471       C  
ATOM   1110  CD1 TYR A 137      19.493  32.120  97.646  1.00 55.31           C  
ANISOU 1110  CD1 TYR A 137     6291   8045   6677  -1189    268   -598       C  
ATOM   1111  CD2 TYR A 137      17.424  32.114  96.454  1.00 51.68           C  
ANISOU 1111  CD2 TYR A 137     6067   7375   6194  -1018    429   -378       C  
ATOM   1112  CE1 TYR A 137      18.816  32.037  98.869  1.00 55.88           C  
ANISOU 1112  CE1 TYR A 137     6589   7985   6658  -1148    183   -661       C  
ATOM   1113  CE2 TYR A 137      16.734  32.053  97.664  1.00 54.22           C  
ANISOU 1113  CE2 TYR A 137     6524   7549   6528   -952    405   -426       C  
ATOM   1114  CZ  TYR A 137      17.427  32.015  98.859  1.00 55.02           C  
ANISOU 1114  CZ  TYR A 137     6671   7685   6549  -1017    312   -582       C  
ATOM   1115  OH  TYR A 137      16.707  31.925 100.015  1.00 58.32           O  
ANISOU 1115  OH  TYR A 137     7328   7930   6901   -957    346   -628       O  
ATOM   1116  N   LEU A 138      17.696  30.327  93.595  1.00 54.84           N  
ANISOU 1116  N   LEU A 138     6498   8034   6305   -900    496   -270       N  
ATOM   1117  CA  LEU A 138      16.589  29.447  93.341  1.00 52.97           C  
ANISOU 1117  CA  LEU A 138     6410   7731   5987   -802    349   -212       C  
ATOM   1118  C   LEU A 138      17.055  27.975  93.324  1.00 53.44           C  
ANISOU 1118  C   LEU A 138     6464   7887   5953   -661    365   -354       C  
ATOM   1119  O   LEU A 138      16.559  27.133  94.112  1.00 53.04           O  
ANISOU 1119  O   LEU A 138     6392   7799   5961   -532    249   -392       O  
ATOM   1120  CB  LEU A 138      15.815  29.816  92.082  1.00 53.27           C  
ANISOU 1120  CB  LEU A 138     6658   7684   5897   -912    276    -21       C  
ATOM   1121  CG  LEU A 138      15.013  31.093  92.099  1.00 54.65           C  
ANISOU 1121  CG  LEU A 138     6824   7695   6247   -993    220    197       C  
ATOM   1122  CD1 LEU A 138      14.414  31.314  90.757  1.00 54.82           C  
ANISOU 1122  CD1 LEU A 138     7059   7662   6107  -1113     73    426       C  
ATOM   1123  CD2 LEU A 138      13.904  31.163  93.191  1.00 53.29           C  
ANISOU 1123  CD2 LEU A 138     6535   7348   6365   -883    138    270       C  
ATOM   1124  N   TYR A 139      18.021  27.665  92.464  1.00 54.96           N  
ANISOU 1124  N   TYR A 139     6685   8167   6028   -674    565   -423       N  
ATOM   1125  CA  TYR A 139      18.452  26.277  92.281  1.00 54.31           C  
ANISOU 1125  CA  TYR A 139     6640   8110   5885   -523    664   -549       C  
ATOM   1126  C   TYR A 139      19.085  25.698  93.507  1.00 53.47           C  
ANISOU 1126  C   TYR A 139     6241   8070   6004   -357    626   -620       C  
ATOM   1127  O   TYR A 139      19.029  24.510  93.690  1.00 54.86           O  
ANISOU 1127  O   TYR A 139     6450   8210   6183   -199    619   -682       O  
ATOM   1128  CB  TYR A 139      19.418  26.193  91.131  1.00 55.64           C  
ANISOU 1128  CB  TYR A 139     6909   8307   5924   -557   1008   -599       C  
ATOM   1129  CG  TYR A 139      20.461  25.105  91.099  1.00 57.06           C  
ANISOU 1129  CG  TYR A 139     6966   8501   6211   -369   1293   -723       C  
ATOM   1130  CD1 TYR A 139      20.269  23.954  90.330  1.00 57.30           C  
ANISOU 1130  CD1 TYR A 139     7343   8409   6021   -294   1449   -831       C  
ATOM   1131  CD2 TYR A 139      21.713  25.268  91.723  1.00 57.25           C  
ANISOU 1131  CD2 TYR A 139     6535   8628   6588   -284   1435   -714       C  
ATOM   1132  CE1 TYR A 139      21.272  22.977  90.199  1.00 55.63           C  
ANISOU 1132  CE1 TYR A 139     7036   8146   5957    -91   1822   -935       C  
ATOM   1133  CE2 TYR A 139      22.720  24.273  91.599  1.00 56.15           C  
ANISOU 1133  CE2 TYR A 139     6214   8466   6655    -78   1747   -769       C  
ATOM   1134  CZ  TYR A 139      22.470  23.121  90.843  1.00 57.62           C  
ANISOU 1134  CZ  TYR A 139     6762   8497   6632     42   1978   -884       C  
ATOM   1135  OH  TYR A 139      23.457  22.121  90.692  1.00 62.81           O  
ANISOU 1135  OH  TYR A 139     7258   9065   7543    284   2378   -933       O  
ATOM   1136  N   GLU A 140      19.695  26.492  94.346  1.00 53.15           N  
ANISOU 1136  N   GLU A 140     5949   8107   6140   -410    573   -602       N  
ATOM   1137  CA  GLU A 140      20.353  25.873  95.449  1.00 55.88           C  
ANISOU 1137  CA  GLU A 140     6057   8520   6657   -279    461   -633       C  
ATOM   1138  C   GLU A 140      19.360  25.561  96.572  1.00 54.94           C  
ANISOU 1138  C   GLU A 140     6071   8322   6481   -218    223   -623       C  
ATOM   1139  O   GLU A 140      19.488  24.527  97.199  1.00 56.09           O  
ANISOU 1139  O   GLU A 140     6174   8470   6669    -53    143   -630       O  
ATOM   1140  CB  GLU A 140      21.506  26.720  95.931  1.00 59.16           C  
ANISOU 1140  CB  GLU A 140     6160   9042   7276   -402    428   -611       C  
ATOM   1141  CG  GLU A 140      22.792  25.864  96.294  1.00 67.14           C  
ANISOU 1141  CG  GLU A 140     6789  10151   8569   -250    429   -582       C  
ATOM   1142  CD  GLU A 140      23.691  25.477  95.098  1.00 67.33           C  
ANISOU 1142  CD  GLU A 140     6640  10181   8761   -162    842   -573       C  
ATOM   1143  OE1 GLU A 140      24.212  26.408  94.494  1.00 73.89           O  
ANISOU 1143  OE1 GLU A 140     7367  11039   9669   -330   1029   -545       O  
ATOM   1144  OE2 GLU A 140      23.897  24.277  94.795  1.00 64.28           O  
ANISOU 1144  OE2 GLU A 140     6242   9739   8442     72   1024   -591       O  
ATOM   1145  N   ILE A 141      18.336  26.391  96.786  1.00 53.37           N  
ANISOU 1145  N   ILE A 141     6043   8018   6216   -328    164   -581       N  
ATOM   1146  CA  ILE A 141      17.404  26.102  97.851  1.00 52.45           C  
ANISOU 1146  CA  ILE A 141     6058   7788   6082   -258     54   -559       C  
ATOM   1147  C   ILE A 141      16.510  24.909  97.433  1.00 52.04           C  
ANISOU 1147  C   ILE A 141     6116   7645   6012   -127     51   -529       C  
ATOM   1148  O   ILE A 141      16.212  23.971  98.229  1.00 50.12           O  
ANISOU 1148  O   ILE A 141     5915   7346   5783      8     -5   -524       O  
ATOM   1149  CB  ILE A 141      16.482  27.295  98.133  1.00 51.95           C  
ANISOU 1149  CB  ILE A 141     6127   7570   6041   -378     94   -501       C  
ATOM   1150  CG1 ILE A 141      17.298  28.515  98.585  1.00 51.83           C  
ANISOU 1150  CG1 ILE A 141     6077   7585   6031   -552     97   -558       C  
ATOM   1151  CG2 ILE A 141      15.471  26.914  99.184  1.00 49.34           C  
ANISOU 1151  CG2 ILE A 141     5946   7077   5726   -282     97   -465       C  
ATOM   1152  CD1 ILE A 141      18.116  28.261  99.717  1.00 45.83           C  
ANISOU 1152  CD1 ILE A 141     5296   6904   5214   -564    -57   -636       C  
ATOM   1153  N   ALA A 142      16.119  24.949  96.169  1.00 50.88           N  
ANISOU 1153  N   ALA A 142     6049   7469   5813   -197     91   -498       N  
ATOM   1154  CA  ALA A 142      15.106  24.041  95.684  1.00 49.97           C  
ANISOU 1154  CA  ALA A 142     6078   7230   5679   -167     15   -457       C  
ATOM   1155  C   ALA A 142      15.678  22.599  95.527  1.00 51.60           C  
ANISOU 1155  C   ALA A 142     6326   7447   5833    -24     69   -572       C  
ATOM   1156  O   ALA A 142      14.975  21.618  95.744  1.00 51.05           O  
ANISOU 1156  O   ALA A 142     6343   7250   5801     42     -1   -561       O  
ATOM   1157  CB  ALA A 142      14.537  24.565  94.387  1.00 48.89           C  
ANISOU 1157  CB  ALA A 142     6076   7049   5450   -336    -43   -368       C  
ATOM   1158  N   ARG A 143      16.969  22.473  95.175  1.00 53.39           N  
ANISOU 1158  N   ARG A 143     6465   7788   6033     32    232   -664       N  
ATOM   1159  CA  ARG A 143      17.553  21.143  95.052  1.00 53.73           C  
ANISOU 1159  CA  ARG A 143     6525   7785   6103    209    356   -753       C  
ATOM   1160  C   ARG A 143      17.823  20.520  96.411  1.00 53.82           C  
ANISOU 1160  C   ARG A 143     6363   7805   6281    393    259   -709       C  
ATOM   1161  O   ARG A 143      17.884  19.297  96.509  1.00 56.31           O  
ANISOU 1161  O   ARG A 143     6729   8013   6655    556    309   -735       O  
ATOM   1162  CB  ARG A 143      18.813  21.152  94.177  1.00 55.87           C  
ANISOU 1162  CB  ARG A 143     6733   8121   6375    241    652   -830       C  
ATOM   1163  CG  ARG A 143      20.027  21.802  94.850  1.00 56.71           C  
ANISOU 1163  CG  ARG A 143     6439   8393   6715    285    682   -774       C  
ATOM   1164  CD  ARG A 143      20.968  22.227  93.820  1.00 55.19           C  
ANISOU 1164  CD  ARG A 143     6181   8243   6544    235   1006   -805       C  
ATOM   1165  NE  ARG A 143      21.686  21.092  93.301  1.00 56.59           N  
ANISOU 1165  NE  ARG A 143     6356   8317   6828    438   1340   -872       N  
ATOM   1166  CZ  ARG A 143      22.979  20.880  93.499  1.00 61.57           C  
ANISOU 1166  CZ  ARG A 143     6581   8990   7824    599   1552   -814       C  
ATOM   1167  NH1 ARG A 143      23.682  21.762  94.196  1.00 58.99           N  
ANISOU 1167  NH1 ARG A 143     5831   8832   7751    523   1378   -692       N  
ATOM   1168  NH2 ARG A 143      23.576  19.792  92.983  1.00 63.36           N  
ANISOU 1168  NH2 ARG A 143     6820   9056   8200    826   1945   -866       N  
ATOM   1169  N   ARG A 144      18.012  21.319  97.463  1.00 52.62           N  
ANISOU 1169  N   ARG A 144     6061   7752   6180    357    118   -640       N  
ATOM   1170  CA  ARG A 144      18.113  20.753  98.798  1.00 51.34           C  
ANISOU 1170  CA  ARG A 144     5855   7578   6075    489    -28   -573       C  
ATOM   1171  C   ARG A 144      16.770  20.670  99.464  1.00 50.41           C  
ANISOU 1171  C   ARG A 144     5953   7313   5888    464    -89   -519       C  
ATOM   1172  O   ARG A 144      16.626  19.993 100.497  1.00 50.66           O  
ANISOU 1172  O   ARG A 144     6051   7279   5917    580   -158   -452       O  
ATOM   1173  CB  ARG A 144      19.020  21.595  99.666  1.00 52.33           C  
ANISOU 1173  CB  ARG A 144     5803   7853   6228    418   -184   -531       C  
ATOM   1174  CG  ARG A 144      20.416  21.604  99.191  1.00 53.37           C  
ANISOU 1174  CG  ARG A 144     5609   8116   6553    455   -132   -524       C  
ATOM   1175  CD  ARG A 144      21.169  22.734  99.855  1.00 53.21           C  
ANISOU 1175  CD  ARG A 144     5417   8232   6569    271   -335   -488       C  
ATOM   1176  NE  ARG A 144      22.579  22.624  99.573  1.00 53.55           N  
ANISOU 1176  NE  ARG A 144     5038   8389   6919    318   -321   -419       N  
ATOM   1177  CZ  ARG A 144      23.123  23.057  98.453  1.00 54.80           C  
ANISOU 1177  CZ  ARG A 144     5022   8582   7218    265    -39   -457       C  
ATOM   1178  NH1 ARG A 144      22.352  23.623  97.549  1.00 54.94           N  
ANISOU 1178  NH1 ARG A 144     5304   8542   7027    151    172   -557       N  
ATOM   1179  NH2 ARG A 144      24.410  22.932  98.239  1.00 55.88           N  
ANISOU 1179  NH2 ARG A 144     4718   8792   7722    325     38   -362       N  
ATOM   1180  N   HIS A 145      15.768  21.380  98.937  1.00 49.63           N  
ANISOU 1180  N   HIS A 145     5951   7139   5765    318    -52   -508       N  
ATOM   1181  CA  HIS A 145      14.393  21.221  99.475  1.00 47.44           C  
ANISOU 1181  CA  HIS A 145     5802   6674   5549    313    -46   -414       C  
ATOM   1182  C   HIS A 145      13.415  20.893  98.385  1.00 48.17           C  
ANISOU 1182  C   HIS A 145     5938   6644   5720    230    -70   -379       C  
ATOM   1183  O   HIS A 145      12.743  21.738  97.839  1.00 49.35           O  
ANISOU 1183  O   HIS A 145     6070   6756   5926     94   -100   -304       O  
ATOM   1184  CB  HIS A 145      13.969  22.419 100.303  1.00 47.19           C  
ANISOU 1184  CB  HIS A 145     5821   6598   5512    229      8   -363       C  
ATOM   1185  CG  HIS A 145      14.997  22.845 101.324  1.00 50.73           C  
ANISOU 1185  CG  HIS A 145     6305   7162   5809    224    -53   -418       C  
ATOM   1186  ND1 HIS A 145      14.864  22.606 102.683  1.00 48.39           N  
ANISOU 1186  ND1 HIS A 145     6210   6785   5392    276    -54   -382       N  
ATOM   1187  CD2 HIS A 145      16.175  23.507 101.169  1.00 50.22           C  
ANISOU 1187  CD2 HIS A 145     6116   7274   5690    137   -147   -489       C  
ATOM   1188  CE1 HIS A 145      15.928  23.080 103.309  1.00 50.44           C  
ANISOU 1188  CE1 HIS A 145     6492   7177   5495    201   -218   -432       C  
ATOM   1189  NE2 HIS A 145      16.731  23.645 102.408  1.00 52.30           N  
ANISOU 1189  NE2 HIS A 145     6488   7570   5815    113   -279   -492       N  
ATOM   1190  N   PRO A 146      13.273  19.623  98.061  1.00 49.62           N  
ANISOU 1190  N   PRO A 146     6198   6733   5922    295    -91   -411       N  
ATOM   1191  CA  PRO A 146      12.540  19.373  96.833  1.00 50.01           C  
ANISOU 1191  CA  PRO A 146     6348   6681   5970    140   -193   -408       C  
ATOM   1192  C   PRO A 146      11.010  19.481  96.906  1.00 50.94           C  
ANISOU 1192  C   PRO A 146     6419   6614   6321     22   -315   -223       C  
ATOM   1193  O   PRO A 146      10.323  19.231  95.915  1.00 52.85           O  
ANISOU 1193  O   PRO A 146     6737   6760   6585   -152   -508   -179       O  
ATOM   1194  CB  PRO A 146      13.016  17.983  96.439  1.00 52.28           C  
ANISOU 1194  CB  PRO A 146     6787   6889   6188    228   -145   -541       C  
ATOM   1195  CG  PRO A 146      13.264  17.301  97.770  1.00 51.54           C  
ANISOU 1195  CG  PRO A 146     6618   6757   6208    443    -68   -497       C  
ATOM   1196  CD  PRO A 146      13.653  18.390  98.768  1.00 50.55           C  
ANISOU 1196  CD  PRO A 146     6352   6790   6065    481    -51   -430       C  
ATOM   1197  N   TYR A 147      10.449  19.905  98.014  1.00 49.60           N  
ANISOU 1197  N   TYR A 147     6134   6372   6341     91   -206    -93       N  
ATOM   1198  CA  TYR A 147       9.018  20.119  98.024  1.00 49.83           C  
ANISOU 1198  CA  TYR A 147     6028   6198   6706     -4   -254    128       C  
ATOM   1199  C   TYR A 147       8.796  21.562  98.501  1.00 50.32           C  
ANISOU 1199  C   TYR A 147     5978   6260   6882      6    -99    235       C  
ATOM   1200  O   TYR A 147       7.707  21.938  98.953  1.00 50.43           O  
ANISOU 1200  O   TYR A 147     5841   6069   7251     13     25    442       O  
ATOM   1201  CB  TYR A 147       8.324  19.166  98.996  1.00 50.17           C  
ANISOU 1201  CB  TYR A 147     6054   6038   6972     92   -123    219       C  
ATOM   1202  CG  TYR A 147       8.289  17.682  98.678  1.00 51.03           C  
ANISOU 1202  CG  TYR A 147     6272   6046   7072     78   -236    151       C  
ATOM   1203  CD1 TYR A 147       9.349  16.867  99.003  1.00 55.00           C  
ANISOU 1203  CD1 TYR A 147     6942   6622   7331    234   -157    -20       C  
ATOM   1204  CD2 TYR A 147       7.143  17.077  98.114  1.00 54.88           C  
ANISOU 1204  CD2 TYR A 147     6677   6319   7856   -100   -429    287       C  
ATOM   1205  CE1 TYR A 147       9.302  15.493  98.769  1.00 56.92           C  
ANISOU 1205  CE1 TYR A 147     7314   6710   7604    243   -200    -79       C  
ATOM   1206  CE2 TYR A 147       7.070  15.734  97.889  1.00 54.32           C  
ANISOU 1206  CE2 TYR A 147     6750   6100   7788   -142   -513    210       C  
ATOM   1207  CZ  TYR A 147       8.169  14.930  98.225  1.00 57.33           C  
ANISOU 1207  CZ  TYR A 147     7345   6536   7901     47   -362     12       C  
ATOM   1208  OH  TYR A 147       8.165  13.547  98.021  1.00 59.45           O  
ANISOU 1208  OH  TYR A 147     7794   6607   8187     34   -387    -76       O  
ATOM   1209  N   PHE A 148       9.830  22.392  98.412  1.00 54.03           N  
ANISOU 1209  N   PHE A 148     7533   7233   5761  -1205    433   -211       N  
ATOM   1210  CA  PHE A 148       9.622  23.804  98.735  1.00 55.32           C  
ANISOU 1210  CA  PHE A 148     7699   7375   5946  -1225    383   -202       C  
ATOM   1211  C   PHE A 148       8.464  24.489  97.994  1.00 54.81           C  
ANISOU 1211  C   PHE A 148     7762   7157   5907  -1279    225    -96       C  
ATOM   1212  O   PHE A 148       8.287  24.318  96.823  1.00 55.19           O  
ANISOU 1212  O   PHE A 148     7991   7127   5851  -1395    159    -38       O  
ATOM   1213  CB  PHE A 148      10.854  24.580  98.414  1.00 57.15           C  
ANISOU 1213  CB  PHE A 148     7968   7624   6122  -1320    495   -269       C  
ATOM   1214  CG  PHE A 148      11.043  25.760  99.280  1.00 60.31           C  
ANISOU 1214  CG  PHE A 148     8285   8048   6583  -1313    491   -306       C  
ATOM   1215  CD1 PHE A 148      10.368  26.941  99.028  1.00 61.43           C  
ANISOU 1215  CD1 PHE A 148     8497   8063   6781  -1351    413   -270       C  
ATOM   1216  CD2 PHE A 148      11.902  25.698 100.354  1.00 58.92           C  
ANISOU 1216  CD2 PHE A 148     7957   8001   6429  -1291    550   -369       C  
ATOM   1217  CE1 PHE A 148      10.562  28.029  99.832  1.00 56.81           C  
ANISOU 1217  CE1 PHE A 148     7841   7470   6274  -1355    443   -342       C  
ATOM   1218  CE2 PHE A 148      12.106  26.791 101.128  1.00 55.58           C  
ANISOU 1218  CE2 PHE A 148     7496   7594   6026  -1326    550   -431       C  
ATOM   1219  CZ  PHE A 148      11.437  27.943 100.864  1.00 57.48           C  
ANISOU 1219  CZ  PHE A 148     7817   7698   6323  -1352    519   -439       C  
ATOM   1220  N   TYR A 149       7.669  25.254  98.730  1.00 55.69           N  
ANISOU 1220  N   TYR A 149     7769   7214   6178  -1211    168    -68       N  
ATOM   1221  CA  TYR A 149       6.568  26.077  98.205  1.00 55.09           C  
ANISOU 1221  CA  TYR A 149     7728   6947   6255  -1245      8     62       C  
ATOM   1222  C   TYR A 149       7.178  27.080  97.249  1.00 55.36           C  
ANISOU 1222  C   TYR A 149     7915   6907   6212  -1396    -23     98       C  
ATOM   1223  O   TYR A 149       8.015  27.902  97.643  1.00 56.91           O  
ANISOU 1223  O   TYR A 149     8078   7137   6407  -1410     93      1       O  
ATOM   1224  CB  TYR A 149       5.907  26.738  99.401  1.00 54.44           C  
ANISOU 1224  CB  TYR A 149     7461   6817   6407  -1132     67     14       C  
ATOM   1225  CG  TYR A 149       4.602  27.405  99.121  1.00 56.28           C  
ANISOU 1225  CG  TYR A 149     7628   6814   6941  -1117    -70    157       C  
ATOM   1226  CD1 TYR A 149       3.831  27.028  98.031  1.00 55.87           C  
ANISOU 1226  CD1 TYR A 149     7655   6641   6932  -1185   -305    363       C  
ATOM   1227  CD2 TYR A 149       4.087  28.343 100.006  1.00 56.46           C  
ANISOU 1227  CD2 TYR A 149     7495   6718   7241  -1044     40     85       C  
ATOM   1228  CE1 TYR A 149       2.649  27.606  97.790  1.00 59.72           C  
ANISOU 1228  CE1 TYR A 149     8037   6892   7761  -1178   -470    539       C  
ATOM   1229  CE2 TYR A 149       2.864  28.934  99.787  1.00 58.39           C  
ANISOU 1229  CE2 TYR A 149     7615   6698   7873  -1012    -63    227       C  
ATOM   1230  CZ  TYR A 149       2.162  28.579  98.641  1.00 60.14           C  
ANISOU 1230  CZ  TYR A 149     7888   6797   8167  -1078   -347    482       C  
ATOM   1231  OH  TYR A 149       0.955  29.131  98.361  1.00 56.97           O  
ANISOU 1231  OH  TYR A 149     7329   6111   8206  -1061   -507    681       O  
ATOM   1232  N   ALA A 150       6.789  27.000  95.990  1.00 55.58           N  
ANISOU 1232  N   ALA A 150     8126   6839   6153  -1540   -189    247       N  
ATOM   1233  CA  ALA A 150       7.597  27.548  94.885  1.00 56.29           C  
ANISOU 1233  CA  ALA A 150     8434   6916   6040  -1743   -184    279       C  
ATOM   1234  C   ALA A 150       7.424  29.072  94.608  1.00 57.93           C  
ANISOU 1234  C   ALA A 150     8643   6962   6405  -1825   -303    407       C  
ATOM   1235  O   ALA A 150       8.408  29.760  94.219  1.00 57.96           O  
ANISOU 1235  O   ALA A 150     8742   6989   6291  -1940   -208    373       O  
ATOM   1236  CB  ALA A 150       7.356  26.810  93.668  1.00 57.02           C  
ANISOU 1236  CB  ALA A 150     8773   6992   5901  -1922   -295    369       C  
ATOM   1237  N   PRO A 151       6.174  29.592  94.752  1.00 58.31           N  
ANISOU 1237  N   PRO A 151     8570   6820   6765  -1774   -507    573       N  
ATOM   1238  CA  PRO A 151       5.957  31.036  94.701  1.00 59.55           C  
ANISOU 1238  CA  PRO A 151     8653   6777   7195  -1809   -598    686       C  
ATOM   1239  C   PRO A 151       6.579  31.750  95.864  1.00 58.11           C  
ANISOU 1239  C   PRO A 151     8303   6623   7153  -1676   -357    464       C  
ATOM   1240  O   PRO A 151       6.832  32.942  95.741  1.00 58.13           O  
ANISOU 1240  O   PRO A 151     8288   6490   7308  -1737   -371    501       O  
ATOM   1241  CB  PRO A 151       4.438  31.174  94.757  1.00 60.22           C  
ANISOU 1241  CB  PRO A 151     8575   6635   7672  -1744   -827    891       C  
ATOM   1242  CG  PRO A 151       3.961  29.951  94.267  1.00 59.25           C  
ANISOU 1242  CG  PRO A 151     8560   6591   7363  -1790   -955    968       C  
ATOM   1243  CD  PRO A 151       4.894  28.886  94.680  1.00 58.30           C  
ANISOU 1243  CD  PRO A 151     8512   6735   6906  -1728   -699    713       C  
ATOM   1244  N   GLU A 152       6.829  31.042  96.964  1.00 55.87           N  
ANISOU 1244  N   GLU A 152     7911   6507   6810  -1527   -160    251       N  
ATOM   1245  CA  GLU A 152       7.583  31.677  98.061  1.00 57.91           C  
ANISOU 1245  CA  GLU A 152     8066   6829   7110  -1467     51     31       C  
ATOM   1246  C   GLU A 152       9.093  31.694  97.814  1.00 57.42           C  
ANISOU 1246  C   GLU A 152     8110   6930   6776  -1568    160    -61       C  
ATOM   1247  O   GLU A 152       9.815  32.572  98.262  1.00 58.26           O  
ANISOU 1247  O   GLU A 152     8178   7029   6927  -1599    255   -169       O  
ATOM   1248  CB  GLU A 152       7.226  31.128  99.453  1.00 57.65           C  
ANISOU 1248  CB  GLU A 152     7880   6894   7128  -1318    199   -138       C  
ATOM   1249  CG  GLU A 152       5.830  31.597  99.960  1.00 60.56           C  
ANISOU 1249  CG  GLU A 152     8089   7041   7882  -1219    196   -110       C  
ATOM   1250  CD  GLU A 152       5.930  32.857 100.850  1.00 68.94           C  
ANISOU 1250  CD  GLU A 152     9059   7975   9162  -1211    375   -295       C  
ATOM   1251  OE1 GLU A 152       6.623  32.776 101.884  1.00 70.72           O  
ANISOU 1251  OE1 GLU A 152     9294   8377   9200  -1219    554   -516       O  
ATOM   1252  OE2 GLU A 152       5.328  33.940 100.536  1.00 72.63           O  
ANISOU 1252  OE2 GLU A 152     9444   8148  10003  -1215    330   -217       O  
ATOM   1253  N   LEU A 153       9.549  30.733  97.058  1.00 56.91           N  
ANISOU 1253  N   LEU A 153     8173   6987   6463  -1632    158    -21       N  
ATOM   1254  CA  LEU A 153      10.931  30.675  96.703  1.00 56.77           C  
ANISOU 1254  CA  LEU A 153     8230   7089   6251  -1729    295    -95       C  
ATOM   1255  C   LEU A 153      11.327  31.873  95.889  1.00 57.96           C  
ANISOU 1255  C   LEU A 153     8490   7121   6413  -1889    257     -5       C  
ATOM   1256  O   LEU A 153      12.403  32.376  96.022  1.00 59.20           O  
ANISOU 1256  O   LEU A 153     8625   7325   6543  -1944    380    -87       O  
ATOM   1257  CB  LEU A 153      11.200  29.427  95.919  1.00 56.80           C  
ANISOU 1257  CB  LEU A 153     8358   7187   6035  -1781    341    -83       C  
ATOM   1258  CG  LEU A 153      12.642  29.051  95.989  1.00 57.63           C  
ANISOU 1258  CG  LEU A 153     8430   7423   6045  -1811    557   -209       C  
ATOM   1259  CD1 LEU A 153      13.224  29.761  97.129  1.00 57.93           C  
ANISOU 1259  CD1 LEU A 153     8288   7506   6219  -1747    602   -301       C  
ATOM   1260  CD2 LEU A 153      12.742  27.618  96.180  1.00 58.66           C  
ANISOU 1260  CD2 LEU A 153     8508   7651   6129  -1728    638   -271       C  
ATOM   1261  N   LEU A 154      10.459  32.304  95.007  1.00 58.83           N  
ANISOU 1261  N   LEU A 154     8712   7068   6573  -1984     62    195       N  
ATOM   1262  CA  LEU A 154      10.738  33.522  94.217  1.00 58.87           C  
ANISOU 1262  CA  LEU A 154     8818   6935   6614  -2158    -17    335       C  
ATOM   1263  C   LEU A 154      10.758  34.766  95.141  1.00 58.93           C  
ANISOU 1263  C   LEU A 154     8636   6809   6944  -2072     10    261       C  
ATOM   1264  O   LEU A 154      11.615  35.629  95.002  1.00 59.04           O  
ANISOU 1264  O   LEU A 154     8669   6796   6967  -2170     75    242       O  
ATOM   1265  CB  LEU A 154       9.707  33.690  93.103  1.00 59.59           C  
ANISOU 1265  CB  LEU A 154     9061   6866   6715  -2307   -301    624       C  
ATOM   1266  CG  LEU A 154       9.407  32.544  92.115  1.00 59.80           C  
ANISOU 1266  CG  LEU A 154     9323   6980   6419  -2446   -386    714       C  
ATOM   1267  CD1 LEU A 154       8.055  32.779  91.430  1.00 59.08           C  
ANISOU 1267  CD1 LEU A 154     9290   6695   6464  -2551   -757   1025       C  
ATOM   1268  CD2 LEU A 154      10.477  32.439  91.073  1.00 57.74           C  
ANISOU 1268  CD2 LEU A 154     9332   6825   5782  -2693   -246    699       C  
ATOM   1269  N   TYR A 155       9.781  34.843  96.054  1.00 58.63           N  
ANISOU 1269  N   TYR A 155     8424   6672   7180  -1906    -19    209       N  
ATOM   1270  CA  TYR A 155       9.712  35.863  97.105  1.00 59.34           C  
ANISOU 1270  CA  TYR A 155     8345   6633   7570  -1821     76     61       C  
ATOM   1271  C   TYR A 155      11.048  36.001  97.836  1.00 59.33           C  
ANISOU 1271  C   TYR A 155     8329   6806   7409  -1842    269   -167       C  
ATOM   1272  O   TYR A 155      11.632  37.092  97.879  1.00 60.92           O  
ANISOU 1272  O   TYR A 155     8518   6906   7723  -1923    302   -204       O  
ATOM   1273  CB  TYR A 155       8.580  35.528  98.124  1.00 59.59           C  
ANISOU 1273  CB  TYR A 155     8212   6603   7828  -1643    122    -36       C  
ATOM   1274  CG  TYR A 155       8.657  36.402  99.339  1.00 60.24           C  
ANISOU 1274  CG  TYR A 155     8166   6597   8126  -1588    307   -276       C  
ATOM   1275  CD1 TYR A 155       8.436  37.783  99.245  1.00 64.42           C  
ANISOU 1275  CD1 TYR A 155     8625   6831   9020  -1625    295   -252       C  
ATOM   1276  CD2 TYR A 155       9.025  35.871 100.573  1.00 60.36           C  
ANISOU 1276  CD2 TYR A 155     8150   6818   7967  -1533    491   -527       C  
ATOM   1277  CE1 TYR A 155       8.598  38.601 100.369  1.00 66.66           C  
ANISOU 1277  CE1 TYR A 155     8826   7024   9476  -1607    504   -527       C  
ATOM   1278  CE2 TYR A 155       9.205  36.671 101.677  1.00 61.33           C  
ANISOU 1278  CE2 TYR A 155     8219   6883   8199  -1547    667   -774       C  
ATOM   1279  CZ  TYR A 155       8.974  38.015 101.579  1.00 64.23           C  
ANISOU 1279  CZ  TYR A 155     8534   6954   8919  -1581    693   -797       C  
ATOM   1280  OH  TYR A 155       9.122  38.765 102.698  1.00 66.47           O  
ANISOU 1280  OH  TYR A 155     8790   7168   9299  -1615    900  -1085       O  
ATOM   1281  N   TYR A 156      11.518  34.899  98.434  1.00 58.75           N  
ANISOU 1281  N   TYR A 156     8238   6977   7109  -1780    373   -298       N  
ATOM   1282  CA  TYR A 156      12.770  34.911  99.185  1.00 59.04           C  
ANISOU 1282  CA  TYR A 156     8229   7180   7023  -1815    503   -470       C  
ATOM   1283  C   TYR A 156      13.894  35.185  98.283  1.00 59.49           C  
ANISOU 1283  C   TYR A 156     8364   7265   6974  -1953    528   -398       C  
ATOM   1284  O   TYR A 156      14.823  35.843  98.694  1.00 60.87           O  
ANISOU 1284  O   TYR A 156     8489   7457   7181  -2023    590   -490       O  
ATOM   1285  CB  TYR A 156      13.080  33.596  99.848  1.00 58.59           C  
ANISOU 1285  CB  TYR A 156     8120   7358   6785  -1742    561   -547       C  
ATOM   1286  CG  TYR A 156      12.191  33.298 101.002  1.00 60.02           C  
ANISOU 1286  CG  TYR A 156     8222   7562   7022  -1636    580   -650       C  
ATOM   1287  CD1 TYR A 156      12.202  34.094 102.126  1.00 60.59           C  
ANISOU 1287  CD1 TYR A 156     8248   7603   7171  -1663    655   -827       C  
ATOM   1288  CD2 TYR A 156      11.357  32.214 100.967  1.00 57.08           C  
ANISOU 1288  CD2 TYR A 156     7837   7238   6611  -1533    545   -584       C  
ATOM   1289  CE1 TYR A 156      11.386  33.827 103.161  1.00 61.46           C  
ANISOU 1289  CE1 TYR A 156     8316   7736   7301  -1600    723   -938       C  
ATOM   1290  CE2 TYR A 156      10.547  31.941 101.995  1.00 57.92           C  
ANISOU 1290  CE2 TYR A 156     7873   7366   6769  -1452    590   -668       C  
ATOM   1291  CZ  TYR A 156      10.553  32.748 103.089  1.00 60.11           C  
ANISOU 1291  CZ  TYR A 156     8118   7618   7104  -1490    694   -848       C  
ATOM   1292  OH  TYR A 156       9.730  32.442 104.143  1.00 59.65           O  
ANISOU 1292  OH  TYR A 156     8015   7589   7061  -1439    789   -953       O  
ATOM   1293  N   ALA A 157      13.857  34.666  97.067  1.00 59.60           N  
ANISOU 1293  N   ALA A 157     8511   7288   6848  -2019    495   -246       N  
ATOM   1294  CA  ALA A 157      15.018  34.877  96.226  1.00 60.95           C  
ANISOU 1294  CA  ALA A 157     8765   7497   6897  -2174    588   -204       C  
ATOM   1295  C   ALA A 157      15.079  36.364  95.857  1.00 62.88           C  
ANISOU 1295  C   ALA A 157     9043   7552   7296  -2293    519   -116       C  
ATOM   1296  O   ALA A 157      16.155  36.969  95.825  1.00 65.20           O  
ANISOU 1296  O   ALA A 157     9311   7857   7605  -2392    611   -152       O  
ATOM   1297  CB  ALA A 157      15.009  33.967  95.038  1.00 60.80           C  
ANISOU 1297  CB  ALA A 157     8921   7533   6648  -2260    622   -105       C  
ATOM   1298  N   ASN A 158      13.937  37.006  95.674  1.00 63.29           N  
ANISOU 1298  N   ASN A 158     9114   7404   7529  -2278    351      6       N  
ATOM   1299  CA  ASN A 158      13.997  38.460  95.578  1.00 66.03           C  
ANISOU 1299  CA  ASN A 158     9434   7536   8119  -2362    289     71       C  
ATOM   1300  C   ASN A 158      14.436  39.188  96.851  1.00 66.00           C  
ANISOU 1300  C   ASN A 158     9270   7497   8309  -2299    390   -161       C  
ATOM   1301  O   ASN A 158      15.043  40.262  96.776  1.00 67.29           O  
ANISOU 1301  O   ASN A 158     9418   7544   8605  -2404    402   -159       O  
ATOM   1302  CB  ASN A 158      12.683  39.049  95.068  1.00 67.85           C  
ANISOU 1302  CB  ASN A 158     9675   7504   8602  -2368     69    292       C  
ATOM   1303  CG  ASN A 158      12.380  38.653  93.626  1.00 71.14           C  
ANISOU 1303  CG  ASN A 158    10304   7926   8800  -2538    -96    577       C  
ATOM   1304  OD1 ASN A 158      13.250  38.656  92.726  1.00 70.43           O  
ANISOU 1304  OD1 ASN A 158    10389   7928   8442  -2734    -42    657       O  
ATOM   1305  ND2 ASN A 158      11.131  38.256  93.410  1.00 75.60           N  
ANISOU 1305  ND2 ASN A 158    10867   8396   9462  -2486   -287    726       N  
ATOM   1306  N   LYS A 159      14.096  38.647  98.021  1.00 65.05           N  
ANISOU 1306  N   LYS A 159     9052   7469   8196  -2157    457   -358       N  
ATOM   1307  CA  LYS A 159      14.467  39.316  99.260  1.00 65.54           C  
ANISOU 1307  CA  LYS A 159     9017   7509   8377  -2152    550   -596       C  
ATOM   1308  C   LYS A 159      15.962  39.351  99.346  1.00 65.03           C  
ANISOU 1308  C   LYS A 159     8945   7603   8161  -2269    611   -653       C  
ATOM   1309  O   LYS A 159      16.574  40.250  99.973  1.00 67.16           O  
ANISOU 1309  O   LYS A 159     9169   7811   8536  -2354    643   -787       O  
ATOM   1310  CB  LYS A 159      13.888  38.608 100.469  1.00 64.87           C  
ANISOU 1310  CB  LYS A 159     8872   7535   8241  -2032    618   -781       C  
ATOM   1311  CG  LYS A 159      12.450  39.001 100.741  1.00 68.80           C  
ANISOU 1311  CG  LYS A 159     9317   7798   9025  -1927    623   -801       C  
ATOM   1312  CD  LYS A 159      12.323  40.511 100.978  1.00 72.96           C  
ANISOU 1312  CD  LYS A 159     9796   8025   9900  -1983    671   -895       C  
ATOM   1313  CE  LYS A 159      10.905  41.006 100.633  1.00 78.78           C  
ANISOU 1313  CE  LYS A 159    10440   8430  11062  -1887    628   -776       C  
ATOM   1314  NZ  LYS A 159      10.387  42.074 101.550  1.00 79.46           N  
ANISOU 1314  NZ  LYS A 159    10424   8230  11537  -1867    805  -1016       N  
ATOM   1315  N   TYR A 160      16.525  38.370  98.674  1.00 63.01           N  
ANISOU 1315  N   TYR A 160     8726   7525   7690  -2283    634   -549       N  
ATOM   1316  CA  TYR A 160      17.912  37.995  98.744  1.00 63.10           C  
ANISOU 1316  CA  TYR A 160     8678   7706   7590  -2360    718   -582       C  
ATOM   1317  C   TYR A 160      18.766  38.906  97.890  1.00 64.13           C  
ANISOU 1317  C   TYR A 160     8842   7739   7787  -2519    753   -484       C  
ATOM   1318  O   TYR A 160      19.720  39.537  98.367  1.00 64.76           O  
ANISOU 1318  O   TYR A 160     8831   7817   7958  -2610    776   -558       O  
ATOM   1319  CB  TYR A 160      18.018  36.589  98.160  1.00 62.57           C  
ANISOU 1319  CB  TYR A 160     8636   7798   7339  -2307    779   -508       C  
ATOM   1320  CG  TYR A 160      19.344  35.964  98.323  1.00 63.08           C  
ANISOU 1320  CG  TYR A 160     8578   8015   7374  -2347    886   -539       C  
ATOM   1321  CD1 TYR A 160      19.782  35.569  99.590  1.00 63.23           C  
ANISOU 1321  CD1 TYR A 160     8440   8163   7423  -2309    843   -641       C  
ATOM   1322  CD2 TYR A 160      20.193  35.792  97.223  1.00 63.41           C  
ANISOU 1322  CD2 TYR A 160     8652   8059   7381  -2448   1036   -453       C  
ATOM   1323  CE1 TYR A 160      21.018  34.977  99.743  1.00 67.41           C  
ANISOU 1323  CE1 TYR A 160     8804   8802   8009  -2350    904   -620       C  
ATOM   1324  CE2 TYR A 160      21.430  35.188  97.371  1.00 64.74           C  
ANISOU 1324  CE2 TYR A 160     8651   8328   7621  -2472   1166   -475       C  
ATOM   1325  CZ  TYR A 160      21.833  34.798  98.619  1.00 65.25           C  
ANISOU 1325  CZ  TYR A 160     8518   8497   7778  -2414   1078   -541       C  
ATOM   1326  OH  TYR A 160      23.042  34.227  98.787  1.00 69.88           O  
ANISOU 1326  OH  TYR A 160     8889   9148   8514  -2442   1164   -517       O  
ATOM   1327  N   ASN A 161      18.459  38.958  96.607  1.00 64.34           N  
ANISOU 1327  N   ASN A 161     9009   7688   7749  -2585    747   -301       N  
ATOM   1328  CA  ASN A 161      19.059  40.058  95.801  1.00 66.21           C  
ANISOU 1328  CA  ASN A 161     9302   7791   8065  -2764    758   -178       C  
ATOM   1329  C   ASN A 161      18.889  41.407  96.509  1.00 65.74           C  
ANISOU 1329  C   ASN A 161     9164   7531   8285  -2778    668   -248       C  
ATOM   1330  O   ASN A 161      19.734  42.234  96.396  1.00 66.04           O  
ANISOU 1330  O   ASN A 161     9166   7502   8423  -2905    699   -234       O  
ATOM   1331  CB  ASN A 161      18.547  40.086  94.346  1.00 66.78           C  
ANISOU 1331  CB  ASN A 161     9583   7785   8003  -2885    710     63       C  
ATOM   1332  CG  ASN A 161      19.185  38.996  93.467  1.00 69.07           C  
ANISOU 1332  CG  ASN A 161     9987   8252   8003  -2970    894     92       C  
ATOM   1333  OD1 ASN A 161      19.578  37.931  93.943  1.00 68.23           O  
ANISOU 1333  OD1 ASN A 161     9786   8307   7831  -2863   1020    -48       O  
ATOM   1334  ND2 ASN A 161      19.279  39.270  92.160  1.00 72.21           N  
ANISOU 1334  ND2 ASN A 161    10598   8603   8236  -3185    920    280       N  
ATOM   1335  N   GLY A 162      17.804  41.575  97.266  1.00 66.50           N  
ANISOU 1335  N   GLY A 162     9225   7522   8522  -2650    588   -343       N  
ATOM   1336  CA  GLY A 162      17.509  42.803  98.081  1.00 68.35           C  
ANISOU 1336  CA  GLY A 162     9383   7528   9059  -2653    560   -481       C  
ATOM   1337  C   GLY A 162      18.580  43.153  99.122  1.00 69.77           C  
ANISOU 1337  C   GLY A 162     9479   7789   9240  -2727    629   -705       C  
ATOM   1338  O   GLY A 162      19.034  44.321  99.250  1.00 72.03           O  
ANISOU 1338  O   GLY A 162     9736   7901   9729  -2842    622   -750       O  
ATOM   1339  N   VAL A 163      19.024  42.138  99.852  1.00 68.43           N  
ANISOU 1339  N   VAL A 163     9267   7878   8856  -2686    667   -822       N  
ATOM   1340  CA  VAL A 163      20.113  42.320 100.800  1.00 69.13           C  
ANISOU 1340  CA  VAL A 163     9276   8074   8916  -2797    671   -978       C  
ATOM   1341  C   VAL A 163      21.381  42.798 100.103  1.00 69.91           C  
ANISOU 1341  C   VAL A 163     9322   8161   9080  -2945    686   -853       C  
ATOM   1342  O   VAL A 163      22.019  43.768 100.563  1.00 72.06           O  
ANISOU 1342  O   VAL A 163     9552   8336   9493  -3081    656   -944       O  
ATOM   1343  CB  VAL A 163      20.418  41.015 101.541  1.00 68.34           C  
ANISOU 1343  CB  VAL A 163     9118   8254   8594  -2745    663  -1032       C  
ATOM   1344  CG1 VAL A 163      21.477  41.280 102.541  1.00 69.48           C  
ANISOU 1344  CG1 VAL A 163     9183   8490   8727  -2900    601  -1150       C  
ATOM   1345  CG2 VAL A 163      19.155  40.445 102.217  1.00 66.88           C  
ANISOU 1345  CG2 VAL A 163     8988   8099   8323  -2608    669  -1139       C  
ATOM   1346  N   PHE A 164      21.753  42.125  99.009  1.00 68.50           N  
ANISOU 1346  N   PHE A 164     9153   8072   8803  -2939    754   -663       N  
ATOM   1347  CA  PHE A 164      22.976  42.484  98.236  1.00 70.16           C  
ANISOU 1347  CA  PHE A 164     9308   8274   9075  -3089    833   -537       C  
ATOM   1348  C   PHE A 164      22.880  43.823  97.564  1.00 72.38           C  
ANISOU 1348  C   PHE A 164     9662   8315   9525  -3207    806   -436       C  
ATOM   1349  O   PHE A 164      23.863  44.556  97.501  1.00 74.33           O  
ANISOU 1349  O   PHE A 164     9832   8503   9907  -3352    827   -413       O  
ATOM   1350  CB  PHE A 164      23.374  41.411  97.224  1.00 68.52           C  
ANISOU 1350  CB  PHE A 164     9117   8205   8713  -3078    986   -400       C  
ATOM   1351  CG  PHE A 164      23.878  40.190  97.879  1.00 67.95           C  
ANISOU 1351  CG  PHE A 164     8897   8334   8587  -2994   1024   -473       C  
ATOM   1352  CD1 PHE A 164      25.208  40.088  98.229  1.00 67.56           C  
ANISOU 1352  CD1 PHE A 164     8639   8351   8680  -3078   1067   -473       C  
ATOM   1353  CD2 PHE A 164      23.002  39.165  98.233  1.00 65.73           C  
ANISOU 1353  CD2 PHE A 164     8656   8155   8162  -2836    987   -522       C  
ATOM   1354  CE1 PHE A 164      25.666  38.980  98.882  1.00 66.80           C  
ANISOU 1354  CE1 PHE A 164     8369   8410   8602  -3009   1057   -496       C  
ATOM   1355  CE2 PHE A 164      23.458  38.056  98.915  1.00 64.23           C  
ANISOU 1355  CE2 PHE A 164     8312   8133   7960  -2767    990   -562       C  
ATOM   1356  CZ  PHE A 164      24.786  37.963  99.238  1.00 63.91           C  
ANISOU 1356  CZ  PHE A 164     8056   8147   8081  -2854   1015   -539       C  
ATOM   1357  N   GLN A 165      21.691  44.139  97.069  1.00 73.13           N  
ANISOU 1357  N   GLN A 165     9883   8255   9648  -3152    739   -350       N  
ATOM   1358  CA  GLN A 165      21.430  45.452  96.555  1.00 76.36           C  
ANISOU 1358  CA  GLN A 165    10336   8391  10286  -3254    665   -231       C  
ATOM   1359  C   GLN A 165      21.758  46.523  97.628  1.00 78.58           C  
ANISOU 1359  C   GLN A 165    10514   8516  10826  -3304    630   -437       C  
ATOM   1360  O   GLN A 165      22.489  47.421  97.299  1.00 79.63           O  
ANISOU 1360  O   GLN A 165    10615   8528  11113  -3454    628   -364       O  
ATOM   1361  CB  GLN A 165      20.018  45.556  95.971  1.00 75.87           C  
ANISOU 1361  CB  GLN A 165    10381   8163  10285  -3181    551    -78       C  
ATOM   1362  CG  GLN A 165      19.739  46.774  95.083  1.00 81.21           C  
ANISOU 1362  CG  GLN A 165    11106   8549  11201  -3316    436    169       C  
ATOM   1363  CD  GLN A 165      20.934  47.223  94.190  1.00 84.93           C  
ANISOU 1363  CD  GLN A 165    11622   9049  11598  -3542    503    343       C  
ATOM   1364  OE1 GLN A 165      20.947  46.964  92.991  1.00 87.64           O  
ANISOU 1364  OE1 GLN A 165    12120   9445  11735  -3671    503    595       O  
ATOM   1365  NE2 GLN A 165      21.929  47.880  94.785  1.00 85.79           N  
ANISOU 1365  NE2 GLN A 165    11609   9125  11862  -3613    567    205       N  
ATOM   1366  N   GLU A 166      21.244  46.391  98.872  1.00 79.46           N  
ANISOU 1366  N   GLU A 166    10593   8638  10959  -3205    618   -698       N  
ATOM   1367  CA  GLU A 166      21.557  47.276 100.031  1.00 82.26           C  
ANISOU 1367  CA  GLU A 166    10899   8874  11481  -3292    609   -961       C  
ATOM   1368  C   GLU A 166      22.929  47.046 100.639  1.00 83.88           C  
ANISOU 1368  C   GLU A 166    11022   9283  11564  -3427    596  -1046       C  
ATOM   1369  O   GLU A 166      23.599  48.005 100.991  1.00 87.47           O  
ANISOU 1369  O   GLU A 166    11438   9610  12185  -3584    562  -1131       O  
ATOM   1370  CB  GLU A 166      20.471  47.240 101.161  1.00 82.35           C  
ANISOU 1370  CB  GLU A 166    10947   8818  11526  -3186    645  -1235       C  
ATOM   1371  CG  GLU A 166      20.514  45.974 102.133  1.00 81.08           C  
ANISOU 1371  CG  GLU A 166    10797   8981  11029  -3129    660  -1387       C  
ATOM   1372  CD  GLU A 166      19.247  45.730 103.013  1.00 81.19           C  
ANISOU 1372  CD  GLU A 166    10868   8950  11030  -3012    739  -1603       C  
ATOM   1373  OE1 GLU A 166      18.600  44.636 102.877  1.00 78.68           O  
ANISOU 1373  OE1 GLU A 166    10559   8789  10549  -2861    747  -1522       O  
ATOM   1374  OE2 GLU A 166      18.920  46.603 103.866  1.00 82.36           O  
ANISOU 1374  OE2 GLU A 166    11055   8904  11334  -3085    820  -1871       O  
ATOM   1375  N   CYS A 167      23.385  45.803 100.779  1.00 83.62           N  
ANISOU 1375  N   CYS A 167    10940   9541  11290  -3379    604  -1010       N  
ATOM   1376  CA  CYS A 167      24.697  45.620 101.448  1.00 85.26           C  
ANISOU 1376  CA  CYS A 167    11021   9908  11464  -3523    545  -1057       C  
ATOM   1377  C   CYS A 167      26.003  45.699 100.651  1.00 85.91           C  
ANISOU 1377  C   CYS A 167    10965  10019  11656  -3638    585   -858       C  
ATOM   1378  O   CYS A 167      27.005  46.043 101.248  1.00 87.83           O  
ANISOU 1378  O   CYS A 167    11091  10283  11998  -3795    499   -902       O  
ATOM   1379  CB  CYS A 167      24.730  44.352 102.327  1.00 83.62           C  
ANISOU 1379  CB  CYS A 167    10772   9971  11028  -3461    493  -1126       C  
ATOM   1380  SG  CYS A 167      23.619  44.570 103.751  1.00 86.73           S  
ANISOU 1380  SG  CYS A 167    11320  10337  11297  -3457    451  -1439       S  
ATOM   1381  N   CYS A 168      26.032  45.397  99.352  1.00 85.21           N  
ANISOU 1381  N   CYS A 168    10896   9930  11552  -3592    718   -648       N  
ATOM   1382  CA  CYS A 168      27.330  45.435  98.641  1.00 87.12           C  
ANISOU 1382  CA  CYS A 168    10997  10197  11907  -3720    822   -486       C  
ATOM   1383  C   CYS A 168      27.857  46.828  98.366  1.00 89.45           C  
ANISOU 1383  C   CYS A 168    11275  10279  12433  -3899    798   -436       C  
ATOM   1384  O   CYS A 168      28.884  46.946  97.704  1.00 91.82           O  
ANISOU 1384  O   CYS A 168    11462  10580  12845  -4017    911   -289       O  
ATOM   1385  CB  CYS A 168      27.329  44.673  97.316  1.00 86.56           C  
ANISOU 1385  CB  CYS A 168    10981  10196  11710  -3674   1031   -304       C  
ATOM   1386  SG  CYS A 168      27.112  42.883  97.437  1.00 86.44           S  
ANISOU 1386  SG  CYS A 168    10927  10423  11494  -3493   1118   -334       S  
ATOM   1387  N   GLN A 169      27.146  47.858  98.845  1.00 90.05           N  
ANISOU 1387  N   GLN A 169    11451  10153  12611  -3919    679   -560       N  
ATOM   1388  CA  GLN A 169      27.552  49.274  98.731  1.00 92.00           C  
ANISOU 1388  CA  GLN A 169    11679  10151  13127  -4090    632   -541       C  
ATOM   1389  C   GLN A 169      28.201  49.823 100.030  1.00 92.95           C  
ANISOU 1389  C   GLN A 169    11709  10242  13365  -4230    491   -765       C  
ATOM   1390  O   GLN A 169      28.762  50.912 100.025  1.00 95.16           O  
ANISOU 1390  O   GLN A 169    11944  10332  13882  -4397    444   -762       O  
ATOM   1391  CB  GLN A 169      26.362  50.172  98.273  1.00 92.85           C  
ANISOU 1391  CB  GLN A 169    11937   9979  13364  -4044    604   -507       C  
ATOM   1392  CG  GLN A 169      26.774  51.553  97.577  1.00 95.88           C  
ANISOU 1392  CG  GLN A 169    12303  10081  14048  -4222    586   -345       C  
ATOM   1393  CD  GLN A 169      25.590  52.484  97.177  1.00 95.84           C  
ANISOU 1393  CD  GLN A 169    12397   9746  14271  -4182    517   -271       C  
ATOM   1394  OE1 GLN A 169      24.417  52.139  97.304  1.00 96.55           O  
ANISOU 1394  OE1 GLN A 169    12562   9800  14321  -4020    495   -320       O  
ATOM   1395  NE2 GLN A 169      25.921  53.656  96.691  1.00 95.31           N  
ANISOU 1395  NE2 GLN A 169    12301   9420  14492  -4336    477   -128       N  
ATOM   1396  N   ALA A 170      28.133  49.057 101.117  1.00 91.54           N  
ANISOU 1396  N   ALA A 170    11522  10253  13007  -4192    408   -941       N  
ATOM   1397  CA  ALA A 170      28.634  49.484 102.431  1.00 93.40           C  
ANISOU 1397  CA  ALA A 170    11734  10490  13263  -4373    241  -1161       C  
ATOM   1398  C   ALA A 170      30.124  49.203 102.549  1.00 94.88           C  
ANISOU 1398  C   ALA A 170    11693  10813  13543  -4533    144  -1021       C  
ATOM   1399  O   ALA A 170      30.671  48.456 101.726  1.00 93.95           O  
ANISOU 1399  O   ALA A 170    11425  10811  13460  -4460    256   -793       O  
ATOM   1400  CB  ALA A 170      27.854  48.801 103.565  1.00 91.82           C  
ANISOU 1400  CB  ALA A 170    11657  10439  12792  -4309    182  -1389       C  
ATOM   1401  N   GLU A 171      30.778  49.798 103.554  1.00 97.42           N  
ANISOU 1401  N   GLU A 171    11984  11101  13930  -4769    -52  -1160       N  
ATOM   1402  CA  GLU A 171      32.250  49.682 103.709  1.00100.12           C  
ANISOU 1402  CA  GLU A 171    12066  11524  14450  -4958   -195   -997       C  
ATOM   1403  C   GLU A 171      32.717  48.408 104.440  1.00 98.88           C  
ANISOU 1403  C   GLU A 171    11766  11646  14158  -4964   -355   -924       C  
ATOM   1404  O   GLU A 171      33.919  48.111 104.466  1.00101.53           O  
ANISOU 1404  O   GLU A 171    11821  12044  14711  -5083   -466   -728       O  
ATOM   1405  CB  GLU A 171      32.876  50.908 104.410  1.00103.81           C  
ANISOU 1405  CB  GLU A 171    12542  11818  15081  -5257   -388  -1131       C  
ATOM   1406  CG  GLU A 171      32.284  52.285 104.047  1.00107.73           C  
ANISOU 1406  CG  GLU A 171    13206  11993  15732  -5284   -281  -1272       C  
ATOM   1407  CD  GLU A 171      30.955  52.606 104.779  1.00109.37           C  
ANISOU 1407  CD  GLU A 171    13704  12100  15750  -5229   -241  -1612       C  
ATOM   1408  OE1 GLU A 171      30.857  53.742 105.329  1.00112.70           O  
ANISOU 1408  OE1 GLU A 171    14247  12281  16294  -5409   -283  -1854       O  
ATOM   1409  OE2 GLU A 171      30.025  51.741 104.780  1.00105.51           O  
ANISOU 1409  OE2 GLU A 171    13310  11749  15030  -5012   -142  -1643       O  
ATOM   1410  N   ASP A 172      31.788  47.714 105.079  1.00 95.33           N  
ANISOU 1410  N   ASP A 172    11487  11338  13398  -4857   -381  -1066       N  
ATOM   1411  CA  ASP A 172      32.034  46.388 105.607  1.00 93.34           C  
ANISOU 1411  CA  ASP A 172    11108  11340  13019  -4818   -508   -953       C  
ATOM   1412  C   ASP A 172      30.887  45.517 105.116  1.00 89.07           C  
ANISOU 1412  C   ASP A 172    10688  10880  12273  -4519   -295   -969       C  
ATOM   1413  O   ASP A 172      29.922  45.345 105.859  1.00 87.78           O  
ANISOU 1413  O   ASP A 172    10741  10780  11832  -4488   -331  -1162       O  
ATOM   1414  CB  ASP A 172      32.046  46.409 107.149  1.00 95.36           C  
ANISOU 1414  CB  ASP A 172    11491  11711  13029  -5069   -820  -1120       C  
ATOM   1415  CG  ASP A 172      32.705  45.158 107.769  1.00 95.57           C  
ANISOU 1415  CG  ASP A 172    11304  11980  13027  -5127  -1065   -903       C  
ATOM   1416  OD1 ASP A 172      32.438  44.014 107.303  1.00 89.51           O  
ANISOU 1416  OD1 ASP A 172    10426  11327  12258  -4881   -937   -758       O  
ATOM   1417  OD2 ASP A 172      33.514  45.342 108.726  1.00 99.11           O  
ANISOU 1417  OD2 ASP A 172    11691  12487  13479  -5442  -1408   -864       O  
ATOM   1418  N   LYS A 173      30.978  45.024 103.866  1.00 86.36           N  
ANISOU 1418  N   LYS A 173    10227  10523  12063  -4328    -60   -783       N  
ATOM   1419  CA  LYS A 173      30.059  44.024 103.325  1.00 83.27           C  
ANISOU 1419  CA  LYS A 173     9919  10224  11498  -4070    116   -756       C  
ATOM   1420  C   LYS A 173      29.771  42.947 104.376  1.00 82.47           C  
ANISOU 1420  C   LYS A 173     9812  10334  11188  -4038    -50   -793       C  
ATOM   1421  O   LYS A 173      28.600  42.718 104.723  1.00 81.04           O  
ANISOU 1421  O   LYS A 173     9843  10194  10753  -3928    -24   -940       O  
ATOM   1422  CB  LYS A 173      30.571  43.363 102.020  1.00 82.43           C  
ANISOU 1422  CB  LYS A 173     9644  10122  11552  -3949    365   -541       C  
ATOM   1423  CG  LYS A 173      31.020  44.374 100.918  1.00 85.60           C  
ANISOU 1423  CG  LYS A 173    10043  10336  12145  -4031    540   -456       C  
ATOM   1424  CD  LYS A 173      31.399  43.767  99.530  1.00 83.60           C  
ANISOU 1424  CD  LYS A 173     9708  10085  11972  -3951    861   -282       C  
ATOM   1425  CE  LYS A 173      32.767  43.071  99.480  1.00 86.01           C  
ANISOU 1425  CE  LYS A 173     9655  10443  12583  -4003    943   -137       C  
ATOM   1426  NZ  LYS A 173      33.959  43.993  99.730  1.00 88.73           N  
ANISOU 1426  NZ  LYS A 173     9779  10679  13255  -4222    840    -60       N  
ATOM   1427  N   GLY A 174      30.825  42.321 104.908  1.00 83.65           N  
ANISOU 1427  N   GLY A 174     9707  10601  11475  -4150   -233   -640       N  
ATOM   1428  CA  GLY A 174      30.677  41.200 105.857  1.00 83.11           C  
ANISOU 1428  CA  GLY A 174     9597  10736  11246  -4144   -426   -598       C  
ATOM   1429  C   GLY A 174      29.708  41.500 106.983  1.00 82.52           C  
ANISOU 1429  C   GLY A 174     9829  10730  10794  -4239   -563   -838       C  
ATOM   1430  O   GLY A 174      28.670  40.866 107.117  1.00 80.35           O  
ANISOU 1430  O   GLY A 174     9704  10539  10288  -4080   -479   -915       O  
ATOM   1431  N   ALA A 175      30.046  42.512 107.761  1.00 85.38           N  
ANISOU 1431  N   ALA A 175    10294  11040  11108  -4514   -744   -974       N  
ATOM   1432  CA  ALA A 175      29.222  42.975 108.856  1.00 86.76           C  
ANISOU 1432  CA  ALA A 175    10787  11245  10932  -4666   -818  -1259       C  
ATOM   1433  C   ALA A 175      27.785  43.325 108.456  1.00 85.11           C  
ANISOU 1433  C   ALA A 175    10825  10913  10601  -4449   -518  -1490       C  
ATOM   1434  O   ALA A 175      26.894  43.309 109.299  1.00 84.86           O  
ANISOU 1434  O   ALA A 175    11027  10930  10284  -4496   -496  -1711       O  
ATOM   1435  CB  ALA A 175      29.884  44.163 109.526  1.00 90.33           C  
ANISOU 1435  CB  ALA A 175    11319  11599  11403  -5010  -1003  -1397       C  
ATOM   1436  N   CYS A 176      27.556  43.660 107.192  1.00 84.49           N  
ANISOU 1436  N   CYS A 176    10692  10664  10747  -4238   -291  -1427       N  
ATOM   1437  CA  CYS A 176      26.212  44.013 106.763  1.00 84.39           C  
ANISOU 1437  CA  CYS A 176    10869  10505  10691  -4045    -59  -1585       C  
ATOM   1438  C   CYS A 176      25.435  42.771 106.346  1.00 81.06           C  
ANISOU 1438  C   CYS A 176    10433  10215  10152  -3783     43  -1474       C  
ATOM   1439  O   CYS A 176      24.234  42.671 106.647  1.00 80.47           O  
ANISOU 1439  O   CYS A 176    10522  10118   9933  -3678    145  -1628       O  
ATOM   1440  CB  CYS A 176      26.209  45.068 105.638  1.00 85.44           C  
ANISOU 1440  CB  CYS A 176    10988  10371  11103  -3989     88  -1548       C  
ATOM   1441  SG  CYS A 176      24.504  45.770 105.162  1.00 89.48           S  
ANISOU 1441  SG  CYS A 176    11702  10613  11684  -3794    312  -1711       S  
ATOM   1442  N   LEU A 177      26.129  41.813 105.715  1.00 80.05           N  
ANISOU 1442  N   LEU A 177    10099  10208  10111  -3693     30  -1222       N  
ATOM   1443  CA  LEU A 177      25.476  40.684 105.006  1.00 77.36           C  
ANISOU 1443  CA  LEU A 177     9737   9944   9714  -3440    164  -1105       C  
ATOM   1444  C   LEU A 177      25.035  39.525 105.843  1.00 75.65           C  
ANISOU 1444  C   LEU A 177     9529   9930   9286  -3387     74  -1106       C  
ATOM   1445  O   LEU A 177      23.894  39.094 105.786  1.00 74.73           O  
ANISOU 1445  O   LEU A 177     9535   9824   9033  -3227    171  -1168       O  
ATOM   1446  CB  LEU A 177      26.384  40.130 103.897  1.00 77.68           C  
ANISOU 1446  CB  LEU A 177     9566   9991   9959  -3372    262   -873       C  
ATOM   1447  CG  LEU A 177      26.356  40.942 102.588  1.00 79.75           C  
ANISOU 1447  CG  LEU A 177     9883  10064  10356  -3342    449   -826       C  
ATOM   1448  CD1 LEU A 177      27.522  40.579 101.685  1.00 79.90           C  
ANISOU 1448  CD1 LEU A 177     9692  10085  10580  -3365    575   -637       C  
ATOM   1449  CD2 LEU A 177      25.007  40.744 101.857  1.00 77.76           C  
ANISOU 1449  CD2 LEU A 177     9824   9752   9971  -3158    581   -843       C  
ATOM   1450  N   LEU A 178      25.962  38.999 106.613  1.00 76.54           N  
ANISOU 1450  N   LEU A 178     9490  10194   9399  -3536   -135  -1002       N  
ATOM   1451  CA  LEU A 178      25.789  37.685 107.202  1.00 74.65           C  
ANISOU 1451  CA  LEU A 178     9184  10148   9030  -3483   -242   -897       C  
ATOM   1452  C   LEU A 178      24.649  37.647 108.218  1.00 73.57           C  
ANISOU 1452  C   LEU A 178     9298  10096   8559  -3520   -267  -1090       C  
ATOM   1453  O   LEU A 178      23.999  36.610 108.341  1.00 71.82           O  
ANISOU 1453  O   LEU A 178     9082   9985   8222  -3382   -245  -1033       O  
ATOM   1454  CB  LEU A 178      27.123  37.214 107.820  1.00 77.11           C  
ANISOU 1454  CB  LEU A 178     9240  10572   9486  -3672   -516   -687       C  
ATOM   1455  CG  LEU A 178      28.332  37.445 106.896  1.00 76.86           C  
ANISOU 1455  CG  LEU A 178     8936  10419   9846  -3670   -453   -524       C  
ATOM   1456  CD1 LEU A 178      29.622  37.586 107.696  1.00 81.68           C  
ANISOU 1456  CD1 LEU A 178     9328  11076  10629  -3945   -773   -368       C  
ATOM   1457  CD2 LEU A 178      28.448  36.350 105.827  1.00 75.42           C  
ANISOU 1457  CD2 LEU A 178     8557  10214   9885  -3423   -234   -364       C  
ATOM   1458  N   PRO A 179      24.406  38.765 108.945  1.00 75.11           N  
ANISOU 1458  N   PRO A 179     9700  10225   8613  -3716   -284  -1332       N  
ATOM   1459  CA  PRO A 179      23.275  38.770 109.903  1.00 75.21           C  
ANISOU 1459  CA  PRO A 179     9965  10294   8317  -3766   -223  -1560       C  
ATOM   1460  C   PRO A 179      21.943  38.717 109.158  1.00 72.71           C  
ANISOU 1460  C   PRO A 179     9724   9843   8058  -3475     51  -1644       C  
ATOM   1461  O   PRO A 179      21.023  37.994 109.582  1.00 70.68           O  
ANISOU 1461  O   PRO A 179     9547   9681   7627  -3389    113  -1680       O  
ATOM   1462  CB  PRO A 179      23.422  40.094 110.641  1.00 78.02           C  
ANISOU 1462  CB  PRO A 179    10512  10544   8587  -4045   -236  -1831       C  
ATOM   1463  CG  PRO A 179      24.751  40.675 110.205  1.00 79.04           C  
ANISOU 1463  CG  PRO A 179    10468  10603   8962  -4167   -388  -1698       C  
ATOM   1464  CD  PRO A 179      25.081  40.079 108.888  1.00 76.87           C  
ANISOU 1464  CD  PRO A 179     9944  10292   8971  -3900   -313  -1434       C  
ATOM   1465  N   LYS A 180      21.886  39.405 108.007  1.00 71.60           N  
ANISOU 1465  N   LYS A 180     9539   9489   8177  -3338    186  -1625       N  
ATOM   1466  CA  LYS A 180      20.680  39.372 107.183  1.00 69.72           C  
ANISOU 1466  CA  LYS A 180     9349   9106   8034  -3088    382  -1638       C  
ATOM   1467  C   LYS A 180      20.452  38.030 106.456  1.00 68.31           C  
ANISOU 1467  C   LYS A 180     9064   9044   7845  -2874    390  -1416       C  
ATOM   1468  O   LYS A 180      19.292  37.546 106.407  1.00 67.04           O  
ANISOU 1468  O   LYS A 180     8969   8874   7631  -2717    481  -1442       O  
ATOM   1469  CB  LYS A 180      20.558  40.572 106.246  1.00 69.17           C  
ANISOU 1469  CB  LYS A 180     9296   8759   8226  -3051    487  -1664       C  
ATOM   1470  CG  LYS A 180      20.302  41.906 106.960  1.00 71.17           C  
ANISOU 1470  CG  LYS A 180     9679   8818   8545  -3209    552  -1943       C  
ATOM   1471  CD  LYS A 180      20.170  43.039 105.961  1.00 71.42           C  
ANISOU 1471  CD  LYS A 180     9691   8549   8897  -3160    630  -1912       C  
ATOM   1472  CE  LYS A 180      20.295  44.421 106.582  1.00 79.41           C  
ANISOU 1472  CE  LYS A 180    10788   9341  10045  -3348    677  -2170       C  
ATOM   1473  NZ  LYS A 180      19.244  44.784 107.599  1.00 80.66           N  
ANISOU 1473  NZ  LYS A 180    11090   9382  10174  -3379    849  -2496       N  
ATOM   1474  N   ILE A 181      21.504  37.403 105.914  1.00 68.53           N  
ANISOU 1474  N   ILE A 181     8923   9164   7953  -2868    316  -1211       N  
ATOM   1475  CA  ILE A 181      21.236  36.072 105.328  1.00 67.42           C  
ANISOU 1475  CA  ILE A 181     8699   9114   7802  -2681    356  -1049       C  
ATOM   1476  C   ILE A 181      20.883  35.085 106.389  1.00 67.53           C  
ANISOU 1476  C   ILE A 181     8710   9316   7634  -2685    255  -1045       C  
ATOM   1477  O   ILE A 181      19.945  34.320 106.196  1.00 66.55           O  
ANISOU 1477  O   ILE A 181     8623   9215   7448  -2522    323  -1023       O  
ATOM   1478  CB  ILE A 181      22.231  35.537 104.256  1.00 66.03           C  
ANISOU 1478  CB  ILE A 181     8349   8934   7804  -2633    407   -858       C  
ATOM   1479  CG1 ILE A 181      23.596  35.216 104.821  1.00 69.87           C  
ANISOU 1479  CG1 ILE A 181     8618   9525   8404  -2773    264   -749       C  
ATOM   1480  CG2 ILE A 181      22.338  36.528 103.155  1.00 67.13           C  
ANISOU 1480  CG2 ILE A 181     8551   8893   8063  -2645    531   -859       C  
ATOM   1481  CD1 ILE A 181      24.760  35.639 103.919  1.00 69.50           C  
ANISOU 1481  CD1 ILE A 181     8421   9377   8610  -2829    353   -653       C  
ATOM   1482  N   GLU A 182      21.557  35.158 107.535  1.00 70.25           N  
ANISOU 1482  N   GLU A 182     9031   9787   7873  -2898     77  -1062       N  
ATOM   1483  CA  GLU A 182      21.300  34.248 108.649  1.00 71.82           C  
ANISOU 1483  CA  GLU A 182     9247  10184   7857  -2967    -57  -1025       C  
ATOM   1484  C   GLU A 182      19.879  34.360 109.208  1.00 70.98           C  
ANISOU 1484  C   GLU A 182     9359  10075   7537  -2927     77  -1222       C  
ATOM   1485  O   GLU A 182      19.247  33.342 109.491  1.00 71.61           O  
ANISOU 1485  O   GLU A 182     9434  10264   7510  -2836     75  -1150       O  
ATOM   1486  CB  GLU A 182      22.320  34.475 109.768  1.00 75.95           C  
ANISOU 1486  CB  GLU A 182     9745  10837   8277  -3277   -317   -990       C  
ATOM   1487  CG  GLU A 182      23.677  33.840 109.509  1.00 82.02           C  
ANISOU 1487  CG  GLU A 182    10212  11653   9300  -3311   -505   -708       C  
ATOM   1488  CD  GLU A 182      23.567  32.485 108.839  1.00 84.34           C  
ANISOU 1488  CD  GLU A 182    10314  11965   9766  -3067   -442   -510       C  
ATOM   1489  OE1 GLU A 182      22.821  31.625 109.352  1.00 83.82           O  
ANISOU 1489  OE1 GLU A 182    10304  12012   9532  -3013   -475   -477       O  
ATOM   1490  OE2 GLU A 182      24.227  32.280 107.798  1.00 86.81           O  
ANISOU 1490  OE2 GLU A 182    10430  12170  10385  -2942   -335   -402       O  
ATOM   1491  N   THR A 183      19.366  35.580 109.355  1.00 71.71           N  
ANISOU 1491  N   THR A 183     9618  10015   7614  -2990    214  -1467       N  
ATOM   1492  CA  THR A 183      17.956  35.747 109.736  1.00 71.46           C  
ANISOU 1492  CA  THR A 183     9747   9913   7492  -2918    411  -1664       C  
ATOM   1493  C   THR A 183      17.062  35.243 108.587  1.00 69.55           C  
ANISOU 1493  C   THR A 183     9429   9555   7441  -2614    530  -1550       C  
ATOM   1494  O   THR A 183      15.930  34.703 108.801  1.00 68.83           O  
ANISOU 1494  O   THR A 183     9379   9471   7301  -2498    633  -1581       O  
ATOM   1495  CB  THR A 183      17.569  37.202 109.955  1.00 73.52           C  
ANISOU 1495  CB  THR A 183    10153   9954   7825  -3015    578  -1951       C  
ATOM   1496  OG1 THR A 183      18.551  37.853 110.763  1.00 77.35           O  
ANISOU 1496  OG1 THR A 183    10717  10503   8171  -3317    453  -2059       O  
ATOM   1497  CG2 THR A 183      16.181  37.312 110.632  1.00 73.00           C  
ANISOU 1497  CG2 THR A 183    10231   9817   7688  -2987    817  -2182       C  
ATOM   1498  N   MET A 184      17.561  35.395 107.368  1.00 68.10           N  
ANISOU 1498  N   MET A 184     9145   9267   7462  -2512    514  -1412       N  
ATOM   1499  CA  MET A 184      16.780  34.970 106.256  1.00 67.50           C  
ANISOU 1499  CA  MET A 184     9043   9088   7518  -2290    592  -1299       C  
ATOM   1500  C   MET A 184      16.732  33.420 106.238  1.00 66.83           C  
ANISOU 1500  C   MET A 184     8871   9182   7338  -2186    528  -1134       C  
ATOM   1501  O   MET A 184      15.631  32.833 106.227  1.00 66.31           O  
ANISOU 1501  O   MET A 184     8834   9108   7251  -2055    583  -1125       O  
ATOM   1502  CB  MET A 184      17.315  35.565 104.948  1.00 66.96           C  
ANISOU 1502  CB  MET A 184     8941   8869   7633  -2264    605  -1198       C  
ATOM   1503  CG  MET A 184      16.470  35.221 103.742  1.00 67.01           C  
ANISOU 1503  CG  MET A 184     8971   8762   7728  -2097    654  -1073       C  
ATOM   1504  SD  MET A 184      17.050  35.851 102.132  1.00 69.09           S  
ANISOU 1504  SD  MET A 184     9256   8873   8122  -2127    673   -926       S  
ATOM   1505  CE  MET A 184      16.276  34.685 101.088  1.00 60.85           C  
ANISOU 1505  CE  MET A 184     8259   7847   7015  -1990    680   -768       C  
ATOM   1506  N   ARG A 185      17.911  32.789 106.293  1.00 67.29           N  
ANISOU 1506  N   ARG A 185     8801   9377   7389  -2250    414  -1002       N  
ATOM   1507  CA AARG A 185      18.072  31.324 106.199  0.50 66.61           C  
ANISOU 1507  CA AARG A 185     8588   9418   7303  -2155    356   -829       C  
ATOM   1508  CA BARG A 185      18.026  31.339 106.160  0.50 66.47           C  
ANISOU 1508  CA BARG A 185     8575   9393   7287  -2149    363   -832       C  
ATOM   1509  C   ARG A 185      17.205  30.571 107.219  1.00 66.30           C  
ANISOU 1509  C   ARG A 185     8593   9508   7090  -2144    315   -840       C  
ATOM   1510  O   ARG A 185      16.610  29.529 106.933  1.00 66.41           O  
ANISOU 1510  O   ARG A 185     8567   9546   7120  -1999    334   -745       O  
ATOM   1511  CB AARG A 185      19.555  30.954 106.349  0.50 67.42           C  
ANISOU 1511  CB AARG A 185     8499   9607   7509  -2262    231   -690       C  
ATOM   1512  CB BARG A 185      19.502  30.922 106.117  0.50 66.89           C  
ANISOU 1512  CB BARG A 185     8432   9517   7465  -2231    259   -685       C  
ATOM   1513  CG AARG A 185      19.850  29.477 106.485  0.50 66.27           C  
ANISOU 1513  CG AARG A 185     8176   9566   7438  -2192    152   -504       C  
ATOM   1514  CG BARG A 185      19.702  29.451 106.189  0.50 65.49           C  
ANISOU 1514  CG BARG A 185     8091   9435   7356  -2148    198   -513       C  
ATOM   1515  CD AARG A 185      20.956  29.204 107.521  0.50 67.52           C  
ANISOU 1515  CD AARG A 185     8165   9856   7633  -2380    -86   -364       C  
ATOM   1516  CD BARG A 185      20.972  28.985 105.527  0.50 65.68           C  
ANISOU 1516  CD BARG A 185     7886   9415   7656  -2140    217   -372       C  
ATOM   1517  NE AARG A 185      21.323  27.788 107.531  0.50 69.56           N  
ANISOU 1517  NE AARG A 185     8197  10160   8075  -2299   -163   -147       N  
ATOM   1518  NE BARG A 185      20.854  27.543 105.332  0.50 66.10           N  
ANISOU 1518  NE BARG A 185     7804   9487   7826  -2005    234   -244       N  
ATOM   1519  CZ AARG A 185      21.640  27.090 108.620  0.50 70.12           C  
ANISOU 1519  CZ AARG A 185     8153  10371   8120  -2424   -413     30       C  
ATOM   1520  CZ BARG A 185      20.398  26.986 104.219  0.50 63.74           C  
ANISOU 1520  CZ BARG A 185     7547   9086   7585  -1849    426   -269       C  
ATOM   1521  NH1AARG A 185      21.640  27.677 109.804  0.50 73.05           N  
ANISOU 1521  NH1AARG A 185     8658  10880   8218  -2667   -604     -3       N  
ATOM   1522  NH1BARG A 185      20.055  27.747 103.193  0.50 61.20           N  
ANISOU 1522  NH1BARG A 185     7401   8654   7200  -1827    587   -381       N  
ATOM   1523  NH2AARG A 185      21.959  25.805 108.524  0.50 67.35           N  
ANISOU 1523  NH2AARG A 185     7563  10010   8016  -2329   -472    243       N  
ATOM   1524  NH2BARG A 185      20.294  25.672 104.136  0.50 63.65           N  
ANISOU 1524  NH2BARG A 185     7413   9074   7695  -1742    440   -172       N  
ATOM   1525  N   GLU A 186      17.098  31.100 108.409  1.00 67.90           N  
ANISOU 1525  N   GLU A 186     8898   9790   7111  -2319    275   -965       N  
ATOM   1526  CA  GLU A 186      16.157  30.497 109.342  1.00 68.40           C  
ANISOU 1526  CA  GLU A 186     9041   9966   6983  -2332    293   -998       C  
ATOM   1527  C   GLU A 186      14.653  30.537 108.870  1.00 66.30           C  
ANISOU 1527  C   GLU A 186     8845   9554   6791  -2136    490  -1088       C  
ATOM   1528  O   GLU A 186      13.893  29.588 109.080  1.00 65.07           O  
ANISOU 1528  O   GLU A 186     8670   9464   6591  -2045    505  -1014       O  
ATOM   1529  CB  GLU A 186      16.398  31.041 110.763  1.00 71.14           C  
ANISOU 1529  CB  GLU A 186     9528  10443   7058  -2624    231  -1133       C  
ATOM   1530  CG  GLU A 186      17.720  30.457 111.428  1.00 75.61           C  
ANISOU 1530  CG  GLU A 186     9984  11208   7537  -2834    -69   -923       C  
ATOM   1531  CD  GLU A 186      17.478  29.496 112.665  1.00 83.44           C  
ANISOU 1531  CD  GLU A 186    11027  12431   8246  -3000   -215   -806       C  
ATOM   1532  OE1 GLU A 186      16.403  28.808 112.766  1.00 83.93           O  
ANISOU 1532  OE1 GLU A 186    11128  12518   8245  -2872    -94   -803       O  
ATOM   1533  OE2 GLU A 186      18.382  29.431 113.552  1.00 84.84           O  
ANISOU 1533  OE2 GLU A 186    11206  12766   8265  -3286   -478   -690       O  
ATOM   1534  N   LYS A 187      14.235  31.617 108.217  1.00 65.40           N  
ANISOU 1534  N   LYS A 187     8789   9227   6835  -2078    618  -1214       N  
ATOM   1535  CA  LYS A 187      12.835  31.729 107.792  1.00 63.34           C  
ANISOU 1535  CA  LYS A 187     8553   8795   6719  -1913    763  -1259       C  
ATOM   1536  C   LYS A 187      12.529  30.761 106.646  1.00 60.84           C  
ANISOU 1536  C   LYS A 187     8153   8449   6513  -1724    701  -1053       C  
ATOM   1537  O   LYS A 187      11.391  30.334 106.498  1.00 59.84           O  
ANISOU 1537  O   LYS A 187     8018   8257   6462  -1602    751  -1022       O  
ATOM   1538  CB  LYS A 187      12.499  33.159 107.362  1.00 63.86           C  
ANISOU 1538  CB  LYS A 187     8668   8602   6994  -1913    878  -1401       C  
ATOM   1539  CG  LYS A 187      12.254  34.102 108.482  1.00 64.24           C  
ANISOU 1539  CG  LYS A 187     8819   8598   6993  -2065   1032  -1670       C  
ATOM   1540  CD  LYS A 187      12.362  35.504 107.978  1.00 67.00           C  
ANISOU 1540  CD  LYS A 187     9184   8689   7586  -2088   1097  -1777       C  
ATOM   1541  CE  LYS A 187      12.156  36.496 109.112  1.00 71.36           C  
ANISOU 1541  CE  LYS A 187     9852   9152   8110  -2261   1294  -2098       C  
ATOM   1542  NZ  LYS A 187      12.696  37.847 108.719  1.00 74.56           N  
ANISOU 1542  NZ  LYS A 187    10269   9338   8721  -2336   1305  -2195       N  
ATOM   1543  N   VAL A 188      13.556  30.426 105.865  1.00 58.10           N  
ANISOU 1543  N   VAL A 188     7749   8141   6187  -1723    609   -927       N  
ATOM   1544  CA  VAL A 188      13.426  29.625 104.664  1.00 55.26           C  
ANISOU 1544  CA  VAL A 188     7355   7733   5907  -1594    587   -777       C  
ATOM   1545  C   VAL A 188      13.318  28.186 105.131  1.00 54.74           C  
ANISOU 1545  C   VAL A 188     7209   7820   5771  -1537    534   -679       C  
ATOM   1546  O   VAL A 188      12.454  27.471 104.722  1.00 52.97           O  
ANISOU 1546  O   VAL A 188     6988   7556   5583  -1423    539   -614       O  
ATOM   1547  CB  VAL A 188      14.695  29.832 103.789  1.00 55.43           C  
ANISOU 1547  CB  VAL A 188     7347   7737   5977  -1652    578   -721       C  
ATOM   1548  CG1 VAL A 188      15.090  28.595 102.931  1.00 52.70           C  
ANISOU 1548  CG1 VAL A 188     6941   7423   5660  -1580    590   -596       C  
ATOM   1549  CG2 VAL A 188      14.579  31.081 102.957  1.00 56.54           C  
ANISOU 1549  CG2 VAL A 188     7582   7695   6207  -1687    620   -756       C  
ATOM   1550  N   LEU A 189      14.176  27.773 106.068  1.00 56.47           N  
ANISOU 1550  N   LEU A 189     7346   8207   5901  -1637    455   -647       N  
ATOM   1551  CA  LEU A 189      14.070  26.403 106.546  1.00 54.82           C  
ANISOU 1551  CA  LEU A 189     7041   8124   5662  -1594    380   -516       C  
ATOM   1552  C   LEU A 189      12.735  26.253 107.226  1.00 54.11           C  
ANISOU 1552  C   LEU A 189     7025   8054   5479  -1559    430   -566       C  
ATOM   1553  O   LEU A 189      12.068  25.273 107.055  1.00 54.31           O  
ANISOU 1553  O   LEU A 189     7009   8082   5545  -1449    422   -473       O  
ATOM   1554  CB  LEU A 189      15.209  26.057 107.488  1.00 55.51           C  
ANISOU 1554  CB  LEU A 189     7016   8376   5700  -1743    233   -423       C  
ATOM   1555  CG  LEU A 189      16.647  26.129 106.990  1.00 55.97           C  
ANISOU 1555  CG  LEU A 189     6933   8409   5924  -1790    183   -347       C  
ATOM   1556  CD1 LEU A 189      17.551  25.865 108.187  1.00 56.86           C  
ANISOU 1556  CD1 LEU A 189     6929   8683   5992  -1976    -28   -221       C  
ATOM   1557  CD2 LEU A 189      17.028  25.212 105.764  1.00 48.58           C  
ANISOU 1557  CD2 LEU A 189     5869   7364   5224  -1641    267   -253       C  
ATOM   1558  N   THR A 190      12.321  27.223 108.018  1.00 55.29           N  
ANISOU 1558  N   THR A 190     7281   8203   5524  -1661    508   -727       N  
ATOM   1559  CA  THR A 190      11.005  27.085 108.657  1.00 55.81           C  
ANISOU 1559  CA  THR A 190     7400   8262   5545  -1629    622   -793       C  
ATOM   1560  C   THR A 190       9.866  26.981 107.598  1.00 55.11           C  
ANISOU 1560  C   THR A 190     7285   7972   5680  -1430    686   -756       C  
ATOM   1561  O   THR A 190       8.886  26.278 107.799  1.00 55.82           O  
ANISOU 1561  O   THR A 190     7342   8062   5804  -1349    720   -703       O  
ATOM   1562  CB  THR A 190      10.778  28.173 109.671  1.00 56.34           C  
ANISOU 1562  CB  THR A 190     7593   8328   5484  -1793    761  -1017       C  
ATOM   1563  OG1 THR A 190      11.611  27.910 110.813  1.00 59.60           O  
ANISOU 1563  OG1 THR A 190     8054   8973   5619  -2019    652   -999       O  
ATOM   1564  CG2 THR A 190       9.313  28.228 110.119  1.00 60.29           C  
ANISOU 1564  CG2 THR A 190     8128   8742   6037  -1736    971  -1124       C  
ATOM   1565  N   SER A 191      10.034  27.633 106.453  1.00 53.52           N  
ANISOU 1565  N   SER A 191     7100   7607   5629  -1375    673   -754       N  
ATOM   1566  CA  SER A 191       8.986  27.682 105.541  1.00 53.32           C  
ANISOU 1566  CA  SER A 191     7072   7393   5796  -1250    682   -697       C  
ATOM   1567  C   SER A 191       8.938  26.360 104.747  1.00 52.58           C  
ANISOU 1567  C   SER A 191     6941   7334   5701  -1161    573   -527       C  
ATOM   1568  O   SER A 191       7.870  25.898 104.351  1.00 52.60           O  
ANISOU 1568  O   SER A 191     6927   7244   5817  -1070    547   -448       O  
ATOM   1569  CB  SER A 191       9.157  28.921 104.671  1.00 52.88           C  
ANISOU 1569  CB  SER A 191     7068   7147   5876  -1273    683   -732       C  
ATOM   1570  OG  SER A 191       8.669  28.723 103.330  1.00 59.33           O  
ANISOU 1570  OG  SER A 191     7906   7821   6814  -1204    585   -582       O  
ATOM   1571  N   SER A 192      10.099  25.826 104.408  1.00 51.71           N  
ANISOU 1571  N   SER A 192     6815   7322   5511  -1195    519   -476       N  
ATOM   1572  CA  SER A 192      10.190  24.524 103.791  1.00 50.44           C  
ANISOU 1572  CA  SER A 192     6616   7184   5367  -1128    466   -360       C  
ATOM   1573  C   SER A 192       9.676  23.391 104.692  1.00 50.18           C  
ANISOU 1573  C   SER A 192     6490   7261   5315  -1079    434   -287       C  
ATOM   1574  O   SER A 192       9.074  22.450 104.213  1.00 47.72           O  
ANISOU 1574  O   SER A 192     6161   6902   5068   -999    398   -204       O  
ATOM   1575  CB  SER A 192      11.633  24.281 103.439  1.00 50.51           C  
ANISOU 1575  CB  SER A 192     6581   7248   5365  -1182    473   -347       C  
ATOM   1576  OG  SER A 192      11.985  22.947 103.572  1.00 51.35           O  
ANISOU 1576  OG  SER A 192     6574   7420   5518  -1138    446   -257       O  
ATOM   1577  N   ALA A 193       9.954  23.466 105.987  1.00 51.18           N  
ANISOU 1577  N   ALA A 193     6574   7539   5335  -1159    437   -311       N  
ATOM   1578  CA  ALA A 193       9.444  22.416 106.900  1.00 53.05           C  
ANISOU 1578  CA  ALA A 193     6739   7892   5525  -1148    402   -214       C  
ATOM   1579  C   ALA A 193       7.912  22.477 106.937  1.00 52.71           C  
ANISOU 1579  C   ALA A 193     6724   7753   5552  -1068    481   -237       C  
ATOM   1580  O   ALA A 193       7.263  21.450 106.843  1.00 53.12           O  
ANISOU 1580  O   ALA A 193     6715   7795   5674   -989    441   -125       O  
ATOM   1581  CB  ALA A 193      10.029  22.550 108.309  1.00 53.57           C  
ANISOU 1581  CB  ALA A 193     6799   8153   5400  -1314    370   -218       C  
ATOM   1582  N   ARG A 194       7.356  23.692 107.039  1.00 53.35           N  
ANISOU 1582  N   ARG A 194     6872   7732   5668  -1088    596   -377       N  
ATOM   1583  CA  ARG A 194       5.918  23.930 106.850  1.00 54.08           C  
ANISOU 1583  CA  ARG A 194     6942   7655   5950   -998    677   -388       C  
ATOM   1584  C   ARG A 194       5.289  23.328 105.597  1.00 52.21           C  
ANISOU 1584  C   ARG A 194     6676   7269   5893   -882    553   -246       C  
ATOM   1585  O   ARG A 194       4.284  22.617 105.656  1.00 52.79           O  
ANISOU 1585  O   ARG A 194     6678   7298   6081   -812    538   -155       O  
ATOM   1586  CB  ARG A 194       5.627  25.427 106.910  1.00 56.51           C  
ANISOU 1586  CB  ARG A 194     7293   7809   6369  -1031    812   -550       C  
ATOM   1587  CG  ARG A 194       5.422  25.937 108.355  1.00 58.51           C  
ANISOU 1587  CG  ARG A 194     7580   8144   6505  -1145   1026   -731       C  
ATOM   1588  CD  ARG A 194       4.846  27.339 108.416  1.00 58.00           C  
ANISOU 1588  CD  ARG A 194     7525   7854   6660  -1151   1218   -915       C  
ATOM   1589  NE  ARG A 194       5.401  28.029 109.571  1.00 61.56           N  
ANISOU 1589  NE  ARG A 194     8093   8416   6883  -1335   1384  -1140       N  
ATOM   1590  CZ  ARG A 194       5.055  27.807 110.833  1.00 59.75           C  
ANISOU 1590  CZ  ARG A 194     7923   8316   6462  -1460   1574  -1258       C  
ATOM   1591  NH1 ARG A 194       4.131  26.905 111.088  1.00 57.22           N  
ANISOU 1591  NH1 ARG A 194     7524   8022   6195  -1391   1632  -1158       N  
ATOM   1592  NH2 ARG A 194       5.651  28.461 111.842  1.00 58.48           N  
ANISOU 1592  NH2 ARG A 194     7921   8267   6031  -1685   1699  -1472       N  
ATOM   1593  N   GLN A 195       5.853  23.625 104.450  1.00 51.11           N  
ANISOU 1593  N   GLN A 195     6607   7048   5765   -889    462   -226       N  
ATOM   1594  CA  GLN A 195       5.347  23.079 103.220  1.00 50.68           C  
ANISOU 1594  CA  GLN A 195     6586   6866   5806   -845    331   -104       C  
ATOM   1595  C   GLN A 195       5.436  21.547 103.219  1.00 50.70           C  
ANISOU 1595  C   GLN A 195     6548   6960   5757   -806    274    -17       C  
ATOM   1596  O   GLN A 195       4.463  20.834 102.876  1.00 50.83           O  
ANISOU 1596  O   GLN A 195     6536   6892   5884   -756    193     83       O  
ATOM   1597  CB  GLN A 195       6.127  23.643 102.050  1.00 50.07           C  
ANISOU 1597  CB  GLN A 195     6637   6721   5668   -916    278   -113       C  
ATOM   1598  CG  GLN A 195       5.406  23.409 100.741  1.00 52.23           C  
ANISOU 1598  CG  GLN A 195     7004   6835   6008   -936    126     10       C  
ATOM   1599  CD  GLN A 195       3.936  23.955 100.690  1.00 50.46           C  
ANISOU 1599  CD  GLN A 195     6708   6419   6044   -897     35    114       C  
ATOM   1600  OE1 GLN A 195       3.505  24.764 101.513  1.00 55.84           O  
ANISOU 1600  OE1 GLN A 195     7279   7048   6889   -853    139     56       O  
ATOM   1601  NE2 GLN A 195       3.211  23.526  99.708  1.00 47.79           N  
ANISOU 1601  NE2 GLN A 195     6430   5960   5766   -934   -152    262       N  
ATOM   1602  N   ARG A 196       6.591  21.026 103.646  1.00 50.41           N  
ANISOU 1602  N   ARG A 196     6480   7074   5598   -835    304    -40       N  
ATOM   1603  CA  ARG A 196       6.755  19.592 103.667  1.00 50.14           C  
ANISOU 1603  CA  ARG A 196     6374   7090   5585   -796    258     48       C  
ATOM   1604  C   ARG A 196       5.628  18.898 104.475  1.00 49.29           C  
ANISOU 1604  C   ARG A 196     6172   7011   5546   -741    238    140       C  
ATOM   1605  O   ARG A 196       5.227  17.838 104.153  1.00 48.59           O  
ANISOU 1605  O   ARG A 196     6045   6876   5540   -694    173    228       O  
ATOM   1606  CB  ARG A 196       8.194  19.180 104.047  1.00 50.29           C  
ANISOU 1606  CB  ARG A 196     6318   7230   5559   -836    278     48       C  
ATOM   1607  CG  ARG A 196       8.468  17.711 103.956  1.00 50.56           C  
ANISOU 1607  CG  ARG A 196     6247   7260   5705   -789    240    145       C  
ATOM   1608  CD  ARG A 196       8.919  17.314 102.606  1.00 53.37           C  
ANISOU 1608  CD  ARG A 196     6678   7476   6126   -786    291     86       C  
ATOM   1609  NE  ARG A 196       8.920  15.864 102.327  1.00 55.81           N  
ANISOU 1609  NE  ARG A 196     6907   7708   6589   -736    287    141       N  
ATOM   1610  CZ  ARG A 196       7.816  15.161 102.144  1.00 54.15           C  
ANISOU 1610  CZ  ARG A 196     6724   7430   6422   -695    216    195       C  
ATOM   1611  NH1 ARG A 196       6.645  15.756 102.292  1.00 56.19           N  
ANISOU 1611  NH1 ARG A 196     7049   7691   6611   -689    144    224       N  
ATOM   1612  NH2 ARG A 196       7.877  13.892 101.847  1.00 49.26           N  
ANISOU 1612  NH2 ARG A 196     6041   6718   5957   -661    223    223       N  
ATOM   1613  N   LEU A 197       5.070  19.534 105.473  1.00 49.91           N  
ANISOU 1613  N   LEU A 197     6221   7143   5601   -759    320    104       N  
ATOM   1614  CA  LEU A 197       4.026  18.892 106.223  1.00 50.57           C  
ANISOU 1614  CA  LEU A 197     6215   7250   5749   -725    346    187       C  
ATOM   1615  C   LEU A 197       2.679  18.986 105.474  1.00 52.77           C  
ANISOU 1615  C   LEU A 197     6473   7322   6254   -649    310    235       C  
ATOM   1616  O   LEU A 197       1.815  18.059 105.520  1.00 52.58           O  
ANISOU 1616  O   LEU A 197     6364   7258   6355   -598    260    355       O  
ATOM   1617  CB  LEU A 197       3.976  19.562 107.580  1.00 50.80           C  
ANISOU 1617  CB  LEU A 197     6247   7410   5644   -814    499     99       C  
ATOM   1618  CG  LEU A 197       2.668  19.371 108.334  1.00 51.62           C  
ANISOU 1618  CG  LEU A 197     6282   7493   5838   -798    627    124       C  
ATOM   1619  CD1 LEU A 197       2.521  17.902 108.754  1.00 48.82           C  
ANISOU 1619  CD1 LEU A 197     5842   7245   5464   -791    539    307       C  
ATOM   1620  CD2 LEU A 197       2.601  20.293 109.531  1.00 47.34           C  
ANISOU 1620  CD2 LEU A 197     5800   7041   5146   -922    852    -38       C  
ATOM   1621  N   ARG A 198       2.507  20.112 104.765  1.00 53.24           N  
ANISOU 1621  N   ARG A 198     6596   7236   6396   -654    306    172       N  
ATOM   1622  CA  ARG A 198       1.332  20.288 103.926  1.00 53.38           C  
ANISOU 1622  CA  ARG A 198     6585   7034   6665   -612    202    268       C  
ATOM   1623  C   ARG A 198       1.241  19.166 102.914  1.00 52.86           C  
ANISOU 1623  C   ARG A 198     6571   6919   6595   -613      9    386       C  
ATOM   1624  O   ARG A 198       0.198  18.500 102.823  1.00 52.91           O  
ANISOU 1624  O   ARG A 198     6491   6835   6777   -575    -78    509       O  
ATOM   1625  CB  ARG A 198       1.254  21.688 103.260  1.00 54.21           C  
ANISOU 1625  CB  ARG A 198     6743   6971   6882   -642    182    229       C  
ATOM   1626  CG  ARG A 198       0.843  22.720 104.246  1.00 51.92           C  
ANISOU 1626  CG  ARG A 198     6359   6635   6732   -626    394    114       C  
ATOM   1627  CD  ARG A 198       0.591  24.001 103.600  1.00 54.24           C  
ANISOU 1627  CD  ARG A 198     6655   6711   7242   -639    359    113       C  
ATOM   1628  NE  ARG A 198       1.778  24.838 103.379  1.00 55.53           N  
ANISOU 1628  NE  ARG A 198     6953   6932   7212   -714    381     -3       N  
ATOM   1629  CZ  ARG A 198       2.126  25.877 104.139  1.00 55.08           C  
ANISOU 1629  CZ  ARG A 198     6894   6875   7161   -744    575   -180       C  
ATOM   1630  NH1 ARG A 198       1.431  26.179 105.236  1.00 55.64           N  
ANISOU 1630  NH1 ARG A 198     6858   6906   7378   -719    809   -297       N  
ATOM   1631  NH2 ARG A 198       3.215  26.562 103.838  1.00 55.29           N  
ANISOU 1631  NH2 ARG A 198     7036   6946   7027   -819    559   -258       N  
ATOM   1632  N   CYS A 199       2.330  18.921 102.188  1.00 53.67           N  
ANISOU 1632  N   CYS A 199     6282   7165   6945    -14   -560    294       N  
ATOM   1633  CA  CYS A 199       2.397  17.766 101.284  1.00 53.50           C  
ANISOU 1633  CA  CYS A 199     6348   7062   6918     47   -575    324       C  
ATOM   1634  C   CYS A 199       2.304  16.425 102.020  1.00 54.03           C  
ANISOU 1634  C   CYS A 199     6519   7073   6936    157   -523    383       C  
ATOM   1635  O   CYS A 199       1.651  15.529 101.535  1.00 54.89           O  
ANISOU 1635  O   CYS A 199     6730   7026   7099    144   -510    408       O  
ATOM   1636  CB  CYS A 199       3.674  17.766 100.503  1.00 53.69           C  
ANISOU 1636  CB  CYS A 199     6350   7202   6850    102   -593    297       C  
ATOM   1637  SG  CYS A 199       4.070  19.330  99.800  1.00 62.20           S  
ANISOU 1637  SG  CYS A 199     7343   8342   7946    -26   -600    231       S  
ATOM   1638  N   ALA A 200       2.912  16.232 103.173  1.00 53.75           N  
ANISOU 1638  N   ALA A 200     6488   7146   6790    268   -489    401       N  
ATOM   1639  CA  ALA A 200       2.669  14.917 103.802  1.00 55.79           C  
ANISOU 1639  CA  ALA A 200     6912   7296   6991    384   -413    471       C  
ATOM   1640  C   ALA A 200       1.182  14.705 104.109  1.00 55.75           C  
ANISOU 1640  C   ALA A 200     6965   7091   7128    259   -332    500       C  
ATOM   1641  O   ALA A 200       0.672  13.632 103.859  1.00 56.65           O  
ANISOU 1641  O   ALA A 200     7214   7036   7275    252   -272    534       O  
ATOM   1642  CB  ALA A 200       3.487  14.668 105.048  1.00 55.33           C  
ANISOU 1642  CB  ALA A 200     6890   7374   6760    567   -394    492       C  
ATOM   1643  N   SER A 201       0.503  15.717 104.628  1.00 54.56           N  
ANISOU 1643  N   SER A 201     6710   6956   7062    156   -320    479       N  
ATOM   1644  CA  SER A 201      -0.917  15.598 104.907  1.00 55.45           C  
ANISOU 1644  CA  SER A 201     6828   6911   7329     39   -232    496       C  
ATOM   1645  C   SER A 201      -1.666  15.007 103.763  1.00 55.40           C  
ANISOU 1645  C   SER A 201     6826   6765   7460    -69   -263    473       C  
ATOM   1646  O   SER A 201      -2.307  14.008 103.943  1.00 57.45           O  
ANISOU 1646  O   SER A 201     7182   6872   7775   -109   -167    498       O  
ATOM   1647  CB  SER A 201      -1.537  16.950 105.242  1.00 55.90           C  
ANISOU 1647  CB  SER A 201     6746   7018   7473    -49   -240    461       C  
ATOM   1648  OG  SER A 201      -0.625  17.646 106.093  1.00 60.35           O  
ANISOU 1648  OG  SER A 201     7305   7733   7891     35   -254    451       O  
ATOM   1649  N   ILE A 202      -1.580  15.600 102.580  1.00 54.81           N  
ANISOU 1649  N   ILE A 202     6665   6730   7429   -117   -392    419       N  
ATOM   1650  CA  ILE A 202      -2.361  15.147 101.453  1.00 54.96           C  
ANISOU 1650  CA  ILE A 202     6685   6629   7568   -213   -457    377       C  
ATOM   1651  C   ILE A 202      -1.885  13.809 100.999  1.00 54.49           C  
ANISOU 1651  C   ILE A 202     6799   6473   7432   -161   -440    396       C  
ATOM   1652  O   ILE A 202      -2.721  12.945 100.765  1.00 55.45           O  
ANISOU 1652  O   ILE A 202     6979   6437   7651   -257   -407    377       O  
ATOM   1653  CB  ILE A 202      -2.244  16.027 100.196  1.00 55.83           C  
ANISOU 1653  CB  ILE A 202     6728   6793   7691   -232   -604    320       C  
ATOM   1654  CG1 ILE A 202      -1.993  17.471 100.552  1.00 54.47           C  
ANISOU 1654  CG1 ILE A 202     6457   6744   7495   -222   -616    313       C  
ATOM   1655  CG2 ILE A 202      -3.476  15.779  99.196  1.00 56.48           C  
ANISOU 1655  CG2 ILE A 202     6772   6763   7925   -338   -701    254       C  
ATOM   1656  CD1 ILE A 202      -2.083  18.401  99.372  1.00 58.31           C  
ANISOU 1656  CD1 ILE A 202     6919   7241   7994   -240   -728    265       C  
ATOM   1657  N   GLN A 203      -0.576  13.644 100.827  1.00 53.60           N  
ANISOU 1657  N   GLN A 203     6762   6451   7152    -17   -459    421       N  
ATOM   1658  CA  GLN A 203      -0.054  12.376 100.271  1.00 56.24           C  
ANISOU 1658  CA  GLN A 203     7287   6690   7394     70   -442    441       C  
ATOM   1659  C   GLN A 203      -0.365  11.142 101.146  1.00 58.10           C  
ANISOU 1659  C   GLN A 203     7704   6769   7601    100   -295    497       C  
ATOM   1660  O   GLN A 203      -0.328  10.029 100.658  1.00 60.58           O  
ANISOU 1660  O   GLN A 203     8209   6934   7876    123   -262    503       O  
ATOM   1661  CB  GLN A 203       1.432  12.412  99.989  1.00 55.04           C  
ANISOU 1661  CB  GLN A 203     7157   6688   7069    247   -470    458       C  
ATOM   1662  CG  GLN A 203       1.926  13.588  99.109  1.00 59.57           C  
ANISOU 1662  CG  GLN A 203     7590   7397   7646    215   -567    407       C  
ATOM   1663  CD  GLN A 203       3.462  13.811  99.241  1.00 64.62           C  
ANISOU 1663  CD  GLN A 203     8174   8243   8137    368   -555    414       C  
ATOM   1664  OE1 GLN A 203       3.985  13.988 100.356  1.00 62.80           O  
ANISOU 1664  OE1 GLN A 203     7873   8147   7839    445   -523    429       O  
ATOM   1665  NE2 GLN A 203       4.181  13.779  98.100  1.00 64.53           N  
ANISOU 1665  NE2 GLN A 203     8188   8261   8068    416   -579    394       N  
ATOM   1666  N   LYS A 204      -0.719  11.342 102.402  1.00 57.71           N  
ANISOU 1666  N   LYS A 204     7630   6732   7566     97   -192    536       N  
ATOM   1667  CA  LYS A 204      -0.620  10.297 103.374  1.00 60.43           C  
ANISOU 1667  CA  LYS A 204     8192   6962   7807    199    -33    611       C  
ATOM   1668  C   LYS A 204      -1.888  10.294 104.234  1.00 61.31           C  
ANISOU 1668  C   LYS A 204     8288   6944   8062     43    112    622       C  
ATOM   1669  O   LYS A 204      -2.207   9.304 104.874  1.00 63.46           O  
ANISOU 1669  O   LYS A 204     8773   7037   8303     51    288    675       O  
ATOM   1670  CB  LYS A 204       0.606  10.541 104.260  1.00 60.51           C  
ANISOU 1670  CB  LYS A 204     8224   7161   7607    440    -38    661       C  
ATOM   1671  CG  LYS A 204       1.809   9.628 104.091  1.00 64.61           C  
ANISOU 1671  CG  LYS A 204     8920   7711   7918    688    -43    702       C  
ATOM   1672  CD  LYS A 204       2.271   9.474 102.640  1.00 68.50           C  
ANISOU 1672  CD  LYS A 204     9390   8216   8423    681   -146    656       C  
ATOM   1673  CE  LYS A 204       3.781   9.347 102.551  1.00 69.24           C  
ANISOU 1673  CE  LYS A 204     9479   8508   8319    945   -200    670       C  
ATOM   1674  NZ  LYS A 204       4.366   8.282 103.398  1.00 71.44           N  
ANISOU 1674  NZ  LYS A 204     9994   8755   8396   1214   -108    748       N  
ATOM   1675  N   PHE A 205      -2.592  11.408 104.272  1.00 59.57           N  
ANISOU 1675  N   PHE A 205     7832   6809   7991    -88     61    575       N  
ATOM   1676  CA  PHE A 205      -3.816  11.454 105.007  1.00 60.64           C  
ANISOU 1676  CA  PHE A 205     7917   6844   8281   -233    208    578       C  
ATOM   1677  C   PHE A 205      -4.988  12.012 104.226  1.00 60.63           C  
ANISOU 1677  C   PHE A 205     7678   6835   8522   -440    126    485       C  
ATOM   1678  O   PHE A 205      -6.049  12.122 104.790  1.00 64.05           O  
ANISOU 1678  O   PHE A 205     8016   7213   9107   -563    248    474       O  
ATOM   1679  CB  PHE A 205      -3.622  12.251 106.302  1.00 61.29           C  
ANISOU 1679  CB  PHE A 205     7971   7039   8278   -132    279    627       C  
ATOM   1680  CG  PHE A 205      -2.699  11.575 107.305  1.00 62.51           C  
ANISOU 1680  CG  PHE A 205     8377   7185   8190     86    379    715       C  
ATOM   1681  CD1 PHE A 205      -3.198  10.665 108.215  1.00 62.83           C  
ANISOU 1681  CD1 PHE A 205     8640   7032   8199     96    610    786       C  
ATOM   1682  CD2 PHE A 205      -1.321  11.849 107.319  1.00 61.70           C  
ANISOU 1682  CD2 PHE A 205     8289   7270   7885    291    243    721       C  
ATOM   1683  CE1 PHE A 205      -2.332  10.001 109.121  1.00 65.48           C  
ANISOU 1683  CE1 PHE A 205     9255   7352   8274    345    693    872       C  
ATOM   1684  CE2 PHE A 205      -0.485  11.225 108.228  1.00 63.00           C  
ANISOU 1684  CE2 PHE A 205     8669   7453   7814    528    305    790       C  
ATOM   1685  CZ  PHE A 205      -1.003  10.296 109.144  1.00 62.34           C  
ANISOU 1685  CZ  PHE A 205     8850   7165   7672    573    525    871       C  
ATOM   1686  N   GLY A 206      -4.807  12.372 102.956  1.00 58.49           N  
ANISOU 1686  N   GLY A 206     7316   6630   8279   -461    -72    417       N  
ATOM   1687  CA  GLY A 206      -5.864  12.864 102.134  1.00 58.04           C  
ANISOU 1687  CA  GLY A 206     7055   6580   8419   -611   -185    322       C  
ATOM   1688  C   GLY A 206      -5.957  14.390 102.022  1.00 58.65           C  
ANISOU 1688  C   GLY A 206     6938   6826   8522   -571   -299    299       C  
ATOM   1689  O   GLY A 206      -5.391  15.168 102.857  1.00 56.42           O  
ANISOU 1689  O   GLY A 206     6654   6645   8139   -471   -251    353       O  
ATOM   1690  N   GLU A 207      -6.689  14.809 100.984  1.00 58.56           N  
ANISOU 1690  N   GLU A 207     6783   6833   8634   -642   -454    211       N  
ATOM   1691  CA  GLU A 207      -6.985  16.179 100.742  1.00 59.26           C  
ANISOU 1691  CA  GLU A 207     6719   7042   8756   -600   -558    183       C  
ATOM   1692  C   GLU A 207      -7.782  16.659 101.944  1.00 60.29           C  
ANISOU 1692  C   GLU A 207     6720   7195   8991   -629   -408    206       C  
ATOM   1693  O   GLU A 207      -7.487  17.708 102.474  1.00 60.40           O  
ANISOU 1693  O   GLU A 207     6717   7294   8937   -545   -387    240       O  
ATOM   1694  CB  GLU A 207      -7.789  16.331  99.444  1.00 61.16           C  
ANISOU 1694  CB  GLU A 207     6850   7284   9105   -648   -752     78       C  
ATOM   1695  CG  GLU A 207      -7.475  17.650  98.711  1.00 63.10           C  
ANISOU 1695  CG  GLU A 207     7084   7627   9265   -529   -900     67       C  
ATOM   1696  CD  GLU A 207      -8.236  17.851  97.371  1.00 66.45           C  
ANISOU 1696  CD  GLU A 207     7440   8058   9751   -522  -1118    -35       C  
ATOM   1697  OE1 GLU A 207      -8.369  16.884  96.567  1.00 65.78           O  
ANISOU 1697  OE1 GLU A 207     7408   7901   9683   -585  -1212    -97       O  
ATOM   1698  OE2 GLU A 207      -8.674  19.004  97.133  1.00 66.72           O  
ANISOU 1698  OE2 GLU A 207     7392   8163   9794   -435  -1199    -54       O  
ATOM   1699  N   ARG A 208      -8.768  15.885 102.395  1.00 61.40           N  
ANISOU 1699  N   ARG A 208     6786   7250   9294   -756   -282    185       N  
ATOM   1700  CA  ARG A 208      -9.538  16.207 103.605  1.00 62.23           C  
ANISOU 1700  CA  ARG A 208     6785   7359   9499   -785    -89    215       C  
ATOM   1701  C   ARG A 208      -8.692  16.731 104.760  1.00 61.01           C  
ANISOU 1701  C   ARG A 208     6771   7243   9165   -655     30    314       C  
ATOM   1702  O   ARG A 208      -9.205  17.433 105.624  1.00 62.78           O  
ANISOU 1702  O   ARG A 208     6919   7503   9430   -630    143    334       O  
ATOM   1703  CB  ARG A 208     -10.248  14.966 104.126  1.00 64.06           C  
ANISOU 1703  CB  ARG A 208     7031   7448   9863   -943    111    210       C  
ATOM   1704  CG  ARG A 208     -11.173  15.285 105.290  1.00 69.51           C  
ANISOU 1704  CG  ARG A 208     7595   8136  10678   -984    336    234       C  
ATOM   1705  CD  ARG A 208     -12.070  14.075 105.692  1.00 71.77           C  
ANISOU 1705  CD  ARG A 208     7863   8265  11141  -1190    566    208       C  
ATOM   1706  NE  ARG A 208     -11.513  13.250 106.770  1.00 68.52           N  
ANISOU 1706  NE  ARG A 208     7752   7700  10583  -1162    820    322       N  
ATOM   1707  CZ  ARG A 208     -11.957  13.263 108.019  1.00 72.06           C  
ANISOU 1707  CZ  ARG A 208     8240   8090  11051  -1165   1099    389       C  
ATOM   1708  NH1 ARG A 208     -12.943  14.064 108.340  1.00 74.72           N  
ANISOU 1708  NH1 ARG A 208     8314   8518  11559  -1201   1165    351       N  
ATOM   1709  NH2 ARG A 208     -11.428  12.472 108.953  1.00 74.51           N  
ANISOU 1709  NH2 ARG A 208     8869   8246  11194  -1110   1321    495       N  
ATOM   1710  N   ALA A 209      -7.415  16.376 104.825  1.00 59.00           N  
ANISOU 1710  N   ALA A 209     6719   6990   8709   -564      7    366       N  
ATOM   1711  CA  ALA A 209      -6.665  16.712 106.028  1.00 58.28           C  
ANISOU 1711  CA  ALA A 209     6754   6943   8448   -446    113    440       C  
ATOM   1712  C   ALA A 209      -6.036  18.117 105.878  1.00 57.13           C  
ANISOU 1712  C   ALA A 209     6560   6941   8206   -364    -16    420       C  
ATOM   1713  O   ALA A 209      -5.972  18.931 106.808  1.00 56.00           O  
ANISOU 1713  O   ALA A 209     6427   6850   8001   -310     51    439       O  
ATOM   1714  CB  ALA A 209      -5.638  15.665 106.296  1.00 57.99           C  
ANISOU 1714  CB  ALA A 209     6936   6860   8237   -365    154    497       C  
ATOM   1715  N   LEU A 210      -5.611  18.397 104.658  1.00 56.66           N  
ANISOU 1715  N   LEU A 210     6468   6925   8134   -366   -191    375       N  
ATOM   1716  CA  LEU A 210      -5.035  19.648 104.348  1.00 56.33           C  
ANISOU 1716  CA  LEU A 210     6408   6983   8012   -319   -289    349       C  
ATOM   1717  C   LEU A 210      -6.117  20.719 104.420  1.00 58.02           C  
ANISOU 1717  C   LEU A 210     6498   7201   8344   -333   -282    321       C  
ATOM   1718  O   LEU A 210      -5.990  21.661 105.199  1.00 58.59           O  
ANISOU 1718  O   LEU A 210     6593   7315   8353   -292   -224    331       O  
ATOM   1719  CB  LEU A 210      -4.440  19.545 102.961  1.00 54.59           C  
ANISOU 1719  CB  LEU A 210     6212   6775   7755   -318   -440    315       C  
ATOM   1720  CG  LEU A 210      -3.890  20.899 102.525  1.00 56.36           C  
ANISOU 1720  CG  LEU A 210     6439   7073   7903   -291   -514    286       C  
ATOM   1721  CD1 LEU A 210      -2.608  21.371 103.336  1.00 54.69           C  
ANISOU 1721  CD1 LEU A 210     6288   6964   7528   -256   -467    295       C  
ATOM   1722  CD2 LEU A 210      -3.570  20.737 101.056  1.00 57.82           C  
ANISOU 1722  CD2 LEU A 210     6662   7238   8069   -289   -639    256       C  
ATOM   1723  N   LYS A 211      -7.158  20.554 103.581  1.00 58.87           N  
ANISOU 1723  N   LYS A 211     6482   7272   8614   -380   -352    276       N  
ATOM   1724  CA  LYS A 211      -8.369  21.314 103.627  1.00 59.95           C  
ANISOU 1724  CA  LYS A 211     6466   7424   8889   -369   -345    244       C  
ATOM   1725  C   LYS A 211      -8.682  21.624 105.078  1.00 60.94           C  
ANISOU 1725  C   LYS A 211     6590   7547   9016   -350   -151    290       C  
ATOM   1726  O   LYS A 211      -8.835  22.799 105.418  1.00 61.31           O  
ANISOU 1726  O   LYS A 211     6638   7629   9028   -277   -132    289       O  
ATOM   1727  CB  LYS A 211      -9.484  20.495 103.010  1.00 62.10           C  
ANISOU 1727  CB  LYS A 211     6574   7662   9357   -454   -391    186       C  
ATOM   1728  CG  LYS A 211     -10.615  21.276 102.475  1.00 63.94           C  
ANISOU 1728  CG  LYS A 211     6618   7952   9724   -409   -487    120       C  
ATOM   1729  CD  LYS A 211     -11.663  20.355 101.832  1.00 66.17           C  
ANISOU 1729  CD  LYS A 211     6706   8227  10208   -517   -559     31       C  
ATOM   1730  CE  LYS A 211     -13.056  21.068 101.790  1.00 72.84           C  
ANISOU 1730  CE  LYS A 211     7278   9165  11233   -464   -592    -39       C  
ATOM   1731  NZ  LYS A 211     -14.144  20.366 101.004  1.00 74.73           N  
ANISOU 1731  NZ  LYS A 211     7268   9444  11681   -564   -721   -166       N  
ATOM   1732  N   ALA A 212      -8.720  20.608 105.950  1.00 60.73           N  
ANISOU 1732  N   ALA A 212     6608   7463   9002   -399      7    333       N  
ATOM   1733  CA  ALA A 212      -9.145  20.860 107.322  1.00 61.92           C  
ANISOU 1733  CA  ALA A 212     6778   7596   9151   -370    212    379       C  
ATOM   1734  C   ALA A 212      -8.163  21.774 108.034  1.00 61.71           C  
ANISOU 1734  C   ALA A 212     6910   7622   8915   -273    213    405       C  
ATOM   1735  O   ALA A 212      -8.520  22.598 108.891  1.00 62.51           O  
ANISOU 1735  O   ALA A 212     7029   7731   8993   -217    318    417       O  
ATOM   1736  CB  ALA A 212      -9.284  19.579 108.071  1.00 63.24           C  
ANISOU 1736  CB  ALA A 212     7022   7667   9338   -430    394    428       C  
ATOM   1737  N   TRP A 213      -6.918  21.645 107.651  1.00 60.30           N  
ANISOU 1737  N   TRP A 213     6840   7485   8585   -256     95    401       N  
ATOM   1738  CA  TRP A 213      -5.935  22.531 108.140  1.00 60.65           C  
ANISOU 1738  CA  TRP A 213     6994   7600   8450   -199     63    392       C  
ATOM   1739  C   TRP A 213      -6.217  23.982 107.806  1.00 60.80           C  
ANISOU 1739  C   TRP A 213     6980   7638   8483   -186     13    349       C  
ATOM   1740  O   TRP A 213      -6.152  24.872 108.686  1.00 61.65           O  
ANISOU 1740  O   TRP A 213     7166   7754   8504   -146     84    343       O  
ATOM   1741  CB  TRP A 213      -4.644  22.132 107.537  1.00 59.24           C  
ANISOU 1741  CB  TRP A 213     6874   7483   8153   -198    -62    377       C  
ATOM   1742  CG  TRP A 213      -3.615  23.022 107.822  1.00 60.08           C  
ANISOU 1742  CG  TRP A 213     7043   7678   8106   -178   -114    339       C  
ATOM   1743  CD1 TRP A 213      -2.763  22.980 108.884  1.00 61.11           C  
ANISOU 1743  CD1 TRP A 213     7266   7882   8071   -124    -88    337       C  
ATOM   1744  CD2 TRP A 213      -3.214  24.128 107.001  1.00 63.50           C  
ANISOU 1744  CD2 TRP A 213     7462   8143   8521   -221   -207    282       C  
ATOM   1745  NE1 TRP A 213      -1.833  24.023 108.781  1.00 60.84           N  
ANISOU 1745  NE1 TRP A 213     7242   7940   7935   -159   -170    263       N  
ATOM   1746  CE2 TRP A 213      -2.102  24.736 107.630  1.00 62.57           C  
ANISOU 1746  CE2 TRP A 213     7410   8118   8245   -228   -222    235       C  
ATOM   1747  CE3 TRP A 213      -3.694  24.669 105.780  1.00 64.39           C  
ANISOU 1747  CE3 TRP A 213     7532   8208   8726   -249   -278    261       C  
ATOM   1748  CZ2 TRP A 213      -1.465  25.866 107.083  1.00 63.93           C  
ANISOU 1748  CZ2 TRP A 213     7604   8318   8368   -298   -273    167       C  
ATOM   1749  CZ3 TRP A 213      -3.080  25.806 105.253  1.00 62.53           C  
ANISOU 1749  CZ3 TRP A 213     7357   7986   8417   -282   -322    212       C  
ATOM   1750  CH2 TRP A 213      -1.971  26.386 105.905  1.00 63.61           C  
ANISOU 1750  CH2 TRP A 213     7557   8198   8415   -325   -305    165       C  
ATOM   1751  N   SER A 214      -6.505  24.247 106.537  1.00 60.64           N  
ANISOU 1751  N   SER A 214     6881   7612   8548   -204   -108    316       N  
ATOM   1752  CA  SER A 214      -6.817  25.614 106.129  1.00 59.90           C  
ANISOU 1752  CA  SER A 214     6798   7510   8449   -161   -149    282       C  
ATOM   1753  C   SER A 214      -8.074  26.187 106.840  1.00 60.87           C  
ANISOU 1753  C   SER A 214     6855   7605   8669    -94    -29    293       C  
ATOM   1754  O   SER A 214      -8.097  27.383 107.108  1.00 61.27           O  
ANISOU 1754  O   SER A 214     6995   7638   8647    -36      1    280       O  
ATOM   1755  CB  SER A 214      -6.946  25.770 104.627  1.00 58.88           C  
ANISOU 1755  CB  SER A 214     6634   7371   8367   -155   -301    251       C  
ATOM   1756  OG  SER A 214      -5.997  25.014 103.927  1.00 60.20           O  
ANISOU 1756  OG  SER A 214     6840   7557   8477   -208   -386    247       O  
ATOM   1757  N   VAL A 215      -9.105  25.385 107.142  1.00 61.51           N  
ANISOU 1757  N   VAL A 215     6786   7675   8911   -106     56    312       N  
ATOM   1758  CA  VAL A 215     -10.262  25.940 107.914  1.00 61.69           C  
ANISOU 1758  CA  VAL A 215     6726   7686   9026    -33    205    322       C  
ATOM   1759  C   VAL A 215      -9.724  26.500 109.255  1.00 62.01           C  
ANISOU 1759  C   VAL A 215     6959   7704   8899      6    346    353       C  
ATOM   1760  O   VAL A 215      -9.910  27.688 109.618  1.00 61.37           O  
ANISOU 1760  O   VAL A 215     6960   7604   8751     91    391    342       O  
ATOM   1761  CB  VAL A 215     -11.371  24.911 108.208  1.00 63.76           C  
ANISOU 1761  CB  VAL A 215     6791   7942   9495    -88    327    331       C  
ATOM   1762  CG1 VAL A 215     -12.678  25.642 108.722  1.00 64.64           C  
ANISOU 1762  CG1 VAL A 215     6755   8071   9733      8    465    325       C  
ATOM   1763  CG2 VAL A 215     -11.643  23.969 107.003  1.00 62.28           C  
ANISOU 1763  CG2 VAL A 215     6446   7769   9448   -179    179    285       C  
ATOM   1764  N   ALA A 216      -9.022  25.640 109.991  1.00 61.73           N  
ANISOU 1764  N   ALA A 216     7021   7662   8770    -41    408    386       N  
ATOM   1765  CA  ALA A 216      -8.344  26.086 111.199  1.00 61.68           C  
ANISOU 1765  CA  ALA A 216     7213   7652   8569      3    493    398       C  
ATOM   1766  C   ALA A 216      -7.515  27.353 110.915  1.00 61.14           C  
ANISOU 1766  C   ALA A 216     7266   7608   8358      8    377    339       C  
ATOM   1767  O   ALA A 216      -7.723  28.376 111.534  1.00 61.30           O  
ANISOU 1767  O   ALA A 216     7390   7594   8306     64    451    322       O  
ATOM   1768  CB  ALA A 216      -7.481  24.984 111.765  1.00 60.12           C  
ANISOU 1768  CB  ALA A 216     7118   7469   8256    -17    508    430       C  
ATOM   1769  N   ARG A 217      -6.604  27.307 109.961  1.00 60.30           N  
ANISOU 1769  N   ARG A 217     7156   7544   8211    -57    216    303       N  
ATOM   1770  CA  ARG A 217      -5.693  28.439 109.871  1.00 60.18           C  
ANISOU 1770  CA  ARG A 217     7275   7541   8050    -89    150    239       C  
ATOM   1771  C   ARG A 217      -6.480  29.687 109.510  1.00 60.44           C  
ANISOU 1771  C   ARG A 217     7348   7495   8122    -33    181    224       C  
ATOM   1772  O   ARG A 217      -6.315  30.719 110.141  1.00 60.93           O  
ANISOU 1772  O   ARG A 217     7566   7514   8071    -18    242    190       O  
ATOM   1773  CB  ARG A 217      -4.501  28.220 108.897  1.00 59.09           C  
ANISOU 1773  CB  ARG A 217     7125   7465   7860   -179      4    199       C  
ATOM   1774  CG  ARG A 217      -3.449  29.336 109.042  1.00 60.28           C  
ANISOU 1774  CG  ARG A 217     7410   7635   7859   -254    -24    116       C  
ATOM   1775  CD  ARG A 217      -2.241  29.183 108.136  1.00 61.99           C  
ANISOU 1775  CD  ARG A 217     7597   7924   8034   -354   -130     69       C  
ATOM   1776  NE  ARG A 217      -1.226  30.266 108.271  1.00 64.21           N  
ANISOU 1776  NE  ARG A 217     7981   8224   8192   -470   -133    -32       N  
ATOM   1777  CZ  ARG A 217      -0.549  30.596 109.376  1.00 63.76           C  
ANISOU 1777  CZ  ARG A 217     7981   8237   8010   -516   -126   -106       C  
ATOM   1778  NH1 ARG A 217      -0.774  30.020 110.539  1.00 64.12           N  
ANISOU 1778  NH1 ARG A 217     8030   8328   8003   -424   -106    -80       N  
ATOM   1779  NH2 ARG A 217       0.347  31.564 109.324  1.00 67.69           N  
ANISOU 1779  NH2 ARG A 217     8550   8747   8422   -660   -132   -217       N  
ATOM   1780  N   LEU A 218      -7.332  29.571 108.497  1.00 60.28           N  
ANISOU 1780  N   LEU A 218     7199   7456   8250     12    132    243       N  
ATOM   1781  CA  LEU A 218      -8.090  30.698 107.985  1.00 60.60           C  
ANISOU 1781  CA  LEU A 218     7277   7430   8316    114    135    232       C  
ATOM   1782  C   LEU A 218      -9.035  31.268 109.040  1.00 61.13           C  
ANISOU 1782  C   LEU A 218     7369   7458   8398    228    296    252       C  
ATOM   1783  O   LEU A 218      -8.859  32.433 109.428  1.00 62.50           O  
ANISOU 1783  O   LEU A 218     7742   7559   8445    270    356    227       O  
ATOM   1784  CB  LEU A 218      -8.828  30.330 106.701  1.00 60.43           C  
ANISOU 1784  CB  LEU A 218     7095   7427   8440    167     17    237       C  
ATOM   1785  CG  LEU A 218      -8.022  30.134 105.394  1.00 63.29           C  
ANISOU 1785  CG  LEU A 218     7495   7791   8760    102   -139    215       C  
ATOM   1786  CD1 LEU A 218      -8.971  29.841 104.212  1.00 63.45           C  
ANISOU 1786  CD1 LEU A 218     7370   7826   8910    193   -266    210       C  
ATOM   1787  CD2 LEU A 218      -7.152  31.337 105.041  1.00 59.76           C  
ANISOU 1787  CD2 LEU A 218     7289   7269   8148     79   -140    184       C  
ATOM   1788  N   SER A 219      -9.999  30.474 109.513  1.00 60.30           N  
ANISOU 1788  N   SER A 219     7081   7390   8441    269    387    291       N  
ATOM   1789  CA  SER A 219     -10.978  30.930 110.523  1.00 61.20           C  
ANISOU 1789  CA  SER A 219     7193   7473   8586    388    574    316       C  
ATOM   1790  C   SER A 219     -10.347  31.742 111.643  1.00 61.58           C  
ANISOU 1790  C   SER A 219     7514   7458   8427    399    677    304       C  
ATOM   1791  O   SER A 219     -10.872  32.819 112.023  1.00 62.68           O  
ANISOU 1791  O   SER A 219     7772   7529   8515    523    776    299       O  
ATOM   1792  CB  SER A 219     -11.745  29.770 111.132  1.00 61.10           C  
ANISOU 1792  CB  SER A 219     6987   7499   8729    366    707    358       C  
ATOM   1793  OG  SER A 219     -12.305  29.026 110.087  1.00 61.35           O  
ANISOU 1793  OG  SER A 219     6770   7588   8953    327    599    344       O  
ATOM   1794  N   GLN A 220      -9.222  31.230 112.149  1.00 60.52           N  
ANISOU 1794  N   GLN A 220     7483   7348   8164    282    644    291       N  
ATOM   1795  CA  GLN A 220      -8.392  31.923 113.153  1.00 60.85           C  
ANISOU 1795  CA  GLN A 220     7779   7355   7986    261    685    247       C  
ATOM   1796  C   GLN A 220      -7.904  33.308 112.723  1.00 60.20           C  
ANISOU 1796  C   GLN A 220     7885   7200   7787    239    629    177       C  
ATOM   1797  O   GLN A 220      -7.973  34.229 113.509  1.00 61.77           O  
ANISOU 1797  O   GLN A 220     8288   7319   7862    288    728    147       O  
ATOM   1798  CB  GLN A 220      -7.200  31.057 113.504  1.00 60.14           C  
ANISOU 1798  CB  GLN A 220     7715   7346   7790    154    600    228       C  
ATOM   1799  CG  GLN A 220      -7.046  30.639 114.969  1.00 62.86           C  
ANISOU 1799  CG  GLN A 220     8188   7698   8000    203    711    245       C  
ATOM   1800  CD  GLN A 220      -5.626  30.056 115.245  1.00 64.70           C  
ANISOU 1800  CD  GLN A 220     8476   8034   8073    127    572    196       C  
ATOM   1801  OE1 GLN A 220      -4.834  29.783 114.308  1.00 63.98           O  
ANISOU 1801  OE1 GLN A 220     8284   8017   8009     31    417    162       O  
ATOM   1802  NE2 GLN A 220      -5.316  29.860 116.512  1.00 63.84           N  
ANISOU 1802  NE2 GLN A 220     8527   7940   7791    192    629    190       N  
ATOM   1803  N   LYS A 221      -7.421  33.477 111.495  1.00 58.79           N  
ANISOU 1803  N   LYS A 221     7673   7027   7637    165    493    149       N  
ATOM   1804  CA  LYS A 221      -6.969  34.785 111.064  1.00 59.16           C  
ANISOU 1804  CA  LYS A 221     7936   6973   7571    130    479     87       C  
ATOM   1805  C   LYS A 221      -8.157  35.683 110.746  1.00 61.15           C  
ANISOU 1805  C   LYS A 221     8250   7116   7868    318    561    122       C  
ATOM   1806  O   LYS A 221      -8.068  36.894 110.864  1.00 63.49           O  
ANISOU 1806  O   LYS A 221     8800   7282   8040    345    627     83       O  
ATOM   1807  CB  LYS A 221      -6.245  34.719 109.740  1.00 58.21           C  
ANISOU 1807  CB  LYS A 221     7781   6867   7470     23    346     63       C  
ATOM   1808  CG  LYS A 221      -5.053  33.892 109.585  1.00 58.88           C  
ANISOU 1808  CG  LYS A 221     7775   7067   7530   -139    242     28       C  
ATOM   1809  CD  LYS A 221      -4.468  34.159 108.139  1.00 63.72           C  
ANISOU 1809  CD  LYS A 221     8410   7651   8151   -220    157      6       C  
ATOM   1810  CE  LYS A 221      -2.897  33.980 108.067  1.00 61.45           C  
ANISOU 1810  CE  LYS A 221     8121   7452   7777   -425     97    -77       C  
ATOM   1811  NZ  LYS A 221      -2.168  34.853 109.099  1.00 61.89           N  
ANISOU 1811  NZ  LYS A 221     8340   7491   7686   -544    154   -182       N  
ATOM   1812  N   PHE A 222      -9.235  35.113 110.219  1.00 60.63           N  
ANISOU 1812  N   PHE A 222     7954   7103   7979    448    544    184       N  
ATOM   1813  CA  PHE A 222     -10.271  35.914 109.596  1.00 60.82           C  
ANISOU 1813  CA  PHE A 222     7995   7063   8051    650    563    206       C  
ATOM   1814  C   PHE A 222     -11.599  35.587 110.248  1.00 62.93           C  
ANISOU 1814  C   PHE A 222     8065   7387   8459    816    681    253       C  
ATOM   1815  O   PHE A 222     -12.566  35.224 109.559  1.00 63.26           O  
ANISOU 1815  O   PHE A 222     7861   7505   8670    933    626    274       O  
ATOM   1816  CB  PHE A 222     -10.364  35.533 108.144  1.00 60.11           C  
ANISOU 1816  CB  PHE A 222     7766   7018   8054    663    395    213       C  
ATOM   1817  CG  PHE A 222      -9.127  35.835 107.328  1.00 60.56           C  
ANISOU 1817  CG  PHE A 222     8005   7016   7989    512    302    174       C  
ATOM   1818  CD1 PHE A 222      -8.318  36.905 107.608  1.00 60.76           C  
ANISOU 1818  CD1 PHE A 222     8337   6912   7836    429    378    126       C  
ATOM   1819  CD2 PHE A 222      -8.815  35.058 106.223  1.00 61.99           C  
ANISOU 1819  CD2 PHE A 222     8051   7263   8239    448    153    177       C  
ATOM   1820  CE1 PHE A 222      -7.221  37.177 106.830  1.00 60.73           C  
ANISOU 1820  CE1 PHE A 222     8475   6856   7743    271    324     84       C  
ATOM   1821  CE2 PHE A 222      -7.714  35.361 105.421  1.00 59.08           C  
ANISOU 1821  CE2 PHE A 222     7849   6837   7763    320     99    145       C  
ATOM   1822  CZ  PHE A 222      -6.928  36.406 105.744  1.00 60.47           C  
ANISOU 1822  CZ  PHE A 222     8301   6895   7781    225    194     99       C  
ATOM   1823  N   PRO A 223     -11.658  35.686 111.587  1.00 63.62           N  
ANISOU 1823  N   PRO A 223     8248   7447   8478    824    848    260       N  
ATOM   1824  CA  PRO A 223     -12.791  35.284 112.439  1.00 65.47           C  
ANISOU 1824  CA  PRO A 223     8313   7728   8834    948   1020    308       C  
ATOM   1825  C   PRO A 223     -14.111  35.965 112.135  1.00 67.64           C  
ANISOU 1825  C   PRO A 223     8488   8003   9210   1202   1088    326       C  
ATOM   1826  O   PRO A 223     -15.135  35.555 112.667  1.00 68.96           O  
ANISOU 1826  O   PRO A 223     8439   8238   9524   1298   1231    358       O  
ATOM   1827  CB  PRO A 223     -12.361  35.735 113.834  1.00 65.36           C  
ANISOU 1827  CB  PRO A 223     8575   7629   8632    936   1179    298       C  
ATOM   1828  CG  PRO A 223     -11.371  36.804 113.580  1.00 66.11           C  
ANISOU 1828  CG  PRO A 223     8983   7612   8524    868   1099    232       C  
ATOM   1829  CD  PRO A 223     -10.618  36.349 112.376  1.00 63.39           C  
ANISOU 1829  CD  PRO A 223     8534   7325   8228    718    894    210       C  
ATOM   1830  N   LYS A 224     -14.069  37.009 111.330  1.00 68.53           N  
ANISOU 1830  N   LYS A 224     8769   8037   9234   1317   1005    305       N  
ATOM   1831  CA  LYS A 224     -15.245  37.760 110.983  1.00 72.49           C  
ANISOU 1831  CA  LYS A 224     9213   8539   9791   1607   1046    320       C  
ATOM   1832  C   LYS A 224     -15.658  37.441 109.550  1.00 73.26           C  
ANISOU 1832  C   LYS A 224     9076   8739  10022   1677    831    308       C  
ATOM   1833  O   LYS A 224     -16.736  37.855 109.117  1.00 76.14           O  
ANISOU 1833  O   LYS A 224     9302   9161  10466   1940    815    310       O  
ATOM   1834  CB  LYS A 224     -15.058  39.264 111.255  1.00 74.17           C  
ANISOU 1834  CB  LYS A 224     9848   8559   9773   1753   1144    311       C  
ATOM   1835  CG  LYS A 224     -15.273  40.178 110.058  1.00 78.13           C  
ANISOU 1835  CG  LYS A 224    10493   8987  10207   1948   1032    306       C  
ATOM   1836  CD  LYS A 224     -14.983  41.652 110.398  1.00 80.59           C  
ANISOU 1836  CD  LYS A 224    11293   9059  10267   2060   1164    296       C  
ATOM   1837  CE  LYS A 224     -14.773  42.418 109.107  1.00 82.11           C  
ANISOU 1837  CE  LYS A 224    11712   9135  10349   2165   1045    292       C  
ATOM   1838  NZ  LYS A 224     -13.948  43.659 109.313  1.00 82.88           N  
ANISOU 1838  NZ  LYS A 224    12347   8958  10185   2101   1161    260       N  
ATOM   1839  N   ALA A 225     -14.828  36.678 108.841  1.00 71.10           N  
ANISOU 1839  N   ALA A 225     8750   8499   9766   1460    663    290       N  
ATOM   1840  CA  ALA A 225     -15.262  36.055 107.614  1.00 71.25           C  
ANISOU 1840  CA  ALA A 225     8502   8638   9933   1493    461    271       C  
ATOM   1841  C   ALA A 225     -16.358  35.065 108.018  1.00 72.93           C  
ANISOU 1841  C   ALA A 225     8291   9017  10402   1502    518    268       C  
ATOM   1842  O   ALA A 225     -16.188  34.289 108.978  1.00 71.16           O  
ANISOU 1842  O   ALA A 225     7992   8809  10236   1333    657    287       O  
ATOM   1843  CB  ALA A 225     -14.084  35.315 106.941  1.00 67.90           C  
ANISOU 1843  CB  ALA A 225     8121   8208   9470   1240    309    256       C  
ATOM   1844  N   GLU A 226     -17.488  35.084 107.313  1.00 75.96           N  
ANISOU 1844  N   GLU A 226     8399   9525  10936   1699    419    237       N  
ATOM   1845  CA  GLU A 226     -18.551  34.095 107.617  1.00 78.55           C  
ANISOU 1845  CA  GLU A 226     8276  10026  11542   1664    477    209       C  
ATOM   1846  C   GLU A 226     -18.162  32.758 106.988  1.00 76.65           C  
ANISOU 1846  C   GLU A 226     7851   9849  11423   1403    323    174       C  
ATOM   1847  O   GLU A 226     -17.186  32.688 106.271  1.00 74.61           O  
ANISOU 1847  O   GLU A 226     7792   9523  11034   1305    166    175       O  
ATOM   1848  CB  GLU A 226     -19.927  34.614 107.171  1.00 81.79           C  
ANISOU 1848  CB  GLU A 226     8415  10579  12082   1972    425    166       C  
ATOM   1849  CG  GLU A 226     -21.191  33.911 107.738  1.00 87.96           C  
ANISOU 1849  CG  GLU A 226     8719  11542  13159   1971    567    127       C  
ATOM   1850  CD  GLU A 226     -21.242  33.696 109.280  1.00 91.10           C  
ANISOU 1850  CD  GLU A 226     9154  11874  13584   1867    917    187       C  
ATOM   1851  OE1 GLU A 226     -21.714  34.625 110.012  1.00 93.53           O  
ANISOU 1851  OE1 GLU A 226     9566  12148  13824   2096   1110    223       O  
ATOM   1852  OE2 GLU A 226     -20.872  32.568 109.726  1.00 85.57           O  
ANISOU 1852  OE2 GLU A 226     8386  11156  12969   1577   1003    198       O  
ATOM   1853  N   PHE A 227     -18.904  31.695 107.254  1.00 77.92           N  
ANISOU 1853  N   PHE A 227     7648  10128  11829   1282    387    142       N  
ATOM   1854  CA  PHE A 227     -18.442  30.373 106.859  1.00 76.14           C  
ANISOU 1854  CA  PHE A 227     7318   9919  11694   1011    293    116       C  
ATOM   1855  C   PHE A 227     -18.333  30.150 105.355  1.00 76.43           C  
ANISOU 1855  C   PHE A 227     7291  10012  11739   1019    -23     49       C  
ATOM   1856  O   PHE A 227     -17.462  29.413 104.935  1.00 73.56           O  
ANISOU 1856  O   PHE A 227     7033   9594  11323    832   -117     51       O  
ATOM   1857  CB  PHE A 227     -19.276  29.233 107.520  1.00 77.90           C  
ANISOU 1857  CB  PHE A 227     7198  10220  12181    845    473     91       C  
ATOM   1858  CG  PHE A 227     -18.708  27.819 107.263  1.00 73.97           C  
ANISOU 1858  CG  PHE A 227     6671   9687  11746    554    423     77       C  
ATOM   1859  CD1 PHE A 227     -17.410  27.472 107.688  1.00 70.67           C  
ANISOU 1859  CD1 PHE A 227     6581   9135  11137    419    469    150       C  
ATOM   1860  CD2 PHE A 227     -19.458  26.877 106.600  1.00 71.51           C  
ANISOU 1860  CD2 PHE A 227     6015   9481  11673    429    325    -19       C  
ATOM   1861  CE1 PHE A 227     -16.866  26.163 107.434  1.00 68.99           C  
ANISOU 1861  CE1 PHE A 227     6371   8882  10961    189    428    143       C  
ATOM   1862  CE2 PHE A 227     -18.967  25.615 106.343  1.00 73.45           C  
ANISOU 1862  CE2 PHE A 227     6274   9670  11963    176    290    -35       C  
ATOM   1863  CZ  PHE A 227     -17.669  25.236 106.750  1.00 70.55           C  
ANISOU 1863  CZ  PHE A 227     6255   9157  11395     68    346     54       C  
ATOM   1864  N   VAL A 228     -19.240  30.732 104.556  1.00 79.31           N  
ANISOU 1864  N   VAL A 228     7480  10491  12162   1255   -185    -15       N  
ATOM   1865  CA  VAL A 228     -19.236  30.472 103.102  1.00 80.15           C  
ANISOU 1865  CA  VAL A 228     7526  10660  12265   1287   -501    -91       C  
ATOM   1866  C   VAL A 228     -18.021  31.097 102.433  1.00 77.81           C  
ANISOU 1866  C   VAL A 228     7665  10211  11687   1326   -613    -37       C  
ATOM   1867  O   VAL A 228     -17.423  30.510 101.518  1.00 77.07           O  
ANISOU 1867  O   VAL A 228     7639  10096  11548   1214   -791    -63       O  
ATOM   1868  CB  VAL A 228     -20.520  30.935 102.361  1.00 83.82           C  
ANISOU 1868  CB  VAL A 228     7697  11311  12843   1568   -685   -186       C  
ATOM   1869  CG1 VAL A 228     -20.557  30.346 100.940  1.00 84.92           C  
ANISOU 1869  CG1 VAL A 228     7736  11528  13002   1548  -1019   -285       C  
ATOM   1870  CG2 VAL A 228     -21.756  30.475 103.086  1.00 87.75           C  
ANISOU 1870  CG2 VAL A 228     7733  11976  13632   1538   -538   -248       C  
ATOM   1871  N   GLU A 229     -17.661  32.289 102.892  1.00 76.57           N  
ANISOU 1871  N   GLU A 229     7812   9939  11343   1477   -490     33       N  
ATOM   1872  CA  GLU A 229     -16.456  32.925 102.424  1.00 74.39           C  
ANISOU 1872  CA  GLU A 229     7956   9498  10809   1467   -531     80       C  
ATOM   1873  C   GLU A 229     -15.260  32.085 102.839  1.00 71.26           C  
ANISOU 1873  C   GLU A 229     7664   9032  10380   1154   -457    111       C  
ATOM   1874  O   GLU A 229     -14.375  31.793 102.028  1.00 69.47           O  
ANISOU 1874  O   GLU A 229     7585   8754  10056   1053   -579    108       O  
ATOM   1875  CB  GLU A 229     -16.379  34.321 103.014  1.00 76.25           C  
ANISOU 1875  CB  GLU A 229     8488   9611  10873   1651   -372    133       C  
ATOM   1876  CG  GLU A 229     -15.165  35.144 102.626  1.00 76.28           C  
ANISOU 1876  CG  GLU A 229     8946   9423  10615   1621   -366    171       C  
ATOM   1877  CD  GLU A 229     -15.336  35.801 101.294  1.00 81.46           C  
ANISOU 1877  CD  GLU A 229     9768  10038  11145   1854   -547    158       C  
ATOM   1878  OE1 GLU A 229     -16.466  36.234 100.937  1.00 85.65           O  
ANISOU 1878  OE1 GLU A 229    10173  10653  11715   2156   -634    135       O  
ATOM   1879  OE2 GLU A 229     -14.317  35.889 100.596  1.00 84.08           O  
ANISOU 1879  OE2 GLU A 229    10365  10256  11328   1748   -597    171       O  
ATOM   1880  N   VAL A 230     -15.230  31.668 104.099  1.00 70.38           N  
ANISOU 1880  N   VAL A 230     7480   8922  10340   1019   -253    141       N  
ATOM   1881  CA  VAL A 230     -14.115  30.836 104.541  1.00 68.14           C  
ANISOU 1881  CA  VAL A 230     7293   8587  10009    764   -194    169       C  
ATOM   1882  C   VAL A 230     -14.017  29.592 103.664  1.00 67.49           C  
ANISOU 1882  C   VAL A 230     7045   8564  10033    625   -358    129       C  
ATOM   1883  O   VAL A 230     -12.947  29.301 103.121  1.00 66.82           O  
ANISOU 1883  O   VAL A 230     7128   8428   9832    520   -441    137       O  
ATOM   1884  CB  VAL A 230     -14.157  30.452 106.048  1.00 68.09           C  
ANISOU 1884  CB  VAL A 230     7252   8573  10047    666     46    209       C  
ATOM   1885  CG1 VAL A 230     -12.966  29.507 106.391  1.00 65.32           C  
ANISOU 1885  CG1 VAL A 230     7008   8186   9625    444     67    233       C  
ATOM   1886  CG2 VAL A 230     -14.099  31.710 106.920  1.00 66.93           C  
ANISOU 1886  CG2 VAL A 230     7330   8344   9754    795    203    241       C  
ATOM   1887  N   THR A 231     -15.145  28.903 103.503  1.00 68.64           N  
ANISOU 1887  N   THR A 231     6863   8818  10399    627   -397     76       N  
ATOM   1888  CA  THR A 231     -15.270  27.725 102.666  1.00 67.79           C  
ANISOU 1888  CA  THR A 231     6582   8763  10413    495   -555     14       C  
ATOM   1889  C   THR A 231     -14.648  27.914 101.293  1.00 66.19           C  
ANISOU 1889  C   THR A 231     6552   8531  10069    550   -792    -10       C  
ATOM   1890  O   THR A 231     -13.929  27.059 100.819  1.00 65.03           O  
ANISOU 1890  O   THR A 231     6470   8348   9890    402   -862    -15       O  
ATOM   1891  CB  THR A 231     -16.738  27.328 102.589  1.00 70.99           C  
ANISOU 1891  CB  THR A 231     6593   9306  11075    525   -583    -71       C  
ATOM   1892  OG1 THR A 231     -17.503  28.489 102.863  1.00 74.04           O  
ANISOU 1892  OG1 THR A 231     6927   9746  11459    768   -539    -68       O  
ATOM   1893  CG2 THR A 231     -17.123  26.285 103.604  1.00 72.05           C  
ANISOU 1893  CG2 THR A 231     6536   9445  11395    319   -365    -68       C  
ATOM   1894  N   LYS A 232     -14.936  29.055 100.689  1.00 66.56           N  
ANISOU 1894  N   LYS A 232     6698   8579  10014    782   -892    -18       N  
ATOM   1895  CA  LYS A 232     -14.454  29.465  99.386  1.00 65.75           C  
ANISOU 1895  CA  LYS A 232     6810   8428   9746    889  -1089    -31       C  
ATOM   1896  C   LYS A 232     -12.900  29.648  99.366  1.00 63.53           C  
ANISOU 1896  C   LYS A 232     6874   8007   9259    766  -1010     37       C  
ATOM   1897  O   LYS A 232     -12.197  28.998  98.581  1.00 62.69           O  
ANISOU 1897  O   LYS A 232     6848   7873   9097    667  -1112     26       O  
ATOM   1898  CB  LYS A 232     -15.193  30.770  99.062  1.00 66.70           C  
ANISOU 1898  CB  LYS A 232     6994   8559   9789   1199  -1145    -36       C  
ATOM   1899  CG  LYS A 232     -15.238  31.162  97.653  1.00 69.35           C  
ANISOU 1899  CG  LYS A 232     7479   8881   9991   1391  -1377    -70       C  
ATOM   1900  CD  LYS A 232     -14.023  31.973  97.264  1.00 72.60           C  
ANISOU 1900  CD  LYS A 232     8339   9106  10139   1403  -1312      3       C  
ATOM   1901  CE  LYS A 232     -14.082  32.345  95.782  1.00 76.64           C  
ANISOU 1901  CE  LYS A 232     9050   9581  10490   1616  -1529    -23       C  
ATOM   1902  NZ  LYS A 232     -13.485  31.274  94.935  1.00 78.00           N  
ANISOU 1902  NZ  LYS A 232     9222   9756  10657   1453  -1664    -56       N  
ATOM   1903  N   LEU A 233     -12.362  30.532 100.210  1.00 62.13           N  
ANISOU 1903  N   LEU A 233     6892   7746   8966    769   -829     95       N  
ATOM   1904  CA  LEU A 233     -10.899  30.645 100.356  1.00 60.11           C  
ANISOU 1904  CA  LEU A 233     6892   7395   8550    615   -743    134       C  
ATOM   1905  C   LEU A 233     -10.230  29.283 100.610  1.00 58.66           C  
ANISOU 1905  C   LEU A 233     6601   7254   8432    397   -733    135       C  
ATOM   1906  O   LEU A 233      -9.124  29.031 100.175  1.00 56.78           O  
ANISOU 1906  O   LEU A 233     6504   6980   8089    298   -753    144       O  
ATOM   1907  CB  LEU A 233     -10.513  31.622 101.484  1.00 59.51           C  
ANISOU 1907  CB  LEU A 233     6985   7248   8378    605   -546    168       C  
ATOM   1908  CG  LEU A 233     -11.147  33.002 101.649  1.00 61.36           C  
ANISOU 1908  CG  LEU A 233     7365   7412   8538    815   -482    178       C  
ATOM   1909  CD1 LEU A 233     -10.531  33.523 102.868  1.00 63.46           C  
ANISOU 1909  CD1 LEU A 233     7777   7614   8721    714   -291    196       C  
ATOM   1910  CD2 LEU A 233     -10.844  33.939 100.501  1.00 62.93           C  
ANISOU 1910  CD2 LEU A 233     7849   7495   8565    942   -554    179       C  
ATOM   1911  N   VAL A 234     -10.911  28.398 101.314  1.00 60.35           N  
ANISOU 1911  N   VAL A 234     6574   7539   8816    333   -686    128       N  
ATOM   1912  CA  VAL A 234     -10.384  27.049 101.542  1.00 61.05           C  
ANISOU 1912  CA  VAL A 234     6594   7645   8957    155   -666    134       C  
ATOM   1913  C   VAL A 234     -10.264  26.166 100.280  1.00 61.54           C  
ANISOU 1913  C   VAL A 234     6628   7714   9042    115   -847     92       C  
ATOM   1914  O   VAL A 234      -9.165  25.640  99.966  1.00 60.35           O  
ANISOU 1914  O   VAL A 234     6607   7531   8791     27   -860    110       O  
ATOM   1915  CB  VAL A 234     -11.101  26.360 102.683  1.00 61.86           C  
ANISOU 1915  CB  VAL A 234     6506   7783   9215     88   -521    144       C  
ATOM   1916  CG1 VAL A 234     -10.846  24.871 102.647  1.00 62.43           C  
ANISOU 1916  CG1 VAL A 234     6512   7851   9359    -67   -523    140       C  
ATOM   1917  CG2 VAL A 234     -10.576  26.941 103.985  1.00 63.38           C  
ANISOU 1917  CG2 VAL A 234     6834   7944   9302     83   -335    197       C  
ATOM   1918  N   THR A 235     -11.363  26.055  99.547  1.00 63.06           N  
ANISOU 1918  N   THR A 235     6654   7954   9352    194   -991     29       N  
ATOM   1919  CA  THR A 235     -11.365  25.440  98.224  1.00 64.20           C  
ANISOU 1919  CA  THR A 235     6805   8100   9489    194  -1197    -29       C  
ATOM   1920  C   THR A 235     -10.167  25.908  97.335  1.00 63.39           C  
ANISOU 1920  C   THR A 235     7003   7919   9163    238  -1251      3       C  
ATOM   1921  O   THR A 235      -9.386  25.084  96.786  1.00 62.74           O  
ANISOU 1921  O   THR A 235     7010   7804   9025    148  -1292      3       O  
ATOM   1922  CB  THR A 235     -12.717  25.735  97.552  1.00 67.00           C  
ANISOU 1922  CB  THR A 235     6967   8539   9953    341  -1373   -116       C  
ATOM   1923  OG1 THR A 235     -13.777  25.336  98.446  1.00 68.34           O  
ANISOU 1923  OG1 THR A 235     6830   8789  10346    279  -1280   -150       O  
ATOM   1924  CG2 THR A 235     -12.854  25.005  96.230  1.00 67.20           C  
ANISOU 1924  CG2 THR A 235     6982   8575   9976    338  -1610   -199       C  
ATOM   1925  N   ASP A 236      -9.993  27.220  97.232  1.00 63.31           N  
ANISOU 1925  N   ASP A 236     7165   7866   9023    371  -1220     33       N  
ATOM   1926  CA  ASP A 236      -8.948  27.755  96.367  1.00 63.11           C  
ANISOU 1926  CA  ASP A 236     7430   7753   8797    402  -1235     59       C  
ATOM   1927  C   ASP A 236      -7.549  27.626  97.023  1.00 60.08           C  
ANISOU 1927  C   ASP A 236     7154   7340   8332    235  -1066    107       C  
ATOM   1928  O   ASP A 236      -6.546  27.417  96.321  1.00 58.89           O  
ANISOU 1928  O   ASP A 236     7154   7151   8070    187  -1071    116       O  
ATOM   1929  CB  ASP A 236      -9.328  29.135  95.724  1.00 64.33           C  
ANISOU 1929  CB  ASP A 236     7777   7842   8823    620  -1280     63       C  
ATOM   1930  CG  ASP A 236     -10.360  28.990  94.482  1.00 72.10           C  
ANISOU 1930  CG  ASP A 236     8713   8865   9817    817  -1536     -2       C  
ATOM   1931  OD1 ASP A 236     -10.184  28.060  93.608  1.00 75.79           O  
ANISOU 1931  OD1 ASP A 236     9176   9343  10280    771  -1677    -42       O  
ATOM   1932  OD2 ASP A 236     -11.338  29.803  94.361  1.00 74.68           O  
ANISOU 1932  OD2 ASP A 236     9015   9217  10142   1036  -1609    -21       O  
ATOM   1933  N   LEU A 237      -7.488  27.647  98.355  1.00 58.78           N  
ANISOU 1933  N   LEU A 237     6898   7211   8225    154   -923    130       N  
ATOM   1934  CA  LEU A 237      -6.189  27.455  99.027  1.00 56.20           C  
ANISOU 1934  CA  LEU A 237     6642   6894   7820     15   -799    155       C  
ATOM   1935  C   LEU A 237      -5.727  25.966  99.053  1.00 54.93           C  
ANISOU 1935  C   LEU A 237     6385   6780   7706    -83   -822    159       C  
ATOM   1936  O   LEU A 237      -4.542  25.707  98.811  1.00 55.08           O  
ANISOU 1936  O   LEU A 237     6493   6808   7625   -143   -798    167       O  
ATOM   1937  CB  LEU A 237      -6.140  28.077 100.435  1.00 55.56           C  
ANISOU 1937  CB  LEU A 237     6553   6826   7732    -18   -649    171       C  
ATOM   1938  CG  LEU A 237      -4.759  27.983 101.148  1.00 53.67           C  
ANISOU 1938  CG  LEU A 237     6376   6624   7393   -146   -553    173       C  
ATOM   1939  CD1 LEU A 237      -3.601  28.568 100.334  1.00 53.79           C  
ANISOU 1939  CD1 LEU A 237     6556   6606   7274   -201   -546    152       C  
ATOM   1940  CD2 LEU A 237      -4.727  28.676 102.475  1.00 53.25           C  
ANISOU 1940  CD2 LEU A 237     6350   6578   7306   -168   -432    170       C  
ATOM   1941  N   THR A 238      -6.606  25.004  99.329  1.00 53.57           N  
ANISOU 1941  N   THR A 238     6044   6632   7678    -99   -853    150       N  
ATOM   1942  CA  THR A 238      -6.213  23.585  99.125  1.00 54.42           C  
ANISOU 1942  CA  THR A 238     6124   6742   7810   -176   -879    151       C  
ATOM   1943  C   THR A 238      -5.738  23.254  97.671  1.00 54.44           C  
ANISOU 1943  C   THR A 238     6241   6710   7734   -151  -1010    127       C  
ATOM   1944  O   THR A 238      -4.729  22.569  97.460  1.00 53.06           O  
ANISOU 1944  O   THR A 238     6146   6534   7479   -188   -988    144       O  
ATOM   1945  CB  THR A 238      -7.346  22.652  99.511  1.00 56.17           C  
ANISOU 1945  CB  THR A 238     6169   6963   8210   -223   -877    130       C  
ATOM   1946  OG1 THR A 238      -7.733  22.963 100.857  1.00 59.91           O  
ANISOU 1946  OG1 THR A 238     6566   7458   8737   -235   -725    162       O  
ATOM   1947  CG2 THR A 238      -6.949  21.167  99.412  1.00 54.72           C  
ANISOU 1947  CG2 THR A 238     6007   6745   8039   -309   -870    134       C  
ATOM   1948  N   LYS A 239      -6.459  23.761  96.682  1.00 55.05           N  
ANISOU 1948  N   LYS A 239     6337   6761   7817    -63  -1143     87       N  
ATOM   1949  CA  LYS A 239      -6.023  23.615  95.293  1.00 55.50           C  
ANISOU 1949  CA  LYS A 239     6553   6771   7766    -11  -1260     66       C  
ATOM   1950  C   LYS A 239      -4.607  24.077  94.982  1.00 54.58           C  
ANISOU 1950  C   LYS A 239     6629   6629   7478    -20  -1165    107       C  
ATOM   1951  O   LYS A 239      -3.881  23.386  94.315  1.00 53.77           O  
ANISOU 1951  O   LYS A 239     6616   6508   7306    -34  -1181    108       O  
ATOM   1952  CB  LYS A 239      -6.980  24.302  94.334  1.00 55.75           C  
ANISOU 1952  CB  LYS A 239     6615   6781   7788    130  -1422     19       C  
ATOM   1953  CG  LYS A 239      -6.505  24.099  92.928  1.00 56.02           C  
ANISOU 1953  CG  LYS A 239     6852   6753   7682    196  -1533      1       C  
ATOM   1954  CD  LYS A 239      -7.497  24.712  91.883  1.00 66.34           C  
ANISOU 1954  CD  LYS A 239     8218   8043   8946    380  -1733    -54       C  
ATOM   1955  CE  LYS A 239      -7.008  24.482  90.446  1.00 65.86           C  
ANISOU 1955  CE  LYS A 239     8407   7903   8712    464  -1842    -71       C  
ATOM   1956  NZ  LYS A 239      -6.406  23.107  90.482  1.00 65.92           N  
ANISOU 1956  NZ  LYS A 239     8378   7908   8760    316  -1815    -79       N  
ATOM   1957  N   VAL A 240      -4.258  25.273  95.436  1.00 54.90           N  
ANISOU 1957  N   VAL A 240     6736   6666   7458    -15  -1058    129       N  
ATOM   1958  CA  VAL A 240      -2.918  25.850  95.291  1.00 54.40           C  
ANISOU 1958  CA  VAL A 240     6821   6590   7258    -67   -935    149       C  
ATOM   1959  C   VAL A 240      -1.839  24.931  95.924  1.00 54.16           C  
ANISOU 1959  C   VAL A 240     6705   6648   7226   -167   -856    160       C  
ATOM   1960  O   VAL A 240      -0.804  24.626  95.306  1.00 54.51           O  
ANISOU 1960  O   VAL A 240     6825   6702   7183   -185   -820    162       O  
ATOM   1961  CB  VAL A 240      -2.910  27.318  95.951  1.00 55.60           C  
ANISOU 1961  CB  VAL A 240     7041   6712   7371    -78   -822    152       C  
ATOM   1962  CG1 VAL A 240      -1.527  27.847  96.252  1.00 52.60           C  
ANISOU 1962  CG1 VAL A 240     6737   6352   6898   -202   -668    146       C  
ATOM   1963  CG2 VAL A 240      -3.749  28.301  95.132  1.00 51.81           C  
ANISOU 1963  CG2 VAL A 240     6720   6128   6839     67   -884    150       C  
ATOM   1964  N   HIS A 241      -2.105  24.462  97.137  1.00 54.20           N  
ANISOU 1964  N   HIS A 241     6560   6717   7317   -207   -824    169       N  
ATOM   1965  CA  HIS A 241      -1.224  23.497  97.784  1.00 54.25           C  
ANISOU 1965  CA  HIS A 241     6500   6806   7305   -250   -770    183       C  
ATOM   1966  C   HIS A 241      -1.130  22.156  97.119  1.00 54.31           C  
ANISOU 1966  C   HIS A 241     6525   6793   7318   -220   -832    192       C  
ATOM   1967  O   HIS A 241      -0.026  21.782  96.789  1.00 55.74           O  
ANISOU 1967  O   HIS A 241     6752   7018   7410   -211   -796    197       O  
ATOM   1968  CB  HIS A 241      -1.468  23.362  99.285  1.00 54.25           C  
ANISOU 1968  CB  HIS A 241     6393   6864   7357   -276   -704    198       C  
ATOM   1969  CG  HIS A 241      -1.024  24.557 100.034  1.00 54.20           C  
ANISOU 1969  CG  HIS A 241     6400   6901   7294   -319   -624    178       C  
ATOM   1970  ND1 HIS A 241      -1.821  25.194 100.951  1.00 57.89           N  
ANISOU 1970  ND1 HIS A 241     6838   7348   7808   -315   -582    180       N  
ATOM   1971  CD2 HIS A 241       0.091  25.307  99.918  1.00 55.54           C  
ANISOU 1971  CD2 HIS A 241     6620   7117   7366   -378   -570    144       C  
ATOM   1972  CE1 HIS A 241      -1.209  26.268 101.404  1.00 53.06           C  
ANISOU 1972  CE1 HIS A 241     6283   6760   7118   -367   -516    148       C  
ATOM   1973  NE2 HIS A 241      -0.051  26.368 100.779  1.00 58.77           N  
ANISOU 1973  NE2 HIS A 241     7046   7524   7760   -421   -509    119       N  
ATOM   1974  N   LYS A 242      -2.245  21.448  96.932  1.00 55.01           N  
ANISOU 1974  N   LYS A 242     6573   6817   7509   -209   -915    183       N  
ATOM   1975  CA  LYS A 242      -2.314  20.229  96.082  1.00 55.16           C  
ANISOU 1975  CA  LYS A 242     6651   6776   7530   -193   -993    170       C  
ATOM   1976  C   LYS A 242      -1.437  20.376  94.864  1.00 55.26           C  
ANISOU 1976  C   LYS A 242     6815   6770   7410   -141  -1018    165       C  
ATOM   1977  O   LYS A 242      -0.565  19.569  94.616  1.00 56.36           O  
ANISOU 1977  O   LYS A 242     7018   6919   7476   -117   -981    181       O  
ATOM   1978  CB  LYS A 242      -3.771  19.911  95.727  1.00 55.43           C  
ANISOU 1978  CB  LYS A 242     6618   6745   7698   -210  -1112    122       C  
ATOM   1979  CG  LYS A 242      -4.086  18.737  94.809  1.00 57.28           C  
ANISOU 1979  CG  LYS A 242     6917   6899   7949   -221  -1219     77       C  
ATOM   1980  CD  LYS A 242      -5.656  18.660  94.417  1.00 61.25           C  
ANISOU 1980  CD  LYS A 242     7295   7371   8605   -256  -1370     -9       C  
ATOM   1981  CE  LYS A 242      -6.218  20.022  93.687  1.00 65.76           C  
ANISOU 1981  CE  LYS A 242     7864   7975   9147   -145  -1499    -43       C  
ATOM   1982  NZ  LYS A 242      -7.692  20.078  93.119  1.00 68.50           N  
ANISOU 1982  NZ  LYS A 242     8072   8338   9616   -120  -1697   -146       N  
ATOM   1983  N   GLU A 243      -1.594  21.439  94.116  1.00 55.46           N  
ANISOU 1983  N   GLU A 243     6921   6763   7388   -107  -1056    150       N  
ATOM   1984  CA  GLU A 243      -0.854  21.518  92.875  1.00 55.43           C  
ANISOU 1984  CA  GLU A 243     7097   6714   7252    -53  -1060    149       C  
ATOM   1985  C   GLU A 243       0.629  21.722  93.181  1.00 55.45           C  
ANISOU 1985  C   GLU A 243     7100   6800   7169    -88   -898    175       C  
ATOM   1986  O   GLU A 243       1.505  21.092  92.572  1.00 54.27           O  
ANISOU 1986  O   GLU A 243     7025   6657   6936    -52   -858    183       O  
ATOM   1987  CB  GLU A 243      -1.388  22.670  92.043  1.00 56.24           C  
ANISOU 1987  CB  GLU A 243     7327   6743   7300     12  -1119    133       C  
ATOM   1988  CG  GLU A 243      -2.838  22.614  91.870  1.00 54.86           C  
ANISOU 1988  CG  GLU A 243     7093   6535   7218     63  -1289     91       C  
ATOM   1989  CD  GLU A 243      -3.340  23.737  91.014  1.00 54.79           C  
ANISOU 1989  CD  GLU A 243     7237   6458   7122    182  -1363     78       C  
ATOM   1990  OE1 GLU A 243      -3.389  24.907  91.405  1.00 58.10           O  
ANISOU 1990  OE1 GLU A 243     7684   6870   7521    199  -1284    100       O  
ATOM   1991  OE2 GLU A 243      -3.725  23.445  89.923  1.00 59.04           O  
ANISOU 1991  OE2 GLU A 243     7896   6940   7596    277  -1507     43       O  
ATOM   1992  N   CYS A 244       0.905  22.618  94.131  1.00 55.51           N  
ANISOU 1992  N   CYS A 244     7017   6878   7197   -155   -807    176       N  
ATOM   1993  CA  CYS A 244       2.316  22.817  94.552  1.00 56.33           C  
ANISOU 1993  CA  CYS A 244     7066   7099   7238   -211   -670    172       C  
ATOM   1994  C   CYS A 244       2.976  21.546  94.964  1.00 54.72           C  
ANISOU 1994  C   CYS A 244     6775   6990   7025   -169   -661    186       C  
ATOM   1995  O   CYS A 244       3.970  21.197  94.368  1.00 55.67           O  
ANISOU 1995  O   CYS A 244     6927   7155   7069   -136   -603    185       O  
ATOM   1996  CB  CYS A 244       2.498  23.977  95.517  1.00 55.55           C  
ANISOU 1996  CB  CYS A 244     6894   7058   7156   -307   -590    148       C  
ATOM   1997  SG  CYS A 244       3.057  25.399  94.492  1.00 64.75           S  
ANISOU 1997  SG  CYS A 244     8243   8133   8226   -369   -471    126       S  
ATOM   1998  N   CYS A 245       2.299  20.767  95.808  1.00 53.80           N  
ANISOU 1998  N   CYS A 245     6588   6875   6980   -149   -715    204       N  
ATOM   1999  CA  CYS A 245       2.802  19.484  96.330  1.00 54.19           C  
ANISOU 1999  CA  CYS A 245     6601   6985   7005    -81   -700    229       C  
ATOM   2000  C   CYS A 245       2.994  18.373  95.299  1.00 54.70           C  
ANISOU 2000  C   CYS A 245     6794   6972   7017      3   -729    242       C  
ATOM   2001  O   CYS A 245       3.736  17.441  95.534  1.00 54.79           O  
ANISOU 2001  O   CYS A 245     6810   7040   6966     90   -689    264       O  
ATOM   2002  CB  CYS A 245       1.962  19.021  97.525  1.00 54.16           C  
ANISOU 2002  CB  CYS A 245     6535   6963   7079    -90   -712    250       C  
ATOM   2003  SG  CYS A 245       2.300  20.112  99.032  1.00 55.94           S  
ANISOU 2003  SG  CYS A 245     6627   7330   7299   -143   -647    234       S  
ATOM   2004  N   HIS A 246       2.343  18.529  94.156  1.00 55.34           N  
ANISOU 2004  N   HIS A 246     6995   6927   7106     -4   -803    226       N  
ATOM   2005  CA  HIS A 246       2.316  17.591  93.050  1.00 55.99           C  
ANISOU 2005  CA  HIS A 246     7239   6904   7132     65   -854    222       C  
ATOM   2006  C   HIS A 246       3.269  18.060  91.893  1.00 57.26           C  
ANISOU 2006  C   HIS A 246     7517   7071   7169    116   -792    220       C  
ATOM   2007  O   HIS A 246       3.280  17.460  90.827  1.00 57.70           O  
ANISOU 2007  O   HIS A 246     7745   7028   7151    186   -830    214       O  
ATOM   2008  CB  HIS A 246       0.858  17.483  92.549  1.00 55.97           C  
ANISOU 2008  CB  HIS A 246     7289   6763   7212     27  -1002    184       C  
ATOM   2009  CG  HIS A 246       0.629  16.397  91.545  1.00 58.31           C  
ANISOU 2009  CG  HIS A 246     7756   6937   7463     73  -1085    157       C  
ATOM   2010  ND1 HIS A 246       0.158  16.645  90.266  1.00 62.78           N  
ANISOU 2010  ND1 HIS A 246     8467   7409   7977    106  -1205    111       N  
ATOM   2011  CD2 HIS A 246       0.803  15.058  91.628  1.00 59.49           C  
ANISOU 2011  CD2 HIS A 246     7985   7026   7592    101  -1065    164       C  
ATOM   2012  CE1 HIS A 246       0.078  15.510  89.596  1.00 63.95           C  
ANISOU 2012  CE1 HIS A 246     8767   7453   8078    139  -1265     81       C  
ATOM   2013  NE2 HIS A 246       0.461  14.529  90.404  1.00 66.74           N  
ANISOU 2013  NE2 HIS A 246     9089   7815   8453    130  -1172    114       N  
ATOM   2014  N   GLY A 247       4.058  19.121  92.088  1.00 57.31           N  
ANISOU 2014  N   GLY A 247     7446   7181   7150     70   -684    217       N  
ATOM   2015  CA  GLY A 247       4.985  19.606  91.005  1.00 57.69           C  
ANISOU 2015  CA  GLY A 247     7607   7223   7088     93   -575    214       C  
ATOM   2016  C   GLY A 247       4.365  20.418  89.839  1.00 58.34           C  
ANISOU 2016  C   GLY A 247     7902   7148   7116     98   -613    207       C  
ATOM   2017  O   GLY A 247       5.048  20.753  88.847  1.00 59.33           O  
ANISOU 2017  O   GLY A 247     8180   7230   7132    130   -506    213       O  
ATOM   2018  N   ASP A 248       3.065  20.688  89.930  1.00 57.25           N  
ANISOU 2018  N   ASP A 248     7785   6925   7043     89   -762    194       N  
ATOM   2019  CA  ASP A 248       2.344  21.550  89.013  1.00 57.85           C  
ANISOU 2019  CA  ASP A 248     8046   6872   7062    129   -830    183       C  
ATOM   2020  C   ASP A 248       2.656  23.028  89.477  1.00 55.51           C  
ANISOU 2020  C   ASP A 248     7722   6601   6768     42   -695    189       C  
ATOM   2021  O   ASP A 248       1.800  23.764  89.911  1.00 52.60           O  
ANISOU 2021  O   ASP A 248     7326   6206   6456     27   -757    181       O  
ATOM   2022  CB  ASP A 248       0.815  21.219  89.023  1.00 58.54           C  
ANISOU 2022  CB  ASP A 248     8110   6897   7234    165  -1055    148       C  
ATOM   2023  CG  ASP A 248       0.504  19.709  88.794  1.00 65.54           C  
ANISOU 2023  CG  ASP A 248     9003   7754   8146    192  -1169    123       C  
ATOM   2024  OD1 ASP A 248       1.327  18.961  88.158  1.00 72.26           O  
ANISOU 2024  OD1 ASP A 248     9984   8578   8894    246  -1112    135       O  
ATOM   2025  OD2 ASP A 248      -0.608  19.250  89.205  1.00 69.01           O  
ANISOU 2025  OD2 ASP A 248     9330   8183   8708    157  -1309     84       O  
ATOM   2026  N   LEU A 249       3.920  23.409  89.374  1.00 55.12           N  
ANISOU 2026  N   LEU A 249     7681   6604   6659    -20   -497    195       N  
ATOM   2027  CA  LEU A 249       4.414  24.667  89.900  1.00 55.05           C  
ANISOU 2027  CA  LEU A 249     7632   6625   6661   -149   -342    180       C  
ATOM   2028  C   LEU A 249       3.909  25.913  89.185  1.00 55.74           C  
ANISOU 2028  C   LEU A 249     7978   6537   6663   -128   -303    190       C  
ATOM   2029  O   LEU A 249       3.715  26.923  89.837  1.00 55.89           O  
ANISOU 2029  O   LEU A 249     7978   6542   6716   -212   -250    177       O  
ATOM   2030  CB  LEU A 249       5.908  24.667  89.885  1.00 55.16           C  
ANISOU 2030  CB  LEU A 249     7562   6750   6645   -238   -138    162       C  
ATOM   2031  CG  LEU A 249       6.580  23.551  90.626  1.00 57.84           C  
ANISOU 2031  CG  LEU A 249     7654   7282   7041   -225   -158    151       C  
ATOM   2032  CD1 LEU A 249       8.044  23.949  90.781  1.00 63.88           C  
ANISOU 2032  CD1 LEU A 249     8277   8198   7798   -338     49    106       C  
ATOM   2033  CD2 LEU A 249       5.939  23.251  92.016  1.00 55.49           C  
ANISOU 2033  CD2 LEU A 249     7158   7073   6851   -243   -291    144       C  
ATOM   2034  N   LEU A 250       3.746  25.831  87.860  1.00 56.27           N  
ANISOU 2034  N   LEU A 250     8315   6465   6600     -1   -323    214       N  
ATOM   2035  CA  LEU A 250       3.139  26.884  87.046  1.00 56.25           C  
ANISOU 2035  CA  LEU A 250     8620   6277   6476     90   -319    232       C  
ATOM   2036  C   LEU A 250       1.662  27.133  87.366  1.00 55.30           C  
ANISOU 2036  C   LEU A 250     8479   6124   6407    196   -546    224       C  
ATOM   2037  O   LEU A 250       1.293  28.303  87.467  1.00 56.01           O  
ANISOU 2037  O   LEU A 250     8701   6122   6457    212   -494    233       O  
ATOM   2038  CB  LEU A 250       3.361  26.657  85.548  1.00 56.90           C  
ANISOU 2038  CB  LEU A 250     9020   6222   6378    230   -292    258       C  
ATOM   2039  CG  LEU A 250       4.775  26.398  84.981  1.00 58.05           C  
ANISOU 2039  CG  LEU A 250     9227   6380   6450    164    -43    271       C  
ATOM   2040  CD1 LEU A 250       4.662  26.145  83.473  1.00 63.77           C  
ANISOU 2040  CD1 LEU A 250    10319   6938   6973    354    -62    300       C  
ATOM   2041  CD2 LEU A 250       5.776  27.506  85.136  1.00 56.92           C  
ANISOU 2041  CD2 LEU A 250     9123   6212   6292    -13    269    269       C  
ATOM   2042  N   GLU A 251       0.858  26.084  87.585  1.00 59.16           N  
ANISOU 2042  N   GLU A 251     8160   7413   6907    -54   -171    510       N  
ATOM   2043  CA  GLU A 251      -0.582  26.219  87.905  1.00 60.52           C  
ANISOU 2043  CA  GLU A 251     8273   7594   7127   -110   -324    384       C  
ATOM   2044  C   GLU A 251      -0.750  26.766  89.287  1.00 59.76           C  
ANISOU 2044  C   GLU A 251     8066   7422   7218    -56   -387    430       C  
ATOM   2045  O   GLU A 251      -1.680  27.543  89.550  1.00 59.34           O  
ANISOU 2045  O   GLU A 251     7925   7397   7226    -61   -562    409       O  
ATOM   2046  CB  GLU A 251      -1.349  24.885  87.922  1.00 61.53           C  
ANISOU 2046  CB  GLU A 251     8462   7677   7239   -212   -184    148       C  
ATOM   2047  CG  GLU A 251      -1.554  24.179  86.617  1.00 66.82           C  
ANISOU 2047  CG  GLU A 251     9234   8437   7719   -320   -123     -3       C  
ATOM   2048  CD  GLU A 251      -0.354  23.355  86.163  1.00 70.84           C  
ANISOU 2048  CD  GLU A 251     9910   8860   8145   -279    129     48       C  
ATOM   2049  OE1 GLU A 251       0.797  23.874  86.226  1.00 68.69           O  
ANISOU 2049  OE1 GLU A 251     9622   8589   7886   -154    147    255       O  
ATOM   2050  OE2 GLU A 251      -0.581  22.183  85.721  1.00 76.37           O  
ANISOU 2050  OE2 GLU A 251    10749   9499   8769   -385    330   -149       O  
ATOM   2051  N   CYS A 252       0.130  26.310  90.170  1.00 59.99           N  
ANISOU 2051  N   CYS A 252     8101   7377   7314     26   -243    481       N  
ATOM   2052  CA  CYS A 252       0.156  26.688  91.566  1.00 60.71           C  
ANISOU 2052  CA  CYS A 252     8107   7420   7540     99   -279    514       C  
ATOM   2053  C   CYS A 252       0.372  28.203  91.708  1.00 60.97           C  
ANISOU 2053  C   CYS A 252     8025   7500   7642     85   -450    618       C  
ATOM   2054  O   CYS A 252      -0.457  28.902  92.333  1.00 60.60           O  
ANISOU 2054  O   CYS A 252     7919   7414   7692     73   -573    594       O  
ATOM   2055  CB  CYS A 252       1.306  25.949  92.263  1.00 61.51           C  
ANISOU 2055  CB  CYS A 252     8236   7512   7623    258   -114    566       C  
ATOM   2056  SG  CYS A 252       1.444  26.411  93.962  1.00 64.38           S  
ANISOU 2056  SG  CYS A 252     8499   7880   8082    378   -180    596       S  
ATOM   2057  N   ALA A 253       1.489  28.691  91.131  1.00 61.19           N  
ANISOU 2057  N   ALA A 253     8034   7590   7624     75   -416    714       N  
ATOM   2058  CA  ALA A 253       1.872  30.115  91.157  1.00 61.41           C  
ANISOU 2058  CA  ALA A 253     8005   7614   7713     13   -489    797       C  
ATOM   2059  C   ALA A 253       0.727  31.012  90.710  1.00 61.95           C  
ANISOU 2059  C   ALA A 253     8151   7609   7779     -7   -634    832       C  
ATOM   2060  O   ALA A 253       0.268  31.906  91.433  1.00 61.73           O  
ANISOU 2060  O   ALA A 253     8086   7507   7862     -1   -721    839       O  
ATOM   2061  CB  ALA A 253       3.031  30.328  90.289  1.00 60.90           C  
ANISOU 2061  CB  ALA A 253     7953   7611   7576    -46   -369    860       C  
ATOM   2062  N   ASP A 254       0.249  30.732  89.510  1.00 63.17           N  
ANISOU 2062  N   ASP A 254     8414   7804   7782      1   -661    842       N  
ATOM   2063  CA  ASP A 254      -0.836  31.488  88.900  1.00 63.85           C  
ANISOU 2063  CA  ASP A 254     8572   7893   7797     62   -823    878       C  
ATOM   2064  C   ASP A 254      -2.132  31.480  89.751  1.00 62.29           C  
ANISOU 2064  C   ASP A 254     8252   7703   7712    115   -963    757       C  
ATOM   2065  O   ASP A 254      -2.878  32.453  89.760  1.00 63.14           O  
ANISOU 2065  O   ASP A 254     8367   7787   7836    212  -1096    803       O  
ATOM   2066  CB  ASP A 254      -1.057  30.977  87.467  1.00 65.31           C  
ANISOU 2066  CB  ASP A 254     8870   8198   7745     79   -840    868       C  
ATOM   2067  CG  ASP A 254      -1.994  31.859  86.652  1.00 69.80           C  
ANISOU 2067  CG  ASP A 254     9535   8827   8160    219  -1024    940       C  
ATOM   2068  OD1 ASP A 254      -2.364  31.490  85.503  1.00 71.68           O  
ANISOU 2068  OD1 ASP A 254     9850   9224   8160    266  -1091    905       O  
ATOM   2069  OD2 ASP A 254      -2.373  32.937  87.155  1.00 74.28           O  
ANISOU 2069  OD2 ASP A 254    10112   9293   8818    312  -1104   1028       O  
ATOM   2070  N   ASP A 255      -2.388  30.392  90.455  1.00 61.06           N  
ANISOU 2070  N   ASP A 255     8007   7564   7628     65   -898    606       N  
ATOM   2071  CA  ASP A 255      -3.597  30.259  91.287  1.00 61.73           C  
ANISOU 2071  CA  ASP A 255     7973   7655   7827     72   -967    459       C  
ATOM   2072  C   ASP A 255      -3.436  30.952  92.644  1.00 59.40           C  
ANISOU 2072  C   ASP A 255     7626   7240   7702    100   -962    502       C  
ATOM   2073  O   ASP A 255      -4.385  31.406  93.192  1.00 60.56           O  
ANISOU 2073  O   ASP A 255     7692   7378   7940    138  -1046    437       O  
ATOM   2074  CB  ASP A 255      -4.025  28.775  91.466  1.00 61.75           C  
ANISOU 2074  CB  ASP A 255     7959   7677   7825    -30   -828    259       C  
ATOM   2075  CG  ASP A 255      -4.648  28.161  90.193  1.00 68.06           C  
ANISOU 2075  CG  ASP A 255     8757   8636   8465    -98   -866    111       C  
ATOM   2076  OD1 ASP A 255      -5.315  28.874  89.399  1.00 74.17           O  
ANISOU 2076  OD1 ASP A 255     9469   9571   9139    -24  -1072    107       O  
ATOM   2077  OD2 ASP A 255      -4.517  26.938  89.985  1.00 72.94           O  
ANISOU 2077  OD2 ASP A 255     9448   9229   9037   -211   -684    -19       O  
ATOM   2078  N   ARG A 256      -2.236  31.002  93.180  1.00 58.01           N  
ANISOU 2078  N   ARG A 256     7476   7009   7556     85   -863    584       N  
ATOM   2079  CA  ARG A 256      -1.920  31.867  94.304  1.00 57.90           C  
ANISOU 2079  CA  ARG A 256     7412   6923   7664     95   -878    611       C  
ATOM   2080  C   ARG A 256      -2.090  33.343  94.000  1.00 59.48           C  
ANISOU 2080  C   ARG A 256     7655   7041   7904    105   -963    699       C  
ATOM   2081  O   ARG A 256      -2.585  34.123  94.846  1.00 58.89           O  
ANISOU 2081  O   ARG A 256     7551   6880   7943    130  -1008    670       O  
ATOM   2082  CB  ARG A 256      -0.496  31.673  94.678  1.00 57.90           C  
ANISOU 2082  CB  ARG A 256     7387   6967   7645     76   -778    646       C  
ATOM   2083  CG  ARG A 256      -0.259  31.732  96.133  1.00 59.79           C  
ANISOU 2083  CG  ARG A 256     7549   7215   7953    111   -769    585       C  
ATOM   2084  CD  ARG A 256       1.240  31.915  96.419  1.00 61.03           C  
ANISOU 2084  CD  ARG A 256     7608   7500   8079     97   -722    590       C  
ATOM   2085  NE  ARG A 256       1.405  32.076  97.844  1.00 65.17           N  
ANISOU 2085  NE  ARG A 256     8049   8082   8631    150   -752    509       N  
ATOM   2086  CZ  ARG A 256       2.483  32.580  98.413  1.00 68.16           C  
ANISOU 2086  CZ  ARG A 256     8278   8615   9002    116   -763    440       C  
ATOM   2087  NH1 ARG A 256       3.501  32.965  97.650  1.00 69.81           N  
ANISOU 2087  NH1 ARG A 256     8398   8918   9208      2   -712    440       N  
ATOM   2088  NH2 ARG A 256       2.537  32.680  99.740  1.00 69.22           N  
ANISOU 2088  NH2 ARG A 256     8344   8835   9119    185   -812    348       N  
ATOM   2089  N   ALA A 257      -1.698  33.756  92.795  1.00 60.40           N  
ANISOU 2089  N   ALA A 257     7884   7152   7915     99   -955    813       N  
ATOM   2090  CA  ALA A 257      -1.889  35.139  92.468  1.00 62.05           C  
ANISOU 2090  CA  ALA A 257     8219   7223   8135    142   -983    925       C  
ATOM   2091  C   ALA A 257      -3.398  35.410  92.453  1.00 63.18           C  
ANISOU 2091  C   ALA A 257     8340   7382   8283    314  -1146    893       C  
ATOM   2092  O   ALA A 257      -3.863  36.384  93.054  1.00 64.35           O  
ANISOU 2092  O   ALA A 257     8515   7401   8536    386  -1172    908       O  
ATOM   2093  CB  ALA A 257      -1.266  35.463  91.168  1.00 63.65           C  
ANISOU 2093  CB  ALA A 257     8598   7401   8187    126   -910   1067       C  
ATOM   2094  N   ASP A 258      -4.174  34.519  91.840  1.00 63.45           N  
ANISOU 2094  N   ASP A 258     8299   7596   8213    372  -1242    810       N  
ATOM   2095  CA  ASP A 258      -5.590  34.794  91.602  1.00 63.94           C  
ANISOU 2095  CA  ASP A 258     8283   7767   8246    551  -1418    746       C  
ATOM   2096  C   ASP A 258      -6.245  34.864  92.911  1.00 62.61           C  
ANISOU 2096  C   ASP A 258     7962   7555   8273    543  -1418    615       C  
ATOM   2097  O   ASP A 258      -7.144  35.672  93.097  1.00 64.80           O  
ANISOU 2097  O   ASP A 258     8201   7823   8597    714  -1520    610       O  
ATOM   2098  CB  ASP A 258      -6.270  33.724  90.759  1.00 65.48           C  
ANISOU 2098  CB  ASP A 258     8364   8220   8294    549  -1508    595       C  
ATOM   2099  CG  ASP A 258      -5.712  33.628  89.335  1.00 68.63           C  
ANISOU 2099  CG  ASP A 258     8932   8695   8449    579  -1518    713       C  
ATOM   2100  OD1 ASP A 258      -5.074  34.582  88.839  1.00 76.32           O  
ANISOU 2100  OD1 ASP A 258    10127   9528   9343    662  -1480    936       O  
ATOM   2101  OD2 ASP A 258      -5.931  32.594  88.675  1.00 73.82           O  
ANISOU 2101  OD2 ASP A 258     9525   9543   8982    504  -1536    568       O  
ATOM   2102  N   LEU A 259      -5.764  34.068  93.856  1.00 59.81           N  
ANISOU 2102  N   LEU A 259     7544   7163   8016    378  -1291    523       N  
ATOM   2103  CA  LEU A 259      -6.263  34.167  95.228  1.00 59.15           C  
ANISOU 2103  CA  LEU A 259     7363   7014   8099    363  -1254    412       C  
ATOM   2104  C   LEU A 259      -5.810  35.456  95.990  1.00 59.59           C  
ANISOU 2104  C   LEU A 259     7504   6880   8258    390  -1229    504       C  
ATOM   2105  O   LEU A 259      -6.646  36.175  96.599  1.00 61.50           O  
ANISOU 2105  O   LEU A 259     7704   7059   8604    487  -1268    454       O  
ATOM   2106  CB  LEU A 259      -5.913  32.889  95.993  1.00 58.25           C  
ANISOU 2106  CB  LEU A 259     7217   6910   8003    229  -1107    307       C  
ATOM   2107  CG  LEU A 259      -6.562  32.801  97.363  1.00 57.46           C  
ANISOU 2107  CG  LEU A 259     7047   6756   8030    215  -1039    181       C  
ATOM   2108  CD1 LEU A 259      -8.064  32.535  97.295  1.00 57.65           C  
ANISOU 2108  CD1 LEU A 259     6911   6883   8112    221  -1069     -7       C  
ATOM   2109  CD2 LEU A 259      -5.822  31.808  98.241  1.00 53.23           C  
ANISOU 2109  CD2 LEU A 259     6589   6173   7463    151   -869    166       C  
ATOM   2110  N   ALA A 260      -4.515  35.765  95.973  1.00 58.27           N  
ANISOU 2110  N   ALA A 260     7441   6630   8069    291  -1144    601       N  
ATOM   2111  CA  ALA A 260      -4.073  37.050  96.491  1.00 59.50           C  
ANISOU 2111  CA  ALA A 260     7692   6604   8314    262  -1090    646       C  
ATOM   2112  C   ALA A 260      -4.969  38.143  95.935  1.00 62.31           C  
ANISOU 2112  C   ALA A 260     8167   6833   8675    447  -1153    736       C  
ATOM   2113  O   ALA A 260      -5.461  38.994  96.661  1.00 63.64           O  
ANISOU 2113  O   ALA A 260     8365   6860   8955    512  -1138    702       O  
ATOM   2114  CB  ALA A 260      -2.624  37.312  96.125  1.00 59.25           C  
ANISOU 2114  CB  ALA A 260     7738   6536   8238    106   -977    715       C  
ATOM   2115  N   LYS A 261      -5.199  38.113  94.634  1.00 64.53           N  
ANISOU 2115  N   LYS A 261     8536   7174   8810    569  -1221    853       N  
ATOM   2116  CA  LYS A 261      -6.076  39.088  94.000  1.00 67.51           C  
ANISOU 2116  CA  LYS A 261     9049   7472   9129    842  -1303    967       C  
ATOM   2117  C   LYS A 261      -7.517  39.012  94.553  1.00 68.37           C  
ANISOU 2117  C   LYS A 261     8951   7710   9318   1031  -1443    825       C  
ATOM   2118  O   LYS A 261      -8.133  40.048  94.800  1.00 71.35           O  
ANISOU 2118  O   LYS A 261     9412   7947   9751   1240  -1453    870       O  
ATOM   2119  CB  LYS A 261      -6.025  38.924  92.478  1.00 68.78           C  
ANISOU 2119  CB  LYS A 261     9339   7740   9054    965  -1370   1111       C  
ATOM   2120  CG  LYS A 261      -7.005  39.810  91.704  1.00 74.19           C  
ANISOU 2120  CG  LYS A 261    10172   8418   9598   1348  -1495   1247       C  
ATOM   2121  CD  LYS A 261      -6.795  39.715  90.196  1.00 76.82           C  
ANISOU 2121  CD  LYS A 261    10695   8852   9641   1479  -1544   1411       C  
ATOM   2122  CE  LYS A 261      -7.544  40.834  89.471  1.00 80.89           C  
ANISOU 2122  CE  LYS A 261    11467   9295   9972   1925  -1626   1614       C  
ATOM   2123  NZ  LYS A 261      -7.462  40.668  87.981  1.00 81.81           N  
ANISOU 2123  NZ  LYS A 261    11772   9572   9741   2104  -1706   1767       N  
ATOM   2124  N   TYR A 262      -8.067  37.827  94.768  1.00 66.94           N  
ANISOU 2124  N   TYR A 262     8511   7775   9149    957  -1514    640       N  
ATOM   2125  CA  TYR A 262      -9.441  37.757  95.265  1.00 68.09           C  
ANISOU 2125  CA  TYR A 262     8423   8066   9381   1096  -1609    464       C  
ATOM   2126  C   TYR A 262      -9.570  38.261  96.702  1.00 68.36           C  
ANISOU 2126  C   TYR A 262     8440   7918   9615   1047  -1498    386       C  
ATOM   2127  O   TYR A 262     -10.620  38.780  97.107  1.00 69.22           O  
ANISOU 2127  O   TYR A 262     8437   8053   9810   1233  -1546    302       O  
ATOM   2128  CB  TYR A 262      -9.954  36.322  95.235  1.00 67.56           C  
ANISOU 2128  CB  TYR A 262     8105   8265   9300    943  -1629    239       C  
ATOM   2129  CG  TYR A 262     -11.342  36.168  95.772  1.00 65.25           C  
ANISOU 2129  CG  TYR A 262     7530   8148   9116   1015  -1678      1       C  
ATOM   2130  CD1 TYR A 262     -12.441  36.136  94.918  1.00 70.09           C  
ANISOU 2130  CD1 TYR A 262     7921   9078   9632   1210  -1868   -123       C  
ATOM   2131  CD2 TYR A 262     -11.560  36.049  97.132  1.00 64.43           C  
ANISOU 2131  CD2 TYR A 262     7359   7931   9191    894  -1531   -123       C  
ATOM   2132  CE1 TYR A 262     -13.781  36.007  95.419  1.00 70.79           C  
ANISOU 2132  CE1 TYR A 262     7670   9390   9836   1267  -1904   -400       C  
ATOM   2133  CE2 TYR A 262     -12.857  35.923  97.666  1.00 66.82           C  
ANISOU 2133  CE2 TYR A 262     7387   8392   9608    937  -1531   -366       C  
ATOM   2134  CZ  TYR A 262     -13.970  35.884  96.795  1.00 70.85           C  
ANISOU 2134  CZ  TYR A 262     7626   9242  10054   1109  -1712   -519       C  
ATOM   2135  OH  TYR A 262     -15.240  35.738  97.317  1.00 71.16           O  
ANISOU 2135  OH  TYR A 262     7332   9487  10220   1129  -1696   -806       O  
ATOM   2136  N   ILE A 263      -8.530  38.052  97.492  1.00 66.66           N  
ANISOU 2136  N   ILE A 263     8307   7563   9456    813  -1356    389       N  
ATOM   2137  CA  ILE A 263      -8.601  38.401  98.906  1.00 67.33           C  
ANISOU 2137  CA  ILE A 263     8375   7519   9688    747  -1255    286       C  
ATOM   2138  C   ILE A 263      -8.632  39.920  99.050  1.00 70.08           C  
ANISOU 2138  C   ILE A 263     8903   7619  10103    883  -1220    375       C  
ATOM   2139  O   ILE A 263      -9.547  40.496  99.662  1.00 72.60           O  
ANISOU 2139  O   ILE A 263     9175   7883  10528   1031  -1215    295       O  
ATOM   2140  CB  ILE A 263      -7.424  37.723  99.718  1.00 65.42           C  
ANISOU 2140  CB  ILE A 263     8161   7262   9432    504  -1140    251       C  
ATOM   2141  CG1 ILE A 263      -7.850  36.323 100.230  1.00 63.49           C  
ANISOU 2141  CG1 ILE A 263     7779   7171   9174    428  -1092    111       C  
ATOM   2142  CG2 ILE A 263      -7.010  38.585 100.864  1.00 63.10           C  
ANISOU 2142  CG2 ILE A 263     7947   6805   9225    441  -1052    203       C  
ATOM   2143  CD1 ILE A 263      -6.708  35.458 100.837  1.00 60.97           C  
ANISOU 2143  CD1 ILE A 263     7518   6876   8774    294   -992    117       C  
ATOM   2144  N   CYS A 264      -7.658  40.579  98.433  1.00 71.17           N  
ANISOU 2144  N   CYS A 264     9269   7590  10182    834  -1160    535       N  
ATOM   2145  CA  CYS A 264      -7.569  42.025  98.446  1.00 73.75           C  
ANISOU 2145  CA  CYS A 264     9852   7608  10560    929  -1054    630       C  
ATOM   2146  C   CYS A 264      -8.797  42.723  97.920  1.00 76.12           C  
ANISOU 2146  C   CYS A 264    10209   7870  10841   1319  -1141    714       C  
ATOM   2147  O   CYS A 264      -9.125  43.804  98.369  1.00 78.31           O  
ANISOU 2147  O   CYS A 264    10652   7895  11209   1456  -1041    729       O  
ATOM   2148  CB  CYS A 264      -6.383  42.421  97.591  1.00 75.30           C  
ANISOU 2148  CB  CYS A 264    10288   7656  10666    794   -942    787       C  
ATOM   2149  SG  CYS A 264      -4.893  41.888  98.368  1.00 74.91           S  
ANISOU 2149  SG  CYS A 264    10134   7674  10655    381   -832    646       S  
ATOM   2150  N   ASP A 265      -9.461  42.120  96.954  1.00 76.64           N  
ANISOU 2150  N   ASP A 265    10141   8204  10775   1516  -1324    754       N  
ATOM   2151  CA  ASP A 265     -10.667  42.694  96.413  1.00 80.95           C  
ANISOU 2151  CA  ASP A 265    10674   8824  11261   1949  -1457    810       C  
ATOM   2152  C   ASP A 265     -11.895  42.343  97.223  1.00 80.78           C  
ANISOU 2152  C   ASP A 265    10302   9023  11369   2050  -1544    573       C  
ATOM   2153  O   ASP A 265     -13.015  42.644  96.810  1.00 85.32           O  
ANISOU 2153  O   ASP A 265    10744   9778  11895   2426  -1691    554       O  
ATOM   2154  CB  ASP A 265     -10.869  42.278  94.956  1.00 83.01           C  
ANISOU 2154  CB  ASP A 265    10924   9340  11277   2145  -1640    925       C  
ATOM   2155  CG  ASP A 265      -9.636  42.570  94.063  1.00 86.70           C  
ANISOU 2155  CG  ASP A 265    11754   9593  11594   2032  -1519   1163       C  
ATOM   2156  OD1 ASP A 265      -8.468  42.635  94.582  1.00 88.09           O  
ANISOU 2156  OD1 ASP A 265    12058   9538  11874   1675  -1315   1164       O  
ATOM   2157  OD2 ASP A 265      -9.847  42.691  92.823  1.00 90.04           O  
ANISOU 2157  OD2 ASP A 265    12310  10125  11777   2303  -1632   1327       O  
ATOM   2158  N   ASN A 266     -11.713  41.722  98.375  1.00 77.48           N  
ANISOU 2158  N   ASN A 266     9729   8612  11099   1743  -1444    384       N  
ATOM   2159  CA  ASN A 266     -12.846  41.409  99.215  1.00 77.61           C  
ANISOU 2159  CA  ASN A 266     9444   8798  11245   1796  -1459    149       C  
ATOM   2160  C   ASN A 266     -12.567  41.660 100.689  1.00 77.02           C  
ANISOU 2160  C   ASN A 266     9431   8504  11331   1598  -1267     41       C  
ATOM   2161  O   ASN A 266     -13.240  41.096 101.564  1.00 77.32           O  
ANISOU 2161  O   ASN A 266     9244   8669  11466   1516  -1215   -170       O  
ATOM   2162  CB  ASN A 266     -13.354  39.987  98.954  1.00 76.13           C  
ANISOU 2162  CB  ASN A 266     8925   8983  11020   1652  -1546    -42       C  
ATOM   2163  CG  ASN A 266     -14.048  39.859  97.597  1.00 78.44           C  
ANISOU 2163  CG  ASN A 266     9064   9589  11151   1916  -1772    -30       C  
ATOM   2164  OD1 ASN A 266     -15.252  40.052  97.507  1.00 82.96           O  
ANISOU 2164  OD1 ASN A 266     9370  10405  11745   2178  -1887   -174       O  
ATOM   2165  ND2 ASN A 266     -13.284  39.582  96.535  1.00 74.60           N  
ANISOU 2165  ND2 ASN A 266     8736   9126  10484   1872  -1841    131       N  
ATOM   2166  N   GLN A 267     -11.591  42.527 100.951  1.00 76.23           N  
ANISOU 2166  N   GLN A 267     9640   8080  11244   1509  -1142    162       N  
ATOM   2167  CA  GLN A 267     -11.246  42.924 102.308  1.00 75.91           C  
ANISOU 2167  CA  GLN A 267     9680   7843  11318   1327   -973     42       C  
ATOM   2168  C   GLN A 267     -12.400  43.059 103.297  1.00 77.73           C  
ANISOU 2168  C   GLN A 267     9745   8111  11679   1451   -922   -148       C  
ATOM   2169  O   GLN A 267     -12.387  42.404 104.355  1.00 76.93           O  
ANISOU 2169  O   GLN A 267     9534   8083  11611   1245   -840   -313       O  
ATOM   2170  CB  GLN A 267     -10.414  44.203 102.313  1.00 76.88           C  
ANISOU 2170  CB  GLN A 267    10153   7597  11461   1290   -829    151       C  
ATOM   2171  CG  GLN A 267      -8.985  43.884 102.128  1.00 72.52           C  
ANISOU 2171  CG  GLN A 267     9693   7029  10830    969   -786    195       C  
ATOM   2172  CD  GLN A 267      -8.163  45.060 101.787  1.00 70.65           C  
ANISOU 2172  CD  GLN A 267     9789   6454  10602    893   -620    296       C  
ATOM   2173  OE1 GLN A 267      -7.748  45.830 102.661  1.00 74.70           O  
ANISOU 2173  OE1 GLN A 267    10435   6745  11201    724   -448    169       O  
ATOM   2174  NE2 GLN A 267      -7.854  45.187 100.521  1.00 68.33           N  
ANISOU 2174  NE2 GLN A 267     9645   6111  10204    978   -637    501       N  
ATOM   2175  N   ASP A 268     -13.387  43.884 102.963  1.00 80.92           N  
ANISOU 2175  N   ASP A 268    10140   8471  12135   1813   -956   -120       N  
ATOM   2176  CA  ASP A 268     -14.456  44.227 103.903  1.00 82.69           C  
ANISOU 2176  CA  ASP A 268    10221   8699  12500   1963   -874   -303       C  
ATOM   2177  C   ASP A 268     -15.252  43.037 104.451  1.00 81.85           C  
ANISOU 2177  C   ASP A 268     9740   8921  12440   1837   -881   -539       C  
ATOM   2178  O   ASP A 268     -15.766  43.075 105.576  1.00 82.95           O  
ANISOU 2178  O   ASP A 268     9801   9032  12685   1788   -734   -723       O  
ATOM   2179  CB  ASP A 268     -15.377  45.292 103.291  1.00 86.97           C  
ANISOU 2179  CB  ASP A 268    10805   9177  13064   2459   -928   -213       C  
ATOM   2180  CG  ASP A 268     -14.631  46.602 103.015  1.00 90.39           C  
ANISOU 2180  CG  ASP A 268    11716   9156  13473   2562   -798      3       C  
ATOM   2181  OD1 ASP A 268     -15.279  47.609 102.611  1.00 92.64           O  
ANISOU 2181  OD1 ASP A 268    12153   9287  13760   3009   -782    115       O  
ATOM   2182  OD2 ASP A 268     -13.378  46.607 103.221  1.00 88.88           O  
ANISOU 2182  OD2 ASP A 268    11750   8764  13256   2192   -689     44       O  
ATOM   2183  N   THR A 269     -15.336  41.967 103.676  1.00 80.29           N  
ANISOU 2183  N   THR A 269     9339   9011  12157   1756  -1009   -551       N  
ATOM   2184  CA  THR A 269     -16.051  40.793 104.122  1.00 78.81           C  
ANISOU 2184  CA  THR A 269     8840   9090  12015   1581   -951   -792       C  
ATOM   2185  C   THR A 269     -15.129  39.722 104.689  1.00 75.35           C  
ANISOU 2185  C   THR A 269     8517   8605  11508   1201   -829   -800       C  
ATOM   2186  O   THR A 269     -15.612  38.685 105.164  1.00 75.98           O  
ANISOU 2186  O   THR A 269     8434   8825  11610   1019   -703   -984       O  
ATOM   2187  CB  THR A 269     -16.823  40.177 102.974  1.00 80.57           C  
ANISOU 2187  CB  THR A 269     8748   9680  12185   1696  -1130   -870       C  
ATOM   2188  OG1 THR A 269     -15.920  39.966 101.891  1.00 77.73           O  
ANISOU 2188  OG1 THR A 269     8554   9314  11664   1662  -1269   -660       O  
ATOM   2189  CG2 THR A 269     -17.995  41.099 102.546  1.00 83.03           C  
ANISOU 2189  CG2 THR A 269     8849  10154  12545   2148  -1264   -922       C  
ATOM   2190  N   ILE A 270     -13.820  39.969 104.646  1.00 71.84           N  
ANISOU 2190  N   ILE A 270     8356   7969  10973   1095   -840   -615       N  
ATOM   2191  CA  ILE A 270     -12.830  38.991 105.063  1.00 67.23           C  
ANISOU 2191  CA  ILE A 270     7879   7381  10283    822   -763   -594       C  
ATOM   2192  C   ILE A 270     -12.069  39.433 106.336  1.00 66.45           C  
ANISOU 2192  C   ILE A 270     7984   7100  10165    711   -640   -611       C  
ATOM   2193  O   ILE A 270     -12.019  38.691 107.342  1.00 64.53           O  
ANISOU 2193  O   ILE A 270     7762   6888   9868    583   -504   -710       O  
ATOM   2194  CB  ILE A 270     -11.800  38.750 103.922  1.00 66.62           C  
ANISOU 2194  CB  ILE A 270     7903   7328  10084    777   -891   -403       C  
ATOM   2195  CG1 ILE A 270     -12.434  38.149 102.669  1.00 65.69           C  
ANISOU 2195  CG1 ILE A 270     7600   7431   9928    854  -1018   -409       C  
ATOM   2196  CG2 ILE A 270     -10.679  37.827 104.352  1.00 62.33           C  
ANISOU 2196  CG2 ILE A 270     7470   6791   9422    562   -818   -370       C  
ATOM   2197  CD1 ILE A 270     -11.365  37.747 101.657  1.00 60.26           C  
ANISOU 2197  CD1 ILE A 270     7034   6763   9101    777  -1099   -238       C  
ATOM   2198  N   SER A 271     -11.445  40.614 106.291  1.00 66.59           N  
ANISOU 2198  N   SER A 271     8172   6929  10200    753   -669   -528       N  
ATOM   2199  CA  SER A 271     -10.664  41.102 107.444  1.00 66.49           C  
ANISOU 2199  CA  SER A 271     8323   6787  10151    615   -569   -599       C  
ATOM   2200  C   SER A 271     -10.181  42.548 107.292  1.00 67.53           C  
ANISOU 2200  C   SER A 271     8645   6669  10345    633   -546   -560       C  
ATOM   2201  O   SER A 271      -9.999  43.060 106.167  1.00 67.85           O  
ANISOU 2201  O   SER A 271     8762   6614  10403    719   -607   -407       O  
ATOM   2202  CB  SER A 271      -9.480  40.158 107.748  1.00 64.84           C  
ANISOU 2202  CB  SER A 271     8153   6714   9769    430   -583   -575       C  
ATOM   2203  OG  SER A 271      -8.374  40.838 108.367  1.00 67.42           O  
ANISOU 2203  OG  SER A 271     8605   6980  10031    298   -566   -626       O  
ATOM   2204  N   SER A 272      -9.948  43.201 108.425  1.00 67.20           N  
ANISOU 2204  N   SER A 272     8714   6504  10316    539   -429   -708       N  
ATOM   2205  CA  SER A 272      -9.582  44.618 108.380  1.00 68.60           C  
ANISOU 2205  CA  SER A 272     9108   6386  10572    517   -335   -722       C  
ATOM   2206  C   SER A 272      -8.090  44.948 108.424  1.00 68.38           C  
ANISOU 2206  C   SER A 272     9194   6326  10463    231   -310   -760       C  
ATOM   2207  O   SER A 272      -7.753  46.104 108.611  1.00 69.73           O  
ANISOU 2207  O   SER A 272     9559   6234  10702    132   -168   -843       O  
ATOM   2208  CB  SER A 272     -10.277  45.362 109.505  1.00 69.65           C  
ANISOU 2208  CB  SER A 272     9311   6360  10791    573   -183   -906       C  
ATOM   2209  OG  SER A 272      -9.893  44.795 110.718  1.00 68.00           O  
ANISOU 2209  OG  SER A 272     9056   6319  10462    394   -156  -1077       O  
ATOM   2210  N   LYS A 273      -7.225  43.949 108.218  1.00 66.66           N  
ANISOU 2210  N   LYS A 273     8852   6370  10107    101   -422   -719       N  
ATOM   2211  CA  LYS A 273      -5.769  44.059 108.448  1.00 66.80           C  
ANISOU 2211  CA  LYS A 273     8871   6486  10022   -172   -420   -820       C  
ATOM   2212  C   LYS A 273      -4.924  43.973 107.192  1.00 66.19           C  
ANISOU 2212  C   LYS A 273     8796   6423   9929   -255   -457   -667       C  
ATOM   2213  O   LYS A 273      -3.702  44.011 107.235  1.00 66.35           O  
ANISOU 2213  O   LYS A 273     8764   6568   9878   -484   -450   -762       O  
ATOM   2214  CB  LYS A 273      -5.318  42.997 109.442  1.00 65.15           C  
ANISOU 2214  CB  LYS A 273     8515   6614   9623   -213   -505   -929       C  
ATOM   2215  CG  LYS A 273      -6.301  42.796 110.566  1.00 64.92           C  
ANISOU 2215  CG  LYS A 273     8501   6589   9577    -94   -452  -1032       C  
ATOM   2216  CD  LYS A 273      -6.313  43.955 111.547  1.00 64.32           C  
ANISOU 2216  CD  LYS A 273     8543   6357   9541   -205   -329  -1265       C  
ATOM   2217  CE  LYS A 273      -6.733  43.479 112.938  1.00 65.64           C  
ANISOU 2217  CE  LYS A 273     8707   6669   9564   -148   -295  -1412       C  
ATOM   2218  NZ  LYS A 273      -6.449  44.491 114.004  1.00 73.55           N  
ANISOU 2218  NZ  LYS A 273     9811   7605  10531   -302   -198  -1690       N  
ATOM   2219  N   LEU A 274      -5.612  43.983 106.077  1.00 66.77           N  
ANISOU 2219  N   LEU A 274     8929   6372  10068    -63   -483   -454       N  
ATOM   2220  CA  LEU A 274      -5.108  43.492 104.814  1.00 67.79           C  
ANISOU 2220  CA  LEU A 274     9037   6582  10139    -63   -552   -269       C  
ATOM   2221  C   LEU A 274      -4.747  44.652 103.945  1.00 70.97           C  
ANISOU 2221  C   LEU A 274     9683   6676  10605   -118   -410   -175       C  
ATOM   2222  O   LEU A 274      -4.011  44.505 102.977  1.00 71.47           O  
ANISOU 2222  O   LEU A 274     9779   6765  10612   -203   -400    -58       O  
ATOM   2223  CB  LEU A 274      -6.226  42.659 104.134  1.00 66.13           C  
ANISOU 2223  CB  LEU A 274     8732   6479   9917    204   -681   -119       C  
ATOM   2224  CG  LEU A 274      -6.540  41.446 105.001  1.00 65.36           C  
ANISOU 2224  CG  LEU A 274     8447   6631   9756    212   -742   -220       C  
ATOM   2225  CD1 LEU A 274      -7.605  40.647 104.386  1.00 68.65           C  
ANISOU 2225  CD1 LEU A 274     8749   7154  10179    389   -820   -149       C  
ATOM   2226  CD2 LEU A 274      -5.272  40.621 105.107  1.00 64.68           C  
ANISOU 2226  CD2 LEU A 274     8288   6758   9529     52   -776   -233       C  
ATOM   2227  N   LYS A 275      -5.330  45.795 104.289  1.00 74.53           N  
ANISOU 2227  N   LYS A 275    10339   6811  11167    -47   -267   -217       N  
ATOM   2228  CA  LYS A 275      -5.139  47.037 103.584  1.00 78.61           C  
ANISOU 2228  CA  LYS A 275    11192   6931  11746    -58    -56   -120       C  
ATOM   2229  C   LYS A 275      -3.676  47.339 103.340  1.00 79.38           C  
ANISOU 2229  C   LYS A 275    11349   6989  11822   -451    102   -207       C  
ATOM   2230  O   LYS A 275      -3.328  47.771 102.267  1.00 80.37           O  
ANISOU 2230  O   LYS A 275    11697   6910  11931   -464    232    -37       O  
ATOM   2231  CB  LYS A 275      -5.802  48.195 104.336  1.00 82.01           C  
ANISOU 2231  CB  LYS A 275    11842   7016  12302     24    126   -227       C  
ATOM   2232  CG  LYS A 275      -7.340  48.042 104.570  1.00 84.93           C  
ANISOU 2232  CG  LYS A 275    12133   7423  12715    442      3   -166       C  
ATOM   2233  CD  LYS A 275      -8.210  48.798 103.534  1.00 88.22           C  
ANISOU 2233  CD  LYS A 275    12808   7567  13144    862     48     89       C  
ATOM   2234  CE  LYS A 275      -9.478  49.323 104.173  1.00 90.06           C  
ANISOU 2234  CE  LYS A 275    13054   7685  13478   1193     78     28       C  
ATOM   2235  NZ  LYS A 275      -9.141  50.436 105.122  1.00 94.86           N  
ANISOU 2235  NZ  LYS A 275    13934   7910  14199    995    373   -161       N  
ATOM   2236  N   GLU A 276      -2.807  47.119 104.310  1.00 79.84           N  
ANISOU 2236  N   GLU A 276    11204   7267  11864   -765    100   -483       N  
ATOM   2237  CA  GLU A 276      -1.382  47.258 103.987  1.00 82.43           C  
ANISOU 2237  CA  GLU A 276    11485   7667  12165  -1141    224   -602       C  
ATOM   2238  C   GLU A 276      -0.883  46.167 103.039  1.00 80.29           C  
ANISOU 2238  C   GLU A 276    11034   7691  11781  -1089     70   -426       C  
ATOM   2239  O   GLU A 276      -0.162  46.477 102.108  1.00 82.12           O  
ANISOU 2239  O   GLU A 276    11380   7810  12010  -1250    225   -354       O  
ATOM   2240  CB  GLU A 276      -0.490  47.369 105.223  1.00 83.74           C  
ANISOU 2240  CB  GLU A 276    11435   8067  12314  -1484    247   -990       C  
ATOM   2241  CG  GLU A 276       1.033  47.218 104.927  1.00 87.55           C  
ANISOU 2241  CG  GLU A 276    11710   8807  12746  -1853    307  -1164       C  
ATOM   2242  CD  GLU A 276       1.631  48.345 104.083  1.00 93.61           C  
ANISOU 2242  CD  GLU A 276    12761   9178  13627  -2162    672  -1183       C  
ATOM   2243  OE1 GLU A 276       1.338  49.534 104.390  1.00 97.16           O  
ANISOU 2243  OE1 GLU A 276    13521   9199  14198  -2293    942  -1294       O  
ATOM   2244  OE2 GLU A 276       2.399  48.036 103.121  1.00 93.60           O  
ANISOU 2244  OE2 GLU A 276    12702   9272  13592  -2276    726  -1091       O  
ATOM   2245  N   CYS A 277      -1.276  44.915 103.264  1.00 77.32           N  
ANISOU 2245  N   CYS A 277    10415   7652  11310   -876   -191   -363       N  
ATOM   2246  CA  CYS A 277      -0.905  43.807 102.358  1.00 76.54           C  
ANISOU 2246  CA  CYS A 277    10175   7804  11101   -799   -321   -198       C  
ATOM   2247  C   CYS A 277      -1.339  43.811 100.950  1.00 75.97           C  
ANISOU 2247  C   CYS A 277    10289   7570  11007   -625   -308     82       C  
ATOM   2248  O   CYS A 277      -0.764  43.121 100.105  1.00 74.35           O  
ANISOU 2248  O   CYS A 277    10011   7529  10712   -647   -345    182       O  
ATOM   2249  CB  CYS A 277      -1.701  42.637 102.971  1.00 73.56           C  
ANISOU 2249  CB  CYS A 277     9620   7674  10657   -556   -536   -178       C  
ATOM   2250  SG  CYS A 277      -0.802  41.552 104.080  1.00 75.78           S  
ANISOU 2250  SG  CYS A 277     9605   8393  10794   -628   -656   -369       S  
ATOM   2251  N   CYS A 278      -2.355  44.633 100.713  1.00 77.56           N  
ANISOU 2251  N   CYS A 278    10739   7458  11271   -424   -251    200       N  
ATOM   2252  CA  CYS A 278      -3.138  44.537  99.508  1.00 78.28           C  
ANISOU 2252  CA  CYS A 278    10978   7471  11292   -124   -321    466       C  
ATOM   2253  C   CYS A 278      -2.640  45.605  98.613  1.00 80.86           C  
ANISOU 2253  C   CYS A 278    11662   7452  11610   -198    -73    600       C  
ATOM   2254  O   CYS A 278      -3.330  46.054  97.731  1.00 83.02           O  
ANISOU 2254  O   CYS A 278    12193   7532  11819     91    -58    826       O  
ATOM   2255  CB  CYS A 278      -4.646  44.526  99.667  1.00 77.96           C  
ANISOU 2255  CB  CYS A 278    10928   7418  11277    239   -464    527       C  
ATOM   2256  SG  CYS A 278      -5.068  42.838 100.134  1.00 77.54           S  
ANISOU 2256  SG  CYS A 278    10479   7809  11172    282   -711    430       S  
ATOM   2257  N   ASP A 279      -1.386  45.957  98.801  1.00 82.04           N  
ANISOU 2257  N   ASP A 279    11817   7552  11801   -586    133    449       N  
ATOM   2258  CA  ASP A 279      -0.857  47.131  98.191  1.00 85.55           C  
ANISOU 2258  CA  ASP A 279    12643   7588  12274   -751    474    510       C  
ATOM   2259  C   ASP A 279       0.589  46.930  97.720  1.00 86.23           C  
ANISOU 2259  C   ASP A 279    12636   7796  12333  -1143    639    416       C  
ATOM   2260  O   ASP A 279       1.205  47.879  97.179  1.00 89.00           O  
ANISOU 2260  O   ASP A 279    13306   7799  12712  -1375    998    432       O  
ATOM   2261  CB  ASP A 279      -0.948  48.238  99.219  1.00 88.21           C  
ANISOU 2261  CB  ASP A 279    13133   7618  12765   -907    683    305       C  
ATOM   2262  CG  ASP A 279      -0.608  49.594  98.650  1.00 94.36           C  
ANISOU 2262  CG  ASP A 279    14417   7848  13589  -1052   1113    374       C  
ATOM   2263  OD1 ASP A 279      -1.486  50.495  98.686  1.00 98.09           O  
ANISOU 2263  OD1 ASP A 279    15254   7916  14098   -785   1241    497       O  
ATOM   2264  OD2 ASP A 279       0.540  49.764  98.184  1.00 95.54           O  
ANISOU 2264  OD2 ASP A 279    14608   7957  13736  -1428   1356    296       O  
ATOM   2265  N   LYS A 280       1.137  45.719  97.905  1.00 82.45           N  
ANISOU 2265  N   LYS A 280    11745   7787  11797  -1211    421    316       N  
ATOM   2266  CA  LYS A 280       2.526  45.471  97.479  1.00 83.35           C  
ANISOU 2266  CA  LYS A 280    11704   8080  11886  -1549    567    201       C  
ATOM   2267  C   LYS A 280       2.599  44.960  96.037  1.00 82.58           C  
ANISOU 2267  C   LYS A 280    11737   7996  11644  -1404    571    479       C  
ATOM   2268  O   LYS A 280       1.561  44.742  95.421  1.00 81.13           O  
ANISOU 2268  O   LYS A 280    11730   7734  11363  -1037    421    737       O  
ATOM   2269  CB  LYS A 280       3.240  44.501  98.421  1.00 81.51           C  
ANISOU 2269  CB  LYS A 280    10975   8352  11641  -1668    365    -61       C  
ATOM   2270  CG  LYS A 280       3.017  44.754  99.883  1.00 81.54           C  
ANISOU 2270  CG  LYS A 280    10830   8435  11718  -1720    279   -315       C  
ATOM   2271  CD  LYS A 280       4.347  44.967 100.560  1.00 83.25           C  
ANISOU 2271  CD  LYS A 280    10749   8919  11964  -2121    383   -690       C  
ATOM   2272  CE  LYS A 280       4.138  45.238 102.039  1.00 85.41           C  
ANISOU 2272  CE  LYS A 280    10885   9302  12265  -2169    287   -966       C  
ATOM   2273  NZ  LYS A 280       3.487  44.091 102.734  1.00 77.22           N  
ANISOU 2273  NZ  LYS A 280     9666   8564  11111  -1805    -49   -884       N  
ATOM   2274  N   PRO A 281       3.822  44.756  95.495  1.00 83.48           N  
ANISOU 2274  N   PRO A 281    11739   8249  11731  -1689    741    399       N  
ATOM   2275  CA  PRO A 281       3.903  44.010  94.228  1.00 82.61           C  
ANISOU 2275  CA  PRO A 281    11688   8242  11458  -1531    699    634       C  
ATOM   2276  C   PRO A 281       3.554  42.547  94.481  1.00 78.91           C  
ANISOU 2276  C   PRO A 281    10879   8191  10911  -1279    333    642       C  
ATOM   2277  O   PRO A 281       3.469  42.115  95.645  1.00 77.56           O  
ANISOU 2277  O   PRO A 281    10423   8241  10805  -1263    154    461       O  
ATOM   2278  CB  PRO A 281       5.375  44.174  93.799  1.00 85.43           C  
ANISOU 2278  CB  PRO A 281    11950   8671  11839  -1940   1005    477       C  
ATOM   2279  CG  PRO A 281       6.042  45.039  94.856  1.00 87.37           C  
ANISOU 2279  CG  PRO A 281    12062   8871  12266  -2336   1201    128       C  
ATOM   2280  CD  PRO A 281       5.153  45.001  96.069  1.00 85.16           C  
ANISOU 2280  CD  PRO A 281    11677   8635  12044  -2141    930     52       C  
ATOM   2281  N   LEU A 282       3.331  41.781  93.423  1.00 78.15           N  
ANISOU 2281  N   LEU A 282    10846   8189  10661  -1083    245    842       N  
ATOM   2282  CA  LEU A 282       2.670  40.459  93.573  1.00 74.49           C  
ANISOU 2282  CA  LEU A 282    10170   8013  10120   -816    -65    872       C  
ATOM   2283  C   LEU A 282       3.306  39.509  94.608  1.00 72.21           C  
ANISOU 2283  C   LEU A 282     9487   8072   9876   -880   -179    657       C  
ATOM   2284  O   LEU A 282       2.637  39.031  95.524  1.00 69.87           O  
ANISOU 2284  O   LEU A 282     9067   7872   9608   -732   -363    597       O  
ATOM   2285  CB  LEU A 282       2.520  39.781  92.205  1.00 75.05           C  
ANISOU 2285  CB  LEU A 282    10364   8146  10004   -664    -96   1065       C  
ATOM   2286  CG  LEU A 282       1.480  38.651  91.998  1.00 74.77           C  
ANISOU 2286  CG  LEU A 282    10248   8295   9865   -383   -365   1122       C  
ATOM   2287  CD1 LEU A 282       0.575  38.961  90.804  1.00 79.36           C  
ANISOU 2287  CD1 LEU A 282    11117   8761  10275   -155   -420   1331       C  
ATOM   2288  CD2 LEU A 282       2.109  37.277  91.817  1.00 75.55           C  
ANISOU 2288  CD2 LEU A 282    10133   8679   9896   -405   -399   1054       C  
ATOM   2289  N   LEU A 283       4.596  39.225  94.478  1.00 72.63           N  
ANISOU 2289  N   LEU A 283     9348   8330   9919  -1072    -58    540       N  
ATOM   2290  CA  LEU A 283       5.183  38.309  95.425  1.00 71.20           C  
ANISOU 2290  CA  LEU A 283     8814   8509   9731  -1035   -184    362       C  
ATOM   2291  C   LEU A 283       4.951  38.727  96.886  1.00 71.23           C  
ANISOU 2291  C   LEU A 283     8693   8549   9821  -1061   -279    180       C  
ATOM   2292  O   LEU A 283       4.594  37.882  97.720  1.00 70.07           O  
ANISOU 2292  O   LEU A 283     8419   8580   9625   -857   -460    149       O  
ATOM   2293  CB  LEU A 283       6.661  38.059  95.125  1.00 72.84           C  
ANISOU 2293  CB  LEU A 283     8776   8985   9916  -1214    -41    224       C  
ATOM   2294  CG  LEU A 283       6.860  37.228  93.845  1.00 72.94           C  
ANISOU 2294  CG  LEU A 283     8868   9039   9807  -1110     13    392       C  
ATOM   2295  CD1 LEU A 283       8.325  37.187  93.396  1.00 70.80           C  
ANISOU 2295  CD1 LEU A 283     8372   8996   9531  -1317    217    252       C  
ATOM   2296  CD2 LEU A 283       6.243  35.796  93.949  1.00 68.87           C  
ANISOU 2296  CD2 LEU A 283     8323   8659   9183   -781   -192    487       C  
ATOM   2297  N   GLU A 284       5.118  40.018  97.182  1.00 72.92           N  
ANISOU 2297  N   GLU A 284     8990   8565  10150  -1310   -127     61       N  
ATOM   2298  CA  GLU A 284       5.182  40.476  98.552  1.00 73.73           C  
ANISOU 2298  CA  GLU A 284     8943   8753  10320  -1404   -179   -180       C  
ATOM   2299  C   GLU A 284       3.825  40.496  99.206  1.00 72.07           C  
ANISOU 2299  C   GLU A 284     8885   8368  10131  -1176   -329    -92       C  
ATOM   2300  O   GLU A 284       3.733  40.348 100.430  1.00 73.03           O  
ANISOU 2300  O   GLU A 284     8855   8650  10242  -1134   -445   -254       O  
ATOM   2301  CB  GLU A 284       5.829  41.846  98.668  1.00 77.51           C  
ANISOU 2301  CB  GLU A 284     9470   9059  10924  -1797     81   -389       C  
ATOM   2302  CG  GLU A 284       7.241  41.964  98.054  1.00 82.14           C  
ANISOU 2302  CG  GLU A 284     9867   9826  11517  -2110    296   -546       C  
ATOM   2303  CD  GLU A 284       7.778  43.390  98.112  1.00 90.85           C  
ANISOU 2303  CD  GLU A 284    11079  10676  12763  -2566    635   -776       C  
ATOM   2304  OE1 GLU A 284       7.458  44.133  99.075  1.00 93.59           O  
ANISOU 2304  OE1 GLU A 284    11466  10903  13191  -2679    646   -957       O  
ATOM   2305  OE2 GLU A 284       8.525  43.779  97.184  1.00 96.78           O  
ANISOU 2305  OE2 GLU A 284    11901  11324  13546  -2833    931   -789       O  
ATOM   2306  N   LYS A 285       2.781  40.668  98.403  1.00 70.59           N  
ANISOU 2306  N   LYS A 285     8979   7890   9953  -1014   -328    147       N  
ATOM   2307  CA  LYS A 285       1.402  40.747  98.862  1.00 68.15           C  
ANISOU 2307  CA  LYS A 285     8792   7424   9677   -790   -450    223       C  
ATOM   2308  C   LYS A 285       0.972  39.382  99.393  1.00 65.91           C  
ANISOU 2308  C   LYS A 285     8331   7402   9312   -576   -646    224       C  
ATOM   2309  O   LYS A 285       0.444  39.228 100.517  1.00 64.57           O  
ANISOU 2309  O   LYS A 285     8096   7278   9158   -497   -727    125       O  
ATOM   2310  CB  LYS A 285       0.540  41.197  97.682  1.00 68.31           C  
ANISOU 2310  CB  LYS A 285     9107   7165   9685   -635   -414    465       C  
ATOM   2311  CG  LYS A 285      -0.989  41.080  97.827  1.00 67.59           C  
ANISOU 2311  CG  LYS A 285     9081   6996   9603   -339   -571    556       C  
ATOM   2312  CD  LYS A 285      -1.761  41.956  96.764  1.00 68.04           C  
ANISOU 2312  CD  LYS A 285     9451   6771   9631   -151   -521    768       C  
ATOM   2313  CE  LYS A 285      -1.727  41.348  95.367  1.00 69.79           C  
ANISOU 2313  CE  LYS A 285     9736   7094   9687    -42   -572    949       C  
ATOM   2314  NZ  LYS A 285      -2.106  42.251  94.203  1.00 71.33           N  
ANISOU 2314  NZ  LYS A 285    10287   7038   9777    139   -488   1178       N  
ATOM   2315  N   SER A 286       1.198  38.379  98.563  1.00 65.05           N  
ANISOU 2315  N   SER A 286     8180   7434   9101   -490   -683    336       N  
ATOM   2316  CA  SER A 286       0.976  36.990  98.943  1.00 63.69           C  
ANISOU 2316  CA  SER A 286     7891   7469   8838   -316   -792    337       C  
ATOM   2317  C   SER A 286       1.721  36.564 100.215  1.00 63.49           C  
ANISOU 2317  C   SER A 286     7677   7689   8757   -308   -827    175       C  
ATOM   2318  O   SER A 286       1.145  35.958 101.099  1.00 62.08           O  
ANISOU 2318  O   SER A 286     7496   7556   8538   -161   -887    148       O  
ATOM   2319  CB  SER A 286       1.359  36.121  97.761  1.00 63.31           C  
ANISOU 2319  CB  SER A 286     7855   7510   8692   -272   -769    454       C  
ATOM   2320  OG  SER A 286       0.591  36.587  96.648  1.00 66.80           O  
ANISOU 2320  OG  SER A 286     8482   7760   9139   -245   -766    594       O  
ATOM   2321  N   HIS A 287       3.002  36.899 100.307  1.00 65.48           N  
ANISOU 2321  N   HIS A 287     7768   8120   8991   -460   -778     51       N  
ATOM   2322  CA  HIS A 287       3.734  36.664 101.526  1.00 66.31           C  
ANISOU 2322  CA  HIS A 287     7662   8525   9009   -426   -845   -136       C  
ATOM   2323  C   HIS A 287       3.153  37.442 102.716  1.00 67.17           C  
ANISOU 2323  C   HIS A 287     7806   8546   9168   -475   -880   -275       C  
ATOM   2324  O   HIS A 287       3.018  36.892 103.795  1.00 66.47           O  
ANISOU 2324  O   HIS A 287     7671   8619   8964   -307   -969   -336       O  
ATOM   2325  CB  HIS A 287       5.207  37.005 101.345  1.00 68.89           C  
ANISOU 2325  CB  HIS A 287     7740   9117   9317   -616   -787   -307       C  
ATOM   2326  CG  HIS A 287       6.003  36.768 102.580  1.00 70.35           C  
ANISOU 2326  CG  HIS A 287     7653   9707   9370   -542   -899   -533       C  
ATOM   2327  ND1 HIS A 287       6.515  35.523 102.908  1.00 72.96           N  
ANISOU 2327  ND1 HIS A 287     7852  10365   9505   -226   -999   -498       N  
ATOM   2328  CD2 HIS A 287       6.325  37.592 103.599  1.00 68.07           C  
ANISOU 2328  CD2 HIS A 287     7221   9559   9085   -704   -932   -800       C  
ATOM   2329  CE1 HIS A 287       7.159  35.606 104.060  1.00 72.30           C  
ANISOU 2329  CE1 HIS A 287     7535  10649   9285   -163  -1115   -724       C  
ATOM   2330  NE2 HIS A 287       7.061  36.852 104.496  1.00 73.65           N  
ANISOU 2330  NE2 HIS A 287     7677  10731   9575   -475  -1084   -931       N  
ATOM   2331  N   CYS A 288       2.841  38.725 102.504  1.00 68.67           N  
ANISOU 2331  N   CYS A 288     8116   8463   9512   -691   -782   -319       N  
ATOM   2332  CA  CYS A 288       2.135  39.550 103.472  1.00 70.36           C  
ANISOU 2332  CA  CYS A 288     8420   8513   9800   -735   -777   -434       C  
ATOM   2333  C   CYS A 288       0.841  38.887 103.945  1.00 68.47           C  
ANISOU 2333  C   CYS A 288     8292   8186   9537   -476   -859   -318       C  
ATOM   2334  O   CYS A 288       0.626  38.761 105.142  1.00 68.42           O  
ANISOU 2334  O   CYS A 288     8253   8279   9465   -407   -907   -438       O  
ATOM   2335  CB  CYS A 288       1.812  40.906 102.864  1.00 71.72           C  
ANISOU 2335  CB  CYS A 288     8803   8305  10143   -927   -613   -415       C  
ATOM   2336  SG  CYS A 288       1.120  42.139 103.999  1.00 78.94           S  
ANISOU 2336  SG  CYS A 288     9853   8971  11170  -1019   -539   -597       S  
ATOM   2337  N   ILE A 289      -0.010  38.451 103.007  1.00 67.84           N  
ANISOU 2337  N   ILE A 289     8334   7946   9497   -346   -862   -113       N  
ATOM   2338  CA  ILE A 289      -1.308  37.880 103.369  1.00 66.61           C  
ANISOU 2338  CA  ILE A 289     8249   7711   9349   -160   -900    -54       C  
ATOM   2339  C   ILE A 289      -1.116  36.590 104.175  1.00 66.88           C  
ANISOU 2339  C   ILE A 289     8221   7967   9223    -17   -932    -76       C  
ATOM   2340  O   ILE A 289      -1.908  36.309 105.093  1.00 66.71           O  
ANISOU 2340  O   ILE A 289     8252   7912   9183     77   -915   -121       O  
ATOM   2341  CB  ILE A 289      -2.204  37.617 102.150  1.00 65.72           C  
ANISOU 2341  CB  ILE A 289     8220   7466   9286    -67   -912    113       C  
ATOM   2342  CG1 ILE A 289      -2.325  38.867 101.279  1.00 65.10           C  
ANISOU 2342  CG1 ILE A 289     8267   7163   9304   -128   -870    185       C  
ATOM   2343  CG2 ILE A 289      -3.602  37.217 102.581  1.00 65.37           C  
ANISOU 2343  CG2 ILE A 289     8190   7363   9283     68   -927     96       C  
ATOM   2344  CD1 ILE A 289      -2.648  38.524  99.862  1.00 66.99           C  
ANISOU 2344  CD1 ILE A 289     8569   7384   9500    -39   -904    354       C  
ATOM   2345  N   ALA A 290      -0.061  35.823 103.865  1.00 66.69           N  
ANISOU 2345  N   ALA A 290     8110   8156   9071     20   -949    -43       N  
ATOM   2346  CA  ALA A 290       0.191  34.575 104.624  1.00 66.39           C  
ANISOU 2346  CA  ALA A 290     8075   8305   8844    228   -952    -32       C  
ATOM   2347  C   ALA A 290       0.781  34.837 106.020  1.00 67.59           C  
ANISOU 2347  C   ALA A 290     8149   8675   8859    278  -1010   -192       C  
ATOM   2348  O   ALA A 290       0.549  34.057 106.910  1.00 67.58           O  
ANISOU 2348  O   ALA A 290     8242   8738   8698    480   -991   -175       O  
ATOM   2349  CB  ALA A 290       1.050  33.578 103.816  1.00 66.11           C  
ANISOU 2349  CB  ALA A 290     7998   8419   8701    326   -938     70       C  
ATOM   2350  N   GLU A 291       1.521  35.949 106.175  1.00 69.18           N  
ANISOU 2350  N   GLU A 291     8198   8980   9109     81  -1057   -362       N  
ATOM   2351  CA  GLU A 291       2.109  36.458 107.460  1.00 71.13           C  
ANISOU 2351  CA  GLU A 291     8322   9475   9228     57  -1131   -596       C  
ATOM   2352  C   GLU A 291       1.205  37.351 108.387  1.00 70.99           C  
ANISOU 2352  C   GLU A 291     8421   9264   9287    -37  -1097   -721       C  
ATOM   2353  O   GLU A 291       1.601  37.707 109.494  1.00 72.65           O  
ANISOU 2353  O   GLU A 291     8555   9684   9363    -50  -1155   -929       O  
ATOM   2354  CB  GLU A 291       3.317  37.326 107.126  1.00 73.50           C  
ANISOU 2354  CB  GLU A 291     8381   9967   9577   -203  -1149   -793       C  
ATOM   2355  CG  GLU A 291       4.746  36.767 107.263  1.00 76.57           C  
ANISOU 2355  CG  GLU A 291     8479  10848   9766   -106  -1251   -911       C  
ATOM   2356  CD  GLU A 291       5.750  37.954 107.378  1.00 86.87           C  
ANISOU 2356  CD  GLU A 291     9511  12358  11139   -469  -1239  -1249       C  
ATOM   2357  OE1 GLU A 291       7.013  37.784 107.221  1.00 89.29           O  
ANISOU 2357  OE1 GLU A 291     9493  13082  11352   -501  -1292  -1412       O  
ATOM   2358  OE2 GLU A 291       5.246  39.098 107.635  1.00 88.83           O  
ANISOU 2358  OE2 GLU A 291     9871  12337  11545   -740  -1148  -1379       O  
ATOM   2359  N   VAL A 292      -0.003  37.687 107.936  1.00 69.51           N  
ANISOU 2359  N   VAL A 292     8403   8711   9296    -77  -1008   -610       N  
ATOM   2360  CA  VAL A 292      -0.844  38.743 108.508  1.00 68.50           C  
ANISOU 2360  CA  VAL A 292     8376   8348   9302   -182   -944   -723       C  
ATOM   2361  C   VAL A 292      -1.492  38.499 109.885  1.00 69.06           C  
ANISOU 2361  C   VAL A 292     8534   8454   9250    -50   -929   -810       C  
ATOM   2362  O   VAL A 292      -1.903  37.397 110.209  1.00 67.85           O  
ANISOU 2362  O   VAL A 292     8459   8353   8969    155   -910   -699       O  
ATOM   2363  CB  VAL A 292      -1.947  39.091 107.498  1.00 67.35           C  
ANISOU 2363  CB  VAL A 292     8354   7858   9378   -183   -873   -563       C  
ATOM   2364  CG1 VAL A 292      -3.231  38.264 107.752  1.00 64.89           C  
ANISOU 2364  CG1 VAL A 292     8124   7463   9067      7   -839   -470       C  
ATOM   2365  CG2 VAL A 292      -2.200  40.589 107.471  1.00 66.88           C  
ANISOU 2365  CG2 VAL A 292     8380   7536   9495   -348   -787   -665       C  
ATOM   2366  N   GLU A 293      -1.604  39.573 110.666  1.00 71.03           N  
ANISOU 2366  N   GLU A 293     8806   8638   9544   -187   -895  -1017       N  
ATOM   2367  CA  GLU A 293      -2.136  39.538 112.009  1.00 72.16           C  
ANISOU 2367  CA  GLU A 293     9041   8819   9559    -95   -864  -1137       C  
ATOM   2368  C   GLU A 293      -3.580  39.131 112.004  1.00 69.82           C  
ANISOU 2368  C   GLU A 293     8890   8267   9370     40   -747  -1000       C  
ATOM   2369  O   GLU A 293      -4.273  39.242 111.011  1.00 69.14           O  
ANISOU 2369  O   GLU A 293     8812   7962   9495     32   -707   -870       O  
ATOM   2370  CB  GLU A 293      -1.969  40.894 112.724  1.00 75.29           C  
ANISOU 2370  CB  GLU A 293     9439   9160  10007   -313   -823  -1421       C  
ATOM   2371  CG  GLU A 293      -2.946  41.097 113.930  1.00 79.72           C  
ANISOU 2371  CG  GLU A 293    10153   9616  10519   -233   -730  -1527       C  
ATOM   2372  CD  GLU A 293      -2.322  41.673 115.240  1.00 87.69           C  
ANISOU 2372  CD  GLU A 293    11138  10863  11316   -336   -766  -1852       C  
ATOM   2373  OE1 GLU A 293      -2.297  40.934 116.266  1.00 88.56           O  
ANISOU 2373  OE1 GLU A 293    11296  11224  11127   -141   -815  -1876       O  
ATOM   2374  OE2 GLU A 293      -1.894  42.860 115.259  1.00 91.80           O  
ANISOU 2374  OE2 GLU A 293    11621  11309  11950   -611   -723  -2091       O  
ATOM   2375  N   LYS A 294      -4.028  38.679 113.149  1.00 69.76           N  
ANISOU 2375  N   LYS A 294     8988   8320   9198    166   -686  -1053       N  
ATOM   2376  CA  LYS A 294      -5.318  38.089 113.251  1.00 68.50           C  
ANISOU 2376  CA  LYS A 294     8942   7976   9111    273   -537   -958       C  
ATOM   2377  C   LYS A 294      -6.371  39.164 113.522  1.00 68.87           C  
ANISOU 2377  C   LYS A 294     9017   7775   9376    198   -431  -1082       C  
ATOM   2378  O   LYS A 294      -6.078  40.230 114.019  1.00 70.09           O  
ANISOU 2378  O   LYS A 294     9182   7901   9550     90   -441  -1255       O  
ATOM   2379  CB  LYS A 294      -5.246  36.968 114.294  1.00 69.46           C  
ANISOU 2379  CB  LYS A 294     9216   8253   8923    459   -464   -927       C  
ATOM   2380  CG  LYS A 294      -4.115  35.957 113.940  1.00 69.53           C  
ANISOU 2380  CG  LYS A 294     9205   8504   8710    600   -572   -788       C  
ATOM   2381  CD  LYS A 294      -4.328  34.562 114.510  1.00 70.90           C  
ANISOU 2381  CD  LYS A 294     9614   8694   8630    839   -420   -648       C  
ATOM   2382  CE  LYS A 294      -2.966  33.886 114.815  1.00 75.43           C  
ANISOU 2382  CE  LYS A 294    10200   9609   8852   1082   -560   -584       C  
ATOM   2383  NZ  LYS A 294      -2.116  33.529 113.608  1.00 73.73           N  
ANISOU 2383  NZ  LYS A 294     9817   9494   8703   1085   -680   -475       N  
ATOM   2384  N   ASP A 295      -7.606  38.911 113.142  1.00 68.33           N  
ANISOU 2384  N   ASP A 295     8945   7535   9483    254   -318  -1017       N  
ATOM   2385  CA  ASP A 295      -8.622  39.953 113.271  1.00 69.37           C  
ANISOU 2385  CA  ASP A 295     9070   7452   9835    243   -227  -1125       C  
ATOM   2386  C   ASP A 295      -9.341  39.770 114.636  1.00 70.15           C  
ANISOU 2386  C   ASP A 295     9274   7542   9838    287    -46  -1264       C  
ATOM   2387  O   ASP A 295      -9.204  38.694 115.281  1.00 69.89           O  
ANISOU 2387  O   ASP A 295     9341   7636   9577    342     27  -1229       O  
ATOM   2388  CB  ASP A 295      -9.563  39.912 112.027  1.00 68.43           C  
ANISOU 2388  CB  ASP A 295     8826   7220   9953    309   -235  -1013       C  
ATOM   2389  CG  ASP A 295     -10.358  41.229 111.826  1.00 71.68           C  
ANISOU 2389  CG  ASP A 295     9223   7420  10593    372   -198  -1081       C  
ATOM   2390  OD1 ASP A 295      -9.937  42.262 112.403  1.00 74.53           O  
ANISOU 2390  OD1 ASP A 295     9698   7664  10957    307   -164  -1193       O  
ATOM   2391  OD2 ASP A 295     -11.387  41.242 111.089  1.00 69.04           O  
ANISOU 2391  OD2 ASP A 295     8763   7046  10421    500   -197  -1039       O  
ATOM   2392  N   ALA A 296     -10.111  40.771 115.081  1.00 74.26           N  
ANISOU 2392  N   ALA A 296     9810   8093  10311    860   -335    319       N  
ATOM   2393  CA  ALA A 296     -10.849  40.622 116.364  1.00 75.60           C  
ANISOU 2393  CA  ALA A 296    10228   8190  10306    887   -144     58       C  
ATOM   2394  C   ALA A 296     -12.076  39.715 116.296  1.00 74.58           C  
ANISOU 2394  C   ALA A 296     9923   8278  10136   1004    146    -53       C  
ATOM   2395  O   ALA A 296     -12.805  39.675 115.327  1.00 73.40           O  
ANISOU 2395  O   ALA A 296     9493   8251  10145   1139    223      5       O  
ATOM   2396  CB  ALA A 296     -11.234  41.974 116.970  1.00 78.71           C  
ANISOU 2396  CB  ALA A 296    10874   8280  10751    973   -124   -122       C  
ATOM   2397  N   ILE A 297     -12.265  38.964 117.361  1.00 75.67           N  
ANISOU 2397  N   ILE A 297    10242   8465  10045    913    276   -188       N  
ATOM   2398  CA  ILE A 297     -13.429  38.123 117.545  1.00 75.36           C  
ANISOU 2398  CA  ILE A 297    10085   8613   9937    985    558   -305       C  
ATOM   2399  C   ILE A 297     -14.668  39.024 117.583  1.00 77.61           C  
ANISOU 2399  C   ILE A 297    10315   8804  10370   1206    788   -485       C  
ATOM   2400  O   ILE A 297     -14.764  39.883 118.450  1.00 78.68           O  
ANISOU 2400  O   ILE A 297    10722   8718  10454   1227    867   -677       O  
ATOM   2401  CB  ILE A 297     -13.347  37.394 118.922  1.00 76.40           C  
ANISOU 2401  CB  ILE A 297    10511   8763   9756    801    642   -424       C  
ATOM   2402  CG1 ILE A 297     -11.910  36.962 119.285  1.00 75.80           C  
ANISOU 2402  CG1 ILE A 297    10600   8635   9566    563    338   -255       C  
ATOM   2403  CG2 ILE A 297     -14.411  36.311 119.057  1.00 75.83           C  
ANISOU 2403  CG2 ILE A 297    10291   8919   9600    822    903   -489       C  
ATOM   2404  CD1 ILE A 297     -11.254  36.030 118.389  1.00 71.38           C  
ANISOU 2404  CD1 ILE A 297     9767   8218   9137    530    198    -31       C  
ATOM   2405  N   PRO A 298     -15.618  38.835 116.630  1.00 77.99           N  
ANISOU 2405  N   PRO A 298    10008   9002  10624   1364    891   -420       N  
ATOM   2406  CA  PRO A 298     -16.923  39.525 116.764  1.00 80.41           C  
ANISOU 2406  CA  PRO A 298    10197   9227  11129   1586   1139   -577       C  
ATOM   2407  C   PRO A 298     -17.471  39.372 118.203  1.00 83.66           C  
ANISOU 2407  C   PRO A 298    10859   9602  11326   1562   1456   -864       C  
ATOM   2408  O   PRO A 298     -17.208  38.367 118.884  1.00 82.25           O  
ANISOU 2408  O   PRO A 298    10836   9571  10847   1368   1502   -887       O  
ATOM   2409  CB  PRO A 298     -17.806  38.806 115.739  1.00 79.26           C  
ANISOU 2409  CB  PRO A 298     9646   9334  11136   1656   1186   -430       C  
ATOM   2410  CG  PRO A 298     -16.836  38.331 114.675  1.00 74.80           C  
ANISOU 2410  CG  PRO A 298     8996   8891  10535   1519    900   -185       C  
ATOM   2411  CD  PRO A 298     -15.576  37.950 115.437  1.00 74.45           C  
ANISOU 2411  CD  PRO A 298     9256   8795  10236   1329    795   -208       C  
ATOM   2412  N   GLU A 299     -18.220  40.376 118.658  1.00 87.48           N  
ANISOU 2412  N   GLU A 299    11388   9879  11972   1748   1680  -1081       N  
ATOM   2413  CA  GLU A 299     -18.393  40.645 120.070  1.00 90.27           C  
ANISOU 2413  CA  GLU A 299    12112  10101  12086   1693   1954  -1396       C  
ATOM   2414  C   GLU A 299     -19.487  39.822 120.758  1.00 92.70           C  
ANISOU 2414  C   GLU A 299    12343  10624  12256   1686   2358  -1555       C  
ATOM   2415  O   GLU A 299     -19.424  39.570 121.980  1.00 94.72           O  
ANISOU 2415  O   GLU A 299    12956  10885  12147   1509   2555  -1761       O  
ATOM   2416  CB  GLU A 299     -18.724  42.111 120.218  1.00 94.04           C  
ANISOU 2416  CB  GLU A 299    12670  10227  12835   1912   2058  -1592       C  
ATOM   2417  CG  GLU A 299     -19.785  42.589 119.209  1.00 95.25           C  
ANISOU 2417  CG  GLU A 299    12336  10352  13502   2225   2128  -1500       C  
ATOM   2418  CD  GLU A 299     -19.193  43.162 117.910  1.00 92.48           C  
ANISOU 2418  CD  GLU A 299    11798   9911  13431   2273   1705  -1190       C  
ATOM   2419  OE1 GLU A 299     -18.445  42.441 117.208  1.00 85.09           O  
ANISOU 2419  OE1 GLU A 299    10792   9186  12350   2098   1425   -930       O  
ATOM   2420  OE2 GLU A 299     -19.490  44.343 117.599  1.00 94.48           O  
ANISOU 2420  OE2 GLU A 299    11974   9867  14056   2482   1668  -1213       O  
ATOM   2421  N   ASN A 300     -20.516  39.442 120.007  1.00 92.26           N  
ANISOU 2421  N   ASN A 300    11832  10745  12478   1852   2481  -1451       N  
ATOM   2422  CA  ASN A 300     -21.675  38.827 120.632  1.00 94.51           C  
ANISOU 2422  CA  ASN A 300    11990  11214  12704   1870   2894  -1599       C  
ATOM   2423  C   ASN A 300     -21.821  37.444 120.075  1.00 91.38           C  
ANISOU 2423  C   ASN A 300    11348  11148  12222   1730   2784  -1359       C  
ATOM   2424  O   ASN A 300     -22.864  37.081 119.544  1.00 91.88           O  
ANISOU 2424  O   ASN A 300    11013  11375  12524   1842   2914  -1277       O  
ATOM   2425  CB  ASN A 300     -22.933  39.663 120.396  1.00 97.97           C  
ANISOU 2425  CB  ASN A 300    12083  11536  13604   2198   3187  -1715       C  
ATOM   2426  CG  ASN A 300     -22.955  40.951 121.231  1.00102.79           C  
ANISOU 2426  CG  ASN A 300    12987  11790  14278   2338   3424  -2053       C  
ATOM   2427  OD1 ASN A 300     -22.537  40.971 122.394  1.00103.07           O  
ANISOU 2427  OD1 ASN A 300    13491  11762  13908   2156   3589  -2302       O  
ATOM   2428  ND2 ASN A 300     -23.470  42.027 120.639  1.00104.67           N  
ANISOU 2428  ND2 ASN A 300    12960  11778  15031   2648   3435  -2059       N  
ATOM   2429  N   LEU A 301     -20.746  36.674 120.186  1.00 88.26           N  
ANISOU 2429  N   LEU A 301    11190  10829  11515   1477   2522  -1236       N  
ATOM   2430  CA  LEU A 301     -20.733  35.376 119.580  1.00 85.06           C  
ANISOU 2430  CA  LEU A 301    10583  10681  11056   1347   2382  -1015       C  
ATOM   2431  C   LEU A 301     -21.528  34.403 120.382  1.00 85.65           C  
ANISOU 2431  C   LEU A 301    10657  10962  10924   1214   2669  -1090       C  
ATOM   2432  O   LEU A 301     -21.301  34.265 121.574  1.00 87.15           O  
ANISOU 2432  O   LEU A 301    11199  11131  10786   1042   2806  -1238       O  
ATOM   2433  CB  LEU A 301     -19.314  34.854 119.349  1.00 82.42           C  
ANISOU 2433  CB  LEU A 301    10441  10330  10546   1153   2016   -846       C  
ATOM   2434  CG  LEU A 301     -18.678  35.374 118.065  1.00 80.73           C  
ANISOU 2434  CG  LEU A 301    10057  10038  10578   1255   1717   -667       C  
ATOM   2435  CD1 LEU A 301     -17.508  36.145 118.548  1.00 83.19           C  
ANISOU 2435  CD1 LEU A 301    10700  10120  10787   1188   1535   -703       C  
ATOM   2436  CD2 LEU A 301     -18.207  34.283 117.130  1.00 75.43           C  
ANISOU 2436  CD2 LEU A 301     9218   9538   9904   1145   1510   -452       C  
ATOM   2437  N   PRO A 302     -22.456  33.706 119.706  1.00 85.01           N  
ANISOU 2437  N   PRO A 302    10191  11089  11018   1258   2736   -967       N  
ATOM   2438  CA  PRO A 302     -23.360  32.699 120.270  1.00 86.52           C  
ANISOU 2438  CA  PRO A 302    10290  11510  11074   1127   2994   -984       C  
ATOM   2439  C   PRO A 302     -22.577  31.498 120.787  1.00 85.00           C  
ANISOU 2439  C   PRO A 302    10374  11406  10516    819   2833   -894       C  
ATOM   2440  O   PRO A 302     -21.867  30.854 119.978  1.00 82.56           O  
ANISOU 2440  O   PRO A 302    10013  11115  10241    751   2510   -702       O  
ATOM   2441  CB  PRO A 302     -24.222  32.303 119.059  1.00 85.65           C  
ANISOU 2441  CB  PRO A 302     9698  11558  11289   1229   2928   -793       C  
ATOM   2442  CG  PRO A 302     -23.335  32.622 117.841  1.00 82.10           C  
ANISOU 2442  CG  PRO A 302     9206  11006  10982   1289   2534   -627       C  
ATOM   2443  CD  PRO A 302     -22.655  33.881 118.254  1.00 82.79           C  
ANISOU 2443  CD  PRO A 302     9543  10834  11079   1407   2520   -769       C  
ATOM   2444  N   PRO A 303     -22.716  31.163 122.091  1.00 87.22           N  
ANISOU 2444  N   PRO A 303    10940  11738  10463    622   3057  -1021       N  
ATOM   2445  CA  PRO A 303     -21.842  30.139 122.698  1.00 86.34           C  
ANISOU 2445  CA  PRO A 303    11138  11655  10013    309   2844   -907       C  
ATOM   2446  C   PRO A 303     -21.796  28.828 121.889  1.00 83.90           C  
ANISOU 2446  C   PRO A 303    10602  11479   9797    215   2617   -665       C  
ATOM   2447  O   PRO A 303     -22.854  28.327 121.471  1.00 84.06           O  
ANISOU 2447  O   PRO A 303    10309  11675   9956    249   2769   -620       O  
ATOM   2448  CB  PRO A 303     -22.461  29.906 124.096  1.00 90.56           C  
ANISOU 2448  CB  PRO A 303    11914  12297  10197    100   3192  -1059       C  
ATOM   2449  CG  PRO A 303     -23.897  30.370 124.005  1.00 92.44           C  
ANISOU 2449  CG  PRO A 303    11821  12648  10653    307   3629  -1209       C  
ATOM   2450  CD  PRO A 303     -23.916  31.435 122.915  1.00 92.26           C  
ANISOU 2450  CD  PRO A 303    11525  12470  11060    657   3536  -1225       C  
ATOM   2451  N   LEU A 304     -20.581  28.314 121.649  1.00 81.21           N  
ANISOU 2451  N   LEU A 304    10407  11037   9414    104   2261   -517       N  
ATOM   2452  CA  LEU A 304     -20.345  27.012 120.949  1.00 79.43           C  
ANISOU 2452  CA  LEU A 304    10031  10876   9272      2   2041   -319       C  
ATOM   2453  C   LEU A 304     -21.379  25.899 121.198  1.00 80.61           C  
ANISOU 2453  C   LEU A 304    10055  11222   9349   -156   2198   -261       C  
ATOM   2454  O   LEU A 304     -21.919  25.322 120.254  1.00 80.30           O  
ANISOU 2454  O   LEU A 304     9730  11281   9500   -112   2167   -178       O  
ATOM   2455  CB  LEU A 304     -18.908  26.469 121.226  1.00 77.73           C  
ANISOU 2455  CB  LEU A 304    10065  10502   8968   -162   1707   -187       C  
ATOM   2456  CG  LEU A 304     -17.785  27.310 120.556  1.00 76.49           C  
ANISOU 2456  CG  LEU A 304     9915  10168   8979     -9   1486   -171       C  
ATOM   2457  CD1 LEU A 304     -16.333  26.861 120.887  1.00 74.75           C  
ANISOU 2457  CD1 LEU A 304     9892   9778   8732   -161   1160    -22       C  
ATOM   2458  CD2 LEU A 304     -18.006  27.446 119.045  1.00 70.51           C  
ANISOU 2458  CD2 LEU A 304     8821   9459   8509    196   1462   -144       C  
ATOM   2459  N   THR A 305     -21.645  25.611 122.463  1.00 82.64           N  
ANISOU 2459  N   THR A 305    10548  11540   9312   -371   2355   -297       N  
ATOM   2460  CA  THR A 305     -22.643  24.625 122.851  1.00 84.74           C  
ANISOU 2460  CA  THR A 305    10719  12003   9477   -559   2528   -234       C  
ATOM   2461  C   THR A 305     -23.968  24.684 122.066  1.00 85.88           C  
ANISOU 2461  C   THR A 305    10433  12322   9875   -399   2750   -253       C  
ATOM   2462  O   THR A 305     -24.628  23.641 121.886  1.00 86.47           O  
ANISOU 2462  O   THR A 305    10342  12538   9974   -546   2754   -127       O  
ATOM   2463  CB  THR A 305     -22.955  24.706 124.372  1.00 87.81           C  
ANISOU 2463  CB  THR A 305    11417  12468   9478   -793   2784   -327       C  
ATOM   2464  OG1 THR A 305     -22.285  25.849 124.926  1.00 89.73           O  
ANISOU 2464  OG1 THR A 305    11953  12558   9582   -730   2806   -490       O  
ATOM   2465  CG2 THR A 305     -22.473  23.453 125.088  1.00 86.39           C  
ANISOU 2465  CG2 THR A 305    11488  12289   9049  -1155   2565   -128       C  
ATOM   2466  N   ALA A 306     -24.355  25.883 121.616  1.00 86.04           N  
ANISOU 2466  N   ALA A 306    10270  12318  10103   -119   2903   -385       N  
ATOM   2467  CA  ALA A 306     -25.614  26.071 120.889  1.00 87.00           C  
ANISOU 2467  CA  ALA A 306     9952  12585  10518     40   3082   -372       C  
ATOM   2468  C   ALA A 306     -25.965  25.121 119.733  1.00 85.66           C  
ANISOU 2468  C   ALA A 306     9496  12512  10540    -12   2863   -176       C  
ATOM   2469  O   ALA A 306     -27.044  24.470 119.733  1.00 87.42           O  
ANISOU 2469  O   ALA A 306     9476  12921  10818   -119   2999    -94       O  
ATOM   2470  CB  ALA A 306     -25.679  27.474 120.284  1.00 86.81           C  
ANISOU 2470  CB  ALA A 306     9770  12443  10772    362   3123   -476       C  
ATOM   2471  N   ASP A 307     -25.035  25.015 118.786  1.00 81.92           N  
ANISOU 2471  N   ASP A 307     9068  11911  10146     35   2534   -105       N  
ATOM   2472  CA  ASP A 307     -25.302  24.319 117.534  1.00 80.61           C  
ANISOU 2472  CA  ASP A 307     8669  11809  10152      2   2330     35       C  
ATOM   2473  C   ASP A 307     -24.844  22.890 117.666  1.00 79.03           C  
ANISOU 2473  C   ASP A 307     8637  11590   9802   -250   2162    128       C  
ATOM   2474  O   ASP A 307     -25.372  22.021 116.974  1.00 78.48           O  
ANISOU 2474  O   ASP A 307     8405  11603   9810   -366   2068    229       O  
ATOM   2475  CB  ASP A 307     -24.599  24.926 116.314  1.00 78.68           C  
ANISOU 2475  CB  ASP A 307     8377  11451  10065    164   2097     51       C  
ATOM   2476  CG  ASP A 307     -25.387  26.065 115.659  1.00 81.07           C  
ANISOU 2476  CG  ASP A 307     8380  11797  10626    380   2166     57       C  
ATOM   2477  OD1 ASP A 307     -25.210  26.249 114.445  1.00 80.11           O  
ANISOU 2477  OD1 ASP A 307     8142  11662  10633    426   1954    141       O  
ATOM   2478  OD2 ASP A 307     -26.178  26.773 116.332  1.00 87.45           O  
ANISOU 2478  OD2 ASP A 307     9065  12642  11520    497   2430    -18       O  
ATOM   2479  N   PHE A 308     -23.861  22.658 118.539  1.00 78.06           N  
ANISOU 2479  N   PHE A 308     8840  11336   9483   -347   2098    105       N  
ATOM   2480  CA  PHE A 308     -23.070  21.430 118.484  1.00 76.41           C  
ANISOU 2480  CA  PHE A 308     8796  11013   9224   -529   1857    205       C  
ATOM   2481  C   PHE A 308     -23.283  20.453 119.619  1.00 78.02           C  
ANISOU 2481  C   PHE A 308     9167  11251   9225   -803   1890    290       C  
ATOM   2482  O   PHE A 308     -22.761  19.349 119.598  1.00 78.48           O  
ANISOU 2482  O   PHE A 308     9335  11195   9290   -963   1682    398       O  
ATOM   2483  CB  PHE A 308     -21.602  21.770 118.389  1.00 74.14           C  
ANISOU 2483  CB  PHE A 308     8709  10508   8952   -443   1656    183       C  
ATOM   2484  CG  PHE A 308     -21.273  22.619 117.208  1.00 72.90           C  
ANISOU 2484  CG  PHE A 308     8408  10315   8976   -218   1595    129       C  
ATOM   2485  CD1 PHE A 308     -21.244  22.068 115.922  1.00 70.03           C  
ANISOU 2485  CD1 PHE A 308     7897   9953   8757   -211   1472    162       C  
ATOM   2486  CD2 PHE A 308     -20.991  23.988 117.367  1.00 70.70           C  
ANISOU 2486  CD2 PHE A 308     8165   9991   8705    -39   1657     43       C  
ATOM   2487  CE1 PHE A 308     -20.970  22.858 114.829  1.00 64.22           C  
ANISOU 2487  CE1 PHE A 308     7050   9209   8142    -51   1417    130       C  
ATOM   2488  CE2 PHE A 308     -20.714  24.761 116.270  1.00 65.08           C  
ANISOU 2488  CE2 PHE A 308     7322   9249   8156    136   1581     27       C  
ATOM   2489  CZ  PHE A 308     -20.729  24.188 114.997  1.00 61.67           C  
ANISOU 2489  CZ  PHE A 308     6739   8854   7840    120   1463     81       C  
ATOM   2490  N   ALA A 309     -24.028  20.841 120.624  1.00 79.91           N  
ANISOU 2490  N   ALA A 309     9438  11635   9291   -870   2158    245       N  
ATOM   2491  CA  ALA A 309     -24.304  19.897 121.669  1.00 81.69           C  
ANISOU 2491  CA  ALA A 309     9824  11925   9291  -1177   2196    350       C  
ATOM   2492  C   ALA A 309     -25.773  19.840 122.031  1.00 84.06           C  
ANISOU 2492  C   ALA A 309     9909  12487   9545  -1266   2526    348       C  
ATOM   2493  O   ALA A 309     -26.298  18.756 122.170  1.00 85.23           O  
ANISOU 2493  O   ALA A 309    10008  12719   9655  -1504   2493    492       O  
ATOM   2494  CB  ALA A 309     -23.426  20.154 122.890  1.00 82.62           C  
ANISOU 2494  CB  ALA A 309    10329  11935   9129  -1307   2155    339       C  
ATOM   2495  N   GLU A 310     -26.456  20.973 122.168  1.00 85.84           N  
ANISOU 2495  N   GLU A 310     9979  12827   9809  -1076   2846    195       N  
ATOM   2496  CA  GLU A 310     -27.861  20.904 122.644  1.00 90.26           C  
ANISOU 2496  CA  GLU A 310    10303  13641  10352  -1166   3214    194       C  
ATOM   2497  C   GLU A 310     -28.770  20.687 121.455  1.00 90.03           C  
ANISOU 2497  C   GLU A 310     9826  13716  10665  -1066   3169    290       C  
ATOM   2498  O   GLU A 310     -29.882  20.196 121.602  1.00 92.00           O  
ANISOU 2498  O   GLU A 310     9827  14167  10960  -1207   3346    383       O  
ATOM   2499  CB  GLU A 310     -28.326  22.142 123.425  1.00 92.59           C  
ANISOU 2499  CB  GLU A 310    10601  14006  10572  -1019   3643    -26       C  
ATOM   2500  CG  GLU A 310     -27.269  22.822 124.284  1.00 94.35           C  
ANISOU 2500  CG  GLU A 310    11275  14065  10509  -1024   3637   -177       C  
ATOM   2501  CD  GLU A 310     -27.423  24.355 124.309  1.00 97.58           C  
ANISOU 2501  CD  GLU A 310    11629  14406  11040   -707   3909   -430       C  
ATOM   2502  OE1 GLU A 310     -26.690  25.045 123.533  1.00 97.66           O  
ANISOU 2502  OE1 GLU A 310    11635  14227  11245   -468   3674   -464       O  
ATOM   2503  OE2 GLU A 310     -28.262  24.858 125.094  1.00 99.03           O  
ANISOU 2503  OE2 GLU A 310    11774  14713  11139   -703   4364   -596       O  
ATOM   2504  N   ASP A 311     -28.276  21.036 120.268  1.00 87.51           N  
ANISOU 2504  N   ASP A 311     9414  13265  10572   -857   2914    285       N  
ATOM   2505  CA  ASP A 311     -29.109  20.923 119.085  1.00 88.11           C  
ANISOU 2505  CA  ASP A 311     9097  13435  10944   -791   2830    387       C  
ATOM   2506  C   ASP A 311     -29.694  19.507 118.891  1.00 89.21           C  
ANISOU 2506  C   ASP A 311     9147  13678  11069  -1092   2702    573       C  
ATOM   2507  O   ASP A 311     -28.992  18.528 118.590  1.00 87.14           O  
ANISOU 2507  O   ASP A 311     9095  13283  10729  -1250   2417    639       O  
ATOM   2508  CB  ASP A 311     -28.392  21.431 117.848  1.00 84.95           C  
ANISOU 2508  CB  ASP A 311     8680  12883  10712   -588   2555    365       C  
ATOM   2509  CG  ASP A 311     -29.265  22.329 117.017  1.00 87.61           C  
ANISOU 2509  CG  ASP A 311     8625  13308  11356   -381   2612    390       C  
ATOM   2510  OD1 ASP A 311     -30.471  22.003 116.873  1.00 93.02           O  
ANISOU 2510  OD1 ASP A 311     8978  14172  12192   -467   2704    510       O  
ATOM   2511  OD2 ASP A 311     -28.767  23.378 116.539  1.00 85.79           O  
ANISOU 2511  OD2 ASP A 311     8401  12960  11237   -144   2553    315       O  
ATOM   2512  N   LYS A 312     -31.000  19.425 119.093  1.00 92.48           N  
ANISOU 2512  N   LYS A 312     9233  14315  11591  -1169   2931    654       N  
ATOM   2513  CA  LYS A 312     -31.738  18.179 119.000  1.00 94.30           C  
ANISOU 2513  CA  LYS A 312     9337  14669  11823  -1476   2844    847       C  
ATOM   2514  C   LYS A 312     -31.694  17.604 117.593  1.00 92.49           C  
ANISOU 2514  C   LYS A 312     9014  14365  11763  -1521   2466    950       C  
ATOM   2515  O   LYS A 312     -32.388  16.634 117.311  1.00 93.96           O  
ANISOU 2515  O   LYS A 312     9067  14639  11994  -1774   2353   1112       O  
ATOM   2516  CB  LYS A 312     -33.178  18.427 119.461  1.00 99.21           C  
ANISOU 2516  CB  LYS A 312     9554  15559  12581  -1511   3203    913       C  
ATOM   2517  CG  LYS A 312     -33.683  19.855 119.192  1.00100.61           C  
ANISOU 2517  CG  LYS A 312     9403  15779  13046  -1157   3435    807       C  
ATOM   2518  CD  LYS A 312     -34.499  19.909 117.920  1.00100.75           C  
ANISOU 2518  CD  LYS A 312     8979  15866  13436  -1105   3230    980       C  
ATOM   2519  CE  LYS A 312     -35.735  20.747 118.158  1.00104.72           C  
ANISOU 2519  CE  LYS A 312     8978  16538  14274   -934   3592   1003       C  
ATOM   2520  NZ  LYS A 312     -36.948  20.010 117.743  1.00106.83           N  
ANISOU 2520  NZ  LYS A 312     8814  17009  14767  -1156   3525   1268       N  
ATOM   2521  N   ASP A 313     -30.846  18.207 116.743  1.00 89.12           N  
ANISOU 2521  N   ASP A 313     8686  13774  11400  -1304   2280    850       N  
ATOM   2522  CA  ASP A 313     -30.671  17.862 115.333  1.00 87.01           C  
ANISOU 2522  CA  ASP A 313     8383  13430  11245  -1331   1953    900       C  
ATOM   2523  C   ASP A 313     -29.209  17.680 114.936  1.00 83.50           C  
ANISOU 2523  C   ASP A 313     8301  12736  10689  -1270   1746    779       C  
ATOM   2524  O   ASP A 313     -28.937  17.568 113.736  1.00 82.58           O  
ANISOU 2524  O   ASP A 313     8191  12552  10634  -1266   1527    770       O  
ATOM   2525  CB  ASP A 313     -31.235  18.966 114.409  1.00 87.38           C  
ANISOU 2525  CB  ASP A 313     8100  13562  11539  -1121   1937    928       C  
ATOM   2526  CG  ASP A 313     -32.757  19.012 114.389  1.00 92.10           C  
ANISOU 2526  CG  ASP A 313     8243  14391  12361  -1197   2049   1102       C  
ATOM   2527  OD1 ASP A 313     -33.309  20.096 114.048  1.00 91.85           O  
ANISOU 2527  OD1 ASP A 313     7893  14422  12584   -980   2123   1134       O  
ATOM   2528  OD2 ASP A 313     -33.404  17.972 114.712  1.00 94.47           O  
ANISOU 2528  OD2 ASP A 313     8481  14796  12616  -1475   2052   1226       O  
ATOM   2529  N   VAL A 314     -28.280  17.651 115.893  1.00 81.35           N  
ANISOU 2529  N   VAL A 314     8321  12333  10257  -1241   1810    695       N  
ATOM   2530  CA  VAL A 314     -26.866  17.437 115.563  1.00 78.92           C  
ANISOU 2530  CA  VAL A 314     8306  11777   9903  -1181   1617    606       C  
ATOM   2531  C   VAL A 314     -26.600  16.232 114.641  1.00 78.25           C  
ANISOU 2531  C   VAL A 314     8311  11561   9860  -1351   1371    630       C  
ATOM   2532  O   VAL A 314     -25.885  16.386 113.646  1.00 76.28           O  
ANISOU 2532  O   VAL A 314     8125  11192   9664  -1249   1245    541       O  
ATOM   2533  CB  VAL A 314     -25.914  17.290 116.804  1.00 78.85           C  
ANISOU 2533  CB  VAL A 314     8602  11625   9733  -1207   1646    579       C  
ATOM   2534  CG1 VAL A 314     -24.492  17.086 116.329  1.00 76.41           C  
ANISOU 2534  CG1 VAL A 314     8507  11056   9469  -1125   1436    514       C  
ATOM   2535  CG2 VAL A 314     -25.939  18.498 117.701  1.00 80.20           C  
ANISOU 2535  CG2 VAL A 314     8787  11872   9813  -1053   1879    502       C  
ATOM   2536  N   CYS A 315     -27.123  15.047 114.987  1.00 79.37           N  
ANISOU 2536  N   CYS A 315     8479  11708   9970  -1618   1317    737       N  
ATOM   2537  CA  CYS A 315     -26.788  13.814 114.252  1.00 79.83           C  
ANISOU 2537  CA  CYS A 315     8681  11576  10075  -1790   1091    731       C  
ATOM   2538  C   CYS A 315     -27.327  13.824 112.840  1.00 78.99           C  
ANISOU 2538  C   CYS A 315     8434  11542  10036  -1830    982    707       C  
ATOM   2539  O   CYS A 315     -26.652  13.386 111.898  1.00 76.87           O  
ANISOU 2539  O   CYS A 315     8323  11095   9787  -1841    845    592       O  
ATOM   2540  CB  CYS A 315     -27.340  12.578 114.938  1.00 82.76           C  
ANISOU 2540  CB  CYS A 315     9103  11930  10411  -2093   1037    875       C  
ATOM   2541  SG  CYS A 315     -26.391  11.941 116.305  1.00 88.35           S  
ANISOU 2541  SG  CYS A 315    10107  12421  11043  -2174    996    935       S  
ATOM   2542  N   LYS A 316     -28.571  14.292 112.733  1.00 80.02           N  
ANISOU 2542  N   LYS A 316     8266  11933  10204  -1874   1049    824       N  
ATOM   2543  CA  LYS A 316     -29.223  14.650 111.472  1.00 80.33           C  
ANISOU 2543  CA  LYS A 316     8112  12096  10312  -1902    932    859       C  
ATOM   2544  C   LYS A 316     -28.359  15.624 110.628  1.00 78.30           C  
ANISOU 2544  C   LYS A 316     7923  11773  10052  -1665    901    725       C  
ATOM   2545  O   LYS A 316     -28.002  15.335 109.490  1.00 78.06           O  
ANISOU 2545  O   LYS A 316     8018  11662   9978  -1744    743    651       O  
ATOM   2546  CB  LYS A 316     -30.581  15.283 111.795  1.00 82.37           C  
ANISOU 2546  CB  LYS A 316     7976  12633  10687  -1903   1054   1031       C  
ATOM   2547  CG  LYS A 316     -31.620  15.150 110.712  1.00 83.79           C  
ANISOU 2547  CG  LYS A 316     7913  12956  10966  -2088    859   1179       C  
ATOM   2548  CD  LYS A 316     -32.113  16.523 110.278  1.00 83.39           C  
ANISOU 2548  CD  LYS A 316     7544  13058  11084  -1872    896   1251       C  
ATOM   2549  CE  LYS A 316     -33.065  16.430 109.074  1.00 87.47           C  
ANISOU 2549  CE  LYS A 316     7829  13703  11703  -2085    621   1440       C  
ATOM   2550  NZ  LYS A 316     -34.118  15.333 109.202  1.00 86.60           N  
ANISOU 2550  NZ  LYS A 316     7575  13698  11632  -2429    526   1619       N  
ATOM   2551  N   ASN A 317     -28.008  16.769 111.204  1.00 77.39           N  
ANISOU 2551  N   ASN A 317     7750  11687   9967  -1398   1063    688       N  
ATOM   2552  CA  ASN A 317     -27.122  17.721 110.544  1.00 76.25           C  
ANISOU 2552  CA  ASN A 317     7678  11470   9823  -1182   1036    584       C  
ATOM   2553  C   ASN A 317     -25.893  17.005 109.997  1.00 75.37           C  
ANISOU 2553  C   ASN A 317     7870  11134   9631  -1222    937    436       C  
ATOM   2554  O   ASN A 317     -25.534  17.178 108.842  1.00 75.40           O  
ANISOU 2554  O   ASN A 317     7930  11117   9602  -1232    840    373       O  
ATOM   2555  CB  ASN A 317     -26.670  18.852 111.505  1.00 74.61           C  
ANISOU 2555  CB  ASN A 317     7461  11247   9639   -913   1222    535       C  
ATOM   2556  CG  ASN A 317     -27.839  19.711 112.061  1.00 75.85           C  
ANISOU 2556  CG  ASN A 317     7307  11596   9918   -818   1391    631       C  
ATOM   2557  OD1 ASN A 317     -28.964  19.718 111.538  1.00 72.86           O  
ANISOU 2557  OD1 ASN A 317     6647  11376   9662   -905   1342    766       O  
ATOM   2558  ND2 ASN A 317     -27.547  20.444 113.147  1.00 74.31           N  
ANISOU 2558  ND2 ASN A 317     7163  11370   9702   -644   1596    557       N  
ATOM   2559  N   TYR A 318     -25.277  16.185 110.845  1.00 75.84           N  
ANISOU 2559  N   TYR A 318     8119  11024   9673  -1260    968    393       N  
ATOM   2560  CA  TYR A 318     -23.933  15.654 110.612  1.00 75.08           C  
ANISOU 2560  CA  TYR A 318     8271  10668   9588  -1217    922    253       C  
ATOM   2561  C   TYR A 318     -24.010  14.631 109.487  1.00 76.54           C  
ANISOU 2561  C   TYR A 318     8560  10764   9757  -1417    805    173       C  
ATOM   2562  O   TYR A 318     -23.271  14.725 108.482  1.00 75.96           O  
ANISOU 2562  O   TYR A 318     8593  10602   9665  -1373    795     30       O  
ATOM   2563  CB  TYR A 318     -23.378  15.091 111.930  1.00 74.77           C  
ANISOU 2563  CB  TYR A 318     8367  10467   9575  -1221    945    288       C  
ATOM   2564  CG  TYR A 318     -22.154  14.217 111.861  1.00 73.86           C  
ANISOU 2564  CG  TYR A 318     8461  10041   9561  -1216    867    197       C  
ATOM   2565  CD1 TYR A 318     -20.953  14.681 111.332  1.00 75.22           C  
ANISOU 2565  CD1 TYR A 318     8695  10078   9806  -1029    885     75       C  
ATOM   2566  CD2 TYR A 318     -22.194  12.916 112.371  1.00 76.95           C  
ANISOU 2566  CD2 TYR A 318     8967  10258  10014  -1399    776    253       C  
ATOM   2567  CE1 TYR A 318     -19.819  13.833 111.286  1.00 76.88           C  
ANISOU 2567  CE1 TYR A 318     9047   9980  10185  -1005    836     -3       C  
ATOM   2568  CE2 TYR A 318     -21.084  12.078 112.360  1.00 76.66           C  
ANISOU 2568  CE2 TYR A 318     9089   9889  10148  -1375    696    186       C  
ATOM   2569  CZ  TYR A 318     -19.916  12.526 111.808  1.00 77.14           C  
ANISOU 2569  CZ  TYR A 318     9179   9816  10316  -1169    738     53       C  
ATOM   2570  OH  TYR A 318     -18.854  11.658 111.773  1.00 78.29           O  
ANISOU 2570  OH  TYR A 318     9431   9617  10698  -1131    682    -12       O  
ATOM   2571  N   GLN A 319     -24.950  13.706 109.611  1.00 77.95           N  
ANISOU 2571  N   GLN A 319     8713  10980   9926  -1658    730    260       N  
ATOM   2572  CA  GLN A 319     -25.139  12.717 108.552  1.00 80.50           C  
ANISOU 2572  CA  GLN A 319     9165  11209  10213  -1890    605    174       C  
ATOM   2573  C   GLN A 319     -25.413  13.244 107.140  1.00 81.08           C  
ANISOU 2573  C   GLN A 319     9213  11420  10174  -1953    538    122       C  
ATOM   2574  O   GLN A 319     -25.016  12.614 106.170  1.00 82.67           O  
ANISOU 2574  O   GLN A 319     9622  11484  10304  -2083    491    -44       O  
ATOM   2575  CB  GLN A 319     -26.155  11.663 108.963  1.00 82.79           C  
ANISOU 2575  CB  GLN A 319     9427  11516  10515  -2169    507    306       C  
ATOM   2576  CG  GLN A 319     -25.484  10.587 109.805  1.00 84.40           C  
ANISOU 2576  CG  GLN A 319     9825  11429  10816  -2204    494    280       C  
ATOM   2577  CD  GLN A 319     -26.344  10.142 110.952  1.00 85.83           C  
ANISOU 2577  CD  GLN A 319     9903  11705  11002  -2368    479    497       C  
ATOM   2578  OE1 GLN A 319     -26.960  10.957 111.623  1.00 85.85           O  
ANISOU 2578  OE1 GLN A 319     9697  11962  10961  -2304    591    630       O  
ATOM   2579  NE2 GLN A 319     -26.381   8.843 111.191  1.00 87.78           N  
ANISOU 2579  NE2 GLN A 319    10303  11737  11311  -2587    357    528       N  
ATOM   2580  N   GLU A 320     -26.034  14.418 107.023  1.00 80.68           N  
ANISOU 2580  N   GLU A 320     8923  11620  10111  -1866    538    257       N  
ATOM   2581  CA  GLU A 320     -26.361  14.961 105.704  1.00 80.63           C  
ANISOU 2581  CA  GLU A 320     8883  11756   9998  -1964    420    271       C  
ATOM   2582  C   GLU A 320     -25.146  15.527 104.948  1.00 78.06           C  
ANISOU 2582  C   GLU A 320     8728  11342   9588  -1822    488     96       C  
ATOM   2583  O   GLU A 320     -25.056  15.313 103.768  1.00 79.00           O  
ANISOU 2583  O   GLU A 320     9000  11468   9551  -2004    409      6       O  
ATOM   2584  CB  GLU A 320     -27.667  15.813 105.728  1.00 81.85           C  
ANISOU 2584  CB  GLU A 320     8684  12186  10228  -1985    334    527       C  
ATOM   2585  CG  GLU A 320     -28.888  14.964 106.312  1.00 85.06           C  
ANISOU 2585  CG  GLU A 320     8929  12678  10712  -2207    272    692       C  
ATOM   2586  CD  GLU A 320     -30.299  15.572 106.112  1.00 89.58           C  
ANISOU 2586  CD  GLU A 320     9111  13514  11409  -2291    157    964       C  
ATOM   2587  OE1 GLU A 320     -30.398  16.774 105.740  1.00 89.73           O  
ANISOU 2587  OE1 GLU A 320     8948  13642  11502  -2125    139   1045       O  
ATOM   2588  OE2 GLU A 320     -31.311  14.836 106.338  1.00 90.64           O  
ANISOU 2588  OE2 GLU A 320     9102  13733  11603  -2528     75   1114       O  
ATOM   2589  N   ALA A 321     -24.251  16.257 105.621  1.00 75.71           N  
ANISOU 2589  N   ALA A 321     8410  10976   9378  -1530    630     57       N  
ATOM   2590  CA  ALA A 321     -22.843  16.474 105.144  1.00 74.63           C  
ANISOU 2590  CA  ALA A 321     8455  10690   9213  -1395    734   -130       C  
ATOM   2591  C   ALA A 321     -21.785  16.444 106.280  1.00 72.33           C  
ANISOU 2591  C   ALA A 321     8204  10201   9079  -1157    861   -185       C  
ATOM   2592  O   ALA A 321     -21.576  17.419 106.971  1.00 70.58           O  
ANISOU 2592  O   ALA A 321     7872  10029   8917   -959    904   -102       O  
ATOM   2593  CB  ALA A 321     -22.699  17.736 104.304  1.00 73.74           C  
ANISOU 2593  CB  ALA A 321     8273  10732   9013  -1331    705    -82       C  
ATOM   2594  N   LYS A 322     -21.128  15.307 106.453  1.00 73.59           N  
ANISOU 2594  N   LYS A 322     8530  10115   9317  -1196    900   -317       N  
ATOM   2595  CA  LYS A 322     -20.248  15.074 107.598  1.00 73.57           C  
ANISOU 2595  CA  LYS A 322     8556   9906   9491  -1031    950   -311       C  
ATOM   2596  C   LYS A 322     -19.096  16.076 107.544  1.00 72.78           C  
ANISOU 2596  C   LYS A 322     8434   9775   9446   -801   1032   -350       C  
ATOM   2597  O   LYS A 322     -18.854  16.836 108.499  1.00 72.24           O  
ANISOU 2597  O   LYS A 322     8294   9728   9427   -650   1031   -241       O  
ATOM   2598  CB  LYS A 322     -19.744  13.625 107.615  1.00 75.09           C  
ANISOU 2598  CB  LYS A 322     8914   9799   9818  -1121    946   -434       C  
ATOM   2599  CG  LYS A 322     -20.849  12.535 107.865  1.00 76.44           C  
ANISOU 2599  CG  LYS A 322     9123   9960   9961  -1372    834   -365       C  
ATOM   2600  CD  LYS A 322     -20.233  11.118 107.884  1.00 74.57           C  
ANISOU 2600  CD  LYS A 322     9065   9359   9910  -1439    818   -493       C  
ATOM   2601  CE  LYS A 322     -21.220  10.030 108.303  1.00 77.06           C  
ANISOU 2601  CE  LYS A 322     9427   9625  10226  -1694    681   -392       C  
ATOM   2602  NZ  LYS A 322     -20.759   9.024 109.387  1.00 76.32           N  
ANISOU 2602  NZ  LYS A 322     9407   9221  10368  -1702    597   -307       N  
ATOM   2603  N   ASP A 323     -18.429  16.139 106.408  1.00 73.18           N  
ANISOU 2603  N   ASP A 323     8554   9789   9460   -801   1108   -502       N  
ATOM   2604  CA  ASP A 323     -17.333  17.068 106.272  1.00 72.47           C  
ANISOU 2604  CA  ASP A 323     8426   9681   9427   -613   1188   -523       C  
ATOM   2605  C   ASP A 323     -17.713  18.584 106.386  1.00 70.98           C  
ANISOU 2605  C   ASP A 323     8106   9721   9143   -519   1137   -370       C  
ATOM   2606  O   ASP A 323     -16.905  19.414 106.848  1.00 69.61           O  
ANISOU 2606  O   ASP A 323     7888   9505   9056   -345   1156   -323       O  
ATOM   2607  CB  ASP A 323     -16.495  16.707 105.020  1.00 73.77           C  
ANISOU 2607  CB  ASP A 323     8698   9758   9573   -657   1332   -737       C  
ATOM   2608  CG  ASP A 323     -15.668  15.397 105.211  1.00 77.63           C  
ANISOU 2608  CG  ASP A 323     9277   9915  10305   -628   1425   -897       C  
ATOM   2609  OD1 ASP A 323     -15.796  14.712 106.259  1.00 78.81           O  
ANISOU 2609  OD1 ASP A 323     9419   9903  10621   -608   1329   -812       O  
ATOM   2610  OD2 ASP A 323     -14.867  15.033 104.312  1.00 82.51           O  
ANISOU 2610  OD2 ASP A 323     9970  10415  10966   -628   1604  -1108       O  
ATOM   2611  N   ALA A 324     -18.925  18.956 105.979  1.00 70.81           N  
ANISOU 2611  N   ALA A 324     8011   9916   8979   -633   1056   -281       N  
ATOM   2612  CA  ALA A 324     -19.279  20.370 106.032  1.00 69.30           C  
ANISOU 2612  CA  ALA A 324     7678   9890   8762   -525   1006   -141       C  
ATOM   2613  C   ALA A 324     -19.603  20.722 107.467  1.00 68.08           C  
ANISOU 2613  C   ALA A 324     7441   9716   8709   -389   1013    -44       C  
ATOM   2614  O   ALA A 324     -19.155  21.728 108.009  1.00 66.59           O  
ANISOU 2614  O   ALA A 324     7220   9507   8575   -220   1028      0       O  
ATOM   2615  CB  ALA A 324     -20.446  20.695 105.103  1.00 69.94           C  
ANISOU 2615  CB  ALA A 324     7671  10186   8717   -687    893    -44       C  
ATOM   2616  N   PHE A 325     -20.387  19.866 108.087  1.00 69.17           N  
ANISOU 2616  N   PHE A 325     7569   9860   8852   -492   1006    -16       N  
ATOM   2617  CA  PHE A 325     -20.750  20.063 109.478  1.00 68.97           C  
ANISOU 2617  CA  PHE A 325     7499   9836   8872   -416   1047     61       C  
ATOM   2618  C   PHE A 325     -19.546  20.101 110.411  1.00 67.45           C  
ANISOU 2618  C   PHE A 325     7436   9452   8741   -300   1071     30       C  
ATOM   2619  O   PHE A 325     -19.576  20.785 111.424  1.00 67.53           O  
ANISOU 2619  O   PHE A 325     7446   9471   8743   -208   1106     79       O  
ATOM   2620  CB  PHE A 325     -21.724  18.999 109.922  1.00 69.89           C  
ANISOU 2620  CB  PHE A 325     7594   9995   8968   -595   1039    108       C  
ATOM   2621  CG  PHE A 325     -22.257  19.232 111.283  1.00 71.25           C  
ANISOU 2621  CG  PHE A 325     7716  10220   9137   -561   1121    187       C  
ATOM   2622  CD1 PHE A 325     -23.200  20.246 111.508  1.00 70.90           C  
ANISOU 2622  CD1 PHE A 325     7478  10353   9107   -475   1201    254       C  
ATOM   2623  CD2 PHE A 325     -21.828  18.440 112.354  1.00 70.95           C  
ANISOU 2623  CD2 PHE A 325     7827  10045   9088   -626   1125    199       C  
ATOM   2624  CE1 PHE A 325     -23.712  20.473 112.785  1.00 71.41           C  
ANISOU 2624  CE1 PHE A 325     7512  10473   9148   -452   1342    288       C  
ATOM   2625  CE2 PHE A 325     -22.334  18.649 113.633  1.00 71.47           C  
ANISOU 2625  CE2 PHE A 325     7887  10182   9086   -644   1221    267       C  
ATOM   2626  CZ  PHE A 325     -23.277  19.683 113.846  1.00 73.42           C  
ANISOU 2626  CZ  PHE A 325     7954  10623   9320   -554   1360    289       C  
ATOM   2627  N   LEU A 326     -18.489  19.384 110.055  1.00 66.66           N  
ANISOU 2627  N   LEU A 326     7444   9170   8714   -312   1051    -50       N  
ATOM   2628  CA  LEU A 326     -17.283  19.347 110.854  1.00 65.87           C  
ANISOU 2628  CA  LEU A 326     7431   8868   8728   -219   1028    -39       C  
ATOM   2629  C   LEU A 326     -16.376  20.522 110.567  1.00 65.44           C  
ANISOU 2629  C   LEU A 326     7351   8805   8710    -64   1035    -44       C  
ATOM   2630  O   LEU A 326     -15.791  21.100 111.512  1.00 65.47           O  
ANISOU 2630  O   LEU A 326     7397   8729   8748     18    990     21       O  
ATOM   2631  CB  LEU A 326     -16.534  18.058 110.585  1.00 67.19           C  
ANISOU 2631  CB  LEU A 326     7674   8810   9045   -277   1010   -111       C  
ATOM   2632  CG  LEU A 326     -17.068  16.813 111.283  1.00 68.63           C  
ANISOU 2632  CG  LEU A 326     7923   8898   9254   -429    950    -63       C  
ATOM   2633  CD1 LEU A 326     -16.259  15.625 110.720  1.00 73.00           C  
ANISOU 2633  CD1 LEU A 326     8538   9185  10015   -451    947   -172       C  
ATOM   2634  CD2 LEU A 326     -16.908  16.980 112.825  1.00 67.35           C  
ANISOU 2634  CD2 LEU A 326     7819   8686   9084   -431    871     89       C  
ATOM   2635  N   GLY A 327     -16.220  20.851 109.274  1.00 64.50           N  
ANISOU 2635  N   GLY A 327     7183   8760   8565    -57   1076   -111       N  
ATOM   2636  CA  GLY A 327     -15.628  22.118 108.851  1.00 63.21           C  
ANISOU 2636  CA  GLY A 327     6974   8642   8400     55   1074    -85       C  
ATOM   2637  C   GLY A 327     -16.302  23.264 109.600  1.00 63.42           C  
ANISOU 2637  C   GLY A 327     6960   8763   8375    138   1037      9       C  
ATOM   2638  O   GLY A 327     -15.636  24.121 110.214  1.00 62.63           O  
ANISOU 2638  O   GLY A 327     6892   8585   8320    244   1002     50       O  
ATOM   2639  N   SER A 328     -17.632  23.235 109.611  1.00 63.77           N  
ANISOU 2639  N   SER A 328     6931   8955   8344     83   1050     37       N  
ATOM   2640  CA  SER A 328     -18.370  24.207 110.344  1.00 64.81           C  
ANISOU 2640  CA  SER A 328     7001   9156   8469    175   1070     93       C  
ATOM   2641  C   SER A 328     -17.983  24.243 111.821  1.00 65.15           C  
ANISOU 2641  C   SER A 328     7170   9082   8504    217   1096     88       C  
ATOM   2642  O   SER A 328     -17.783  25.328 112.378  1.00 65.42           O  
ANISOU 2642  O   SER A 328     7240   9075   8541    327   1103     93       O  
ATOM   2643  CB  SER A 328     -19.842  23.962 110.213  1.00 66.31           C  
ANISOU 2643  CB  SER A 328     7049   9510   8634    101   1101    134       C  
ATOM   2644  OG  SER A 328     -20.497  24.683 111.246  1.00 68.68           O  
ANISOU 2644  OG  SER A 328     7298   9840   8959    201   1190    154       O  
ATOM   2645  N   PHE A 329     -17.835  23.078 112.445  1.00 64.65           N  
ANISOU 2645  N   PHE A 329     7197   8944   8421    105   1091     86       N  
ATOM   2646  CA  PHE A 329     -17.353  23.070 113.816  1.00 65.03           C  
ANISOU 2646  CA  PHE A 329     7402   8879   8429     90   1070    113       C  
ATOM   2647  C   PHE A 329     -15.953  23.656 113.923  1.00 63.77           C  
ANISOU 2647  C   PHE A 329     7327   8556   8346    169    965    132       C  
ATOM   2648  O   PHE A 329     -15.647  24.337 114.868  1.00 64.08           O  
ANISOU 2648  O   PHE A 329     7488   8535   8325    188    935    153       O  
ATOM   2649  CB  PHE A 329     -17.401  21.644 114.442  1.00 66.66           C  
ANISOU 2649  CB  PHE A 329     7694   9014   8621    -77   1032    154       C  
ATOM   2650  CG  PHE A 329     -16.704  21.531 115.793  1.00 66.86           C  
ANISOU 2650  CG  PHE A 329     7909   8899   8596   -146    943    227       C  
ATOM   2651  CD1 PHE A 329     -17.345  21.912 116.955  1.00 69.28           C  
ANISOU 2651  CD1 PHE A 329     8325   9288   8710   -216   1024    239       C  
ATOM   2652  CD2 PHE A 329     -15.399  21.059 115.885  1.00 67.43           C  
ANISOU 2652  CD2 PHE A 329     8046   8756   8818   -156    780    291       C  
ATOM   2653  CE1 PHE A 329     -16.717  21.791 118.204  1.00 71.37           C  
ANISOU 2653  CE1 PHE A 329     8812   9435   8869   -341    916    320       C  
ATOM   2654  CE2 PHE A 329     -14.752  20.959 117.127  1.00 68.60           C  
ANISOU 2654  CE2 PHE A 329     8370   8771   8924   -258    637    406       C  
ATOM   2655  CZ  PHE A 329     -15.409  21.316 118.286  1.00 70.65           C  
ANISOU 2655  CZ  PHE A 329     8788   9125   8928   -372    690    423       C  
ATOM   2656  N   LEU A 330     -15.098  23.400 112.944  1.00 63.25           N  
ANISOU 2656  N   LEU A 330     7200   8421   8410    199    920    122       N  
ATOM   2657  CA  LEU A 330     -13.722  23.854 113.035  1.00 61.92           C  
ANISOU 2657  CA  LEU A 330     7066   8100   8360    259    823    167       C  
ATOM   2658  C   LEU A 330     -13.675  25.372 112.854  1.00 62.13           C  
ANISOU 2658  C   LEU A 330     7081   8180   8347    363    817    173       C  
ATOM   2659  O   LEU A 330     -13.085  26.108 113.680  1.00 62.19           O  
ANISOU 2659  O   LEU A 330     7197   8086   8348    383    728    220       O  
ATOM   2660  CB  LEU A 330     -12.904  23.123 111.989  1.00 61.96           C  
ANISOU 2660  CB  LEU A 330     6980   8031   8533    264    841    132       C  
ATOM   2661  CG  LEU A 330     -11.402  23.006 112.040  1.00 60.29           C  
ANISOU 2661  CG  LEU A 330     6738   7626   8544    304    764    189       C  
ATOM   2662  CD1 LEU A 330     -10.815  22.842 113.468  1.00 58.11           C  
ANISOU 2662  CD1 LEU A 330     6568   7177   8332    256    584    324       C  
ATOM   2663  CD2 LEU A 330     -11.118  21.843 111.146  1.00 59.98           C  
ANISOU 2663  CD2 LEU A 330     6620   7518   8652    288    866     95       C  
ATOM   2664  N   TYR A 331     -14.363  25.857 111.818  1.00 61.77           N  
ANISOU 2664  N   TYR A 331     6919   8281   8270    405    887    139       N  
ATOM   2665  CA  TYR A 331     -14.596  27.294 111.697  1.00 61.48           C  
ANISOU 2665  CA  TYR A 331     6861   8281   8217    503    870    161       C  
ATOM   2666  C   TYR A 331     -15.012  27.901 113.037  1.00 61.62           C  
ANISOU 2666  C   TYR A 331     7004   8245   8165    540    887    140       C  
ATOM   2667  O   TYR A 331     -14.253  28.695 113.593  1.00 62.17           O  
ANISOU 2667  O   TYR A 331     7190   8187   8245    571    804    160       O  
ATOM   2668  CB  TYR A 331     -15.648  27.567 110.639  1.00 62.48           C  
ANISOU 2668  CB  TYR A 331     6840   8577   8322    512    914    164       C  
ATOM   2669  CG  TYR A 331     -16.274  28.955 110.643  1.00 63.75           C  
ANISOU 2669  CG  TYR A 331     6944   8758   8518    625    898    200       C  
ATOM   2670  CD1 TYR A 331     -15.628  30.030 110.068  1.00 61.25           C  
ANISOU 2670  CD1 TYR A 331     6618   8389   8263    678    802    266       C  
ATOM   2671  CD2 TYR A 331     -17.556  29.158 111.213  1.00 65.58           C  
ANISOU 2671  CD2 TYR A 331     7111   9051   8755    678    990    174       C  
ATOM   2672  CE1 TYR A 331     -16.202  31.271 110.060  1.00 65.38           C  
ANISOU 2672  CE1 TYR A 331     7089   8887   8866    787    767    307       C  
ATOM   2673  CE2 TYR A 331     -18.145  30.383 111.202  1.00 66.25           C  
ANISOU 2673  CE2 TYR A 331     7115   9114   8942    808    991    197       C  
ATOM   2674  CZ  TYR A 331     -17.475  31.458 110.635  1.00 67.28           C  
ANISOU 2674  CZ  TYR A 331     7255   9158   9149    869    866    264       C  
ATOM   2675  OH  TYR A 331     -18.088  32.715 110.653  1.00 67.52           O  
ANISOU 2675  OH  TYR A 331     7204   9118   9331   1012    851    293       O  
ATOM   2676  N   GLU A 332     -16.198  27.521 113.536  1.00 60.62           N  
ANISOU 2676  N   GLU A 332     6860   8216   7959    515   1005     94       N  
ATOM   2677  CA  GLU A 332     -16.733  28.025 114.801  1.00 61.51           C  
ANISOU 2677  CA  GLU A 332     7097   8302   7971    531   1098     35       C  
ATOM   2678  C   GLU A 332     -15.758  28.022 115.963  1.00 62.38           C  
ANISOU 2678  C   GLU A 332     7460   8257   7985    447   1006     43       C  
ATOM   2679  O   GLU A 332     -15.752  28.941 116.751  1.00 63.60           O  
ANISOU 2679  O   GLU A 332     7769   8337   8061    475   1034    -16       O  
ATOM   2680  CB  GLU A 332     -17.987  27.241 115.256  1.00 61.61           C  
ANISOU 2680  CB  GLU A 332     7052   8456   7903    458   1258      2       C  
ATOM   2681  CG  GLU A 332     -19.155  27.311 114.323  1.00 58.57           C  
ANISOU 2681  CG  GLU A 332     6408   8230   7616    516   1336     16       C  
ATOM   2682  CD  GLU A 332     -19.534  28.736 113.941  1.00 61.86           C  
ANISOU 2682  CD  GLU A 332     6713   8631   8162    694   1360      5       C  
ATOM   2683  OE1 GLU A 332     -19.094  29.728 114.598  1.00 62.88           O  
ANISOU 2683  OE1 GLU A 332     6985   8622   8284    784   1375    -57       O  
ATOM   2684  OE2 GLU A 332     -20.289  28.861 112.966  1.00 62.26           O  
ANISOU 2684  OE2 GLU A 332     6536   8790   8332    729   1341     71       O  
ATOM   2685  N   TYR A 333     -14.964  26.965 116.077  1.00 62.80           N  
ANISOU 2685  N   TYR A 333     7559   8245   8056    330    886    121       N  
ATOM   2686  CA  TYR A 333     -14.066  26.800 117.194  1.00 63.70           C  
ANISOU 2686  CA  TYR A 333     7894   8210   8098    207    741    185       C  
ATOM   2687  C   TYR A 333     -12.854  27.668 116.998  1.00 63.43           C  
ANISOU 2687  C   TYR A 333     7894   8035   8173    258    574    243       C  
ATOM   2688  O   TYR A 333     -12.415  28.324 117.917  1.00 64.15           O  
ANISOU 2688  O   TYR A 333     8195   8019   8160    194    478    255       O  
ATOM   2689  CB  TYR A 333     -13.656  25.322 117.360  1.00 64.31           C  
ANISOU 2689  CB  TYR A 333     7968   8233   8235     72    640    286       C  
ATOM   2690  CG  TYR A 333     -13.411  24.984 118.781  1.00 64.60           C  
ANISOU 2690  CG  TYR A 333     8251   8185   8108   -118    529    364       C  
ATOM   2691  CD1 TYR A 333     -12.309  25.479 119.438  1.00 67.03           C  
ANISOU 2691  CD1 TYR A 333     8722   8333   8414   -188    316    459       C  
ATOM   2692  CD2 TYR A 333     -14.343  24.235 119.508  1.00 68.88           C  
ANISOU 2692  CD2 TYR A 333     8880   8823   8468   -264    630    358       C  
ATOM   2693  CE1 TYR A 333     -12.102  25.204 120.805  1.00 69.80           C  
ANISOU 2693  CE1 TYR A 333     9348   8613   8561   -421    177    553       C  
ATOM   2694  CE2 TYR A 333     -14.159  23.948 120.859  1.00 68.18           C  
ANISOU 2694  CE2 TYR A 333     9059   8678   8168   -492    525    445       C  
ATOM   2695  CZ  TYR A 333     -13.039  24.447 121.497  1.00 70.71           C  
ANISOU 2695  CZ  TYR A 333     9568   8835   8465   -575    290    541       C  
ATOM   2696  OH  TYR A 333     -12.829  24.198 122.825  1.00 76.14           O  
ANISOU 2696  OH  TYR A 333    10555   9468   8907   -847    146    649       O  
ATOM   2697  N   SER A 334     -12.327  27.681 115.777  1.00 63.45           N  
ANISOU 2697  N   SER A 334     7700   8044   8365    348    545    279       N  
ATOM   2698  CA  SER A 334     -11.043  28.335 115.479  1.00 62.66           C  
ANISOU 2698  CA  SER A 334     7581   7819   8408    372    386    369       C  
ATOM   2699  C   SER A 334     -11.120  29.837 115.548  1.00 64.09           C  
ANISOU 2699  C   SER A 334     7842   7970   8537    442    367    335       C  
ATOM   2700  O   SER A 334     -10.109  30.525 115.863  1.00 65.93           O  
ANISOU 2700  O   SER A 334     8165   8064   8823    404    192    418       O  
ATOM   2701  CB  SER A 334     -10.603  27.967 114.094  1.00 61.98           C  
ANISOU 2701  CB  SER A 334     7265   7783   8501    433    429    389       C  
ATOM   2702  OG  SER A 334     -10.482  26.574 113.968  1.00 62.46           O  
ANISOU 2702  OG  SER A 334     7257   7827   8649    383    459    393       O  
ATOM   2703  N   ARG A 335     -12.300  30.378 115.252  1.00 63.68           N  
ANISOU 2703  N   ARG A 335     7750   8027   8421    540    525    229       N  
ATOM   2704  CA  ARG A 335     -12.405  31.812 115.195  1.00 63.85           C  
ANISOU 2704  CA  ARG A 335     7821   7980   8458    633    506    198       C  
ATOM   2705  C   ARG A 335     -12.488  32.378 116.624  1.00 65.99           C  
ANISOU 2705  C   ARG A 335     8384   8121   8567    578    502    109       C  
ATOM   2706  O   ARG A 335     -12.109  33.523 116.836  1.00 67.03           O  
ANISOU 2706  O   ARG A 335     8643   8111   8715    604    414     94       O  
ATOM   2707  CB  ARG A 335     -13.575  32.246 114.303  1.00 64.09           C  
ANISOU 2707  CB  ARG A 335     7667   8137   8548    765    644    150       C  
ATOM   2708  CG  ARG A 335     -15.005  32.018 114.852  1.00 63.63           C  
ANISOU 2708  CG  ARG A 335     7594   8172   8411    809    852     29       C  
ATOM   2709  CD  ARG A 335     -16.051  31.884 113.732  1.00 62.89           C  
ANISOU 2709  CD  ARG A 335     7230   8245   8421    884    932     58       C  
ATOM   2710  NE  ARG A 335     -16.324  33.144 113.010  1.00 65.40           N  
ANISOU 2710  NE  ARG A 335     7437   8517   8894   1014    878    103       N  
ATOM   2711  CZ  ARG A 335     -17.494  33.798 113.038  1.00 66.25           C  
ANISOU 2711  CZ  ARG A 335     7422   8631   9120   1146    986     62       C  
ATOM   2712  NH1 ARG A 335     -18.524  33.306 113.742  1.00 62.13           N  
ANISOU 2712  NH1 ARG A 335     6858   8188   8559   1163   1191    -38       N  
ATOM   2713  NH2 ARG A 335     -17.627  34.939 112.357  1.00 63.93           N  
ANISOU 2713  NH2 ARG A 335     7027   8255   9010   1256    886    139       N  
ATOM   2714  N   ARG A 336     -12.949  31.570 117.587  1.00 66.31           N  
ANISOU 2714  N   ARG A 336     8555   8205   8435    472    590     52       N  
ATOM   2715  CA  ARG A 336     -13.093  32.003 119.009  1.00 68.64           C  
ANISOU 2715  CA  ARG A 336     9179   8404   8496    365    624    -54       C  
ATOM   2716  C   ARG A 336     -11.855  31.766 119.860  1.00 69.22           C  
ANISOU 2716  C   ARG A 336     9491   8336   8474    150    356     69       C  
ATOM   2717  O   ARG A 336     -11.784  32.265 120.975  1.00 71.19           O  
ANISOU 2717  O   ARG A 336    10064   8485   8500     17    330     -6       O  
ATOM   2718  CB  ARG A 336     -14.270  31.315 119.709  1.00 68.90           C  
ANISOU 2718  CB  ARG A 336     9259   8575   8344    311    871   -167       C  
ATOM   2719  CG  ARG A 336     -15.564  31.413 118.928  1.00 70.00           C  
ANISOU 2719  CG  ARG A 336     9119   8865   8611    499   1116   -252       C  
ATOM   2720  CD  ARG A 336     -16.706  30.781 119.671  1.00 70.34           C  
ANISOU 2720  CD  ARG A 336     9186   9051   8490    431   1373   -349       C  
ATOM   2721  NE  ARG A 336     -17.744  30.463 118.711  1.00 72.91           N  
ANISOU 2721  NE  ARG A 336     9169   9541   8993    561   1510   -334       N  
ATOM   2722  CZ  ARG A 336     -18.953  31.000 118.718  1.00 76.95           C  
ANISOU 2722  CZ  ARG A 336     9534  10123   9580    698   1763   -448       C  
ATOM   2723  NH1 ARG A 336     -19.309  31.867 119.655  1.00 80.14           N  
ANISOU 2723  NH1 ARG A 336    10115  10440   9894    742   1964   -627       N  
ATOM   2724  NH2 ARG A 336     -19.826  30.638 117.804  1.00 80.42           N  
ANISOU 2724  NH2 ARG A 336     9647  10712  10196    778   1820   -383       N  
ATOM   2725  N   HIS A 337     -10.911  30.988 119.333  1.00 70.81           N  
ANISOU 2725  N   HIS A 337     9140   8391   9373    838   1206  -1585       N  
ATOM   2726  CA  HIS A 337      -9.708  30.629 120.057  1.00 71.37           C  
ANISOU 2726  CA  HIS A 337     9519   8628   8971    551    901  -1681       C  
ATOM   2727  C   HIS A 337      -8.460  30.775 119.211  1.00 69.17           C  
ANISOU 2727  C   HIS A 337     9098   8430   8753    588    503  -1564       C  
ATOM   2728  O   HIS A 337      -7.816  29.812 118.949  1.00 65.82           O  
ANISOU 2728  O   HIS A 337     8587   8208   8214    587    133  -1403       O  
ATOM   2729  CB  HIS A 337      -9.772  29.202 120.572  1.00 70.41           C  
ANISOU 2729  CB  HIS A 337     9484   8746   8521    451    675  -1557       C  
ATOM   2730  CG  HIS A 337     -10.798  28.992 121.623  1.00 75.06           C  
ANISOU 2730  CG  HIS A 337    10305   9291   8923    304   1059  -1700       C  
ATOM   2731  ND1 HIS A 337     -10.738  29.607 122.849  1.00 82.11           N  
ANISOU 2731  ND1 HIS A 337    11624  10097   9476    -41   1343  -1996       N  
ATOM   2732  CD2 HIS A 337     -11.916  28.231 121.636  1.00 78.15           C  
ANISOU 2732  CD2 HIS A 337    10576   9714   9404    406   1241  -1609       C  
ATOM   2733  CE1 HIS A 337     -11.782  29.240 123.572  1.00 87.23           C  
ANISOU 2733  CE1 HIS A 337    12415  10717  10012   -138   1725  -2092       C  
ATOM   2734  NE2 HIS A 337     -12.507  28.395 122.864  1.00 82.97           N  
ANISOU 2734  NE2 HIS A 337    11527  10248   9749    144   1658  -1847       N  
ATOM   2735  N   PRO A 338      -8.092  32.017 118.846  1.00 71.61           N  
ANISOU 2735  N   PRO A 338     9392   8541   9274    601    627  -1664       N  
ATOM   2736  CA  PRO A 338      -6.862  32.332 118.083  1.00 70.23           C  
ANISOU 2736  CA  PRO A 338     9100   8415   9167    590    318  -1591       C  
ATOM   2737  C   PRO A 338      -5.620  32.236 118.930  1.00 72.64           C  
ANISOU 2737  C   PRO A 338     9630   8847   9122    271     40  -1707       C  
ATOM   2738  O   PRO A 338      -4.530  32.529 118.454  1.00 73.23           O  
ANISOU 2738  O   PRO A 338     9600   8956   9270    219   -193  -1674       O  
ATOM   2739  CB  PRO A 338      -7.061  33.802 117.725  1.00 71.33           C  
ANISOU 2739  CB  PRO A 338     9229   8242   9633    649    634  -1688       C  
ATOM   2740  CG  PRO A 338      -7.874  34.350 118.828  1.00 73.88           C  
ANISOU 2740  CG  PRO A 338     9811   8340   9919    538   1091  -1953       C  
ATOM   2741  CD  PRO A 338      -8.801  33.248 119.264  1.00 74.17           C  
ANISOU 2741  CD  PRO A 338     9836   8531   9812    591   1139  -1886       C  
ATOM   2742  N   GLU A 339      -5.816  31.950 120.217  1.00 75.97           N  
ANISOU 2742  N   GLU A 339    10371   9328   9166     11     90  -1843       N  
ATOM   2743  CA  GLU A 339      -4.739  31.601 121.127  1.00 77.64           C  
ANISOU 2743  CA  GLU A 339    10789   9734   8978   -347   -288  -1849       C  
ATOM   2744  C   GLU A 339      -4.167  30.222 120.753  1.00 74.52           C  
ANISOU 2744  C   GLU A 339    10127   9566   8621   -219   -753  -1520       C  
ATOM   2745  O   GLU A 339      -2.965  30.034 120.848  1.00 74.74           O  
ANISOU 2745  O   GLU A 339    10066   9713   8618   -362  -1152  -1408       O  
ATOM   2746  CB  GLU A 339      -5.232  31.543 122.583  1.00 81.24           C  
ANISOU 2746  CB  GLU A 339    11700  10224   8944   -715   -114  -2036       C  
ATOM   2747  CG  GLU A 339      -6.189  32.643 123.001  1.00 86.31           C  
ANISOU 2747  CG  GLU A 339    12599  10572   9620   -791    532  -2398       C  
ATOM   2748  CD  GLU A 339      -7.666  32.234 122.915  1.00 87.29           C  
ANISOU 2748  CD  GLU A 339    12635  10592   9939   -527    949  -2382       C  
ATOM   2749  OE1 GLU A 339      -7.991  31.429 122.041  1.00 78.63           O  
ANISOU 2749  OE1 GLU A 339    11179   9589   9107   -181    771  -2095       O  
ATOM   2750  OE2 GLU A 339      -8.493  32.734 123.728  1.00 91.54           O  
ANISOU 2750  OE2 GLU A 339    13463  10945  10375   -701   1487  -2680       O  
ATOM   2751  N   TYR A 340      -5.027  29.278 120.363  1.00 71.02           N  
ANISOU 2751  N   TYR A 340     9541   9154   8289     29   -676  -1372       N  
ATOM   2752  CA  TYR A 340      -4.639  27.863 120.313  1.00 70.14           C  
ANISOU 2752  CA  TYR A 340     9271   9197   8180     92  -1031  -1099       C  
ATOM   2753  C   TYR A 340      -3.703  27.569 119.139  1.00 68.31           C  
ANISOU 2753  C   TYR A 340     8656   8971   8325    289  -1247   -963       C  
ATOM   2754  O   TYR A 340      -3.679  28.289 118.118  1.00 65.84           O  
ANISOU 2754  O   TYR A 340     8186   8572   8257    431  -1083  -1045       O  
ATOM   2755  CB  TYR A 340      -5.868  26.957 120.159  1.00 68.21           C  
ANISOU 2755  CB  TYR A 340     8993   8956   7969    271   -835  -1018       C  
ATOM   2756  CG  TYR A 340      -6.837  26.900 121.337  1.00 73.46           C  
ANISOU 2756  CG  TYR A 340    10005   9626   8282     74   -591  -1119       C  
ATOM   2757  CD1 TYR A 340      -6.792  27.826 122.412  1.00 79.87           C  
ANISOU 2757  CD1 TYR A 340    11194  10404   8747   -260   -428  -1356       C  
ATOM   2758  CD2 TYR A 340      -7.804  25.936 121.370  1.00 72.82           C  
ANISOU 2758  CD2 TYR A 340     9896   9570   8200    172   -471  -1015       C  
ATOM   2759  CE1 TYR A 340      -7.706  27.754 123.478  1.00 81.51           C  
ANISOU 2759  CE1 TYR A 340    11753  10606   8611   -490   -112  -1495       C  
ATOM   2760  CE2 TYR A 340      -8.713  25.858 122.407  1.00 77.75           C  
ANISOU 2760  CE2 TYR A 340    10826  10194   8521    -24   -190  -1117       C  
ATOM   2761  CZ  TYR A 340      -8.678  26.762 123.448  1.00 82.32           C  
ANISOU 2761  CZ  TYR A 340    11784  10738   8755   -352     13  -1364       C  
ATOM   2762  OH  TYR A 340      -9.642  26.606 124.438  1.00 85.71           O  
ANISOU 2762  OH  TYR A 340    12530  11158   8878   -575    378  -1495       O  
ATOM   2763  N   ALA A 341      -2.953  26.487 119.252  1.00 68.59           N  
ANISOU 2763  N   ALA A 341     8535   9085   8441    291  -1584   -739       N  
ATOM   2764  CA  ALA A 341      -2.220  26.031 118.093  1.00 67.44           C  
ANISOU 2764  CA  ALA A 341     8015   8898   8711    491  -1658   -651       C  
ATOM   2765  C   ALA A 341      -3.185  25.262 117.202  1.00 64.84           C  
ANISOU 2765  C   ALA A 341     7586   8529   8520    717  -1418   -638       C  
ATOM   2766  O   ALA A 341      -4.109  24.632 117.689  1.00 64.52           O  
ANISOU 2766  O   ALA A 341     7688   8510   8318    724  -1348   -588       O  
ATOM   2767  CB  ALA A 341      -0.969  25.152 118.497  1.00 69.28           C  
ANISOU 2767  CB  ALA A 341     8030   9157   9134    435  -2074   -397       C  
ATOM   2768  N   VAL A 342      -2.969  25.350 115.893  1.00 63.92           N  
ANISOU 2768  N   VAL A 342     7249   8370   8668    845  -1285   -693       N  
ATOM   2769  CA  VAL A 342      -3.727  24.559 114.929  1.00 63.11           C  
ANISOU 2769  CA  VAL A 342     7050   8259   8668    972  -1097   -685       C  
ATOM   2770  C   VAL A 342      -3.764  23.054 115.308  1.00 64.38           C  
ANISOU 2770  C   VAL A 342     7168   8381   8911   1012  -1189   -550       C  
ATOM   2771  O   VAL A 342      -4.857  22.479 115.561  1.00 63.88           O  
ANISOU 2771  O   VAL A 342     7225   8342   8704   1025  -1093   -517       O  
ATOM   2772  CB  VAL A 342      -3.142  24.705 113.523  1.00 62.52           C  
ANISOU 2772  CB  VAL A 342     6773   8157   8824   1000   -979   -760       C  
ATOM   2773  CG1 VAL A 342      -3.901  23.808 112.602  1.00 61.91           C  
ANISOU 2773  CG1 VAL A 342     6654   8096   8773   1030   -805   -771       C  
ATOM   2774  CG2 VAL A 342      -3.240  26.138 113.037  1.00 62.12           C  
ANISOU 2774  CG2 VAL A 342     6773   8122   8706    959   -881   -836       C  
ATOM   2775  N   SER A 343      -2.570  22.447 115.391  1.00 65.36           N  
ANISOU 2775  N   SER A 343     7094   8419   9319   1030  -1368   -447       N  
ATOM   2776  CA  SER A 343      -2.425  21.067 115.695  1.00 66.58           C  
ANISOU 2776  CA  SER A 343     7157   8461   9680   1090  -1454   -276       C  
ATOM   2777  C   SER A 343      -3.424  20.744 116.760  1.00 67.74           C  
ANISOU 2777  C   SER A 343     7578   8677   9482   1021  -1521   -166       C  
ATOM   2778  O   SER A 343      -4.087  19.705 116.700  1.00 68.71           O  
ANISOU 2778  O   SER A 343     7729   8732   9648   1066  -1418   -107       O  
ATOM   2779  CB  SER A 343      -1.029  20.828 116.211  1.00 70.74           C  
ANISOU 2779  CB  SER A 343     7450   8903  10525   1089  -1761    -77       C  
ATOM   2780  OG  SER A 343      -0.099  21.666 115.528  1.00 70.69           O  
ANISOU 2780  OG  SER A 343     7246   8897  10718   1080  -1720   -209       O  
ATOM   2781  N   VAL A 344      -3.582  21.657 117.718  1.00 68.17           N  
ANISOU 2781  N   VAL A 344     7865   8857   9179    873  -1636   -174       N  
ATOM   2782  CA  VAL A 344      -4.536  21.476 118.797  1.00 68.54           C  
ANISOU 2782  CA  VAL A 344     8221   8976   8847    745  -1626   -116       C  
ATOM   2783  C   VAL A 344      -5.993  21.542 118.278  1.00 67.06           C  
ANISOU 2783  C   VAL A 344     8109   8807   8566    819  -1258   -278       C  
ATOM   2784  O   VAL A 344      -6.832  20.718 118.691  1.00 67.89           O  
ANISOU 2784  O   VAL A 344     8323   8907   8564    793  -1180   -199       O  
ATOM   2785  CB  VAL A 344      -4.298  22.503 119.893  1.00 70.49           C  
ANISOU 2785  CB  VAL A 344     8731   9333   8719    500  -1759   -159       C  
ATOM   2786  CG1 VAL A 344      -5.240  22.299 121.086  1.00 73.23           C  
ANISOU 2786  CG1 VAL A 344     9448   9751   8623    294  -1686   -131       C  
ATOM   2787  CG2 VAL A 344      -2.896  22.416 120.364  1.00 73.73           C  
ANISOU 2787  CG2 VAL A 344     9021   9764   9229    384  -2189     49       C  
ATOM   2788  N   LEU A 345      -6.312  22.487 117.384  1.00 64.49           N  
ANISOU 2788  N   LEU A 345     7701   8498   8305    894  -1055   -459       N  
ATOM   2789  CA  LEU A 345      -7.724  22.639 116.996  1.00 63.42           C  
ANISOU 2789  CA  LEU A 345     7584   8393   8120    943   -773   -535       C  
ATOM   2790  C   LEU A 345      -8.082  21.434 116.154  1.00 63.33           C  
ANISOU 2790  C   LEU A 345     7421   8367   8273   1004   -730   -477       C  
ATOM   2791  O   LEU A 345      -9.110  20.821 116.379  1.00 64.09           O  
ANISOU 2791  O   LEU A 345     7570   8484   8298    979   -612   -442       O  
ATOM   2792  CB  LEU A 345      -8.031  23.939 116.251  1.00 61.19           C  
ANISOU 2792  CB  LEU A 345     7223   8113   7915   1001   -614   -650       C  
ATOM   2793  CG  LEU A 345      -7.830  25.289 116.939  1.00 62.13           C  
ANISOU 2793  CG  LEU A 345     7498   8181   7928    934   -547   -768       C  
ATOM   2794  CD1 LEU A 345      -7.655  26.369 115.901  1.00 60.18           C  
ANISOU 2794  CD1 LEU A 345     7104   7886   7877   1014   -477   -809       C  
ATOM   2795  CD2 LEU A 345      -8.968  25.731 117.945  1.00 64.88           C  
ANISOU 2795  CD2 LEU A 345     8049   8484   8117    869   -266   -860       C  
ATOM   2796  N   LEU A 346      -7.224  21.062 115.201  1.00 62.86           N  
ANISOU 2796  N   LEU A 346     7186   8256   8442   1047   -784   -494       N  
ATOM   2797  CA  LEU A 346      -7.494  19.868 114.446  1.00 63.08           C  
ANISOU 2797  CA  LEU A 346     7122   8230   8615   1044   -687   -497       C  
ATOM   2798  C   LEU A 346      -7.605  18.645 115.288  1.00 65.02           C  
ANISOU 2798  C   LEU A 346     7444   8371   8890   1034   -744   -362       C  
ATOM   2799  O   LEU A 346      -8.221  17.679 114.863  1.00 67.16           O  
ANISOU 2799  O   LEU A 346     7700   8592   9225    998   -610   -377       O  
ATOM   2800  CB  LEU A 346      -6.439  19.612 113.420  1.00 64.07           C  
ANISOU 2800  CB  LEU A 346     7079   8264   9002   1056   -652   -584       C  
ATOM   2801  CG  LEU A 346      -6.040  20.804 112.584  1.00 65.38           C  
ANISOU 2801  CG  LEU A 346     7180   8514   9148   1035   -617   -688       C  
ATOM   2802  CD1 LEU A 346      -4.839  20.317 111.774  1.00 67.83           C  
ANISOU 2802  CD1 LEU A 346     7327   8690   9755   1023   -531   -787       C  
ATOM   2803  CD2 LEU A 346      -7.207  21.276 111.713  1.00 65.80           C  
ANISOU 2803  CD2 LEU A 346     7259   8722   9021    950   -499   -717       C  
ATOM   2804  N   ARG A 347      -6.991  18.647 116.462  1.00 66.37           N  
ANISOU 2804  N   ARG A 347     7708   8506   9004   1025   -960   -208       N  
ATOM   2805  CA  ARG A 347      -7.126  17.540 117.386  1.00 67.85           C  
ANISOU 2805  CA  ARG A 347     8002   8599   9179    983  -1062      3       C  
ATOM   2806  C   ARG A 347      -8.443  17.619 118.153  1.00 68.34           C  
ANISOU 2806  C   ARG A 347     8303   8777   8886    868   -933      3       C  
ATOM   2807  O   ARG A 347      -9.002  16.621 118.584  1.00 70.69           O  
ANISOU 2807  O   ARG A 347     8694   9010   9156    811   -892    125       O  
ATOM   2808  CB  ARG A 347      -5.981  17.626 118.371  1.00 70.64           C  
ANISOU 2808  CB  ARG A 347     8373   8922   9546    945  -1409    227       C  
ATOM   2809  CG  ARG A 347      -5.412  16.338 118.837  1.00 70.56           C  
ANISOU 2809  CG  ARG A 347     8284   8712   9814    973  -1607    536       C  
ATOM   2810  CD  ARG A 347      -4.409  16.683 119.937  1.00 74.57           C  
ANISOU 2810  CD  ARG A 347     8825   9282  10227    859  -2043    817       C  
ATOM   2811  NE  ARG A 347      -3.048  16.796 119.444  1.00 76.77           N  
ANISOU 2811  NE  ARG A 347     8748   9447  10972    982  -2216    881       N  
ATOM   2812  CZ  ARG A 347      -2.084  17.528 120.013  1.00 80.00           C  
ANISOU 2812  CZ  ARG A 347     9102   9969  11325    872  -2565   1012       C  
ATOM   2813  NH1 ARG A 347      -2.348  18.256 121.093  1.00 79.57           N  
ANISOU 2813  NH1 ARG A 347     9387  10148  10697    599  -2759   1050       N  
ATOM   2814  NH2 ARG A 347      -0.847  17.545 119.497  1.00 78.91           N  
ANISOU 2814  NH2 ARG A 347     8567   9705  11710    996  -2690   1080       N  
ATOM   2815  N   LEU A 348      -8.895  18.834 118.394  1.00 67.46           N  
ANISOU 2815  N   LEU A 348     8291   8803   8539    826   -837   -133       N  
ATOM   2816  CA  LEU A 348     -10.206  19.057 118.980  1.00 67.32           C  
ANISOU 2816  CA  LEU A 348     8435   8862   8280    734   -601   -191       C  
ATOM   2817  C   LEU A 348     -11.354  18.562 118.065  1.00 65.35           C  
ANISOU 2817  C   LEU A 348     8018   8630   8184    783   -377   -246       C  
ATOM   2818  O   LEU A 348     -12.267  17.956 118.549  1.00 66.67           O  
ANISOU 2818  O   LEU A 348     8268   8802   8260    697   -239   -201       O  
ATOM   2819  CB  LEU A 348     -10.394  20.541 119.328  1.00 66.70           C  
ANISOU 2819  CB  LEU A 348     8451   8847   8043    702   -469   -357       C  
ATOM   2820  CG  LEU A 348      -9.652  21.170 120.500  1.00 70.62           C  
ANISOU 2820  CG  LEU A 348     9221   9369   8244    521   -606   -364       C  
ATOM   2821  CD1 LEU A 348     -10.178  22.577 120.580  1.00 73.50           C  
ANISOU 2821  CD1 LEU A 348     9647   9723   8555    508   -311   -603       C  
ATOM   2822  CD2 LEU A 348      -9.825  20.465 121.891  1.00 74.46           C  
ANISOU 2822  CD2 LEU A 348    10039   9892   8361    265   -670   -221       C  
ATOM   2823  N   ALA A 349     -11.277  18.819 116.767  1.00 62.81           N  
ANISOU 2823  N   ALA A 349     7474   8333   8058    868   -361   -329       N  
ATOM   2824  CA  ALA A 349     -12.307  18.454 115.830  1.00 62.41           C  
ANISOU 2824  CA  ALA A 349     7264   8349   8100    835   -222   -359       C  
ATOM   2825  C   ALA A 349     -12.338  16.960 115.579  1.00 63.78           C  
ANISOU 2825  C   ALA A 349     7446   8429   8360    754   -214   -325       C  
ATOM   2826  O   ALA A 349     -13.397  16.387 115.582  1.00 64.40           O  
ANISOU 2826  O   ALA A 349     7509   8546   8415    655    -90   -307       O  
ATOM   2827  CB  ALA A 349     -12.070  19.174 114.548  1.00 61.56           C  
ANISOU 2827  CB  ALA A 349     6980   8316   8096    867   -255   -425       C  
ATOM   2828  N   LYS A 350     -11.176  16.349 115.302  1.00 64.36           N  
ANISOU 2828  N   LYS A 350     7511   8349   8595    793   -314   -324       N  
ATOM   2829  CA  LYS A 350     -11.016  14.877 115.238  1.00 65.81           C  
ANISOU 2829  CA  LYS A 350     7715   8329   8959    742   -266   -283       C  
ATOM   2830  C   LYS A 350     -11.705  14.111 116.385  1.00 67.24           C  
ANISOU 2830  C   LYS A 350     8062   8453   9032    673   -247   -115       C  
ATOM   2831  O   LYS A 350     -12.319  13.063 116.188  1.00 68.84           O  
ANISOU 2831  O   LYS A 350     8282   8561   9313    567   -113   -116       O  
ATOM   2832  CB  LYS A 350      -9.537  14.550 115.290  1.00 66.21           C  
ANISOU 2832  CB  LYS A 350     7707   8165   9284    858   -391   -223       C  
ATOM   2833  CG  LYS A 350      -9.180  13.103 115.088  1.00 68.71           C  
ANISOU 2833  CG  LYS A 350     7987   8174   9944    853   -291   -186       C  
ATOM   2834  CD  LYS A 350      -8.985  12.706 113.608  1.00 68.90           C  
ANISOU 2834  CD  LYS A 350     7899   8099  10179    772    -28   -468       C  
ATOM   2835  CE  LYS A 350      -8.674  11.167 113.462  1.00 66.96           C  
ANISOU 2835  CE  LYS A 350     7636   7450  10356    755    176   -475       C  
ATOM   2836  NZ  LYS A 350      -7.186  10.902 113.577  1.00 67.96           N  
ANISOU 2836  NZ  LYS A 350     7569   7258  10994    958    137   -375       N  
ATOM   2837  N   GLU A 351     -11.611  14.665 117.582  1.00 67.62           N  
ANISOU 2837  N   GLU A 351     8264   8563   8865    682   -362     14       N  
ATOM   2838  CA  GLU A 351     -12.136  14.029 118.786  1.00 69.67           C  
ANISOU 2838  CA  GLU A 351     8742   8785   8943    561   -350    195       C  
ATOM   2839  C   GLU A 351     -13.635  14.228 118.762  1.00 69.19           C  
ANISOU 2839  C   GLU A 351     8679   8872   8737    456    -79     81       C  
ATOM   2840  O   GLU A 351     -14.420  13.326 119.149  1.00 71.58           O  
ANISOU 2840  O   GLU A 351     9068   9123   9005    325     52    158       O  
ATOM   2841  CB  GLU A 351     -11.490  14.669 120.011  1.00 70.88           C  
ANISOU 2841  CB  GLU A 351     9102   8996   8833    515   -556    336       C  
ATOM   2842  CG  GLU A 351     -12.100  14.317 121.374  1.00 77.01           C  
ANISOU 2842  CG  GLU A 351    10193   9807   9261    297   -518    501       C  
ATOM   2843  CD  GLU A 351     -11.426  13.135 122.099  1.00 82.59           C  
ANISOU 2843  CD  GLU A 351    11028  10333  10018    223   -788    874       C  
ATOM   2844  OE1 GLU A 351     -10.408  12.592 121.600  1.00 84.45           O  
ANISOU 2844  OE1 GLU A 351    11064  10376  10645    381  -1000   1011       O  
ATOM   2845  OE2 GLU A 351     -11.940  12.728 123.169  1.00 85.95           O  
ANISOU 2845  OE2 GLU A 351    11744  10787  10128     -3   -764   1049       O  
ATOM   2846  N   TYR A 352     -14.020  15.402 118.255  1.00 66.42           N  
ANISOU 2846  N   TYR A 352     8189   8682   8364    517      5    -77       N  
ATOM   2847  CA  TYR A 352     -15.395  15.776 118.100  1.00 65.32           C  
ANISOU 2847  CA  TYR A 352     7927   8672   8218    462    243   -151       C  
ATOM   2848  C   TYR A 352     -16.055  14.835 117.068  1.00 64.60           C  
ANISOU 2848  C   TYR A 352     7655   8593   8296    367    290   -168       C  
ATOM   2849  O   TYR A 352     -17.111  14.270 117.325  1.00 65.63           O  
ANISOU 2849  O   TYR A 352     7765   8749   8424    233    455   -138       O  
ATOM   2850  CB  TYR A 352     -15.548  17.277 117.779  1.00 63.26           C  
ANISOU 2850  CB  TYR A 352     7520   8518   7998    577    295   -250       C  
ATOM   2851  CG  TYR A 352     -16.993  17.622 117.610  1.00 66.05           C  
ANISOU 2851  CG  TYR A 352     7654   8963   8479    548    535   -261       C  
ATOM   2852  CD1 TYR A 352     -17.571  17.704 116.363  1.00 66.86           C  
ANISOU 2852  CD1 TYR A 352     7442   9177   8787    547    475   -227       C  
ATOM   2853  CD2 TYR A 352     -17.829  17.765 118.714  1.00 70.69           C  
ANISOU 2853  CD2 TYR A 352     8339   9529   8990    476    828   -283       C  
ATOM   2854  CE1 TYR A 352     -18.934  17.959 116.229  1.00 67.59           C  
ANISOU 2854  CE1 TYR A 352     7252   9356   9074    512    645   -164       C  
ATOM   2855  CE2 TYR A 352     -19.182  18.030 118.574  1.00 69.73           C  
ANISOU 2855  CE2 TYR A 352     7936   9459   9098    464   1086   -276       C  
ATOM   2856  CZ  TYR A 352     -19.720  18.127 117.336  1.00 68.31           C  
ANISOU 2856  CZ  TYR A 352     7379   9389   9188    500    963   -190       C  
ATOM   2857  OH  TYR A 352     -21.061  18.387 117.200  1.00 71.53           O  
ANISOU 2857  OH  TYR A 352     7429   9851   9896    487   1164   -116       O  
ATOM   2858  N   GLU A 353     -15.391  14.596 115.944  1.00 63.53           N  
ANISOU 2858  N   GLU A 353     7422   8428   8289    384    170   -235       N  
ATOM   2859  CA  GLU A 353     -15.833  13.557 115.015  1.00 63.90           C  
ANISOU 2859  CA  GLU A 353     7390   8453   8435    205    231   -298       C  
ATOM   2860  C   GLU A 353     -16.023  12.217 115.684  1.00 65.64           C  
ANISOU 2860  C   GLU A 353     7772   8477   8692    100    328   -227       C  
ATOM   2861  O   GLU A 353     -17.049  11.560 115.490  1.00 67.29           O  
ANISOU 2861  O   GLU A 353     7932   8724   8910    -95    457   -244       O  
ATOM   2862  CB  GLU A 353     -14.830  13.360 113.905  1.00 63.65           C  
ANISOU 2862  CB  GLU A 353     7330   8343   8510    198    167   -427       C  
ATOM   2863  CG  GLU A 353     -15.309  12.452 112.775  1.00 64.89           C  
ANISOU 2863  CG  GLU A 353     7447   8507   8702    -77    273   -570       C  
ATOM   2864  CD  GLU A 353     -14.349  12.500 111.599  1.00 71.37           C  
ANISOU 2864  CD  GLU A 353     8263   9282   9572   -136    287   -755       C  
ATOM   2865  OE1 GLU A 353     -13.117  12.576 111.874  1.00 71.01           O  
ANISOU 2865  OE1 GLU A 353     8258   9038   9684     68    271   -762       O  
ATOM   2866  OE2 GLU A 353     -14.804  12.456 110.412  1.00 74.28           O  
ANISOU 2866  OE2 GLU A 353     8588   9820   9816   -422    314   -884       O  
ATOM   2867  N   ALA A 354     -15.036  11.797 116.467  1.00 65.11           N  
ANISOU 2867  N   ALA A 354     7879   8192   8668    207    242   -110       N  
ATOM   2868  CA  ALA A 354     -15.109  10.461 117.012  1.00 66.74           C  
ANISOU 2868  CA  ALA A 354     8233   8155   8972    112    311     17       C  
ATOM   2869  C   ALA A 354     -16.386  10.302 117.881  1.00 66.86           C  
ANISOU 2869  C   ALA A 354     8339   8277   8787    -47    461    104       C  
ATOM   2870  O   ALA A 354     -16.978   9.223 118.003  1.00 68.37           O  
ANISOU 2870  O   ALA A 354     8596   8337   9043   -215    598    150       O  
ATOM   2871  CB  ALA A 354     -13.822  10.129 117.778  1.00 67.39           C  
ANISOU 2871  CB  ALA A 354     8438   7994   9174    258    118    235       C  
ATOM   2872  N   THR A 355     -16.814  11.417 118.434  1.00 65.26           N  
ANISOU 2872  N   THR A 355     8130   8291   8376     -7    487     97       N  
ATOM   2873  CA  THR A 355     -17.894  11.439 119.403  1.00 66.53           C  
ANISOU 2873  CA  THR A 355     8385   8534   8358   -149    699    153       C  
ATOM   2874  C   THR A 355     -19.267  11.300 118.698  1.00 66.19           C  
ANISOU 2874  C   THR A 355     8073   8629   8446   -287    900     48       C  
ATOM   2875  O   THR A 355     -20.129  10.565 119.154  1.00 67.04           O  
ANISOU 2875  O   THR A 355     8226   8706   8540   -475   1089    100       O  
ATOM   2876  CB  THR A 355     -17.801  12.718 120.343  1.00 66.99           C  
ANISOU 2876  CB  THR A 355     8563   8717   8171    -87    742    135       C  
ATOM   2877  OG1 THR A 355     -16.537  12.737 121.024  1.00 67.93           O  
ANISOU 2877  OG1 THR A 355     8935   8742   8133    -43    491    270       O  
ATOM   2878  CG2 THR A 355     -18.919  12.766 121.375  1.00 67.80           C  
ANISOU 2878  CG2 THR A 355     8789   8880   8093   -272   1073    135       C  
ATOM   2879  N   LEU A 356     -19.461  11.978 117.584  1.00 64.03           N  
ANISOU 2879  N   LEU A 356     7511   8515   8302   -230    829    -61       N  
ATOM   2880  CA  LEU A 356     -20.684  11.740 116.871  1.00 65.92           C  
ANISOU 2880  CA  LEU A 356     7469   8903   8675   -412    921    -90       C  
ATOM   2881  C   LEU A 356     -20.709  10.310 116.268  1.00 67.43           C  
ANISOU 2881  C   LEU A 356     7731   8967   8922   -649    916   -134       C  
ATOM   2882  O   LEU A 356     -21.728   9.647 116.350  1.00 67.82           O  
ANISOU 2882  O   LEU A 356     7704   9045   9019   -876   1062   -117       O  
ATOM   2883  CB  LEU A 356     -20.916  12.810 115.800  1.00 65.01           C  
ANISOU 2883  CB  LEU A 356     7022   9006   8670   -345    782   -116       C  
ATOM   2884  CG  LEU A 356     -20.660  14.295 116.080  1.00 63.03           C  
ANISOU 2884  CG  LEU A 356     6691   8813   8446    -89    773    -99       C  
ATOM   2885  CD1 LEU A 356     -21.338  15.049 114.977  1.00 61.90           C  
ANISOU 2885  CD1 LEU A 356     6146   8876   8496   -105    649    -25       C  
ATOM   2886  CD2 LEU A 356     -21.222  14.759 117.412  1.00 63.67           C  
ANISOU 2886  CD2 LEU A 356     6836   8841   8513    -29   1070    -88       C  
ATOM   2887  N   GLU A 357     -19.610   9.828 115.679  1.00 67.63           N  
ANISOU 2887  N   GLU A 357     7893   8821   8982   -615    799   -212       N  
ATOM   2888  CA  GLU A 357     -19.641   8.487 115.090  1.00 72.99           C  
ANISOU 2888  CA  GLU A 357     8656   9312   9765   -859    886   -310       C  
ATOM   2889  C   GLU A 357     -20.255   7.459 116.048  1.00 76.70           C  
ANISOU 2889  C   GLU A 357     9279   9603  10260   -999   1069   -192       C  
ATOM   2890  O   GLU A 357     -21.144   6.665 115.686  1.00 78.78           O  
ANISOU 2890  O   GLU A 357     9487   9871  10573  -1299   1200   -257       O  
ATOM   2891  CB  GLU A 357     -18.253   8.030 114.692  1.00 73.59           C  
ANISOU 2891  CB  GLU A 357     8885   9100   9975   -747    848   -395       C  
ATOM   2892  CG  GLU A 357     -17.644   8.847 113.516  1.00 74.11           C  
ANISOU 2892  CG  GLU A 357     8828   9324  10008   -707    729   -562       C  
ATOM   2893  CD  GLU A 357     -18.308   8.475 112.226  1.00 76.32           C  
ANISOU 2893  CD  GLU A 357     9025   9753  10220  -1084    783   -761       C  
ATOM   2894  OE1 GLU A 357     -18.291   7.273 111.949  1.00 81.92           O  
ANISOU 2894  OE1 GLU A 357     9873  10213  11041  -1307    972   -903       O  
ATOM   2895  OE2 GLU A 357     -18.873   9.338 111.515  1.00 76.72           O  
ANISOU 2895  OE2 GLU A 357     8881  10153  10116  -1194    633   -755       O  
ATOM   2896  N   GLU A 358     -19.814   7.531 117.294  1.00 78.37           N  
ANISOU 2896  N   GLU A 358     9693   9686  10398   -829   1065     -3       N  
ATOM   2897  CA  GLU A 358     -20.141   6.540 118.272  1.00 81.99           C  
ANISOU 2897  CA  GLU A 358    10371   9935  10846   -963   1207    166       C  
ATOM   2898  C   GLU A 358     -21.401   6.911 119.080  1.00 84.30           C  
ANISOU 2898  C   GLU A 358    10616  10445  10969  -1099   1403    222       C  
ATOM   2899  O   GLU A 358     -22.163   6.011 119.495  1.00 87.25           O  
ANISOU 2899  O   GLU A 358    11071  10722  11359  -1338   1599    288       O  
ATOM   2900  CB  GLU A 358     -18.905   6.302 119.128  1.00 82.68           C  
ANISOU 2900  CB  GLU A 358    10720   9760  10935   -775   1050    395       C  
ATOM   2901  CG  GLU A 358     -18.837   7.123 120.363  1.00 84.11           C  
ANISOU 2901  CG  GLU A 358    11060  10092  10805   -707    988    564       C  
ATOM   2902  CD  GLU A 358     -19.312   6.316 121.531  1.00 87.44           C  
ANISOU 2902  CD  GLU A 358    11760  10389  11075   -918   1113    806       C  
ATOM   2903  OE1 GLU A 358     -18.531   5.474 122.011  1.00 88.67           O  
ANISOU 2903  OE1 GLU A 358    12121  10249  11319   -905    961   1081       O  
ATOM   2904  OE2 GLU A 358     -20.474   6.506 121.949  1.00 91.13           O  
ANISOU 2904  OE2 GLU A 358    12217  11033  11376  -1103   1374    745       O  
ATOM   2905  N   CYS A 359     -21.644   8.213 119.276  1.00 83.27           N  
ANISOU 2905  N   CYS A 359    10340  10571  10728   -962   1404    180       N  
ATOM   2906  CA  CYS A 359     -22.870   8.665 119.943  1.00 85.78           C  
ANISOU 2906  CA  CYS A 359    10540  11060  10991  -1075   1684    182       C  
ATOM   2907  C   CYS A 359     -24.068   8.477 119.034  1.00 86.77           C  
ANISOU 2907  C   CYS A 359    10270  11350  11349  -1261   1769     99       C  
ATOM   2908  O   CYS A 359     -25.135   8.007 119.463  1.00 89.63           O  
ANISOU 2908  O   CYS A 359    10554  11735  11766  -1484   2026    130       O  
ATOM   2909  CB  CYS A 359     -22.806  10.130 120.389  1.00 84.77           C  
ANISOU 2909  CB  CYS A 359    10349  11087  10773   -876   1736    131       C  
ATOM   2910  SG  CYS A 359     -21.764  10.580 121.874  1.00 88.50           S  
ANISOU 2910  SG  CYS A 359    11321  11460  10845   -809   1718    222       S  
ATOM   2911  N   CYS A 360     -23.902   8.842 117.774  1.00 85.54           N  
ANISOU 2911  N   CYS A 360     9861  11326  11314  -1216   1540     12       N  
ATOM   2912  CA  CYS A 360     -24.999   8.705 116.801  1.00 87.75           C  
ANISOU 2912  CA  CYS A 360     9747  11818  11776  -1459   1515    -17       C  
ATOM   2913  C   CYS A 360     -25.428   7.257 116.628  1.00 89.33           C  
ANISOU 2913  C   CYS A 360    10053  11889  11998  -1813   1610    -55       C  
ATOM   2914  O   CYS A 360     -26.596   6.990 116.339  1.00 92.87           O  
ANISOU 2914  O   CYS A 360    10209  12498  12579  -2088   1684    -40       O  
ATOM   2915  CB  CYS A 360     -24.711   9.415 115.463  1.00 86.50           C  
ANISOU 2915  CB  CYS A 360     9346  11861  11658  -1416   1207    -61       C  
ATOM   2916  SG  CYS A 360     -24.602  11.300 115.577  1.00 88.88           S  
ANISOU 2916  SG  CYS A 360     9386  12327  12059  -1031   1132     29       S  
ATOM   2917  N   ALA A 361     -24.519   6.329 116.899  1.00 88.29           N  
ANISOU 2917  N   ALA A 361    10317  11439  11788  -1809   1629    -77       N  
ATOM   2918  CA  ALA A 361     -24.877   4.914 116.976  1.00 90.80           C  
ANISOU 2918  CA  ALA A 361    10800  11529  12168  -2122   1795    -95       C  
ATOM   2919  C   ALA A 361     -25.924   4.625 118.064  1.00 93.12           C  
ANISOU 2919  C   ALA A 361    11090  11833  12459  -2275   2076     36       C  
ATOM   2920  O   ALA A 361     -26.950   4.053 117.773  1.00 95.89           O  
ANISOU 2920  O   ALA A 361    11256  12259  12919  -2604   2198     -2       O  
ATOM   2921  CB  ALA A 361     -23.632   4.032 117.151  1.00 90.32           C  
ANISOU 2921  CB  ALA A 361    11130  11045  12141  -2023   1781    -81       C  
ATOM   2922  N   LYS A 362     -25.670   5.044 119.299  1.00 93.04           N  
ANISOU 2922  N   LYS A 362    11289  11765  12298  -2087   2189    178       N  
ATOM   2923  CA  LYS A 362     -26.550   4.761 120.455  1.00 96.43           C  
ANISOU 2923  CA  LYS A 362    11807  12176  12655  -2269   2525    289       C  
ATOM   2924  C   LYS A 362     -28.024   5.216 120.321  1.00 99.10           C  
ANISOU 2924  C   LYS A 362    11675  12795  13183  -2436   2755    228       C  
ATOM   2925  O   LYS A 362     -28.328   6.183 119.605  1.00 98.31           O  
ANISOU 2925  O   LYS A 362    11159  12945  13248  -2306   2630    165       O  
ATOM   2926  CB  LYS A 362     -26.064   5.543 121.685  1.00 95.52           C  
ANISOU 2926  CB  LYS A 362    11965  12062  12267  -2075   2607    392       C  
ATOM   2927  CG  LYS A 362     -24.748   5.068 122.305  1.00 94.54           C  
ANISOU 2927  CG  LYS A 362    12321  11669  11931  -1970   2403    578       C  
ATOM   2928  CD  LYS A 362     -24.143   6.106 123.310  1.00 95.07           C  
ANISOU 2928  CD  LYS A 362    12626  11828  11669  -1811   2375    643       C  
ATOM   2929  CE  LYS A 362     -24.728   6.038 124.762  1.00 96.49           C  
ANISOU 2929  CE  LYS A 362    13133  12022  11508  -2080   2720    756       C  
ATOM   2930  NZ  LYS A 362     -25.722   7.121 125.142  1.00 95.65           N  
ANISOU 2930  NZ  LYS A 362    12823  12147  11373  -2122   3134    541       N  
ATOM   2931  N   ASP A 363     -28.958   4.612 121.039  1.00102.84           N  
ANISOU 2931  N   ASP A 363    12167  13226  13680  -2713   3098    281       N  
ATOM   2932  CA  ASP A 363     -30.341   5.112 120.948  1.00105.86           C  
ANISOU 2932  CA  ASP A 363    12018  13861  14344  -2843   3342    243       C  
ATOM   2933  C   ASP A 363     -30.599   6.524 121.437  1.00105.61           C  
ANISOU 2933  C   ASP A 363    11751  13980  14395  -2579   3536    214       C  
ATOM   2934  O   ASP A 363     -31.474   7.193 120.930  1.00106.76           O  
ANISOU 2934  O   ASP A 363    11321  14329  14916  -2551   3579    207       O  
ATOM   2935  CB  ASP A 363     -31.404   4.173 121.500  1.00110.44           C  
ANISOU 2935  CB  ASP A 363    12577  14378  15007  -3234   3712    282       C  
ATOM   2936  CG  ASP A 363     -32.771   4.449 120.886  1.00114.94           C  
ANISOU 2936  CG  ASP A 363    12449  15217  16007  -3413   3802    258       C  
ATOM   2937  OD1 ASP A 363     -32.951   4.135 119.694  1.00115.43           O  
ANISOU 2937  OD1 ASP A 363    12228  15408  16220  -3570   3467    237       O  
ATOM   2938  OD2 ASP A 363     -33.660   5.001 121.569  1.00118.38           O  
ANISOU 2938  OD2 ASP A 363    12598  15735  16645  -3421   4208    267       O  
ATOM   2939  N   ASP A 364     -29.903   6.944 122.474  1.00104.90           N  
ANISOU 2939  N   ASP A 364    12098  13773  13987  -2429   3682    212       N  
ATOM   2940  CA  ASP A 364     -30.087   8.291 123.023  1.00104.74           C  
ANISOU 2940  CA  ASP A 364    11939  13834  14024  -2217   3955    121       C  
ATOM   2941  C   ASP A 364     -28.811   9.126 122.799  1.00100.56           C  
ANISOU 2941  C   ASP A 364    11615  13295  13301  -1883   3608     92       C  
ATOM   2942  O   ASP A 364     -28.087   9.448 123.759  1.00 99.98           O  
ANISOU 2942  O   ASP A 364    12008  13129  12850  -1841   3698     72       O  
ATOM   2943  CB  ASP A 364     -30.437   8.204 124.507  1.00108.47           C  
ANISOU 2943  CB  ASP A 364    12783  14205  14224  -2428   4501     87       C  
ATOM   2944  CG  ASP A 364     -30.832   9.541 125.100  1.00110.66           C  
ANISOU 2944  CG  ASP A 364    12899  14520  14626  -2288   4949    -86       C  
ATOM   2945  OD1 ASP A 364     -30.754  10.577 124.394  1.00107.87           O  
ANISOU 2945  OD1 ASP A 364    12145  14240  14600  -1974   4797   -139       O  
ATOM   2946  OD2 ASP A 364     -31.229   9.543 126.287  1.00116.05           O  
ANISOU 2946  OD2 ASP A 364    13877  15133  15083  -2523   5493   -174       O  
ATOM   2947  N   PRO A 365     -28.530   9.476 121.521  1.00 97.53           N  
ANISOU 2947  N   PRO A 365    10893  13021  13141  -1697   3198     99       N  
ATOM   2948  CA  PRO A 365     -27.325  10.228 121.175  1.00 93.78           C  
ANISOU 2948  CA  PRO A 365    10573  12538  12522  -1401   2867     72       C  
ATOM   2949  C   PRO A 365     -27.181  11.502 122.007  1.00 94.44           C  
ANISOU 2949  C   PRO A 365    10735  12605  12544  -1212   3136    -24       C  
ATOM   2950  O   PRO A 365     -26.081  11.815 122.471  1.00 92.41           O  
ANISOU 2950  O   PRO A 365    10889  12272  11953  -1104   3001    -49       O  
ATOM   2951  CB  PRO A 365     -27.536  10.555 119.685  1.00 92.47           C  
ANISOU 2951  CB  PRO A 365     9912  12548  12675  -1321   2525     97       C  
ATOM   2952  CG  PRO A 365     -29.023  10.273 119.432  1.00 95.76           C  
ANISOU 2952  CG  PRO A 365     9828  13098  13459  -1549   2718    156       C  
ATOM   2953  CD  PRO A 365     -29.305   9.137 120.315  1.00 97.63           C  
ANISOU 2953  CD  PRO A 365    10395  13193  13508  -1824   3003    145       C  
ATOM   2954  N   HIS A 366     -28.293  12.200 122.225  1.00 97.46           N  
ANISOU 2954  N   HIS A 366    10719  13033  13278  -1201   3543    -84       N  
ATOM   2955  CA  HIS A 366     -28.268  13.478 122.933  1.00 98.66           C  
ANISOU 2955  CA  HIS A 366    10903  13115  13470  -1036   3902   -234       C  
ATOM   2956  C   HIS A 366     -27.708  13.368 124.371  1.00100.33           C  
ANISOU 2956  C   HIS A 366    11803  13211  13107  -1223   4189   -349       C  
ATOM   2957  O   HIS A 366     -27.048  14.302 124.846  1.00100.15           O  
ANISOU 2957  O   HIS A 366    12036  13133  12884  -1118   4261   -483       O  
ATOM   2958  CB  HIS A 366     -29.663  14.143 122.924  1.00102.91           C  
ANISOU 2958  CB  HIS A 366    10821  13652  14626   -995   4379   -269       C  
ATOM   2959  CG  HIS A 366     -29.633  15.592 123.297  1.00103.32           C  
ANISOU 2959  CG  HIS A 366    10775  13574  14908   -755   4727   -430       C  
ATOM   2960  ND1 HIS A 366     -29.701  16.025 124.602  1.00105.93           N  
ANISOU 2960  ND1 HIS A 366    11485  13744  15018   -881   5351   -684       N  
ATOM   2961  CD2 HIS A 366     -29.503  16.705 122.537  1.00101.36           C  
ANISOU 2961  CD2 HIS A 366    10136  13305  15071   -431   4556   -380       C  
ATOM   2962  CE1 HIS A 366     -29.619  17.343 124.629  1.00107.66           C  
ANISOU 2962  CE1 HIS A 366    11545  13823  15538   -636   5587   -825       C  
ATOM   2963  NE2 HIS A 366     -29.497  17.780 123.389  1.00104.37           N  
ANISOU 2963  NE2 HIS A 366    10646  13476  15533   -338   5100   -620       N  
ATOM   2964  N   ALA A 367     -27.977  12.246 125.054  1.00 98.92           N  
ANISOU 2964  N   ALA A 367    13278  11799  12509   -450   1309   2062       N  
ATOM   2965  CA  ALA A 367     -27.371  11.968 126.372  1.00103.07           C  
ANISOU 2965  CA  ALA A 367    13391  12978  12792   -638   1207   2780       C  
ATOM   2966  C   ALA A 367     -25.868  11.761 126.233  1.00102.80           C  
ANISOU 2966  C   ALA A 367    13397  12559  13103   -550   1128   2841       C  
ATOM   2967  O   ALA A 367     -25.075  12.111 127.112  1.00103.73           O  
ANISOU 2967  O   ALA A 367    13340  13332  12743   -631   1123   3087       O  
ATOM   2968  CB  ALA A 367     -27.994  10.747 127.011  1.00109.26           C  
ANISOU 2968  CB  ALA A 367    13584  13885  14046   -917    978   3858       C  
ATOM   2969  N   CYS A 368     -25.483  11.207 125.094  1.00101.85           N  
ANISOU 2969  N   CYS A 368    13405  11525  13770   -392   1077   2457       N  
ATOM   2970  CA  CYS A 368     -24.087  10.912 124.843  1.00102.33           C  
ANISOU 2970  CA  CYS A 368    13411  11190  14279   -298    993   2354       C  
ATOM   2971  C   CYS A 368     -23.265  12.141 124.416  1.00 96.66           C  
ANISOU 2971  C   CYS A 368    13135  10761  12830   -148   1177   1748       C  
ATOM   2972  O   CYS A 368     -22.173  12.357 124.940  1.00 96.71           O  
ANISOU 2972  O   CYS A 368    13132  10922  12693   -138   1151   1924       O  
ATOM   2973  CB  CYS A 368     -23.955   9.775 123.831  1.00105.69           C  
ANISOU 2973  CB  CYS A 368    13488  10715  15955   -205    839   1889       C  
ATOM   2974  SG  CYS A 368     -22.244   9.358 123.454  1.00109.83           S  
ANISOU 2974  SG  CYS A 368    13764  10780  17186    -76    723   1476       S  
ATOM   2975  N   TYR A 369     -23.772  12.933 123.475  1.00 92.44           N  
ANISOU 2975  N   TYR A 369    12865  10314  11944    -72   1308   1199       N  
ATOM   2976  CA  TYR A 369     -22.961  14.010 122.894  1.00 89.28           C  
ANISOU 2976  CA  TYR A 369    12651  10097  11174      4   1364    904       C  
ATOM   2977  C   TYR A 369     -23.164  15.395 123.550  1.00 87.89           C  
ANISOU 2977  C   TYR A 369    12547  10184  10664     13   1386    912       C  
ATOM   2978  O   TYR A 369     -22.327  16.264 123.391  1.00 87.24           O  
ANISOU 2978  O   TYR A 369    12472  10107  10570     62   1348    834       O  
ATOM   2979  CB  TYR A 369     -23.122  14.076 121.360  1.00 89.37           C  
ANISOU 2979  CB  TYR A 369    12567  10272  11119    -15   1388    513       C  
ATOM   2980  CG  TYR A 369     -24.445  14.650 120.894  1.00 88.81           C  
ANISOU 2980  CG  TYR A 369    12503  10381  10858    -92   1410    565       C  
ATOM   2981  CD1 TYR A 369     -25.360  13.855 120.237  1.00 90.29           C  
ANISOU 2981  CD1 TYR A 369    12523  10621  11161   -140   1440    287       C  
ATOM   2982  CD2 TYR A 369     -24.793  15.992 121.142  1.00 88.13           C  
ANISOU 2982  CD2 TYR A 369    12461  10317  10706   -112   1355    824       C  
ATOM   2983  CE1 TYR A 369     -26.596  14.362 119.831  1.00 91.60           C  
ANISOU 2983  CE1 TYR A 369    12685  10974  11146   -224   1453    401       C  
ATOM   2984  CE2 TYR A 369     -26.029  16.507 120.732  1.00 88.34           C  
ANISOU 2984  CE2 TYR A 369    12386  10381  10797   -190   1316    931       C  
ATOM   2985  CZ  TYR A 369     -26.923  15.683 120.073  1.00 89.83           C  
ANISOU 2985  CZ  TYR A 369    12528  10738  10863   -255   1384    788       C  
ATOM   2986  OH  TYR A 369     -28.152  16.146 119.655  1.00 89.80           O  
ANISOU 2986  OH  TYR A 369    12416  10810  10893   -346   1344    943       O  
ATOM   2987  N   SER A 370     -24.273  15.589 124.273  1.00 88.63           N  
ANISOU 2987  N   SER A 370    12539  10494  10640    -39   1415    892       N  
ATOM   2988  CA  SER A 370     -24.491  16.773 125.149  1.00 89.45           C  
ANISOU 2988  CA  SER A 370    12398  10945  10645    -18   1415    502       C  
ATOM   2989  C   SER A 370     -23.298  17.137 126.053  1.00 91.18           C  
ANISOU 2989  C   SER A 370    12431  11534  10680      8   1409    341       C  
ATOM   2990  O   SER A 370     -23.130  18.317 126.428  1.00 92.97           O  
ANISOU 2990  O   SER A 370    12336  11838  11149     85   1360   -274       O  
ATOM   2991  CB  SER A 370     -25.692  16.537 126.072  1.00 92.12           C  
ANISOU 2991  CB  SER A 370    12449  11885  10665   -133   1476    405       C  
ATOM   2992  OG  SER A 370     -25.405  15.502 126.991  1.00 90.74           O  
ANISOU 2992  OG  SER A 370    12070  12331  10074   -301   1480    970       O  
ATOM   2993  N   THR A 371     -22.500  16.127 126.415  1.00 90.89           N  
ANISOU 2993  N   THR A 371    12449  11669  10417    -60   1412    847       N  
ATOM   2994  CA  THR A 371     -21.401  16.308 127.364  1.00 93.02           C  
ANISOU 2994  CA  THR A 371    12480  12487  10376    -88   1406    838       C  
ATOM   2995  C   THR A 371     -20.013  16.453 126.722  1.00 90.04           C  
ANISOU 2995  C   THR A 371    12392  11539  10280     45   1362    873       C  
ATOM   2996  O   THR A 371     -19.032  16.692 127.420  1.00 91.73           O  
ANISOU 2996  O   THR A 371    12443  12125  10283     44   1355    821       O  
ATOM   2997  CB  THR A 371     -21.403  15.189 128.442  1.00 97.81           C  
ANISOU 2997  CB  THR A 371    12681  13918  10562   -347   1360   1635       C  
ATOM   2998  OG1 THR A 371     -21.672  13.923 127.834  1.00 98.45           O  
ANISOU 2998  OG1 THR A 371    12897  13273  11235   -394   1247   2345       O  
ATOM   2999  CG2 THR A 371     -22.487  15.444 129.473  1.00102.32           C  
ANISOU 2999  CG2 THR A 371    12660  15761  10456   -553   1420   1448       C  
ATOM   3000  N   VAL A 372     -19.941  16.359 125.391  1.00 86.94           N  
ANISOU 3000  N   VAL A 372    12310  10477  10248    124   1336    906       N  
ATOM   3001  CA  VAL A 372     -18.660  16.361 124.649  1.00 84.59           C  
ANISOU 3001  CA  VAL A 372    12157   9896  10085    195   1298    941       C  
ATOM   3002  C   VAL A 372     -17.665  17.485 125.038  1.00 85.05           C  
ANISOU 3002  C   VAL A 372    12133  10023  10158    266   1252    752       C  
ATOM   3003  O   VAL A 372     -16.470  17.230 125.187  1.00 84.74           O  
ANISOU 3003  O   VAL A 372    12152   9993  10052    298   1245    854       O  
ATOM   3004  CB  VAL A 372     -18.892  16.285 123.110  1.00 83.33           C  
ANISOU 3004  CB  VAL A 372    12041   9587  10032    175   1283    890       C  
ATOM   3005  CG1 VAL A 372     -19.649  17.475 122.600  1.00 82.67           C  
ANISOU 3005  CG1 VAL A 372    11837   9514  10061    127   1206    948       C  
ATOM   3006  CG2 VAL A 372     -17.585  16.135 122.371  1.00 83.50           C  
ANISOU 3006  CG2 VAL A 372    12017   9698  10009    189   1258    833       C  
ATOM   3007  N   PHE A 373     -18.161  18.711 125.242  1.00 86.08           N  
ANISOU 3007  N   PHE A 373    12010  10106  10591    298   1182    402       N  
ATOM   3008  CA  PHE A 373     -17.276  19.852 125.486  1.00 87.03           C  
ANISOU 3008  CA  PHE A 373    11856  10063  11147    378   1056    115       C  
ATOM   3009  C   PHE A 373     -16.368  19.755 126.721  1.00 88.51           C  
ANISOU 3009  C   PHE A 373    11895  10780  10954    411   1134   -225       C  
ATOM   3010  O   PHE A 373     -15.273  20.305 126.762  1.00 87.87           O  
ANISOU 3010  O   PHE A 373    11730  10543  11113    480   1057   -328       O  
ATOM   3011  CB  PHE A 373     -18.073  21.164 125.476  1.00 90.46           C  
ANISOU 3011  CB  PHE A 373    11755  10100  12514    415    861   -324       C  
ATOM   3012  CG  PHE A 373     -18.376  21.685 124.083  1.00 89.48           C  
ANISOU 3012  CG  PHE A 373    11537   9425  13035    320    630    392       C  
ATOM   3013  CD1 PHE A 373     -19.567  21.358 123.442  1.00 87.55           C  
ANISOU 3013  CD1 PHE A 373    11377   9208  12680    222    649    685       C  
ATOM   3014  CD2 PHE A 373     -17.463  22.481 123.406  1.00 89.67           C  
ANISOU 3014  CD2 PHE A 373    11264   9097  13711    265    365    931       C  
ATOM   3015  CE1 PHE A 373     -19.837  21.829 122.160  1.00 88.58           C  
ANISOU 3015  CE1 PHE A 373    11233   9189  13232     43    410   1515       C  
ATOM   3016  CE2 PHE A 373     -17.732  22.951 122.120  1.00 90.19           C  
ANISOU 3016  CE2 PHE A 373    10989   9047  14232     48     91   1926       C  
ATOM   3017  CZ  PHE A 373     -18.915  22.617 121.497  1.00 89.88           C  
ANISOU 3017  CZ  PHE A 373    10979   9215  13956    -79    119   2227       C  
ATOM   3018  N   ASP A 374     -16.818  19.057 127.737  1.00 91.19           N  
ANISOU 3018  N   ASP A 374    12084  11909  10654    309   1259   -282       N  
ATOM   3019  CA  ASP A 374     -15.967  18.888 128.888  1.00 95.50           C  
ANISOU 3019  CA  ASP A 374    12317  13317  10649    239   1308   -381       C  
ATOM   3020  C   ASP A 374     -14.813  18.002 128.444  1.00 93.43           C  
ANISOU 3020  C   ASP A 374    12494  12654  10352    242   1285    397       C  
ATOM   3021  O   ASP A 374     -13.636  18.391 128.556  1.00 93.60           O  
ANISOU 3021  O   ASP A 374    12516  12621  10426    315   1256    274       O  
ATOM   3022  CB  ASP A 374     -16.796  18.325 130.003  1.00100.24           C  
ANISOU 3022  CB  ASP A 374    12422  15187  10478      9   1389   -318       C  
ATOM   3023  CG  ASP A 374     -18.190  18.964 130.040  1.00103.66           C  
ANISOU 3023  CG  ASP A 374    12530  15772  11085     26   1416  -1079       C  
ATOM   3024  OD1 ASP A 374     -18.657  19.382 128.957  1.00 99.94           O  
ANISOU 3024  OD1 ASP A 374    12432  14146  11396    180   1346  -1133       O  
ATOM   3025  OD2 ASP A 374     -18.812  19.071 131.128  1.00111.64           O  
ANISOU 3025  OD2 ASP A 374    12787  18200  11431   -149   1490  -1621       O  
ATOM   3026  N   LYS A 375     -15.161  16.854 127.853  1.00 92.46           N  
ANISOU 3026  N   LYS A 375    12649  12140  10342    184   1270   1037       N  
ATOM   3027  CA  LYS A 375     -14.202  15.968 127.209  1.00 90.74           C  
ANISOU 3027  CA  LYS A 375    12666  11358  10452    221   1208   1456       C  
ATOM   3028  C   LYS A 375     -13.199  16.798 126.459  1.00 88.49           C  
ANISOU 3028  C   LYS A 375    12595  10727  10302    366   1205   1115       C  
ATOM   3029  O   LYS A 375     -12.006  16.592 126.585  1.00 89.40           O  
ANISOU 3029  O   LYS A 375    12732  10802  10433    398   1175   1233       O  
ATOM   3030  CB  LYS A 375     -14.903  15.020 126.222  1.00 89.89           C  
ANISOU 3030  CB  LYS A 375    12669  10684  10801    219   1177   1582       C  
ATOM   3031  CG  LYS A 375     -15.230  13.635 126.781  1.00 93.73           C  
ANISOU 3031  CG  LYS A 375    12807  11084  11722     68   1038   2258       C  
ATOM   3032  CD  LYS A 375     -15.485  12.551 125.680  1.00 92.61           C  
ANISOU 3032  CD  LYS A 375    12565  10121  12502    129    941   2058       C  
ATOM   3033  CE  LYS A 375     -14.309  12.342 124.677  1.00 92.32           C  
ANISOU 3033  CE  LYS A 375    12519   9689  12869    279    928   1441       C  
ATOM   3034  NZ  LYS A 375     -12.934  12.111 125.255  1.00 86.51           N  
ANISOU 3034  NZ  LYS A 375    11643   8835  12392    291    816   1750       N  
ATOM   3035  N   LEU A 376     -13.693  17.736 125.663  1.00 87.71           N  
ANISOU 3035  N   LEU A 376    12542  10404  10380    412   1186    850       N  
ATOM   3036  CA  LEU A 376     -12.835  18.578 124.835  1.00 87.08           C  
ANISOU 3036  CA  LEU A 376    12461  10103  10523    453   1095    857       C  
ATOM   3037  C   LEU A 376     -12.018  19.490 125.716  1.00 88.33           C  
ANISOU 3037  C   LEU A 376    12421  10304  10835    528   1039    588       C  
ATOM   3038  O   LEU A 376     -10.807  19.474 125.656  1.00 87.83           O  
ANISOU 3038  O   LEU A 376    12430  10220  10719    563   1020    692       O  
ATOM   3039  CB  LEU A 376     -13.675  19.442 123.879  1.00 88.40           C  
ANISOU 3039  CB  LEU A 376    12443  10101  11044    385    971    995       C  
ATOM   3040  CG  LEU A 376     -14.409  18.821 122.683  1.00 88.64           C  
ANISOU 3040  CG  LEU A 376    12497  10335  10848    264   1001   1216       C  
ATOM   3041  CD1 LEU A 376     -15.422  19.823 122.078  1.00 91.78           C  
ANISOU 3041  CD1 LEU A 376    12567  10639  11665    147    825   1540       C  
ATOM   3042  CD2 LEU A 376     -13.436  18.376 121.634  1.00 89.96           C  
ANISOU 3042  CD2 LEU A 376    12566  10939  10675    181   1006   1317       C  
ATOM   3043  N   LYS A 377     -12.693  20.278 126.544  1.00 91.38           N  
ANISOU 3043  N   LYS A 377    12439  10818  11464    556   1009     62       N  
ATOM   3044  CA  LYS A 377     -12.013  21.155 127.488  1.00 95.18           C  
ANISOU 3044  CA  LYS A 377    12480  11495  12190    634    954   -583       C  
ATOM   3045  C   LYS A 377     -10.844  20.551 128.259  1.00 94.87           C  
ANISOU 3045  C   LYS A 377    12531  12022  11492    617   1060   -488       C  
ATOM   3046  O   LYS A 377      -9.863  21.238 128.513  1.00 96.39           O  
ANISOU 3046  O   LYS A 377    12517  12149  11960    696    988   -809       O  
ATOM   3047  CB  LYS A 377     -12.994  21.876 128.418  1.00100.26           C  
ANISOU 3047  CB  LYS A 377    12449  12536  13108    652    942  -1578       C  
ATOM   3048  CG  LYS A 377     -13.288  23.280 127.931  1.00104.90           C  
ANISOU 3048  CG  LYS A 377    12476  12186  15195    757    644  -2039       C  
ATOM   3049  CD  LYS A 377     -11.981  24.075 127.670  1.00107.72           C  
ANISOU 3049  CD  LYS A 377    12621  11936  16372    835    423  -1954       C  
ATOM   3050  CE  LYS A 377     -12.078  24.952 126.408  1.00110.67           C  
ANISOU 3050  CE  LYS A 377    12723  11183  18144    785     28  -1139       C  
ATOM   3051  NZ  LYS A 377     -11.217  26.187 126.463  1.00117.39           N  
ANISOU 3051  NZ  LYS A 377    12791  11239  20572    859   -355  -1368       N  
ATOM   3052  N   HIS A 378     -10.936  19.273 128.599  1.00 94.20           N  
ANISOU 3052  N   HIS A 378    12650  12403  10739    496   1172     60       N  
ATOM   3053  CA  HIS A 378      -9.772  18.533 129.099  1.00 95.25           C  
ANISOU 3053  CA  HIS A 378    12827  12861  10502    439   1184    514       C  
ATOM   3054  C   HIS A 378      -8.642  18.259 128.077  1.00 91.57           C  
ANISOU 3054  C   HIS A 378    12785  11631  10376    543   1132    835       C  
ATOM   3055  O   HIS A 378      -7.490  18.108 128.447  1.00 91.83           O  
ANISOU 3055  O   HIS A 378    12802  11790  10301    554   1114    969       O  
ATOM   3056  CB  HIS A 378     -10.238  17.249 129.789  1.00 98.39           C  
ANISOU 3056  CB  HIS A 378    13023  13870  10489    216   1182   1261       C  
ATOM   3057  CG  HIS A 378     -11.321  17.489 130.799  1.00104.55           C  
ANISOU 3057  CG  HIS A 378    13229  15814  10680     37   1240    996       C  
ATOM   3058  ND1 HIS A 378     -12.570  16.911 130.706  1.00106.89           N  
ANISOU 3058  ND1 HIS A 378    13485  16178  10952    -82   1239   1340       N  
ATOM   3059  CD2 HIS A 378     -11.354  18.281 131.901  1.00110.19           C  
ANISOU 3059  CD2 HIS A 378    13243  17836  10789    -53   1306    222       C  
ATOM   3060  CE1 HIS A 378     -13.320  17.320 131.716  1.00112.38           C  
ANISOU 3060  CE1 HIS A 378    13508  18233  10958   -257   1307    900       C  
ATOM   3061  NE2 HIS A 378     -12.606  18.154 132.453  1.00115.89           N  
ANISOU 3061  NE2 HIS A 378    13476  19532  11026   -244   1354    106       N  
ATOM   3062  N   LEU A 379      -8.946  18.209 126.793  1.00 89.60           N  
ANISOU 3062  N   LEU A 379    12789  10815  10439    584   1108    906       N  
ATOM   3063  CA  LEU A 379      -7.861  18.012 125.825  1.00 88.49           C  
ANISOU 3063  CA  LEU A 379    12807  10398  10419    627   1073   1022       C  
ATOM   3064  C   LEU A 379      -6.740  19.050 125.879  1.00 88.41           C  
ANISOU 3064  C   LEU A 379    12732  10358  10503    688   1003    934       C  
ATOM   3065  O   LEU A 379      -5.580  18.678 125.830  1.00 87.19           O  
ANISOU 3065  O   LEU A 379    12655  10207  10264    718   1005   1018       O  
ATOM   3066  CB  LEU A 379      -8.387  17.854 124.407  1.00 88.09           C  
ANISOU 3066  CB  LEU A 379    12761  10281  10427    573   1063   1030       C  
ATOM   3067  CG  LEU A 379      -8.778  16.406 124.115  1.00 89.20           C  
ANISOU 3067  CG  LEU A 379    12864  10325  10702    557   1105    922       C  
ATOM   3068  CD1 LEU A 379      -8.351  16.042 122.702  1.00 89.17           C  
ANISOU 3068  CD1 LEU A 379    12627  10608  10645    518   1110    554       C  
ATOM   3069  CD2 LEU A 379      -8.145  15.441 125.121  1.00 92.74           C  
ANISOU 3069  CD2 LEU A 379    13239  10550  11449    582   1055   1136       C  
ATOM   3070  N   VAL A 380      -7.102  20.327 126.030  1.00 90.59           N  
ANISOU 3070  N   VAL A 380    12748  10501  11170    709    897    719       N  
ATOM   3071  CA  VAL A 380      -6.151  21.476 126.127  1.00 92.87           C  
ANISOU 3071  CA  VAL A 380    12762  10559  11967    767    738    603       C  
ATOM   3072  C   VAL A 380      -4.971  21.374 127.117  1.00 93.84           C  
ANISOU 3072  C   VAL A 380    12885  10953  11819    845    805    321       C  
ATOM   3073  O   VAL A 380      -3.913  21.975 126.917  1.00 94.17           O  
ANISOU 3073  O   VAL A 380    12830  10776  12172    885    693    382       O  
ATOM   3074  CB  VAL A 380      -6.876  22.802 126.530  1.00 96.86           C  
ANISOU 3074  CB  VAL A 380    12671  10699  13433    814    543     93       C  
ATOM   3075  CG1 VAL A 380      -6.069  24.010 126.032  1.00 98.86           C  
ANISOU 3075  CG1 VAL A 380    12457  10339  14766    815    217    345       C  
ATOM   3076  CG2 VAL A 380      -8.317  22.844 126.007  1.00 96.68           C  
ANISOU 3076  CG2 VAL A 380    12568  10504  13660    740    497    234       C  
ATOM   3077  N   ASP A 381      -5.175  20.623 128.190  1.00 95.44           N  
ANISOU 3077  N   ASP A 381    13080  11754  11429    813    955    155       N  
ATOM   3078  CA  ASP A 381      -4.398  20.777 129.400  1.00 98.62           C  
ANISOU 3078  CA  ASP A 381    13172  12800  11501    815    995   -205       C  
ATOM   3079  C   ASP A 381      -3.482  19.590 129.555  1.00 97.44           C  
ANISOU 3079  C   ASP A 381    13291  12841  10892    747   1041    477       C  
ATOM   3080  O   ASP A 381      -2.546  19.617 130.352  1.00 99.18           O  
ANISOU 3080  O   ASP A 381    13304  13565  10816    722   1046    441       O  
ATOM   3081  CB  ASP A 381      -5.372  20.903 130.562  1.00103.61           C  
ANISOU 3081  CB  ASP A 381    13235  14410  11721    716   1071   -793       C  
ATOM   3082  CG  ASP A 381      -6.671  21.614 130.147  1.00106.08           C  
ANISOU 3082  CG  ASP A 381    13354  14301  12649    769   1012  -1301       C  
ATOM   3083  OD1 ASP A 381      -7.223  21.277 129.072  1.00103.72           O  
ANISOU 3083  OD1 ASP A 381    13514  13292  12604    770    980   -709       O  
ATOM   3084  OD2 ASP A 381      -7.143  22.517 130.876  1.00113.64           O  
ANISOU 3084  OD2 ASP A 381    13571  15691  13914    804    979  -2403       O  
ATOM   3085  N   GLU A 382      -3.744  18.559 128.752  1.00 95.64           N  
ANISOU 3085  N   GLU A 382    13389  12166  10784    718   1036   1014       N  
ATOM   3086  CA  GLU A 382      -2.899  17.371 128.716  1.00 96.08           C  
ANISOU 3086  CA  GLU A 382    13512  12054  10941    681    986   1548       C  
ATOM   3087  C   GLU A 382      -1.410  17.748 128.468  1.00 95.16           C  
ANISOU 3087  C   GLU A 382    13518  11749  10890    786    965   1427       C  
ATOM   3088  O   GLU A 382      -0.553  17.365 129.270  1.00 97.44           O  
ANISOU 3088  O   GLU A 382    13642  12323  11058    736    923   1727       O  
ATOM   3089  CB  GLU A 382      -3.444  16.301 127.735  1.00 95.23           C  
ANISOU 3089  CB  GLU A 382    13496  11367  11319    680    945   1703       C  
ATOM   3090  CG  GLU A 382      -3.342  14.860 128.318  1.00 99.52           C  
ANISOU 3090  CG  GLU A 382    13674  11745  12391    555    778   2387       C  
ATOM   3091  CD  GLU A 382      -3.760  13.708 127.379  1.00 99.58           C  
ANISOU 3091  CD  GLU A 382    13507  10981  13348    590    665   2254       C  
ATOM   3092  OE1 GLU A 382      -4.741  13.839 126.610  1.00 94.54           O  
ANISOU 3092  OE1 GLU A 382    13000  10277  12643    623    756   1825       O  
ATOM   3093  OE2 GLU A 382      -3.115  12.632 127.463  1.00105.11           O  
ANISOU 3093  OE2 GLU A 382    13778  11124  15037    572    441   2542       O  
ATOM   3094  N   PRO A 383      -1.104  18.498 127.373  1.00 93.05           N  
ANISOU 3094  N   PRO A 383    13425  11141  10789    876    958   1150       N  
ATOM   3095  CA  PRO A 383       0.189  19.142 127.058  1.00 91.99           C  
ANISOU 3095  CA  PRO A 383    13322  10924  10704    942    912   1082       C  
ATOM   3096  C   PRO A 383       0.935  19.937 128.142  1.00 93.15           C  
ANISOU 3096  C   PRO A 383    13301  11304  10787    990    893    872       C  
ATOM   3097  O   PRO A 383       2.145  19.732 128.318  1.00 92.87           O  
ANISOU 3097  O   PRO A 383    13317  11296  10671   1023    884    974       O  
ATOM   3098  CB  PRO A 383      -0.201  20.096 125.945  1.00 92.29           C  
ANISOU 3098  CB  PRO A 383    13273  10831  10961    904    826   1114       C  
ATOM   3099  CG  PRO A 383      -1.179  19.279 125.147  1.00 93.35           C  
ANISOU 3099  CG  PRO A 383    13450  11039  10979    830    883   1153       C  
ATOM   3100  CD  PRO A 383      -1.928  18.409 126.151  1.00 92.11           C  
ANISOU 3100  CD  PRO A 383    13363  10838  10794    846    959   1110       C  
ATOM   3101  N   GLN A 384       0.223  20.826 128.846  1.00 94.86           N  
ANISOU 3101  N   GLN A 384    13196  11742  11106    998    880    411       N  
ATOM   3102  CA  GLN A 384       0.825  21.855 129.724  1.00 97.23           C  
ANISOU 3102  CA  GLN A 384    13060  12299  11585   1064    831   -226       C  
ATOM   3103  C   GLN A 384       1.996  21.480 130.680  1.00 97.66           C  
ANISOU 3103  C   GLN A 384    13015  13001  11091   1037    894   -216       C  
ATOM   3104  O   GLN A 384       2.939  22.252 130.879  1.00 98.56           O  
ANISOU 3104  O   GLN A 384    12932  13034  11483   1126    830   -604       O  
ATOM   3105  CB  GLN A 384      -0.281  22.575 130.512  1.00102.18           C  
ANISOU 3105  CB  GLN A 384    13084  13346  12395   1059    827  -1090       C  
ATOM   3106  CG  GLN A 384      -0.064  24.082 130.661  1.00106.74           C  
ANISOU 3106  CG  GLN A 384    12988  13479  14088   1195    626  -2036       C  
ATOM   3107  CD  GLN A 384      -0.011  24.790 129.319  1.00106.01           C  
ANISOU 3107  CD  GLN A 384    12981  12147  15151   1231    353  -1430       C  
ATOM   3108  OE1 GLN A 384      -0.880  24.583 128.465  1.00105.66           O  
ANISOU 3108  OE1 GLN A 384    13160  11777  15209   1155    313   -850       O  
ATOM   3109  NE2 GLN A 384       1.017  25.613 129.117  1.00106.24           N  
ANISOU 3109  NE2 GLN A 384    12716  11633  16019   1293    133  -1421       N  
ATOM   3110  N   ASN A 385       1.947  20.308 131.277  1.00 97.23           N  
ANISOU 3110  N   ASN A 385    12975  13573  10396    885    966    349       N  
ATOM   3111  CA  ASN A 385       3.011  19.932 132.199  1.00 99.45           C  
ANISOU 3111  CA  ASN A 385    13007  14588  10191    787    966    612       C  
ATOM   3112  C   ASN A 385       4.226  19.374 131.498  1.00 95.28           C  
ANISOU 3112  C   ASN A 385    12925  13287   9990    873    905   1146       C  
ATOM   3113  O   ASN A 385       5.312  19.345 132.076  1.00 96.61           O  
ANISOU 3113  O   ASN A 385    12943  13821   9943    848    883   1263       O  
ATOM   3114  CB  ASN A 385       2.455  18.952 133.198  1.00104.82           C  
ANISOU 3114  CB  ASN A 385    13218  16401  10209    488    958   1312       C  
ATOM   3115  CG  ASN A 385       1.022  18.621 132.884  1.00105.88           C  
ANISOU 3115  CG  ASN A 385    13402  16390  10437    430    974   1435       C  
ATOM   3116  OD1 ASN A 385       0.642  18.551 131.694  1.00101.36           O  
ANISOU 3116  OD1 ASN A 385    13383  14634  10496    599    968   1397       O  
ATOM   3117  ND2 ASN A 385       0.199  18.483 133.925  1.00110.28           N  
ANISOU 3117  ND2 ASN A 385    13274  18369  10259    161   1000   1520       N  
ATOM   3118  N   LEU A 386       4.041  18.954 130.244  1.00 90.91           N  
ANISOU 3118  N   LEU A 386    12796  11834   9913    958    880   1333       N  
ATOM   3119  CA  LEU A 386       5.155  18.596 129.388  1.00 87.32           C  
ANISOU 3119  CA  LEU A 386    12595  10815   9767   1048    837   1459       C  
ATOM   3120  C   LEU A 386       6.009  19.835 129.350  1.00 86.00           C  
ANISOU 3120  C   LEU A 386    12435  10649   9591   1144    829   1083       C  
ATOM   3121  O   LEU A 386       7.176  19.799 129.723  1.00 86.94           O  
ANISOU 3121  O   LEU A 386    12536  10867   9628   1172    811   1146       O  
ATOM   3122  CB  LEU A 386       4.682  18.225 127.972  1.00 85.61           C  
ANISOU 3122  CB  LEU A 386    12552  10120   9857   1080    838   1356       C  
ATOM   3123  CG  LEU A 386       5.751  17.916 126.890  1.00 84.24           C  
ANISOU 3123  CG  LEU A 386    12396   9766   9847   1131    815   1179       C  
ATOM   3124  CD1 LEU A 386       5.211  17.024 125.774  1.00 84.50           C  
ANISOU 3124  CD1 LEU A 386    12254   9719  10134   1106    820    855       C  
ATOM   3125  CD2 LEU A 386       6.354  19.156 126.303  1.00 79.71           C  
ANISOU 3125  CD2 LEU A 386    11843   9369   9072   1133    795   1132       C  
ATOM   3126  N   ILE A 387       5.389  20.927 128.914  1.00 85.12           N  
ANISOU 3126  N   ILE A 387    12239  10343   9761   1178    787    768       N  
ATOM   3127  CA  ILE A 387       6.028  22.222 128.699  1.00 85.12           C  
ANISOU 3127  CA  ILE A 387    12026  10063  10253   1245    653    541       C  
ATOM   3128  C   ILE A 387       6.976  22.702 129.778  1.00 85.97           C  
ANISOU 3128  C   ILE A 387    11871  10464  10330   1312    650     99       C  
ATOM   3129  O   ILE A 387       8.158  22.942 129.502  1.00 84.33           O  
ANISOU 3129  O   ILE A 387    11733  10056  10254   1356    587    251       O  
ATOM   3130  CB  ILE A 387       4.962  23.366 128.560  1.00 88.43           C  
ANISOU 3130  CB  ILE A 387    12030  10142  11427   1249    500    224       C  
ATOM   3131  CG1 ILE A 387       3.720  22.887 127.786  1.00 89.03           C  
ANISOU 3131  CG1 ILE A 387    12283  10149  11395   1159    532    565       C  
ATOM   3132  CG2 ILE A 387       5.584  24.665 127.975  1.00 90.55           C  
ANISOU 3132  CG2 ILE A 387    11873   9792  12741   1258    200    382       C  
ATOM   3133  CD1 ILE A 387       3.951  22.584 126.273  1.00 90.73           C  
ANISOU 3133  CD1 ILE A 387    12655  10338  11482   1035    475   1266       C  
ATOM   3134  N   LYS A 388       6.445  22.823 131.000  1.00 88.51           N  
ANISOU 3134  N   LYS A 388    11778  11484  10370   1287    723   -503       N  
ATOM   3135  CA  LYS A 388       7.185  23.368 132.147  1.00 92.14           C  
ANISOU 3135  CA  LYS A 388    11704  12635  10670   1309    735  -1222       C  
ATOM   3136  C   LYS A 388       8.536  22.653 132.281  1.00 89.89           C  
ANISOU 3136  C   LYS A 388    11739  12533   9884   1282    778   -614       C  
ATOM   3137  O   LYS A 388       9.606  23.291 132.350  1.00 90.74           O  
ANISOU 3137  O   LYS A 388    11733  12460  10283   1376    713   -900       O  
ATOM   3138  CB  LYS A 388       6.351  23.224 133.429  1.00 97.71           C  
ANISOU 3138  CB  LYS A 388    11755  14723  10647   1165    856  -1848       C  
ATOM   3139  CG  LYS A 388       7.142  23.287 134.739  1.00103.35           C  
ANISOU 3139  CG  LYS A 388    11795  16893  10580   1050    928  -2362       C  
ATOM   3140  CD  LYS A 388       6.205  23.236 135.952  1.00111.70           C  
ANISOU 3140  CD  LYS A 388    11897  19838  10706    811   1040  -3059       C  
ATOM   3141  CE  LYS A 388       5.921  24.627 136.518  1.00118.33           C  
ANISOU 3141  CE  LYS A 388    11657  21149  12154    945   1010  -5113       C  
ATOM   3142  NZ  LYS A 388       4.711  24.656 137.400  1.00125.72           N  
ANISOU 3142  NZ  LYS A 388    11606  23829  12332    737   1121  -6049       N  
ATOM   3143  N   GLN A 389       8.464  21.324 132.278  1.00 87.31           N  
ANISOU 3143  N   GLN A 389    11715  12414   9044   1154    836    241       N  
ATOM   3144  CA  GLN A 389       9.606  20.454 132.476  1.00 86.34           C  
ANISOU 3144  CA  GLN A 389    11726  12385   8693   1100    814    902       C  
ATOM   3145  C   GLN A 389      10.722  20.725 131.504  1.00 81.68           C  
ANISOU 3145  C   GLN A 389    11535  10947   8554   1263    767    903       C  
ATOM   3146  O   GLN A 389      11.864  20.942 131.906  1.00 82.01           O  
ANISOU 3146  O   GLN A 389    11501  11163   8498   1294    750    850       O  
ATOM   3147  CB  GLN A 389       9.146  19.003 132.356  1.00 87.67           C  
ANISOU 3147  CB  GLN A 389    11968  12429   8913    958    758   1805       C  
ATOM   3148  CG  GLN A 389       8.147  18.632 133.473  1.00 95.34           C  
ANISOU 3148  CG  GLN A 389    12364  14558   9305    690    755   2155       C  
ATOM   3149  CD  GLN A 389       7.569  17.249 133.323  1.00 99.92           C  
ANISOU 3149  CD  GLN A 389    12856  14805  10304    526    604   3193       C  
ATOM   3150  OE1 GLN A 389       8.278  16.300 132.946  1.00 99.62           O  
ANISOU 3150  OE1 GLN A 389    12857  13986  11007    538    435   3807       O  
ATOM   3151  NE2 GLN A 389       6.268  17.110 133.636  1.00104.09           N  
ANISOU 3151  NE2 GLN A 389    13120  15868  10560    370    622   3330       N  
ATOM   3152  N   ASN A 390      10.366  20.741 130.224  1.00 77.46           N  
ANISOU 3152  N   ASN A 390    11307   9720   8403   1322    742    971       N  
ATOM   3153  CA  ASN A 390      11.310  20.924 129.166  1.00 74.17           C  
ANISOU 3153  CA  ASN A 390    11079   8893   8212   1382    691   1061       C  
ATOM   3154  C   ASN A 390      11.940  22.327 129.148  1.00 75.06           C  
ANISOU 3154  C   ASN A 390    10994   8860   8666   1439    582    831       C  
ATOM   3155  O   ASN A 390      13.154  22.462 128.935  1.00 74.39           O  
ANISOU 3155  O   ASN A 390    10954   8714   8596   1471    542    941       O  
ATOM   3156  CB  ASN A 390      10.625  20.561 127.859  1.00 73.56           C  
ANISOU 3156  CB  ASN A 390    11092   8634   8225   1330    689   1178       C  
ATOM   3157  CG  ASN A 390      10.515  19.046 127.671  1.00 71.42           C  
ANISOU 3157  CG  ASN A 390    10848   8280   8011   1317    728   1217       C  
ATOM   3158  OD1 ASN A 390      11.509  18.370 127.628  1.00 72.86           O  
ANISOU 3158  OD1 ASN A 390    10973   8355   8357   1354    698   1194       O  
ATOM   3159  ND2 ASN A 390       9.324  18.536 127.548  1.00 68.07           N  
ANISOU 3159  ND2 ASN A 390    10393   7792   7678   1270    748   1227       N  
ATOM   3160  N   CYS A 391      11.148  23.361 129.426  1.00 76.56           N  
ANISOU 3160  N   CYS A 391    10836   8917   9337   1455    490    460       N  
ATOM   3161  CA  CYS A 391      11.721  24.697 129.560  1.00 79.49           C  
ANISOU 3161  CA  CYS A 391    10748   8922  10532   1521    287    138       C  
ATOM   3162  C   CYS A 391      12.656  24.860 130.761  1.00 79.92           C  
ANISOU 3162  C   CYS A 391    10584   9401  10380   1607    350   -480       C  
ATOM   3163  O   CYS A 391      13.621  25.580 130.678  1.00 80.23           O  
ANISOU 3163  O   CYS A 391    10413   9111  10959   1665    205   -556       O  
ATOM   3164  CB  CYS A 391      10.657  25.780 129.495  1.00 84.59           C  
ANISOU 3164  CB  CYS A 391    10814   9080  12246   1530     72   -224       C  
ATOM   3165  SG  CYS A 391       9.822  25.800 127.865  1.00 89.12           S  
ANISOU 3165  SG  CYS A 391    11465   9279  13116   1343    -97    854       S  
ATOM   3166  N   ASP A 392      12.422  24.129 131.840  1.00 80.45           N  
ANISOU 3166  N   ASP A 392    10613  10355   9600   1559    542   -755       N  
ATOM   3167  CA  ASP A 392      13.352  24.135 132.987  1.00 83.48           C  
ANISOU 3167  CA  ASP A 392    10669  11559   9490   1550    610  -1171       C  
ATOM   3168  C   ASP A 392      14.694  23.456 132.659  1.00 79.22           C  
ANISOU 3168  C   ASP A 392    10613  10829   8657   1554    624   -428       C  
ATOM   3169  O   ASP A 392      15.767  24.039 132.809  1.00 79.40           O  
ANISOU 3169  O   ASP A 392    10506  10754   8909   1633    565   -685       O  
ATOM   3170  CB  ASP A 392      12.691  23.494 134.218  1.00 87.68           C  
ANISOU 3170  CB  ASP A 392    10772  13514   9029   1362    757  -1339       C  
ATOM   3171  CG  ASP A 392      11.426  24.249 134.677  1.00 96.32           C  
ANISOU 3171  CG  ASP A 392    11183  15067  10347   1359    762  -2422       C  
ATOM   3172  OD1 ASP A 392      11.332  25.504 134.550  1.00101.07           O  
ANISOU 3172  OD1 ASP A 392    11284  15061  12056   1529    618  -3488       O  
ATOM   3173  OD2 ASP A 392      10.503  23.580 135.194  1.00103.37           O  
ANISOU 3173  OD2 ASP A 392    11885  16922  10468   1168    866  -2213       O  
ATOM   3174  N   GLN A 393      14.608  22.217 132.207  1.00 75.51           N  
ANISOU 3174  N   GLN A 393    10587  10241   7862   1479    675    376       N  
ATOM   3175  CA  GLN A 393      15.742  21.493 131.676  1.00 73.54           C  
ANISOU 3175  CA  GLN A 393    10679   9635   7628   1504    653    900       C  
ATOM   3176  C   GLN A 393      16.481  22.386 130.643  1.00 71.44           C  
ANISOU 3176  C   GLN A 393    10546   8782   7814   1607    570    779       C  
ATOM   3177  O   GLN A 393      17.727  22.464 130.658  1.00 70.67           O  
ANISOU 3177  O   GLN A 393    10496   8650   7704   1652    544    836       O  
ATOM   3178  CB  GLN A 393      15.233  20.204 131.023  1.00 72.35           C  
ANISOU 3178  CB  GLN A 393    10741   9158   7591   1449    650   1397       C  
ATOM   3179  CG  GLN A 393      16.149  19.012 131.084  1.00 75.35           C  
ANISOU 3179  CG  GLN A 393    11089   9352   8186   1425    575   1857       C  
ATOM   3180  CD  GLN A 393      15.642  17.801 130.251  1.00 78.52           C  
ANISOU 3180  CD  GLN A 393    11453   9185   9197   1419    504   1974       C  
ATOM   3181  OE1 GLN A 393      14.733  17.919 129.415  1.00 78.27           O  
ANISOU 3181  OE1 GLN A 393    11530   9017   9191   1437    563   1667       O  
ATOM   3182  NE2 GLN A 393      16.227  16.634 130.503  1.00 80.58           N  
ANISOU 3182  NE2 GLN A 393    11398   9094  10125   1381    332   2382       N  
ATOM   3183  N   PHE A 394      15.716  23.075 129.784  1.00 70.59           N  
ANISOU 3183  N   PHE A 394    10377   8317   8125   1592    485    771       N  
ATOM   3184  CA  PHE A 394      16.319  23.954 128.784  1.00 70.87           C  
ANISOU 3184  CA  PHE A 394    10272   8017   8638   1565    308   1054       C  
ATOM   3185  C   PHE A 394      17.034  25.132 129.437  1.00 74.94           C  
ANISOU 3185  C   PHE A 394    10387   8279   9806   1649    151    701       C  
ATOM   3186  O   PHE A 394      18.198  25.361 129.089  1.00 75.80           O  
ANISOU 3186  O   PHE A 394    10495   8314   9992   1644     71    980       O  
ATOM   3187  CB  PHE A 394      15.331  24.465 127.677  1.00 71.08           C  
ANISOU 3187  CB  PHE A 394    10073   7867   9066   1427    153   1480       C  
ATOM   3188  CG  PHE A 394      15.900  25.606 126.819  1.00 68.87           C  
ANISOU 3188  CG  PHE A 394     9291   7379   9498   1286   -167   2139       C  
ATOM   3189  CD1 PHE A 394      16.758  25.352 125.732  1.00 66.53           C  
ANISOU 3189  CD1 PHE A 394     8931   7667   8681   1104   -200   2771       C  
ATOM   3190  CD2 PHE A 394      15.618  26.930 127.118  1.00 71.85           C  
ANISOU 3190  CD2 PHE A 394     9041   7049  11211   1300   -491   2125       C  
ATOM   3191  CE1 PHE A 394      17.279  26.412 124.934  1.00 67.87           C  
ANISOU 3191  CE1 PHE A 394     8434   7893   9461    864   -564   3731       C  
ATOM   3192  CE2 PHE A 394      16.160  27.992 126.339  1.00 73.57           C  
ANISOU 3192  CE2 PHE A 394     8567   6939  12448   1108   -917   3064       C  
ATOM   3193  CZ  PHE A 394      16.988  27.714 125.255  1.00 71.40           C  
ANISOU 3193  CZ  PHE A 394     8267   7431  11430    858   -951   4023       C  
ATOM   3194  N   GLU A 395      16.351  25.902 130.310  1.00 78.74           N  
ANISOU 3194  N   GLU A 395    10389   8663  10866   1721     84    -42       N  
ATOM   3195  CA  GLU A 395      17.005  27.056 130.941  1.00 84.38           C  
ANISOU 3195  CA  GLU A 395    10464   9086  12509   1826   -107   -730       C  
ATOM   3196  C   GLU A 395      18.209  26.546 131.688  1.00 82.89           C  
ANISOU 3196  C   GLU A 395    10498   9499  11496   1873     72   -919       C  
ATOM   3197  O   GLU A 395      19.269  27.168 131.680  1.00 84.74           O  
ANISOU 3197  O   GLU A 395    10521   9434  12244   1930    -68   -984       O  
ATOM   3198  CB  GLU A 395      16.146  27.831 131.954  1.00 90.59           C  
ANISOU 3198  CB  GLU A 395    10440   9967  14015   1917   -169  -2040       C  
ATOM   3199  CG  GLU A 395      14.634  27.883 131.763  1.00 95.50           C  
ANISOU 3199  CG  GLU A 395    10893  10446  14948   1878   -197  -2183       C  
ATOM   3200  CD  GLU A 395      14.126  28.774 130.617  1.00100.21           C  
ANISOU 3200  CD  GLU A 395    11114   9848  17114   1822   -601  -1502       C  
ATOM   3201  OE1 GLU A 395      14.964  29.318 129.856  1.00101.01           O  
ANISOU 3201  OE1 GLU A 395    11055   9323  18003   1756   -888   -664       O  
ATOM   3202  OE2 GLU A 395      12.870  28.897 130.476  1.00102.18           O  
ANISOU 3202  OE2 GLU A 395    11144   9906  17774   1793   -658  -1646       O  
ATOM   3203  N   LYS A 396      18.029  25.406 132.337  1.00 81.03           N  
ANISOU 3203  N   LYS A 396    10589  10100  10100   1815    330   -861       N  
ATOM   3204  CA  LYS A 396      19.071  24.796 133.120  1.00 81.02           C  
ANISOU 3204  CA  LYS A 396    10670  10782   9334   1793    453   -800       C  
ATOM   3205  C   LYS A 396      20.309  24.544 132.245  1.00 78.02           C  
ANISOU 3205  C   LYS A 396    10755   9849   9040   1830    402   -132       C  
ATOM   3206  O   LYS A 396      21.403  25.018 132.589  1.00 79.57           O  
ANISOU 3206  O   LYS A 396    10792  10075   9365   1891    354   -359       O  
ATOM   3207  CB  LYS A 396      18.541  23.514 133.768  1.00 80.77           C  
ANISOU 3207  CB  LYS A 396    10732  11605   8350   1631    607   -346       C  
ATOM   3208  CG  LYS A 396      19.218  23.099 135.061  1.00 85.19           C  
ANISOU 3208  CG  LYS A 396    10871  13398   8100   1489    668   -314       C  
ATOM   3209  CD  LYS A 396      18.773  21.698 135.477  1.00 88.26           C  
ANISOU 3209  CD  LYS A 396    11231  14412   7893   1243    675    734       C  
ATOM   3210  CE  LYS A 396      19.779  21.051 136.429  1.00 95.70           C  
ANISOU 3210  CE  LYS A 396    11781  16326   8254   1037    621   1423       C  
ATOM   3211  NZ  LYS A 396      21.130  20.846 135.798  1.00 93.21           N  
ANISOU 3211  NZ  LYS A 396    11958  15012   8445   1200    556   1725       N  
ATOM   3212  N   LEU A 397      20.148  23.851 131.105  1.00 74.29           N  
ANISOU 3212  N   LEU A 397    10717   9014   8496   1785    411    520       N  
ATOM   3213  CA  LEU A 397      21.312  23.342 130.387  1.00 71.25           C  
ANISOU 3213  CA  LEU A 397    10603   8502   7966   1787    408    924       C  
ATOM   3214  C   LEU A 397      21.806  24.206 129.242  1.00 71.92           C  
ANISOU 3214  C   LEU A 397    10554   8316   8457   1741    244   1216       C  
ATOM   3215  O   LEU A 397      22.957  24.082 128.849  1.00 71.44           O  
ANISOU 3215  O   LEU A 397    10548   8350   8246   1734    229   1399       O  
ATOM   3216  CB  LEU A 397      21.042  21.928 129.886  1.00 69.79           C  
ANISOU 3216  CB  LEU A 397    10654   8349   7515   1742    494   1186       C  
ATOM   3217  CG  LEU A 397      20.888  20.787 130.872  1.00 70.58           C  
ANISOU 3217  CG  LEU A 397    10715   8636   7467   1708    532   1382       C  
ATOM   3218  CD1 LEU A 397      19.975  19.694 130.306  1.00 68.14           C  
ANISOU 3218  CD1 LEU A 397    10411   8080   7398   1661    526   1525       C  
ATOM   3219  CD2 LEU A 397      22.284  20.224 131.292  1.00 71.10           C  
ANISOU 3219  CD2 LEU A 397    10738   8713   7564   1729    486   1596       C  
ATOM   3220  N   GLY A 398      20.953  25.083 128.712  1.00 74.62           N  
ANISOU 3220  N   GLY A 398    10584   8401   9368   1662     75   1396       N  
ATOM   3221  CA  GLY A 398      21.265  25.844 127.491  1.00 77.83           C  
ANISOU 3221  CA  GLY A 398    10611   8781  10180   1477   -178   2145       C  
ATOM   3222  C   GLY A 398      21.053  24.953 126.263  1.00 78.14           C  
ANISOU 3222  C   GLY A 398    10735   9553   9402   1293    -72   2514       C  
ATOM   3223  O   GLY A 398      21.019  23.707 126.387  1.00 75.84           O  
ANISOU 3223  O   GLY A 398    10815   9497   8502   1382    176   2032       O  
ATOM   3224  N   GLU A 399      20.933  25.581 125.096  1.00 69.41           N  
ANISOU 3224  N   GLU A 399     5603  11761   9009   -527   1577  -3416       N  
ATOM   3225  CA  GLU A 399      20.584  24.936 123.850  1.00 68.11           C  
ANISOU 3225  CA  GLU A 399     5985  11065   8830   -334   1388  -2810       C  
ATOM   3226  C   GLU A 399      21.395  23.636 123.474  1.00 66.90           C  
ANISOU 3226  C   GLU A 399     5872  11236   8311   -215   1229  -2503       C  
ATOM   3227  O   GLU A 399      20.782  22.600 123.169  1.00 63.73           O  
ANISOU 3227  O   GLU A 399     5654  10802   7759     33    940  -2020       O  
ATOM   3228  CB  GLU A 399      20.593  25.971 122.716  1.00 69.81           C  
ANISOU 3228  CB  GLU A 399     6708  10429   9387   -452   1656  -2789       C  
ATOM   3229  CG  GLU A 399      20.296  25.405 121.259  1.00 70.72           C  
ANISOU 3229  CG  GLU A 399     7486   9965   9422   -234   1460  -2184       C  
ATOM   3230  CD  GLU A 399      19.915  26.540 120.281  1.00 76.27           C  
ANISOU 3230  CD  GLU A 399     8780   9786  10412   -220   1665  -2094       C  
ATOM   3231  OE1 GLU A 399      19.404  27.566 120.750  1.00 81.91           O  
ANISOU 3231  OE1 GLU A 399     9393  10286  11444   -268   1818  -2362       O  
ATOM   3232  OE2 GLU A 399      20.109  26.445 119.062  1.00 76.96           O  
ANISOU 3232  OE2 GLU A 399     9465   9375  10401   -138   1695  -1756       O  
ATOM   3233  N   TYR A 400      22.732  23.707 123.495  1.00 68.26           N  
ANISOU 3233  N   TYR A 400     5841  11693   8402   -396   1444  -2836       N  
ATOM   3234  CA  TYR A 400      23.585  22.564 123.187  1.00 68.25           C  
ANISOU 3234  CA  TYR A 400     5817  12000   8116   -282   1324  -2625       C  
ATOM   3235  C   TYR A 400      23.347  21.440 124.184  1.00 68.00           C  
ANISOU 3235  C   TYR A 400     5474  12656   7706     19   1001  -2426       C  
ATOM   3236  O   TYR A 400      23.116  20.288 123.769  1.00 67.04           O  
ANISOU 3236  O   TYR A 400     5569  12487   7418    248    801  -1919       O  
ATOM   3237  CB  TYR A 400      25.061  22.963 123.172  1.00 70.48           C  
ANISOU 3237  CB  TYR A 400     5811  12511   8456   -540   1631  -3171       C  
ATOM   3238  CG  TYR A 400      26.055  21.911 122.717  1.00 72.34           C  
ANISOU 3238  CG  TYR A 400     6013  12978   8496   -448   1560  -3032       C  
ATOM   3239  CD1 TYR A 400      25.823  21.108 121.587  1.00 68.41           C  
ANISOU 3239  CD1 TYR A 400     6027  12017   7949   -329   1467  -2450       C  
ATOM   3240  CD2 TYR A 400      27.287  21.778 123.368  1.00 75.49           C  
ANISOU 3240  CD2 TYR A 400     5836  14054   8792   -486   1599  -3563       C  
ATOM   3241  CE1 TYR A 400      26.763  20.187 121.164  1.00 66.22           C  
ANISOU 3241  CE1 TYR A 400     5697  11917   7547   -270   1452  -2370       C  
ATOM   3242  CE2 TYR A 400      28.225  20.872 122.964  1.00 73.00           C  
ANISOU 3242  CE2 TYR A 400     5441  13936   8361   -386   1544  -3494       C  
ATOM   3243  CZ  TYR A 400      27.977  20.066 121.856  1.00 73.54           C  
ANISOU 3243  CZ  TYR A 400     6035  13500   8408   -292   1495  -2884       C  
ATOM   3244  OH  TYR A 400      28.977  19.160 121.432  1.00 69.47           O  
ANISOU 3244  OH  TYR A 400     5413  13158   7825   -213   1484  -2860       O  
ATOM   3245  N   GLY A 401      23.360  21.775 125.477  1.00 69.81           N  
ANISOU 3245  N   GLY A 401     5245  13485   7795     22    991  -2819       N  
ATOM   3246  CA  GLY A 401      23.234  20.801 126.529  1.00 69.99           C  
ANISOU 3246  CA  GLY A 401     5028  14187   7378    330    754  -2654       C  
ATOM   3247  C   GLY A 401      21.861  20.176 126.481  1.00 69.05           C  
ANISOU 3247  C   GLY A 401     5211  13755   7268    512    624  -2118       C  
ATOM   3248  O   GLY A 401      21.650  19.085 127.026  1.00 69.81           O  
ANISOU 3248  O   GLY A 401     5300  14191   7032    793    495  -1781       O  
ATOM   3249  N   PHE A 402      20.904  20.880 125.874  1.00 67.10           N  
ANISOU 3249  N   PHE A 402     5219  12856   7419    373    682  -2072       N  
ATOM   3250  CA  PHE A 402      19.541  20.407 125.846  1.00 64.24           C  
ANISOU 3250  CA  PHE A 402     5043  12202   7163    520    562  -1715       C  
ATOM   3251  C   PHE A 402      19.406  19.469 124.658  1.00 61.98           C  
ANISOU 3251  C   PHE A 402     5137  11495   6919    653    425  -1221       C  
ATOM   3252  O   PHE A 402      18.675  18.500 124.718  1.00 60.15           O  
ANISOU 3252  O   PHE A 402     4981  11232   6641    831    331   -889       O  
ATOM   3253  CB  PHE A 402      18.557  21.577 125.732  1.00 64.46           C  
ANISOU 3253  CB  PHE A 402     5120  11749   7621    376    626  -1940       C  
ATOM   3254  CG  PHE A 402      17.112  21.188 125.841  1.00 60.10           C  
ANISOU 3254  CG  PHE A 402     4630  10954   7250    515    508  -1727       C  
ATOM   3255  CD1 PHE A 402      16.642  20.470 126.921  1.00 57.75           C  
ANISOU 3255  CD1 PHE A 402     4124  11088   6731    617    546  -1678       C  
ATOM   3256  CD2 PHE A 402      16.219  21.553 124.864  1.00 61.89           C  
ANISOU 3256  CD2 PHE A 402     5129  10517   7871    561    378  -1610       C  
ATOM   3257  CE1 PHE A 402      15.302  20.105 127.040  1.00 58.98           C  
ANISOU 3257  CE1 PHE A 402     4294  10988   7126    695    525  -1567       C  
ATOM   3258  CE2 PHE A 402      14.826  21.220 124.970  1.00 62.79           C  
ANISOU 3258  CE2 PHE A 402     5201  10418   8238    688    257  -1535       C  
ATOM   3259  CZ  PHE A 402      14.373  20.479 126.072  1.00 61.28           C  
ANISOU 3259  CZ  PHE A 402     4751  10637   7893    719    367  -1539       C  
ATOM   3260  N   GLN A 403      20.127  19.766 123.576  1.00 62.14           N  
ANISOU 3260  N   GLN A 403     5399  11177   7036    542    468  -1213       N  
ATOM   3261  CA  GLN A 403      20.144  18.890 122.398  1.00 59.80           C  
ANISOU 3261  CA  GLN A 403     5468  10522   6731    645    355   -797       C  
ATOM   3262  C   GLN A 403      20.700  17.516 122.750  1.00 60.15           C  
ANISOU 3262  C   GLN A 403     5380  11008   6465    826    311   -545       C  
ATOM   3263  O   GLN A 403      20.086  16.545 122.368  1.00 60.66           O  
ANISOU 3263  O   GLN A 403     5613  10891   6544    976    213   -189       O  
ATOM   3264  CB  GLN A 403      20.916  19.474 121.221  1.00 59.23           C  
ANISOU 3264  CB  GLN A 403     5724  10024   6758    474    486   -853       C  
ATOM   3265  CG  GLN A 403      20.352  20.716 120.701  1.00 57.01           C  
ANISOU 3265  CG  GLN A 403     5717   9187   6756    373    554   -981       C  
ATOM   3266  CD  GLN A 403      21.235  21.387 119.680  1.00 59.23           C  
ANISOU 3266  CD  GLN A 403     6369   9041   7094    181    820  -1062       C  
ATOM   3267  OE1 GLN A 403      22.461  21.246 119.675  1.00 63.65           O  
ANISOU 3267  OE1 GLN A 403     6794   9833   7557     17   1042  -1247       O  
ATOM   3268  NE2 GLN A 403      20.618  22.135 118.799  1.00 62.12           N  
ANISOU 3268  NE2 GLN A 403     7222   8760   7623    220    823   -941       N  
ATOM   3269  N   ASN A 404      21.829  17.441 123.459  1.00 61.61           N  
ANISOU 3269  N   ASN A 404     5255  11754   6399    836    384   -759       N  
ATOM   3270  CA  ASN A 404      22.359  16.204 124.003  1.00 61.82           C  
ANISOU 3270  CA  ASN A 404     5135  12259   6093   1102    324   -526       C  
ATOM   3271  C   ASN A 404      21.373  15.622 125.041  1.00 64.05           C  
ANISOU 3271  C   ASN A 404     5356  12769   6210   1316    299   -312       C  
ATOM   3272  O   ASN A 404      21.314  14.434 125.295  1.00 65.10           O  
ANISOU 3272  O   ASN A 404     5555  13035   6145   1570    304     57       O  
ATOM   3273  CB  ASN A 404      23.735  16.473 124.662  1.00 63.92           C  
ANISOU 3273  CB  ASN A 404     5009  13153   6125   1114    346   -929       C  
ATOM   3274  CG  ASN A 404      24.717  17.222 123.735  1.00 62.53           C  
ANISOU 3274  CG  ASN A 404     4845  12723   6190    817    497  -1278       C  
ATOM   3275  OD1 ASN A 404      24.565  17.234 122.538  1.00 62.79           O  
ANISOU 3275  OD1 ASN A 404     5259  12155   6444    681    572  -1083       O  
ATOM   3276  ND2 ASN A 404      25.708  17.841 124.301  1.00 67.13           N  
ANISOU 3276  ND2 ASN A 404     5018  13768   6722    718    570  -1826       N  
ATOM   3277  N   ALA A 405      20.572  16.447 125.666  1.00 65.66           N  
ANISOU 3277  N   ALA A 405     5454  12977   6515   1208    336   -549       N  
ATOM   3278  CA  ALA A 405      19.624  15.867 126.552  1.00 67.98           C  
ANISOU 3278  CA  ALA A 405     5734  13409   6686   1368    395   -359       C  
ATOM   3279  C   ALA A 405      18.592  15.098 125.716  1.00 66.56           C  
ANISOU 3279  C   ALA A 405     5835  12642   6812   1398    398      3       C  
ATOM   3280  O   ALA A 405      18.159  14.034 126.113  1.00 67.20           O  
ANISOU 3280  O   ALA A 405     5986  12764   6781   1576    515    307       O  
ATOM   3281  CB  ALA A 405      18.957  16.925 127.371  1.00 69.39           C  
ANISOU 3281  CB  ALA A 405     5717  13692   6955   1216    465   -742       C  
ATOM   3282  N   LEU A 406      18.220  15.649 124.559  1.00 65.54           N  
ANISOU 3282  N   LEU A 406     5877  11969   7057   1238    287    -60       N  
ATOM   3283  CA  LEU A 406      17.112  15.101 123.756  1.00 64.78           C  
ANISOU 3283  CA  LEU A 406     5976  11355   7284   1267    222    138       C  
ATOM   3284  C   LEU A 406      17.629  13.891 122.982  1.00 63.67           C  
ANISOU 3284  C   LEU A 406     6026  11113   7054   1375    220    484       C  
ATOM   3285  O   LEU A 406      16.974  12.860 122.909  1.00 64.38           O  
ANISOU 3285  O   LEU A 406     6167  11046   7249   1470    301    699       O  
ATOM   3286  CB  LEU A 406      16.480  16.174 122.837  1.00 63.71           C  
ANISOU 3286  CB  LEU A 406     5978  10718   7512   1148     43    -63       C  
ATOM   3287  CG  LEU A 406      15.499  17.088 123.584  1.00 64.88           C  
ANISOU 3287  CG  LEU A 406     5917  10835   7898   1086     65   -372       C  
ATOM   3288  CD1 LEU A 406      15.394  18.385 122.903  1.00 65.34           C  
ANISOU 3288  CD1 LEU A 406     6111  10519   8198   1004    -60   -585       C  
ATOM   3289  CD2 LEU A 406      14.103  16.444 123.748  1.00 61.56           C  
ANISOU 3289  CD2 LEU A 406     5405  10217   7768   1163     69   -351       C  
ATOM   3290  N   ILE A 407      18.838  14.021 122.478  1.00 62.36           N  
ANISOU 3290  N   ILE A 407     5929  11040   6726   1338    187    485       N  
ATOM   3291  CA  ILE A 407      19.559  12.936 121.881  1.00 62.15           C  
ANISOU 3291  CA  ILE A 407     6028  10996   6591   1434    220    761       C  
ATOM   3292  C   ILE A 407      19.579  11.666 122.728  1.00 63.09           C  
ANISOU 3292  C   ILE A 407     6059  11399   6512   1679    379   1057       C  
ATOM   3293  O   ILE A 407      19.515  10.565 122.180  1.00 63.85           O  
ANISOU 3293  O   ILE A 407     6298  11274   6689   1765    458   1331       O  
ATOM   3294  CB  ILE A 407      21.012  13.309 121.673  1.00 62.46           C  
ANISOU 3294  CB  ILE A 407     6014  11265   6452   1369    233    618       C  
ATOM   3295  CG1 ILE A 407      21.139  14.262 120.519  1.00 62.17           C  
ANISOU 3295  CG1 ILE A 407     6225  10793   6605   1136    193    442       C  
ATOM   3296  CG2 ILE A 407      21.799  12.085 121.413  1.00 61.71           C  
ANISOU 3296  CG2 ILE A 407     5947  11274   6227   1528    294    885       C  
ATOM   3297  CD1 ILE A 407      22.456  14.119 119.800  1.00 64.73           C  
ANISOU 3297  CD1 ILE A 407     6625  11117   6853   1046    291    401       C  
ATOM   3298  N   VAL A 408      19.745  11.808 124.030  1.00 63.64           N  
ANISOU 3298  N   VAL A 408     5930  11952   6297   1807    452   1001       N  
ATOM   3299  CA  VAL A 408      19.708  10.670 124.926  1.00 64.81           C  
ANISOU 3299  CA  VAL A 408     6094  12347   6183   2098    645   1330       C  
ATOM   3300  C   VAL A 408      18.235  10.214 125.101  1.00 65.07           C  
ANISOU 3300  C   VAL A 408     6226  12010   6487   2056    856   1441       C  
ATOM   3301  O   VAL A 408      17.925   9.023 125.003  1.00 64.77           O  
ANISOU 3301  O   VAL A 408     6336  11749   6525   2182   1087   1756       O  
ATOM   3302  CB  VAL A 408      20.299  11.083 126.293  1.00 67.75           C  
ANISOU 3302  CB  VAL A 408     6259  13398   6084   2275    629   1191       C  
ATOM   3303  CG1 VAL A 408      19.824  10.184 127.377  1.00 69.72           C  
ANISOU 3303  CG1 VAL A 408     6624  13829   6039   2564    878   1516       C  
ATOM   3304  CG2 VAL A 408      21.849  11.148 126.255  1.00 69.25           C  
ANISOU 3304  CG2 VAL A 408     6277  14035   5999   2412    455   1074       C  
ATOM   3305  N   ARG A 409      17.325  11.167 125.362  1.00 64.93           N  
ANISOU 3305  N   ARG A 409     6098  11900   6670   1868    819   1133       N  
ATOM   3306  CA  ARG A 409      15.901  10.836 125.625  1.00 66.48           C  
ANISOU 3306  CA  ARG A 409     6298  11776   7184   1804   1042   1113       C  
ATOM   3307  C   ARG A 409      15.326  10.121 124.392  1.00 64.43           C  
ANISOU 3307  C   ARG A 409     6149  10972   7359   1735   1022   1188       C  
ATOM   3308  O   ARG A 409      14.781   9.042 124.481  1.00 66.80           O  
ANISOU 3308  O   ARG A 409     6513  11058   7811   1787   1326   1363       O  
ATOM   3309  CB  ARG A 409      15.113  12.088 126.094  1.00 66.90           C  
ANISOU 3309  CB  ARG A 409     6159  11843   7417   1623    973    702       C  
ATOM   3310  CG  ARG A 409      13.656  12.193 125.732  1.00 66.34           C  
ANISOU 3310  CG  ARG A 409     6008  11299   7900   1480   1007    481       C  
ATOM   3311  CD  ARG A 409      12.806  12.730 126.877  1.00 69.19           C  
ANISOU 3311  CD  ARG A 409     6183  11780   8327   1395   1227    214       C  
ATOM   3312  NE  ARG A 409      12.315  14.119 126.773  1.00 70.49           N  
ANISOU 3312  NE  ARG A 409     6155  11846   8784   1242    997   -214       N  
ATOM   3313  CZ  ARG A 409      12.977  15.228 127.146  1.00 72.25           C  
ANISOU 3313  CZ  ARG A 409     6295  12366   8791   1185    870   -407       C  
ATOM   3314  NH1 ARG A 409      14.250  15.205 127.583  1.00 71.48           N  
ANISOU 3314  NH1 ARG A 409     6238  12750   8171   1264    869   -279       N  
ATOM   3315  NH2 ARG A 409      12.381  16.393 127.032  1.00 70.66           N  
ANISOU 3315  NH2 ARG A 409     5940  11964   8942   1059    737   -779       N  
ATOM   3316  N   TYR A 410      15.593  10.663 123.234  1.00 61.01           N  
ANISOU 3316  N   TYR A 410     5770  10337   7074   1632    700   1063       N  
ATOM   3317  CA  TYR A 410      15.132  10.084 121.997  1.00 60.10           C  
ANISOU 3317  CA  TYR A 410     5765   9781   7288   1585    607   1076       C  
ATOM   3318  C   TYR A 410      15.876   8.835 121.491  1.00 58.67           C  
ANISOU 3318  C   TYR A 410     5736   9547   7008   1679    755   1397       C  
ATOM   3319  O   TYR A 410      15.330   8.054 120.769  1.00 59.37           O  
ANISOU 3319  O   TYR A 410     5868   9302   7387   1644    818   1399       O  
ATOM   3320  CB  TYR A 410      15.010  11.203 120.912  1.00 58.94           C  
ANISOU 3320  CB  TYR A 410     5704   9402   7288   1481    206    827       C  
ATOM   3321  CG  TYR A 410      13.596  11.747 120.874  1.00 60.12           C  
ANISOU 3321  CG  TYR A 410     5707   9298   7839   1442     72    508       C  
ATOM   3322  CD1 TYR A 410      13.142  12.747 121.769  1.00 59.81           C  
ANISOU 3322  CD1 TYR A 410     5482   9386   7858   1398     82    276       C  
ATOM   3323  CD2 TYR A 410      12.683  11.198 119.979  1.00 60.52           C  
ANISOU 3323  CD2 TYR A 410     5749   9003   8245   1457    -55    378       C  
ATOM   3324  CE1 TYR A 410      11.776  13.191 121.719  1.00 63.53           C  
ANISOU 3324  CE1 TYR A 410     5763   9597   8777   1385    -40    -64       C  
ATOM   3325  CE2 TYR A 410      11.376  11.630 119.907  1.00 65.11           C  
ANISOU 3325  CE2 TYR A 410     6124   9374   9240   1463   -219     15       C  
ATOM   3326  CZ  TYR A 410      10.908  12.620 120.751  1.00 66.90           C  
ANISOU 3326  CZ  TYR A 410     6168   9686   9566   1436   -217   -199       C  
ATOM   3327  OH  TYR A 410       9.553  12.962 120.573  1.00 72.16           O  
ANISOU 3327  OH  TYR A 410     6585  10109  10723   1470   -403   -608       O  
ATOM   3328  N   THR A 411      17.105   8.615 121.868  1.00 58.11           N  
ANISOU 3328  N   THR A 411     5708   9806   6563   1807    814   1619       N  
ATOM   3329  CA  THR A 411      17.735   7.364 121.450  1.00 58.06           C  
ANISOU 3329  CA  THR A 411     5823   9712   6525   1927    990   1921       C  
ATOM   3330  C   THR A 411      17.302   6.113 122.231  1.00 61.59           C  
ANISOU 3330  C   THR A 411     6305  10091   7005   2100   1432   2209       C  
ATOM   3331  O   THR A 411      17.287   5.004 121.669  1.00 62.00           O  
ANISOU 3331  O   THR A 411     6455   9843   7259   2128   1650   2379       O  
ATOM   3332  CB  THR A 411      19.228   7.475 121.459  1.00 57.21           C  
ANISOU 3332  CB  THR A 411     5720   9945   6074   2038    891   2021       C  
ATOM   3333  OG1 THR A 411      19.559   8.472 120.519  1.00 52.84           O  
ANISOU 3333  OG1 THR A 411     5212   9290   5576   1827    615   1761       O  
ATOM   3334  CG2 THR A 411      19.877   6.159 121.043  1.00 55.94           C  
ANISOU 3334  CG2 THR A 411     5661   9669   5925   2190   1085   2324       C  
ATOM   3335  N   ARG A 412      16.999   6.287 123.516  1.00 64.06           N  
ANISOU 3335  N   ARG A 412     6573  10663   7106   2215   1614   2262       N  
ATOM   3336  CA  ARG A 412      16.475   5.204 124.304  1.00 68.29           C  
ANISOU 3336  CA  ARG A 412     7227  11064   7656   2368   2123   2540       C  
ATOM   3337  C   ARG A 412      15.101   4.898 123.817  1.00 67.99           C  
ANISOU 3337  C   ARG A 412     7121  10511   8200   2118   2331   2298       C  
ATOM   3338  O   ARG A 412      14.623   3.790 123.986  1.00 70.96           O  
ANISOU 3338  O   ARG A 412     7597  10569   8794   2152   2826   2463       O  
ATOM   3339  CB  ARG A 412      16.339   5.596 125.768  1.00 71.71           C  
ANISOU 3339  CB  ARG A 412     7669  11883   7694   2516   2280   2594       C  
ATOM   3340  CG  ARG A 412      17.621   5.953 126.407  1.00 74.37           C  
ANISOU 3340  CG  ARG A 412     8001  12828   7429   2796   2042   2728       C  
ATOM   3341  CD  ARG A 412      17.375   6.202 127.838  1.00 76.69           C  
ANISOU 3341  CD  ARG A 412     8341  13497   7299   2960   2230   2773       C  
ATOM   3342  NE  ARG A 412      18.642   6.005 128.560  1.00 86.05           N  
ANISOU 3342  NE  ARG A 412     9585  15274   7835   3392   2091   3020       N  
ATOM   3343  CZ  ARG A 412      19.285   7.000 129.136  1.00 89.09           C  
ANISOU 3343  CZ  ARG A 412     9758  16263   7828   3446   1749   2740       C  
ATOM   3344  NH1 ARG A 412      18.723   8.207 129.077  1.00 89.69           N  
ANISOU 3344  NH1 ARG A 412     9610  16341   8129   3077   1594   2274       N  
ATOM   3345  NH2 ARG A 412      20.435   6.801 129.783  1.00 93.57           N  
ANISOU 3345  NH2 ARG A 412    10314  17425   7814   3876   1569   2882       N  
ATOM   3346  N   LYS A 413      14.460   5.923 123.266  1.00 65.98           N  
ANISOU 3346  N   LYS A 413     6684  10178   8207   1888   1970   1873       N  
ATOM   3347  CA  LYS A 413      13.059   5.888 122.869  1.00 65.69           C  
ANISOU 3347  CA  LYS A 413     6476   9742   8740   1676   2046   1496       C  
ATOM   3348  C   LYS A 413      12.856   5.025 121.595  1.00 65.16           C  
ANISOU 3348  C   LYS A 413     6414   9284   9059   1591   2039   1413       C  
ATOM   3349  O   LYS A 413      11.974   4.120 121.568  1.00 67.72           O  
ANISOU 3349  O   LYS A 413     6648   9256   9828   1495   2452   1277       O  
ATOM   3350  CB  LYS A 413      12.593   7.319 122.623  1.00 64.07           C  
ANISOU 3350  CB  LYS A 413     6098   9611   8637   1555   1572   1096       C  
ATOM   3351  CG  LYS A 413      11.580   7.876 123.609  1.00 63.85           C  
ANISOU 3351  CG  LYS A 413     5873   9608   8780   1471   1749    825       C  
ATOM   3352  CD  LYS A 413      11.006   9.229 123.085  1.00 61.71           C  
ANISOU 3352  CD  LYS A 413     5415   9283   8748   1377   1244    391       C  
ATOM   3353  CE  LYS A 413      10.296  10.091 124.147  1.00 65.84           C  
ANISOU 3353  CE  LYS A 413     5733   9926   9356   1302   1354    116       C  
ATOM   3354  NZ  LYS A 413       8.834   9.680 124.486  1.00 62.04           N  
ANISOU 3354  NZ  LYS A 413     4985   9137   9451   1170   1700   -251       N  
ATOM   3355  N   VAL A 414      13.685   5.307 120.593  1.00 60.93           N  
ANISOU 3355  N   VAL A 414     5983   8811   8356   1605   1631   1455       N  
ATOM   3356  CA  VAL A 414      13.637   4.715 119.251  1.00 60.32           C  
ANISOU 3356  CA  VAL A 414     5939   8443   8535   1521   1510   1331       C  
ATOM   3357  C   VAL A 414      15.029   4.404 118.682  1.00 58.90           C  
ANISOU 3357  C   VAL A 414     5977   8374   8027   1603   1431   1640       C  
ATOM   3358  O   VAL A 414      15.433   4.932 117.678  1.00 56.53           O  
ANISOU 3358  O   VAL A 414     5782   8068   7630   1542   1056   1529       O  
ATOM   3359  CB  VAL A 414      12.825   5.584 118.241  1.00 60.15           C  
ANISOU 3359  CB  VAL A 414     5817   8290   8747   1417    991    869       C  
ATOM   3360  CG1 VAL A 414      11.326   5.511 118.559  1.00 60.29           C  
ANISOU 3360  CG1 VAL A 414     5522   8108   9277   1329   1117    448       C  
ATOM   3361  CG2 VAL A 414      13.253   7.100 118.279  1.00 59.68           C  
ANISOU 3361  CG2 VAL A 414     5852   8468   8357   1457    544    850       C  
ATOM   3362  N   PRO A 415      15.735   3.454 119.320  1.00 60.19           N  
ANISOU 3362  N   PRO A 415     6228   8599   8040   1761   1838   2029       N  
ATOM   3363  CA  PRO A 415      17.096   3.119 119.076  1.00 58.54           C  
ANISOU 3363  CA  PRO A 415     6158   8546   7540   1894   1818   2319       C  
ATOM   3364  C   PRO A 415      17.336   2.663 117.641  1.00 58.70           C  
ANISOU 3364  C   PRO A 415     6251   8296   7755   1751   1715   2194       C  
ATOM   3365  O   PRO A 415      18.458   2.795 117.136  1.00 57.03           O  
ANISOU 3365  O   PRO A 415     6142   8212   7317   1774   1565   2288       O  
ATOM   3366  CB  PRO A 415      17.341   1.984 120.023  1.00 61.49           C  
ANISOU 3366  CB  PRO A 415     6603   8904   7858   2136   2336   2718       C  
ATOM   3367  CG  PRO A 415      16.239   2.054 121.045  1.00 64.43           C  
ANISOU 3367  CG  PRO A 415     6919   9226   8333   2129   2619   2670       C  
ATOM   3368  CD  PRO A 415      15.107   2.639 120.379  1.00 62.87           C  
ANISOU 3368  CD  PRO A 415     6545   8817   8526   1842   2394   2185       C  
ATOM   3369  N   GLN A 416      16.319   2.141 116.967  1.00 60.21           N  
ANISOU 3369  N   GLN A 416     6372   8137   8367   1591   1803   1923       N  
ATOM   3370  CA  GLN A 416      16.551   1.624 115.603  1.00 60.60           C  
ANISOU 3370  CA  GLN A 416     6499   7966   8560   1462   1723   1771       C  
ATOM   3371  C   GLN A 416      16.752   2.692 114.543  1.00 59.21           C  
ANISOU 3371  C   GLN A 416     6466   7867   8162   1361   1177   1543       C  
ATOM   3372  O   GLN A 416      17.465   2.445 113.550  1.00 58.13           O  
ANISOU 3372  O   GLN A 416     6498   7660   7927   1292   1119   1541       O  
ATOM   3373  CB  GLN A 416      15.433   0.725 115.123  1.00 63.24           C  
ANISOU 3373  CB  GLN A 416     6675   7940   9414   1318   1963   1450       C  
ATOM   3374  CG  GLN A 416      15.194  -0.464 116.022  1.00 67.88           C  
ANISOU 3374  CG  GLN A 416     7192   8307  10292   1382   2650   1666       C  
ATOM   3375  CD  GLN A 416      14.050  -0.241 117.031  1.00 72.33           C  
ANISOU 3375  CD  GLN A 416     7588   8826  11070   1363   2860   1528       C  
ATOM   3376  OE1 GLN A 416      13.368   0.868 117.141  1.00 68.16           O  
ANISOU 3376  OE1 GLN A 416     6931   8459  10508   1311   2451   1239       O  
ATOM   3377  NE2 GLN A 416      13.861  -1.293 117.833  1.00 73.46           N  
ANISOU 3377  NE2 GLN A 416     7760   8716  11434   1423   3560   1757       N  
ATOM   3378  N   VAL A 417      16.077   3.845 114.718  1.00 57.21           N  
ANISOU 3378  N   VAL A 417     6177   7712   7849   1357    825   1343       N  
ATOM   3379  CA  VAL A 417      16.246   4.947 113.795  1.00 55.92           C  
ANISOU 3379  CA  VAL A 417     6236   7571   7441   1317    354   1189       C  
ATOM   3380  C   VAL A 417      17.740   5.213 113.389  1.00 53.99           C  
ANISOU 3380  C   VAL A 417     6251   7434   6828   1288    363   1409       C  
ATOM   3381  O   VAL A 417      18.621   5.025 114.174  1.00 51.26           O  
ANISOU 3381  O   VAL A 417     5831   7286   6361   1351    592   1650       O  
ATOM   3382  CB  VAL A 417      15.638   6.234 114.435  1.00 55.93           C  
ANISOU 3382  CB  VAL A 417     6166   7694   7390   1372     84   1071       C  
ATOM   3383  CG1 VAL A 417      15.897   7.438 113.546  1.00 55.01           C  
ANISOU 3383  CG1 VAL A 417     6363   7540   7000   1371   -326    982       C  
ATOM   3384  CG2 VAL A 417      14.112   6.107 114.688  1.00 56.83           C  
ANISOU 3384  CG2 VAL A 417     5993   7680   7920   1384     34    743       C  
ATOM   3385  N   SER A 418      18.053   5.714 112.204  1.00 49.21           N  
ANISOU 3385  N   SER A 418     6113   5235   7348    293   -720    257       N  
ATOM   3386  CA  SER A 418      19.482   5.783 111.890  1.00 51.44           C  
ANISOU 3386  CA  SER A 418     6303   5600   7640    417   -812    143       C  
ATOM   3387  C   SER A 418      20.180   6.919 112.648  1.00 51.97           C  
ANISOU 3387  C   SER A 418     6347   5850   7549    439   -853    170       C  
ATOM   3388  O   SER A 418      19.533   7.867 113.143  1.00 52.00           O  
ANISOU 3388  O   SER A 418     6397   5940   7421    348   -793    241       O  
ATOM   3389  CB  SER A 418      19.741   5.898 110.387  1.00 51.57           C  
ANISOU 3389  CB  SER A 418     6186   5702   7705    404   -773    -76       C  
ATOM   3390  OG  SER A 418      19.135   7.075 109.897  1.00 52.15           O  
ANISOU 3390  OG  SER A 418     6241   5934   7638    302   -681    -88       O  
ATOM   3391  N   THR A 419      21.497   6.860 112.726  1.00 52.27           N  
ANISOU 3391  N   THR A 419     6286   5951   7623    560   -953     74       N  
ATOM   3392  CA  THR A 419      22.160   7.832 113.539  1.00 52.68           C  
ANISOU 3392  CA  THR A 419     6286   6167   7563    577  -1012     51       C  
ATOM   3393  C   THR A 419      22.050   9.268 112.999  1.00 52.10           C  
ANISOU 3393  C   THR A 419     6128   6224   7444    424   -880    -44       C  
ATOM   3394  O   THR A 419      21.766  10.183 113.785  1.00 52.92           O  
ANISOU 3394  O   THR A 419     6266   6400   7439    367   -868     -8       O  
ATOM   3395  CB  THR A 419      23.605   7.482 113.732  1.00 54.23           C  
ANISOU 3395  CB  THR A 419     6344   6424   7837    742  -1161    -77       C  
ATOM   3396  OG1 THR A 419      23.666   6.304 114.529  1.00 55.28           O  
ANISOU 3396  OG1 THR A 419     6602   6430   7971    925  -1299     70       O  
ATOM   3397  CG2 THR A 419      24.317   8.640 114.417  1.00 52.27           C  
ANISOU 3397  CG2 THR A 419     5976   6373   7511    726  -1216   -191       C  
ATOM   3398  N   PRO A 420      22.277   9.474 111.681  1.00 51.76           N  
ANISOU 3398  N   PRO A 420     5988   6203   7475    373   -768   -158       N  
ATOM   3399  CA  PRO A 420      22.065  10.849 111.149  1.00 50.88           C  
ANISOU 3399  CA  PRO A 420     5848   6172   7314    243   -608   -183       C  
ATOM   3400  C   PRO A 420      20.634  11.466 111.397  1.00 50.09           C  
ANISOU 3400  C   PRO A 420     5888   6046   7098    159   -541    -44       C  
ATOM   3401  O   PRO A 420      20.568  12.661 111.672  1.00 50.60           O  
ANISOU 3401  O   PRO A 420     5948   6149   7128     86   -465    -43       O  
ATOM   3402  CB  PRO A 420      22.447  10.764 109.663  1.00 49.71           C  
ANISOU 3402  CB  PRO A 420     5620   6058   7211    242   -486   -281       C  
ATOM   3403  CG  PRO A 420      22.859   9.269 109.381  1.00 52.87           C  
ANISOU 3403  CG  PRO A 420     5981   6398   7709    367   -598   -360       C  
ATOM   3404  CD  PRO A 420      22.646   8.466 110.643  1.00 52.80           C  
ANISOU 3404  CD  PRO A 420     6059   6282   7720    445   -767   -257       C  
ATOM   3405  N   THR A 421      19.557  10.666 111.407  1.00 49.78           N  
ANISOU 3405  N   THR A 421     5947   5931   7037    167   -566     47       N  
ATOM   3406  CA  THR A 421      18.171  11.144 111.653  1.00 48.85           C  
ANISOU 3406  CA  THR A 421     5918   5803   6839     96   -505    146       C  
ATOM   3407  C   THR A 421      17.944  11.506 113.104  1.00 48.97           C  
ANISOU 3407  C   THR A 421     6002   5828   6778     81   -535    229       C  
ATOM   3408  O   THR A 421      17.398  12.550 113.400  1.00 48.51           O  
ANISOU 3408  O   THR A 421     5963   5814   6655     26   -467    244       O  
ATOM   3409  CB  THR A 421      17.088  10.068 111.316  1.00 48.86           C  
ANISOU 3409  CB  THR A 421     5959   5716   6890     88   -514    175       C  
ATOM   3410  OG1 THR A 421      17.071   9.830 109.922  1.00 49.73           O  
ANISOU 3410  OG1 THR A 421     6007   5861   7029    112   -495     61       O  
ATOM   3411  CG2 THR A 421      15.687  10.536 111.681  1.00 46.81           C  
ANISOU 3411  CG2 THR A 421     5745   5465   6577     16   -451    248       C  
ATOM   3412  N   LEU A 422      18.318  10.619 114.017  1.00 50.25           N  
ANISOU 3412  N   LEU A 422     6213   5950   6931    152   -635    288       N  
ATOM   3413  CA  LEU A 422      18.368  10.939 115.458  1.00 50.48           C  
ANISOU 3413  CA  LEU A 422     6312   6044   6822    184   -686    352       C  
ATOM   3414  C   LEU A 422      19.173  12.237 115.806  1.00 50.74           C  
ANISOU 3414  C   LEU A 422     6252   6211   6817    170   -709    205       C  
ATOM   3415  O   LEU A 422      18.679  13.068 116.564  1.00 49.12           O  
ANISOU 3415  O   LEU A 422     6086   6069   6508    129   -672    201       O  
ATOM   3416  CB  LEU A 422      18.866   9.723 116.276  1.00 52.76           C  
ANISOU 3416  CB  LEU A 422     6685   6279   7081    323   -808    459       C  
ATOM   3417  CG  LEU A 422      17.835   8.605 116.551  1.00 53.57           C  
ANISOU 3417  CG  LEU A 422     6934   6216   7205    310   -735    655       C  
ATOM   3418  CD1 LEU A 422      18.432   7.238 117.005  1.00 52.27           C  
ANISOU 3418  CD1 LEU A 422     6866   5911   7082    469   -831    785       C  
ATOM   3419  CD2 LEU A 422      16.707   9.094 117.513  1.00 49.77           C  
ANISOU 3419  CD2 LEU A 422     6560   5787   6564    234   -619    776       C  
ATOM   3420  N   VAL A 423      20.396  12.401 115.287  1.00 50.99           N  
ANISOU 3420  N   VAL A 423     6142   6278   6955    194   -755     57       N  
ATOM   3421  CA  VAL A 423      21.089  13.695 115.430  1.00 51.52           C  
ANISOU 3421  CA  VAL A 423     6085   6426   7066    128   -725   -117       C  
ATOM   3422  C   VAL A 423      20.223  14.905 114.902  1.00 53.05           C  
ANISOU 3422  C   VAL A 423     6311   6564   7280     -2   -537    -98       C  
ATOM   3423  O   VAL A 423      19.778  15.774 115.698  1.00 53.78           O  
ANISOU 3423  O   VAL A 423     6436   6683   7313    -41   -513   -131       O  
ATOM   3424  CB  VAL A 423      22.569  13.717 114.799  1.00 53.39           C  
ANISOU 3424  CB  VAL A 423     6117   6696   7471    140   -749   -303       C  
ATOM   3425  CG1 VAL A 423      23.222  15.053 115.007  1.00 49.69           C  
ANISOU 3425  CG1 VAL A 423     5503   6273   7103     34   -684   -500       C  
ATOM   3426  CG2 VAL A 423      23.493  12.610 115.377  1.00 48.78           C  
ANISOU 3426  CG2 VAL A 423     5476   6178   6881    314   -965   -348       C  
ATOM   3427  N   GLU A 424      19.944  14.960 113.599  1.00 52.49           N  
ANISOU 3427  N   GLU A 424     6243   6426   7276    -39   -412    -48       N  
ATOM   3428  CA  GLU A 424      19.213  16.101 113.048  1.00 53.50           C  
ANISOU 3428  CA  GLU A 424     6414   6499   7413   -108   -249     -6       C  
ATOM   3429  C   GLU A 424      17.903  16.419 113.808  1.00 53.62           C  
ANISOU 3429  C   GLU A 424     6533   6511   7328   -111   -247     71       C  
ATOM   3430  O   GLU A 424      17.595  17.593 114.078  1.00 53.49           O  
ANISOU 3430  O   GLU A 424     6527   6460   7336   -154   -160     37       O  
ATOM   3431  CB  GLU A 424      19.039  15.950 111.523  1.00 54.18           C  
ANISOU 3431  CB  GLU A 424     6516   6560   7511    -91   -144     60       C  
ATOM   3432  CG  GLU A 424      17.764  16.493 110.877  1.00 55.58           C  
ANISOU 3432  CG  GLU A 424     6791   6712   7614    -70    -55    176       C  
ATOM   3433  CD  GLU A 424      17.874  16.685 109.347  1.00 59.60           C  
ANISOU 3433  CD  GLU A 424     7320   7235   8091    -23     63    227       C  
ATOM   3434  OE1 GLU A 424      18.525  15.857 108.577  1.00 61.03           O  
ANISOU 3434  OE1 GLU A 424     7452   7473   8265     10     50    178       O  
ATOM   3435  OE2 GLU A 424      17.267  17.687 108.904  1.00 57.49           O  
ANISOU 3435  OE2 GLU A 424     7128   6929   7786      4    174    320       O  
ATOM   3436  N   VAL A 425      17.142  15.399 114.186  1.00 52.93           N  
ANISOU 3436  N   VAL A 425     6512   6443   7154    -72   -319    163       N  
ATOM   3437  CA  VAL A 425      15.858  15.674 114.845  1.00 52.24           C  
ANISOU 3437  CA  VAL A 425     6496   6366   6988    -86   -277    225       C  
ATOM   3438  C   VAL A 425      15.959  16.274 116.235  1.00 52.18           C  
ANISOU 3438  C   VAL A 425     6508   6424   6893    -92   -298    160       C  
ATOM   3439  O   VAL A 425      15.112  17.128 116.658  1.00 51.70           O  
ANISOU 3439  O   VAL A 425     6471   6370   6802   -113   -218    140       O  
ATOM   3440  CB  VAL A 425      15.059  14.427 114.972  1.00 53.41           C  
ANISOU 3440  CB  VAL A 425     6693   6499   7102    -74   -304    329       C  
ATOM   3441  CG1 VAL A 425      13.728  14.712 115.734  1.00 52.52           C  
ANISOU 3441  CG1 VAL A 425     6622   6412   6921   -105   -225    376       C  
ATOM   3442  CG2 VAL A 425      14.802  13.911 113.582  1.00 55.57           C  
ANISOU 3442  CG2 VAL A 425     6926   6730   7457    -65   -295    331       C  
ATOM   3443  N   SER A 426      16.976  15.807 116.962  1.00 52.35           N  
ANISOU 3443  N   SER A 426     6514   6513   6864    -47   -421    108       N  
ATOM   3444  CA  SER A 426      17.202  16.197 118.346  1.00 52.48           C  
ANISOU 3444  CA  SER A 426     6549   6649   6740    -12   -488     19       C  
ATOM   3445  C   SER A 426      17.772  17.649 118.396  1.00 52.42           C  
ANISOU 3445  C   SER A 426     6433   6641   6843    -75   -452   -206       C  
ATOM   3446  O   SER A 426      17.511  18.444 119.314  1.00 53.90           O  
ANISOU 3446  O   SER A 426     6626   6895   6957    -81   -442   -329       O  
ATOM   3447  CB  SER A 426      18.212  15.239 118.918  1.00 54.86           C  
ANISOU 3447  CB  SER A 426     6850   7036   6958     99   -662     22       C  
ATOM   3448  OG  SER A 426      17.693  13.942 119.202  1.00 55.65           O  
ANISOU 3448  OG  SER A 426     7083   7106   6954    168   -680    239       O  
ATOM   3449  N   ARG A 427      18.578  17.973 117.406  1.00 50.77           N  
ANISOU 3449  N   ARG A 427     6120   6344   6825   -128   -412   -272       N  
ATOM   3450  CA  ARG A 427      19.142  19.301 117.260  1.00 50.83           C  
ANISOU 3450  CA  ARG A 427     6020   6278   7013   -221   -320   -463       C  
ATOM   3451  C   ARG A 427      17.992  20.340 117.110  1.00 51.07           C  
ANISOU 3451  C   ARG A 427     6131   6192   7080   -260   -158   -417       C  
ATOM   3452  O   ARG A 427      17.858  21.258 117.928  1.00 51.39           O  
ANISOU 3452  O   ARG A 427     6152   6234   7140   -287   -138   -581       O  
ATOM   3453  CB  ARG A 427      20.141  19.295 116.105  1.00 48.65           C  
ANISOU 3453  CB  ARG A 427     5636   5918   6930   -275   -250   -486       C  
ATOM   3454  CG  ARG A 427      21.402  18.562 116.535  1.00 50.27           C  
ANISOU 3454  CG  ARG A 427     5704   6254   7142   -225   -427   -630       C  
ATOM   3455  CD  ARG A 427      22.698  18.709 115.651  1.00 50.45           C  
ANISOU 3455  CD  ARG A 427     5537   6232   7398   -297   -352   -760       C  
ATOM   3456  NE  ARG A 427      22.837  20.051 115.133  1.00 49.20           N  
ANISOU 3456  NE  ARG A 427     5323   5912   7457   -451   -119   -838       N  
ATOM   3457  CZ  ARG A 427      23.561  21.035 115.630  1.00 52.06           C  
ANISOU 3457  CZ  ARG A 427     5521   6239   8021   -563    -78  -1105       C  
ATOM   3458  NH1 ARG A 427      24.344  20.833 116.680  1.00 60.41           N  
ANISOU 3458  NH1 ARG A 427     6413   7472   9070   -523   -298  -1372       N  
ATOM   3459  NH2 ARG A 427      23.567  22.217 115.021  1.00 61.42           N  
ANISOU 3459  NH2 ARG A 427     6697   7204   9436   -708    188  -1116       N  
ATOM   3460  N   SER A 428      17.169  20.116 116.082  1.00 49.98           N  
ANISOU 3460  N   SER A 428     6074   5975   6943   -239    -67   -216       N  
ATOM   3461  CA  SER A 428      15.935  20.778 115.817  1.00 50.70           C  
ANISOU 3461  CA  SER A 428     6241   5987   7036   -216     43   -130       C  
ATOM   3462  C   SER A 428      14.986  20.720 116.994  1.00 52.12           C  
ANISOU 3462  C   SER A 428     6461   6269   7073   -183      6   -161       C  
ATOM   3463  O   SER A 428      14.487  21.731 117.397  1.00 53.73           O  
ANISOU 3463  O   SER A 428     6669   6421   7324   -184     83   -250       O  
ATOM   3464  CB  SER A 428      15.281  20.129 114.608  1.00 50.15           C  
ANISOU 3464  CB  SER A 428     6220   5904   6929   -159     65     60       C  
ATOM   3465  OG  SER A 428      16.146  20.183 113.478  1.00 48.49           O  
ANISOU 3465  OG  SER A 428     5988   5629   6808   -173    126     95       O  
ATOM   3466  N   LEU A 429      14.752  19.577 117.607  1.00 53.10           N  
ANISOU 3466  N   LEU A 429     6620   6525   7029   -152    -88    -93       N  
ATOM   3467  CA  LEU A 429      13.911  19.664 118.811  1.00 54.75           C  
ANISOU 3467  CA  LEU A 429     6874   6843   7087   -129    -72   -126       C  
ATOM   3468  C   LEU A 429      14.452  20.633 119.855  1.00 56.15           C  
ANISOU 3468  C   LEU A 429     7016   7079   7238   -135    -94   -362       C  
ATOM   3469  O   LEU A 429      13.655  21.359 120.517  1.00 57.51           O  
ANISOU 3469  O   LEU A 429     7201   7281   7368   -122    -16   -455       O  
ATOM   3470  CB  LEU A 429      13.691  18.315 119.467  1.00 55.16           C  
ANISOU 3470  CB  LEU A 429     6996   7011   6951    -97   -132      7       C  
ATOM   3471  CG  LEU A 429      12.869  17.297 118.693  1.00 57.09           C  
ANISOU 3471  CG  LEU A 429     7260   7194   7237   -111    -89    190       C  
ATOM   3472  CD1 LEU A 429      12.955  15.952 119.432  1.00 54.57           C  
ANISOU 3472  CD1 LEU A 429     7028   6930   6777    -87   -131    327       C  
ATOM   3473  CD2 LEU A 429      11.382  17.768 118.492  1.00 57.86           C  
ANISOU 3473  CD2 LEU A 429     7327   7276   7380   -126     42    201       C  
ATOM   3474  N   GLY A 430      15.778  20.633 120.023  1.00 55.72           N  
ANISOU 3474  N   GLY A 430     6894   7059   7219   -149   -205   -496       N  
ATOM   3475  CA  GLY A 430      16.445  21.484 121.043  1.00 56.51           C  
ANISOU 3475  CA  GLY A 430     6918   7247   7307   -155   -268   -794       C  
ATOM   3476  C   GLY A 430      16.363  22.982 120.741  1.00 56.57           C  
ANISOU 3476  C   GLY A 430     6858   7061   7574   -238   -128   -977       C  
ATOM   3477  O   GLY A 430      16.221  23.802 121.648  1.00 58.14           O  
ANISOU 3477  O   GLY A 430     7027   7306   7756   -236   -121  -1217       O  
ATOM   3478  N   LYS A 431      16.447  23.372 119.471  1.00 55.03           N  
ANISOU 3478  N   LYS A 431     6652   6639   7620   -297     -2   -866       N  
ATOM   3479  CA  LYS A 431      16.126  24.765 119.109  1.00 55.26           C  
ANISOU 3479  CA  LYS A 431     6673   6426   7896   -345    173   -950       C  
ATOM   3480  C   LYS A 431      14.679  25.206 119.449  1.00 56.18           C  
ANISOU 3480  C   LYS A 431     6873   6531   7943   -263    251   -908       C  
ATOM   3481  O   LYS A 431      14.430  26.413 119.653  1.00 59.39           O  
ANISOU 3481  O   LYS A 431     7264   6773   8530   -274    360  -1069       O  
ATOM   3482  CB  LYS A 431      16.509  25.080 117.690  1.00 54.79           C  
ANISOU 3482  CB  LYS A 431     6622   6135   8061   -394    315   -792       C  
ATOM   3483  CG  LYS A 431      17.990  24.880 117.406  1.00 56.26           C  
ANISOU 3483  CG  LYS A 431     6681   6315   8379   -497    290   -899       C  
ATOM   3484  CD  LYS A 431      18.420  25.021 115.937  1.00 60.23           C  
ANISOU 3484  CD  LYS A 431     7205   6629   9051   -542    463   -708       C  
ATOM   3485  CE  LYS A 431      20.021  25.177 115.830  1.00 67.48           C  
ANISOU 3485  CE  LYS A 431     7931   7508  10199   -689    500   -918       C  
ATOM   3486  NZ  LYS A 431      20.822  24.164 114.906  1.00 67.26           N  
ANISOU 3486  NZ  LYS A 431     7853   7571  10131   -688    485   -793       N  
ATOM   3487  N   VAL A 432      13.738  24.270 119.604  1.00 54.63           N  
ANISOU 3487  N   VAL A 432     6743   6497   7516   -187    207   -732       N  
ATOM   3488  CA  VAL A 432      12.394  24.619 120.143  1.00 55.40           C  
ANISOU 3488  CA  VAL A 432     6872   6640   7538   -116    281   -750       C  
ATOM   3489  C   VAL A 432      12.434  25.266 121.564  1.00 57.53           C  
ANISOU 3489  C   VAL A 432     7109   7027   7723   -112    273  -1053       C  
ATOM   3490  O   VAL A 432      11.492  25.950 121.969  1.00 58.27           O  
ANISOU 3490  O   VAL A 432     7201   7104   7836    -59    369  -1150       O  
ATOM   3491  CB  VAL A 432      11.423  23.434 120.100  1.00 53.40           C  
ANISOU 3491  CB  VAL A 432     6660   6541   7090    -71    266   -536       C  
ATOM   3492  CG1 VAL A 432      10.076  23.825 120.538  1.00 53.80           C  
ANISOU 3492  CG1 VAL A 432     6697   6634   7109    -10    368   -573       C  
ATOM   3493  CG2 VAL A 432      11.324  22.915 118.700  1.00 55.19           C  
ANISOU 3493  CG2 VAL A 432     6896   6666   7406    -61    261   -315       C  
ATOM   3494  N   GLY A 433      13.551  25.091 122.266  1.00 58.50           N  
ANISOU 3494  N   GLY A 433     7188   7277   7760   -150    147  -1232       N  
ATOM   3495  CA  GLY A 433      13.778  25.690 123.552  1.00 60.65           C  
ANISOU 3495  CA  GLY A 433     7415   7699   7930   -134    100  -1569       C  
ATOM   3496  C   GLY A 433      13.901  27.180 123.402  1.00 63.44           C  
ANISOU 3496  C   GLY A 433     7689   7792   8622   -190    208  -1835       C  
ATOM   3497  O   GLY A 433      13.148  27.949 124.048  1.00 64.63           O  
ANISOU 3497  O   GLY A 433     7838   7943   8777   -142    290  -2025       O  
ATOM   3498  N   THR A 434      14.836  27.567 122.532  1.00 63.68           N  
ANISOU 3498  N   THR A 434     7656   7584   8954   -292    235  -1842       N  
ATOM   3499  CA  THR A 434      15.163  28.947 122.164  1.00 65.97           C  
ANISOU 3499  CA  THR A 434     7879   7532   9654   -380    382  -2042       C  
ATOM   3500  C   THR A 434      13.970  29.602 121.448  1.00 66.79           C  
ANISOU 3500  C   THR A 434     8088   7378   9910   -301    568  -1840       C  
ATOM   3501  O   THR A 434      13.742  30.808 121.547  1.00 69.60           O  
ANISOU 3501  O   THR A 434     8429   7478  10538   -304    699  -2024       O  
ATOM   3502  CB  THR A 434      16.381  28.957 121.155  1.00 66.49           C  
ANISOU 3502  CB  THR A 434     7877   7400   9987   -514    424  -1974       C  
ATOM   3503  OG1 THR A 434      17.371  27.983 121.529  1.00 65.84           O  
ANISOU 3503  OG1 THR A 434     7703   7591   9721   -537    224  -2044       O  
ATOM   3504  CG2 THR A 434      17.049  30.345 120.991  1.00 66.50           C  
ANISOU 3504  CG2 THR A 434     7774   7044  10450   -657    592  -2248       C  
ATOM   3505  N   ARG A 435      13.224  28.818 120.691  1.00 65.45           N  
ANISOU 3505  N   ARG A 435     8015   7264   9588   -215    570  -1477       N  
ATOM   3506  CA  ARG A 435      12.065  29.350 119.990  1.00 66.46           C  
ANISOU 3506  CA  ARG A 435     8220   7205   9825    -95    698  -1291       C  
ATOM   3507  C   ARG A 435      10.993  29.651 120.996  1.00 67.30           C  
ANISOU 3507  C   ARG A 435     8306   7442   9822      0    711  -1468       C  
ATOM   3508  O   ARG A 435      10.429  30.724 120.957  1.00 70.37           O  
ANISOU 3508  O   ARG A 435     8700   7609  10429     75    828  -1565       O  
ATOM   3509  CB  ARG A 435      11.510  28.357 118.936  1.00 64.73           C  
ANISOU 3509  CB  ARG A 435     8070   7069   9454    -18    663   -916       C  
ATOM   3510  CG  ARG A 435      12.354  28.214 117.632  1.00 67.49           C  
ANISOU 3510  CG  ARG A 435     8466   7257   9922    -66    700   -697       C  
ATOM   3511  CD  ARG A 435      11.979  26.927 116.751  1.00 69.82           C  
ANISOU 3511  CD  ARG A 435     8800   7729  10000     -4    609   -407       C  
ATOM   3512  NE  ARG A 435      12.880  26.713 115.595  1.00 69.79           N  
ANISOU 3512  NE  ARG A 435     8832   7626  10059    -46    647   -239       N  
ATOM   3513  CZ  ARG A 435      12.967  27.543 114.547  1.00 71.54           C  
ANISOU 3513  CZ  ARG A 435     9138   7598  10445      6    799    -86       C  
ATOM   3514  NH1 ARG A 435      12.218  28.662 114.504  1.00 69.84           N  
ANISOU 3514  NH1 ARG A 435     8984   7175  10376    118    907    -73       N  
ATOM   3515  NH2 ARG A 435      13.813  27.274 113.556  1.00 70.00           N  
ANISOU 3515  NH2 ARG A 435     8975   7356  10267    -38    858     62       N  
ATOM   3516  N   CYS A 436      10.710  28.737 121.915  1.00 66.09           N  
ANISOU 3516  N   CYS A 436     8137   7635   9340      9    614  -1510       N  
ATOM   3517  CA  CYS A 436       9.459  28.862 122.676  1.00 67.06           C  
ANISOU 3517  CA  CYS A 436     8244   7906   9329    113    675  -1601       C  
ATOM   3518  C   CYS A 436       9.513  29.136 124.166  1.00 69.39           C  
ANISOU 3518  C   CYS A 436     8498   8422   9444    113    661  -1951       C  
ATOM   3519  O   CYS A 436       8.484  29.481 124.740  1.00 71.52           O  
ANISOU 3519  O   CYS A 436     8743   8774   9656    202    756  -2067       O  
ATOM   3520  CB  CYS A 436       8.587  27.631 122.487  1.00 65.64           C  
ANISOU 3520  CB  CYS A 436     8085   7945   8911    152    658  -1328       C  
ATOM   3521  SG  CYS A 436       8.234  27.268 120.773  1.00 65.31           S  
ANISOU 3521  SG  CYS A 436     8069   7725   9021    199    652   -973       S  
ATOM   3522  N   CYS A 437      10.665  28.974 124.807  1.00 69.41           N  
ANISOU 3522  N   CYS A 437     8481   8554   9339     36    539  -2140       N  
ATOM   3523  CA  CYS A 437      10.678  28.989 126.249  1.00 71.07           C  
ANISOU 3523  CA  CYS A 437     8672   9075   9258     75    492  -2442       C  
ATOM   3524  C   CYS A 437      10.896  30.332 126.812  1.00 73.83           C  
ANISOU 3524  C   CYS A 437     8934   9297   9823     71    529  -2893       C  
ATOM   3525  O   CYS A 437      10.721  30.499 128.003  1.00 76.60           O  
ANISOU 3525  O   CYS A 437     9264   9914   9927    132    510  -3190       O  
ATOM   3526  CB  CYS A 437      11.706  28.018 126.814  1.00 71.19           C  
ANISOU 3526  CB  CYS A 437     8710   9377   8963     54    301  -2434       C  
ATOM   3527  SG  CYS A 437      11.297  26.295 126.463  1.00 70.95           S  
ANISOU 3527  SG  CYS A 437     8803   9521   8633     79    279  -1930       S  
ATOM   3528  N   THR A 438      11.292  31.301 125.981  1.00 74.24           N  
ANISOU 3528  N   THR A 438     8940   8936  10332      1    600  -2955       N  
ATOM   3529  CA  THR A 438      11.369  32.715 126.452  1.00 76.55           C  
ANISOU 3529  CA  THR A 438     9146   9007  10934     -9    682  -3405       C  
ATOM   3530  C   THR A 438      10.105  33.518 126.252  1.00 75.93           C  
ANISOU 3530  C   THR A 438     9091   8710  11049    114    863  -3395       C  
ATOM   3531  O   THR A 438       9.984  34.592 126.825  1.00 80.10           O  
ANISOU 3531  O   THR A 438     9553   9097  11784    138    935  -3790       O  
ATOM   3532  CB  THR A 438      12.467  33.539 125.798  1.00 77.04           C  
ANISOU 3532  CB  THR A 438     9136   8668  11466   -160    718  -3539       C  
ATOM   3533  OG1 THR A 438      13.339  32.680 125.088  1.00 78.44           O  
ANISOU 3533  OG1 THR A 438     9326   8885  11595   -254    628  -3263       O  
ATOM   3534  CG2 THR A 438      13.238  34.281 126.859  1.00 82.62           C  
ANISOU 3534  CG2 THR A 438     9692   9431  12267   -234    647  -4134       C  
ATOM   3535  N   LYS A 439       9.226  33.038 125.386  1.00 72.14           N  
ANISOU 3535  N   LYS A 439     8686   8181  10542    199    924  -2975       N  
ATOM   3536  CA  LYS A 439       7.858  33.533 125.222  1.00 72.32           C  
ANISOU 3536  CA  LYS A 439     8710   8103  10667    365   1057  -2927       C  
ATOM   3537  C   LYS A 439       7.035  33.573 126.496  1.00 74.01           C  
ANISOU 3537  C   LYS A 439     8860   8636  10622    454   1101  -3222       C  
ATOM   3538  O   LYS A 439       7.278  32.784 127.396  1.00 73.62           O  
ANISOU 3538  O   LYS A 439     8815   8982  10176    411   1024  -3295       O  
ATOM   3539  CB  LYS A 439       7.120  32.663 124.199  1.00 68.95           C  
ANISOU 3539  CB  LYS A 439     8336   7719  10145    434   1052  -2455       C  
ATOM   3540  CG  LYS A 439       7.622  32.933 122.810  1.00 66.62           C  
ANISOU 3540  CG  LYS A 439     8115   7061  10136    419   1062  -2173       C  
ATOM   3541  CD  LYS A 439       6.553  32.743 121.791  1.00 66.27           C  
ANISOU 3541  CD  LYS A 439     8099   6958  10123    586   1087  -1843       C  
ATOM   3542  CE  LYS A 439       7.038  33.147 120.434  1.00 67.58           C  
ANISOU 3542  CE  LYS A 439     8371   6772  10535    612   1118  -1564       C  
ATOM   3543  NZ  LYS A 439       8.248  32.368 120.139  1.00 67.84           N  
ANISOU 3543  NZ  LYS A 439     8437   6880  10457    423   1042  -1447       N  
ATOM   3544  N   PRO A 440       6.043  34.489 126.567  1.00 76.51           N  
ANISOU 3544  N   PRO A 440     9127   8787  11155    601   1235  -3379       N  
ATOM   3545  CA  PRO A 440       5.071  34.541 127.659  1.00 78.76           C  
ANISOU 3545  CA  PRO A 440     9336   9378  11212    708   1323  -3640       C  
ATOM   3546  C   PRO A 440       4.570  33.171 128.033  1.00 77.01           C  
ANISOU 3546  C   PRO A 440     9129   9608  10525    690   1315  -3399       C  
ATOM   3547  O   PRO A 440       4.473  32.317 127.175  1.00 75.02           O  
ANISOU 3547  O   PRO A 440     8917   9349  10239    654   1270  -2998       O  
ATOM   3548  CB  PRO A 440       3.937  35.379 127.055  1.00 79.98           C  
ANISOU 3548  CB  PRO A 440     9437   9239  11712    897   1450  -3613       C  
ATOM   3549  CG  PRO A 440       4.660  36.430 126.298  1.00 80.23           C  
ANISOU 3549  CG  PRO A 440     9525   8745  12215    882   1455  -3640       C  
ATOM   3550  CD  PRO A 440       5.890  35.673 125.694  1.00 78.63           C  
ANISOU 3550  CD  PRO A 440     9412   8539  11927    687   1329  -3365       C  
ATOM   3551  N   GLU A 441       4.263  32.953 129.302  1.00 79.57           N  
ANISOU 3551  N   GLU A 441     9427  10314  10492    714   1375  -3644       N  
ATOM   3552  CA  GLU A 441       3.823  31.646 129.747  1.00 79.14           C  
ANISOU 3552  CA  GLU A 441     9412  10663   9996    684   1418  -3395       C  
ATOM   3553  C   GLU A 441       2.648  31.087 128.958  1.00 77.51           C  
ANISOU 3553  C   GLU A 441     9140  10424   9886    720   1525  -3063       C  
ATOM   3554  O   GLU A 441       2.716  29.957 128.458  1.00 75.25           O  
ANISOU 3554  O   GLU A 441     8904  10210   9475    633   1480  -2698       O  
ATOM   3555  CB  GLU A 441       3.540  31.611 131.242  1.00 82.01           C  
ANISOU 3555  CB  GLU A 441     9773  11443   9944    736   1522  -3700       C  
ATOM   3556  CG  GLU A 441       4.777  31.322 132.076  1.00 85.85           C  
ANISOU 3556  CG  GLU A 441    10363  12174  10083    687   1355  -3852       C  
ATOM   3557  CD  GLU A 441       5.494  32.595 132.584  1.00 91.28           C  
ANISOU 3557  CD  GLU A 441    10984  12751  10947    715   1265  -4404       C  
ATOM   3558  OE1 GLU A 441       5.344  32.916 133.793  1.00 93.82           O  
ANISOU 3558  OE1 GLU A 441    11289  13394  10965    802   1314  -4791       O  
ATOM   3559  OE2 GLU A 441       6.206  33.260 131.779  1.00 91.18           O  
ANISOU 3559  OE2 GLU A 441    10934  12333  11377    644   1163  -4460       O  
ATOM   3560  N   SER A 442       1.577  31.840 128.806  1.00 79.27           N  
ANISOU 3560  N   SER A 442     9231  10535  10353    855   1653  -3205       N  
ATOM   3561  CA  SER A 442       0.392  31.194 128.225  1.00 79.29           C  
ANISOU 3561  CA  SER A 442     9121  10605  10400    893   1746  -2951       C  
ATOM   3562  C   SER A 442       0.517  30.985 126.702  1.00 76.39           C  
ANISOU 3562  C   SER A 442     8769   9948  10306    899   1601  -2612       C  
ATOM   3563  O   SER A 442      -0.405  30.505 126.036  1.00 76.06           O  
ANISOU 3563  O   SER A 442     8612   9939  10349    945   1627  -2429       O  
ATOM   3564  CB  SER A 442      -0.889  31.937 128.596  1.00 82.01           C  
ANISOU 3564  CB  SER A 442     9279  10992  10888   1059   1927  -3221       C  
ATOM   3565  OG  SER A 442      -1.052  33.045 127.754  1.00 82.51           O  
ANISOU 3565  OG  SER A 442     9296  10668  11387   1222   1860  -3292       O  
ATOM   3566  N   GLU A 443       1.681  31.339 126.183  1.00 74.97           N  
ANISOU 3566  N   GLU A 443     8719   9513  10253    850   1455  -2557       N  
ATOM   3567  CA  GLU A 443       1.971  31.280 124.782  1.00 73.29           C  
ANISOU 3567  CA  GLU A 443     8556   9027  10264    867   1335  -2258       C  
ATOM   3568  C   GLU A 443       2.999  30.166 124.447  1.00 70.03           C  
ANISOU 3568  C   GLU A 443     8260   8692   9656    690   1210  -1992       C  
ATOM   3569  O   GLU A 443       3.127  29.739 123.267  1.00 67.49           O  
ANISOU 3569  O   GLU A 443     7969   8244   9429    689   1120  -1704       O  
ATOM   3570  CB  GLU A 443       2.453  32.672 124.317  1.00 75.11           C  
ANISOU 3570  CB  GLU A 443     8840   8839  10859    962   1321  -2385       C  
ATOM   3571  CG  GLU A 443       2.882  32.711 122.845  1.00 76.84           C  
ANISOU 3571  CG  GLU A 443     9154   8762  11281    993   1228  -2050       C  
ATOM   3572  CD  GLU A 443       3.380  34.076 122.331  1.00 83.93           C  
ANISOU 3572  CD  GLU A 443    10138   9191  12561   1077   1269  -2110       C  
ATOM   3573  OE1 GLU A 443       4.097  34.007 121.293  1.00 85.44           O  
ANISOU 3573  OE1 GLU A 443    10445   9173  12845   1039   1221  -1835       O  
ATOM   3574  OE2 GLU A 443       3.078  35.177 122.907  1.00 84.86           O  
ANISOU 3574  OE2 GLU A 443    10215   9133  12895   1176   1368  -2414       O  
ATOM   3575  N   ARG A 444       3.715  29.702 125.480  1.00 69.53           N  
ANISOU 3575  N   ARG A 444     8259   8853   9306    570   1196  -2101       N  
ATOM   3576  CA  ARG A 444       4.794  28.720 125.326  1.00 66.85           C  
ANISOU 3576  CA  ARG A 444     8027   8588   8786    432   1066  -1898       C  
ATOM   3577  C   ARG A 444       4.232  27.418 124.732  1.00 65.75           C  
ANISOU 3577  C   ARG A 444     7876   8563   8542    391   1066  -1561       C  
ATOM   3578  O   ARG A 444       4.780  26.843 123.796  1.00 62.72           O  
ANISOU 3578  O   ARG A 444     7541   8073   8215    338    956  -1327       O  
ATOM   3579  CB  ARG A 444       5.518  28.477 126.671  1.00 68.05           C  
ANISOU 3579  CB  ARG A 444     8239   9011   8606    375   1038  -2098       C  
ATOM   3580  CG  ARG A 444       6.760  29.370 126.888  1.00 70.39           C  
ANISOU 3580  CG  ARG A 444     8551   9163   9031    342    926  -2379       C  
ATOM   3581  CD  ARG A 444       7.595  29.165 128.186  1.00 71.78           C  
ANISOU 3581  CD  ARG A 444     8764   9649   8861    321    833  -2630       C  
ATOM   3582  NE  ARG A 444       7.957  30.474 128.749  1.00 76.46           N  
ANISOU 3582  NE  ARG A 444     9283  10142   9625    344    831  -3100       N  
ATOM   3583  CZ  ARG A 444       8.237  30.727 130.045  1.00 83.30           C  
ANISOU 3583  CZ  ARG A 444    10136  11301  10214    387    791  -3477       C  
ATOM   3584  NH1 ARG A 444       8.277  29.743 130.940  1.00 82.84           N  
ANISOU 3584  NH1 ARG A 444    10164  11667   9645    431    748  -3392       N  
ATOM   3585  NH2 ARG A 444       8.494  31.981 130.461  1.00 83.62           N  
ANISOU 3585  NH2 ARG A 444    10082  11205  10483    400    798  -3952       N  
ATOM   3586  N   MET A 445       3.109  26.945 125.235  1.00 67.26           N  
ANISOU 3586  N   MET A 445     7985   8963   8608    406   1208  -1556       N  
ATOM   3587  CA  MET A 445       2.559  25.710 124.712  1.00 65.93           C  
ANISOU 3587  CA  MET A 445     7777   8876   8396    338   1228  -1285       C  
ATOM   3588  C   MET A 445       2.107  25.718 123.275  1.00 63.04           C  
ANISOU 3588  C   MET A 445     7323   8326   8302    398   1145  -1141       C  
ATOM   3589  O   MET A 445       2.485  24.858 122.538  1.00 61.69           O  
ANISOU 3589  O   MET A 445     7192   8121   8126    328   1048   -928       O  
ATOM   3590  CB  MET A 445       1.415  25.252 125.583  1.00 68.83           C  
ANISOU 3590  CB  MET A 445     8046   9490   8616    318   1447  -1334       C  
ATOM   3591  CG  MET A 445       0.938  23.871 125.302  1.00 71.06           C  
ANISOU 3591  CG  MET A 445     8292   9855   8853    198   1512  -1084       C  
ATOM   3592  SD  MET A 445      -0.446  23.856 124.184  1.00 77.20           S  
ANISOU 3592  SD  MET A 445     8800  10565   9967    252   1538  -1089       S  
ATOM   3593  CE  MET A 445      -1.671  24.729 125.110  1.00 75.68           C  
ANISOU 3593  CE  MET A 445     8422  10531   9801    353   1772  -1388       C  
ATOM   3594  N   PRO A 446       1.354  26.714 122.852  1.00 63.71           N  
ANISOU 3594  N   PRO A 446     7297   8295   8614    555   1166  -1265       N  
ATOM   3595  CA  PRO A 446       1.013  26.854 121.415  1.00 62.11           C  
ANISOU 3595  CA  PRO A 446     7038   7929   8631    674   1048  -1122       C  
ATOM   3596  C   PRO A 446       2.244  26.910 120.524  1.00 60.55           C  
ANISOU 3596  C   PRO A 446     7006   7529   8471    649    904   -949       C  
ATOM   3597  O   PRO A 446       2.338  26.191 119.534  1.00 59.93           O  
ANISOU 3597  O   PRO A 446     6933   7445   8393    636    802   -754       O  
ATOM   3598  CB  PRO A 446       0.233  28.174 121.372  1.00 63.47           C  
ANISOU 3598  CB  PRO A 446     7116   7980   9019    892   1096  -1309       C  
ATOM   3599  CG  PRO A 446      -0.499  28.159 122.762  1.00 66.53           C  
ANISOU 3599  CG  PRO A 446     7388   8603   9288    850   1288  -1550       C  
ATOM   3600  CD  PRO A 446       0.581  27.663 123.700  1.00 65.97           C  
ANISOU 3600  CD  PRO A 446     7484   8636   8948    663   1310  -1547       C  
ATOM   3601  N   CYS A 447       3.206  27.734 120.889  1.00 61.57           N  
ANISOU 3601  N   CYS A 447     7253   7501   8638    629    907  -1049       N  
ATOM   3602  CA  CYS A 447       4.462  27.785 120.181  1.00 61.50           C  
ANISOU 3602  CA  CYS A 447     7379   7311   8679    568    816   -915       C  
ATOM   3603  C   CYS A 447       5.028  26.394 120.037  1.00 59.28           C  
ANISOU 3603  C   CYS A 447     7134   7186   8205    423    734   -743       C  
ATOM   3604  O   CYS A 447       5.302  25.965 118.899  1.00 58.33           O  
ANISOU 3604  O   CYS A 447     7045   6994   8123    434    650   -547       O  
ATOM   3605  CB  CYS A 447       5.460  28.656 120.934  1.00 62.69           C  
ANISOU 3605  CB  CYS A 447     7597   7334   8887    503    849  -1126       C  
ATOM   3606  SG  CYS A 447       7.041  28.816 120.122  1.00 71.02           S  
ANISOU 3606  SG  CYS A 447     8767   8154  10063    400    784  -1011       S  
ATOM   3607  N   THR A 448       5.232  25.698 121.170  1.00 59.38           N  
ANISOU 3607  N   THR A 448     7156   7405   8000    309    760   -811       N  
ATOM   3608  CA  THR A 448       5.800  24.331 121.175  1.00 59.21           C  
ANISOU 3608  CA  THR A 448     7189   7506   7801    189    691   -639       C  
ATOM   3609  C   THR A 448       5.028  23.385 120.296  1.00 58.12           C  
ANISOU 3609  C   THR A 448     6979   7401   7700    188    675   -461       C  
ATOM   3610  O   THR A 448       5.610  22.740 119.407  1.00 58.15           O  
ANISOU 3610  O   THR A 448     7023   7345   7725    154    572   -309       O  
ATOM   3611  CB  THR A 448       5.996  23.696 122.621  1.00 60.75           C  
ANISOU 3611  CB  THR A 448     7436   7933   7713    114    740   -698       C  
ATOM   3612  OG1 THR A 448       7.236  24.129 123.186  1.00 63.25           O  
ANISOU 3612  OG1 THR A 448     7830   8248   7955     95    653   -833       O  
ATOM   3613  CG2 THR A 448       6.078  22.186 122.563  1.00 60.86           C  
ANISOU 3613  CG2 THR A 448     7495   8041   7586     29    719   -471       C  
ATOM   3614  N   GLU A 449       3.723  23.302 120.494  1.00 59.52           N  
ANISOU 3614  N   GLU A 449     7027   7680   7908    224    775   -511       N  
ATOM   3615  CA  GLU A 449       2.934  22.356 119.696  1.00 59.15           C  
ANISOU 3615  CA  GLU A 449     6863   7681   7930    205    755   -405       C  
ATOM   3616  C   GLU A 449       3.176  22.537 118.194  1.00 58.02           C  
ANISOU 3616  C   GLU A 449     6722   7410   7912    307    599   -313       C  
ATOM   3617  O   GLU A 449       3.505  21.593 117.469  1.00 57.20           O  
ANISOU 3617  O   GLU A 449     6631   7307   7794    249    511   -197       O  
ATOM   3618  CB  GLU A 449       1.443  22.411 120.073  1.00 61.38           C  
ANISOU 3618  CB  GLU A 449     6945   8091   8283    237    893   -529       C  
ATOM   3619  CG  GLU A 449       1.015  21.275 121.006  1.00 62.11           C  
ANISOU 3619  CG  GLU A 449     7004   8335   8259     66   1063   -491       C  
ATOM   3620  CD  GLU A 449       1.318  19.842 120.463  1.00 66.35           C  
ANISOU 3620  CD  GLU A 449     7567   8839   8805    -71   1011   -312       C  
ATOM   3621  OE1 GLU A 449       0.972  18.900 121.198  1.00 64.95           O  
ANISOU 3621  OE1 GLU A 449     7384   8731   8563   -213   1180   -246       O  
ATOM   3622  OE2 GLU A 449       1.850  19.616 119.305  1.00 64.81           O  
ANISOU 3622  OE2 GLU A 449     7396   8540   8688    -37    826   -239       O  
ATOM   3623  N   ASP A 450       3.094  23.778 117.769  1.00 58.56           N  
ANISOU 3623  N   ASP A 450     6804   7357   8090    468    578   -363       N  
ATOM   3624  CA  ASP A 450       3.244  24.173 116.381  1.00 59.08           C  
ANISOU 3624  CA  ASP A 450     6905   7304   8238    616    464   -251       C  
ATOM   3625  C   ASP A 450       4.530  23.684 115.654  1.00 56.82           C  
ANISOU 3625  C   ASP A 450     6760   6940   7888    539    383    -96       C  
ATOM   3626  O   ASP A 450       4.380  23.101 114.570  1.00 57.23           O  
ANISOU 3626  O   ASP A 450     6785   7039   7920    595    283     -4       O  
ATOM   3627  CB  ASP A 450       2.947  25.697 116.279  1.00 61.37           C  
ANISOU 3627  CB  ASP A 450     7222   7430   8667    814    505   -310       C  
ATOM   3628  CG  ASP A 450       3.690  26.386 115.158  1.00 65.40           C  
ANISOU 3628  CG  ASP A 450     7888   7729   9234    931    459   -145       C  
ATOM   3629  OD1 ASP A 450       3.737  25.825 114.039  1.00 67.67           O  
ANISOU 3629  OD1 ASP A 450     8189   8070   9453    992    353      1       O  
ATOM   3630  OD2 ASP A 450       4.197  27.529 115.383  1.00 70.30           O  
ANISOU 3630  OD2 ASP A 450     8614   8119   9976    968    546   -171       O  
ATOM   3631  N   TYR A 451       5.735  23.878 116.227  1.00 55.98           N  
ANISOU 3631  N   TYR A 451     6773   6745   7750    422    418   -102       N  
ATOM   3632  CA  TYR A 451       7.035  23.520 115.589  1.00 55.25           C  
ANISOU 3632  CA  TYR A 451     6785   6578   7630    350    362     11       C  
ATOM   3633  C   TYR A 451       7.375  22.023 115.731  1.00 54.39           C  
ANISOU 3633  C   TYR A 451     6659   6603   7404    220    295     59       C  
ATOM   3634  O   TYR A 451       8.159  21.468 114.947  1.00 54.58           O  
ANISOU 3634  O   TYR A 451     6725   6602   7409    195    230    149       O  
ATOM   3635  CB  TYR A 451       8.223  24.273 116.211  1.00 55.49           C  
ANISOU 3635  CB  TYR A 451     6896   6477   7712    267    415    -72       C  
ATOM   3636  CG  TYR A 451       8.464  25.727 115.810  1.00 61.47           C  
ANISOU 3636  CG  TYR A 451     7714   6989   8652    350    505    -85       C  
ATOM   3637  CD1 TYR A 451       8.103  26.777 116.676  1.00 68.80           C  
ANISOU 3637  CD1 TYR A 451     8624   7827   9689    381    589   -264       C  
ATOM   3638  CD2 TYR A 451       9.069  26.070 114.598  1.00 62.35           C  
ANISOU 3638  CD2 TYR A 451     7912   6940   8837    398    534     77       C  
ATOM   3639  CE1 TYR A 451       8.318  28.123 116.330  1.00 70.48           C  
ANISOU 3639  CE1 TYR A 451     8902   7751  10125    453    696   -278       C  
ATOM   3640  CE2 TYR A 451       9.292  27.383 114.244  1.00 63.57           C  
ANISOU 3640  CE2 TYR A 451     8149   6823   9184    466    661    105       C  
ATOM   3641  CZ  TYR A 451       8.921  28.429 115.123  1.00 71.40           C  
ANISOU 3641  CZ  TYR A 451     9120   7678  10330    490    742    -76       C  
ATOM   3642  OH  TYR A 451       9.114  29.801 114.800  1.00 75.25           O  
ANISOU 3642  OH  TYR A 451     9697   7823  11069    559    895    -55       O  
ATOM   3643  N   LEU A 452       6.864  21.391 116.774  1.00 54.04           N  
ANISOU 3643  N   LEU A 452     6566   6681   7284    141    334      4       N  
ATOM   3644  CA  LEU A 452       7.094  19.999 117.001  1.00 53.71           C  
ANISOU 3644  CA  LEU A 452     6531   6717   7159     32    303     75       C  
ATOM   3645  C   LEU A 452       6.496  19.240 115.882  1.00 53.96           C  
ANISOU 3645  C   LEU A 452     6478   6766   7259     55    243    126       C  
ATOM   3646  O   LEU A 452       7.015  18.199 115.452  1.00 55.38           O  
ANISOU 3646  O   LEU A 452     6678   6935   7428     -4    178    190       O  
ATOM   3647  CB  LEU A 452       6.453  19.544 118.325  1.00 55.20           C  
ANISOU 3647  CB  LEU A 452     6702   7021   7251    -42    412     43       C  
ATOM   3648  CG  LEU A 452       7.379  19.896 119.481  1.00 55.18           C  
ANISOU 3648  CG  LEU A 452     6809   7055   7102    -65    419     -8       C  
ATOM   3649  CD1 LEU A 452       6.871  19.265 120.772  1.00 59.78           C  
ANISOU 3649  CD1 LEU A 452     7421   7782   7510   -117    536     12       C  
ATOM   3650  CD2 LEU A 452       8.806  19.472 119.159  1.00 49.40           C  
ANISOU 3650  CD2 LEU A 452     6157   6267   6345    -89    291     52       C  
ATOM   3651  N   SER A 453       5.415  19.755 115.363  1.00 54.45           N  
ANISOU 3651  N   SER A 453     6431   6860   7397    161    246     70       N  
ATOM   3652  CA  SER A 453       4.767  19.029 114.340  1.00 54.70           C  
ANISOU 3652  CA  SER A 453     6347   6953   7483    197    162     59       C  
ATOM   3653  C   SER A 453       5.493  19.182 113.019  1.00 54.17           C  
ANISOU 3653  C   SER A 453     6355   6845   7381    303     47    130       C  
ATOM   3654  O   SER A 453       5.367  18.344 112.149  1.00 55.39           O  
ANISOU 3654  O   SER A 453     6449   7060   7538    312    -46    112       O  
ATOM   3655  CB  SER A 453       3.301  19.417 114.272  1.00 56.47           C  
ANISOU 3655  CB  SER A 453     6386   7273   7796    293    181    -60       C  
ATOM   3656  OG  SER A 453       3.135  20.513 113.429  1.00 57.86           O  
ANISOU 3656  OG  SER A 453     6579   7427   7978    512    106    -49       O  
ATOM   3657  N   LEU A 454       6.246  20.255 112.838  1.00 53.78           N  
ANISOU 3657  N   LEU A 454     6435   6691   7308    379     71    199       N  
ATOM   3658  CA  LEU A 454       7.145  20.332 111.686  1.00 52.12           C  
ANISOU 3658  CA  LEU A 454     6324   6434   7046    446     22    298       C  
ATOM   3659  C   LEU A 454       8.294  19.364 111.868  1.00 50.09           C  
ANISOU 3659  C   LEU A 454     6112   6160   6762    292      7    315       C  
ATOM   3660  O   LEU A 454       8.902  18.884 110.874  1.00 47.91           O  
ANISOU 3660  O   LEU A 454     5864   5901   6439    319    -45    355       O  
ATOM   3661  CB  LEU A 454       7.750  21.736 111.571  1.00 52.42           C  
ANISOU 3661  CB  LEU A 454     6490   6312   7117    523    113    375       C  
ATOM   3662  CG  LEU A 454       6.687  22.834 111.561  1.00 54.74           C  
ANISOU 3662  CG  LEU A 454     6761   6569   7468    700    141    365       C  
ATOM   3663  CD1 LEU A 454       7.249  24.226 111.843  1.00 43.41           C  
ANISOU 3663  CD1 LEU A 454     5449   4905   6140    728    273    405       C  
ATOM   3664  CD2 LEU A 454       5.774  22.743 110.282  1.00 52.79           C  
ANISOU 3664  CD2 LEU A 454     6465   6449   7143    931     21    412       C  
ATOM   3665  N   ILE A 455       8.636  19.119 113.131  1.00 48.39           N  
ANISOU 3665  N   ILE A 455     5908   5923   6556    160     52    282       N  
ATOM   3666  CA  ILE A 455       9.920  18.470 113.380  1.00 47.66           C  
ANISOU 3666  CA  ILE A 455     5872   5799   6438     63     26    303       C  
ATOM   3667  C   ILE A 455       9.619  16.969 113.436  1.00 46.11           C  
ANISOU 3667  C   ILE A 455     5628   5653   6240     -3    -28    306       C  
ATOM   3668  O   ILE A 455      10.246  16.153 112.803  1.00 45.22           O  
ANISOU 3668  O   ILE A 455     5519   5527   6134    -13    -90    319       O  
ATOM   3669  CB  ILE A 455      10.577  19.012 114.647  1.00 48.82           C  
ANISOU 3669  CB  ILE A 455     6065   5915   6568     -2     70    255       C  
ATOM   3670  CG1 ILE A 455      11.202  20.366 114.382  1.00 48.63           C  
ANISOU 3670  CG1 ILE A 455     6078   5780   6618     28    132    226       C  
ATOM   3671  CG2 ILE A 455      11.690  18.050 115.153  1.00 48.44           C  
ANISOU 3671  CG2 ILE A 455     6045   5888   6472    -73      2    262       C  
ATOM   3672  CD1 ILE A 455      11.542  21.082 115.724  1.00 51.73           C  
ANISOU 3672  CD1 ILE A 455     6477   6162   7016    -26    169     94       C  
ATOM   3673  N   LEU A 456       8.539  16.625 114.092  1.00 46.60           N  
ANISOU 3673  N   LEU A 456     5627   5757   6320    -45     18    282       N  
ATOM   3674  CA  LEU A 456       8.089  15.256 114.015  1.00 45.82           C  
ANISOU 3674  CA  LEU A 456     5468   5656   6284   -122      6    279       C  
ATOM   3675  C   LEU A 456       7.742  14.835 112.602  1.00 45.84           C  
ANISOU 3675  C   LEU A 456     5375   5692   6350    -63    -87    206       C  
ATOM   3676  O   LEU A 456       8.005  13.707 112.214  1.00 47.67           O  
ANISOU 3676  O   LEU A 456     5587   5882   6643   -114   -133    182       O  
ATOM   3677  CB  LEU A 456       7.018  14.984 115.028  1.00 45.71           C  
ANISOU 3677  CB  LEU A 456     5398   5670   6300   -205    127    272       C  
ATOM   3678  CG  LEU A 456       7.713  15.171 116.391  1.00 46.73           C  
ANISOU 3678  CG  LEU A 456     5666   5796   6294   -237    189    353       C  
ATOM   3679  CD1 LEU A 456       6.793  15.166 117.563  1.00 49.18           C  
ANISOU 3679  CD1 LEU A 456     5962   6165   6558   -297    349    363       C  
ATOM   3680  CD2 LEU A 456       8.768  14.118 116.583  1.00 45.47           C  
ANISOU 3680  CD2 LEU A 456     5610   5564   6103   -269    132    451       C  
ATOM   3681  N   ASN A 457       7.171  15.711 111.807  1.00 45.87           N  
ANISOU 3681  N   ASN A 457     5325   5772   6330     66   -126    160       N  
ATOM   3682  CA  ASN A 457       6.973  15.358 110.415  1.00 46.61           C  
ANISOU 3682  CA  ASN A 457     5349   5946   6413    166   -242     82       C  
ATOM   3683  C   ASN A 457       8.298  15.138 109.645  1.00 45.90           C  
ANISOU 3683  C   ASN A 457     5368   5827   6243    197   -284    133       C  
ATOM   3684  O   ASN A 457       8.346  14.394 108.731  1.00 46.47           O  
ANISOU 3684  O   ASN A 457     5391   5956   6309    230   -367     47       O  
ATOM   3685  CB  ASN A 457       6.175  16.392 109.695  1.00 46.20           C  
ANISOU 3685  CB  ASN A 457     5250   6001   6302    356   -291     57       C  
ATOM   3686  CG  ASN A 457       5.921  16.011 108.304  1.00 49.21           C  
ANISOU 3686  CG  ASN A 457     5563   6520   6616    493   -432    -37       C  
ATOM   3687  OD1 ASN A 457       5.343  14.924 108.033  1.00 49.68           O  
ANISOU 3687  OD1 ASN A 457     5462   6644   6770    429   -508   -211       O  
ATOM   3688  ND2 ASN A 457       6.364  16.865 107.374  1.00 46.29           N  
ANISOU 3688  ND2 ASN A 457     5315   6194   6080    682   -459     67       N  
ATOM   3689  N   ARG A 458       9.362  15.772 110.046  1.00 45.46           N  
ANISOU 3689  N   ARG A 458     5438   5693   6144    180   -219    239       N  
ATOM   3690  CA  ARG A 458      10.592  15.546 109.355  1.00 47.43           C  
ANISOU 3690  CA  ARG A 458     5751   5924   6348    196   -232    263       C  
ATOM   3691  C   ARG A 458      11.144  14.206 109.712  1.00 47.45           C  
ANISOU 3691  C   ARG A 458     5730   5873   6426     94   -273    218       C  
ATOM   3692  O   ARG A 458      11.722  13.564 108.856  1.00 47.47           O  
ANISOU 3692  O   ARG A 458     5720   5898   6419    126   -319    163       O  
ATOM   3693  CB  ARG A 458      11.653  16.611 109.680  1.00 47.16           C  
ANISOU 3693  CB  ARG A 458     5813   5808   6297    185   -136    350       C  
ATOM   3694  CG  ARG A 458      12.963  16.062 109.355  1.00 48.85           C  
ANISOU 3694  CG  ARG A 458     6040   6001   6518    148   -138    337       C  
ATOM   3695  CD  ARG A 458      13.905  16.947 108.641  1.00 45.34           C  
ANISOU 3695  CD  ARG A 458     5651   5530   6045    184    -32    393       C  
ATOM   3696  NE  ARG A 458      13.822  16.759 107.218  1.00 51.18           N  
ANISOU 3696  NE  ARG A 458     6410   6369   6667    303    -32    408       N  
ATOM   3697  CZ  ARG A 458      14.845  16.453 106.409  1.00 49.75           C  
ANISOU 3697  CZ  ARG A 458     6232   6223   6447    315     20    393       C  
ATOM   3698  NH1 ARG A 458      16.047  16.220 106.857  1.00 48.79           N  
ANISOU 3698  NH1 ARG A 458     6067   6039   6432    214     60    345       N  
ATOM   3699  NH2 ARG A 458      14.656  16.418 105.122  1.00 50.66           N  
ANISOU 3699  NH2 ARG A 458     6387   6463   6400    451     32    411       N  
ATOM   3700  N   LEU A 459      10.992  13.800 110.988  1.00 48.53           N  
ANISOU 3700  N   LEU A 459     5876   5939   6626     -9   -244    250       N  
ATOM   3701  CA  LEU A 459      11.385  12.492 111.402  1.00 48.88           C  
ANISOU 3701  CA  LEU A 459     5925   5897   6750    -79   -272    249       C  
ATOM   3702  C   LEU A 459      10.660  11.398 110.561  1.00 50.54           C  
ANISOU 3702  C   LEU A 459     6033   6097   7072    -94   -321    128       C  
ATOM   3703  O   LEU A 459      11.318  10.545 109.920  1.00 49.11           O  
ANISOU 3703  O   LEU A 459     5842   5875   6943    -75   -379     59       O  
ATOM   3704  CB  LEU A 459      11.129  12.328 112.878  1.00 51.46           C  
ANISOU 3704  CB  LEU A 459     6306   6169   7076   -156   -209    340       C  
ATOM   3705  CG  LEU A 459      11.253  10.869 113.432  1.00 52.98           C  
ANISOU 3705  CG  LEU A 459     6536   6231   7363   -216   -204    397       C  
ATOM   3706  CD1 LEU A 459      12.639  10.480 113.886  1.00 50.03           C  
ANISOU 3706  CD1 LEU A 459     6255   5808   6948   -161   -271    464       C  
ATOM   3707  CD2 LEU A 459      10.369  10.853 114.581  1.00 52.83           C  
ANISOU 3707  CD2 LEU A 459     6547   6200   7325   -289    -86    484       C  
ATOM   3708  N   CYS A 460       9.316  11.469 110.505  1.00 51.01           N  
ANISOU 3708  N   CYS A 460     5989   6208   7185   -119   -302     58       N  
ATOM   3709  CA  CYS A 460       8.544  10.522 109.692  1.00 51.93           C  
ANISOU 3709  CA  CYS A 460     5959   6335   7437   -143   -360   -125       C  
ATOM   3710  C   CYS A 460       9.020  10.473 108.233  1.00 51.27           C  
ANISOU 3710  C   CYS A 460     5850   6368   7264    -12   -480   -254       C  
ATOM   3711  O   CYS A 460       9.276   9.415 107.649  1.00 50.18           O  
ANISOU 3711  O   CYS A 460     5659   6182   7223    -29   -536   -395       O  
ATOM   3712  CB  CYS A 460       7.100  10.899 109.731  1.00 52.82           C  
ANISOU 3712  CB  CYS A 460     5924   6544   7603   -155   -343   -219       C  
ATOM   3713  SG  CYS A 460       6.483  10.943 111.404  1.00 56.65           S  
ANISOU 3713  SG  CYS A 460     6432   6927   8167   -308   -157    -83       S  
ATOM   3714  N   VAL A 461       9.112  11.650 107.643  1.00 51.38           N  
ANISOU 3714  N   VAL A 461     5909   6529   7086    129   -501   -204       N  
ATOM   3715  CA  VAL A 461       9.591  11.799 106.259  1.00 51.65           C  
ANISOU 3715  CA  VAL A 461     5960   6707   6958    284   -575   -274       C  
ATOM   3716  C   VAL A 461      10.949  11.146 106.024  1.00 50.84           C  
ANISOU 3716  C   VAL A 461     5922   6531   6864    261   -559   -276       C  
ATOM   3717  O   VAL A 461      11.075  10.383 105.131  1.00 52.02           O  
ANISOU 3717  O   VAL A 461     6013   6744   7010    309   -629   -445       O  
ATOM   3718  CB  VAL A 461       9.536  13.254 105.864  1.00 51.29           C  
ANISOU 3718  CB  VAL A 461     6003   6769   6714    435   -544   -137       C  
ATOM   3719  CG1 VAL A 461      10.545  13.611 104.727  1.00 53.78           C  
ANISOU 3719  CG1 VAL A 461     6425   7177   6830    569   -519    -85       C  
ATOM   3720  CG2 VAL A 461       8.081  13.581 105.493  1.00 53.30           C  
ANISOU 3720  CG2 VAL A 461     6137   7175   6940    548   -639   -238       C  
ATOM   3721  N   LEU A 462      11.948  11.443 106.849  1.00 50.78           N  
ANISOU 3721  N   LEU A 462     6012   6404   6876    199   -475   -122       N  
ATOM   3722  CA  LEU A 462      13.285  10.862 106.752  1.00 50.56           C  
ANISOU 3722  CA  LEU A 462     6014   6311   6884    191   -465   -136       C  
ATOM   3723  C   LEU A 462      13.224   9.360 106.938  1.00 52.99           C  
ANISOU 3723  C   LEU A 462     6261   6490   7383    129   -527   -258       C  
ATOM   3724  O   LEU A 462      13.954   8.600 106.243  1.00 55.54           O  
ANISOU 3724  O   LEU A 462     6553   6807   7741    176   -562   -385       O  
ATOM   3725  CB  LEU A 462      14.165  11.452 107.845  1.00 49.35           C  
ANISOU 3725  CB  LEU A 462     5935   6068   6749    134   -398     13       C  
ATOM   3726  CG  LEU A 462      14.786  12.844 107.549  1.00 46.91           C  
ANISOU 3726  CG  LEU A 462     5680   5821   6322    175   -299    102       C  
ATOM   3727  CD1 LEU A 462      15.566  13.264 108.757  1.00 43.73           C  
ANISOU 3727  CD1 LEU A 462     5301   5330   5984     99   -266    168       C  
ATOM   3728  CD2 LEU A 462      15.785  12.762 106.425  1.00 43.21           C  
ANISOU 3728  CD2 LEU A 462     5201   5426   5792    241   -253     47       C  
ATOM   3729  N   HIS A 463      12.320   8.933 107.840  1.00 52.84           N  
ANISOU 3729  N   HIS A 463     6222   6354   7500     25   -516   -226       N  
ATOM   3730  CA  HIS A 463      12.117   7.547 108.241  1.00 52.86           C  
ANISOU 3730  CA  HIS A 463     6193   6158   7734    -63   -522   -287       C  
ATOM   3731  C   HIS A 463      11.190   6.771 107.345  1.00 55.33           C  
ANISOU 3731  C   HIS A 463     6358   6485   8181    -87   -577   -539       C  
ATOM   3732  O   HIS A 463      11.345   5.586 107.231  1.00 57.31           O  
ANISOU 3732  O   HIS A 463     6573   6565   8638   -130   -589   -656       O  
ATOM   3733  CB  HIS A 463      11.580   7.448 109.669  1.00 51.56           C  
ANISOU 3733  CB  HIS A 463     6089   5852   7650   -175   -431   -110       C  
ATOM   3734  CG  HIS A 463      11.457   6.038 110.143  1.00 55.50           C  
ANISOU 3734  CG  HIS A 463     6598   6094   8393   -261   -389   -106       C  
ATOM   3735  ND1 HIS A 463      10.254   5.376 110.204  1.00 59.10           N  
ANISOU 3735  ND1 HIS A 463     6954   6440   9061   -394   -317   -196       N  
ATOM   3736  CD2 HIS A 463      12.405   5.126 110.480  1.00 53.98           C  
ANISOU 3736  CD2 HIS A 463     6495   5713   8303   -223   -404    -37       C  
ATOM   3737  CE1 HIS A 463      10.462   4.128 110.582  1.00 60.15           C  
ANISOU 3737  CE1 HIS A 463     7136   6292   9425   -453   -261   -159       C  
ATOM   3738  NE2 HIS A 463      11.759   3.956 110.752  1.00 57.61           N  
ANISOU 3738  NE2 HIS A 463     6940   5919   9028   -331   -325    -52       N  
ATOM   3739  N   GLU A 464      10.193   7.376 106.711  1.00 58.32           N  
ANISOU 3739  N   GLU A 464     6634   7056   8468    -50   -620   -654       N  
ATOM   3740  CA  GLU A 464       9.366   6.561 105.798  1.00 62.13           C  
ANISOU 3740  CA  GLU A 464     6934   7586   9086    -60   -710   -969       C  
ATOM   3741  C   GLU A 464      10.185   6.101 104.616  1.00 63.02           C  
ANISOU 3741  C   GLU A 464     7038   7789   9117     62   -801  -1158       C  
ATOM   3742  O   GLU A 464       9.943   5.054 104.084  1.00 66.12           O  
ANISOU 3742  O   GLU A 464     7309   8121   9694     29   -861  -1432       O  
ATOM   3743  CB  GLU A 464       8.119   7.286 105.295  1.00 63.86           C  
ANISOU 3743  CB  GLU A 464     7014   8043   9205      2   -784  -1093       C  
ATOM   3744  CG  GLU A 464       8.107   7.637 103.753  1.00 68.81           C  
ANISOU 3744  CG  GLU A 464     7587   8983   9576    222   -943  -1297       C  
ATOM   3745  CD  GLU A 464       8.578   9.097 103.473  1.00 72.61           C  
ANISOU 3745  CD  GLU A 464     8235   9644   9710    402   -920  -1048       C  
ATOM   3746  OE1 GLU A 464       7.703  10.045 103.583  1.00 70.85           O  
ANISOU 3746  OE1 GLU A 464     7985   9541   9393    478   -941   -978       O  
ATOM   3747  OE2 GLU A 464       9.811   9.277 103.159  1.00 67.50           O  
ANISOU 3747  OE2 GLU A 464     7732   8994   8920    463   -865   -933       O  
ATOM   3748  N   LYS A 465      11.154   6.888 104.189  1.00 62.50           N  
ANISOU 3748  N   LYS A 465     7090   7866   8790    196   -792  -1034       N  
ATOM   3749  CA  LYS A 465      12.039   6.438 103.106  1.00 63.93           C  
ANISOU 3749  CA  LYS A 465     7266   8144   8879    312   -836  -1206       C  
ATOM   3750  C   LYS A 465      12.672   5.072 103.398  1.00 63.92           C  
ANISOU 3750  C   LYS A 465     7240   7878   9167    235   -829  -1319       C  
ATOM   3751  O   LYS A 465      12.558   4.166 102.621  1.00 65.42           O  
ANISOU 3751  O   LYS A 465     7324   8072   9462    260   -900  -1618       O  
ATOM   3752  CB  LYS A 465      13.108   7.496 102.819  1.00 62.78           C  
ANISOU 3752  CB  LYS A 465     7254   8136   8462    423   -754  -1007       C  
ATOM   3753  CG  LYS A 465      14.211   7.063 101.838  1.00 63.45           C  
ANISOU 3753  CG  LYS A 465     7338   8315   8454    529   -741  -1152       C  
ATOM   3754  CD  LYS A 465      15.224   8.232 101.708  1.00 65.26           C  
ANISOU 3754  CD  LYS A 465     7686   8646   8464    591   -600   -922       C  
ATOM   3755  CE  LYS A 465      15.548   8.921 103.088  1.00 64.31           C  
ANISOU 3755  CE  LYS A 465     7638   8342   8457    470   -521   -649       C  
ATOM   3756  NZ  LYS A 465      15.737  10.450 102.990  1.00 65.18           N  
ANISOU 3756  NZ  LYS A 465     7849   8550   8366    507   -395   -429       N  
ATOM   3757  N   THR A 466      13.291   4.913 104.554  1.00 63.03           N  
ANISOU 3757  N   THR A 466     7227   7533   9190    158   -753  -1090       N  
ATOM   3758  CA  THR A 466      14.024   3.655 104.863  1.00 63.93           C  
ANISOU 3758  CA  THR A 466     7348   7374   9567    139   -750  -1148       C  
ATOM   3759  C   THR A 466      13.479   3.041 106.181  1.00 62.75           C  
ANISOU 3759  C   THR A 466     7252   6912   9677     -6   -684   -975       C  
ATOM   3760  O   THR A 466      14.060   3.212 107.225  1.00 61.91           O  
ANISOU 3760  O   THR A 466     7272   6699   9554     -3   -639   -712       O  
ATOM   3761  CB  THR A 466      15.538   3.991 104.943  1.00 63.80           C  
ANISOU 3761  CB  THR A 466     7409   7399   9434    246   -728  -1028       C  
ATOM   3762  OG1 THR A 466      16.300   2.847 105.357  1.00 65.52           O  
ANISOU 3762  OG1 THR A 466     7641   7354   9900    272   -744  -1052       O  
ATOM   3763  CG2 THR A 466      15.775   5.188 105.903  1.00 63.47           C  
ANISOU 3763  CG2 THR A 466     7469   7415   9230    221   -670   -724       C  
ATOM   3764  N   PRO A 467      12.332   2.343 106.122  1.00 63.60           N  
ANISOU 3764  N   PRO A 467     7256   6891  10019   -131   -668  -1135       N  
ATOM   3765  CA  PRO A 467      11.553   2.116 107.367  1.00 63.08           C  
ANISOU 3765  CA  PRO A 467     7242   6597  10130   -290   -544   -924       C  
ATOM   3766  C   PRO A 467      12.186   1.092 108.324  1.00 64.24           C  
ANISOU 3766  C   PRO A 467     7534   6372  10503   -308   -463   -727       C  
ATOM   3767  O   PRO A 467      12.385  -0.055 107.933  1.00 67.84           O  
ANISOU 3767  O   PRO A 467     7951   6587  11238   -311   -470   -899       O  
ATOM   3768  CB  PRO A 467      10.192   1.625 106.851  1.00 64.69           C  
ANISOU 3768  CB  PRO A 467     7241   6777  10563   -428   -537  -1216       C  
ATOM   3769  CG  PRO A 467      10.259   1.755 105.289  1.00 65.25           C  
ANISOU 3769  CG  PRO A 467     7163   7136  10494   -297   -706  -1586       C  
ATOM   3770  CD  PRO A 467      11.680   1.796 104.904  1.00 64.55           C  
ANISOU 3770  CD  PRO A 467     7188   7099  10240   -133   -754  -1538       C  
ATOM   3771  N   VAL A 468      12.514   1.467 109.554  1.00 62.41           N  
ANISOU 3771  N   VAL A 468     7474   6089  10151   -294   -395   -380       N  
ATOM   3772  CA  VAL A 468      13.277   0.545 110.429  1.00 63.38           C  
ANISOU 3772  CA  VAL A 468     7766   5900  10416   -231   -355   -160       C  
ATOM   3773  C   VAL A 468      12.851   0.495 111.913  1.00 64.21           C  
ANISOU 3773  C   VAL A 468     8047   5850  10499   -298   -202    200       C  
ATOM   3774  O   VAL A 468      13.245  -0.449 112.636  1.00 66.82           O  
ANISOU 3774  O   VAL A 468     8539   5875  10977   -244   -141    406       O  
ATOM   3775  CB  VAL A 468      14.831   0.781 110.420  1.00 62.63           C  
ANISOU 3775  CB  VAL A 468     7741   5908  10148    -15   -489   -100       C  
ATOM   3776  CG1 VAL A 468      15.425   0.603 109.045  1.00 61.83           C  
ANISOU 3776  CG1 VAL A 468     7495   5915  10083     70   -595   -427       C  
ATOM   3777  CG2 VAL A 468      15.174   2.153 110.988  1.00 57.38           C  
ANISOU 3777  CG2 VAL A 468     7128   5538   9136     31   -520     67       C  
ATOM   3778  N   SER A 469      12.057   1.457 112.364  1.00 64.58           N  
ANISOU 3778  N   SER A 469     7006   7788   9745   -343   -402   2686       N  
ATOM   3779  CA  SER A 469      11.472   1.338 113.690  1.00 65.03           C  
ANISOU 3779  CA  SER A 469     7038   7932   9736   -298   -309   2870       C  
ATOM   3780  C   SER A 469       9.986   1.260 113.579  1.00 64.90           C  
ANISOU 3780  C   SER A 469     7000   7789   9870   -379   -230   2714       C  
ATOM   3781  O   SER A 469       9.328   2.093 112.994  1.00 64.26           O  
ANISOU 3781  O   SER A 469     6946   7729   9742   -456   -358   2467       O  
ATOM   3782  CB  SER A 469      11.913   2.501 114.592  1.00 64.55           C  
ANISOU 3782  CB  SER A 469     7016   8179   9330   -267   -459   2921       C  
ATOM   3783  OG  SER A 469      10.897   2.916 115.472  1.00 62.40           O  
ANISOU 3783  OG  SER A 469     6750   7998   8961   -291   -424   2923       O  
ATOM   3784  N   GLU A 470       9.444   0.248 114.178  1.00 67.63           N  
ANISOU 3784  N   GLU A 470     7290   7995  10411   -353     -4   2866       N  
ATOM   3785  CA  GLU A 470       8.010  -0.018 114.080  1.00 68.83           C  
ANISOU 3785  CA  GLU A 470     7385   7983  10783   -437    119   2701       C  
ATOM   3786  C   GLU A 470       7.254   1.014 114.905  1.00 67.93           C  
ANISOU 3786  C   GLU A 470     7303   8053  10454   -465     50   2659       C  
ATOM   3787  O   GLU A 470       6.120   1.391 114.576  1.00 68.29           O  
ANISOU 3787  O   GLU A 470     7310   8039  10599   -550     25   2416       O  
ATOM   3788  CB  GLU A 470       7.740  -1.452 114.559  1.00 71.43           C  
ANISOU 3788  CB  GLU A 470     7643   8079  11418   -398    440   2899       C  
ATOM   3789  CG  GLU A 470       8.846  -2.450 114.107  1.00 75.30           C  
ANISOU 3789  CG  GLU A 470     8109   8432  12070   -328    526   3050       C  
ATOM   3790  CD  GLU A 470      10.109  -2.556 115.053  1.00 83.78           C  
ANISOU 3790  CD  GLU A 470     9234   9679  12919   -167    516   3430       C  
ATOM   3791  OE1 GLU A 470      11.254  -2.072 114.686  1.00 80.04           O  
ANISOU 3791  OE1 GLU A 470     8790   9355  12267   -129    317   3427       O  
ATOM   3792  OE2 GLU A 470       9.953  -3.204 116.140  1.00 87.47           O  
ANISOU 3792  OE2 GLU A 470     9703  10120  13412    -69    728   3733       O  
ATOM   3793  N   LYS A 471       7.917   1.459 115.969  1.00 68.09           N  
ANISOU 3793  N   LYS A 471     7379   8308  10185   -388     13   2882       N  
ATOM   3794  CA  LYS A 471       7.478   2.514 116.869  1.00 67.46           C  
ANISOU 3794  CA  LYS A 471     7333   8451   9847   -408    -58   2859       C  
ATOM   3795  C   LYS A 471       7.224   3.829 116.117  1.00 63.99           C  
ANISOU 3795  C   LYS A 471     6916   8091   9307   -492   -293   2556       C  
ATOM   3796  O   LYS A 471       6.237   4.525 116.282  1.00 63.29           O  
ANISOU 3796  O   LYS A 471     6814   8026   9209   -557   -318   2393       O  
ATOM   3797  CB  LYS A 471       8.572   2.692 117.931  1.00 68.72           C  
ANISOU 3797  CB  LYS A 471     7535   8879   9697   -295    -96   3124       C  
ATOM   3798  CG  LYS A 471       8.217   2.075 119.292  1.00 74.84           C  
ANISOU 3798  CG  LYS A 471     8320   9710  10404   -217    124   3403       C  
ATOM   3799  CD  LYS A 471       9.432   1.994 120.202  1.00 82.81           C  
ANISOU 3799  CD  LYS A 471     9358  10986  11119    -64     72   3688       C  
ATOM   3800  CE  LYS A 471       9.052   1.889 121.670  1.00 88.42           C  
ANISOU 3800  CE  LYS A 471    10111  11878  11607     14    220   3918       C  
ATOM   3801  NZ  LYS A 471      10.055   2.633 122.520  1.00 90.95           N  
ANISOU 3801  NZ  LYS A 471    10443  12608  11504    109     28   3997       N  
ATOM   3802  N   VAL A 472       8.111   4.133 115.217  1.00 62.20           N  
ANISOU 3802  N   VAL A 472     6723   7878   9031   -483   -447   2484       N  
ATOM   3803  CA  VAL A 472       8.001   5.370 114.515  1.00 58.98           C  
ANISOU 3803  CA  VAL A 472     6359   7536   8515   -537   -643   2249       C  
ATOM   3804  C   VAL A 472       6.980   5.256 113.436  1.00 58.81           C  
ANISOU 3804  C   VAL A 472     6313   7327   8707   -592   -669   2013       C  
ATOM   3805  O   VAL A 472       6.181   6.140 113.215  1.00 58.57           O  
ANISOU 3805  O   VAL A 472     6286   7320   8647   -630   -768   1829       O  
ATOM   3806  CB  VAL A 472       9.370   5.764 114.044  1.00 58.32           C  
ANISOU 3806  CB  VAL A 472     6328   7541   8289   -504   -764   2274       C  
ATOM   3807  CG1 VAL A 472       9.339   6.918 112.971  1.00 53.84           C  
ANISOU 3807  CG1 VAL A 472     5831   6968   7658   -550   -933   2038       C  
ATOM   3808  CG2 VAL A 472      10.193   6.099 115.259  1.00 53.48           C  
ANISOU 3808  CG2 VAL A 472     5707   7172   7443   -451   -773   2447       C  
ATOM   3809  N   THR A 473       6.971   4.130 112.774  1.00 60.45           N  
ANISOU 3809  N   THR A 473     6478   7346   9144   -590   -575   2006       N  
ATOM   3810  CA  THR A 473       5.946   3.899 111.765  1.00 60.83           C  
ANISOU 3810  CA  THR A 473     6471   7235   9406   -640   -600   1746       C  
ATOM   3811  C   THR A 473       4.528   4.110 112.312  1.00 61.79           C  
ANISOU 3811  C   THR A 473     6511   7331   9634   -685   -547   1629       C  
ATOM   3812  O   THR A 473       3.726   4.815 111.739  1.00 60.91           O  
ANISOU 3812  O   THR A 473     6383   7228   9530   -706   -686   1398       O  
ATOM   3813  CB  THR A 473       6.162   2.506 111.134  1.00 60.79           C  
ANISOU 3813  CB  THR A 473     6401   7026   9669   -643   -458   1747       C  
ATOM   3814  OG1 THR A 473       7.453   2.540 110.538  1.00 59.85           O  
ANISOU 3814  OG1 THR A 473     6361   6945   9434   -608   -535   1815       O  
ATOM   3815  CG2 THR A 473       5.133   2.212 110.019  1.00 59.10           C  
ANISOU 3815  CG2 THR A 473     6104   6675   9677   -696   -498   1425       C  
ATOM   3816  N   LYS A 474       4.250   3.487 113.442  1.00 64.75           N  
ANISOU 3816  N   LYS A 474     6838   7674  10089   -687   -333   1802       N  
ATOM   3817  CA  LYS A 474       2.959   3.602 114.102  1.00 66.61           C  
ANISOU 3817  CA  LYS A 474     6994   7871  10444   -738   -227   1711       C  
ATOM   3818  C   LYS A 474       2.608   5.082 114.447  1.00 66.10           C  
ANISOU 3818  C   LYS A 474     6971   7994  10151   -753   -397   1612       C  
ATOM   3819  O   LYS A 474       1.491   5.538 114.189  1.00 66.57           O  
ANISOU 3819  O   LYS A 474     6957   8007  10328   -794   -451   1380       O  
ATOM   3820  CB  LYS A 474       2.984   2.704 115.331  1.00 68.06           C  
ANISOU 3820  CB  LYS A 474     7163   8007  10689   -718     59   1984       C  
ATOM   3821  CG  LYS A 474       1.907   2.995 116.373  1.00 72.89           C  
ANISOU 3821  CG  LYS A 474     7733   8639  11321   -764    201   1969       C  
ATOM   3822  CD  LYS A 474       2.004   2.082 117.621  1.00 77.58           C  
ANISOU 3822  CD  LYS A 474     8349   9196  11933   -722    513   2288       C  
ATOM   3823  CE  LYS A 474       3.382   2.156 118.330  1.00 79.63           C  
ANISOU 3823  CE  LYS A 474     8728   9679  11850   -609    467   2618       C  
ATOM   3824  NZ  LYS A 474       4.144   3.486 118.176  1.00 72.99           N  
ANISOU 3824  NZ  LYS A 474     7955   9111  10669   -599    159   2540       N  
ATOM   3825  N   CYS A 475       3.550   5.834 115.009  1.00 64.95           N  
ANISOU 3825  N   CYS A 475     6922   8051   9704   -717   -478   1764       N  
ATOM   3826  CA  CYS A 475       3.230   7.190 115.415  1.00 64.77           C  
ANISOU 3826  CA  CYS A 475     6923   8184   9504   -742   -594   1662       C  
ATOM   3827  C   CYS A 475       3.099   8.089 114.176  1.00 63.05           C  
ANISOU 3827  C   CYS A 475     6733   7944   9278   -736   -821   1439       C  
ATOM   3828  O   CYS A 475       2.365   9.087 114.212  1.00 63.13           O  
ANISOU 3828  O   CYS A 475     6725   7990   9272   -756   -904   1285       O  
ATOM   3829  CB  CYS A 475       4.248   7.741 116.427  1.00 64.92           C  
ANISOU 3829  CB  CYS A 475     7009   8438   9218   -714   -601   1847       C  
ATOM   3830  SG  CYS A 475       4.185   7.113 118.161  1.00 72.41           S  
ANISOU 3830  SG  CYS A 475     7944   9507  10059   -696   -360   2105       S  
ATOM   3831  N   CYS A 476       3.780   7.744 113.086  1.00 61.11           N  
ANISOU 3831  N   CYS A 476     6538   7636   9047   -701   -908   1427       N  
ATOM   3832  CA  CYS A 476       3.662   8.537 111.839  1.00 60.11           C  
ANISOU 3832  CA  CYS A 476     6464   7490   8884   -673  -1110   1241       C  
ATOM   3833  C   CYS A 476       2.434   8.265 110.981  1.00 60.20           C  
ANISOU 3833  C   CYS A 476     6387   7378   9107   -670  -1173   1004       C  
ATOM   3834  O   CYS A 476       1.988   9.105 110.203  1.00 60.73           O  
ANISOU 3834  O   CYS A 476     6482   7461   9131   -627  -1347    847       O  
ATOM   3835  CB  CYS A 476       4.886   8.397 110.976  1.00 57.81           C  
ANISOU 3835  CB  CYS A 476     6276   7199   8491   -636  -1174   1304       C  
ATOM   3836  SG  CYS A 476       6.344   8.930 111.865  1.00 62.37           S  
ANISOU 3836  SG  CYS A 476     6927   7946   8825   -631  -1145   1515       S  
ATOM   3837  N   THR A 477       1.881   7.085 111.085  1.00 62.04           N  
ANISOU 3837  N   THR A 477     6506   7486   9581   -706  -1032    968       N  
ATOM   3838  CA  THR A 477       0.828   6.706 110.139  1.00 62.34           C  
ANISOU 3838  CA  THR A 477     6430   7416   9839   -705  -1103    696       C  
ATOM   3839  C   THR A 477      -0.509   6.715 110.803  1.00 64.17           C  
ANISOU 3839  C   THR A 477     6511   7595  10276   -751  -1020    562       C  
ATOM   3840  O   THR A 477      -1.516   6.896 110.141  1.00 65.83           O  
ANISOU 3840  O   THR A 477     6616   7771  10624   -734  -1141    301       O  
ATOM   3841  CB  THR A 477       1.100   5.321 109.552  1.00 63.62           C  
ANISOU 3841  CB  THR A 477     6534   7442  10194   -725   -993    668       C  
ATOM   3842  OG1 THR A 477       1.349   4.371 110.615  1.00 61.13           O  
ANISOU 3842  OG1 THR A 477     6177   7043  10008   -771   -722    877       O  
ATOM   3843  CG2 THR A 477       2.279   5.384 108.554  1.00 60.89           C  
ANISOU 3843  CG2 THR A 477     6328   7142   9667   -677  -1112    717       C  
ATOM   3844  N   GLU A 478      -0.495   6.571 112.127  1.00 65.89           N  
ANISOU 3844  N   GLU A 478     6719   7821  10494   -800   -817    740       N  
ATOM   3845  CA  GLU A 478      -1.671   6.347 112.939  1.00 68.64           C  
ANISOU 3845  CA  GLU A 478     6928   8091  11063   -863   -648    651       C  
ATOM   3846  C   GLU A 478      -2.546   7.596 112.847  1.00 68.59           C  
ANISOU 3846  C   GLU A 478     6880   8154  11027   -850   -821    454       C  
ATOM   3847  O   GLU A 478      -3.769   7.489 112.629  1.00 69.65           O  
ANISOU 3847  O   GLU A 478     6849   8196  11419   -872   -824    203       O  
ATOM   3848  CB  GLU A 478      -1.281   6.080 114.417  1.00 69.88           C  
ANISOU 3848  CB  GLU A 478     7135   8289  11126   -896   -400    933       C  
ATOM   3849  CG  GLU A 478      -2.292   5.298 115.274  1.00 73.74           C  
ANISOU 3849  CG  GLU A 478     7497   8632  11888   -967   -106    914       C  
ATOM   3850  CD  GLU A 478      -2.059   3.784 115.185  1.00 82.34           C  
ANISOU 3850  CD  GLU A 478     8544   9532  13211   -976    129   1021       C  
ATOM   3851  OE1 GLU A 478      -0.966   3.400 114.696  1.00 85.62           O  
ANISOU 3851  OE1 GLU A 478     9046   9967  13518   -923     67   1164       O  
ATOM   3852  OE2 GLU A 478      -2.927   2.970 115.610  1.00 82.61           O  
ANISOU 3852  OE2 GLU A 478     8456   9380  13554  -1037    398    966       O  
ATOM   3853  N   SER A 479      -1.932   8.760 113.044  1.00 66.66           N  
ANISOU 3853  N   SER A 479     6764   8061  10502   -813   -948    554       N  
ATOM   3854  CA  SER A 479      -2.665  10.025 112.924  1.00 67.49           C  
ANISOU 3854  CA  SER A 479     6840   8218  10586   -786  -1105    390       C  
ATOM   3855  C   SER A 479      -1.767  11.167 112.473  1.00 66.36           C  
ANISOU 3855  C   SER A 479     6857   8191  10166   -717  -1286    469       C  
ATOM   3856  O   SER A 479      -0.545  11.185 112.723  1.00 65.12           O  
ANISOU 3856  O   SER A 479     6826   8115   9801   -720  -1250    668       O  
ATOM   3857  CB  SER A 479      -3.284  10.431 114.265  1.00 68.17           C  
ANISOU 3857  CB  SER A 479     6862   8332  10709   -861   -936    401       C  
ATOM   3858  OG  SER A 479      -2.484  11.459 114.831  1.00 68.12           O  
ANISOU 3858  OG  SER A 479     6977   8477  10426   -858   -968    536       O  
ATOM   3859  N   LEU A 480      -2.365  12.163 111.852  1.00 66.44           N  
ANISOU 3859  N   LEU A 480     6854   8204  10185   -648  -1467    316       N  
ATOM   3860  CA  LEU A 480      -1.568  13.331 111.555  1.00 65.60           C  
ANISOU 3860  CA  LEU A 480     6900   8177   9848   -589  -1580    401       C  
ATOM   3861  C   LEU A 480      -1.448  14.135 112.835  1.00 65.70           C  
ANISOU 3861  C   LEU A 480     6910   8269   9786   -663  -1456    466       C  
ATOM   3862  O   LEU A 480      -0.343  14.530 113.254  1.00 65.78           O  
ANISOU 3862  O   LEU A 480     7025   8374   9595   -687  -1410    609       O  
ATOM   3863  CB  LEU A 480      -2.174  14.153 110.419  1.00 65.31           C  
ANISOU 3863  CB  LEU A 480     6874   8110   9829   -462  -1804    256       C  
ATOM   3864  CG  LEU A 480      -1.278  15.324 110.029  1.00 65.15           C  
ANISOU 3864  CG  LEU A 480     7031   8132   9589   -395  -1877    370       C  
ATOM   3865  CD1 LEU A 480       0.201  14.947 109.755  1.00 59.15           C  
ANISOU 3865  CD1 LEU A 480     6428   7411   8635   -412  -1832    545       C  
ATOM   3866  CD2 LEU A 480      -1.892  16.057 108.840  1.00 65.85           C  
ANISOU 3866  CD2 LEU A 480     7153   8187   9680   -234  -2090    267       C  
ATOM   3867  N   VAL A 481      -2.584  14.299 113.508  1.00 66.94           N  
ANISOU 3867  N   VAL A 481     6926   8393  10116   -709  -1385    336       N  
ATOM   3868  CA  VAL A 481      -2.697  15.310 114.562  1.00 66.98           C  
ANISOU 3868  CA  VAL A 481     6913   8470  10068   -769  -1293    327       C  
ATOM   3869  C   VAL A 481      -2.269  14.884 115.974  1.00 66.58           C  
ANISOU 3869  C   VAL A 481     6860   8528   9908   -880  -1073    454       C  
ATOM   3870  O   VAL A 481      -2.151  15.712 116.880  1.00 66.46           O  
ANISOU 3870  O   VAL A 481     6843   8617   9794   -937   -995    444       O  
ATOM   3871  CB  VAL A 481      -4.124  15.892 114.603  1.00 68.66           C  
ANISOU 3871  CB  VAL A 481     6974   8598  10515   -759  -1324    110       C  
ATOM   3872  CG1 VAL A 481      -5.190  14.813 114.905  1.00 70.74           C  
ANISOU 3872  CG1 VAL A 481     7074   8772  11032   -815  -1210     -4       C  
ATOM   3873  CG2 VAL A 481      -4.187  17.018 115.590  1.00 69.79           C  
ANISOU 3873  CG2 VAL A 481     7100   8805  10612   -823  -1227     80       C  
ATOM   3874  N   ASN A 482      -2.039  13.590 116.159  1.00 66.18           N  
ANISOU 3874  N   ASN A 482     6810   8462   9874   -902   -965    572       N  
ATOM   3875  CA  ASN A 482      -1.733  13.061 117.468  1.00 65.02           C  
ANISOU 3875  CA  ASN A 482     6668   8417   9618   -973   -751    722       C  
ATOM   3876  C   ASN A 482      -0.303  12.542 117.509  1.00 63.71           C  
ANISOU 3876  C   ASN A 482     6620   8358   9228   -940   -753    951       C  
ATOM   3877  O   ASN A 482       0.019  11.646 118.274  1.00 64.48           O  
ANISOU 3877  O   ASN A 482     6731   8506   9265   -953   -595   1125       O  
ATOM   3878  CB  ASN A 482      -2.781  12.006 117.860  1.00 66.35           C  
ANISOU 3878  CB  ASN A 482     6724   8456  10031  -1020   -563    685       C  
ATOM   3879  CG  ASN A 482      -4.049  12.639 118.478  1.00 68.43           C  
ANISOU 3879  CG  ASN A 482     6863   8682  10455  -1086   -475    489       C  
ATOM   3880  OD1 ASN A 482      -3.951  13.448 119.401  1.00 70.91           O  
ANISOU 3880  OD1 ASN A 482     7195   9130  10616  -1135   -408    492       O  
ATOM   3881  ND2 ASN A 482      -5.220  12.281 117.971  1.00 65.84           N  
ANISOU 3881  ND2 ASN A 482     6393   8178  10445  -1092   -473    293       N  
ATOM   3882  N   ARG A 483       0.584  13.135 116.716  1.00 61.45           N  
ANISOU 3882  N   ARG A 483     6421   8106   8820   -889   -920    959       N  
ATOM   3883  CA  ARG A 483       1.949  12.610 116.667  1.00 59.48           C  
ANISOU 3883  CA  ARG A 483     6261   7941   8396   -857   -927   1151       C  
ATOM   3884  C   ARG A 483       2.730  12.967 117.880  1.00 59.36           C  
ANISOU 3884  C   ARG A 483     6264   8148   8140   -886   -852   1257       C  
ATOM   3885  O   ARG A 483       3.404  12.117 118.462  1.00 60.38           O  
ANISOU 3885  O   ARG A 483     6414   8369   8160   -863   -768   1449       O  
ATOM   3886  CB  ARG A 483       2.684  13.078 115.418  1.00 58.75           C  
ANISOU 3886  CB  ARG A 483     6257   7804   8262   -799  -1099   1120       C  
ATOM   3887  CG  ARG A 483       2.321  12.297 114.202  1.00 56.21           C  
ANISOU 3887  CG  ARG A 483     5937   7314   8107   -751  -1170   1073       C  
ATOM   3888  CD  ARG A 483       2.566  13.117 113.020  1.00 55.61           C  
ANISOU 3888  CD  ARG A 483     5946   7194   7987   -689  -1337    988       C  
ATOM   3889  NE  ARG A 483       2.397  12.292 111.847  1.00 57.79           N  
ANISOU 3889  NE  ARG A 483     6233   7354   8370   -639  -1410    943       N  
ATOM   3890  CZ  ARG A 483       2.966  12.545 110.687  1.00 57.19           C  
ANISOU 3890  CZ  ARG A 483     6267   7248   8214   -574  -1528    931       C  
ATOM   3891  NH1 ARG A 483       3.737  13.643 110.558  1.00 55.94           N  
ANISOU 3891  NH1 ARG A 483     6218   7142   7895   -553  -1567    972       N  
ATOM   3892  NH2 ARG A 483       2.715  11.736 109.659  1.00 53.70           N  
ANISOU 3892  NH2 ARG A 483     5819   6721   7863   -534  -1591    857       N  
ATOM   3893  N   ARG A 484       2.622  14.229 118.272  1.00 59.00           N  
ANISOU 3893  N   ARG A 484     6202   8197   8018   -928   -881   1124       N  
ATOM   3894  CA  ARG A 484       3.384  14.803 119.377  1.00 59.10           C  
ANISOU 3894  CA  ARG A 484     6210   8455   7788   -966   -835   1151       C  
ATOM   3895  C   ARG A 484       3.056  13.996 120.646  1.00 61.95           C  
ANISOU 3895  C   ARG A 484     6540   8939   8059   -984   -664   1277       C  
ATOM   3896  O   ARG A 484       3.966  13.521 121.305  1.00 63.74           O  
ANISOU 3896  O   ARG A 484     6793   9350   8073   -947   -634   1445       O  
ATOM   3897  CB  ARG A 484       3.086  16.317 119.498  1.00 57.54           C  
ANISOU 3897  CB  ARG A 484     5976   8286   7601  -1023   -864    934       C  
ATOM   3898  CG  ARG A 484       4.084  17.189 120.199  1.00 57.97           C  
ANISOU 3898  CG  ARG A 484     6017   8565   7445  -1064   -862    879       C  
ATOM   3899  CD  ARG A 484       4.036  17.121 121.729  1.00 57.20           C  
ANISOU 3899  CD  ARG A 484     5859   8725   7149  -1119   -740    885       C  
ATOM   3900  NE  ARG A 484       2.663  17.313 122.150  1.00 54.53           N  
ANISOU 3900  NE  ARG A 484     5464   8305   6948  -1177   -632    775       N  
ATOM   3901  CZ  ARG A 484       2.047  16.657 123.123  1.00 58.86           C  
ANISOU 3901  CZ  ARG A 484     5992   8935   7438  -1202   -484    846       C  
ATOM   3902  NH1 ARG A 484       2.709  15.733 123.831  1.00 64.21           N  
ANISOU 3902  NH1 ARG A 484     6712   9797   7887  -1153   -429   1060       N  
ATOM   3903  NH2 ARG A 484       0.735  16.902 123.369  1.00 59.09           N  
ANISOU 3903  NH2 ARG A 484     5957   8846   7650  -1264   -377    710       N  
ATOM   3904  N   PRO A 485       1.756  13.779 120.966  1.00 63.77           N  
ANISOU 3904  N   PRO A 485     6714   9061   8456  -1028   -542   1209       N  
ATOM   3905  CA  PRO A 485       1.562  12.911 122.173  1.00 65.79           C  
ANISOU 3905  CA  PRO A 485     6969   9424   8603  -1033   -339   1377       C  
ATOM   3906  C   PRO A 485       1.914  11.425 121.976  1.00 66.65           C  
ANISOU 3906  C   PRO A 485     7123   9441   8760   -955   -264   1627       C  
ATOM   3907  O   PRO A 485       2.313  10.745 122.944  1.00 68.21           O  
ANISOU 3907  O   PRO A 485     7359   9784   8774   -912   -131   1847       O  
ATOM   3908  CB  PRO A 485       0.063  13.076 122.558  1.00 65.72           C  
ANISOU 3908  CB  PRO A 485     6880   9294   8796  -1113   -192   1220       C  
ATOM   3909  CG  PRO A 485      -0.612  13.832 121.413  1.00 65.58           C  
ANISOU 3909  CG  PRO A 485     6804   9078   9036  -1127   -344    982       C  
ATOM   3910  CD  PRO A 485       0.492  14.389 120.460  1.00 62.82           C  
ANISOU 3910  CD  PRO A 485     6522   8756   8590  -1069   -563    986       C  
ATOM   3911  N   CYS A 486       1.758  10.920 120.757  1.00 65.87           N  
ANISOU 3911  N   CYS A 486     7018   9109   8902   -930   -339   1595       N  
ATOM   3912  CA  CYS A 486       2.222   9.555 120.448  1.00 66.82           C  
ANISOU 3912  CA  CYS A 486     7169   9123   9097   -861   -269   1807       C  
ATOM   3913  C   CYS A 486       3.766   9.437 120.618  1.00 65.72           C  
ANISOU 3913  C   CYS A 486     7099   9174   8696   -781   -356   2003       C  
ATOM   3914  O   CYS A 486       4.270   8.397 121.017  1.00 65.61           O  
ANISOU 3914  O   CYS A 486     7112   9176   8639   -708   -248   2248       O  
ATOM   3915  CB  CYS A 486       1.781   9.090 119.047  1.00 65.39           C  
ANISOU 3915  CB  CYS A 486     6952   8676   9218   -859   -343   1683       C  
ATOM   3916  SG  CYS A 486       2.096   7.272 118.628  1.00 71.89           S  
ANISOU 3916  SG  CYS A 486     7774   9298  10244   -802   -192   1888       S  
ATOM   3917  N   PHE A 487       4.500  10.493 120.297  1.00 64.45           N  
ANISOU 3917  N   PHE A 487     6956   9142   8391   -789   -539   1889       N  
ATOM   3918  CA  PHE A 487       5.932  10.439 120.470  1.00 65.13           C  
ANISOU 3918  CA  PHE A 487     7075   9411   8259   -722   -621   2027       C  
ATOM   3919  C   PHE A 487       6.361  10.730 121.888  1.00 66.74           C  
ANISOU 3919  C   PHE A 487     7268   9932   8158   -704   -576   2111       C  
ATOM   3920  O   PHE A 487       7.370  10.173 122.341  1.00 69.64           O  
ANISOU 3920  O   PHE A 487     7647  10461   8350   -610   -588   2310       O  
ATOM   3921  CB  PHE A 487       6.663  11.329 119.497  1.00 62.78           C  
ANISOU 3921  CB  PHE A 487     6796   9100   7957   -736   -802   1875       C  
ATOM   3922  CG  PHE A 487       6.922  10.692 118.198  1.00 63.27           C  
ANISOU 3922  CG  PHE A 487     6895   8943   8201   -701   -857   1899       C  
ATOM   3923  CD1 PHE A 487       8.082   9.942 118.004  1.00 66.87           C  
ANISOU 3923  CD1 PHE A 487     7370   9424   8612   -630   -873   2066       C  
ATOM   3924  CD2 PHE A 487       6.063  10.897 117.126  1.00 63.75           C  
ANISOU 3924  CD2 PHE A 487     6966   8790   8469   -731   -906   1735       C  
ATOM   3925  CE1 PHE A 487       8.348   9.352 116.777  1.00 63.94           C  
ANISOU 3925  CE1 PHE A 487     7032   8851   8411   -608   -909   2066       C  
ATOM   3926  CE2 PHE A 487       6.308  10.345 115.891  1.00 62.12           C  
ANISOU 3926  CE2 PHE A 487     6795   8409   8397   -699   -964   1729       C  
ATOM   3927  CZ  PHE A 487       7.429   9.540 115.717  1.00 66.20           C  
ANISOU 3927  CZ  PHE A 487     7336   8936   8882   -647   -950   1890       C  
ATOM   3928  N   SER A 488       5.624  11.564 122.607  1.00 66.54           N  
ANISOU 3928  N   SER A 488     7211  10011   8061   -782   -526   1959       N  
ATOM   3929  CA  SER A 488       5.915  11.713 124.043  1.00 68.79           C  
ANISOU 3929  CA  SER A 488     7487  10621   8029   -762   -459   2036       C  
ATOM   3930  C   SER A 488       5.486  10.521 124.883  1.00 69.53           C  
ANISOU 3930  C   SER A 488     7624  10724   8072   -692   -253   2306       C  
ATOM   3931  O   SER A 488       6.080  10.235 125.845  1.00 71.92           O  
ANISOU 3931  O   SER A 488     7949  11288   8090   -608   -223   2480       O  
ATOM   3932  CB  SER A 488       5.356  13.014 124.599  1.00 68.96           C  
ANISOU 3932  CB  SER A 488     7455  10770   7976   -875   -453   1770       C  
ATOM   3933  OG  SER A 488       5.928  14.131 123.918  1.00 68.92           O  
ANISOU 3933  OG  SER A 488     7414  10768   8004   -923   -615   1551       O  
ATOM   3934  N   ALA A 489       4.478   9.782 124.492  1.00 70.19           N  
ANISOU 3934  N   ALA A 489     7716  10513   8438   -715   -103   2346       N  
ATOM   3935  CA  ALA A 489       4.094   8.606 125.283  1.00 72.79           C  
ANISOU 3935  CA  ALA A 489     8093  10810   8754   -647    144   2621       C  
ATOM   3936  C   ALA A 489       5.008   7.394 125.065  1.00 73.92           C  
ANISOU 3936  C   ALA A 489     8280  10903   8902   -503    161   2930       C  
ATOM   3937  O   ALA A 489       4.736   6.333 125.624  1.00 77.05           O  
ANISOU 3937  O   ALA A 489     8723  11225   9328   -429    390   3192       O  
ATOM   3938  CB  ALA A 489       2.656   8.220 125.013  1.00 71.05           C  
ANISOU 3938  CB  ALA A 489     7839  10278   8879   -735    340   2526       C  
ATOM   3939  N   LEU A 490       6.034   7.504 124.222  1.00 72.43           N  
ANISOU 3939  N   LEU A 490     8076  10718   8725   -465    -48   2905       N  
ATOM   3940  CA  LEU A 490       6.904   6.341 123.974  1.00 73.14           C  
ANISOU 3940  CA  LEU A 490     8191  10738   8859   -329    -24   3186       C  
ATOM   3941  C   LEU A 490       7.890   6.168 125.091  1.00 75.67           C  
ANISOU 3941  C   LEU A 490     8540  11404   8806   -180    -49   3434       C  
ATOM   3942  O   LEU A 490       8.386   7.146 125.664  1.00 75.82           O  
ANISOU 3942  O   LEU A 490     8534  11750   8524   -190   -200   3311       O  
ATOM   3943  CB  LEU A 490       7.688   6.443 122.674  1.00 70.61           C  
ANISOU 3943  CB  LEU A 490     7844  10294   8691   -337   -217   3074       C  
ATOM   3944  CG  LEU A 490       6.947   6.270 121.349  1.00 68.98           C  
ANISOU 3944  CG  LEU A 490     7616   9737   8855   -431   -211   2886       C  
ATOM   3945  CD1 LEU A 490       7.614   7.056 120.231  1.00 64.18           C  
ANISOU 3945  CD1 LEU A 490     7002   9117   8265   -470   -441   2680       C  
ATOM   3946  CD2 LEU A 490       6.792   4.830 120.960  1.00 67.81           C  
ANISOU 3946  CD2 LEU A 490     7465   9318   8982   -378    -33   3067       C  
ATOM   3947  N   THR A 491       8.220   4.907 125.340  1.00 78.41           N  
ANISOU 3947  N   THR A 491     8927  11676   9191    -34     93   3775       N  
ATOM   3948  CA  THR A 491       9.122   4.510 126.409  1.00 82.28           C  
ANISOU 3948  CA  THR A 491     9450  12482   9332    158     84   4080       C  
ATOM   3949  C   THR A 491      10.330   3.772 125.820  1.00 83.19           C  
ANISOU 3949  C   THR A 491     9534  12539   9535    296    -18   4259       C  
ATOM   3950  O   THR A 491      10.217   3.192 124.736  1.00 82.31           O  
ANISOU 3950  O   THR A 491     9404  12077   9791    250     33   4230       O  
ATOM   3951  CB  THR A 491       8.399   3.564 127.387  1.00 85.30           C  
ANISOU 3951  CB  THR A 491     9923  12813   9673    253    401   4402       C  
ATOM   3952  OG1 THR A 491       8.021   2.377 126.683  1.00 84.94           O  
ANISOU 3952  OG1 THR A 491     9887  12341  10045    266    613   4553       O  
ATOM   3953  CG2 THR A 491       7.151   4.224 127.934  1.00 84.67           C  
ANISOU 3953  CG2 THR A 491     9867  12753   9552    105    538   4214       C  
ATOM   3954  N   PRO A 492      11.484   3.799 126.517  1.00 85.66           N  
ANISOU 3954  N   PRO A 492     9825  13204   9517    464   -167   4420       N  
ATOM   3955  CA  PRO A 492      12.598   2.931 126.144  1.00 87.22           C  
ANISOU 3955  CA  PRO A 492     9988  13348   9804    630   -225   4648       C  
ATOM   3956  C   PRO A 492      12.191   1.464 126.331  1.00 90.41           C  
ANISOU 3956  C   PRO A 492    10464  13476  10410    761     74   5039       C  
ATOM   3957  O   PRO A 492      11.803   1.094 127.434  1.00 93.13           O  
ANISOU 3957  O   PRO A 492    10890  13955  10539    876    242   5301       O  
ATOM   3958  CB  PRO A 492      13.686   3.291 127.172  1.00 89.04           C  
ANISOU 3958  CB  PRO A 492    10173  14077   9582    804   -426   4748       C  
ATOM   3959  CG  PRO A 492      12.989   3.931 128.295  1.00 89.59           C  
ANISOU 3959  CG  PRO A 492    10294  14433   9313    772   -376   4699       C  
ATOM   3960  CD  PRO A 492      11.773   4.576 127.741  1.00 87.67           C  
ANISOU 3960  CD  PRO A 492    10074  13936   9301    520   -279   4394       C  
ATOM   3961  N   ASP A 493      12.258   0.647 125.275  1.00 90.43           N  
ANISOU 3961  N   ASP A 493    10441  13091  10828    740    164   5069       N  
ATOM   3962  CA  ASP A 493      11.731  -0.718 125.367  1.00 93.80           C  
ANISOU 3962  CA  ASP A 493    10920  13188  11530    827    499   5387       C  
ATOM   3963  C   ASP A 493      12.856  -1.659 125.707  1.00 96.94           C  
ANISOU 3963  C   ASP A 493    11307  13647  11878   1089    506   5777       C  
ATOM   3964  O   ASP A 493      14.012  -1.387 125.408  1.00 96.76           O  
ANISOU 3964  O   ASP A 493    11205  13797  11763   1157    251   5725       O  
ATOM   3965  CB  ASP A 493      11.001  -1.150 124.066  1.00 92.27           C  
ANISOU 3965  CB  ASP A 493    10686  12518  11852    647    637   5172       C  
ATOM   3966  CG  ASP A 493       9.426  -0.932 124.119  1.00 93.29           C  
ANISOU 3966  CG  ASP A 493    10846  12466  12134    465    838   4983       C  
ATOM   3967  OD1 ASP A 493       8.915   0.063 124.703  1.00 90.86           O  
ANISOU 3967  OD1 ASP A 493    10566  12393  11563    385    759   4825       O  
ATOM   3968  OD2 ASP A 493       8.691  -1.775 123.544  1.00 95.53           O  
ANISOU 3968  OD2 ASP A 493    11104  12358  12836    397   1083   4966       O  
ATOM   3969  N   GLU A 494      12.543  -2.757 126.372  1.00100.67           N  
ANISOU 3969  N   GLU A 494    11855  13979  12414   1251    808   6178       N  
ATOM   3970  CA  GLU A 494      13.573  -3.756 126.585  1.00103.82           C  
ANISOU 3970  CA  GLU A 494    12238  14371  12836   1519    840   6574       C  
ATOM   3971  C   GLU A 494      13.563  -4.897 125.607  1.00102.92           C  
ANISOU 3971  C   GLU A 494    12075  13755  13275   1503   1064   6649       C  
ATOM   3972  O   GLU A 494      13.953  -6.036 125.914  1.00106.17           O  
ANISOU 3972  O   GLU A 494    12504  14015  13823   1722   1268   7058       O  
ATOM   3973  CB  GLU A 494      13.677  -4.135 128.060  1.00109.33           C  
ANISOU 3973  CB  GLU A 494    13046  15357  13137   1790    951   7025       C  
ATOM   3974  CG  GLU A 494      14.226  -3.003 128.915  1.00111.62           C  
ANISOU 3974  CG  GLU A 494    13328  16241  12842   1851    617   6919       C  
ATOM   3975  CD  GLU A 494      14.812  -3.513 130.214  1.00118.25           C  
ANISOU 3975  CD  GLU A 494    14241  17428  13261   2198    631   7398       C  
ATOM   3976  OE1 GLU A 494      14.061  -3.563 131.219  1.00121.24           O  
ANISOU 3976  OE1 GLU A 494    14761  17930  13375   2256    833   7592       O  
ATOM   3977  OE2 GLU A 494      16.013  -3.876 130.213  1.00120.66           O  
ANISOU 3977  OE2 GLU A 494    14463  17879  13503   2421    446   7580       O  
ATOM   3978  N   THR A 495      13.174  -4.521 124.401  1.00 97.96           N  
ANISOU 3978  N   THR A 495    11380  12893  12949   1248   1005   6233       N  
ATOM   3979  CA  THR A 495      12.844  -5.410 123.306  1.00 96.20           C  
ANISOU 3979  CA  THR A 495    11097  12181  13273   1144   1221   6148       C  
ATOM   3980  C   THR A 495      13.899  -5.102 122.244  1.00 93.06           C  
ANISOU 3980  C   THR A 495    10599  11804  12958   1099    944   5918       C  
ATOM   3981  O   THR A 495      13.850  -5.597 121.111  1.00 92.59           O  
ANISOU 3981  O   THR A 495    10472  11406  13303    986   1026   5744       O  
ATOM   3982  CB  THR A 495      11.422  -4.917 122.897  1.00 94.24           C  
ANISOU 3982  CB  THR A 495    10861  11767  13179    880   1316   5790       C  
ATOM   3983  OG1 THR A 495      10.528  -5.127 124.005  1.00 96.56           O  
ANISOU 3983  OG1 THR A 495    11249  12078  13359    929   1577   6009       O  
ATOM   3984  CG2 THR A 495      10.888  -5.620 121.628  1.00 91.76           C  
ANISOU 3984  CG2 THR A 495    10461  10985  13418    718   1494   5560       C  
ATOM   3985  N   TYR A 496      14.893  -4.313 122.651  1.00 90.82           N  
ANISOU 3985  N   TYR A 496    10297  11925  12286   1195    630   5917       N  
ATOM   3986  CA  TYR A 496      15.979  -3.865 121.786  1.00 85.50           C  
ANISOU 3986  CA  TYR A 496     9528  11320  11637   1156    363   5695       C  
ATOM   3987  C   TYR A 496      17.311  -4.460 122.257  1.00 87.44           C  
ANISOU 3987  C   TYR A 496     9708  11715  11802   1427    288   6023       C  
ATOM   3988  O   TYR A 496      17.742  -4.249 123.397  1.00 89.85           O  
ANISOU 3988  O   TYR A 496    10028  12388  11721   1622    175   6251       O  
ATOM   3989  CB  TYR A 496      16.038  -2.363 121.852  1.00 82.12           C  
ANISOU 3989  CB  TYR A 496     9103  11234  10865   1029     68   5368       C  
ATOM   3990  CG  TYR A 496      17.299  -1.807 121.269  1.00 77.90           C  
ANISOU 3990  CG  TYR A 496     8473  10847  10278   1028   -200   5187       C  
ATOM   3991  CD1 TYR A 496      17.457  -1.765 119.844  1.00 71.75           C  
ANISOU 3991  CD1 TYR A 496     7659   9792   9811    863   -219   4906       C  
ATOM   3992  CD2 TYR A 496      18.332  -1.339 122.119  1.00 75.71           C  
ANISOU 3992  CD2 TYR A 496     8135  10988   9645   1191   -425   5279       C  
ATOM   3993  CE1 TYR A 496      18.603  -1.268 119.291  1.00 72.11           C  
ANISOU 3993  CE1 TYR A 496     7625   9944   9830    853   -423   4739       C  
ATOM   3994  CE2 TYR A 496      19.476  -0.826 121.586  1.00 73.13           C  
ANISOU 3994  CE2 TYR A 496     7699  10776   9310   1178   -646   5083       C  
ATOM   3995  CZ  TYR A 496      19.616  -0.814 120.182  1.00 70.49           C  
ANISOU 3995  CZ  TYR A 496     7345  10131   9307   1009   -627   4830       C  
ATOM   3996  OH  TYR A 496      20.720  -0.301 119.637  1.00 67.71           O  
ANISOU 3996  OH  TYR A 496     6897   9868   8964    984   -806   4632       O  
ATOM   3997  N   VAL A 497      17.927  -5.253 121.394  1.00 86.37           N  
ANISOU 3997  N   VAL A 497     9491  11290  12034   1451    359   6047       N  
ATOM   3998  CA  VAL A 497      19.229  -5.826 121.658  1.00 87.94           C  
ANISOU 3998  CA  VAL A 497     9599  11585  12231   1699    281   6317       C  
ATOM   3999  C   VAL A 497      20.196  -4.699 121.355  1.00 85.92           C  
ANISOU 3999  C   VAL A 497     9256  11645  11746   1638    -79   6010       C  
ATOM   4000  O   VAL A 497      20.074  -4.080 120.321  1.00 80.75           O  
ANISOU 4000  O   VAL A 497     8591  10874  11218   1404   -151   5628       O  
ATOM   4001  CB  VAL A 497      19.533  -6.963 120.670  1.00 88.13           C  
ANISOU 4001  CB  VAL A 497     9547  11156  12781   1695    491   6363       C  
ATOM   4002  CG1 VAL A 497      20.874  -7.607 120.966  1.00 88.55           C  
ANISOU 4002  CG1 VAL A 497     9490  11285  12869   1970    424   6661       C  
ATOM   4003  CG2 VAL A 497      18.422  -7.954 120.682  1.00 88.72           C  
ANISOU 4003  CG2 VAL A 497     9689  10843  13179   1666    880   6527       C  
ATOM   4004  N   PRO A 498      21.162  -4.452 122.254  1.00 63.43           N  
ANISOU 4004  N   PRO A 498     9014   6752   8335   -422   1802   1185       N  
ATOM   4005  CA  PRO A 498      22.150  -3.390 122.073  1.00 61.44           C  
ANISOU 4005  CA  PRO A 498     8730   6731   7884   -240   1586   1079       C  
ATOM   4006  C   PRO A 498      23.001  -3.654 120.849  1.00 61.46           C  
ANISOU 4006  C   PRO A 498     8834   6530   7987   -274   1573    883       C  
ATOM   4007  O   PRO A 498      23.178  -4.792 120.449  1.00 63.80           O  
ANISOU 4007  O   PRO A 498     9253   6499   8488   -333   1750    885       O  
ATOM   4008  CB  PRO A 498      23.022  -3.480 123.325  1.00 63.32           C  
ANISOU 4008  CB  PRO A 498     8992   7076   7991     72   1608   1355       C  
ATOM   4009  CG  PRO A 498      22.015  -4.073 124.439  1.00 65.47           C  
ANISOU 4009  CG  PRO A 498     9283   7348   8243     38   1810   1626       C  
ATOM   4010  CD  PRO A 498      21.257  -5.097 123.594  1.00 65.93           C  
ANISOU 4010  CD  PRO A 498     9387   7042   8621   -246   1991   1549       C  
ATOM   4011  N   LYS A 499      23.476  -2.593 120.234  1.00 58.61           N  
ANISOU 4011  N   LYS A 499     8428   6347   7494   -251   1394    704       N  
ATOM   4012  CA  LYS A 499      24.421  -2.751 119.166  1.00 60.12           C  
ANISOU 4012  CA  LYS A 499     8722   6380   7741   -253   1431    538       C  
ATOM   4013  C   LYS A 499      25.782  -3.302 119.661  1.00 60.65           C  
ANISOU 4013  C   LYS A 499     8800   6322   7923     20   1543    683       C  
ATOM   4014  O   LYS A 499      26.382  -2.807 120.629  1.00 60.29           O  
ANISOU 4014  O   LYS A 499     8639   6470   7798    253   1439    838       O  
ATOM   4015  CB  LYS A 499      24.636  -1.406 118.488  1.00 57.52           C  
ANISOU 4015  CB  LYS A 499     8338   6272   7244   -282   1241    367       C  
ATOM   4016  CG  LYS A 499      25.057  -1.466 117.052  1.00 57.25           C  
ANISOU 4016  CG  LYS A 499     8454   6101   7195   -414   1293    144       C  
ATOM   4017  CD  LYS A 499      25.492  -0.064 116.649  1.00 57.51           C  
ANISOU 4017  CD  LYS A 499     8423   6352   7076   -378   1139     73       C  
ATOM   4018  CE  LYS A 499      25.214   0.234 115.173  1.00 60.63           C  
ANISOU 4018  CE  LYS A 499     8990   6720   7326   -595   1103   -125       C  
ATOM   4019  NZ  LYS A 499      25.065   1.708 114.930  1.00 57.82           N  
ANISOU 4019  NZ  LYS A 499     8556   6589   6823   -602    896   -125       N  
ATOM   4020  N   ALA A 500      26.262  -4.318 118.966  1.00 61.83           N  
ANISOU 4020  N   ALA A 500     9077   6143   8272     -9   1740    608       N  
ATOM   4021  CA  ALA A 500      27.669  -4.723 119.079  1.00 62.20           C  
ANISOU 4021  CA  ALA A 500     9100   6045   8490    245   1842    675       C  
ATOM   4022  C   ALA A 500      28.597  -3.489 118.979  1.00 60.06           C  
ANISOU 4022  C   ALA A 500     8680   6032   8108    373   1688    593       C  
ATOM   4023  O   ALA A 500      28.346  -2.554 118.209  1.00 58.03           O  
ANISOU 4023  O   ALA A 500     8431   5925   7693    215   1603    401       O  
ATOM   4024  CB  ALA A 500      28.000  -5.758 118.040  1.00 61.74           C  
ANISOU 4024  CB  ALA A 500     9198   5604   8658    153   2097    496       C  
ATOM   4025  N   PHE A 501      29.647  -3.507 119.787  1.00 60.91           N  
ANISOU 4025  N   PHE A 501     8646   6177   8321    660   1639    757       N  
ATOM   4026  CA  PHE A 501      30.630  -2.449 119.859  1.00 60.71           C  
ANISOU 4026  CA  PHE A 501     8428   6360   8278    796   1493    689       C  
ATOM   4027  C   PHE A 501      31.342  -2.314 118.543  1.00 60.85           C  
ANISOU 4027  C   PHE A 501     8470   6228   8423    708   1675    446       C  
ATOM   4028  O   PHE A 501      31.632  -3.314 117.924  1.00 62.81           O  
ANISOU 4028  O   PHE A 501     8828   6172   8863    696   1921    385       O  
ATOM   4029  CB  PHE A 501      31.640  -2.716 120.989  1.00 62.25           C  
ANISOU 4029  CB  PHE A 501     8451   6594   8607   1128   1382    911       C  
ATOM   4030  CG  PHE A 501      32.738  -1.706 121.056  1.00 61.60           C  
ANISOU 4030  CG  PHE A 501     8123   6693   8589   1257   1225    808       C  
ATOM   4031  CD1 PHE A 501      32.493  -0.425 121.498  1.00 59.77           C  
ANISOU 4031  CD1 PHE A 501     7786   6786   8139   1219    985    740       C  
ATOM   4032  CD2 PHE A 501      34.012  -2.038 120.647  1.00 65.52           C  
ANISOU 4032  CD2 PHE A 501     8472   7006   9417   1406   1344    757       C  
ATOM   4033  CE1 PHE A 501      33.490   0.485 121.568  1.00 60.58           C  
ANISOU 4033  CE1 PHE A 501     7647   7019   8352   1312    848    628       C  
ATOM   4034  CE2 PHE A 501      35.016  -1.145 120.724  1.00 62.51           C  
ANISOU 4034  CE2 PHE A 501     7823   6770   9158   1506   1213    659       C  
ATOM   4035  CZ  PHE A 501      34.782   0.103 121.172  1.00 61.78           C  
ANISOU 4035  CZ  PHE A 501     7632   6988   8855   1451    962    591       C  
ATOM   4036  N   ASP A 502      31.582  -1.075 118.115  1.00 59.97           N  
ANISOU 4036  N   ASP A 502     8271   6313   8203    638   1580    307       N  
ATOM   4037  CA  ASP A 502      32.202  -0.764 116.814  1.00 60.76           C  
ANISOU 4037  CA  ASP A 502     8421   6309   8358    526   1781     93       C  
ATOM   4038  C   ASP A 502      33.244   0.338 117.023  1.00 60.73           C  
ANISOU 4038  C   ASP A 502     8153   6459   8460    645   1691     68       C  
ATOM   4039  O   ASP A 502      32.926   1.539 117.119  1.00 58.46           O  
ANISOU 4039  O   ASP A 502     7804   6391   8018    567   1506     41       O  
ATOM   4040  CB  ASP A 502      31.158  -0.369 115.762  1.00 59.79           C  
ANISOU 4040  CB  ASP A 502     8536   6226   7955    229   1790    -55       C  
ATOM   4041  CG  ASP A 502      31.763  -0.178 114.290  1.00 64.69           C  
ANISOU 4041  CG  ASP A 502     9304   6732   8545     97   2051   -265       C  
ATOM   4042  OD1 ASP A 502      30.956   0.055 113.343  1.00 63.84           O  
ANISOU 4042  OD1 ASP A 502     9432   6658   8165   -138   2042   -378       O  
ATOM   4043  OD2 ASP A 502      33.015  -0.266 114.055  1.00 64.97           O  
ANISOU 4043  OD2 ASP A 502     9224   6650   8813    223   2271   -317       O  
ATOM   4044  N   GLU A 503      34.500  -0.105 117.094  1.00 63.38           N  
ANISOU 4044  N   GLU A 503     8312   6650   9120    837   1830     69       N  
ATOM   4045  CA  GLU A 503      35.675   0.764 117.253  1.00 65.23           C  
ANISOU 4045  CA  GLU A 503     8235   6974   9575    953   1782     21       C  
ATOM   4046  C   GLU A 503      35.663   2.062 116.426  1.00 63.00           C  
ANISOU 4046  C   GLU A 503     7965   6795   9177    750   1826   -121       C  
ATOM   4047  O   GLU A 503      35.958   3.129 116.944  1.00 61.60           O  
ANISOU 4047  O   GLU A 503     7566   6793   9044    782   1620   -126       O  
ATOM   4048  CB  GLU A 503      36.933  -0.011 116.856  1.00 69.42           C  
ANISOU 4048  CB  GLU A 503     8619   7247  10512   1108   2068    -30       C  
ATOM   4049  CG  GLU A 503      36.971  -1.451 117.372  1.00 76.66           C  
ANISOU 4049  CG  GLU A 503     9575   7952  11600   1301   2114    114       C  
ATOM   4050  CD  GLU A 503      36.053  -2.343 116.594  1.00 82.58           C  
ANISOU 4050  CD  GLU A 503    10695   8492  12188   1116   2351     47       C  
ATOM   4051  OE1 GLU A 503      36.372  -2.569 115.388  1.00 82.88           O  
ANISOU 4051  OE1 GLU A 503    10862   8339  12291    994   2701   -166       O  
ATOM   4052  OE2 GLU A 503      35.007  -2.778 117.192  1.00 83.70           O  
ANISOU 4052  OE2 GLU A 503    10997   8670  12134   1080   2193    190       O  
ATOM   4053  N   LYS A 504      35.395   1.937 115.126  1.00 63.64           N  
ANISOU 4053  N   LYS A 504     8312   6747   9120    547   2106   -239       N  
ATOM   4054  CA  LYS A 504      35.413   3.071 114.202  1.00 63.52           C  
ANISOU 4054  CA  LYS A 504     8368   6793   8972    357   2197   -325       C  
ATOM   4055  C   LYS A 504      34.432   4.194 114.547  1.00 60.85           C  
ANISOU 4055  C   LYS A 504     8057   6680   8383    253   1874   -263       C  
ATOM   4056  O   LYS A 504      34.646   5.293 114.164  1.00 61.38           O  
ANISOU 4056  O   LYS A 504     8073   6797   8451    167   1880   -284       O  
ATOM   4057  CB  LYS A 504      35.186   2.557 112.790  1.00 65.49           C  
ANISOU 4057  CB  LYS A 504     8971   6887   9024    169   2529   -447       C  
ATOM   4058  CG  LYS A 504      36.346   1.691 112.276  1.00 70.44           C  
ANISOU 4058  CG  LYS A 504     9547   7268   9950    264   2942   -562       C  
ATOM   4059  CD  LYS A 504      36.138   1.194 110.835  1.00 72.65           C  
ANISOU 4059  CD  LYS A 504    10223   7406   9976     67   3305   -737       C  
ATOM   4060  CE  LYS A 504      36.707  -0.207 110.678  1.00 75.14           C  
ANISOU 4060  CE  LYS A 504    10556   7439  10555    185   3621   -861       C  
ATOM   4061  NZ  LYS A 504      37.764  -0.363 109.571  1.00 75.99           N  
ANISOU 4061  NZ  LYS A 504    10716   7365  10793    157   4158  -1056       N  
ATOM   4062  N   LEU A 505      33.391   3.920 115.334  1.00 59.72           N  
ANISOU 4062  N   LEU A 505     7967   6651   8074    274   1616   -180       N  
ATOM   4063  CA  LEU A 505      32.463   4.936 115.786  1.00 56.92           C  
ANISOU 4063  CA  LEU A 505     7592   6496   7540    211   1328   -137       C  
ATOM   4064  C   LEU A 505      32.973   5.788 116.933  1.00 57.25           C  
ANISOU 4064  C   LEU A 505     7320   6690   7743    363   1103   -126       C  
ATOM   4065  O   LEU A 505      32.249   6.698 117.412  1.00 56.42           O  
ANISOU 4065  O   LEU A 505     7173   6740   7525    330    879   -124       O  
ATOM   4066  CB  LEU A 505      31.175   4.263 116.277  1.00 55.36           C  
ANISOU 4066  CB  LEU A 505     7531   6358   7146    181   1184    -66       C  
ATOM   4067  CG  LEU A 505      30.451   3.404 115.220  1.00 59.12           C  
ANISOU 4067  CG  LEU A 505     8312   6696   7457     -1   1334   -116       C  
ATOM   4068  CD1 LEU A 505      29.175   2.711 115.792  1.00 59.14           C  
ANISOU 4068  CD1 LEU A 505     8388   6733   7351    -47   1202    -49       C  
ATOM   4069  CD2 LEU A 505      30.163   4.169 113.891  1.00 51.97           C  
ANISOU 4069  CD2 LEU A 505     7600   5796   6351   -206   1377   -191       C  
ATOM   4070  N   PHE A 506      34.141   5.461 117.481  1.00 57.31           N  
ANISOU 4070  N   PHE A 506     7094   6662   8020    543   1129   -134       N  
ATOM   4071  CA  PHE A 506      34.542   6.142 118.685  1.00 55.91           C  
ANISOU 4071  CA  PHE A 506     6634   6660   7950    689    849   -149       C  
ATOM   4072  C   PHE A 506      36.004   6.423 118.631  1.00 58.05           C  
ANISOU 4072  C   PHE A 506     6604   6858   8595    776    920   -232       C  
ATOM   4073  O   PHE A 506      36.613   6.557 119.658  1.00 58.40           O  
ANISOU 4073  O   PHE A 506     6386   7019   8784    945    687   -250       O  
ATOM   4074  CB  PHE A 506      34.225   5.296 119.911  1.00 57.02           C  
ANISOU 4074  CB  PHE A 506     6771   6916   7979    872    661    -27       C  
ATOM   4075  CG  PHE A 506      32.761   5.003 120.121  1.00 53.53           C  
ANISOU 4075  CG  PHE A 506     6572   6549   7219    785    610     58       C  
ATOM   4076  CD1 PHE A 506      32.288   3.689 120.045  1.00 57.26           C  
ANISOU 4076  CD1 PHE A 506     7236   6898   7623    793    743    182       C  
ATOM   4077  CD2 PHE A 506      31.867   5.995 120.432  1.00 54.58           C  
ANISOU 4077  CD2 PHE A 506     6713   6848   7177    699    445      8       C  
ATOM   4078  CE1 PHE A 506      30.918   3.364 120.257  1.00 53.70           C  
ANISOU 4078  CE1 PHE A 506     6969   6497   6938    692    717    258       C  
ATOM   4079  CE2 PHE A 506      30.449   5.677 120.696  1.00 52.60           C  
ANISOU 4079  CE2 PHE A 506     6637   6668   6681    624    414     86       C  
ATOM   4080  CZ  PHE A 506      30.001   4.374 120.577  1.00 50.14           C  
ANISOU 4080  CZ  PHE A 506     6497   6238   6315    609    553    209       C  
ATOM   4081  N   THR A 507      36.560   6.409 117.417  1.00 59.56           N  
ANISOU 4081  N   THR A 507     6841   6855   8933    663   1254   -284       N  
ATOM   4082  CA  THR A 507      37.890   6.887 117.106  1.00 62.60           C  
ANISOU 4082  CA  THR A 507     6929   7139   9716    680   1411   -381       C  
ATOM   4083  C   THR A 507      37.878   8.289 116.496  1.00 61.87           C  
ANISOU 4083  C   THR A 507     6819   7033   9656    484   1475   -446       C  
ATOM   4084  O   THR A 507      37.106   8.544 115.596  1.00 61.54           O  
ANISOU 4084  O   THR A 507     7088   6949   9344    309   1612   -400       O  
ATOM   4085  CB  THR A 507      38.521   6.028 116.050  1.00 64.85           C  
ANISOU 4085  CB  THR A 507     7300   7195  10147    661   1838   -400       C  
ATOM   4086  OG1 THR A 507      38.270   4.667 116.379  1.00 67.71           O  
ANISOU 4086  OG1 THR A 507     7781   7504  10442    803   1834   -323       O  
ATOM   4087  CG2 THR A 507      40.018   6.274 115.980  1.00 66.57           C  
ANISOU 4087  CG2 THR A 507     7112   7304  10875    740   2004   -493       C  
ATOM   4088  N   PHE A 508      38.803   9.149 116.938  1.00 62.59           N  
ANISOU 4088  N   PHE A 508     6536   7133  10111    513   1384   -548       N  
ATOM   4089  CA  PHE A 508      38.811  10.563 116.636  1.00 61.15           C  
ANISOU 4089  CA  PHE A 508     6284   6918  10035    347   1390   -606       C  
ATOM   4090  C   PHE A 508      40.225  10.945 116.183  1.00 64.58           C  
ANISOU 4090  C   PHE A 508     6382   7180  10976    306   1664   -696       C  
ATOM   4091  O   PHE A 508      41.206  10.381 116.651  1.00 65.89           O  
ANISOU 4091  O   PHE A 508     6225   7336  11474    460   1643   -764       O  
ATOM   4092  CB  PHE A 508      38.375  11.364 117.868  1.00 60.46           C  
ANISOU 4092  CB  PHE A 508     6041   7018   9914    405    950   -691       C  
ATOM   4093  CG  PHE A 508      36.979  10.993 118.398  1.00 58.65           C  
ANISOU 4093  CG  PHE A 508     6100   6962   9223    450    721   -608       C  
ATOM   4094  CD1 PHE A 508      35.828  11.612 117.887  1.00 55.71           C  
ANISOU 4094  CD1 PHE A 508     5994   6581   8593    305    727   -547       C  
ATOM   4095  CD2 PHE A 508      36.812  10.016 119.370  1.00 59.90           C  
ANISOU 4095  CD2 PHE A 508     6256   7275   9229    638    520   -568       C  
ATOM   4096  CE1 PHE A 508      34.538  11.284 118.333  1.00 56.28           C  
ANISOU 4096  CE1 PHE A 508     6277   6797   8308    333    549   -483       C  
ATOM   4097  CE2 PHE A 508      35.443   9.672 119.874  1.00 63.43           C  
ANISOU 4097  CE2 PHE A 508     6965   7872   9263    658    362   -479       C  
ATOM   4098  CZ  PHE A 508      34.323  10.283 119.323  1.00 55.81           C  
ANISOU 4098  CZ  PHE A 508     6219   6893   8094    498    393   -452       C  
ATOM   4099  N   HIS A 509      40.319  11.899 115.255  1.00 65.15           N  
ANISOU 4099  N   HIS A 509     6523   7103  11128    100   1931   -675       N  
ATOM   4100  CA  HIS A 509      41.595  12.347 114.725  1.00 68.53           C  
ANISOU 4100  CA  HIS A 509     6644   7339  12053     19   2269   -743       C  
ATOM   4101  C   HIS A 509      41.631  13.818 114.863  1.00 69.30           C  
ANISOU 4101  C   HIS A 509     6583   7373  12375   -126   2173   -791       C  
ATOM   4102  O   HIS A 509      40.677  14.410 115.354  1.00 66.91           O  
ANISOU 4102  O   HIS A 509     6416   7174  11832   -139   1852   -781       O  
ATOM   4103  CB  HIS A 509      41.687  11.994 113.258  1.00 69.66           C  
ANISOU 4103  CB  HIS A 509     7109   7317  12044   -118   2814   -633       C  
ATOM   4104  CG  HIS A 509      41.047  10.698 112.971  1.00 68.30           C  
ANISOU 4104  CG  HIS A 509     7293   7206  11452    -36   2860   -576       C  
ATOM   4105  ND1 HIS A 509      41.762   9.602 112.544  1.00 68.89           N  
ANISOU 4105  ND1 HIS A 509     7336   7174  11664     48   3196   -625       N  
ATOM   4106  CD2 HIS A 509      39.780  10.277 113.190  1.00 63.28           C  
ANISOU 4106  CD2 HIS A 509     6996   6712  10335    -11   2589   -503       C  
ATOM   4107  CE1 HIS A 509      40.949   8.568 112.457  1.00 67.88           C  
ANISOU 4107  CE1 HIS A 509     7549   7103  11141    106   3136   -586       C  
ATOM   4108  NE2 HIS A 509      39.743   8.950 112.847  1.00 69.91           N  
ANISOU 4108  NE2 HIS A 509     8024   7516  11024     63   2767   -507       N  
ATOM   4109  N   ALA A 510      42.740  14.388 114.414  1.00 72.99           N  
ANISOU 4109  N   ALA A 510     6747   7644  13342   -238   2485   -849       N  
ATOM   4110  CA  ALA A 510      43.059  15.795 114.600  1.00 75.10           C  
ANISOU 4110  CA  ALA A 510     6753   7782  14000   -386   2433   -931       C  
ATOM   4111  C   ALA A 510      42.065  16.678 113.851  1.00 74.24           C  
ANISOU 4111  C   ALA A 510     7065   7575  13570   -558   2535   -739       C  
ATOM   4112  O   ALA A 510      41.981  17.856 114.132  1.00 75.51           O  
ANISOU 4112  O   ALA A 510     7091   7630  13969   -657   2406   -789       O  
ATOM   4113  CB  ALA A 510      44.513  16.055 114.148  1.00 78.86           C  
ANISOU 4113  CB  ALA A 510     6803   8034  15125   -485   2837  -1012       C  
ATOM   4114  N   ASP A 511      41.297  16.098 112.919  1.00 73.36           N  
ANISOU 4114  N   ASP A 511     7454   7490  12927   -585   2737   -530       N  
ATOM   4115  CA  ASP A 511      40.320  16.869 112.163  1.00 73.66           C  
ANISOU 4115  CA  ASP A 511     7903   7455  12630   -722   2785   -313       C  
ATOM   4116  C   ASP A 511      39.264  17.467 113.087  1.00 71.18           C  
ANISOU 4116  C   ASP A 511     7598   7258  12189   -655   2278   -360       C  
ATOM   4117  O   ASP A 511      38.838  18.624 112.925  1.00 72.01           O  
ANISOU 4117  O   ASP A 511     7760   7222  12378   -754   2232   -275       O  
ATOM   4118  CB  ASP A 511      39.675  16.070 111.021  1.00 73.60           C  
ANISOU 4118  CB  ASP A 511     8429   7495  12041   -760   3026   -115       C  
ATOM   4119  CG  ASP A 511      38.841  14.894 111.492  1.00 73.45           C  
ANISOU 4119  CG  ASP A 511     8586   7711  11609   -605   2730   -165       C  
ATOM   4120  OD1 ASP A 511      37.980  15.072 112.384  1.00 76.70           O  
ANISOU 4120  OD1 ASP A 511     8970   8265  11908   -518   2291   -205       O  
ATOM   4121  OD2 ASP A 511      39.013  13.765 110.954  1.00 75.34           O  
ANISOU 4121  OD2 ASP A 511     9007   7979  11642   -577   2964   -170       O  
ATOM   4122  N   ILE A 512      38.894  16.715 114.109  1.00 67.91           N  
ANISOU 4122  N   ILE A 512     7104   7080  11619   -479   1919   -500       N  
ATOM   4123  CA  ILE A 512      37.816  17.160 114.953  1.00 64.92           C  
ANISOU 4123  CA  ILE A 512     6772   6833  11060   -409   1499   -550       C  
ATOM   4124  C   ILE A 512      38.090  18.635 115.416  1.00 66.94           C  
ANISOU 4124  C   ILE A 512     6744   6925  11764   -489   1388   -681       C  
ATOM   4125  O   ILE A 512      37.158  19.427 115.662  1.00 66.03           O  
ANISOU 4125  O   ILE A 512     6730   6790  11567   -495   1184   -668       O  
ATOM   4126  CB  ILE A 512      37.546  16.173 116.117  1.00 61.87           C  
ANISOU 4126  CB  ILE A 512     6302   6722  10483   -209   1167   -686       C  
ATOM   4127  CG1 ILE A 512      36.173  16.492 116.702  1.00 59.77           C  
ANISOU 4127  CG1 ILE A 512     6206   6595   9910   -159    847   -681       C  
ATOM   4128  CG2 ILE A 512      38.630  16.321 117.201  1.00 61.52           C  
ANISOU 4128  CG2 ILE A 512     5786   6728  10860   -119    981   -939       C  
ATOM   4129  CD1 ILE A 512      35.780  15.627 117.883  1.00 63.14           C  
ANISOU 4129  CD1 ILE A 512     6594   7291  10107     23    552   -780       C  
ATOM   4130  N   CYS A 513      39.362  18.991 115.515  1.00 69.94           N  
ANISOU 4130  N   CYS A 513     6751   7164  12660   -552   1535   -822       N  
ATOM   4131  CA  CYS A 513      39.762  20.337 115.911  1.00 73.37           C  
ANISOU 4131  CA  CYS A 513     6881   7397  13599   -658   1464   -985       C  
ATOM   4132  C   CYS A 513      39.676  21.339 114.710  1.00 74.99           C  
ANISOU 4132  C   CYS A 513     7281   7265  13946   -861   1833   -729       C  
ATOM   4133  O   CYS A 513      40.137  22.429 114.789  1.00 76.56           O  
ANISOU 4133  O   CYS A 513     7243   7212  14632   -986   1894   -812       O  
ATOM   4134  CB  CYS A 513      41.213  20.300 116.494  1.00 77.38           C  
ANISOU 4134  CB  CYS A 513     6856   7878  14667   -663   1458  -1254       C  
ATOM   4135  SG  CYS A 513      41.635  18.935 117.709  1.00 76.56           S  
ANISOU 4135  SG  CYS A 513     6515   8150  14424   -400   1081  -1464       S  
ATOM   4136  N   THR A 514      39.113  20.940 113.581  1.00 74.61           N  
ANISOU 4136  N   THR A 514     7676   7206  13466   -898   2082   -409       N  
ATOM   4137  CA  THR A 514      39.253  21.724 112.362  1.00 77.88           C  
ANISOU 4137  CA  THR A 514     8296   7322  13973  -1082   2485   -122       C  
ATOM   4138  C   THR A 514      37.920  22.189 111.886  1.00 76.39           C  
ANISOU 4138  C   THR A 514     8523   7113  13389  -1073   2344    139       C  
ATOM   4139  O   THR A 514      37.749  23.347 111.451  1.00 79.09           O  
ANISOU 4139  O   THR A 514     8933   7174  13945  -1177   2441    319       O  
ATOM   4140  CB  THR A 514      39.819  20.845 111.240  1.00 79.13           C  
ANISOU 4140  CB  THR A 514     8674   7490  13903  -1144   2951     55       C  
ATOM   4141  OG1 THR A 514      41.204  20.674 111.478  1.00 82.06           O  
ANISOU 4141  OG1 THR A 514     8602   7778  14797  -1183   3185   -144       O  
ATOM   4142  CG2 THR A 514      39.614  21.476 109.848  1.00 81.88           C  
ANISOU 4142  CG2 THR A 514     9428   7614  14067  -1309   3343    436       C  
ATOM   4143  N   LEU A 515      36.998  21.248 111.942  1.00 72.30           N  
ANISOU 4143  N   LEU A 515     8270   6875  12327   -947   2122    173       N  
ATOM   4144  CA  LEU A 515      35.659  21.399 111.441  1.00 70.87           C  
ANISOU 4144  CA  LEU A 515     8479   6740  11708   -918   1950    416       C  
ATOM   4145  C   LEU A 515      35.070  22.733 111.757  1.00 71.37           C  
ANISOU 4145  C   LEU A 515     8465   6600  12053   -917   1753    456       C  
ATOM   4146  O   LEU A 515      35.352  23.295 112.799  1.00 71.77           O  
ANISOU 4146  O   LEU A 515     8154   6593  12524   -883   1585    178       O  
ATOM   4147  CB  LEU A 515      34.775  20.320 112.028  1.00 66.29           C  
ANISOU 4147  CB  LEU A 515     7989   6487  10711   -767   1627    302       C  
ATOM   4148  CG  LEU A 515      35.379  18.914 111.938  1.00 66.60           C  
ANISOU 4148  CG  LEU A 515     8052   6704  10551   -736   1789    210       C  
ATOM   4149  CD1 LEU A 515      34.473  17.986 112.724  1.00 65.15           C  
ANISOU 4149  CD1 LEU A 515     7906   6796  10051   -589   1448     95       C  
ATOM   4150  CD2 LEU A 515      35.607  18.406 110.504  1.00 65.87           C  
ANISOU 4150  CD2 LEU A 515     8333   6562  10135   -851   2176    434       C  
ATOM   4151  N   PRO A 516      34.247  23.248 110.843  1.00 72.96           N  
ANISOU 4151  N   PRO A 516     9013   6686  12022   -948   1761    799       N  
ATOM   4152  CA  PRO A 516      33.270  24.297 111.176  1.00 73.24           C  
ANISOU 4152  CA  PRO A 516     9026   6577  12224   -878   1476    859       C  
ATOM   4153  C   PRO A 516      32.561  23.981 112.505  1.00 69.42           C  
ANISOU 4153  C   PRO A 516     8318   6331  11729   -715   1078    525       C  
ATOM   4154  O   PRO A 516      32.493  22.829 112.912  1.00 67.14           O  
ANISOU 4154  O   PRO A 516     8029   6347  11134   -648    986    374       O  
ATOM   4155  CB  PRO A 516      32.283  24.223 110.008  1.00 74.14           C  
ANISOU 4155  CB  PRO A 516     9604   6719  11848   -874   1435   1270       C  
ATOM   4156  CG  PRO A 516      33.133  23.650 108.812  1.00 77.37           C  
ANISOU 4156  CG  PRO A 516    10300   7129  11967  -1020   1866   1480       C  
ATOM   4157  CD  PRO A 516      34.398  23.044 109.385  1.00 75.33           C  
ANISOU 4157  CD  PRO A 516     9723   6925  11972  -1064   2098   1158       C  
ATOM   4158  N   ASP A 517      32.009  24.970 113.172  1.00 69.67           N  
ANISOU 4158  N   ASP A 517     8177   6213  12081   -647    868    416       N  
ATOM   4159  CA  ASP A 517      31.408  24.682 114.479  1.00 68.32           C  
ANISOU 4159  CA  ASP A 517     7800   6278  11880   -499    553     73       C  
ATOM   4160  C   ASP A 517      30.247  23.702 114.469  1.00 64.53           C  
ANISOU 4160  C   ASP A 517     7523   6112  10883   -389    349    152       C  
ATOM   4161  O   ASP A 517      30.251  22.741 115.246  1.00 61.40           O  
ANISOU 4161  O   ASP A 517     7045   6005  10277   -320    250    -65       O  
ATOM   4162  CB  ASP A 517      31.040  25.963 115.263  1.00 70.50           C  
ANISOU 4162  CB  ASP A 517     7842   6322  12623   -443    401   -128       C  
ATOM   4163  CG  ASP A 517      31.569  25.906 116.699  1.00 74.47           C  
ANISOU 4163  CG  ASP A 517     8003   6969  13322   -396    265   -623       C  
ATOM   4164  OD1 ASP A 517      31.012  25.104 117.498  1.00 73.93           O  
ANISOU 4164  OD1 ASP A 517     7927   7241  12921   -271     70   -796       O  
ATOM   4165  OD2 ASP A 517      32.593  26.601 117.014  1.00 81.87           O  
ANISOU 4165  OD2 ASP A 517     8686   7693  14729   -496    358   -836       O  
ATOM   4166  N   THR A 518      29.252  23.945 113.609  1.00 64.59           N  
ANISOU 4166  N   THR A 518     7782   6053  10706   -372    271    470       N  
ATOM   4167  CA  THR A 518      28.154  22.995 113.417  1.00 61.89           C  
ANISOU 4167  CA  THR A 518     7626   5987   9901   -305     81    563       C  
ATOM   4168  C   THR A 518      28.719  21.590 113.168  1.00 59.70           C  
ANISOU 4168  C   THR A 518     7487   5953   9245   -366    218    531       C  
ATOM   4169  O   THR A 518      28.300  20.621 113.778  1.00 57.17           O  
ANISOU 4169  O   THR A 518     7132   5888   8702   -302     98    379       O  
ATOM   4170  CB  THR A 518      27.308  23.422 112.217  1.00 63.77           C  
ANISOU 4170  CB  THR A 518     8146   6105   9978   -316     -2    960       C  
ATOM   4171  OG1 THR A 518      26.883  24.750 112.439  1.00 68.65           O  
ANISOU 4171  OG1 THR A 518     8619   6442  11024   -242   -102   1007       O  
ATOM   4172  CG2 THR A 518      26.124  22.597 112.037  1.00 59.58           C  
ANISOU 4172  CG2 THR A 518     7746   5827   9063   -259   -244   1025       C  
ATOM   4173  N   GLU A 519      29.679  21.457 112.277  1.00 61.46           N  
ANISOU 4173  N   GLU A 519     7864   6075   9414   -490    503    674       N  
ATOM   4174  CA  GLU A 519      30.187  20.121 112.085  1.00 61.69           C  
ANISOU 4174  CA  GLU A 519     8000   6303   9134   -526    648    609       C  
ATOM   4175  C   GLU A 519      30.746  19.472 113.405  1.00 59.49           C  
ANISOU 4175  C   GLU A 519     7414   6190   9000   -439    599    269       C  
ATOM   4176  O   GLU A 519      30.400  18.322 113.719  1.00 56.98           O  
ANISOU 4176  O   GLU A 519     7152   6097   8403   -385    521    195       O  
ATOM   4177  CB  GLU A 519      31.178  20.069 110.942  1.00 63.98           C  
ANISOU 4177  CB  GLU A 519     8491   6458   9361   -666   1020    785       C  
ATOM   4178  CG  GLU A 519      30.545  19.814 109.587  1.00 67.58           C  
ANISOU 4178  CG  GLU A 519     9395   6943   9340   -740   1051   1090       C  
ATOM   4179  CD  GLU A 519      31.584  19.235 108.564  1.00 74.19           C  
ANISOU 4179  CD  GLU A 519    10468   7749   9971   -871   1485   1169       C  
ATOM   4180  OE1 GLU A 519      31.621  19.698 107.391  1.00 78.06           O  
ANISOU 4180  OE1 GLU A 519    11284   8123  10253   -972   1666   1462       O  
ATOM   4181  OE2 GLU A 519      32.367  18.307 108.935  1.00 72.70           O  
ANISOU 4181  OE2 GLU A 519    10145   7649   9828   -863   1660    945       O  
ATOM   4182  N   LYS A 520      31.575  20.218 114.146  1.00 59.85           N  
ANISOU 4182  N   LYS A 520     7149   6115   9478   -430    630     78       N  
ATOM   4183  CA  LYS A 520      32.187  19.743 115.391  1.00 59.49           C  
ANISOU 4183  CA  LYS A 520     6811   6229   9564   -341    537   -231       C  
ATOM   4184  C   LYS A 520      31.140  19.120 116.338  1.00 57.41           C  
ANISOU 4184  C   LYS A 520     6550   6230   9033   -203    263   -344       C  
ATOM   4185  O   LYS A 520      31.335  18.021 116.852  1.00 55.42           O  
ANISOU 4185  O   LYS A 520     6282   6182   8594   -134    237   -427       O  
ATOM   4186  CB  LYS A 520      32.860  20.903 116.124  1.00 60.88           C  
ANISOU 4186  CB  LYS A 520     6656   6238  10238   -352    494   -455       C  
ATOM   4187  CG  LYS A 520      34.341  20.911 116.290  1.00 65.16           C  
ANISOU 4187  CG  LYS A 520     6932   6702  11126   -412    654   -608       C  
ATOM   4188  CD  LYS A 520      34.700  22.019 117.303  1.00 71.94           C  
ANISOU 4188  CD  LYS A 520     7444   7450  12438   -408    483   -919       C  
ATOM   4189  CE  LYS A 520      36.004  22.821 117.049  1.00 77.37           C  
ANISOU 4189  CE  LYS A 520     7854   7850  13693   -559    692  -1006       C  
ATOM   4190  NZ  LYS A 520      36.122  23.438 115.673  1.00 82.98           N  
ANISOU 4190  NZ  LYS A 520     8755   8234  14539   -720   1046   -670       N  
ATOM   4191  N   GLN A 521      30.037  19.839 116.546  1.00 57.27           N  
ANISOU 4191  N   GLN A 521     6546   6184   9031   -161     88   -330       N  
ATOM   4192  CA  GLN A 521      28.990  19.415 117.438  1.00 55.71           C  
ANISOU 4192  CA  GLN A 521     6323   6207   8636    -44   -117   -438       C  
ATOM   4193  C   GLN A 521      28.291  18.196 116.904  1.00 54.49           C  
ANISOU 4193  C   GLN A 521     6407   6211   8087    -58   -113   -264       C  
ATOM   4194  O   GLN A 521      27.999  17.266 117.672  1.00 54.03           O  
ANISOU 4194  O   GLN A 521     6327   6367   7836     16   -175   -356       O  
ATOM   4195  CB  GLN A 521      27.965  20.551 117.666  1.00 57.27           C  
ANISOU 4195  CB  GLN A 521     6450   6291   9020      6   -262   -462       C  
ATOM   4196  CG  GLN A 521      28.571  21.930 117.882  1.00 57.00           C  
ANISOU 4196  CG  GLN A 521     6223   5992   9442    -17   -238   -599       C  
ATOM   4197  CD  GLN A 521      27.511  23.066 117.873  1.00 63.78           C  
ANISOU 4197  CD  GLN A 521     7041   6662  10532     41   -348   -571       C  
ATOM   4198  OE1 GLN A 521      26.285  22.848 117.689  1.00 66.54           O  
ANISOU 4198  OE1 GLN A 521     7480   7093  10708    106   -460   -439       O  
ATOM   4199  NE2 GLN A 521      27.983  24.282 118.058  1.00 63.84           N  
ANISOU 4199  NE2 GLN A 521     6885   6389  10982     18   -314   -699       N  
ATOM   4200  N   ILE A 522      28.035  18.192 115.594  1.00 54.65           N  
ANISOU 4200  N   ILE A 522     6666   6121   7978   -158    -38    -15       N  
ATOM   4201  CA  ILE A 522      27.463  17.027 114.899  1.00 54.02           C  
ANISOU 4201  CA  ILE A 522     6836   6166   7524   -209    -30    121       C  
ATOM   4202  C   ILE A 522      28.388  15.745 114.953  1.00 53.06           C  
ANISOU 4202  C   ILE A 522     6764   6134   7262   -223    153     51       C  
ATOM   4203  O   ILE A 522      27.906  14.587 115.102  1.00 51.89           O  
ANISOU 4203  O   ILE A 522     6708   6126   6882   -211    125     39       O  
ATOM   4204  CB  ILE A 522      27.089  17.359 113.424  1.00 55.53           C  
ANISOU 4204  CB  ILE A 522     7308   6234   7557   -319    -11    388       C  
ATOM   4205  CG1 ILE A 522      25.994  18.415 113.378  1.00 57.56           C  
ANISOU 4205  CG1 ILE A 522     7513   6412   7947   -269   -242    494       C  
ATOM   4206  CG2 ILE A 522      26.610  16.112 112.727  1.00 53.50           C  
ANISOU 4206  CG2 ILE A 522     7309   6111   6908   -391    -12    455       C  
ATOM   4207  CD1 ILE A 522      25.519  18.713 112.003  1.00 57.76           C  
ANISOU 4207  CD1 ILE A 522     7822   6350   7775   -348   -299    789       C  
ATOM   4208  N   LYS A 523      29.694  15.937 114.902  1.00 53.07           N  
ANISOU 4208  N   LYS A 523     6670   6034   7460   -240    342     -3       N  
ATOM   4209  CA  LYS A 523      30.573  14.769 115.065  1.00 53.71           C  
ANISOU 4209  CA  LYS A 523     6736   6180   7490   -212    499    -78       C  
ATOM   4210  C   LYS A 523      30.430  14.203 116.456  1.00 51.35           C  
ANISOU 4210  C   LYS A 523     6254   6065   7191    -68    329   -228       C  
ATOM   4211  O   LYS A 523      30.185  13.038 116.654  1.00 49.86           O  
ANISOU 4211  O   LYS A 523     6156   5979   6810    -29    338   -213       O  
ATOM   4212  CB  LYS A 523      32.017  15.071 114.650  1.00 55.75           C  
ANISOU 4212  CB  LYS A 523     6889   6283   8011   -261    758   -102       C  
ATOM   4213  CG  LYS A 523      32.954  13.895 114.765  1.00 60.24           C  
ANISOU 4213  CG  LYS A 523     7405   6888   8595   -209    929   -174       C  
ATOM   4214  CD  LYS A 523      33.772  13.554 113.488  1.00 62.10           C  
ANISOU 4214  CD  LYS A 523     7806   6973   8816   -320   1312    -92       C  
ATOM   4215  CE  LYS A 523      33.851  12.005 113.285  1.00 63.54           C  
ANISOU 4215  CE  LYS A 523     8140   7209   8796   -278   1443   -117       C  
ATOM   4216  NZ  LYS A 523      34.412  11.272 114.501  1.00 63.25           N  
ANISOU 4216  NZ  LYS A 523     7819   7257   8956    -98   1330   -240       N  
ATOM   4217  N   LYS A 524      30.469  15.080 117.438  1.00 52.83           N  
ANISOU 4217  N   LYS A 524     6208   6288   7577      7    169   -372       N  
ATOM   4218  CA  LYS A 524      30.256  14.675 118.822  1.00 51.71           C  
ANISOU 4218  CA  LYS A 524     5930   6351   7365    148     -4   -512       C  
ATOM   4219  C   LYS A 524      28.883  14.139 119.074  1.00 50.92           C  
ANISOU 4219  C   LYS A 524     5965   6383   7000    170    -92   -444       C  
ATOM   4220  O   LYS A 524      28.778  13.205 119.861  1.00 50.20           O  
ANISOU 4220  O   LYS A 524     5877   6446   6751    259   -121   -458       O  
ATOM   4221  CB  LYS A 524      30.429  15.852 119.736  1.00 52.89           C  
ANISOU 4221  CB  LYS A 524     5842   6511   7741    202   -158   -719       C  
ATOM   4222  CG  LYS A 524      31.827  16.164 120.032  1.00 54.51           C  
ANISOU 4222  CG  LYS A 524     5819   6664   8227    216   -145   -866       C  
ATOM   4223  CD  LYS A 524      31.972  17.619 120.472  1.00 56.14           C  
ANISOU 4223  CD  LYS A 524     5821   6766   8744    192   -253  -1073       C  
ATOM   4224  CE  LYS A 524      33.186  18.194 119.697  1.00 58.36           C  
ANISOU 4224  CE  LYS A 524     5964   6799   9410     72    -79  -1069       C  
ATOM   4225  NZ  LYS A 524      33.687  19.490 120.137  1.00 62.59           N  
ANISOU 4225  NZ  LYS A 524     6242   7187  10352     26   -158  -1303       N  
ATOM   4226  N   GLN A 525      27.818  14.711 118.448  1.00 50.75           N  
ANISOU 4226  N   GLN A 525     6038   6295   6950     96   -140   -357       N  
ATOM   4227  CA  GLN A 525      26.474  14.231 118.805  1.00 48.73           C  
ANISOU 4227  CA  GLN A 525     5832   6167   6514    116   -231   -323       C  
ATOM   4228  C   GLN A 525      26.174  12.874 118.216  1.00 47.87           C  
ANISOU 4228  C   GLN A 525     5923   6085   6180     46   -147   -195       C  
ATOM   4229  O   GLN A 525      25.512  12.096 118.831  1.00 46.79           O  
ANISOU 4229  O   GLN A 525     5790   6065   5922     78   -162   -193       O  
ATOM   4230  CB  GLN A 525      25.409  15.235 118.559  1.00 49.43           C  
ANISOU 4230  CB  GLN A 525     5880   6195   6704     98   -349   -300       C  
ATOM   4231  CG  GLN A 525      25.530  16.533 119.429  1.00 50.97           C  
ANISOU 4231  CG  GLN A 525     5855   6358   7155    190   -426   -490       C  
ATOM   4232  CD  GLN A 525      24.812  17.749 118.772  1.00 52.17           C  
ANISOU 4232  CD  GLN A 525     5978   6322   7524    166   -508   -415       C  
ATOM   4233  OE1 GLN A 525      24.755  17.902 117.542  1.00 48.38           O  
ANISOU 4233  OE1 GLN A 525     5650   5701   7032     74   -503   -205       O  
ATOM   4234  NE2 GLN A 525      24.249  18.585 119.603  1.00 52.40           N  
ANISOU 4234  NE2 GLN A 525     5826   6349   7734    260   -582   -583       N  
ATOM   4235  N   THR A 526      26.753  12.569 117.061  1.00 48.27           N  
ANISOU 4235  N   THR A 526     6142   6012   6186    -54    -24   -107       N  
ATOM   4236  CA  THR A 526      26.727  11.242 116.478  1.00 47.60           C  
ANISOU 4236  CA  THR A 526     6255   5917   5914   -125     93    -46       C  
ATOM   4237  C   THR A 526      27.285  10.219 117.471  1.00 47.98           C  
ANISOU 4237  C   THR A 526     6229   6037   5965    -10    166    -93       C  
ATOM   4238  O   THR A 526      26.658   9.174 117.705  1.00 48.44           O  
ANISOU 4238  O   THR A 526     6367   6135   5904    -21    183    -55       O  
ATOM   4239  CB  THR A 526      27.541  11.271 115.171  1.00 49.23           C  
ANISOU 4239  CB  THR A 526     6643   5977   6087   -229    268      9       C  
ATOM   4240  OG1 THR A 526      26.946  12.221 114.293  1.00 52.36           O  
ANISOU 4240  OG1 THR A 526     7141   6318   6436   -320    173    106       O  
ATOM   4241  CG2 THR A 526      27.666   9.933 114.483  1.00 47.15           C  
ANISOU 4241  CG2 THR A 526     6601   5669   5644   -306    430     16       C  
ATOM   4242  N   ALA A 527      28.450  10.512 118.060  1.00 47.91           N  
ANISOU 4242  N   ALA A 527     6059   6033   6113     99    195   -164       N  
ATOM   4243  CA  ALA A 527      29.148   9.546 118.916  1.00 48.25           C  
ANISOU 4243  CA  ALA A 527     6034   6134   6166    234    233   -172       C  
ATOM   4244  C   ALA A 527      28.291   9.418 120.180  1.00 49.25           C  
ANISOU 4244  C   ALA A 527     6101   6445   6167    329     90   -175       C  
ATOM   4245  O   ALA A 527      28.171   8.352 120.782  1.00 51.35           O  
ANISOU 4245  O   ALA A 527     6419   6762   6328    402    126    -95       O  
ATOM   4246  CB  ALA A 527      30.551  10.038 119.210  1.00 47.28           C  
ANISOU 4246  CB  ALA A 527     5706   5987   6273    324    238   -262       C  
ATOM   4247  N   LEU A 528      27.665  10.503 120.582  1.00 49.08           N  
ANISOU 4247  N   LEU A 528     5981   6504   6162    328    -41   -258       N  
ATOM   4248  CA  LEU A 528      26.715  10.402 121.644  1.00 50.63           C  
ANISOU 4248  CA  LEU A 528     6146   6869   6222    395   -111   -271       C  
ATOM   4249  C   LEU A 528      25.639   9.359 121.361  1.00 50.90           C  
ANISOU 4249  C   LEU A 528     6326   6886   6129    309    -21   -137       C  
ATOM   4250  O   LEU A 528      25.331   8.556 122.249  1.00 53.01           O  
ANISOU 4250  O   LEU A 528     6617   7253   6271    379     26    -71       O  
ATOM   4251  CB  LEU A 528      26.089  11.764 121.957  1.00 50.84           C  
ANISOU 4251  CB  LEU A 528     6042   6941   6333    398   -225   -408       C  
ATOM   4252  CG  LEU A 528      25.245  11.701 123.230  1.00 54.44           C  
ANISOU 4252  CG  LEU A 528     6449   7595   6639    490   -247   -465       C  
ATOM   4253  CD1 LEU A 528      26.104  11.263 124.385  1.00 55.68           C  
ANISOU 4253  CD1 LEU A 528     6589   7918   6649    641   -283   -503       C  
ATOM   4254  CD2 LEU A 528      24.608  13.049 123.568  1.00 56.80           C  
ANISOU 4254  CD2 LEU A 528     6604   7915   7061    509   -325   -641       C  
ATOM   4255  N   VAL A 529      25.086   9.358 120.140  1.00 49.34           N  
ANISOU 4255  N   VAL A 529     6228   6560   5959    152     -2    -94       N  
ATOM   4256  CA  VAL A 529      24.045   8.430 119.748  1.00 48.89           C  
ANISOU 4256  CA  VAL A 529     6281   6468   5827     34     46    -12       C  
ATOM   4257  C   VAL A 529      24.561   6.997 119.626  1.00 50.07           C  
ANISOU 4257  C   VAL A 529     6576   6524   5926     24    202     65       C  
ATOM   4258  O   VAL A 529      23.882   6.012 119.999  1.00 51.53           O  
ANISOU 4258  O   VAL A 529     6806   6701   6073     -9    280    137       O  
ATOM   4259  CB  VAL A 529      23.405   8.873 118.353  1.00 49.73           C  
ANISOU 4259  CB  VAL A 529     6472   6475   5948   -134    -40     -4       C  
ATOM   4260  CG1 VAL A 529      22.664   7.756 117.718  1.00 42.58           C  
ANISOU 4260  CG1 VAL A 529     5703   5505   4971   -284     -4     36       C  
ATOM   4261  CG2 VAL A 529      22.470  10.123 118.563  1.00 46.51           C  
ANISOU 4261  CG2 VAL A 529     5894   6134   5643   -114   -205    -40       C  
ATOM   4262  N   GLU A 530      25.761   6.862 119.091  1.00 50.50           N  
ANISOU 4262  N   GLU A 530     6688   6476   6023     51    278     50       N  
ATOM   4263  CA  GLU A 530      26.303   5.554 118.881  1.00 52.21           C  
ANISOU 4263  CA  GLU A 530     7029   6558   6249     58    444    104       C  
ATOM   4264  C   GLU A 530      26.622   4.937 120.249  1.00 52.78           C  
ANISOU 4264  C   GLU A 530     7024   6711   6318    243    459    198       C  
ATOM   4265  O   GLU A 530      26.356   3.746 120.519  1.00 53.98           O  
ANISOU 4265  O   GLU A 530     7270   6778   6461    248    574    307       O  
ATOM   4266  CB  GLU A 530      27.485   5.626 117.898  1.00 54.25           C  
ANISOU 4266  CB  GLU A 530     7349   6679   6584     42    561     47       C  
ATOM   4267  CG  GLU A 530      27.049   5.972 116.406  1.00 56.63           C  
ANISOU 4267  CG  GLU A 530     7831   6897   6788   -164    581     -5       C  
ATOM   4268  CD  GLU A 530      26.255   4.827 115.718  1.00 62.58           C  
ANISOU 4268  CD  GLU A 530     8796   7546   7436   -321    648    -22       C  
ATOM   4269  OE1 GLU A 530      26.034   3.778 116.386  1.00 60.13           O  
ANISOU 4269  OE1 GLU A 530     8477   7188   7180   -280    715     20       O  
ATOM   4270  OE2 GLU A 530      25.888   4.968 114.501  1.00 64.76           O  
ANISOU 4270  OE2 GLU A 530     9255   7778   7572   -490    633    -78       O  
ATOM   4271  N   LEU A 531      27.071   5.774 121.164  1.00 52.50           N  
ANISOU 4271  N   LEU A 531     6831   6844   6275    388    329    162       N  
ATOM   4272  CA  LEU A 531      27.229   5.314 122.557  1.00 53.59           C  
ANISOU 4272  CA  LEU A 531     6925   7120   6316    570    293    261       C  
ATOM   4273  C   LEU A 531      25.927   4.802 123.160  1.00 53.75           C  
ANISOU 4273  C   LEU A 531     7018   7207   6200    521    358    366       C  
ATOM   4274  O   LEU A 531      25.954   3.774 123.815  1.00 55.83           O  
ANISOU 4274  O   LEU A 531     7362   7451   6402    605    450    537       O  
ATOM   4275  CB  LEU A 531      27.830   6.426 123.415  1.00 53.01           C  
ANISOU 4275  CB  LEU A 531     6678   7245   6217    707    104    142       C  
ATOM   4276  CG  LEU A 531      28.041   6.219 124.904  1.00 55.97           C  
ANISOU 4276  CG  LEU A 531     7024   7835   6407    905      1    205       C  
ATOM   4277  CD1 LEU A 531      29.062   5.145 125.058  1.00 57.48           C  
ANISOU 4277  CD1 LEU A 531     7242   7940   6660   1049     22    364       C  
ATOM   4278  CD2 LEU A 531      28.473   7.568 125.536  1.00 52.60           C  
ANISOU 4278  CD2 LEU A 531     6423   7595   5966    978   -209    -17       C  
ATOM   4279  N   LEU A 532      24.795   5.483 122.945  1.00 51.97           N  
ANISOU 4279  N   LEU A 532     6749   7038   5960    392    328    284       N  
ATOM   4280  CA  LEU A 532      23.543   4.952 123.530  1.00 52.92           C  
ANISOU 4280  CA  LEU A 532     6892   7208   6008    334    434    378       C  
ATOM   4281  C   LEU A 532      22.875   3.801 122.783  1.00 52.46           C  
ANISOU 4281  C   LEU A 532     6944   6941   6049    156    578    465       C  
ATOM   4282  O   LEU A 532      22.230   3.043 123.410  1.00 54.06           O  
ANISOU 4282  O   LEU A 532     7177   7136   6228    139    716    593       O  
ATOM   4283  CB  LEU A 532      22.515   6.025 123.902  1.00 51.42           C  
ANISOU 4283  CB  LEU A 532     6560   7175   5802    303    373    261       C  
ATOM   4284  CG  LEU A 532      22.862   6.509 125.293  1.00 55.62           C  
ANISOU 4284  CG  LEU A 532     7045   7939   6149    496    342    231       C  
ATOM   4285  CD1 LEU A 532      23.079   8.008 125.199  1.00 55.47           C  
ANISOU 4285  CD1 LEU A 532     6883   7994   6200    529    172      4       C  
ATOM   4286  CD2 LEU A 532      21.862   6.158 126.417  1.00 56.80           C  
ANISOU 4286  CD2 LEU A 532     7206   8236   6140    522    510    318       C  
ATOM   4287  N   LYS A 533      22.965   3.698 121.463  1.00 51.79           N  
ANISOU 4287  N   LYS A 533     6925   6689   6065     10    554    382       N  
ATOM   4288  CA  LYS A 533      22.621   2.412 120.821  1.00 53.12           C  
ANISOU 4288  CA  LYS A 533     7230   6633   6321   -142    694    428       C  
ATOM   4289  C   LYS A 533      23.456   1.224 121.369  1.00 54.33           C  
ANISOU 4289  C   LYS A 533     7490   6649   6504    -10    863    586       C  
ATOM   4290  O   LYS A 533      23.032   0.094 121.286  1.00 56.11           O  
ANISOU 4290  O   LYS A 533     7808   6684   6828   -104   1018    664       O  
ATOM   4291  CB  LYS A 533      22.769   2.454 119.273  1.00 52.25           C  
ANISOU 4291  CB  LYS A 533     7230   6380   6244   -307    644    282       C  
ATOM   4292  CG  LYS A 533      22.106   3.640 118.598  1.00 49.09           C  
ANISOU 4292  CG  LYS A 533     6753   6090   5807   -408    442    174       C  
ATOM   4293  CD  LYS A 533      22.143   3.495 117.121  1.00 46.16           C  
ANISOU 4293  CD  LYS A 533     6550   5596   5394   -579    400     68       C  
ATOM   4294  CE  LYS A 533      21.396   4.646 116.516  1.00 50.70           C  
ANISOU 4294  CE  LYS A 533     7055   6282   5928   -657    165     22       C  
ATOM   4295  NZ  LYS A 533      20.824   4.438 115.133  1.00 50.56           N  
ANISOU 4295  NZ  LYS A 533     7194   6197   5821   -870     40    -66       N  
ATOM   4296  N   HIS A 534      24.656   1.476 121.881  1.00 55.10           N  
ANISOU 4296  N   HIS A 534     7560   6818   6559    207    818    629       N  
ATOM   4297  CA  HIS A 534      25.525   0.378 122.386  1.00 57.91           C  
ANISOU 4297  CA  HIS A 534     7992   7035   6978    374    935    806       C  
ATOM   4298  C   HIS A 534      25.260   0.104 123.844  1.00 59.88           C  
ANISOU 4298  C   HIS A 534     8238   7432   7083    526    950   1028       C  
ATOM   4299  O   HIS A 534      25.115  -1.067 124.235  1.00 62.95           O  
ANISOU 4299  O   HIS A 534     8737   7653   7527    555   1116   1241       O  
ATOM   4300  CB  HIS A 534      26.997   0.724 122.177  1.00 57.78           C  
ANISOU 4300  CB  HIS A 534     7909   7014   7029    539    859    746       C  
ATOM   4301  CG  HIS A 534      27.970  -0.305 122.660  1.00 60.94           C  
ANISOU 4301  CG  HIS A 534     8336   7270   7547    748    936    926       C  
ATOM   4302  ND1 HIS A 534      27.821  -1.658 122.414  1.00 63.17           N  
ANISOU 4302  ND1 HIS A 534     8761   7257   7985    715   1146   1046       N  
ATOM   4303  CD2 HIS A 534      29.161  -0.165 123.300  1.00 60.37           C  
ANISOU 4303  CD2 HIS A 534     8145   7283   7510    998    812    993       C  
ATOM   4304  CE1 HIS A 534      28.875  -2.304 122.888  1.00 62.60           C  
ANISOU 4304  CE1 HIS A 534     8662   7081   8043    956   1160   1207       C  
ATOM   4305  NE2 HIS A 534      29.699  -1.424 123.429  1.00 63.29           N  
ANISOU 4305  NE2 HIS A 534     8582   7411   8054   1134    942   1180       N  
ATOM   4306  N   LYS A 535      25.167   1.181 124.637  1.00 58.56           N  
ANISOU 4306  N   LYS A 535     7963   7563   6722    618    796    976       N  
ATOM   4307  CA  LYS A 535      25.006   1.057 126.066  1.00 60.10           C  
ANISOU 4307  CA  LYS A 535     8189   7958   6690    779    802   1160       C  
ATOM   4308  C   LYS A 535      23.668   1.657 126.449  1.00 60.43           C  
ANISOU 4308  C   LYS A 535     8179   8165   6618    653    863   1092       C  
ATOM   4309  O   LYS A 535      23.600   2.673 127.138  1.00 59.99           O  
ANISOU 4309  O   LYS A 535     8041   8372   6381    737    748    977       O  
ATOM   4310  CB  LYS A 535      26.163   1.742 126.825  1.00 60.77           C  
ANISOU 4310  CB  LYS A 535     8196   8270   6624   1023    568   1124       C  
ATOM   4311  CG  LYS A 535      27.547   1.051 126.776  1.00 61.06           C  
ANISOU 4311  CG  LYS A 535     8236   8174   6790   1212    498   1244       C  
ATOM   4312  CD  LYS A 535      27.520  -0.256 127.559  1.00 66.49           C  
ANISOU 4312  CD  LYS A 535     9086   8768   7408   1348    623   1601       C  
ATOM   4313  CE  LYS A 535      28.590  -1.208 127.107  1.00 67.35           C  
ANISOU 4313  CE  LYS A 535     9199   8596   7795   1476    650   1725       C  
ATOM   4314  NZ  LYS A 535      28.205  -2.610 127.453  1.00 69.65           N  
ANISOU 4314  NZ  LYS A 535     9677   8647   8138   1511    873   2063       N  
ATOM   4315  N   PRO A 536      22.572   1.005 126.035  1.00 61.16           N  
ANISOU 4315  N   PRO A 536     8299   8090   6850    449   1055   1144       N  
ATOM   4316  CA  PRO A 536      21.288   1.701 126.167  1.00 60.65           C  
ANISOU 4316  CA  PRO A 536     8108   8159   6778    314   1097   1029       C  
ATOM   4317  C   PRO A 536      20.744   1.927 127.561  1.00 63.10           C  
ANISOU 4317  C   PRO A 536     8417   8715   6844    417   1221   1127       C  
ATOM   4318  O   PRO A 536      19.770   2.672 127.668  1.00 64.29           O  
ANISOU 4318  O   PRO A 536     8422   8984   7022    332   1257    984       O  
ATOM   4319  CB  PRO A 536      20.328   0.802 125.374  1.00 61.37           C  
ANISOU 4319  CB  PRO A 536     8202   7990   7124     61   1258   1059       C  
ATOM   4320  CG  PRO A 536      20.996  -0.472 125.298  1.00 63.18           C  
ANISOU 4320  CG  PRO A 536     8603   7977   7424     99   1378   1248       C  
ATOM   4321  CD  PRO A 536      22.445  -0.177 125.180  1.00 60.46           C  
ANISOU 4321  CD  PRO A 536     8304   7668   6999    300   1203   1216       C  
ATOM   4322  N   LYS A 537      21.297   1.296 128.606  1.00 64.51           N  
ANISOU 4322  N   LYS A 537     8756   8968   6786    600   1296   1370       N  
ATOM   4323  CA  LYS A 537      20.762   1.473 129.960  1.00 65.99           C  
ANISOU 4323  CA  LYS A 537     8999   9416   6658    695   1448   1475       C  
ATOM   4324  C   LYS A 537      21.627   2.451 130.764  1.00 66.11           C  
ANISOU 4324  C   LYS A 537     9027   9749   6342    925   1205   1340       C  
ATOM   4325  O   LYS A 537      21.278   2.794 131.894  1.00 67.06           O  
ANISOU 4325  O   LYS A 537     9213  10137   6131   1019   1295   1352       O  
ATOM   4326  CB  LYS A 537      20.734   0.153 130.738  1.00 69.90           C  
ANISOU 4326  CB  LYS A 537     9711   9821   7026    758   1695   1875       C  
ATOM   4327  CG  LYS A 537      20.180  -1.043 130.021  1.00 71.37           C  
ANISOU 4327  CG  LYS A 537     9919   9631   7569    554   1924   2037       C  
ATOM   4328  CD  LYS A 537      18.652  -0.992 129.933  1.00 74.39           C  
ANISOU 4328  CD  LYS A 537    10153   9978   8134    305   2188   1969       C  
ATOM   4329  CE  LYS A 537      17.979  -1.316 131.264  1.00 78.70           C  
ANISOU 4329  CE  LYS A 537    10807  10672   8424    350   2530   2230       C  
ATOM   4330  NZ  LYS A 537      16.850  -0.370 131.352  1.00 78.66           N  
ANISOU 4330  NZ  LYS A 537    10569  10845   8474    227   2631   1978       N  
ATOM   4331  N   ALA A 538      22.775   2.862 130.200  1.00 69.36           N  
ANISOU 4331  N   ALA A 538     7602  10191   8558    646   1237   -305       N  
ATOM   4332  CA  ALA A 538      23.778   3.670 130.950  1.00 68.00           C  
ANISOU 4332  CA  ALA A 538     7720   9953   8164    893   1132   -338       C  
ATOM   4333  C   ALA A 538      23.139   4.873 131.600  1.00 69.49           C  
ANISOU 4333  C   ALA A 538     7771  10205   8429   1092   1243   -469       C  
ATOM   4334  O   ALA A 538      22.384   5.574 130.961  1.00 70.32           O  
ANISOU 4334  O   ALA A 538     7525  10378   8816   1132   1171   -520       O  
ATOM   4335  CB  ALA A 538      24.935   4.105 130.051  1.00 64.11           C  
ANISOU 4335  CB  ALA A 538     7290   9387   7680    950    746   -319       C  
ATOM   4336  N   THR A 539      23.432   5.119 132.860  1.00 71.38           N  
ANISOU 4336  N   THR A 539     8292  10419   8410   1236   1408   -530       N  
ATOM   4337  CA  THR A 539      22.691   6.137 133.607  1.00 74.99           C  
ANISOU 4337  CA  THR A 539     8640  10929   8925   1413   1606   -684       C  
ATOM   4338  C   THR A 539      23.046   7.568 133.233  1.00 75.42           C  
ANISOU 4338  C   THR A 539     8592  10927   9137   1616   1333   -802       C  
ATOM   4339  O   THR A 539      24.026   7.844 132.502  1.00 73.49           O  
ANISOU 4339  O   THR A 539     8412  10597   8916   1624    993   -766       O  
ATOM   4340  CB  THR A 539      22.971   6.059 135.118  1.00 77.41           C  
ANISOU 4340  CB  THR A 539     9346  11226   8840   1525   1854   -744       C  
ATOM   4341  OG1 THR A 539      24.275   6.618 135.383  1.00 74.57           O  
ANISOU 4341  OG1 THR A 539     9276  10790   8268   1676   1545   -812       O  
ATOM   4342  CG2 THR A 539      22.825   4.615 135.655  1.00 76.79           C  
ANISOU 4342  CG2 THR A 539     9504  11149   8524   1351   2145   -584       C  
ATOM   4343  N   GLU A 540      22.291   8.487 133.812  1.00 78.78           N  
ANISOU 4343  N   GLU A 540     8890  11376   9669   1785   1525   -953       N  
ATOM   4344  CA  GLU A 540      22.508   9.903 133.566  1.00 80.00           C  
ANISOU 4344  CA  GLU A 540     8964  11429  10002   1993   1329  -1077       C  
ATOM   4345  C   GLU A 540      23.758  10.415 134.282  1.00 79.42           C  
ANISOU 4345  C   GLU A 540     9280  11241   9655   2098   1185  -1200       C  
ATOM   4346  O   GLU A 540      24.509  11.205 133.731  1.00 78.81           O  
ANISOU 4346  O   GLU A 540     9213  11034   9697   2159    900  -1234       O  
ATOM   4347  CB  GLU A 540      21.263  10.693 133.968  1.00 83.65           C  
ANISOU 4347  CB  GLU A 540     9152  11932  10698   2159   1603  -1216       C  
ATOM   4348  CG  GLU A 540      21.033  11.967 133.187  1.00 84.62           C  
ANISOU 4348  CG  GLU A 540     9019  11953  11181   2349   1395  -1258       C  
ATOM   4349  CD  GLU A 540      20.730  13.142 134.103  1.00 91.22           C  
ANISOU 4349  CD  GLU A 540     9901  12691  12066   2606   1595  -1494       C  
ATOM   4350  OE1 GLU A 540      21.679  13.940 134.308  1.00 92.11           O  
ANISOU 4350  OE1 GLU A 540    10276  12629  12091   2702   1423  -1602       O  
ATOM   4351  OE2 GLU A 540      19.579  13.250 134.643  1.00 95.74           O  
ANISOU 4351  OE2 GLU A 540    10251  13353  12771   2698   1942  -1593       O  
ATOM   4352  N   GLU A 541      23.975   9.951 135.503  1.00 81.54           N  
ANISOU 4352  N   GLU A 541     9868  11559   9554   2112   1381  -1266       N  
ATOM   4353  CA  GLU A 541      25.228  10.184 136.224  1.00 81.54           C  
ANISOU 4353  CA  GLU A 541    10247  11497   9237   2189   1193  -1382       C  
ATOM   4354  C   GLU A 541      26.438   9.681 135.439  1.00 76.97           C  
ANISOU 4354  C   GLU A 541     9735  10863   8648   2076    830  -1250       C  
ATOM   4355  O   GLU A 541      27.437  10.370 135.355  1.00 76.27           O  
ANISOU 4355  O   GLU A 541     9728  10675   8576   2132    559  -1364       O  
ATOM   4356  CB  GLU A 541      25.195   9.497 137.618  1.00 85.18           C  
ANISOU 4356  CB  GLU A 541    11077  12057   9230   2218   1456  -1414       C  
ATOM   4357  CG  GLU A 541      26.608   9.402 138.317  1.00 88.56           C  
ANISOU 4357  CG  GLU A 541    11912  12470   9267   2286   1175  -1490       C  
ATOM   4358  CD  GLU A 541      27.002   7.989 138.891  1.00 92.40           C  
ANISOU 4358  CD  GLU A 541    12732  13033   9341   2228   1230  -1292       C  
ATOM   4359  OE1 GLU A 541      26.804   6.943 138.222  1.00 89.91           O  
ANISOU 4359  OE1 GLU A 541    12318  12714   9130   2068   1284  -1049       O  
ATOM   4360  OE2 GLU A 541      27.537   7.950 140.028  1.00 96.58           O  
ANISOU 4360  OE2 GLU A 541    13649  13616   9431   2356   1204  -1388       O  
ATOM   4361  N   GLN A 542      26.355   8.472 134.893  1.00 74.14           N  
ANISOU 4361  N   GLN A 542     9337  10557   8275   1908    851  -1031       N  
ATOM   4362  CA  GLN A 542      27.472   7.929 134.149  1.00 70.46           C  
ANISOU 4362  CA  GLN A 542     8930  10035   7806   1812    553   -917       C  
ATOM   4363  C   GLN A 542      27.736   8.730 132.889  1.00 67.87           C  
ANISOU 4363  C   GLN A 542     8354   9614   7820   1789    313   -914       C  
ATOM   4364  O   GLN A 542      28.885   9.075 132.615  1.00 66.05           O  
ANISOU 4364  O   GLN A 542     8199   9292   7604   1799     59   -958       O  
ATOM   4365  CB  GLN A 542      27.252   6.458 133.783  1.00 70.03           C  
ANISOU 4365  CB  GLN A 542     8894  10023   7691   1634    660   -701       C  
ATOM   4366  CG  GLN A 542      26.703   5.581 134.898  1.00 72.72           C  
ANISOU 4366  CG  GLN A 542     9463  10428   7739   1623    993   -643       C  
ATOM   4367  CD  GLN A 542      26.481   4.146 134.459  1.00 73.98           C  
ANISOU 4367  CD  GLN A 542     9640  10571   7898   1422   1117   -435       C  
ATOM   4368  OE1 GLN A 542      26.148   3.867 133.312  1.00 72.53           O  
ANISOU 4368  OE1 GLN A 542     9189  10378   7991   1263   1056   -369       O  
ATOM   4369  NE2 GLN A 542      26.686   3.223 135.375  1.00 77.93           N  
ANISOU 4369  NE2 GLN A 542    10486  11053   8070   1433   1287   -332       N  
ATOM   4370  N   LEU A 543      26.688   9.029 132.124  1.00 66.92           N  
ANISOU 4370  N   LEU A 543     7936   9518   7974   1763    391   -858       N  
ATOM   4371  CA  LEU A 543      26.882   9.771 130.888  1.00 64.90           C  
ANISOU 4371  CA  LEU A 543     7491   9170   7997   1761    168   -812       C  
ATOM   4372  C   LEU A 543      27.476  11.116 131.201  1.00 65.73           C  
ANISOU 4372  C   LEU A 543     7671   9122   8181   1913     61   -981       C  
ATOM   4373  O   LEU A 543      28.321  11.621 130.436  1.00 63.35           O  
ANISOU 4373  O   LEU A 543     7372   8689   8008   1887   -150   -958       O  
ATOM   4374  CB  LEU A 543      25.567   9.972 130.119  1.00 65.50           C  
ANISOU 4374  CB  LEU A 543     7233   9317   8337   1763    236   -735       C  
ATOM   4375  CG  LEU A 543      24.998   8.660 129.590  1.00 64.52           C  
ANISOU 4375  CG  LEU A 543     6990   9329   8194   1561    302   -596       C  
ATOM   4376  CD1 LEU A 543      23.562   8.782 129.217  1.00 61.30           C  
ANISOU 4376  CD1 LEU A 543     6223   9041   8026   1572    406   -584       C  
ATOM   4377  CD2 LEU A 543      25.870   8.058 128.474  1.00 57.37           C  
ANISOU 4377  CD2 LEU A 543     6150   8385   7262   1407     70   -468       C  
ATOM   4378  N   LYS A 544      27.019  11.707 132.315  1.00 68.45           N  
ANISOU 4378  N   LYS A 544     8083   9469   8457   2060    237  -1163       N  
ATOM   4379  CA  LYS A 544      27.600  12.970 132.805  1.00 70.05           C  
ANISOU 4379  CA  LYS A 544     8398   9506   8714   2195    157  -1385       C  
ATOM   4380  C   LYS A 544      29.111  12.799 132.857  1.00 68.54           C  
ANISOU 4380  C   LYS A 544     8399   9252   8390   2112    -89  -1435       C  
ATOM   4381  O   LYS A 544      29.857  13.565 132.231  1.00 67.39           O  
ANISOU 4381  O   LYS A 544     8218   8935   8453   2090   -266  -1471       O  
ATOM   4382  CB  LYS A 544      27.056  13.307 134.178  1.00 73.68           C  
ANISOU 4382  CB  LYS A 544     8988  10011   8996   2338    396  -1603       C  
ATOM   4383  CG  LYS A 544      27.100  14.795 134.596  1.00 77.40           C  
ANISOU 4383  CG  LYS A 544     9493  10291   9624   2506    405  -1865       C  
ATOM   4384  CD  LYS A 544      26.672  14.930 136.071  1.00 81.23           C  
ANISOU 4384  CD  LYS A 544    10179  10855   9828   2631    660  -2108       C  
ATOM   4385  CE  LYS A 544      25.312  14.231 136.283  1.00 83.32           C  
ANISOU 4385  CE  LYS A 544    10296  11302  10062   2647   1006  -1989       C  
ATOM   4386  NZ  LYS A 544      24.793  14.316 137.665  1.00 87.96           N  
ANISOU 4386  NZ  LYS A 544    11083  11972  10365   2763   1332  -2200       N  
ATOM   4387  N   THR A 545      29.540  11.753 133.564  1.00 68.67           N  
ANISOU 4387  N   THR A 545     8608   9403   8079   2067    -87  -1420       N  
ATOM   4388  CA  THR A 545      30.951  11.363 133.652  1.00 68.99           C  
ANISOU 4388  CA  THR A 545     8796   9428   7989   2010   -335  -1452       C  
ATOM   4389  C   THR A 545      31.655  11.232 132.286  1.00 66.45           C  
ANISOU 4389  C   THR A 545     8321   9015   7912   1874   -512  -1302       C  
ATOM   4390  O   THR A 545      32.711  11.805 132.106  1.00 66.15           O  
ANISOU 4390  O   THR A 545     8282   8861   7992   1850   -698  -1416       O  
ATOM   4391  CB  THR A 545      31.126  10.046 134.459  1.00 70.31           C  
ANISOU 4391  CB  THR A 545     9187   9754   7774   2009   -291  -1370       C  
ATOM   4392  OG1 THR A 545      30.453  10.171 135.731  1.00 73.15           O  
ANISOU 4392  OG1 THR A 545     9734  10201   7860   2133    -83  -1496       O  
ATOM   4393  CG2 THR A 545      32.668   9.675 134.647  1.00 67.91           C  
ANISOU 4393  CG2 THR A 545     9015   9444   7345   2007   -596  -1424       C  
ATOM   4394  N   VAL A 546      31.040  10.520 131.330  1.00 65.44           N  
ANISOU 4394  N   VAL A 546     8059   8939   7866   1775   -436  -1071       N  
ATOM   4395  CA  VAL A 546      31.591  10.357 129.966  1.00 63.21           C  
ANISOU 4395  CA  VAL A 546     7662   8586   7770   1646   -565   -924       C  
ATOM   4396  C   VAL A 546      31.739  11.648 129.151  1.00 63.12           C  
ANISOU 4396  C   VAL A 546     7537   8396   8050   1658   -636   -946       C  
ATOM   4397  O   VAL A 546      32.778  11.939 128.608  1.00 62.99           O  
ANISOU 4397  O   VAL A 546     7525   8260   8150   1586   -757   -959       O  
ATOM   4398  CB  VAL A 546      30.794   9.348 129.150  1.00 62.08           C  
ANISOU 4398  CB  VAL A 546     7419   8546   7621   1535   -475   -712       C  
ATOM   4399  CG1 VAL A 546      31.533   9.064 127.821  1.00 60.53           C  
ANISOU 4399  CG1 VAL A 546     7174   8289   7537   1402   -604   -588       C  
ATOM   4400  CG2 VAL A 546      30.664   8.058 129.930  1.00 61.51           C  
ANISOU 4400  CG2 VAL A 546     7489   8594   7290   1505   -364   -670       C  
ATOM   4401  N   MET A 547      30.671  12.395 129.043  1.00 64.84           N  
ANISOU 4401  N   MET A 547     7650   8583   8402   1755   -539   -935       N  
ATOM   4402  CA  MET A 547      30.701  13.675 128.378  1.00 65.64           C  
ANISOU 4402  CA  MET A 547     7687   8478   8775   1810   -583   -934       C  
ATOM   4403  C   MET A 547      31.886  14.588 128.910  1.00 67.08           C  
ANISOU 4403  C   MET A 547     7985   8459   9044   1811   -665  -1162       C  
ATOM   4404  O   MET A 547      32.675  15.112 128.119  1.00 66.56           O  
ANISOU 4404  O   MET A 547     7911   8215   9164   1726   -739  -1123       O  
ATOM   4405  CB  MET A 547      29.266  14.289 128.387  1.00 66.76           C  
ANISOU 4405  CB  MET A 547     7689   8630   9049   1972   -462   -904       C  
ATOM   4406  CG  MET A 547      28.107  13.343 127.731  1.00 67.94           C  
ANISOU 4406  CG  MET A 547     7651   8999   9163   1932   -418   -701       C  
ATOM   4407  SD  MET A 547      26.251  13.873 127.748  1.00 74.82           S  
ANISOU 4407  SD  MET A 547     8235   9955  10237   2135   -285   -677       S  
ATOM   4408  CE  MET A 547      26.369  15.471 126.951  1.00 67.44           C  
ANISOU 4408  CE  MET A 547     7292   8734   9597   2311   -405   -617       C  
ATOM   4409  N   GLU A 548      32.030  14.758 130.229  1.00 69.23           N  
ANISOU 4409  N   GLU A 548     8366   8762   9176   1889   -647  -1411       N  
ATOM   4410  CA  GLU A 548      33.150  15.542 130.789  1.00 71.04           C  
ANISOU 4410  CA  GLU A 548     8683   8830   9478   1867   -762  -1678       C  
ATOM   4411  C   GLU A 548      34.495  14.890 130.420  1.00 69.54           C  
ANISOU 4411  C   GLU A 548     8484   8667   9270   1710   -932  -1656       C  
ATOM   4412  O   GLU A 548      35.410  15.552 129.873  1.00 69.69           O  
ANISOU 4412  O   GLU A 548     8449   8491   9539   1605  -1003  -1715       O  
ATOM   4413  CB  GLU A 548      33.054  15.689 132.332  1.00 74.26           C  
ANISOU 4413  CB  GLU A 548     9244   9322   9650   1983   -743  -1969       C  
ATOM   4414  CG  GLU A 548      31.615  15.836 132.935  1.00 76.38           C  
ANISOU 4414  CG  GLU A 548     9530   9668   9824   2148   -509  -1982       C  
ATOM   4415  CD  GLU A 548      31.593  15.954 134.497  1.00 82.24           C  
ANISOU 4415  CD  GLU A 548    10484  10502  10263   2260   -459  -2284       C  
ATOM   4416  OE1 GLU A 548      32.177  15.049 135.165  1.00 80.91           O  
ANISOU 4416  OE1 GLU A 548    10465  10516   9760   2232   -563  -2310       O  
ATOM   4417  OE2 GLU A 548      30.987  16.947 135.048  1.00 82.92           O  
ANISOU 4417  OE2 GLU A 548    10606  10470  10428   2392   -313  -2492       O  
ATOM   4418  N   ASN A 549      34.598  13.592 130.694  1.00 67.09           N  
ANISOU 4418  N   ASN A 549     8219   8579   8694   1695   -968  -1566       N  
ATOM   4419  CA  ASN A 549      35.773  12.841 130.299  1.00 66.08           C  
ANISOU 4419  CA  ASN A 549     8060   8486   8562   1583  -1109  -1523       C  
ATOM   4420  C   ASN A 549      36.115  13.152 128.835  1.00 65.53           C  
ANISOU 4420  C   ASN A 549     7863   8259   8775   1446  -1078  -1361       C  
ATOM   4421  O   ASN A 549      37.287  13.343 128.523  1.00 66.11           O  
ANISOU 4421  O   ASN A 549     7871   8234   9013   1344  -1165  -1444       O  
ATOM   4422  CB  ASN A 549      35.586  11.327 130.511  1.00 64.59           C  
ANISOU 4422  CB  ASN A 549     7945   8508   8087   1598  -1096  -1364       C  
ATOM   4423  CG  ASN A 549      35.632  10.892 132.012  1.00 65.44           C  
ANISOU 4423  CG  ASN A 549     8241   8765   7859   1732  -1153  -1509       C  
ATOM   4424  OD1 ASN A 549      36.262  11.511 132.836  1.00 68.22           O  
ANISOU 4424  OD1 ASN A 549     8650   9099   8174   1792  -1297  -1761       O  
ATOM   4425  ND2 ASN A 549      34.977   9.800 132.327  1.00 68.04           N  
ANISOU 4425  ND2 ASN A 549     8682   9235   7935   1768  -1037  -1347       N  
ATOM   4426  N   PHE A 550      35.086  13.256 127.962  1.00 64.26           N  
ANISOU 4426  N   PHE A 550     7666   8080   8671   1451   -952  -1143       N  
ATOM   4427  CA  PHE A 550      35.274  13.452 126.536  1.00 62.36           C  
ANISOU 4427  CA  PHE A 550     7366   7723   8606   1342   -917   -948       C  
ATOM   4428  C   PHE A 550      35.682  14.876 126.187  1.00 64.90           C  
ANISOU 4428  C   PHE A 550     7680   7760   9218   1321   -892  -1016       C  
ATOM   4429  O   PHE A 550      36.597  15.043 125.378  1.00 66.20           O  
ANISOU 4429  O   PHE A 550     7823   7795   9537   1183   -877   -968       O  
ATOM   4430  CB  PHE A 550      34.058  12.972 125.710  1.00 61.64           C  
ANISOU 4430  CB  PHE A 550     7244   7745   8431   1362   -848   -697       C  
ATOM   4431  CG  PHE A 550      34.202  13.208 124.208  1.00 60.59           C  
ANISOU 4431  CG  PHE A 550     7103   7510   8410   1270   -830   -488       C  
ATOM   4432  CD1 PHE A 550      34.921  12.374 123.425  1.00 61.24           C  
ANISOU 4432  CD1 PHE A 550     7202   7639   8429   1128   -831   -399       C  
ATOM   4433  CD2 PHE A 550      33.626  14.309 123.594  1.00 67.15           C  
ANISOU 4433  CD2 PHE A 550     7936   8181   9395   1348   -802   -378       C  
ATOM   4434  CE1 PHE A 550      35.071  12.581 122.042  1.00 59.97           C  
ANISOU 4434  CE1 PHE A 550     7079   7395   8312   1043   -789   -211       C  
ATOM   4435  CE2 PHE A 550      33.772  14.516 122.200  1.00 65.84           C  
ANISOU 4435  CE2 PHE A 550     7821   7926   9268   1279   -786   -156       C  
ATOM   4436  CZ  PHE A 550      34.502  13.637 121.447  1.00 61.48           C  
ANISOU 4436  CZ  PHE A 550     7304   7448   8609   1117   -773    -82       C  
ATOM   4437  N   VAL A 551      35.015  15.895 126.752  1.00 65.78           N  
ANISOU 4437  N   VAL A 551     7818   7751   9424   1449   -851  -1124       N  
ATOM   4438  CA  VAL A 551      35.448  17.306 126.617  1.00 66.64           C  
ANISOU 4438  CA  VAL A 551     7952   7532   9837   1431   -809  -1233       C  
ATOM   4439  C   VAL A 551      36.950  17.510 126.918  1.00 67.07           C  
ANISOU 4439  C   VAL A 551     7974   7474  10035   1265   -882  -1470       C  
ATOM   4440  O   VAL A 551      37.663  18.040 126.081  1.00 67.79           O  
ANISOU 4440  O   VAL A 551     8044   7344  10367   1125   -815  -1410       O  
ATOM   4441  CB  VAL A 551      34.581  18.310 127.494  1.00 69.14           C  
ANISOU 4441  CB  VAL A 551     8315   7728  10226   1617   -752  -1403       C  
ATOM   4442  CG1 VAL A 551      35.152  19.689 127.438  1.00 70.50           C  
ANISOU 4442  CG1 VAL A 551     8534   7523  10728   1573   -702  -1553       C  
ATOM   4443  CG2 VAL A 551      33.129  18.357 127.031  1.00 67.65           C  
ANISOU 4443  CG2 VAL A 551     8093   7598  10014   1791   -671  -1170       C  
ATOM   4444  N   ALA A 552      37.395  17.120 128.115  1.00 66.51           N  
ANISOU 4444  N   ALA A 552     7898   7555   9816   1287  -1014  -1738       N  
ATOM   4445  CA  ALA A 552      38.830  17.121 128.538  1.00 67.31           C  
ANISOU 4445  CA  ALA A 552     7914   7632  10028   1152  -1156  -2001       C  
ATOM   4446  C   ALA A 552      39.788  16.581 127.473  1.00 66.95           C  
ANISOU 4446  C   ALA A 552     7748   7575  10116    979  -1132  -1850       C  
ATOM   4447  O   ALA A 552      40.828  17.208 127.143  1.00 68.73           O  
ANISOU 4447  O   ALA A 552     7864   7597  10653    811  -1110  -1980       O  
ATOM   4448  CB  ALA A 552      39.015  16.266 129.842  1.00 65.78           C  
ANISOU 4448  CB  ALA A 552     7758   7727   9510   1255  -1350  -2195       C  
ATOM   4449  N   PHE A 553      39.434  15.392 126.981  1.00 63.93           N  
ANISOU 4449  N   PHE A 553     7380   7404   9505   1012  -1115  -1602       N  
ATOM   4450  CA  PHE A 553      40.160  14.707 125.947  1.00 63.16           C  
ANISOU 4450  CA  PHE A 553     7201   7326   9470    880  -1059  -1443       C  
ATOM   4451  C   PHE A 553      40.316  15.575 124.666  1.00 64.79           C  
ANISOU 4451  C   PHE A 553     7415   7263   9937    742   -861  -1283       C  
ATOM   4452  O   PHE A 553      41.432  15.776 124.171  1.00 66.78           O  
ANISOU 4452  O   PHE A 553     7560   7384  10429    575   -791  -1343       O  
ATOM   4453  CB  PHE A 553      39.454  13.345 125.706  1.00 61.03           C  
ANISOU 4453  CB  PHE A 553     6997   7304   8886    956  -1055  -1219       C  
ATOM   4454  CG  PHE A 553      39.833  12.631 124.421  1.00 57.37           C  
ANISOU 4454  CG  PHE A 553     6508   6852   8437    837   -946  -1011       C  
ATOM   4455  CD1 PHE A 553      41.093  12.089 124.246  1.00 59.03           C  
ANISOU 4455  CD1 PHE A 553     6598   7074   8758    747   -963  -1097       C  
ATOM   4456  CD2 PHE A 553      38.891  12.452 123.416  1.00 55.94           C  
ANISOU 4456  CD2 PHE A 553     6420   6692   8143    831   -835   -748       C  
ATOM   4457  CE1 PHE A 553      41.433  11.376 123.043  1.00 57.57           C  
ANISOU 4457  CE1 PHE A 553     6408   6897   8567    644   -820   -923       C  
ATOM   4458  CE2 PHE A 553      39.200  11.790 122.220  1.00 56.49           C  
ANISOU 4458  CE2 PHE A 553     6508   6781   8174    720   -731   -580       C  
ATOM   4459  CZ  PHE A 553      40.489  11.237 122.040  1.00 57.07           C  
ANISOU 4459  CZ  PHE A 553     6484   6846   8352    623   -701   -672       C  
ATOM   4460  N   VAL A 554      39.224  16.104 124.132  1.00 64.03           N  
ANISOU 4460  N   VAL A 554     7445   7078   9804    819   -763  -1074       N  
ATOM   4461  CA  VAL A 554      39.335  16.911 122.947  1.00 64.99           C  
ANISOU 4461  CA  VAL A 554     7634   6941  10118    724   -585   -882       C  
ATOM   4462  C   VAL A 554      40.110  18.171 123.258  1.00 69.71           C  
ANISOU 4462  C   VAL A 554     8198   7214  11075    617   -519  -1097       C  
ATOM   4463  O   VAL A 554      40.969  18.603 122.441  1.00 71.85           O  
ANISOU 4463  O   VAL A 554     8454   7266  11580    431   -349  -1044       O  
ATOM   4464  CB  VAL A 554      37.969  17.283 122.404  1.00 65.23           C  
ANISOU 4464  CB  VAL A 554     7801   6946  10038    878   -547   -620       C  
ATOM   4465  CG1 VAL A 554      38.092  18.223 121.176  1.00 65.57           C  
ANISOU 4465  CG1 VAL A 554     7975   6687  10251    813   -371   -384       C  
ATOM   4466  CG2 VAL A 554      37.197  16.020 122.061  1.00 61.26           C  
ANISOU 4466  CG2 VAL A 554     7301   6764   9213    942   -617   -443       C  
ATOM   4467  N   ASP A 555      39.831  18.769 124.424  1.00 70.45           N  
ANISOU 4467  N   ASP A 555     8286   7260  11220    714   -623  -1355       N  
ATOM   4468  CA  ASP A 555      40.551  19.975 124.818  1.00 73.86           C  
ANISOU 4468  CA  ASP A 555     8686   7369  12010    595   -575  -1621       C  
ATOM   4469  C   ASP A 555      42.054  19.680 124.851  1.00 73.70           C  
ANISOU 4469  C   ASP A 555     8459   7360  12185    367   -606  -1834       C  
ATOM   4470  O   ASP A 555      42.864  20.355 124.206  1.00 74.60           O  
ANISOU 4470  O   ASP A 555     8521   7191  12634    158   -427  -1846       O  
ATOM   4471  CB  ASP A 555      40.050  20.504 126.172  1.00 75.07           C  
ANISOU 4471  CB  ASP A 555     8874   7519  12129    739   -704  -1926       C  
ATOM   4472  CG  ASP A 555      38.783  21.322 126.049  1.00 80.46           C  
ANISOU 4472  CG  ASP A 555     9722   8022  12826    929   -593  -1776       C  
ATOM   4473  OD1 ASP A 555      38.129  21.600 127.110  1.00 85.43           O  
ANISOU 4473  OD1 ASP A 555    10399   8697  13365   1092   -660  -1987       O  
ATOM   4474  OD2 ASP A 555      38.423  21.702 124.895  1.00 83.30           O  
ANISOU 4474  OD2 ASP A 555    10175   8196  13281    936   -436  -1447       O  
ATOM   4475  N   LYS A 556      42.380  18.648 125.619  1.00 72.38           N  
ANISOU 4475  N   LYS A 556     8173   7520  11808    424   -826  -1991       N  
ATOM   4476  CA  LYS A 556      43.737  18.177 125.836  1.00 73.54           C  
ANISOU 4476  CA  LYS A 556     8078   7759  12106    280   -933  -2216       C  
ATOM   4477  C   LYS A 556      44.499  18.078 124.511  1.00 74.40           C  
ANISOU 4477  C   LYS A 556     8095   7734  12440     79   -688  -2028       C  
ATOM   4478  O   LYS A 556      45.530  18.734 124.320  1.00 75.95           O  
ANISOU 4478  O   LYS A 556     8121   7712  13026   -140   -584  -2208       O  
ATOM   4479  CB  LYS A 556      43.623  16.807 126.506  1.00 71.55           C  
ANISOU 4479  CB  LYS A 556     7804   7896  11486    451  -1162  -2220       C  
ATOM   4480  CG  LYS A 556      44.805  15.901 126.384  1.00 70.51           C  
ANISOU 4480  CG  LYS A 556     7443   7917  11429    380  -1251  -2294       C  
ATOM   4481  CD  LYS A 556      45.834  16.242 127.389  1.00 68.12           C  
ANISOU 4481  CD  LYS A 556     6924   7636  11322    333  -1496  -2710       C  
ATOM   4482  CE  LYS A 556      46.960  15.281 127.204  1.00 70.03           C  
ANISOU 4482  CE  LYS A 556     6905   8042  11660    306  -1589  -2756       C  
ATOM   4483  NZ  LYS A 556      48.261  15.769 127.784  1.00 73.13           N  
ANISOU 4483  NZ  LYS A 556     6964   8404  12417    179  -1784  -3171       N  
ATOM   4484  N   CYS A 557      43.921  17.300 123.583  1.00 72.36           N  
ANISOU 4484  N   CYS A 557     7965   7597  11932    142   -572  -1674       N  
ATOM   4485  CA  CYS A 557      44.534  16.996 122.299  1.00 72.82           C  
ANISOU 4485  CA  CYS A 557     7992   7588  12090    -17   -326  -1474       C  
ATOM   4486  C   CYS A 557      44.462  18.051 121.212  1.00 74.76           C  
ANISOU 4486  C   CYS A 557     8392   7487  12527   -155    -16  -1263       C  
ATOM   4487  O   CYS A 557      45.304  18.077 120.304  1.00 76.24           O  
ANISOU 4487  O   CYS A 557     8521   7548  12898   -348    235  -1191       O  
ATOM   4488  CB  CYS A 557      44.011  15.675 121.783  1.00 69.86           C  
ANISOU 4488  CB  CYS A 557     7706   7489  11347     97   -345  -1229       C  
ATOM   4489  SG  CYS A 557      44.702  14.318 122.716  1.00 71.34           S  
ANISOU 4489  SG  CYS A 557     7680   7996  11429    188   -600  -1448       S  
ATOM   4490  N   CYS A 558      43.469  18.911 121.284  1.00 75.39           N  
ANISOU 4490  N   CYS A 558     8678   7401  12566    -45     -8  -1151       N  
ATOM   4491  CA  CYS A 558      43.481  20.052 120.412  1.00 79.34           C  
ANISOU 4491  CA  CYS A 558     9345   7513  13287   -156    271   -967       C  
ATOM   4492  C   CYS A 558      44.503  21.096 120.866  1.00 82.88           C  
ANISOU 4492  C   CYS A 558     9642   7632  14219   -378    374  -1280       C  
ATOM   4493  O   CYS A 558      44.664  22.080 120.156  1.00 86.79           O  
ANISOU 4493  O   CYS A 558    10278   7745  14954   -510    656  -1139       O  
ATOM   4494  CB  CYS A 558      42.080  20.681 120.269  1.00 79.30           C  
ANISOU 4494  CB  CYS A 558     9608   7404  13119     68    247   -724       C  
ATOM   4495  SG  CYS A 558      40.811  19.549 119.488  1.00 79.56           S  
ANISOU 4495  SG  CYS A 558     9801   7802  12627    289    142   -338       S  
ATOM   4496  N   ALA A 559      45.190  20.911 122.001  1.00 82.48           N  
ANISOU 4496  N   ALA A 559     9320   7709  14311   -427    153  -1695       N  
ATOM   4497  CA  ALA A 559      46.220  21.902 122.425  1.00 86.52           C  
ANISOU 4497  CA  ALA A 559     9640   7913  15319   -677    227  -2050       C  
ATOM   4498  C   ALA A 559      47.708  21.547 122.172  1.00 87.79           C  
ANISOU 4498  C   ALA A 559     9453   8102  15801   -946    324  -2247       C  
ATOM   4499  O   ALA A 559      48.544  22.448 121.995  1.00 92.17           O  
ANISOU 4499  O   ALA A 559     9878   8320  16824  -1224    540  -2419       O  
ATOM   4500  CB  ALA A 559      46.002  22.378 123.877  1.00 87.01           C  
ANISOU 4500  CB  ALA A 559     9649   7993  15417   -585    -70  -2449       C  
ATOM   4501  N   ALA A 560      48.022  20.264 122.113  1.00 84.34           N  
ANISOU 4501  N   ALA A 560     8861   8036  15151   -867    197  -2218       N  
ATOM   4502  CA  ALA A 560      49.411  19.782 122.034  1.00 86.16           C  
ANISOU 4502  CA  ALA A 560     8698   8354  15683  -1056    230  -2445       C  
ATOM   4503  C   ALA A 560      50.162  20.069 120.708  1.00 88.84           C  
ANISOU 4503  C   ALA A 560     8997   8436  16321  -1331    714  -2270       C  
ATOM   4504  O   ALA A 560      49.530  20.272 119.657  1.00 88.00           O  
ANISOU 4504  O   ALA A 560     9232   8174  16029  -1323   1006  -1872       O  
ATOM   4505  CB  ALA A 560      49.431  18.276 122.347  1.00 82.63           C  
ANISOU 4505  CB  ALA A 560     8142   8354  14900   -839    -35  -2430       C  
ATOM   4506  N   ASP A 561      51.505  20.058 120.761  1.00 92.35           N  
ANISOU 4506  N   ASP A 561     9020   8853  17214  -1564    794  -2569       N  
ATOM   4507  CA  ASP A 561      52.375  20.260 119.575  1.00 96.06           C  
ANISOU 4507  CA  ASP A 561     9390   9097  18012  -1852   1300  -2455       C  
ATOM   4508  C   ASP A 561      52.271  19.182 118.476  1.00 94.44           C  
ANISOU 4508  C   ASP A 561     9327   9083  17473  -1762   1525  -2105       C  
ATOM   4509  O   ASP A 561      52.759  19.401 117.359  1.00 97.21           O  
ANISOU 4509  O   ASP A 561     9728   9229  17980  -1975   2005  -1930       O  
ATOM   4510  CB  ASP A 561      53.845  20.393 120.007  1.00100.72           C  
ANISOU 4510  CB  ASP A 561     9406   9668  19195  -2108   1297  -2914       C  
ATOM   4511  CG  ASP A 561      54.791  20.898 118.875  1.00106.25           C  
ANISOU 4511  CG  ASP A 561     9973  10044  20353  -2478   1902  -2852       C  
ATOM   4512  OD1 ASP A 561      54.856  22.128 118.619  1.00110.52           O  
ANISOU 4512  OD1 ASP A 561    10632  10147  21212  -2736   2206  -2846       O  
ATOM   4513  OD2 ASP A 561      55.518  20.069 118.281  1.00107.72           O  
ANISOU 4513  OD2 ASP A 561     9924  10396  20610  -2517   2096  -2830       O  
ATOM   4514  N   ASP A 562      51.672  18.024 118.794  1.00 90.60           N  
ANISOU 4514  N   ASP A 562     8915   8971  16538  -1465   1207  -2022       N  
ATOM   4515  CA  ASP A 562      51.506  16.891 117.860  1.00 88.33           C  
ANISOU 4515  CA  ASP A 562     8771   8884  15908  -1362   1365  -1743       C  
ATOM   4516  C   ASP A 562      50.165  16.217 118.222  1.00 83.75           C  
ANISOU 4516  C   ASP A 562     8501   8554  14768  -1048   1031  -1548       C  
ATOM   4517  O   ASP A 562      50.075  15.343 119.103  1.00 82.36           O  
ANISOU 4517  O   ASP A 562     8191   8665  14438   -849    670  -1695       O  
ATOM   4518  CB  ASP A 562      52.734  15.953 117.924  1.00 89.57           C  
ANISOU 4518  CB  ASP A 562     8479   9236  16319  -1397   1376  -1987       C  
ATOM   4519  CG  ASP A 562      52.555  14.616 117.156  1.00 89.08           C  
ANISOU 4519  CG  ASP A 562     8552   9402  15891  -1247   1481  -1766       C  
ATOM   4520  OD1 ASP A 562      51.570  14.425 116.397  1.00 87.37           O  
ANISOU 4520  OD1 ASP A 562     8771   9192  15233  -1171   1593  -1423       O  
ATOM   4521  OD2 ASP A 562      53.438  13.730 117.324  1.00 90.25           O  
ANISOU 4521  OD2 ASP A 562     8350   9726  16215  -1199   1436  -1961       O  
ATOM   4522  N   LYS A 563      49.118  16.652 117.536  1.00 81.97           N  
ANISOU 4522  N   LYS A 563     8689   8206  14248  -1005   1161  -1209       N  
ATOM   4523  CA  LYS A 563      47.772  16.338 117.938  1.00 78.52           C  
ANISOU 4523  CA  LYS A 563     8509   7946  13380   -746    865  -1055       C  
ATOM   4524  C   LYS A 563      47.483  14.925 117.579  1.00 75.24           C  
ANISOU 4524  C   LYS A 563     8153   7836  12599   -608    799   -929       C  
ATOM   4525  O   LYS A 563      46.810  14.227 118.315  1.00 72.23           O  
ANISOU 4525  O   LYS A 563     7792   7689  11962   -408    491   -958       O  
ATOM   4526  CB  LYS A 563      46.752  17.244 117.228  1.00 80.14           C  
ANISOU 4526  CB  LYS A 563     9104   7930  13415   -722   1012   -726       C  
ATOM   4527  CG  LYS A 563      46.778  18.731 117.612  1.00 83.22           C  
ANISOU 4527  CG  LYS A 563     9522   7954  14142   -817   1078   -813       C  
ATOM   4528  CD  LYS A 563      47.018  19.600 116.381  1.00 88.38           C  
ANISOU 4528  CD  LYS A 563    10407   8248  14924  -1003   1518   -543       C  
ATOM   4529  CE  LYS A 563      45.716  20.055 115.739  1.00 89.02           C  
ANISOU 4529  CE  LYS A 563    10921   8238  14665   -818   1523   -145       C  
ATOM   4530  NZ  LYS A 563      45.223  21.335 116.377  1.00 91.03           N  
ANISOU 4530  NZ  LYS A 563    11265   8177  15146   -761   1457   -195       N  
ATOM   4531  N   GLU A 564      48.012  14.504 116.434  1.00 76.29           N  
ANISOU 4531  N   GLU A 564     8327   7946  12712   -730   1123   -798       N  
ATOM   4532  CA  GLU A 564      47.875  13.131 115.989  1.00 73.83           C  
ANISOU 4532  CA  GLU A 564     8072   7887  12093   -630   1112   -715       C  
ATOM   4533  C   GLU A 564      48.426  12.163 117.032  1.00 72.66           C  
ANISOU 4533  C   GLU A 564     7606   7956  12047   -506    837   -988       C  
ATOM   4534  O   GLU A 564      47.745  11.226 117.462  1.00 69.73           O  
ANISOU 4534  O   GLU A 564     7321   7799  11373   -318    594   -951       O  
ATOM   4535  CB  GLU A 564      48.545  12.945 114.650  1.00 75.88           C  
ANISOU 4535  CB  GLU A 564     8405   8057  12367   -800   1549   -596       C  
ATOM   4536  CG  GLU A 564      48.160  13.994 113.632  1.00 79.95           C  
ANISOU 4536  CG  GLU A 564     9258   8327  12792   -923   1842   -311       C  
ATOM   4537  CD  GLU A 564      49.058  15.214 113.721  1.00 87.30           C  
ANISOU 4537  CD  GLU A 564    10021   8935  14214  -1145   2091   -423       C  
ATOM   4538  OE1 GLU A 564      48.809  16.059 114.628  1.00 86.56           O  
ANISOU 4538  OE1 GLU A 564     9850   8721  14320  -1120   1877   -536       O  
ATOM   4539  OE2 GLU A 564      50.022  15.307 112.892  1.00 89.69           O  
ANISOU 4539  OE2 GLU A 564    10265   9098  14716  -1356   2525   -420       O  
ATOM   4540  N   ALA A 565      49.645  12.395 117.485  1.00 75.34           N  
ANISOU 4540  N   ALA A 565     7572   8233  12820   -604    859  -1265       N  
ATOM   4541  CA  ALA A 565      50.162  11.520 118.527  1.00 75.21           C  
ANISOU 4541  CA  ALA A 565     7264   8429  12883   -441    541  -1509       C  
ATOM   4542  C   ALA A 565      49.268  11.657 119.758  1.00 73.10           C  
ANISOU 4542  C   ALA A 565     7100   8273  12400   -255    130  -1554       C  
ATOM   4543  O   ALA A 565      49.106  10.718 120.496  1.00 72.00           O  
ANISOU 4543  O   ALA A 565     6937   8342  12076    -53   -139  -1603       O  
ATOM   4544  CB  ALA A 565      51.595  11.833 118.848  1.00 78.45           C  
ANISOU 4544  CB  ALA A 565     7212   8775  13819   -567    579  -1825       C  
ATOM   4545  N   CYS A 566      48.653  12.812 119.961  1.00 72.26           N  
ANISOU 4545  N   CYS A 566     7139   8013  12304   -313    112  -1523       N  
ATOM   4546  CA  CYS A 566      47.841  12.945 121.142  1.00 71.10           C  
ANISOU 4546  CA  CYS A 566     7082   7972  11961   -136   -233  -1595       C  
ATOM   4547  C   CYS A 566      46.511  12.139 121.080  1.00 67.55           C  
ANISOU 4547  C   CYS A 566     6939   7697  11032     49   -319  -1340       C  
ATOM   4548  O   CYS A 566      46.211  11.403 122.002  1.00 65.89           O  
ANISOU 4548  O   CYS A 566     6731   7682  10622    228   -577  -1404       O  
ATOM   4549  CB  CYS A 566      47.611  14.430 121.468  1.00 73.37           C  
ANISOU 4549  CB  CYS A 566     7413   8020  12444   -237   -221  -1685       C  
ATOM   4550  SG  CYS A 566      46.769  14.711 123.058  1.00 74.68           S  
ANISOU 4550  SG  CYS A 566     7662   8306  12407    -27   -618  -1863       S  
ATOM   4551  N   PHE A 567      45.747  12.235 119.991  1.00 66.10           N  
ANISOU 4551  N   PHE A 567     7006   7447  10662      1   -106  -1056       N  
ATOM   4552  CA  PHE A 567      44.613  11.336 119.791  1.00 63.47           C  
ANISOU 4552  CA  PHE A 567     6896   7295   9925    135   -176   -849       C  
ATOM   4553  C   PHE A 567      44.956   9.832 119.800  1.00 61.91           C  
ANISOU 4553  C   PHE A 567     6643   7285   9595    208   -216   -869       C  
ATOM   4554  O   PHE A 567      44.219   9.016 120.406  1.00 61.48           O  
ANISOU 4554  O   PHE A 567     6680   7395   9285    355   -391   -834       O  
ATOM   4555  CB  PHE A 567      43.828  11.702 118.536  1.00 63.21           C  
ANISOU 4555  CB  PHE A 567     7119   7178   9720     70     24   -563       C  
ATOM   4556  CG  PHE A 567      43.053  12.987 118.662  1.00 66.99           C  
ANISOU 4556  CG  PHE A 567     7720   7498  10235     97     -1   -481       C  
ATOM   4557  CD1 PHE A 567      41.771  12.997 119.237  1.00 66.01           C  
ANISOU 4557  CD1 PHE A 567     7699   7487   9897    265   -196   -418       C  
ATOM   4558  CD2 PHE A 567      43.596  14.209 118.205  1.00 69.63           C  
ANISOU 4558  CD2 PHE A 567     8064   7544  10847    -43    201   -467       C  
ATOM   4559  CE1 PHE A 567      41.063  14.194 119.370  1.00 67.98           C  
ANISOU 4559  CE1 PHE A 567     8042   7572  10214    324   -210   -355       C  
ATOM   4560  CE2 PHE A 567      42.879  15.401 118.325  1.00 68.93           C  
ANISOU 4560  CE2 PHE A 567     8110   7264  10816      7    188   -384       C  
ATOM   4561  CZ  PHE A 567      41.620  15.398 118.908  1.00 68.00           C  
ANISOU 4561  CZ  PHE A 567     8080   7268  10490    206    -26   -333       C  
ATOM   4562  N   ALA A 568      46.035   9.457 119.138  1.00 62.02           N  
ANISOU 4562  N   ALA A 568     6518   7253   9793    109    -25   -923       N  
ATOM   4563  CA  ALA A 568      46.512   8.053 119.124  1.00 62.10           C  
ANISOU 4563  CA  ALA A 568     6457   7395   9745    196    -36   -965       C  
ATOM   4564  C   ALA A 568      46.570   7.424 120.520  1.00 61.68           C  
ANISOU 4564  C   ALA A 568     6301   7484   9651    402   -364  -1103       C  
ATOM   4565  O   ALA A 568      45.983   6.365 120.787  1.00 59.83           O  
ANISOU 4565  O   ALA A 568     6212   7366   9156    533   -455  -1017       O  
ATOM   4566  CB  ALA A 568      47.897   7.981 118.506  1.00 63.73           C  
ANISOU 4566  CB  ALA A 568     6422   7513  10280     82    199  -1088       C  
ATOM   4567  N   VAL A 569      47.261   8.107 121.416  1.00 63.29           N  
ANISOU 4567  N   VAL A 569     6278   7670  10102    423   -540  -1321       N  
ATOM   4568  CA  VAL A 569      47.428   7.607 122.756  1.00 64.06           C  
ANISOU 4568  CA  VAL A 569     6296   7911  10133    630   -874  -1461       C  
ATOM   4569  C   VAL A 569      46.188   7.779 123.651  1.00 62.34           C  
ANISOU 4569  C   VAL A 569     6322   7776   9590    745  -1059  -1392       C  
ATOM   4570  O   VAL A 569      45.766   6.823 124.271  1.00 62.74           O  
ANISOU 4570  O   VAL A 569     6503   7953   9384    914  -1192  -1326       O  
ATOM   4571  CB  VAL A 569      48.733   8.189 123.370  1.00 67.62           C  
ANISOU 4571  CB  VAL A 569     6380   8344  10970    612  -1030  -1765       C  
ATOM   4572  CG1 VAL A 569      48.748   8.066 124.927  1.00 67.41           C  
ANISOU 4572  CG1 VAL A 569     6328   8476  10809    829  -1449  -1932       C  
ATOM   4573  CG2 VAL A 569      49.934   7.547 122.690  1.00 67.26           C  
ANISOU 4573  CG2 VAL A 569     6061   8279  11215    582   -874  -1833       C  
ATOM   4574  N   GLU A 570      45.593   8.956 123.708  1.00 62.16           N  
ANISOU 4574  N   GLU A 570     6372   7664   9584    659  -1036  -1398       N  
ATOM   4575  CA  GLU A 570      44.479   9.205 124.635  1.00 61.82           C  
ANISOU 4575  CA  GLU A 570     6519   7696   9275    779  -1187  -1377       C  
ATOM   4576  C   GLU A 570      43.174   8.601 124.139  1.00 61.20           C  
ANISOU 4576  C   GLU A 570     6682   7676   8896    803  -1066  -1114       C  
ATOM   4577  O   GLU A 570      42.253   8.312 124.931  1.00 61.85           O  
ANISOU 4577  O   GLU A 570     6909   7865   8724    926  -1162  -1073       O  
ATOM   4578  CB  GLU A 570      44.260  10.710 124.882  1.00 61.73           C  
ANISOU 4578  CB  GLU A 570     6497   7539   9419    699  -1189  -1496       C  
ATOM   4579  CG  GLU A 570      45.485  11.545 125.298  1.00 64.90           C  
ANISOU 4579  CG  GLU A 570     6641   7840  10179    608  -1288  -1800       C  
ATOM   4580  CD  GLU A 570      46.197  11.103 126.637  1.00 70.66           C  
ANISOU 4580  CD  GLU A 570     7236   8747  10864    765  -1635  -2063       C  
ATOM   4581  OE1 GLU A 570      45.536  10.978 127.714  1.00 68.84           O  
ANISOU 4581  OE1 GLU A 570     7177   8646  10332    934  -1827  -2104       O  
ATOM   4582  OE2 GLU A 570      47.456  10.938 126.616  1.00 71.87           O  
ANISOU 4582  OE2 GLU A 570     7101   8912  11295    722  -1717  -2241       O  
ATOM   4583  N   GLY A 571      43.056   8.395 122.829  1.00 61.31           N  
ANISOU 4583  N   GLY A 571     6740   7628   8926    679   -849   -945       N  
ATOM   4584  CA  GLY A 571      41.842   7.794 122.333  1.00 59.85           C  
ANISOU 4584  CA  GLY A 571     6751   7519   8472    686   -774   -735       C  
ATOM   4585  C   GLY A 571      41.464   6.511 123.057  1.00 59.88           C  
ANISOU 4585  C   GLY A 571     6839   7664   8248    812   -867   -709       C  
ATOM   4586  O   GLY A 571      40.340   6.421 123.593  1.00 60.13           O  
ANISOU 4586  O   GLY A 571     6988   7776   8082    875   -909   -643       O  
ATOM   4587  N   PRO A 572      42.361   5.489 123.026  1.00 59.24           N  
ANISOU 4587  N   PRO A 572     6704   7596   8207    851   -868   -747       N  
ATOM   4588  CA  PRO A 572      42.147   4.182 123.631  1.00 58.41           C  
ANISOU 4588  CA  PRO A 572     6711   7569   7912    978   -925   -697       C  
ATOM   4589  C   PRO A 572      41.983   4.273 125.141  1.00 58.64           C  
ANISOU 4589  C   PRO A 572     6787   7682   7811   1152  -1133   -770       C  
ATOM   4590  O   PRO A 572      41.170   3.552 125.735  1.00 56.50           O  
ANISOU 4590  O   PRO A 572     6694   7473   7299   1229  -1133   -670       O  
ATOM   4591  CB  PRO A 572      43.437   3.442 123.318  1.00 60.03           C  
ANISOU 4591  CB  PRO A 572     6791   7727   8291   1017   -901   -766       C  
ATOM   4592  CG  PRO A 572      43.892   4.026 122.040  1.00 61.27           C  
ANISOU 4592  CG  PRO A 572     6845   7793   8641    836   -706   -776       C  
ATOM   4593  CD  PRO A 572      43.332   5.422 121.932  1.00 60.38           C  
ANISOU 4593  CD  PRO A 572     6736   7650   8556    736   -705   -766       C  
ATOM   4594  N   LYS A 573      42.751   5.157 125.760  1.00 60.00           N  
ANISOU 4594  N   LYS A 573     6811   7852   8134   1200  -1294   -954       N  
ATOM   4595  CA  LYS A 573      42.549   5.402 127.164  1.00 61.62           C  
ANISOU 4595  CA  LYS A 573     7094   8149   8171   1356  -1498  -1051       C  
ATOM   4596  C   LYS A 573      41.069   5.651 127.429  1.00 59.88           C  
ANISOU 4596  C   LYS A 573     7061   7967   7723   1341  -1398   -943       C  
ATOM   4597  O   LYS A 573      40.473   4.961 128.237  1.00 58.77           O  
ANISOU 4597  O   LYS A 573     7101   7909   7319   1455  -1413   -870       O  
ATOM   4598  CB  LYS A 573      43.417   6.528 127.683  1.00 63.83           C  
ANISOU 4598  CB  LYS A 573     7186   8411   8655   1358  -1681  -1308       C  
ATOM   4599  CG  LYS A 573      44.752   6.020 128.255  1.00 67.04           C  
ANISOU 4599  CG  LYS A 573     7431   8881   9161   1498  -1920  -1460       C  
ATOM   4600  CD  LYS A 573      45.805   7.139 128.405  1.00 66.62           C  
ANISOU 4600  CD  LYS A 573     7088   8786   9440   1420  -2069  -1753       C  
ATOM   4601  CE  LYS A 573      47.176   6.487 128.444  1.00 69.15           C  
ANISOU 4601  CE  LYS A 573     7149   9153   9971   1516  -2233  -1866       C  
ATOM   4602  NZ  LYS A 573      48.219   7.235 129.200  1.00 71.84           N  
ANISOU 4602  NZ  LYS A 573     7216   9548  10533   1539  -2537  -2202       N  
ATOM   4603  N   LEU A 574      40.482   6.576 126.678  1.00 59.98           N  
ANISOU 4603  N   LEU A 574     7029   7909   7851   1206  -1274   -914       N  
ATOM   4604  CA  LEU A 574      39.046   6.958 126.797  1.00 59.33           C  
ANISOU 4604  CA  LEU A 574     7056   7860   7627   1201  -1177   -825       C  
ATOM   4605  C   LEU A 574      38.063   5.795 126.643  1.00 57.94           C  
ANISOU 4605  C   LEU A 574     7007   7763   7243   1189  -1053   -641       C  
ATOM   4606  O   LEU A 574      37.181   5.554 127.511  1.00 58.41           O  
ANISOU 4606  O   LEU A 574     7183   7905   7106   1266  -1019   -615       O  
ATOM   4607  CB  LEU A 574      38.701   7.927 125.688  1.00 59.24           C  
ANISOU 4607  CB  LEU A 574     6967   7742   7798   1073  -1069   -768       C  
ATOM   4608  CG  LEU A 574      37.556   8.804 126.163  1.00 63.41           C  
ANISOU 4608  CG  LEU A 574     7536   8277   8279   1134  -1046   -778       C  
ATOM   4609  CD1 LEU A 574      38.169   9.911 127.073  1.00 62.84           C  
ANISOU 4609  CD1 LEU A 574     7428   8126   8323   1197  -1162  -1018       C  
ATOM   4610  CD2 LEU A 574      36.762   9.351 124.983  1.00 59.93           C  
ANISOU 4610  CD2 LEU A 574     7069   7774   7927   1055   -938   -621       C  
ATOM   4611  N   VAL A 575      38.228   5.073 125.543  1.00 55.51           N  
ANISOU 4611  N   VAL A 575     6683   7422   6986   1078   -961   -532       N  
ATOM   4612  CA  VAL A 575      37.415   3.891 125.295  1.00 54.75           C  
ANISOU 4612  CA  VAL A 575     6697   7371   6736   1027   -842   -393       C  
ATOM   4613  C   VAL A 575      37.430   2.990 126.545  1.00 55.88           C  
ANISOU 4613  C   VAL A 575     6990   7553   6688   1165   -869   -382       C  
ATOM   4614  O   VAL A 575      36.348   2.644 127.083  1.00 56.91           O  
ANISOU 4614  O   VAL A 575     7224   7741   6659   1166   -769   -312       O  
ATOM   4615  CB  VAL A 575      37.857   3.189 123.983  1.00 54.79           C  
ANISOU 4615  CB  VAL A 575     6686   7316   6816    897   -753   -332       C  
ATOM   4616  CG1 VAL A 575      37.163   1.880 123.778  1.00 54.32           C  
ANISOU 4616  CG1 VAL A 575     6746   7269   6622    829   -639   -236       C  
ATOM   4617  CG2 VAL A 575      37.670   4.152 122.744  1.00 50.73           C  
ANISOU 4617  CG2 VAL A 575     6088   6774   6414    771   -711   -304       C  
ATOM   4618  N   VAL A 576      38.621   2.705 127.077  1.00 55.54           N  
ANISOU 4618  N   VAL A 576     6955   7486   6661   1294  -1004   -453       N  
ATOM   4619  CA  VAL A 576      38.754   1.797 128.247  1.00 55.07           C  
ANISOU 4619  CA  VAL A 576     7086   7453   6384   1467  -1058   -408       C  
ATOM   4620  C   VAL A 576      37.964   2.207 129.485  1.00 57.39           C  
ANISOU 4620  C   VAL A 576     7521   7840   6444   1563  -1065   -426       C  
ATOM   4621  O   VAL A 576      37.203   1.382 130.087  1.00 57.43           O  
ANISOU 4621  O   VAL A 576     7735   7859   6228   1593   -926   -296       O  
ATOM   4622  CB  VAL A 576      40.233   1.523 128.708  1.00 56.80           C  
ANISOU 4622  CB  VAL A 576     7262   7658   6660   1646  -1277   -496       C  
ATOM   4623  CG1 VAL A 576      40.209   0.595 129.921  1.00 54.63           C  
ANISOU 4623  CG1 VAL A 576     7246   7410   6099   1855  -1340   -400       C  
ATOM   4624  CG2 VAL A 576      41.164   0.914 127.564  1.00 52.63           C  
ANISOU 4624  CG2 VAL A 576     6595   7026   6377   1588  -1230   -488       C  
ATOM   4625  N   SER A 577      38.170   3.471 129.901  1.00 58.93           N  
ANISOU 4625  N   SER A 577     7621   8081   6690   1606  -1198   -598       N  
ATOM   4626  CA  SER A 577      37.489   4.006 131.080  1.00 60.38           C  
ANISOU 4626  CA  SER A 577     7940   8351   6651   1706  -1195   -665       C  
ATOM   4627  C   SER A 577      35.967   4.044 130.931  1.00 60.43           C  
ANISOU 4627  C   SER A 577     7975   8381   6604   1604   -935   -564       C  
ATOM   4628  O   SER A 577      35.267   3.807 131.898  1.00 62.04           O  
ANISOU 4628  O   SER A 577     8357   8649   6565   1679   -822   -533       O  
ATOM   4629  CB  SER A 577      38.083   5.352 131.534  1.00 62.13           C  
ANISOU 4629  CB  SER A 577     8057   8588   6964   1762  -1390   -915       C  
ATOM   4630  OG  SER A 577      37.740   6.457 130.744  1.00 59.98           O  
ANISOU 4630  OG  SER A 577     7605   8240   6945   1632  -1322   -978       O  
ATOM   4631  N   THR A 578      35.494   4.248 129.695  1.00 58.81           N  
ANISOU 4631  N   THR A 578     7595   8130   6619   1439   -839   -505       N  
ATOM   4632  CA  THR A 578      34.104   4.311 129.343  1.00 59.08           C  
ANISOU 4632  CA  THR A 578     7571   8202   6674   1338   -644   -425       C  
ATOM   4633  C   THR A 578      33.503   2.929 129.408  1.00 59.45           C  
ANISOU 4633  C   THR A 578     7740   8259   6588   1265   -466   -272       C  
ATOM   4634  O   THR A 578      32.491   2.714 130.091  1.00 61.50           O  
ANISOU 4634  O   THR A 578     8069   8575   6722   1265   -283   -235       O  
ATOM   4635  CB  THR A 578      33.982   4.876 127.885  1.00 58.56           C  
ANISOU 4635  CB  THR A 578     7300   8090   6858   1202   -665   -399       C  
ATOM   4636  OG1 THR A 578      34.801   6.045 127.799  1.00 61.12           O  
ANISOU 4636  OG1 THR A 578     7547   8347   7329   1253   -809   -526       O  
ATOM   4637  CG2 THR A 578      32.541   5.244 127.454  1.00 55.32           C  
ANISOU 4637  CG2 THR A 578     6763   7741   6514   1135   -542   -346       C  
ATOM   4638  N   GLN A 579      34.116   1.990 128.696  1.00 57.93           N  
ANISOU 4638  N   GLN A 579     7574   7992   6445   1192   -486   -194       N  
ATOM   4639  CA  GLN A 579      33.767   0.549 128.805  1.00 57.69           C  
ANISOU 4639  CA  GLN A 579     7706   7908   6305   1126   -316    -58       C  
ATOM   4640  C   GLN A 579      33.692   0.009 130.242  1.00 60.73           C  
ANISOU 4640  C   GLN A 579     8359   8296   6421   1274   -235      5       C  
ATOM   4641  O   GLN A 579      32.902  -0.908 130.559  1.00 61.32           O  
ANISOU 4641  O   GLN A 579     8573   8330   6395   1195      2    125       O  
ATOM   4642  CB  GLN A 579      34.774  -0.284 128.032  1.00 55.98           C  
ANISOU 4642  CB  GLN A 579     7517   7577   6175   1099   -380    -23       C  
ATOM   4643  CG  GLN A 579      34.543  -0.329 126.517  1.00 55.70           C  
ANISOU 4643  CG  GLN A 579     7320   7522   6322    893   -345    -32       C  
ATOM   4644  CD  GLN A 579      35.632  -1.093 125.742  1.00 54.32           C  
ANISOU 4644  CD  GLN A 579     7179   7228   6234    880   -375    -31       C  
ATOM   4645  OE1 GLN A 579      36.750  -1.196 126.196  1.00 56.51           O  
ANISOU 4645  OE1 GLN A 579     7501   7456   6516   1045   -486    -55       O  
ATOM   4646  NE2 GLN A 579      35.305  -1.569 124.549  1.00 52.12           N  
ANISOU 4646  NE2 GLN A 579     6860   6914   6029    689   -285    -28       N  
ATOM   4647  N   THR A 580      34.561   0.553 131.097  1.00 61.62           N  
ANISOU 4647  N   THR A 580     8555   8447   6408   1481   -432    -79       N  
ATOM   4648  CA  THR A 580      34.633   0.133 132.465  1.00 64.95           C  
ANISOU 4648  CA  THR A 580     9274   8893   6512   1661   -410    -22       C  
ATOM   4649  C   THR A 580      33.466   0.753 133.235  1.00 66.97           C  
ANISOU 4649  C   THR A 580     9571   9249   6624   1651   -214    -63       C  
ATOM   4650  O   THR A 580      32.729   0.037 133.925  1.00 67.82           O  
ANISOU 4650  O   THR A 580     9897   9346   6527   1642     42     66       O  
ATOM   4651  CB  THR A 580      35.994   0.501 133.042  1.00 65.50           C  
ANISOU 4651  CB  THR A 580     9390   8997   6499   1885   -741   -132       C  
ATOM   4652  OG1 THR A 580      36.969  -0.387 132.472  1.00 68.43           O  
ANISOU 4652  OG1 THR A 580     9751   9261   6988   1920   -849    -54       O  
ATOM   4653  CG2 THR A 580      36.006   0.295 134.465  1.00 66.40           C  
ANISOU 4653  CG2 THR A 580     9820   9176   6232   2089   -764    -97       C  
ATOM   4654  N   ALA A 581      33.295   2.076 133.059  1.00 66.52           N  
ANISOU 4654  N   ALA A 581     9304   9266   6706   1647   -302   -241       N  
ATOM   4655  CA  ALA A 581      32.304   2.874 133.787  1.00 67.79           C  
ANISOU 4655  CA  ALA A 581     9471   9516   6772   1679   -136   -333       C  
ATOM   4656  C   ALA A 581      30.908   2.367 133.413  1.00 68.16           C  
ANISOU 4656  C   ALA A 581     9417   9567   6915   1499    197   -217       C  
ATOM   4657  O   ALA A 581      29.993   2.268 134.271  1.00 71.32           O  
ANISOU 4657  O   ALA A 581     9929  10020   7149   1514    471   -199       O  
ATOM   4658  CB  ALA A 581      32.456   4.389 133.441  1.00 65.77           C  
ANISOU 4658  CB  ALA A 581     8982   9275   6731   1704   -300   -541       C  
ATOM   4659  N   LEU A 582      30.754   1.992 132.149  1.00 65.42           N  
ANISOU 4659  N   LEU A 582     8860   9169   6826   1322    185   -151       N  
ATOM   4660  CA  LEU A 582      29.442   1.582 131.651  1.00 65.80           C  
ANISOU 4660  CA  LEU A 582     8739   9242   7021   1127    439    -87       C  
ATOM   4661  C   LEU A 582      29.217   0.096 131.581  1.00 66.58           C  
ANISOU 4661  C   LEU A 582     8982   9250   7066    978    636     69       C  
ATOM   4662  O   LEU A 582      28.135  -0.354 131.248  1.00 67.34           O  
ANISOU 4662  O   LEU A 582     8935   9360   7293    786    859    100       O  
ATOM   4663  CB  LEU A 582      29.166   2.161 130.281  1.00 62.72           C  
ANISOU 4663  CB  LEU A 582     8021   8876   6933   1012    305   -133       C  
ATOM   4664  CG  LEU A 582      29.185   3.663 130.102  1.00 63.35           C  
ANISOU 4664  CG  LEU A 582     7927   8999   7145   1128    149   -261       C  
ATOM   4665  CD1 LEU A 582      28.304   3.957 128.912  1.00 61.71           C  
ANISOU 4665  CD1 LEU A 582     7416   8840   7190   1004    133   -244       C  
ATOM   4666  CD2 LEU A 582      28.722   4.446 131.339  1.00 62.61           C  
ANISOU 4666  CD2 LEU A 582     7895   8960   6933   1288    275   -371       C  
ATOM   4667  N   ALA A 583      30.236  -0.679 131.858  1.00 67.79           N  
ANISOU 4667  N   ALA A 583     9400   9296   7061   1063    549    158       N  
ATOM   4668  CA  ALA A 583      30.094  -2.087 131.625  1.00 70.40           C  
ANISOU 4668  CA  ALA A 583     9871   9483   7393    919    731    306       C  
ATOM   4669  C   ALA A 583      30.864  -2.804 132.676  1.00 73.47           C  
ANISOU 4669  C   ALA A 583    10657   9772   7485   1112    741    438       C  
ATOM   4670  O   ALA A 583      31.253  -3.967 132.509  1.00 75.93           O  
ANISOU 4670  O   ALA A 583    11155   9910   7786   1083    800    573       O  
ATOM   4671  CB  ALA A 583      30.614  -2.446 130.231  1.00 69.44           C  
ANISOU 4671  CB  ALA A 583     9597   9286   7501    790    570    284       C  
ATOM   4672  OXT ALA A 583      31.139  -2.198 133.706  1.00 74.81           O  
ANISOU 4672  OXT ALA A 583    10978  10031   7413   1321    667    404       O  
TER    4673      ALA A 583                                                      
ATOM   4674  N   ASP B   1      65.124  18.249  57.399  1.00108.62           N  
ANISOU 4674  N   ASP B   1    15231  14534  11506   2184   2218   -926       N  
ATOM   4675  CA  ASP B   1      64.008  18.993  58.102  1.00104.65           C  
ANISOU 4675  CA  ASP B   1    14740  13824  11199   1762   1905   -862       C  
ATOM   4676  C   ASP B   1      63.452  20.156  57.250  1.00102.85           C  
ANISOU 4676  C   ASP B   1    14582  13580  10914   1325   1855   -832       C  
ATOM   4677  O   ASP B   1      63.625  21.331  57.619  1.00101.29           O  
ANISOU 4677  O   ASP B   1    14067  13595  10824   1039   1787   -731       O  
ATOM   4678  CB  ASP B   1      64.428  19.507  59.509  1.00103.08           C  
ANISOU 4678  CB  ASP B   1    14076  13854  11235   1705   1788   -749       C  
ATOM   4679  CG  ASP B   1      64.371  18.410  60.600  1.00104.62           C  
ANISOU 4679  CG  ASP B   1    14332  13885  11535   2004   1681   -769       C  
ATOM   4680  OD1 ASP B   1      64.844  17.283  60.298  1.00106.91           O  
ANISOU 4680  OD1 ASP B   1    14799  14121  11702   2420   1819   -845       O  
ATOM   4681  OD2 ASP B   1      63.870  18.676  61.752  1.00 99.19           O  
ANISOU 4681  OD2 ASP B   1    13542  13113  11032   1832   1463   -711       O  
ATOM   4682  N   THR B   2      62.827  19.821  56.105  1.00102.67           N  
ANISOU 4682  N   THR B   2    15010  13297  10703   1275   1878   -913       N  
ATOM   4683  CA  THR B   2      61.886  20.739  55.431  1.00100.09           C  
ANISOU 4683  CA  THR B   2    14867  12812  10352    854   1721   -883       C  
ATOM   4684  C   THR B   2      60.424  20.353  55.717  1.00 96.86           C  
ANISOU 4684  C   THR B   2    14785  11989  10030    721   1433   -898       C  
ATOM   4685  O   THR B   2      59.880  19.431  55.092  1.00 98.25           O  
ANISOU 4685  O   THR B   2    15400  11878  10051    795   1412   -970       O  
ATOM   4686  CB  THR B   2      62.130  20.914  53.905  1.00102.33           C  
ANISOU 4686  CB  THR B   2    15394  13126  10360    771   1902   -926       C  
ATOM   4687  OG1 THR B   2      63.187  20.050  53.467  1.00106.81           O  
ANISOU 4687  OG1 THR B   2    15974  13868  10743   1161   2217  -1005       O  
ATOM   4688  CG2 THR B   2      62.513  22.372  53.580  1.00102.52           C  
ANISOU 4688  CG2 THR B   2    15148  13428  10378    423   1917   -827       C  
ATOM   4689  N   HIS B   3      59.812  21.070  56.669  1.00 92.15           N  
ANISOU 4689  N   HIS B   3    13974  11380   9659    516   1217   -822       N  
ATOM   4690  CA  HIS B   3      58.399  20.867  57.071  1.00 88.30           C  
ANISOU 4690  CA  HIS B   3    13685  10589   9278    362    947   -810       C  
ATOM   4691  C   HIS B   3      57.527  22.058  56.669  1.00 85.03           C  
ANISOU 4691  C   HIS B   3    13276  10117   8916     17    769   -745       C  
ATOM   4692  O   HIS B   3      57.701  23.171  57.186  1.00 83.64           O  
ANISOU 4692  O   HIS B   3    12811  10099   8869   -113    726   -683       O  
ATOM   4693  CB  HIS B   3      58.284  20.616  58.586  1.00 86.43           C  
ANISOU 4693  CB  HIS B   3    13218  10371   9250    453    845   -784       C  
ATOM   4694  CG  HIS B   3      59.417  19.805  59.147  1.00 89.45           C  
ANISOU 4694  CG  HIS B   3    13467  10898   9621    794   1012   -815       C  
ATOM   4695  ND1 HIS B   3      59.453  18.426  59.083  1.00 90.93           N  
ANISOU 4695  ND1 HIS B   3    13956  10897   9694   1061   1048   -887       N  
ATOM   4696  CD2 HIS B   3      60.569  20.182  59.755  1.00 89.71           C  
ANISOU 4696  CD2 HIS B   3    13109  11249   9729    917   1137   -774       C  
ATOM   4697  CE1 HIS B   3      60.581  17.990  59.618  1.00 92.07           C  
ANISOU 4697  CE1 HIS B   3    13891  11234   9856   1376   1195   -895       C  
ATOM   4698  NE2 HIS B   3      61.267  19.033  60.048  1.00 92.69           N  
ANISOU 4698  NE2 HIS B   3    13522  11641  10056   1285   1248   -819       N  
ATOM   4699  N   LYS B   4      56.589  21.811  55.755  1.00 83.10           N  
ANISOU 4699  N   LYS B   4    13387   9632   8557   -126    649   -753       N  
ATOM   4700  CA  LYS B   4      55.657  22.840  55.279  1.00 79.49           C  
ANISOU 4700  CA  LYS B   4    12973   9092   8139   -422    449   -684       C  
ATOM   4701  C   LYS B   4      54.769  23.312  56.417  1.00 75.33           C  
ANISOU 4701  C   LYS B   4    12221   8544   7857   -495    242   -625       C  
ATOM   4702  O   LYS B   4      54.539  24.493  56.613  1.00 74.93           O  
ANISOU 4702  O   LYS B   4    12004   8553   7912   -628    147   -570       O  
ATOM   4703  CB  LYS B   4      54.721  22.247  54.235  1.00 80.61           C  
ANISOU 4703  CB  LYS B   4    13538   8969   8119   -551    319   -687       C  
ATOM   4704  CG  LYS B   4      55.298  22.019  52.909  1.00 81.20           C  
ANISOU 4704  CG  LYS B   4    13916   9013   7922   -557    479   -737       C  
ATOM   4705  CD  LYS B   4      54.197  21.492  52.019  1.00 81.72           C  
ANISOU 4705  CD  LYS B   4    14419   8791   7842   -740    283   -718       C  
ATOM   4706  CE  LYS B   4      53.088  22.544  51.847  1.00 79.32           C  
ANISOU 4706  CE  LYS B   4    14043   8433   7660  -1030     -5   -603       C  
ATOM   4707  NZ  LYS B   4      52.363  22.415  50.532  1.00 77.31           N  
ANISOU 4707  NZ  LYS B   4    14213   7965   7198  -1266   -161   -564       N  
ATOM   4708  N   SER B   5      54.248  22.360  57.155  1.00 72.17           N  
ANISOU 4708  N   SER B   5    11852   8047   7520   -404    174   -640       N  
ATOM   4709  CA  SER B   5      53.338  22.654  58.189  1.00 68.43           C  
ANISOU 4709  CA  SER B   5    11188   7567   7244   -469      3   -590       C  
ATOM   4710  C   SER B   5      53.922  22.273  59.520  1.00 66.58           C  
ANISOU 4710  C   SER B   5    10729   7444   7126   -296     89   -615       C  
ATOM   4711  O   SER B   5      54.066  21.118  59.827  1.00 67.46           O  
ANISOU 4711  O   SER B   5    10964   7485   7185   -166    124   -652       O  
ATOM   4712  CB  SER B   5      52.000  21.989  57.945  1.00 67.58           C  
ANISOU 4712  CB  SER B   5    11293   7277   7109   -603   -200   -551       C  
ATOM   4713  OG  SER B   5      51.139  22.358  59.011  1.00 70.04           O  
ANISOU 4713  OG  SER B   5    11354   7645   7614   -652   -334   -499       O  
ATOM   4714  N   GLU B   6      54.232  23.288  60.319  1.00 65.03           N  
ANISOU 4714  N   GLU B   6    10238   7399   7073   -308     99   -589       N  
ATOM   4715  CA  GLU B   6      54.765  23.160  61.662  1.00 62.79           C  
ANISOU 4715  CA  GLU B   6     9721   7232   6906   -190    152   -594       C  
ATOM   4716  C   GLU B   6      53.837  22.418  62.620  1.00 61.28           C  
ANISOU 4716  C   GLU B   6     9540   6947   6799   -186     36   -590       C  
ATOM   4717  O   GLU B   6      54.293  21.591  63.408  1.00 61.33           O  
ANISOU 4717  O   GLU B   6     9523   6967   6814    -55     84   -611       O  
ATOM   4718  CB  GLU B   6      55.063  24.584  62.175  1.00 62.53           C  
ANISOU 4718  CB  GLU B   6     9451   7333   6973   -280    140   -555       C  
ATOM   4719  CG  GLU B   6      56.130  24.749  63.259  1.00 62.73           C  
ANISOU 4719  CG  GLU B   6     9236   7538   7062   -198    231   -545       C  
ATOM   4720  CD  GLU B   6      57.339  23.752  63.265  1.00 69.69           C  
ANISOU 4720  CD  GLU B   6    10069   8541   7868      4    393   -566       C  
ATOM   4721  OE1 GLU B   6      57.757  23.150  62.201  1.00 71.19           O  
ANISOU 4721  OE1 GLU B   6    10407   8727   7917     99    505   -600       O  
ATOM   4722  OE2 GLU B   6      57.882  23.587  64.412  1.00 70.89           O  
ANISOU 4722  OE2 GLU B   6    10036   8798   8101     84    405   -547       O  
ATOM   4723  N   ILE B   7      52.550  22.744  62.579  1.00 59.46           N  
ANISOU 4723  N   ILE B   7     9327   6642   6624   -334   -121   -552       N  
ATOM   4724  CA  ILE B   7      51.567  22.063  63.375  1.00 59.22           C  
ANISOU 4724  CA  ILE B   7     9292   6563   6645   -382   -230   -531       C  
ATOM   4725  C   ILE B   7      51.469  20.563  63.013  1.00 60.91           C  
ANISOU 4725  C   ILE B   7     9804   6629   6711   -370   -253   -546       C  
ATOM   4726  O   ILE B   7      51.378  19.700  63.919  1.00 59.93           O  
ANISOU 4726  O   ILE B   7     9704   6476   6589   -341   -276   -548       O  
ATOM   4727  CB  ILE B   7      50.212  22.784  63.297  1.00 58.82           C  
ANISOU 4727  CB  ILE B   7     9150   6520   6677   -527   -384   -471       C  
ATOM   4728  CG1 ILE B   7      49.192  22.138  64.223  1.00 62.10           C  
ANISOU 4728  CG1 ILE B   7     9494   6960   7142   -600   -475   -435       C  
ATOM   4729  CG2 ILE B   7      49.644  22.732  61.935  1.00 61.59           C  
ANISOU 4729  CG2 ILE B   7     9706   6770   6927   -646   -486   -434       C  
ATOM   4730  CD1 ILE B   7      48.502  23.157  65.181  1.00 64.66           C  
ANISOU 4730  CD1 ILE B   7     9529   7418   7623   -593   -499   -414       C  
ATOM   4731  N   ALA B   8      51.518  20.258  61.700  1.00 62.86           N  
ANISOU 4731  N   ALA B   8    10320   6760   6803   -401   -254   -556       N  
ATOM   4732  CA  ALA B   8      51.419  18.860  61.212  1.00 65.18           C  
ANISOU 4732  CA  ALA B   8    10997   6860   6907   -395   -287   -577       C  
ATOM   4733  C   ALA B   8      52.617  18.065  61.695  1.00 66.27           C  
ANISOU 4733  C   ALA B   8    11199   6988   6994   -131   -133   -648       C  
ATOM   4734  O   ALA B   8      52.469  16.957  62.158  1.00 66.40           O  
ANISOU 4734  O   ALA B   8    11422   6871   6935    -97   -191   -656       O  
ATOM   4735  CB  ALA B   8      51.320  18.783  59.687  1.00 66.51           C  
ANISOU 4735  CB  ALA B   8    11477   6898   6896   -475   -302   -583       C  
ATOM   4736  N   HIS B   9      53.797  18.690  61.641  1.00 66.61           N  
ANISOU 4736  N   HIS B   9    11042   7190   7079     46     46   -685       N  
ATOM   4737  CA  HIS B   9      55.036  18.055  62.014  1.00 67.37           C  
ANISOU 4737  CA  HIS B   9    11126   7337   7136    333    202   -737       C  
ATOM   4738  C   HIS B   9      55.103  17.692  63.488  1.00 66.80           C  
ANISOU 4738  C   HIS B   9    10895   7300   7184    395    148   -717       C  
ATOM   4739  O   HIS B   9      55.513  16.577  63.853  1.00 69.46           O  
ANISOU 4739  O   HIS B   9    11419   7530   7444    583    157   -747       O  
ATOM   4740  CB  HIS B   9      56.164  18.968  61.633  1.00 67.72           C  
ANISOU 4740  CB  HIS B   9    10916   7611   7202    432    383   -746       C  
ATOM   4741  CG  HIS B   9      57.480  18.544  62.168  1.00 70.77           C  
ANISOU 4741  CG  HIS B   9    11149   8149   7592    724    538   -768       C  
ATOM   4742  ND1 HIS B   9      58.255  19.368  62.953  1.00 72.45           N  
ANISOU 4742  ND1 HIS B   9    10964   8622   7942    739    592   -721       N  
ATOM   4743  CD2 HIS B   9      58.147  17.372  62.068  1.00 74.88           C  
ANISOU 4743  CD2 HIS B   9    11864   8597   7991   1024    632   -822       C  
ATOM   4744  CE1 HIS B   9      59.354  18.725  63.304  1.00 75.68           C  
ANISOU 4744  CE1 HIS B   9    11281   9148   8328   1025    709   -731       C  
ATOM   4745  NE2 HIS B   9      59.312  17.512  62.784  1.00 76.44           N  
ANISOU 4745  NE2 HIS B   9    11729   9042   8272   1231    741   -799       N  
ATOM   4746  N   ARG B  10      54.665  18.600  64.348  1.00 64.14           N  
ANISOU 4746  N   ARG B  10    10260   7089   7019    243     81   -669       N  
ATOM   4747  CA  ARG B  10      54.654  18.307  65.759  1.00 62.60           C  
ANISOU 4747  CA  ARG B  10     9938   6925   6921    263     27   -648       C  
ATOM   4748  C   ARG B  10      53.619  17.261  66.114  1.00 63.07           C  
ANISOU 4748  C   ARG B  10    10255   6798   6912    141   -125   -632       C  
ATOM   4749  O   ARG B  10      53.870  16.385  66.975  1.00 64.18           O  
ANISOU 4749  O   ARG B  10    10487   6870   7027    226   -162   -633       O  
ATOM   4750  CB  ARG B  10      54.450  19.556  66.575  1.00 60.31           C  
ANISOU 4750  CB  ARG B  10     9316   6802   6798    137     11   -612       C  
ATOM   4751  CG  ARG B  10      55.460  20.624  66.298  1.00 61.84           C  
ANISOU 4751  CG  ARG B  10     9288   7175   7032    190    128   -607       C  
ATOM   4752  CD  ARG B  10      56.874  20.125  66.397  1.00 64.15           C  
ANISOU 4752  CD  ARG B  10     9516   7575   7283    422    250   -616       C  
ATOM   4753  NE  ARG B  10      57.813  21.166  65.997  1.00 64.74           N  
ANISOU 4753  NE  ARG B  10     9367   7865   7368    413    359   -589       N  
ATOM   4754  CZ  ARG B  10      59.144  21.055  66.071  1.00 66.92           C  
ANISOU 4754  CZ  ARG B  10     9468   8340   7620    582    479   -568       C  
ATOM   4755  NH1 ARG B  10      59.705  19.935  66.539  1.00 62.05           N  
ANISOU 4755  NH1 ARG B  10     8883   7712   6983    828    503   -578       N  
ATOM   4756  NH2 ARG B  10      59.911  22.096  65.712  1.00 64.00           N  
ANISOU 4756  NH2 ARG B  10     8883   8193   7240    494    559   -522       N  
ATOM   4757  N   PHE B  11      52.480  17.311  65.425  1.00 62.95           N  
ANISOU 4757  N   PHE B  11    10371   6700   6847    -75   -232   -604       N  
ATOM   4758  CA  PHE B  11      51.392  16.391  65.717  1.00 62.49           C  
ANISOU 4758  CA  PHE B  11    10533   6506   6704   -270   -398   -560       C  
ATOM   4759  C   PHE B  11      51.920  15.019  65.482  1.00 64.21           C  
ANISOU 4759  C   PHE B  11    11165   6500   6733   -129   -408   -599       C  
ATOM   4760  O   PHE B  11      51.860  14.181  66.370  1.00 65.99           O  
ANISOU 4760  O   PHE B  11    11517   6640   6917   -136   -484   -585       O  
ATOM   4761  CB  PHE B  11      50.154  16.704  64.893  1.00 62.24           C  
ANISOU 4761  CB  PHE B  11    10545   6462   6643   -529   -523   -500       C  
ATOM   4762  CG  PHE B  11      48.895  16.001  65.350  1.00 62.70           C  
ANISOU 4762  CG  PHE B  11    10700   6483   6639   -805   -706   -417       C  
ATOM   4763  CD1 PHE B  11      48.456  14.838  64.706  1.00 67.33           C  
ANISOU 4763  CD1 PHE B  11    11726   6851   7003   -954   -842   -386       C  
ATOM   4764  CD2 PHE B  11      48.096  16.536  66.341  1.00 61.65           C  
ANISOU 4764  CD2 PHE B  11    10237   6544   6644   -941   -744   -361       C  
ATOM   4765  CE1 PHE B  11      47.269  14.173  65.085  1.00 67.53           C  
ANISOU 4765  CE1 PHE B  11    11848   6870   6942  -1278  -1033   -283       C  
ATOM   4766  CE2 PHE B  11      46.882  15.893  66.718  1.00 64.78           C  
ANISOU 4766  CE2 PHE B  11    10681   6968   6964  -1233   -905   -266       C  
ATOM   4767  CZ  PHE B  11      46.482  14.700  66.081  1.00 67.58           C  
ANISOU 4767  CZ  PHE B  11    11464   7120   7093  -1424  -1060   -217       C  
ATOM   4768  N   LYS B  12      52.538  14.800  64.333  1.00 65.37           N  
ANISOU 4768  N   LYS B  12    11539   6546   6752     30   -318   -655       N  
ATOM   4769  CA  LYS B  12      52.972  13.461  64.009  1.00 67.40           C  
ANISOU 4769  CA  LYS B  12    12267   6549   6795    201   -325   -704       C  
ATOM   4770  C   LYS B  12      54.177  12.982  64.823  1.00 67.88           C  
ANISOU 4770  C   LYS B  12    12275   6630   6885    548   -225   -749       C  
ATOM   4771  O   LYS B  12      54.376  11.810  64.954  1.00 69.20           O  
ANISOU 4771  O   LYS B  12    12828   6568   6895    685   -282   -775       O  
ATOM   4772  CB  LYS B  12      53.052  13.185  62.501  1.00 68.10           C  
ANISOU 4772  CB  LYS B  12    12721   6475   6679    239   -278   -752       C  
ATOM   4773  CG  LYS B  12      53.732  14.270  61.647  1.00 71.05           C  
ANISOU 4773  CG  LYS B  12    12840   7040   7114    349    -87   -789       C  
ATOM   4774  CD  LYS B  12      54.414  13.713  60.354  1.00 71.69           C  
ANISOU 4774  CD  LYS B  12    13316   6970   6954    562     55   -877       C  
ATOM   4775  CE  LYS B  12      55.838  13.198  60.663  1.00 72.85           C  
ANISOU 4775  CE  LYS B  12    13433   7174   7073   1019    260   -956       C  
ATOM   4776  NZ  LYS B  12      56.635  13.056  59.384  1.00 76.08           N  
ANISOU 4776  NZ  LYS B  12    14061   7563   7282   1257    478  -1045       N  
ATOM   4777  N   ASP B  13      54.954  13.866  65.426  1.00 67.67           N  
ANISOU 4777  N   ASP B  13    11794   6867   7049    677   -103   -745       N  
ATOM   4778  CA  ASP B  13      56.009  13.365  66.313  1.00 68.57           C  
ANISOU 4778  CA  ASP B  13    11838   7018   7197    973    -55   -757       C  
ATOM   4779  C   ASP B  13      55.542  13.109  67.745  1.00 67.80           C  
ANISOU 4779  C   ASP B  13    11678   6903   7180    822   -208   -700       C  
ATOM   4780  O   ASP B  13      56.153  12.312  68.439  1.00 69.32           O  
ANISOU 4780  O   ASP B  13    11988   7013   7338   1026   -244   -701       O  
ATOM   4781  CB  ASP B  13      57.169  14.330  66.367  1.00 68.11           C  
ANISOU 4781  CB  ASP B  13    11333   7267   7278   1160    126   -757       C  
ATOM   4782  CG  ASP B  13      57.725  14.623  65.033  1.00 71.98           C  
ANISOU 4782  CG  ASP B  13    11848   7824   7678   1297    300   -807       C  
ATOM   4783  OD1 ASP B  13      58.325  15.722  64.877  1.00 75.71           O  
ANISOU 4783  OD1 ASP B  13    11941   8572   8252   1284    422   -784       O  
ATOM   4784  OD2 ASP B  13      57.567  13.767  64.137  1.00 74.64           O  
ANISOU 4784  OD2 ASP B  13    12611   7932   7817   1394    311   -865       O  
ATOM   4785  N   LEU B  14      54.529  13.830  68.227  1.00 65.40           N  
ANISOU 4785  N   LEU B  14    11168   6697   6983    491   -289   -648       N  
ATOM   4786  CA  LEU B  14      54.095  13.663  69.632  1.00 64.84           C  
ANISOU 4786  CA  LEU B  14    11016   6646   6975    334   -403   -597       C  
ATOM   4787  C   LEU B  14      52.914  12.738  69.774  1.00 65.86           C  
ANISOU 4787  C   LEU B  14    11487   6579   6958     62   -583   -557       C  
ATOM   4788  O   LEU B  14      52.714  12.165  70.837  1.00 66.30           O  
ANISOU 4788  O   LEU B  14    11626   6580   6984    -32   -687   -520       O  
ATOM   4789  CB  LEU B  14      53.751  15.006  70.298  1.00 62.47           C  
ANISOU 4789  CB  LEU B  14    10273   6597   6865    163   -363   -565       C  
ATOM   4790  CG  LEU B  14      54.891  16.022  70.234  1.00 61.97           C  
ANISOU 4790  CG  LEU B  14     9881   6738   6926    351   -215   -581       C  
ATOM   4791  CD1 LEU B  14      54.403  17.460  70.266  1.00 48.16           C  
ANISOU 4791  CD1 LEU B  14     7828   5164   5308    175   -176   -567       C  
ATOM   4792  CD2 LEU B  14      56.031  15.687  71.296  1.00 59.64           C  
ANISOU 4792  CD2 LEU B  14     9488   6501   6671    549   -210   -561       C  
ATOM   4793  N   GLY B  15      52.158  12.561  68.686  1.00 66.73           N  
ANISOU 4793  N   GLY B  15    11817   6584   6954    -91   -632   -553       N  
ATOM   4794  CA  GLY B  15      50.940  11.749  68.705  1.00 67.96           C  
ANISOU 4794  CA  GLY B  15    12282   6590   6949   -427   -826   -487       C  
ATOM   4795  C   GLY B  15      49.819  12.485  69.407  1.00 66.80           C  
ANISOU 4795  C   GLY B  15    11777   6680   6926   -749   -873   -411       C  
ATOM   4796  O   GLY B  15      50.062  13.457  70.129  1.00 64.87           O  
ANISOU 4796  O   GLY B  15    11124   6653   6872   -682   -767   -422       O  
ATOM   4797  N   GLU B  16      48.596  12.006  69.223  1.00 68.22           N  
ANISOU 4797  N   GLU B  16    12118   6824   6979  -1099  -1033   -327       N  
ATOM   4798  CA  GLU B  16      47.425  12.734  69.696  1.00 68.30           C  
ANISOU 4798  CA  GLU B  16    11749   7107   7096  -1382  -1060   -246       C  
ATOM   4799  C   GLU B  16      47.396  12.982  71.203  1.00 67.33           C  
ANISOU 4799  C   GLU B  16    11359   7152   7072  -1417  -1013   -237       C  
ATOM   4800  O   GLU B  16      47.220  14.089  71.639  1.00 66.16           O  
ANISOU 4800  O   GLU B  16    10798   7238   7100  -1379   -902   -247       O  
ATOM   4801  CB  GLU B  16      46.128  12.077  69.213  1.00 69.80           C  
ANISOU 4801  CB  GLU B  16    12142   7270   7108  -1781  -1258   -130       C  
ATOM   4802  CG  GLU B  16      45.034  13.115  69.140  1.00 70.35           C  
ANISOU 4802  CG  GLU B  16    11749   7661   7322  -1957  -1250    -56       C  
ATOM   4803  CD  GLU B  16      43.673  12.599  68.715  1.00 74.40           C  
ANISOU 4803  CD  GLU B  16    12342   8244   7682  -2381  -1453     94       C  
ATOM   4804  OE1 GLU B  16      43.527  11.852  67.682  1.00 76.83           O  
ANISOU 4804  OE1 GLU B  16    13071   8329   7793  -2525  -1605    133       O  
ATOM   4805  OE2 GLU B  16      42.727  13.004  69.429  1.00 75.84           O  
ANISOU 4805  OE2 GLU B  16    12143   8735   7939  -2574  -1456    178       O  
ATOM   4806  N   GLU B  17      47.628  11.938  71.979  1.00 69.83           N  
ANISOU 4806  N   GLU B  17    11964   7315   7252  -1475  -1101   -222       N  
ATOM   4807  CA  GLU B  17      47.561  12.005  73.417  1.00 70.02           C  
ANISOU 4807  CA  GLU B  17    11817   7467   7321  -1559  -1081   -203       C  
ATOM   4808  C   GLU B  17      48.413  13.128  73.997  1.00 68.08           C  
ANISOU 4808  C   GLU B  17    11203   7372   7293  -1284   -902   -276       C  
ATOM   4809  O   GLU B  17      47.917  13.925  74.826  1.00 67.14           O  
ANISOU 4809  O   GLU B  17    10751   7484   7276  -1382   -825   -264       O  
ATOM   4810  CB  GLU B  17      47.902  10.662  74.075  1.00 71.23           C  
ANISOU 4810  CB  GLU B  17    12415   7370   7277  -1620  -1225   -180       C  
ATOM   4811  CG  GLU B  17      47.796  10.788  75.584  1.00 75.85           C  
ANISOU 4811  CG  GLU B  17    12824   8100   7896  -1744  -1205   -154       C  
ATOM   4812  CD  GLU B  17      47.836   9.479  76.345  1.00 82.21           C  
ANISOU 4812  CD  GLU B  17    14072   8683   8480  -1914  -1385   -101       C  
ATOM   4813  OE1 GLU B  17      47.223   8.473  75.880  1.00 89.85           O  
ANISOU 4813  OE1 GLU B  17    15443   9474   9222  -2167  -1562    -34       O  
ATOM   4814  OE2 GLU B  17      48.467   9.471  77.428  1.00 80.32           O  
ANISOU 4814  OE2 GLU B  17    13803   8437   8278  -1820  -1368   -117       O  
ATOM   4815  N   HIS B  18      49.669  13.206  73.565  1.00 67.02           N  
ANISOU 4815  N   HIS B  18    11131   7121   7210   -950   -834   -346       N  
ATOM   4816  CA  HIS B  18      50.584  14.184  74.139  1.00 65.04           C  
ANISOU 4816  CA  HIS B  18    10569   7010   7134   -733   -698   -393       C  
ATOM   4817  C   HIS B  18      50.348  15.528  73.537  1.00 63.17           C  
ANISOU 4817  C   HIS B  18    10005   6953   7043   -702   -582   -417       C  
ATOM   4818  O   HIS B  18      50.575  16.549  74.178  1.00 63.44           O  
ANISOU 4818  O   HIS B  18     9760   7142   7204   -658   -491   -435       O  
ATOM   4819  CB  HIS B  18      52.045  13.813  73.881  1.00 65.69           C  
ANISOU 4819  CB  HIS B  18    10778   6967   7215   -395   -666   -436       C  
ATOM   4820  CG  HIS B  18      52.544  12.704  74.749  1.00 69.08           C  
ANISOU 4820  CG  HIS B  18    11476   7232   7540   -341   -777   -415       C  
ATOM   4821  ND1 HIS B  18      53.780  12.116  74.565  1.00 71.09           N  
ANISOU 4821  ND1 HIS B  18    11885   7360   7765     -5   -777   -440       N  
ATOM   4822  CD2 HIS B  18      51.989  12.096  75.827  1.00 66.95           C  
ANISOU 4822  CD2 HIS B  18    11345   6913   7180   -571   -895   -364       C  
ATOM   4823  CE1 HIS B  18      53.951  11.171  75.473  1.00 71.95           C  
ANISOU 4823  CE1 HIS B  18    12246   7317   7776    -14   -914   -405       C  
ATOM   4824  NE2 HIS B  18      52.888  11.154  76.261  1.00 71.58           N  
ANISOU 4824  NE2 HIS B  18    12203   7309   7685   -378   -989   -359       N  
ATOM   4825  N   PHE B  19      49.932  15.558  72.281  1.00 61.82           N  
ANISOU 4825  N   PHE B  19     9911   6739   6839   -724   -599   -416       N  
ATOM   4826  CA  PHE B  19      49.745  16.824  71.640  1.00 59.23           C  
ANISOU 4826  CA  PHE B  19     9318   6551   6636   -684   -514   -433       C  
ATOM   4827  C   PHE B  19      48.658  17.566  72.447  1.00 58.98           C  
ANISOU 4827  C   PHE B  19     9008   6718   6685   -857   -504   -400       C  
ATOM   4828  O   PHE B  19      48.896  18.689  72.879  1.00 56.41           O  
ANISOU 4828  O   PHE B  19     8440   6511   6481   -764   -407   -432       O  
ATOM   4829  CB  PHE B  19      49.462  16.624  70.136  1.00 59.16           C  
ANISOU 4829  CB  PHE B  19     9487   6441   6551   -702   -559   -427       C  
ATOM   4830  CG  PHE B  19      49.040  17.860  69.395  1.00 58.00           C  
ANISOU 4830  CG  PHE B  19     9111   6416   6509   -710   -519   -425       C  
ATOM   4831  CD1 PHE B  19      47.700  18.267  69.368  1.00 57.56           C  
ANISOU 4831  CD1 PHE B  19     8895   6486   6488   -903   -592   -361       C  
ATOM   4832  CD2 PHE B  19      49.958  18.581  68.654  1.00 55.02           C  
ANISOU 4832  CD2 PHE B  19     8690   6035   6180   -529   -422   -474       C  
ATOM   4833  CE1 PHE B  19      47.306  19.373  68.630  1.00 55.05           C  
ANISOU 4833  CE1 PHE B  19     8404   6252   6261   -879   -583   -353       C  
ATOM   4834  CE2 PHE B  19      49.568  19.703  67.967  1.00 53.18           C  
ANISOU 4834  CE2 PHE B  19     8302   5880   6022   -551   -412   -465       C  
ATOM   4835  CZ  PHE B  19      48.243  20.097  67.939  1.00 52.01           C  
ANISOU 4835  CZ  PHE B  19     8027   5819   5916   -710   -502   -407       C  
ATOM   4836  N   LYS B  20      47.512  16.921  72.711  1.00 60.73           N  
ANISOU 4836  N   LYS B  20     9277   6981   6818  -1106   -600   -332       N  
ATOM   4837  CA  LYS B  20      46.433  17.538  73.532  1.00 62.34           C  
ANISOU 4837  CA  LYS B  20     9186   7422   7077  -1250   -563   -297       C  
ATOM   4838  C   LYS B  20      46.879  17.994  74.920  1.00 62.54           C  
ANISOU 4838  C   LYS B  20     9080   7524   7158  -1183   -457   -342       C  
ATOM   4839  O   LYS B  20      46.593  19.121  75.370  1.00 63.98           O  
ANISOU 4839  O   LYS B  20     9007   7861   7443  -1114   -352   -372       O  
ATOM   4840  CB  LYS B  20      45.267  16.572  73.667  1.00 64.98           C  
ANISOU 4840  CB  LYS B  20     9603   7818   7269  -1568   -687   -198       C  
ATOM   4841  CG  LYS B  20      44.632  16.204  72.269  1.00 67.43           C  
ANISOU 4841  CG  LYS B  20    10040   8073   7506  -1696   -821   -129       C  
ATOM   4842  CD  LYS B  20      43.573  15.116  72.402  1.00 73.91           C  
ANISOU 4842  CD  LYS B  20    10996   8942   8143  -2074   -981     -6       C  
ATOM   4843  CE  LYS B  20      42.513  15.515  73.439  1.00 76.11           C  
ANISOU 4843  CE  LYS B  20    10899   9563   8455  -2245   -922     56       C  
ATOM   4844  NZ  LYS B  20      41.537  16.496  72.860  1.00 77.11           N  
ANISOU 4844  NZ  LYS B  20    10644   9953   8703  -2228   -902    109       N  
ATOM   4845  N   GLY B  21      47.633  17.143  75.586  1.00 62.79           N  
ANISOU 4845  N   GLY B  21     9322   7424   7110  -1185   -495   -348       N  
ATOM   4846  CA  GLY B  21      48.150  17.445  76.885  1.00 62.49           C  
ANISOU 4846  CA  GLY B  21     9215   7429   7099  -1150   -428   -378       C  
ATOM   4847  C   GLY B  21      48.847  18.757  76.913  1.00 61.52           C  
ANISOU 4847  C   GLY B  21     8902   7359   7114   -947   -315   -438       C  
ATOM   4848  O   GLY B  21      48.477  19.648  77.701  1.00 62.39           O  
ANISOU 4848  O   GLY B  21     8838   7600   7267   -963   -223   -463       O  
ATOM   4849  N   LEU B  22      49.845  18.888  76.046  1.00 60.44           N  
ANISOU 4849  N   LEU B  22     8820   7124   7022   -766   -317   -460       N  
ATOM   4850  CA  LEU B  22      50.674  20.069  76.039  1.00 58.40           C  
ANISOU 4850  CA  LEU B  22     8418   6910   6863   -618   -234   -498       C  
ATOM   4851  C   LEU B  22      49.956  21.263  75.555  1.00 58.99           C  
ANISOU 4851  C   LEU B  22     8328   7074   7011   -606   -176   -520       C  
ATOM   4852  O   LEU B  22      50.119  22.332  76.097  1.00 60.69           O  
ANISOU 4852  O   LEU B  22     8441   7343   7275   -565   -112   -549       O  
ATOM   4853  CB  LEU B  22      51.871  19.886  75.165  1.00 57.33           C  
ANISOU 4853  CB  LEU B  22     8351   6696   6737   -451   -239   -503       C  
ATOM   4854  CG  LEU B  22      52.889  18.814  75.484  1.00 55.13           C  
ANISOU 4854  CG  LEU B  22     8221   6325   6399   -353   -290   -484       C  
ATOM   4855  CD1 LEU B  22      53.372  18.339  74.169  1.00 52.66           C  
ANISOU 4855  CD1 LEU B  22     8023   5932   6052   -203   -285   -496       C  
ATOM   4856  CD2 LEU B  22      54.014  19.370  76.292  1.00 53.65           C  
ANISOU 4856  CD2 LEU B  22     7908   6214   6263   -279   -265   -471       C  
ATOM   4857  N   VAL B  23      49.180  21.128  74.499  1.00 59.77           N  
ANISOU 4857  N   VAL B  23     8431   7172   7108   -636   -215   -500       N  
ATOM   4858  CA  VAL B  23      48.350  22.243  74.071  1.00 58.80           C  
ANISOU 4858  CA  VAL B  23     8146   7138   7056   -610   -185   -508       C  
ATOM   4859  C   VAL B  23      47.481  22.707  75.264  1.00 58.17           C  
ANISOU 4859  C   VAL B  23     7915   7201   6987   -654   -118   -519       C  
ATOM   4860  O   VAL B  23      47.329  23.868  75.512  1.00 57.35           O  
ANISOU 4860  O   VAL B  23     7713   7140   6936   -552    -51   -558       O  
ATOM   4861  CB  VAL B  23      47.509  21.788  72.890  1.00 59.56           C  
ANISOU 4861  CB  VAL B  23     8274   7228   7127   -684   -273   -459       C  
ATOM   4862  CG1 VAL B  23      46.266  22.632  72.724  1.00 61.25           C  
ANISOU 4862  CG1 VAL B  23     8282   7586   7404   -687   -274   -435       C  
ATOM   4863  CG2 VAL B  23      48.342  21.866  71.647  1.00 61.32           C  
ANISOU 4863  CG2 VAL B  23     8627   7326   7346   -594   -294   -472       C  
ATOM   4864  N   LEU B  24      46.947  21.770  76.032  1.00 58.47           N  
ANISOU 4864  N   LEU B  24     7968   7301   6948   -808   -133   -487       N  
ATOM   4865  CA  LEU B  24      46.183  22.134  77.199  1.00 58.05           C  
ANISOU 4865  CA  LEU B  24     7774   7406   6875   -856    -40   -500       C  
ATOM   4866  C   LEU B  24      46.994  22.786  78.297  1.00 56.96           C  
ANISOU 4866  C   LEU B  24     7682   7224   6735   -782     45   -564       C  
ATOM   4867  O   LEU B  24      46.473  23.648  78.997  1.00 58.87           O  
ANISOU 4867  O   LEU B  24     7823   7564   6980   -725    153   -607       O  
ATOM   4868  CB  LEU B  24      45.430  20.912  77.735  1.00 60.18           C  
ANISOU 4868  CB  LEU B  24     8068   7769   7030  -1097    -85   -434       C  
ATOM   4869  CG  LEU B  24      44.896  20.986  79.182  1.00 59.88           C  
ANISOU 4869  CG  LEU B  24     7941   7891   6921  -1195     25   -448       C  
ATOM   4870  CD1 LEU B  24      43.859  22.081  79.381  1.00 59.20           C  
ANISOU 4870  CD1 LEU B  24     7579   8028   6885  -1082    163   -475       C  
ATOM   4871  CD2 LEU B  24      44.378  19.607  79.609  1.00 59.01           C  
ANISOU 4871  CD2 LEU B  24     7926   7833   6662  -1492    -57   -365       C  
ATOM   4872  N   ILE B  25      48.259  22.401  78.441  1.00 55.72           N  
ANISOU 4872  N   ILE B  25     7681   6926   6564   -773     -6   -565       N  
ATOM   4873  CA  ILE B  25      49.145  22.943  79.479  1.00 54.43           C  
ANISOU 4873  CA  ILE B  25     7576   6721   6384   -749     35   -598       C  
ATOM   4874  C   ILE B  25      49.467  24.333  79.075  1.00 54.91           C  
ANISOU 4874  C   ILE B  25     7597   6756   6509   -613     79   -640       C  
ATOM   4875  O   ILE B  25      49.514  25.210  79.881  1.00 57.49           O  
ANISOU 4875  O   ILE B  25     7949   7085   6809   -594    143   -682       O  
ATOM   4876  CB  ILE B  25      50.505  22.143  79.631  1.00 53.10           C  
ANISOU 4876  CB  ILE B  25     7544   6439   6192   -756    -59   -561       C  
ATOM   4877  CG1 ILE B  25      50.281  20.831  80.372  1.00 50.61           C  
ANISOU 4877  CG1 ILE B  25     7348   6102   5780   -900   -122   -522       C  
ATOM   4878  CG2 ILE B  25      51.596  23.000  80.327  1.00 50.21           C  
ANISOU 4878  CG2 ILE B  25     7198   6048   5831   -724    -48   -571       C  
ATOM   4879  CD1 ILE B  25      51.367  19.875  80.363  1.00 44.93           C  
ANISOU 4879  CD1 ILE B  25     6774   5263   5034   -860   -232   -480       C  
ATOM   4880  N   ALA B  26      49.699  24.538  77.800  1.00 55.74           N  
ANISOU 4880  N   ALA B  26     7684   6819   6675   -533     36   -628       N  
ATOM   4881  CA  ALA B  26      50.002  25.866  77.254  1.00 55.98           C  
ANISOU 4881  CA  ALA B  26     7716   6807   6748   -431     51   -655       C  
ATOM   4882  C   ALA B  26      48.911  26.900  77.506  1.00 57.61           C  
ANISOU 4882  C   ALA B  26     7869   7055   6965   -345    120   -704       C  
ATOM   4883  O   ALA B  26      49.232  28.002  77.883  1.00 58.99           O  
ANISOU 4883  O   ALA B  26     8132   7164   7116   -289    148   -744       O  
ATOM   4884  CB  ALA B  26      50.262  25.764  75.783  1.00 54.37           C  
ANISOU 4884  CB  ALA B  26     7509   6562   6585   -388     -6   -628       C  
ATOM   4885  N   PHE B  27      47.641  26.560  77.274  1.00 58.38           N  
ANISOU 4885  N   PHE B  27     7832   7264   7084   -328    140   -693       N  
ATOM   4886  CA  PHE B  27      46.573  27.554  77.418  1.00 60.51           C  
ANISOU 4886  CA  PHE B  27     8009   7607   7374   -181    211   -733       C  
ATOM   4887  C   PHE B  27      46.371  27.773  78.922  1.00 61.54           C  
ANISOU 4887  C   PHE B  27     8166   7793   7424   -183    337   -790       C  
ATOM   4888  O   PHE B  27      46.121  28.883  79.395  1.00 62.41           O  
ANISOU 4888  O   PHE B  27     8336   7872   7506    -31    418   -857       O  
ATOM   4889  CB  PHE B  27      45.249  27.061  76.762  1.00 61.78           C  
ANISOU 4889  CB  PHE B  27     7958   7936   7578   -180    187   -678       C  
ATOM   4890  CG  PHE B  27      45.163  27.279  75.269  1.00 60.94           C  
ANISOU 4890  CG  PHE B  27     7844   7769   7540   -131     71   -634       C  
ATOM   4891  CD1 PHE B  27      44.819  26.229  74.412  1.00 63.91           C  
ANISOU 4891  CD1 PHE B  27     8173   8190   7918   -271    -29   -554       C  
ATOM   4892  CD2 PHE B  27      45.397  28.527  74.714  1.00 61.39           C  
ANISOU 4892  CD2 PHE B  27     7987   7705   7634     31     45   -667       C  
ATOM   4893  CE1 PHE B  27      44.766  26.423  73.003  1.00 64.44           C  
ANISOU 4893  CE1 PHE B  27     8274   8186   8026   -248   -143   -512       C  
ATOM   4894  CE2 PHE B  27      45.329  28.737  73.328  1.00 63.18           C  
ANISOU 4894  CE2 PHE B  27     8234   7866   7905     52    -73   -621       C  
ATOM   4895  CZ  PHE B  27      45.016  27.697  72.469  1.00 62.71           C  
ANISOU 4895  CZ  PHE B  27     8118   7858   7851    -85   -161   -546       C  
ATOM   4896  N   SER B  28      46.504  26.675  79.655  1.00 61.38           N  
ANISOU 4896  N   SER B  28     8145   7833   7345   -359    345   -762       N  
ATOM   4897  CA  SER B  28      46.364  26.666  81.081  1.00 62.80           C  
ANISOU 4897  CA  SER B  28     8372   8067   7423   -418    453   -803       C  
ATOM   4898  C   SER B  28      47.345  27.625  81.714  1.00 61.80           C  
ANISOU 4898  C   SER B  28     8463   7773   7244   -377    467   -859       C  
ATOM   4899  O   SER B  28      46.952  28.363  82.587  1.00 63.85           O  
ANISOU 4899  O   SER B  28     8792   8043   7424   -302    585   -929       O  
ATOM   4900  CB  SER B  28      46.613  25.256  81.607  1.00 62.69           C  
ANISOU 4900  CB  SER B  28     8390   8084   7345   -648    401   -745       C  
ATOM   4901  OG  SER B  28      45.489  24.438  81.395  1.00 66.57           O  
ANISOU 4901  OG  SER B  28     8714   8757   7822   -745    409   -693       O  
ATOM   4902  N   GLN B  29      48.608  27.594  81.289  1.00 59.64           N  
ANISOU 4902  N   GLN B  29     8302   7362   6997   -436    348   -822       N  
ATOM   4903  CA  GLN B  29      49.614  28.589  81.664  1.00 60.40           C  
ANISOU 4903  CA  GLN B  29     8596   7313   7039   -442    319   -843       C  
ATOM   4904  C   GLN B  29      49.429  30.000  81.009  1.00 62.54           C  
ANISOU 4904  C   GLN B  29     8954   7484   7323   -278    323   -889       C  
ATOM   4905  O   GLN B  29      49.892  31.033  81.540  1.00 64.47           O  
ANISOU 4905  O   GLN B  29     9424   7597   7474   -279    322   -925       O  
ATOM   4906  CB  GLN B  29      51.004  28.052  81.322  1.00 59.41           C  
ANISOU 4906  CB  GLN B  29     8495   7139   6937   -562    189   -763       C  
ATOM   4907  CG  GLN B  29      51.399  26.815  82.131  1.00 57.92           C  
ANISOU 4907  CG  GLN B  29     8304   6993   6712   -699    151   -716       C  
ATOM   4908  CD  GLN B  29      52.786  26.285  81.818  1.00 56.37           C  
ANISOU 4908  CD  GLN B  29     8102   6774   6543   -753     28   -632       C  
ATOM   4909  OE1 GLN B  29      53.234  26.260  80.666  1.00 53.65           O  
ANISOU 4909  OE1 GLN B  29     7682   6435   6269   -684    -12   -602       O  
ATOM   4910  NE2 GLN B  29      53.476  25.834  82.862  1.00 57.51           N  
ANISOU 4910  NE2 GLN B  29     8321   6910   6621   -870    -31   -589       N  
ATOM   4911  N   TYR B  30      48.777  30.075  79.853  1.00 62.46           N  
ANISOU 4911  N   TYR B  30     8812   7511   7410   -155    305   -880       N  
ATOM   4912  CA  TYR B  30      48.514  31.384  79.257  1.00 62.95           C  
ANISOU 4912  CA  TYR B  30     8983   7461   7475     12    289   -919       C  
ATOM   4913  C   TYR B  30      47.338  31.987  80.003  1.00 64.18           C  
ANISOU 4913  C   TYR B  30     9141   7659   7584    212    425  -1003       C  
ATOM   4914  O   TYR B  30      47.317  33.153  80.320  1.00 63.39           O  
ANISOU 4914  O   TYR B  30     9268   7414   7404    344    450  -1069       O  
ATOM   4915  CB  TYR B  30      48.218  31.235  77.746  1.00 62.66           C  
ANISOU 4915  CB  TYR B  30     8814   7447   7548     69    204   -869       C  
ATOM   4916  CG  TYR B  30      49.426  31.290  76.834  1.00 63.55           C  
ANISOU 4916  CG  TYR B  30     9012   7468   7667    -54     89   -811       C  
ATOM   4917  CD1 TYR B  30      50.421  32.219  77.033  1.00 69.12           C  
ANISOU 4917  CD1 TYR B  30     9937   8041   8287   -131     40   -811       C  
ATOM   4918  CD2 TYR B  30      49.541  30.443  75.724  1.00 69.98           C  
ANISOU 4918  CD2 TYR B  30     9698   8340   8551   -105     32   -753       C  
ATOM   4919  CE1 TYR B  30      51.533  32.296  76.188  1.00 71.81           C  
ANISOU 4919  CE1 TYR B  30    10313   8354   8616   -265    -51   -744       C  
ATOM   4920  CE2 TYR B  30      50.663  30.513  74.848  1.00 71.71           C  
ANISOU 4920  CE2 TYR B  30     9981   8509   8758   -200    -41   -704       C  
ATOM   4921  CZ  TYR B  30      51.659  31.461  75.115  1.00 73.77           C  
ANISOU 4921  CZ  TYR B  30    10408   8684   8938   -283    -75   -696       C  
ATOM   4922  OH  TYR B  30      52.780  31.582  74.312  1.00 77.10           O  
ANISOU 4922  OH  TYR B  30    10856   9111   9328   -403   -131   -635       O  
ATOM   4923  N   LEU B  31      46.355  31.160  80.312  1.00 65.37           N  
ANISOU 4923  N   LEU B  31     9051   8021   7766    231    519   -998       N  
ATOM   4924  CA  LEU B  31      45.085  31.691  80.821  1.00 68.72           C  
ANISOU 4924  CA  LEU B  31     9383   8566   8161    465    672  -1066       C  
ATOM   4925  C   LEU B  31      44.676  31.041  82.111  1.00 68.76           C  
ANISOU 4925  C   LEU B  31     9317   8737   8071    372    825  -1093       C  
ATOM   4926  O   LEU B  31      43.947  30.061  82.116  1.00 68.58           O  
ANISOU 4926  O   LEU B  31     9028   8950   8078    281    862  -1040       O  
ATOM   4927  CB  LEU B  31      43.981  31.455  79.799  1.00 70.08           C  
ANISOU 4927  CB  LEU B  31     9252   8919   8456    593    645  -1011       C  
ATOM   4928  CG  LEU B  31      43.926  32.155  78.447  1.00 71.69           C  
ANISOU 4928  CG  LEU B  31     9478   9007   8753    738    506   -981       C  
ATOM   4929  CD1 LEU B  31      42.481  32.080  78.007  1.00 74.90           C  
ANISOU 4929  CD1 LEU B  31     9559   9660   9241    923    538   -942       C  
ATOM   4930  CD2 LEU B  31      44.315  33.622  78.573  1.00 76.33           C  
ANISOU 4930  CD2 LEU B  31    10396   9338   9270    932    496  -1063       C  
ATOM   4931  N   GLN B  32      45.138  31.622  83.201  1.00 69.56           N  
ANISOU 4931  N   GLN B  32     9689   8708   8032    367    902  -1170       N  
ATOM   4932  CA  GLN B  32      45.085  30.988  84.515  1.00 70.17           C  
ANISOU 4932  CA  GLN B  32     9791   8886   7983    204   1021  -1192       C  
ATOM   4933  C   GLN B  32      43.723  31.070  85.150  1.00 72.72           C  
ANISOU 4933  C   GLN B  32     9930   9458   8244    376   1247  -1251       C  
ATOM   4934  O   GLN B  32      43.482  30.464  86.179  1.00 73.45           O  
ANISOU 4934  O   GLN B  32     9999   9687   8220    226   1366  -1262       O  
ATOM   4935  CB  GLN B  32      46.154  31.590  85.434  1.00 69.26           C  
ANISOU 4935  CB  GLN B  32    10067   8529   7720     98    997  -1239       C  
ATOM   4936  CG  GLN B  32      47.582  31.194  84.994  1.00 67.99           C  
ANISOU 4936  CG  GLN B  32    10000   8222   7610   -142    779  -1145       C  
ATOM   4937  CD  GLN B  32      48.672  32.107  85.562  1.00 68.03           C  
ANISOU 4937  CD  GLN B  32    10380   7985   7483   -236    703  -1163       C  
ATOM   4938  OE1 GLN B  32      48.890  33.207  85.078  1.00 69.55           O  
ANISOU 4938  OE1 GLN B  32    10760   8011   7656   -124    651  -1191       O  
ATOM   4939  NE2 GLN B  32      49.361  31.635  86.585  1.00 65.98           N  
ANISOU 4939  NE2 GLN B  32    10250   7703   7118   -470    671  -1133       N  
ATOM   4940  N   GLN B  33      42.809  31.791  84.533  1.00 74.76           N  
ANISOU 4940  N   GLN B  33    10038   9798   8570    692   1308  -1281       N  
ATOM   4941  CA  GLN B  33      41.561  32.037  85.241  1.00 79.07           C  
ANISOU 4941  CA  GLN B  33    10403  10603   9035    915   1556  -1347       C  
ATOM   4942  C   GLN B  33      40.337  31.549  84.502  1.00 80.36           C  
ANISOU 4942  C   GLN B  33    10086  11123   9324   1006   1579  -1261       C  
ATOM   4943  O   GLN B  33      39.204  31.696  85.012  1.00 83.41           O  
ANISOU 4943  O   GLN B  33    10224  11813   9655   1201   1795  -1292       O  
ATOM   4944  CB  GLN B  33      41.451  33.494  85.665  1.00 81.01           C  
ANISOU 4944  CB  GLN B  33    10952  10656   9173   1279   1676  -1488       C  
ATOM   4945  CG  GLN B  33      42.681  33.897  86.423  1.00 80.66           C  
ANISOU 4945  CG  GLN B  33    11400  10271   8976   1104   1621  -1546       C  
ATOM   4946  CD  GLN B  33      42.692  35.327  86.865  1.00 85.66           C  
ANISOU 4946  CD  GLN B  33    12449  10642   9456   1409   1706  -1683       C  
ATOM   4947  OE1 GLN B  33      42.884  35.587  88.037  1.00 90.43           O  
ANISOU 4947  OE1 GLN B  33    13351  11155   9854   1369   1836  -1772       O  
ATOM   4948  NE2 GLN B  33      42.488  36.271  85.943  1.00 88.94           N  
ANISOU 4948  NE2 GLN B  33    12938  10908   9947   1711   1620  -1702       N  
ATOM   4949  N   CYS B  34      40.584  30.927  83.351  1.00 77.13           N  
ANISOU 4949  N   CYS B  34     9546  10697   9063    844   1364  -1146       N  
ATOM   4950  CA  CYS B  34      39.541  30.196  82.641  1.00 79.42           C  
ANISOU 4950  CA  CYS B  34     9404  11320   9451    797   1330  -1027       C  
ATOM   4951  C   CYS B  34      39.195  28.856  83.296  1.00 79.97           C  
ANISOU 4951  C   CYS B  34     9290  11660   9434    440   1384   -949       C  
ATOM   4952  O   CYS B  34      40.054  28.194  83.905  1.00 78.22           O  
ANISOU 4952  O   CYS B  34     9300  11291   9128    160   1345   -954       O  
ATOM   4953  CB  CYS B  34      39.916  29.936  81.178  1.00 77.09           C  
ANISOU 4953  CB  CYS B  34     9092  10891   9306    714   1075   -930       C  
ATOM   4954  SG  CYS B  34      39.899  31.416  80.188  1.00 78.55           S  
ANISOU 4954  SG  CYS B  34     9394  10860   9593   1113    989   -976       S  
ATOM   4955  N   PRO B  35      37.918  28.465  83.204  1.00 83.03           N  
ANISOU 4955  N   PRO B  35     9260  12459   9828    440   1464   -866       N  
ATOM   4956  CA  PRO B  35      37.618  27.121  83.668  1.00 83.40           C  
ANISOU 4956  CA  PRO B  35     9169  12745   9776     27   1463   -764       C  
ATOM   4957  C   PRO B  35      38.095  26.038  82.707  1.00 81.16           C  
ANISOU 4957  C   PRO B  35     8949  12333   9557   -298   1190   -639       C  
ATOM   4958  O   PRO B  35      38.495  26.297  81.550  1.00 78.88           O  
ANISOU 4958  O   PRO B  35     8729  11839   9403   -201   1013   -617       O  
ATOM   4959  CB  PRO B  35      36.092  27.134  83.807  1.00 87.58           C  
ANISOU 4959  CB  PRO B  35     9206  13790  10280    120   1627   -696       C  
ATOM   4960  CG  PRO B  35      35.769  28.554  84.076  1.00 89.56           C  
ANISOU 4960  CG  PRO B  35     9441  14036  10550    633   1822   -830       C  
ATOM   4961  CD  PRO B  35      36.716  29.317  83.188  1.00 86.14           C  
ANISOU 4961  CD  PRO B  35     9334  13145  10248    824   1631   -887       C  
ATOM   4962  N   PHE B  36      38.056  24.823  83.223  1.00 81.54           N  
ANISOU 4962  N   PHE B  36     9012  12487   9481   -687   1159   -562       N  
ATOM   4963  CA  PHE B  36      38.667  23.688  82.598  1.00 80.01           C  
ANISOU 4963  CA  PHE B  36     9002  12107   9290  -1002    919   -470       C  
ATOM   4964  C   PHE B  36      38.049  23.388  81.227  1.00 81.34           C  
ANISOU 4964  C   PHE B  36     8967  12380   9558  -1047    743   -343       C  
ATOM   4965  O   PHE B  36      38.738  22.946  80.312  1.00 79.51           O  
ANISOU 4965  O   PHE B  36     8944  11885   9380  -1129    543   -310       O  
ATOM   4966  CB  PHE B  36      38.558  22.504  83.562  1.00 81.06           C  
ANISOU 4966  CB  PHE B  36     9211  12355   9234  -1399    931   -410       C  
ATOM   4967  CG  PHE B  36      38.948  21.186  82.956  1.00 80.82           C  
ANISOU 4967  CG  PHE B  36     9377  12166   9163  -1736    679   -298       C  
ATOM   4968  CD1 PHE B  36      40.292  20.905  82.669  1.00 75.50           C  
ANISOU 4968  CD1 PHE B  36     9073  11081   8530  -1717    529   -341       C  
ATOM   4969  CD2 PHE B  36      37.963  20.217  82.676  1.00 81.07           C  
ANISOU 4969  CD2 PHE B  36     9236  12470   9097  -2073    588   -142       C  
ATOM   4970  CE1 PHE B  36      40.650  19.685  82.108  1.00 75.60           C  
ANISOU 4970  CE1 PHE B  36     9307  10928   8489  -1969    310   -252       C  
ATOM   4971  CE2 PHE B  36      38.310  19.009  82.106  1.00 79.36           C  
ANISOU 4971  CE2 PHE B  36     9281  12060   8810  -2376    344    -45       C  
ATOM   4972  CZ  PHE B  36      39.650  18.738  81.802  1.00 75.64           C  
ANISOU 4972  CZ  PHE B  36     9206  11149   8383  -2296    211   -109       C  
ATOM   4973  N   ASP B  37      36.750  23.668  81.094  1.00 85.31           N  
ANISOU 4973  N   ASP B  37     9057  13281  10075   -978    824   -270       N  
ATOM   4974  CA  ASP B  37      35.975  23.445  79.873  1.00 86.15           C  
ANISOU 4974  CA  ASP B  37     8916  13557  10262  -1040    653   -124       C  
ATOM   4975  C   ASP B  37      36.203  24.426  78.774  1.00 85.05           C  
ANISOU 4975  C   ASP B  37     8793  13223  10298   -700    562   -162       C  
ATOM   4976  O   ASP B  37      36.093  24.071  77.607  1.00 85.55           O  
ANISOU 4976  O   ASP B  37     8855  13233  10416   -813    350    -58       O  
ATOM   4977  CB  ASP B  37      34.494  23.467  80.187  1.00 90.58           C  
ANISOU 4977  CB  ASP B  37     8968  14670  10776  -1071    773    -15       C  
ATOM   4978  CG  ASP B  37      34.085  22.323  81.018  1.00 92.65           C  
ANISOU 4978  CG  ASP B  37     9181  15185  10839  -1520    808     79       C  
ATOM   4979  OD1 ASP B  37      34.965  21.510  81.389  1.00 90.63           O  
ANISOU 4979  OD1 ASP B  37     9322  14633  10480  -1786    727     51       O  
ATOM   4980  OD2 ASP B  37      32.879  22.248  81.311  1.00 99.60           O  
ANISOU 4980  OD2 ASP B  37     9616  16572  11654  -1605    913    189       O  
ATOM   4981  N   GLU B  38      36.436  25.677  79.119  1.00 84.49           N  
ANISOU 4981  N   GLU B  38     8756  13052  10294   -297    713   -301       N  
ATOM   4982  CA  GLU B  38      36.872  26.590  78.105  1.00 82.74           C  
ANISOU 4982  CA  GLU B  38     8663  12563  10211    -18    601   -344       C  
ATOM   4983  C   GLU B  38      38.097  25.944  77.481  1.00 78.99           C  
ANISOU 4983  C   GLU B  38     8562  11714   9735   -240    420   -345       C  
ATOM   4984  O   GLU B  38      38.135  25.742  76.277  1.00 77.66           O  
ANISOU 4984  O   GLU B  38     8425  11452   9629   -302    231   -268       O  
ATOM   4985  CB  GLU B  38      37.260  27.921  78.723  1.00 83.29           C  
ANISOU 4985  CB  GLU B  38     8883  12466  10298    377    768   -510       C  
ATOM   4986  CG  GLU B  38      36.102  28.654  79.389  1.00 88.55           C  
ANISOU 4986  CG  GLU B  38     9221  13477  10949    689    984   -538       C  
ATOM   4987  CD  GLU B  38      35.821  30.010  78.718  1.00 91.63           C  
ANISOU 4987  CD  GLU B  38     9595  13767  11453   1156    956   -584       C  
ATOM   4988  OE1 GLU B  38      35.151  30.024  77.644  1.00 90.09           O  
ANISOU 4988  OE1 GLU B  38     9154  13709  11366   1205    794   -460       O  
ATOM   4989  OE2 GLU B  38      36.282  31.047  79.275  1.00 89.73           O  
ANISOU 4989  OE2 GLU B  38     9627  13292  11176   1455   1077   -737       O  
ATOM   4990  N   HIS B  39      39.090  25.592  78.303  1.00 76.89           N  
ANISOU 4990  N   HIS B  39     8576  11249   9389   -355    478   -427       N  
ATOM   4991  CA  HIS B  39      40.323  25.063  77.759  1.00 73.91           C  
ANISOU 4991  CA  HIS B  39     8528  10540   9015   -493    332   -435       C  
ATOM   4992  C   HIS B  39      40.174  23.713  77.055  1.00 73.53           C  
ANISOU 4992  C   HIS B  39     8515  10508   8916   -815    156   -311       C  
ATOM   4993  O   HIS B  39      40.828  23.468  76.041  1.00 71.10           O  
ANISOU 4993  O   HIS B  39     8399   9975   8641   -842     12   -295       O  
ATOM   4994  CB  HIS B  39      41.391  25.031  78.818  1.00 72.69           C  
ANISOU 4994  CB  HIS B  39     8629  10200   8790   -521    417   -532       C  
ATOM   4995  CG  HIS B  39      41.894  26.390  79.184  1.00 74.74           C  
ANISOU 4995  CG  HIS B  39     8999  10313   9084   -236    519   -651       C  
ATOM   4996  ND1 HIS B  39      42.194  27.349  78.236  1.00 75.25           N  
ANISOU 4996  ND1 HIS B  39     9131  10215   9245    -26    448   -676       N  
ATOM   4997  CD2 HIS B  39      42.174  26.948  80.385  1.00 74.13           C  
ANISOU 4997  CD2 HIS B  39     9032  10202   8931   -156    669   -747       C  
ATOM   4998  CE1 HIS B  39      42.628  28.442  78.838  1.00 73.35           C  
ANISOU 4998  CE1 HIS B  39     9048   9841   8982    166    541   -779       C  
ATOM   4999  NE2 HIS B  39      42.622  28.227  80.141  1.00 74.55           N  
ANISOU 4999  NE2 HIS B  39     9233  10065   9029     96    678   -826       N  
ATOM   5000  N   VAL B  40      39.320  22.842  77.580  1.00 75.14           N  
ANISOU 5000  N   VAL B  40     8563  10973   9016  -1072    167   -221       N  
ATOM   5001  CA  VAL B  40      38.978  21.633  76.842  1.00 76.58           C  
ANISOU 5001  CA  VAL B  40     8798  11178   9121  -1400    -26    -84       C  
ATOM   5002  C   VAL B  40      38.544  22.017  75.428  1.00 76.85           C  
ANISOU 5002  C   VAL B  40     8728  11218   9254  -1316   -169    -14       C  
ATOM   5003  O   VAL B  40      39.094  21.499  74.451  1.00 76.53           O  
ANISOU 5003  O   VAL B  40     8945  10935   9200  -1411   -331     12       O  
ATOM   5004  CB  VAL B  40      37.858  20.809  77.518  1.00 80.26           C  
ANISOU 5004  CB  VAL B  40     9046  12002   9446  -1723     -9     37       C  
ATOM   5005  CG1 VAL B  40      37.847  19.335  77.002  1.00 80.36           C  
ANISOU 5005  CG1 VAL B  40     9306  11917   9310  -2141   -235    164       C  
ATOM   5006  CG2 VAL B  40      38.019  20.834  79.019  1.00 80.33           C  
ANISOU 5006  CG2 VAL B  40     9064  12090   9368  -1736    186    -42       C  
ATOM   5007  N   LYS B  41      37.617  22.965  75.300  1.00 78.19           N  
ANISOU 5007  N   LYS B  41     8547  11643   9519  -1106   -107     10       N  
ATOM   5008  CA  LYS B  41      37.145  23.333  73.966  1.00 79.20           C  
ANISOU 5008  CA  LYS B  41     8573  11784   9736  -1038   -272     96       C  
ATOM   5009  C   LYS B  41      38.282  23.697  73.040  1.00 76.42           C  
ANISOU 5009  C   LYS B  41     8563  11030   9444   -905   -359     16       C  
ATOM   5010  O   LYS B  41      38.587  22.955  72.102  1.00 77.07           O  
ANISOU 5010  O   LYS B  41     8865  10944   9474  -1104   -528     75       O  
ATOM   5011  CB  LYS B  41      36.020  24.376  73.986  1.00 81.76           C  
ANISOU 5011  CB  LYS B  41     8468  12434  10163   -763   -201    134       C  
ATOM   5012  CG  LYS B  41      34.660  23.703  74.061  1.00 85.76           C  
ANISOU 5012  CG  LYS B  41     8580  13401  10603  -1023   -253    320       C  
ATOM   5013  CD  LYS B  41      33.522  24.610  74.536  1.00 89.70           C  
ANISOU 5013  CD  LYS B  41     8577  14327  11176   -725   -100    347       C  
ATOM   5014  CE  LYS B  41      33.239  24.420  76.026  1.00 90.54           C  
ANISOU 5014  CE  LYS B  41     8521  14702  11178   -761    160    295       C  
ATOM   5015  NZ  LYS B  41      33.041  22.991  76.385  1.00 90.82           N  
ANISOU 5015  NZ  LYS B  41     8590  14884  11036  -1297     92    415       N  
ATOM   5016  N   LEU B  42      38.903  24.830  73.311  1.00 75.34           N  
ANISOU 5016  N   LEU B  42     8490  10743   9392   -585   -241   -116       N  
ATOM   5017  CA  LEU B  42      40.098  25.300  72.598  1.00 72.93           C  
ANISOU 5017  CA  LEU B  42     8496  10087   9127   -468   -291   -198       C  
ATOM   5018  C   LEU B  42      41.088  24.225  72.140  1.00 70.50           C  
ANISOU 5018  C   LEU B  42     8505   9547   8736   -690   -378   -196       C  
ATOM   5019  O   LEU B  42      41.681  24.351  71.068  1.00 69.50           O  
ANISOU 5019  O   LEU B  42     8566   9219   8621   -667   -471   -200       O  
ATOM   5020  CB  LEU B  42      40.890  26.248  73.488  1.00 72.20           C  
ANISOU 5020  CB  LEU B  42     8510   9863   9058   -236   -130   -340       C  
ATOM   5021  CG  LEU B  42      40.482  27.645  73.925  1.00 74.66           C  
ANISOU 5021  CG  LEU B  42     8709  10226   9433     91    -22   -410       C  
ATOM   5022  CD1 LEU B  42      41.823  28.367  74.024  1.00 72.02           C  
ANISOU 5022  CD1 LEU B  42     8692   9582   9091    189      6   -520       C  
ATOM   5023  CD2 LEU B  42      39.551  28.332  72.966  1.00 75.27           C  
ANISOU 5023  CD2 LEU B  42     8606  10397   9597    264   -129   -340       C  
ATOM   5024  N   VAL B  43      41.303  23.207  72.966  1.00 69.61           N  
ANISOU 5024  N   VAL B  43     8471   9452   8526   -880   -339   -195       N  
ATOM   5025  CA  VAL B  43      42.230  22.170  72.610  1.00 68.25           C  
ANISOU 5025  CA  VAL B  43     8616   9052   8266  -1030   -416   -199       C  
ATOM   5026  C   VAL B  43      41.685  21.302  71.447  1.00 69.61           C  
ANISOU 5026  C   VAL B  43     8886   9204   8360  -1252   -603    -84       C  
ATOM   5027  O   VAL B  43      42.389  21.109  70.424  1.00 67.65           O  
ANISOU 5027  O   VAL B  43     8889   8728   8086  -1233   -679   -101       O  
ATOM   5028  CB  VAL B  43      42.616  21.326  73.813  1.00 68.25           C  
ANISOU 5028  CB  VAL B  43     8718   9042   8171  -1159   -354   -223       C  
ATOM   5029  CG1 VAL B  43      43.423  20.107  73.349  1.00 67.60           C  
ANISOU 5029  CG1 VAL B  43     8983   8721   7980  -1291   -463   -210       C  
ATOM   5030  CG2 VAL B  43      43.431  22.152  74.758  1.00 65.95           C  
ANISOU 5030  CG2 VAL B  43     8427   8695   7936   -959   -204   -335       C  
ATOM   5031  N   ASN B  44      40.448  20.818  71.595  1.00 71.89           N  
ANISOU 5031  N   ASN B  44     8981   9741   8593  -1471   -675     37       N  
ATOM   5032  CA  ASN B  44      39.778  20.041  70.535  1.00 74.70           C  
ANISOU 5032  CA  ASN B  44     9424  10107   8853  -1736   -883    173       C  
ATOM   5033  C   ASN B  44      39.708  20.716  69.144  1.00 75.39           C  
ANISOU 5033  C   ASN B  44     9528  10106   9011  -1627   -992    199       C  
ATOM   5034  O   ASN B  44      39.793  20.030  68.115  1.00 76.53           O  
ANISOU 5034  O   ASN B  44     9945  10085   9049  -1804  -1151    256       O  
ATOM   5035  CB  ASN B  44      38.386  19.558  70.983  1.00 77.44           C  
ANISOU 5035  CB  ASN B  44     9482  10812   9128  -2018   -946    327       C  
ATOM   5036  CG  ASN B  44      38.427  18.723  72.283  1.00 79.39           C  
ANISOU 5036  CG  ASN B  44     9780  11132   9254  -2210   -867    321       C  
ATOM   5037  OD1 ASN B  44      39.299  17.871  72.495  1.00 76.85           O  
ANISOU 5037  OD1 ASN B  44     9838  10540   8823  -2295   -892    268       O  
ATOM   5038  ND2 ASN B  44      37.476  18.989  73.163  1.00 81.90           N  
ANISOU 5038  ND2 ASN B  44     9713  11824   9581  -2261   -767    376       N  
ATOM   5039  N   GLU B  45      39.588  22.044  69.113  1.00 75.34           N  
ANISOU 5039  N   GLU B  45     9287  10178   9161  -1341   -916    153       N  
ATOM   5040  CA  GLU B  45      39.709  22.821  67.862  1.00 75.22           C  
ANISOU 5040  CA  GLU B  45     9339  10032   9211  -1210  -1013    159       C  
ATOM   5041  C   GLU B  45      41.108  22.819  67.239  1.00 73.28           C  
ANISOU 5041  C   GLU B  45     9466   9447   8929  -1131   -983     51       C  
ATOM   5042  O   GLU B  45      41.217  22.841  66.005  1.00 74.22           O  
ANISOU 5042  O   GLU B  45     9765   9426   9008  -1181  -1105     85       O  
ATOM   5043  CB  GLU B  45      39.264  24.279  68.038  1.00 75.45           C  
ANISOU 5043  CB  GLU B  45     9079  10192   9397   -902   -952    134       C  
ATOM   5044  CG  GLU B  45      37.832  24.436  68.480  1.00 81.97           C  
ANISOU 5044  CG  GLU B  45     9479  11397  10270   -905   -971    248       C  
ATOM   5045  CD  GLU B  45      37.119  25.623  67.838  1.00 88.98           C  
ANISOU 5045  CD  GLU B  45    10146  12380  11281   -655  -1056    299       C  
ATOM   5046  OE1 GLU B  45      36.018  25.997  68.356  1.00 91.62           O  
ANISOU 5046  OE1 GLU B  45    10076  13056  11680   -535  -1021    369       O  
ATOM   5047  OE2 GLU B  45      37.635  26.161  66.806  1.00 88.84           O  
ANISOU 5047  OE2 GLU B  45    10359  12110  11286   -575  -1161    278       O  
ATOM   5048  N   LEU B  46      42.165  22.881  68.063  1.00 70.92           N  
ANISOU 5048  N   LEU B  46     9264   9043   8641  -1004   -819    -72       N  
ATOM   5049  CA  LEU B  46      43.526  22.909  67.547  1.00 68.30           C  
ANISOU 5049  CA  LEU B  46     9214   8460   8276   -917   -770   -162       C  
ATOM   5050  C   LEU B  46      43.901  21.518  67.137  1.00 68.71           C  
ANISOU 5050  C   LEU B  46     9563   8369   8176  -1094   -831   -144       C  
ATOM   5051  O   LEU B  46      44.665  21.304  66.187  1.00 68.25           O  
ANISOU 5051  O   LEU B  46     9764   8123   8045  -1072   -844   -176       O  
ATOM   5052  CB  LEU B  46      44.511  23.399  68.583  1.00 66.51           C  
ANISOU 5052  CB  LEU B  46     8967   8202   8103   -747   -602   -271       C  
ATOM   5053  CG  LEU B  46      44.900  24.867  68.479  1.00 67.47           C  
ANISOU 5053  CG  LEU B  46     9027   8290   8317   -546   -547   -327       C  
ATOM   5054  CD1 LEU B  46      45.937  25.160  67.384  1.00 64.19           C  
ANISOU 5054  CD1 LEU B  46     8827   7700   7863   -516   -560   -356       C  
ATOM   5055  CD2 LEU B  46      43.623  25.642  68.218  1.00 71.73           C  
ANISOU 5055  CD2 LEU B  46     9358   8964   8932   -487   -627   -265       C  
ATOM   5056  N   THR B  47      43.336  20.546  67.838  1.00 69.34           N  
ANISOU 5056  N   THR B  47     9634   8532   8181  -1275   -869    -90       N  
ATOM   5057  CA  THR B  47      43.621  19.180  67.495  1.00 68.78           C  
ANISOU 5057  CA  THR B  47     9913   8287   7935  -1446   -953    -70       C  
ATOM   5058  C   THR B  47      42.931  18.882  66.187  1.00 69.54           C  
ANISOU 5058  C   THR B  47    10155   8332   7935  -1633  -1133     28       C  
ATOM   5059  O   THR B  47      43.583  18.400  65.276  1.00 69.26           O  
ANISOU 5059  O   THR B  47    10467   8066   7784  -1627  -1162     -6       O  
ATOM   5060  CB  THR B  47      43.273  18.220  68.642  1.00 69.68           C  
ANISOU 5060  CB  THR B  47    10039   8472   7965  -1622   -965    -34       C  
ATOM   5061  OG1 THR B  47      43.987  18.668  69.794  1.00 69.31           O  
ANISOU 5061  OG1 THR B  47     9863   8459   8012  -1433   -800   -128       O  
ATOM   5062  CG2 THR B  47      43.696  16.766  68.333  1.00 68.87           C  
ANISOU 5062  CG2 THR B  47    10395   8119   7653  -1768  -1065    -25       C  
ATOM   5063  N   GLU B  48      41.655  19.230  66.052  1.00 70.39           N  
ANISOU 5063  N   GLU B  48     9994   8663   8086  -1778  -1249    150       N  
ATOM   5064  CA  GLU B  48      40.961  18.905  64.791  1.00 72.16           C  
ANISOU 5064  CA  GLU B  48    10368   8846   8204  -2002  -1460    270       C  
ATOM   5065  C   GLU B  48      41.667  19.512  63.594  1.00 70.04           C  
ANISOU 5065  C   GLU B  48    10294   8374   7944  -1847  -1454    207       C  
ATOM   5066  O   GLU B  48      41.668  18.967  62.496  1.00 70.76           O  
ANISOU 5066  O   GLU B  48    10714   8291   7881  -2003  -1583    248       O  
ATOM   5067  CB  GLU B  48      39.479  19.297  64.809  1.00 74.56           C  
ANISOU 5067  CB  GLU B  48    10279   9477   8574  -2158  -1597    433       C  
ATOM   5068  CG  GLU B  48      38.599  18.212  65.428  1.00 79.20           C  
ANISOU 5068  CG  GLU B  48    10825  10240   9026  -2511  -1703    563       C  
ATOM   5069  CD  GLU B  48      38.900  16.775  64.915  1.00 83.90           C  
ANISOU 5069  CD  GLU B  48    11970  10553   9356  -2809  -1847    594       C  
ATOM   5070  OE1 GLU B  48      39.607  16.010  65.633  1.00 83.64           O  
ANISOU 5070  OE1 GLU B  48    12188  10359   9233  -2798  -1760    508       O  
ATOM   5071  OE2 GLU B  48      38.426  16.398  63.807  1.00 84.55           O  
ANISOU 5071  OE2 GLU B  48    12267  10554   9304  -3051  -2061    707       O  
ATOM   5072  N   PHE B  49      42.290  20.647  63.854  1.00 67.59           N  
ANISOU 5072  N   PHE B  49     9806   8083   7793  -1560  -1301    107       N  
ATOM   5073  CA  PHE B  49      42.863  21.451  62.849  1.00 66.21           C  
ANISOU 5073  CA  PHE B  49     9743   7775   7639  -1429  -1290     62       C  
ATOM   5074  C   PHE B  49      44.217  20.898  62.446  1.00 64.50           C  
ANISOU 5074  C   PHE B  49     9886   7321   7300  -1354  -1172    -50       C  
ATOM   5075  O   PHE B  49      44.551  20.864  61.284  1.00 65.18           O  
ANISOU 5075  O   PHE B  49    10231   7255   7281  -1388  -1211    -56       O  
ATOM   5076  CB  PHE B  49      42.987  22.884  63.347  1.00 65.73           C  
ANISOU 5076  CB  PHE B  49     9388   7821   7765  -1181  -1189     10       C  
ATOM   5077  CG  PHE B  49      43.693  23.774  62.364  1.00 65.99           C  
ANISOU 5077  CG  PHE B  49     9568   7707   7799  -1072  -1178    -37       C  
ATOM   5078  CD1 PHE B  49      43.053  24.156  61.187  1.00 65.49           C  
ANISOU 5078  CD1 PHE B  49     9567   7609   7708  -1165  -1358     54       C  
ATOM   5079  CD2 PHE B  49      45.018  24.154  62.581  1.00 64.05           C  
ANISOU 5079  CD2 PHE B  49     9413   7367   7557   -918  -1003   -154       C  
ATOM   5080  CE1 PHE B  49      43.695  24.938  60.252  1.00 68.75           C  
ANISOU 5080  CE1 PHE B  49    10153   7878   8091  -1106  -1358     19       C  
ATOM   5081  CE2 PHE B  49      45.689  24.922  61.650  1.00 65.92           C  
ANISOU 5081  CE2 PHE B  49     9794   7492   7760   -872   -992   -183       C  
ATOM   5082  CZ  PHE B  49      45.021  25.338  60.474  1.00 67.22           C  
ANISOU 5082  CZ  PHE B  49    10047   7604   7890   -968  -1167   -101       C  
ATOM   5083  N   ALA B  50      44.999  20.481  63.423  1.00 63.53           N  
ANISOU 5083  N   ALA B  50     9767   7184   7187  -1240  -1024   -135       N  
ATOM   5084  CA  ALA B  50      46.237  19.799  63.179  1.00 63.31           C  
ANISOU 5084  CA  ALA B  50    10039   6973   7042  -1136   -912   -228       C  
ATOM   5085  C   ALA B  50      45.992  18.616  62.249  1.00 66.16           C  
ANISOU 5085  C   ALA B  50    10811   7144   7181  -1312  -1034   -190       C  
ATOM   5086  O   ALA B  50      46.759  18.399  61.296  1.00 67.57           O  
ANISOU 5086  O   ALA B  50    11283   7156   7234  -1236   -977   -248       O  
ATOM   5087  CB  ALA B  50      46.827  19.296  64.492  1.00 61.64           C  
ANISOU 5087  CB  ALA B  50     9768   6789   6862  -1032   -800   -284       C  
ATOM   5088  N   LYS B  51      44.945  17.845  62.539  1.00 67.10           N  
ANISOU 5088  N   LYS B  51    10972   7293   7229  -1560  -1198    -89       N  
ATOM   5089  CA  LYS B  51      44.705  16.618  61.824  1.00 70.48           C  
ANISOU 5089  CA  LYS B  51    11856   7512   7411  -1767  -1339    -46       C  
ATOM   5090  C   LYS B  51      44.458  16.970  60.374  1.00 72.34           C  
ANISOU 5090  C   LYS B  51    12265   7659   7562  -1862  -1437     -6       C  
ATOM   5091  O   LYS B  51      44.872  16.239  59.463  1.00 74.38           O  
ANISOU 5091  O   LYS B  51    12990   7669   7601  -1896  -1457    -41       O  
ATOM   5092  CB  LYS B  51      43.501  15.847  62.389  1.00 71.43           C  
ANISOU 5092  CB  LYS B  51    11958   7726   7458  -2097  -1531     91       C  
ATOM   5093  CG  LYS B  51      43.676  15.387  63.819  1.00 71.22           C  
ANISOU 5093  CG  LYS B  51    11819   7771   7472  -2059  -1454     62       C  
ATOM   5094  CD  LYS B  51      42.455  14.672  64.373  1.00 74.23           C  
ANISOU 5094  CD  LYS B  51    12161   8285   7757  -2434  -1639    212       C  
ATOM   5095  CE  LYS B  51      42.730  13.164  64.518  1.00 76.08           C  
ANISOU 5095  CE  LYS B  51    12938   8242   7725  -2589  -1734    210       C  
ATOM   5096  NZ  LYS B  51      41.704  12.369  65.257  1.00 72.93           N  
ANISOU 5096  NZ  LYS B  51    12544   7966   7200  -2987  -1906    354       N  
ATOM   5097  N   THR B  52      43.789  18.095  60.159  1.00 71.67           N  
ANISOU 5097  N   THR B  52    11834   7760   7637  -1891  -1502     65       N  
ATOM   5098  CA  THR B  52      43.402  18.423  58.830  1.00 73.41           C  
ANISOU 5098  CA  THR B  52    12214   7904   7774  -2025  -1643    131       C  
ATOM   5099  C   THR B  52      44.685  18.714  58.094  1.00 72.15           C  
ANISOU 5099  C   THR B  52    12292   7572   7551  -1809  -1461     -5       C  
ATOM   5100  O   THR B  52      44.776  18.507  56.898  1.00 73.36           O  
ANISOU 5100  O   THR B  52    12795   7554   7525  -1909  -1522      2       O  
ATOM   5101  CB  THR B  52      42.430  19.604  58.828  1.00 74.02           C  
ANISOU 5101  CB  THR B  52    11857   8220   8047  -2051  -1760    240       C  
ATOM   5102  OG1 THR B  52      41.144  19.117  59.197  1.00 77.23           O  
ANISOU 5102  OG1 THR B  52    12098   8803   8445  -2314  -1958    398       O  
ATOM   5103  CG2 THR B  52      42.295  20.197  57.480  1.00 75.02           C  
ANISOU 5103  CG2 THR B  52    12136   8252   8117  -2118  -1881    287       C  
ATOM   5104  N   CYS B  53      45.677  19.188  58.831  1.00 69.82           N  
ANISOU 5104  N   CYS B  53    11802   7342   7385  -1532  -1236   -120       N  
ATOM   5105  CA  CYS B  53      46.895  19.628  58.218  1.00 68.96           C  
ANISOU 5105  CA  CYS B  53    11811   7157   7234  -1339  -1050   -228       C  
ATOM   5106  C   CYS B  53      47.663  18.409  57.959  1.00 69.64           C  
ANISOU 5106  C   CYS B  53    12299   7053   7110  -1266   -951   -310       C  
ATOM   5107  O   CYS B  53      48.335  18.340  56.946  1.00 70.08           O  
ANISOU 5107  O   CYS B  53    12632   6988   7009  -1207   -860   -370       O  
ATOM   5108  CB  CYS B  53      47.675  20.589  59.112  1.00 67.85           C  
ANISOU 5108  CB  CYS B  53    11311   7179   7291  -1109   -871   -297       C  
ATOM   5109  SG  CYS B  53      46.955  22.286  59.315  1.00 69.22           S  
ANISOU 5109  SG  CYS B  53    11085   7526   7689  -1116   -962   -229       S  
ATOM   5110  N   VAL B  54      47.542  17.429  58.869  1.00 69.78           N  
ANISOU 5110  N   VAL B  54    12373   7036   7104  -1265   -972   -312       N  
ATOM   5111  CA  VAL B  54      48.158  16.121  58.693  1.00 70.80           C  
ANISOU 5111  CA  VAL B  54    12955   6937   7009  -1179   -917   -384       C  
ATOM   5112  C   VAL B  54      47.651  15.521  57.376  1.00 72.23           C  
ANISOU 5112  C   VAL B  54    13629   6890   6926  -1397  -1063   -344       C  
ATOM   5113  O   VAL B  54      48.444  15.103  56.532  1.00 74.16           O  
ANISOU 5113  O   VAL B  54    14249   6955   6973  -1255   -939   -437       O  
ATOM   5114  CB  VAL B  54      47.960  15.229  59.949  1.00 71.97           C  
ANISOU 5114  CB  VAL B  54    13101   7073   7173  -1190   -967   -369       C  
ATOM   5115  CG1 VAL B  54      47.685  13.774  59.598  1.00 75.14           C  
ANISOU 5115  CG1 VAL B  54    14079   7186   7286  -1330  -1103   -355       C  
ATOM   5116  CG2 VAL B  54      49.186  15.309  60.889  1.00 71.18           C  
ANISOU 5116  CG2 VAL B  54    12804   7051   7191   -849   -749   -472       C  
ATOM   5117  N   ALA B  55      46.345  15.594  57.147  1.00 72.17           N  
ANISOU 5117  N   ALA B  55    13592   6917   6913  -1739  -1319   -200       N  
ATOM   5118  CA  ALA B  55      45.740  15.114  55.894  1.00 73.90           C  
ANISOU 5118  CA  ALA B  55    14266   6934   6878  -2016  -1509   -130       C  
ATOM   5119  C   ALA B  55      46.186  15.888  54.662  1.00 74.48           C  
ANISOU 5119  C   ALA B  55    14435   6964   6898  -1959  -1430   -171       C  
ATOM   5120  O   ALA B  55      46.470  15.290  53.627  1.00 75.15           O  
ANISOU 5120  O   ALA B  55    15040   6805   6707  -2004  -1424   -215       O  
ATOM   5121  CB  ALA B  55      44.231  15.106  55.993  1.00 74.24           C  
ANISOU 5121  CB  ALA B  55    14162   7096   6950  -2409  -1817     65       C  
ATOM   5122  N   ASP B  56      46.254  17.224  54.787  1.00 73.55           N  
ANISOU 5122  N   ASP B  56    13852   7071   7022  -1867  -1370   -161       N  
ATOM   5123  CA  ASP B  56      46.553  18.132  53.666  1.00 74.30           C  
ANISOU 5123  CA  ASP B  56    13999   7152   7079  -1869  -1334   -173       C  
ATOM   5124  C   ASP B  56      47.444  19.326  54.036  1.00 73.28           C  
ANISOU 5124  C   ASP B  56    13481   7208   7153  -1615  -1117   -250       C  
ATOM   5125  O   ASP B  56      46.940  20.374  54.441  1.00 72.20           O  
ANISOU 5125  O   ASP B  56    12956   7241   7235  -1636  -1202   -182       O  
ATOM   5126  CB  ASP B  56      45.260  18.644  53.005  1.00 74.71           C  
ANISOU 5126  CB  ASP B  56    14006   7235   7148  -2187  -1643     -2       C  
ATOM   5127  CG  ASP B  56      45.524  19.273  51.636  1.00 78.70           C  
ANISOU 5127  CG  ASP B  56    14752   7634   7515  -2258  -1653     -5       C  
ATOM   5128  OD1 ASP B  56      46.647  19.798  51.399  1.00 79.47           O  
ANISOU 5128  OD1 ASP B  56    14846   7744   7604  -2047  -1404   -127       O  
ATOM   5129  OD2 ASP B  56      44.633  19.210  50.750  1.00 84.25           O  
ANISOU 5129  OD2 ASP B  56    15673   8246   8093  -2554  -1916    122       O  
ATOM   5130  N   GLU B  57      48.754  19.199  53.829  1.00 74.34           N  
ANISOU 5130  N   GLU B  57    13739   7315   7192  -1384   -847   -383       N  
ATOM   5131  CA  GLU B  57      49.713  20.271  54.161  1.00 73.62           C  
ANISOU 5131  CA  GLU B  57    13303   7416   7252  -1190   -644   -441       C  
ATOM   5132  C   GLU B  57      49.401  21.645  53.530  1.00 73.42           C  
ANISOU 5132  C   GLU B  57    13141   7458   7297  -1328   -743   -373       C  
ATOM   5133  O   GLU B  57      49.695  22.668  54.151  1.00 73.02           O  
ANISOU 5133  O   GLU B  57    12744   7569   7432  -1243   -691   -372       O  
ATOM   5134  CB  GLU B  57      51.130  19.937  53.677  1.00 75.76           C  
ANISOU 5134  CB  GLU B  57    13756   7679   7351   -973   -350   -567       C  
ATOM   5135  CG  GLU B  57      51.783  18.659  54.144  1.00 78.80           C  
ANISOU 5135  CG  GLU B  57    14317   7987   7635   -737   -200   -660       C  
ATOM   5136  CD  GLU B  57      51.982  18.644  55.620  1.00 77.11           C  
ANISOU 5136  CD  GLU B  57    13729   7920   7648   -583   -168   -662       C  
ATOM   5137  OE1 GLU B  57      52.999  18.114  56.131  1.00 78.52           O  
ANISOU 5137  OE1 GLU B  57    13870   8150   7813   -307     25   -742       O  
ATOM   5138  OE2 GLU B  57      51.088  19.175  56.262  1.00 77.41           O  
ANISOU 5138  OE2 GLU B  57    13511   8028   7872   -735   -343   -577       O  
ATOM   5139  N   SER B  58      48.861  21.655  52.309  1.00 73.73           N  
ANISOU 5139  N   SER B  58    13495   7353   7166  -1543   -894   -316       N  
ATOM   5140  CA  SER B  58      48.720  22.860  51.499  1.00 74.36           C  
ANISOU 5140  CA  SER B  58    13557   7448   7249  -1673   -987   -257       C  
ATOM   5141  C   SER B  58      47.456  23.632  51.820  1.00 73.25           C  
ANISOU 5141  C   SER B  58    13154   7363   7313  -1788  -1275   -122       C  
ATOM   5142  O   SER B  58      47.180  24.640  51.180  1.00 73.55           O  
ANISOU 5142  O   SER B  58    13197   7386   7364  -1887  -1408    -56       O  
ATOM   5143  CB  SER B  58      48.698  22.573  49.965  1.00 76.91           C  
ANISOU 5143  CB  SER B  58    14369   7579   7273  -1870  -1038   -247       C  
ATOM   5144  OG  SER B  58      49.415  21.405  49.568  1.00 82.96           O  
ANISOU 5144  OG  SER B  58    15504   8225   7791  -1784   -837   -356       O  
ATOM   5145  N   HIS B  59      46.708  23.177  52.814  1.00 72.46           N  
ANISOU 5145  N   HIS B  59    12829   7339   7365  -1761  -1367    -78       N  
ATOM   5146  CA  HIS B  59      45.436  23.760  53.173  1.00 72.44           C  
ANISOU 5146  CA  HIS B  59    12542   7435   7548  -1836  -1620     55       C  
ATOM   5147  C   HIS B  59      45.630  25.076  53.887  1.00 70.81           C  
ANISOU 5147  C   HIS B  59    11981   7362   7560  -1651  -1566     36       C  
ATOM   5148  O   HIS B  59      46.619  25.257  54.593  1.00 69.34           O  
ANISOU 5148  O   HIS B  59    11680   7238   7428  -1478  -1337    -70       O  
ATOM   5149  CB  HIS B  59      44.747  22.765  54.100  1.00 73.88           C  
ANISOU 5149  CB  HIS B  59    12593   7692   7787  -1867  -1675     92       C  
ATOM   5150  CG  HIS B  59      43.293  23.022  54.297  1.00 76.27           C  
ANISOU 5150  CG  HIS B  59    12634   8128   8217  -1998  -1947    255       C  
ATOM   5151  ND1 HIS B  59      42.799  23.632  55.430  1.00 76.40           N  
ANISOU 5151  ND1 HIS B  59    12198   8357   8474  -1846  -1940    278       N  
ATOM   5152  CD2 HIS B  59      42.223  22.748  53.508  1.00 79.51           C  
ANISOU 5152  CD2 HIS B  59    13156   8514   8538  -2262  -2231    411       C  
ATOM   5153  CE1 HIS B  59      41.485  23.744  55.317  1.00 80.66           C  
ANISOU 5153  CE1 HIS B  59    12545   9025   9076  -1981  -2193    441       C  
ATOM   5154  NE2 HIS B  59      41.108  23.193  54.174  1.00 79.84           N  
ANISOU 5154  NE2 HIS B  59    12764   8792   8781  -2250  -2387    534       N  
ATOM   5155  N   ALA B  60      44.706  26.015  53.685  1.00 71.02           N  
ANISOU 5155  N   ALA B  60    11858   7425   7700  -1684  -1789    146       N  
ATOM   5156  CA  ALA B  60      44.793  27.342  54.329  1.00 69.62           C  
ANISOU 5156  CA  ALA B  60    11417   7328   7707  -1494  -1768    130       C  
ATOM   5157  C   ALA B  60      44.941  27.248  55.841  1.00 68.10           C  
ANISOU 5157  C   ALA B  60    10907   7286   7682  -1300  -1607     61       C  
ATOM   5158  O   ALA B  60      44.126  26.620  56.536  1.00 67.36           O  
ANISOU 5158  O   ALA B  60    10615   7308   7671  -1299  -1658    106       O  
ATOM   5159  CB  ALA B  60      43.568  28.155  54.001  1.00 71.08           C  
ANISOU 5159  CB  ALA B  60    11478   7533   7994  -1506  -2056    267       C  
ATOM   5160  N   GLY B  61      45.977  27.898  56.349  1.00 66.67           N  
ANISOU 5160  N   GLY B  61    10686   7114   7533  -1167  -1423    -35       N  
ATOM   5161  CA  GLY B  61      46.209  27.956  57.771  1.00 64.07           C  
ANISOU 5161  CA  GLY B  61    10093   6906   7344   -997  -1279    -99       C  
ATOM   5162  C   GLY B  61      47.463  27.182  58.080  1.00 63.46           C  
ANISOU 5162  C   GLY B  61    10092   6840   7181   -977  -1044   -198       C  
ATOM   5163  O   GLY B  61      48.269  27.583  58.912  1.00 63.68           O  
ANISOU 5163  O   GLY B  61     9999   6931   7264   -867   -896   -262       O  
ATOM   5164  N   CYS B  62      47.651  26.069  57.403  1.00 63.34           N  
ANISOU 5164  N   CYS B  62    10294   6756   7015  -1075  -1017   -206       N  
ATOM   5165  CA  CYS B  62      48.613  25.079  57.842  1.00 62.87           C  
ANISOU 5165  CA  CYS B  62    10287   6714   6888   -998   -814   -292       C  
ATOM   5166  C   CYS B  62      50.106  25.563  57.783  1.00 62.35           C  
ANISOU 5166  C   CYS B  62    10224   6699   6766   -910   -601   -368       C  
ATOM   5167  O   CYS B  62      50.993  24.934  58.425  1.00 61.78           O  
ANISOU 5167  O   CYS B  62    10091   6695   6686   -786   -426   -432       O  
ATOM   5168  CB  CYS B  62      48.397  23.750  57.061  1.00 64.78           C  
ANISOU 5168  CB  CYS B  62    10839   6829   6946  -1106   -851   -286       C  
ATOM   5169  SG  CYS B  62      46.784  22.932  57.342  1.00 68.90           S  
ANISOU 5169  SG  CYS B  62    11337   7344   7499  -1272  -1096   -175       S  
ATOM   5170  N   GLU B  63      50.371  26.639  57.037  1.00 61.38           N  
ANISOU 5170  N   GLU B  63    10166   6558   6598   -986   -630   -346       N  
ATOM   5171  CA  GLU B  63      51.706  27.193  56.898  1.00 63.27           C  
ANISOU 5171  CA  GLU B  63    10393   6885   6760   -972   -453   -386       C  
ATOM   5172  C   GLU B  63      52.037  28.133  58.050  1.00 63.21           C  
ANISOU 5172  C   GLU B  63    10139   6981   6897   -908   -432   -387       C  
ATOM   5173  O   GLU B  63      53.145  28.647  58.121  1.00 64.93           O  
ANISOU 5173  O   GLU B  63    10307   7306   7059   -930   -307   -399       O  
ATOM   5174  CB  GLU B  63      51.849  27.995  55.585  1.00 64.92           C  
ANISOU 5174  CB  GLU B  63    10822   7025   6820  -1142   -512   -349       C  
ATOM   5175  CG  GLU B  63      51.187  29.447  55.625  1.00 67.38           C  
ANISOU 5175  CG  GLU B  63    11108   7270   7224  -1214   -722   -280       C  
ATOM   5176  CD  GLU B  63      49.613  29.491  55.513  1.00 71.47           C  
ANISOU 5176  CD  GLU B  63    11632   7673   7850  -1214   -984   -209       C  
ATOM   5177  OE1 GLU B  63      49.058  30.543  55.105  1.00 77.79           O  
ANISOU 5177  OE1 GLU B  63    12503   8383   8669  -1264  -1173   -145       O  
ATOM   5178  OE2 GLU B  63      48.912  28.496  55.781  1.00 69.98           O  
ANISOU 5178  OE2 GLU B  63    11385   7491   7712  -1176  -1019   -202       O  
ATOM   5179  N   LYS B  64      51.086  28.403  58.932  1.00 62.49           N  
ANISOU 5179  N   LYS B  64     9903   6871   6970   -846   -554   -367       N  
ATOM   5180  CA  LYS B  64      51.269  29.462  59.931  1.00 62.52           C  
ANISOU 5180  CA  LYS B  64     9755   6922   7079   -794   -559   -369       C  
ATOM   5181  C   LYS B  64      52.114  28.978  61.125  1.00 60.77           C  
ANISOU 5181  C   LYS B  64     9353   6832   6906   -703   -396   -415       C  
ATOM   5182  O   LYS B  64      52.078  27.829  61.453  1.00 61.05           O  
ANISOU 5182  O   LYS B  64     9342   6898   6955   -633   -333   -442       O  
ATOM   5183  CB  LYS B  64      49.898  29.898  60.412  1.00 63.09           C  
ANISOU 5183  CB  LYS B  64     9743   6938   7290   -721   -726   -338       C  
ATOM   5184  CG  LYS B  64      49.353  31.119  59.718  1.00 66.63           C  
ANISOU 5184  CG  LYS B  64    10321   7268   7726   -758   -903   -286       C  
ATOM   5185  CD  LYS B  64      47.908  31.257  60.011  1.00 68.44           C  
ANISOU 5185  CD  LYS B  64    10432   7484   8087   -645  -1060   -244       C  
ATOM   5186  CE  LYS B  64      47.253  32.080  58.912  1.00 72.61           C  
ANISOU 5186  CE  LYS B  64    11127   7882   8580   -688  -1275   -169       C  
ATOM   5187  NZ  LYS B  64      45.786  31.793  59.082  1.00 75.32           N  
ANISOU 5187  NZ  LYS B  64    11284   8287   9049   -585  -1419   -105       N  
ATOM   5188  N   SER B  65      52.876  29.837  61.765  1.00 59.70           N  
ANISOU 5188  N   SER B  65     9145   6761   6779   -721   -351   -415       N  
ATOM   5189  CA  SER B  65      53.673  29.391  62.925  1.00 58.85           C  
ANISOU 5189  CA  SER B  65     8862   6783   6714   -651   -227   -441       C  
ATOM   5190  C   SER B  65      52.802  29.034  64.124  1.00 56.71           C  
ANISOU 5190  C   SER B  65     8475   6492   6579   -541   -265   -464       C  
ATOM   5191  O   SER B  65      51.616  29.326  64.178  1.00 56.49           O  
ANISOU 5191  O   SER B  65     8458   6385   6622   -509   -376   -458       O  
ATOM   5192  CB  SER B  65      54.702  30.489  63.306  1.00 58.84           C  
ANISOU 5192  CB  SER B  65     8832   6862   6662   -758   -201   -411       C  
ATOM   5193  OG  SER B  65      54.096  31.470  64.091  1.00 58.97           O  
ANISOU 5193  OG  SER B  65     8878   6780   6746   -751   -310   -411       O  
ATOM   5194  N   LEU B  66      53.373  28.379  65.103  1.00 56.75           N  
ANISOU 5194  N   LEU B  66     8356   6590   6616   -481   -174   -484       N  
ATOM   5195  CA  LEU B  66      52.533  27.915  66.222  1.00 57.32           C  
ANISOU 5195  CA  LEU B  66     8336   6652   6789   -407   -199   -505       C  
ATOM   5196  C   LEU B  66      51.926  29.080  67.067  1.00 58.44           C  
ANISOU 5196  C   LEU B  66     8446   6759   6999   -391   -259   -512       C  
ATOM   5197  O   LEU B  66      50.710  29.145  67.258  1.00 59.91           O  
ANISOU 5197  O   LEU B  66     8599   6914   7251   -334   -321   -516       O  
ATOM   5198  CB  LEU B  66      53.287  26.869  67.043  1.00 56.01           C  
ANISOU 5198  CB  LEU B  66     8088   6569   6624   -351   -108   -519       C  
ATOM   5199  CG  LEU B  66      53.592  25.578  66.220  1.00 58.15           C  
ANISOU 5199  CG  LEU B  66     8452   6825   6818   -301    -59   -528       C  
ATOM   5200  CD1 LEU B  66      54.691  24.739  66.871  1.00 58.82           C  
ANISOU 5200  CD1 LEU B  66     8469   6997   6884   -200     34   -535       C  
ATOM   5201  CD2 LEU B  66      52.333  24.687  65.966  1.00 55.76           C  
ANISOU 5201  CD2 LEU B  66     8252   6420   6516   -318   -145   -529       C  
ATOM   5202  N   HIS B  67      52.763  30.026  67.499  1.00 58.62           N  
ANISOU 5202  N   HIS B  67     8494   6794   6986   -443   -243   -506       N  
ATOM   5203  CA  HIS B  67      52.285  31.237  68.142  1.00 59.75           C  
ANISOU 5203  CA  HIS B  67     8704   6852   7146   -420   -304   -521       C  
ATOM   5204  C   HIS B  67      51.155  31.879  67.389  1.00 60.77           C  
ANISOU 5204  C   HIS B  67     8920   6867   7300   -353   -412   -517       C  
ATOM   5205  O   HIS B  67      50.181  32.271  68.021  1.00 62.70           O  
ANISOU 5205  O   HIS B  67     9139   7077   7608   -224   -440   -544       O  
ATOM   5206  CB  HIS B  67      53.379  32.295  68.211  1.00 60.56           C  
ANISOU 5206  CB  HIS B  67     8923   6939   7149   -556   -322   -491       C  
ATOM   5207  CG  HIS B  67      54.601  31.866  68.945  1.00 60.58           C  
ANISOU 5207  CG  HIS B  67     8817   7083   7118   -641   -244   -466       C  
ATOM   5208  ND1 HIS B  67      55.864  32.343  68.629  1.00 63.98           N  
ANISOU 5208  ND1 HIS B  67     9262   7606   7441   -815   -239   -401       N  
ATOM   5209  CD2 HIS B  67      54.769  30.994  69.960  1.00 59.30           C  
ANISOU 5209  CD2 HIS B  67     8519   7005   7009   -586   -181   -480       C  
ATOM   5210  CE1 HIS B  67      56.755  31.800  69.444  1.00 61.76           C  
ANISOU 5210  CE1 HIS B  67     8829   7475   7161   -845   -181   -372       C  
ATOM   5211  NE2 HIS B  67      56.119  30.958  70.240  1.00 62.26           N  
ANISOU 5211  NE2 HIS B  67     8817   7517   7321   -700   -150   -423       N  
ATOM   5212  N   THR B  68      51.312  32.066  66.066  1.00 60.35           N  
ANISOU 5212  N   THR B  68     8977   6767   7188   -432   -473   -481       N  
ATOM   5213  CA  THR B  68      50.262  32.675  65.290  1.00 60.86           C  
ANISOU 5213  CA  THR B  68     9134   6718   7273   -373   -608   -460       C  
ATOM   5214  C   THR B  68      49.026  31.840  65.533  1.00 61.61           C  
ANISOU 5214  C   THR B  68     9054   6879   7475   -256   -620   -461       C  
ATOM   5215  O   THR B  68      48.025  32.356  65.960  1.00 63.36           O  
ANISOU 5215  O   THR B  68     9220   7087   7768   -112   -675   -466       O  
ATOM   5216  CB  THR B  68      50.594  32.748  63.760  1.00 62.19           C  
ANISOU 5216  CB  THR B  68     9454   6833   7342   -510   -673   -412       C  
ATOM   5217  OG1 THR B  68      51.697  33.635  63.526  1.00 63.89           O  
ANISOU 5217  OG1 THR B  68     9825   7015   7433   -659   -669   -394       O  
ATOM   5218  CG2 THR B  68      49.377  33.251  62.944  1.00 60.04           C  
ANISOU 5218  CG2 THR B  68     9268   6444   7102   -444   -850   -373       C  
ATOM   5219  N   LEU B  69      49.109  30.525  65.312  1.00 61.40           N  
ANISOU 5219  N   LEU B  69     8947   6936   7445   -317   -566   -453       N  
ATOM   5220  CA  LEU B  69      47.963  29.680  65.497  1.00 62.11           C  
ANISOU 5220  CA  LEU B  69     8896   7100   7604   -278   -600   -431       C  
ATOM   5221  C   LEU B  69      47.378  29.722  66.927  1.00 63.49           C  
ANISOU 5221  C   LEU B  69     8895   7368   7858   -168   -538   -463       C  
ATOM   5222  O   LEU B  69      46.149  29.843  67.048  1.00 64.42           O  
ANISOU 5222  O   LEU B  69     8879   7555   8042    -85   -598   -434       O  
ATOM   5223  CB  LEU B  69      48.268  28.257  65.017  1.00 62.75           C  
ANISOU 5223  CB  LEU B  69     9014   7206   7623   -386   -566   -419       C  
ATOM   5224  CG  LEU B  69      48.606  28.043  63.508  1.00 62.20           C  
ANISOU 5224  CG  LEU B  69     9138   7049   7446   -490   -617   -390       C  
ATOM   5225  CD1 LEU B  69      49.350  26.781  63.263  1.00 60.10           C  
ANISOU 5225  CD1 LEU B  69     8966   6783   7086   -535   -523   -414       C  
ATOM   5226  CD2 LEU B  69      47.432  28.195  62.501  1.00 62.22           C  
ANISOU 5226  CD2 LEU B  69     9188   7003   7449   -543   -797   -316       C  
ATOM   5227  N   PHE B  70      48.234  29.651  67.976  1.00 62.85           N  
ANISOU 5227  N   PHE B  70     8807   7309   7763   -169   -422   -514       N  
ATOM   5228  CA  PHE B  70      47.822  29.737  69.403  1.00 64.22           C  
ANISOU 5228  CA  PHE B  70     8864   7557   7980    -86   -346   -554       C  
ATOM   5229  C   PHE B  70      47.167  31.064  69.795  1.00 65.01           C  
ANISOU 5229  C   PHE B  70     8982   7612   8108     79   -366   -582       C  
ATOM   5230  O   PHE B  70      46.015  31.116  70.282  1.00 65.37           O  
ANISOU 5230  O   PHE B  70     8873   7756   8208    206   -351   -585       O  
ATOM   5231  CB  PHE B  70      49.035  29.507  70.361  1.00 64.61           C  
ANISOU 5231  CB  PHE B  70     8953   7611   7985   -147   -248   -589       C  
ATOM   5232  CG  PHE B  70      49.392  28.040  70.568  1.00 66.38           C  
ANISOU 5232  CG  PHE B  70     9124   7903   8194   -228   -207   -575       C  
ATOM   5233  CD1 PHE B  70      49.210  27.436  71.801  1.00 68.29           C  
ANISOU 5233  CD1 PHE B  70     9291   8215   8441   -239   -150   -593       C  
ATOM   5234  CD2 PHE B  70      49.902  27.264  69.510  1.00 65.16           C  
ANISOU 5234  CD2 PHE B  70     9039   7723   7997   -285   -230   -548       C  
ATOM   5235  CE1 PHE B  70      49.561  26.072  71.966  1.00 69.66           C  
ANISOU 5235  CE1 PHE B  70     9474   8411   8581   -309   -141   -575       C  
ATOM   5236  CE2 PHE B  70      50.253  25.927  69.675  1.00 62.34           C  
ANISOU 5236  CE2 PHE B  70     8698   7385   7604   -320   -203   -542       C  
ATOM   5237  CZ  PHE B  70      50.086  25.326  70.882  1.00 63.53           C  
ANISOU 5237  CZ  PHE B  70     8790   7584   7764   -332   -172   -552       C  
ATOM   5238  N   GLY B  71      47.918  32.143  69.575  1.00 64.98           N  
ANISOU 5238  N   GLY B  71     9177   7464   8048     78   -400   -599       N  
ATOM   5239  CA  GLY B  71      47.448  33.495  69.901  1.00 66.88           C  
ANISOU 5239  CA  GLY B  71     9542   7591   8278    249   -437   -635       C  
ATOM   5240  C   GLY B  71      46.163  33.913  69.183  1.00 68.27           C  
ANISOU 5240  C   GLY B  71     9654   7764   8521    428   -542   -603       C  
ATOM   5241  O   GLY B  71      45.446  34.817  69.647  1.00 70.14           O  
ANISOU 5241  O   GLY B  71     9923   7954   8771    660   -548   -639       O  
ATOM   5242  N   ASP B  72      45.915  33.306  68.022  1.00 67.20           N  
ANISOU 5242  N   ASP B  72     9454   7668   8412    331   -635   -531       N  
ATOM   5243  CA AASP B  72      44.650  33.459  67.306  0.18 69.01           C  
ANISOU 5243  CA AASP B  72     9565   7944   8711    459   -760   -468       C  
ATOM   5244  CA BASP B  72      44.655  33.475  67.309  0.82 68.99           C  
ANISOU 5244  CA BASP B  72     9565   7939   8708    460   -760   -469       C  
ATOM   5245  C   ASP B  72      43.484  32.997  68.188  1.00 70.16           C  
ANISOU 5245  C   ASP B  72     9400   8317   8940    601   -683   -465       C  
ATOM   5246  O   ASP B  72      42.437  33.652  68.245  1.00 72.69           O  
ANISOU 5246  O   ASP B  72     9605   8695   9319    841   -730   -448       O  
ATOM   5247  CB AASP B  72      44.692  32.654  66.002  0.18 68.17           C  
ANISOU 5247  CB AASP B  72     9465   7847   8587    260   -866   -387       C  
ATOM   5248  CB BASP B  72      44.701  32.759  65.937  0.82 67.50           C  
ANISOU 5248  CB BASP B  72     9400   7748   8501    266   -876   -386       C  
ATOM   5249  CG AASP B  72      43.390  32.717  65.226  0.18 70.36           C  
ANISOU 5249  CG AASP B  72     9610   8194   8931    341  -1030   -294       C  
ATOM   5250  CG BASP B  72      45.417  33.603  64.859  0.82 69.37           C  
ANISOU 5250  CG BASP B  72     9932   7775   8651    188   -989   -370       C  
ATOM   5251  OD1AASP B  72      43.061  31.716  64.550  0.18 70.65           O  
ANISOU 5251  OD1AASP B  72     9568   8316   8959    170  -1095   -219       O  
ATOM   5252  OD1BASP B  72      46.019  34.655  65.208  0.82 69.20           O  
ANISOU 5252  OD1BASP B  72    10107   7610   8574    238   -981   -417       O  
ATOM   5253  OD2AASP B  72      42.693  33.757  65.280  0.18 72.25           O  
ANISOU 5253  OD2AASP B  72     9838   8397   9217    578  -1108   -287       O  
ATOM   5254  OD2BASP B  72      45.382  33.243  63.645  0.82 72.58           O  
ANISOU 5254  OD2BASP B  72    10409   8149   9019     48  -1096   -305       O  
ATOM   5255  N   GLU B  73      43.690  31.893  68.903  1.00 68.14           N  
ANISOU 5255  N   GLU B  73     9014   8198   8677    461   -564   -479       N  
ATOM   5256  CA  GLU B  73      42.663  31.274  69.709  1.00 69.52           C  
ANISOU 5256  CA  GLU B  73     8896   8620   8897    508   -485   -460       C  
ATOM   5257  C   GLU B  73      42.334  31.946  71.061  1.00 70.66           C  
ANISOU 5257  C   GLU B  73     8978   8828   9043    729   -332   -545       C  
ATOM   5258  O   GLU B  73      41.229  31.789  71.611  1.00 72.54           O  
ANISOU 5258  O   GLU B  73     8941   9304   9318    847   -266   -525       O  
ATOM   5259  CB  GLU B  73      43.097  29.847  69.942  1.00 68.28           C  
ANISOU 5259  CB  GLU B  73     8706   8539   8699    249   -437   -441       C  
ATOM   5260  CG  GLU B  73      43.139  29.046  68.649  1.00 70.70           C  
ANISOU 5260  CG  GLU B  73     9072   8809   8981     54   -576   -356       C  
ATOM   5261  CD  GLU B  73      41.778  28.981  68.008  1.00 76.13           C  
ANISOU 5261  CD  GLU B  73     9552   9656   9719     67   -711   -246       C  
ATOM   5262  OE1 GLU B  73      40.816  28.629  68.733  1.00 80.35           O  
ANISOU 5262  OE1 GLU B  73     9815  10433  10280     81   -665   -208       O  
ATOM   5263  OE2 GLU B  73      41.650  29.336  66.805  1.00 79.16           O  
ANISOU 5263  OE2 GLU B  73    10029   9942  10105     57   -866   -188       O  
ATOM   5264  N   LEU B  74      43.329  32.631  71.615  1.00 69.63           N  
ANISOU 5264  N   LEU B  74     9106   8501   8847    757   -269   -635       N  
ATOM   5265  CA  LEU B  74      43.206  33.449  72.782  1.00 69.98           C  
ANISOU 5265  CA  LEU B  74     9223   8518   8851    960   -142   -728       C  
ATOM   5266  C   LEU B  74      42.335  34.616  72.367  1.00 73.33           C  
ANISOU 5266  C   LEU B  74     9667   8886   9308   1284   -211   -733       C  
ATOM   5267  O   LEU B  74      41.321  34.883  73.001  1.00 75.11           O  
ANISOU 5267  O   LEU B  74     9708   9272   9557   1539   -113   -759       O  
ATOM   5268  CB  LEU B  74      44.606  33.889  73.227  1.00 68.20           C  
ANISOU 5268  CB  LEU B  74     9322   8066   8525    837   -121   -791       C  
ATOM   5269  CG  LEU B  74      45.492  32.641  73.502  1.00 68.62           C  
ANISOU 5269  CG  LEU B  74     9322   8190   8561    548    -79   -766       C  
ATOM   5270  CD1 LEU B  74      47.023  32.846  73.582  1.00 66.36           C  
ANISOU 5270  CD1 LEU B  74     9277   7742   8194    369   -102   -777       C  
ATOM   5271  CD2 LEU B  74      45.022  31.871  74.763  1.00 70.17           C  
ANISOU 5271  CD2 LEU B  74     9343   8574   8746    529     67   -794       C  
ATOM   5272  N   CYS B  75      42.672  35.265  71.244  1.00 74.21           N  
ANISOU 5272  N   CYS B  75     9988   8792   9418   1282   -385   -697       N  
ATOM   5273  CA  CYS B  75      41.938  36.475  70.789  1.00 77.79           C  
ANISOU 5273  CA  CYS B  75    10539   9129   9889   1608   -493   -697       C  
ATOM   5274  C   CYS B  75      40.462  36.250  70.458  1.00 79.99           C  
ANISOU 5274  C   CYS B  75    10432   9676  10285   1823   -531   -618       C  
ATOM   5275  O   CYS B  75      39.725  37.210  70.226  1.00 82.04           O  
ANISOU 5275  O   CYS B  75    10716   9883  10571   2164   -606   -615       O  
ATOM   5276  CB  CYS B  75      42.678  37.199  69.659  1.00 76.83           C  
ANISOU 5276  CB  CYS B  75    10765   8716   9712   1506   -689   -665       C  
ATOM   5277  SG  CYS B  75      44.340  37.671  70.210  1.00 79.81           S  
ANISOU 5277  SG  CYS B  75    11561   8837   9928   1268   -642   -741       S  
ATOM   5278  N   LYS B  76      40.036  34.984  70.478  1.00 79.66           N  
ANISOU 5278  N   LYS B  76    10043   9926  10299   1624   -487   -544       N  
ATOM   5279  CA  LYS B  76      38.625  34.645  70.308  1.00 82.32           C  
ANISOU 5279  CA  LYS B  76     9954  10594  10730   1760   -515   -443       C  
ATOM   5280  C   LYS B  76      37.911  34.447  71.648  1.00 83.94           C  
ANISOU 5280  C   LYS B  76     9872  11092  10930   1921   -281   -493       C  
ATOM   5281  O   LYS B  76      36.686  34.434  71.710  1.00 86.01           O  
ANISOU 5281  O   LYS B  76     9754  11669  11257   2117   -263   -421       O  
ATOM   5282  CB  LYS B  76      38.501  33.403  69.443  1.00 81.52           C  
ANISOU 5282  CB  LYS B  76     9682  10637  10657   1402   -640   -310       C  
ATOM   5283  CG  LYS B  76      38.552  33.681  67.934  1.00 81.52           C  
ANISOU 5283  CG  LYS B  76     9830  10466  10678   1336   -896   -217       C  
ATOM   5284  CD  LYS B  76      38.866  32.391  67.101  1.00 82.83           C  
ANISOU 5284  CD  LYS B  76    10003  10659  10809    918   -996   -124       C  
ATOM   5285  CE  LYS B  76      37.962  31.157  67.397  1.00 82.82           C  
ANISOU 5285  CE  LYS B  76     9635  11013  10822    729   -977    -19       C  
ATOM   5286  NZ  LYS B  76      38.622  30.238  68.364  1.00 83.77           N  
ANISOU 5286  NZ  LYS B  76     9797  11158  10873    530   -795    -94       N  
ATOM   5287  N   VAL B  77      38.689  34.284  72.714  1.00 82.77           N  
ANISOU 5287  N   VAL B  77     9895  10859  10693   1823   -104   -605       N  
ATOM   5288  CA  VAL B  77      38.146  34.101  74.052  1.00 84.95           C  
ANISOU 5288  CA  VAL B  77     9968  11382  10928   1936    136   -667       C  
ATOM   5289  C   VAL B  77      37.313  35.348  74.270  1.00 89.34           C  
ANISOU 5289  C   VAL B  77    10493  11955  11497   2442    193   -722       C  
ATOM   5290  O   VAL B  77      37.859  36.442  74.439  1.00 90.32           O  
ANISOU 5290  O   VAL B  77    11015  11747  11554   2655    191   -831       O  
ATOM   5291  CB  VAL B  77      39.287  33.925  75.116  1.00 83.12           C  
ANISOU 5291  CB  VAL B  77    10033  10969  10578   1755    278   -784       C  
ATOM   5292  CG1 VAL B  77      38.756  33.825  76.550  1.00 84.63           C  
ANISOU 5292  CG1 VAL B  77    10078  11385  10694   1867    534   -859       C  
ATOM   5293  CG2 VAL B  77      40.172  32.674  74.784  1.00 79.93           C  
ANISOU 5293  CG2 VAL B  77     9672  10530  10168   1304    198   -722       C  
ATOM   5294  N   ALA B  78      35.989  35.197  74.192  1.00 92.65           N  
ANISOU 5294  N   ALA B  78    10450  12760  11993   2636    221   -632       N  
ATOM   5295  CA  ALA B  78      35.095  36.357  74.215  1.00 96.80           C  
ANISOU 5295  CA  ALA B  78    10895  13333  12551   3184    250   -663       C  
ATOM   5296  C   ALA B  78      35.065  37.023  75.587  1.00 98.62           C  
ANISOU 5296  C   ALA B  78    11274  13535  12661   3504    533   -837       C  
ATOM   5297  O   ALA B  78      34.400  38.039  75.756  1.00102.54           O  
ANISOU 5297  O   ALA B  78    11777  14030  13152   4018    595   -895       O  
ATOM   5298  CB  ALA B  78      33.672  35.993  73.740  1.00100.22           C  
ANISOU 5298  CB  ALA B  78    10728  14250  13102   3311    196   -495       C  
ATOM   5299  N   SER B  79      35.804  36.454  76.543  1.00 96.04           N  
ANISOU 5299  N   SER B  79    11100  13164  12226   3208    693   -918       N  
ATOM   5300  CA  SER B  79      35.988  37.044  77.872  1.00 97.54           C  
ANISOU 5300  CA  SER B  79    11541  13257  12263   3424    948  -1090       C  
ATOM   5301  C   SER B  79      37.430  37.535  78.182  1.00 95.36           C  
ANISOU 5301  C   SER B  79    11895  12477  11859   3251    898  -1205       C  
ATOM   5302  O   SER B  79      37.808  37.709  79.347  1.00 95.15           O  
ANISOU 5302  O   SER B  79    12107  12363  11682   3251   1085  -1328       O  
ATOM   5303  CB  SER B  79      35.506  36.059  78.943  1.00 98.07           C  
ANISOU 5303  CB  SER B  79    11251  13741  12271   3246   1198  -1085       C  
ATOM   5304  OG  SER B  79      34.096  36.088  79.053  1.00 99.95           O  
ANISOU 5304  OG  SER B  79    10971  14447  12558   3565   1333  -1028       O  
ATOM   5305  N   LEU B  80      38.222  37.782  77.136  1.00 93.84           N  
ANISOU 5305  N   LEU B  80    11970  11972  11712   3087    642  -1156       N  
ATOM   5306  CA  LEU B  80      39.624  38.212  77.305  1.00 91.96           C  
ANISOU 5306  CA  LEU B  80    12276  11313  11353   2863    565  -1227       C  
ATOM   5307  C   LEU B  80      39.806  39.579  78.008  1.00 94.42           C  
ANISOU 5307  C   LEU B  80    13089  11292  11493   3191    633  -1375       C  
ATOM   5308  O   LEU B  80      40.696  39.743  78.853  1.00 93.24           O  
ANISOU 5308  O   LEU B  80    13300  10936  11189   3009    695  -1456       O  
ATOM   5309  CB  LEU B  80      40.401  38.144  75.985  1.00 89.11           C  
ANISOU 5309  CB  LEU B  80    12050  10747  11060   2597    295  -1129       C  
ATOM   5310  CG  LEU B  80      41.912  38.345  76.166  1.00 89.25           C  
ANISOU 5310  CG  LEU B  80    12513  10441  10955   2275    227  -1165       C  
ATOM   5311  CD1 LEU B  80      42.647  37.068  76.648  1.00 86.82           C  
ANISOU 5311  CD1 LEU B  80    12051  10286  10650   1860    297  -1131       C  
ATOM   5312  CD2 LEU B  80      42.555  38.871  74.912  1.00 91.13           C  
ANISOU 5312  CD2 LEU B  80    13002  10419  11202   2162    -18  -1101       C  
ATOM   5313  N   ARG B  81      38.971  40.550  77.674  1.00 98.25           N  
ANISOU 5313  N   ARG B  81    13625  11714  11991   3671    605  -1406       N  
ATOM   5314  CA  ARG B  81      39.076  41.825  78.346  1.00102.10           C  
ANISOU 5314  CA  ARG B  81    14645  11860  12290   4013    668  -1554       C  
ATOM   5315  C   ARG B  81      38.661  41.679  79.816  1.00104.63           C  
ANISOU 5315  C   ARG B  81    14905  12363  12485   4172    995  -1678       C  
ATOM   5316  O   ARG B  81      39.483  41.844  80.708  1.00103.69           O  
ANISOU 5316  O   ARG B  81    15190  12022  12184   3978   1067  -1767       O  
ATOM   5317  CB  ARG B  81      38.249  42.902  77.635  1.00105.98           C  
ANISOU 5317  CB  ARG B  81    15235  12218  12815   4548    551  -1560       C  
ATOM   5318  CG  ARG B  81      38.360  44.306  78.280  1.00109.16           C  
ANISOU 5318  CG  ARG B  81    16301  12189  12987   4943    590  -1723       C  
ATOM   5319  CD  ARG B  81      38.197  45.392  77.244  1.00110.86           C  
ANISOU 5319  CD  ARG B  81    16854  12063  13203   5245    319  -1695       C  
ATOM   5320  NE  ARG B  81      39.194  45.202  76.196  1.00108.79           N  
ANISOU 5320  NE  ARG B  81    16744  11608  12982   4734     31  -1574       N  
ATOM   5321  CZ  ARG B  81      39.023  45.475  74.904  1.00109.43           C  
ANISOU 5321  CZ  ARG B  81    16813  11599  13168   4768   -236  -1463       C  
ATOM   5322  NH1 ARG B  81      37.876  45.991  74.458  1.00112.27           N  
ANISOU 5322  NH1 ARG B  81    17015  12025  13618   5311   -290  -1444       N  
ATOM   5323  NH2 ARG B  81      40.020  45.228  74.052  1.00106.04           N  
ANISOU 5323  NH2 ARG B  81    16524  11022  12743   4258   -451  -1363       N  
ATOM   5324  N   GLU B  82      37.399  41.306  80.027  1.00107.90           N  
ANISOU 5324  N   GLU B  82    14787  13219  12992   4478   1184  -1663       N  
ATOM   5325  CA  GLU B  82      36.724  41.303  81.321  1.00111.70           C  
ANISOU 5325  CA  GLU B  82    15155  13937  13348   4743   1527  -1781       C  
ATOM   5326  C   GLU B  82      37.541  40.707  82.430  1.00109.58           C  
ANISOU 5326  C   GLU B  82    15074  13633  12930   4323   1666  -1841       C  
ATOM   5327  O   GLU B  82      37.375  41.053  83.598  1.00112.40           O  
ANISOU 5327  O   GLU B  82    15640  13974  13095   4508   1916  -1980       O  
ATOM   5328  CB  GLU B  82      35.422  40.509  81.234  1.00113.81           C  
ANISOU 5328  CB  GLU B  82    14652  14820  13769   4885   1676  -1682       C  
ATOM   5329  CG  GLU B  82      34.463  40.994  80.154  1.00118.01           C  
ANISOU 5329  CG  GLU B  82    14887  15482  14469   5311   1532  -1591       C  
ATOM   5330  CD  GLU B  82      34.617  40.215  78.851  1.00115.57           C  
ANISOU 5330  CD  GLU B  82    14280  15267  14364   4916   1235  -1393       C  
ATOM   5331  OE1 GLU B  82      35.716  40.236  78.238  1.00111.64           O  
ANISOU 5331  OE1 GLU B  82    14164  14387  13866   4567   1002  -1370       O  
ATOM   5332  OE2 GLU B  82      33.624  39.577  78.443  1.00117.37           O  
ANISOU 5332  OE2 GLU B  82    13889  15970  14737   4946   1239  -1254       O  
ATOM   5333  N   THR B  83      38.441  39.818  82.059  1.00105.12           N  
ANISOU 5333  N   THR B  83    14456  13045  12440   3768   1500  -1735       N  
ATOM   5334  CA  THR B  83      39.067  38.967  83.036  1.00103.06           C  
ANISOU 5334  CA  THR B  83    14218  12858  12081   3351   1614  -1749       C  
ATOM   5335  C   THR B  83      40.569  39.213  83.228  1.00100.49           C  
ANISOU 5335  C   THR B  83    14443  12105  11635   2986   1452  -1770       C  
ATOM   5336  O   THR B  83      41.096  39.001  84.322  1.00100.08           O  
ANISOU 5336  O   THR B  83    14606  11998  11423   2775   1564  -1829       O  
ATOM   5337  CB  THR B  83      38.766  37.515  82.656  1.00100.84           C  
ANISOU 5337  CB  THR B  83    13357  12989  11968   3012   1591  -1600       C  
ATOM   5338  OG1 THR B  83      37.346  37.387  82.476  1.00104.09           O  
ANISOU 5338  OG1 THR B  83    13254  13825  12473   3333   1723  -1560       O  
ATOM   5339  CG2 THR B  83      39.284  36.501  83.707  1.00 98.38           C  
ANISOU 5339  CG2 THR B  83    13036  12790  11555   2591   1707  -1602       C  
ATOM   5340  N   TYR B  84      41.252  39.680  82.185  1.00 98.99           N  
ANISOU 5340  N   TYR B  84    14476  11631  11505   2897   1186  -1710       N  
ATOM   5341  CA  TYR B  84      42.710  39.685  82.202  1.00 95.65           C  
ANISOU 5341  CA  TYR B  84    14428  10916  10999   2467   1012  -1678       C  
ATOM   5342  C   TYR B  84      43.334  41.069  82.103  1.00 97.74           C  
ANISOU 5342  C   TYR B  84    15331  10716  11091   2559    869  -1739       C  
ATOM   5343  O   TYR B  84      44.535  41.207  82.365  1.00 96.74           O  
ANISOU 5343  O   TYR B  84    15555  10361  10840   2197    748  -1716       O  
ATOM   5344  CB  TYR B  84      43.251  38.742  81.134  1.00 91.23           C  
ANISOU 5344  CB  TYR B  84    13562  10474  10625   2114    824  -1526       C  
ATOM   5345  CG  TYR B  84      42.926  37.293  81.400  1.00 87.86           C  
ANISOU 5345  CG  TYR B  84    12651  10428  10306   1906    930  -1461       C  
ATOM   5346  CD1 TYR B  84      43.773  36.494  82.190  1.00 84.21           C  
ANISOU 5346  CD1 TYR B  84    12233   9987   9775   1537    955  -1444       C  
ATOM   5347  CD2 TYR B  84      41.769  36.718  80.879  1.00 87.35           C  
ANISOU 5347  CD2 TYR B  84    12101  10695  10392   2060    982  -1404       C  
ATOM   5348  CE1 TYR B  84      43.459  35.185  82.463  1.00 82.53           C  
ANISOU 5348  CE1 TYR B  84    11645  10081   9631   1346   1033  -1385       C  
ATOM   5349  CE2 TYR B  84      41.449  35.395  81.127  1.00 85.97           C  
ANISOU 5349  CE2 TYR B  84    11535  10850  10280   1828   1056  -1333       C  
ATOM   5350  CZ  TYR B  84      42.295  34.624  81.919  1.00 84.79           C  
ANISOU 5350  CZ  TYR B  84    11485  10682  10051   1475   1082  -1329       C  
ATOM   5351  OH  TYR B  84      41.964  33.294  82.157  1.00 85.57           O  
ANISOU 5351  OH  TYR B  84    11250  11074  10188   1235   1132  -1255       O  
ATOM   5352  N   GLY B  85      42.525  42.067  81.723  1.00101.08           N  
ANISOU 5352  N   GLY B  85    15901  11007  11497   3031    866  -1803       N  
ATOM   5353  CA  GLY B  85      42.892  43.501  81.799  1.00104.24           C  
ANISOU 5353  CA  GLY B  85    17001  10926  11679   3206    754  -1889       C  
ATOM   5354  C   GLY B  85      43.493  44.239  80.593  1.00104.16           C  
ANISOU 5354  C   GLY B  85    17309  10597  11672   3103    440  -1809       C  
ATOM   5355  O   GLY B  85      42.890  45.180  80.054  1.00107.02           O  
ANISOU 5355  O   GLY B  85    17893  10758  12012   3504    356  -1845       O  
ATOM   5356  N   ASP B  86      44.695  43.814  80.195  1.00100.93           N  
ANISOU 5356  N   ASP B  86    16927  10149  11275   2567    268  -1696       N  
ATOM   5357  CA  ASP B  86      45.565  44.526  79.256  1.00100.22           C  
ANISOU 5357  CA  ASP B  86    17218   9750  11112   2330    -19  -1614       C  
ATOM   5358  C   ASP B  86      46.085  43.458  78.340  1.00 96.18           C  
ANISOU 5358  C   ASP B  86    16233   9508  10804   1961   -107  -1468       C  
ATOM   5359  O   ASP B  86      46.543  43.729  77.235  1.00 95.65           O  
ANISOU 5359  O   ASP B  86    16252   9330  10759   1796   -314  -1377       O  
ATOM   5360  CB  ASP B  86      46.763  45.171  79.971  1.00101.16           C  
ANISOU 5360  CB  ASP B  86    17941   9548  10949   1974   -118  -1624       C  
ATOM   5361  CG  ASP B  86      46.421  45.717  81.385  1.00105.36           C  
ANISOU 5361  CG  ASP B  86    18871   9909  11254   2211     61  -1781       C  
ATOM   5362  OD1 ASP B  86      46.312  44.896  82.338  1.00104.53           O  
ANISOU 5362  OD1 ASP B  86    18487  10056  11175   2150    272  -1818       O  
ATOM   5363  OD2 ASP B  86      46.305  46.967  81.541  1.00108.62           O  
ANISOU 5363  OD2 ASP B  86    19922   9912  11436   2439    -18  -1866       O  
ATOM   5364  N   MET B  87      46.063  42.234  78.853  1.00 93.24           N  
ANISOU 5364  N   MET B  87    15403   9473  10550   1816     55  -1450       N  
ATOM   5365  CA  MET B  87      46.009  41.061  78.031  1.00 89.64           C  
ANISOU 5365  CA  MET B  87    14412   9329  10320   1655     38  -1345       C  
ATOM   5366  C   MET B  87      45.167  41.370  76.815  1.00 89.76           C  
ANISOU 5366  C   MET B  87    14292   9348  10464   1923    -67  -1307       C  
ATOM   5367  O   MET B  87      45.599  41.148  75.690  1.00 88.45           O  
ANISOU 5367  O   MET B  87    14048   9184  10374   1717   -227  -1206       O  
ATOM   5368  CB  MET B  87      45.300  39.980  78.820  1.00 89.73           C  
ANISOU 5368  CB  MET B  87    13982   9682  10430   1728    263  -1374       C  
ATOM   5369  CG  MET B  87      46.189  39.232  79.779  1.00 89.11           C  
ANISOU 5369  CG  MET B  87    13897   9678  10283   1377    332  -1364       C  
ATOM   5370  SD  MET B  87      46.791  37.805  78.893  1.00 87.97           S  
ANISOU 5370  SD  MET B  87    13322   9780  10324   1028    245  -1223       S  
ATOM   5371  CE  MET B  87      45.464  36.623  79.000  1.00 84.83           C  
ANISOU 5371  CE  MET B  87    12386   9759  10087   1184    408  -1218       C  
ATOM   5372  N   ALA B  88      43.962  41.889  77.073  1.00 91.52           N  
ANISOU 5372  N   ALA B  88    14489   9583  10699   2396     28  -1387       N  
ATOM   5373  CA  ALA B  88      42.996  42.315  76.062  1.00 92.03           C  
ANISOU 5373  CA  ALA B  88    14434   9654  10878   2738    -78  -1353       C  
ATOM   5374  C   ALA B  88      43.633  43.035  74.880  1.00 90.60           C  
ANISOU 5374  C   ALA B  88    14602   9170  10652   2590   -357  -1280       C  
ATOM   5375  O   ALA B  88      43.212  42.891  73.728  1.00 89.72           O  
ANISOU 5375  O   ALA B  88    14287   9130  10674   2632   -496  -1190       O  
ATOM   5376  CB  ALA B  88      41.918  43.206  76.704  1.00 95.99           C  
ANISOU 5376  CB  ALA B  88    15073  10088  11312   3309     46  -1473       C  
ATOM   5377  N   ASP B  89      44.672  43.796  75.178  1.00 89.31           N  
ANISOU 5377  N   ASP B  89    14978   8677  10279   2372   -448  -1307       N  
ATOM   5378  CA  ASP B  89      45.283  44.612  74.171  1.00 88.43           C  
ANISOU 5378  CA  ASP B  89    15266   8262  10071   2210   -710  -1240       C  
ATOM   5379  C   ASP B  89      46.323  43.881  73.384  1.00 84.45           C  
ANISOU 5379  C   ASP B  89    14588   7884   9615   1700   -802  -1116       C  
ATOM   5380  O   ASP B  89      46.491  44.190  72.235  1.00 85.07           O  
ANISOU 5380  O   ASP B  89    14769   7858   9695   1599   -990  -1036       O  
ATOM   5381  CB  ASP B  89      45.805  45.887  74.792  1.00 90.84           C  
ANISOU 5381  CB  ASP B  89    16281   8141  10094   2220   -793  -1313       C  
ATOM   5382  CG  ASP B  89      44.723  46.613  75.568  1.00 93.55           C  
ANISOU 5382  CG  ASP B  89    16825   8348  10373   2801   -674  -1455       C  
ATOM   5383  OD1 ASP B  89      43.575  46.107  75.702  1.00 90.97           O  
ANISOU 5383  OD1 ASP B  89    16023   8314  10228   3189   -505  -1491       O  
ATOM   5384  OD2 ASP B  89      45.018  47.712  76.039  1.00 97.98           O  
ANISOU 5384  OD2 ASP B  89    18037   8510  10680   2871   -751  -1528       O  
ATOM   5385  N   CYS B  90      46.993  42.891  73.966  1.00 81.46           N  
ANISOU 5385  N   CYS B  90    13943   7737   9271   1402   -669  -1099       N  
ATOM   5386  CA  CYS B  90      47.945  42.063  73.185  1.00 78.50           C  
ANISOU 5386  CA  CYS B  90    13341   7528   8956    980   -727   -985       C  
ATOM   5387  C   CYS B  90      47.392  41.707  71.780  1.00 76.55           C  
ANISOU 5387  C   CYS B  90    12845   7381   8861   1039   -825   -909       C  
ATOM   5388  O   CYS B  90      48.127  41.778  70.806  1.00 74.58           O  
ANISOU 5388  O   CYS B  90    12690   7081   8567    762   -957   -825       O  
ATOM   5389  CB  CYS B  90      48.369  40.764  73.911  1.00 76.15           C  
ANISOU 5389  CB  CYS B  90    12660   7529   8743    786   -554   -977       C  
ATOM   5390  SG  CYS B  90      49.141  40.936  75.517  1.00 78.88           S  
ANISOU 5390  SG  CYS B  90    13243   7808   8918    628   -458  -1034       S  
ATOM   5391  N   CYS B  91      46.108  41.352  71.710  1.00 76.41           N  
ANISOU 5391  N   CYS B  91    12516   7516   9001   1379   -762   -932       N  
ATOM   5392  CA  CYS B  91      45.392  41.145  70.435  1.00 77.70           C  
ANISOU 5392  CA  CYS B  91    12479   7751   9293   1471   -886   -853       C  
ATOM   5393  C   CYS B  91      45.391  42.264  69.353  1.00 78.65           C  
ANISOU 5393  C   CYS B  91    12983   7574   9328   1516  -1133   -806       C  
ATOM   5394  O   CYS B  91      45.116  41.975  68.218  1.00 78.15           O  
ANISOU 5394  O   CYS B  91    12784   7568   9343   1461  -1253   -721       O  
ATOM   5395  CB  CYS B  91      43.961  40.675  70.702  1.00 78.81           C  
ANISOU 5395  CB  CYS B  91    12211   8137   9596   1829   -786   -869       C  
ATOM   5396  SG  CYS B  91      43.963  39.144  71.647  1.00 82.69           S  
ANISOU 5396  SG  CYS B  91    12241   8999  10179   1667   -544   -883       S  
ATOM   5397  N   GLU B  92      45.692  43.517  69.698  1.00 80.15           N  
ANISOU 5397  N   GLU B  92    13688   7430   9337   1594  -1223   -857       N  
ATOM   5398  CA  GLU B  92      45.781  44.575  68.703  1.00 81.60           C  
ANISOU 5398  CA  GLU B  92    14302   7299   9405   1587  -1480   -805       C  
ATOM   5399  C   GLU B  92      47.191  44.600  68.046  1.00 79.24           C  
ANISOU 5399  C   GLU B  92    14220   6930   8958   1041  -1582   -720       C  
ATOM   5400  O   GLU B  92      47.621  45.611  67.507  1.00 80.91           O  
ANISOU 5400  O   GLU B  92    14912   6842   8986    909  -1784   -681       O  
ATOM   5401  CB  GLU B  92      45.381  45.948  69.344  1.00 86.28           C  
ANISOU 5401  CB  GLU B  92    15417   7526   9840   1946  -1553   -897       C  
ATOM   5402  CG  GLU B  92      44.755  47.029  68.413  1.00 88.80           C  
ANISOU 5402  CG  GLU B  92    16102   7531  10105   2216  -1820   -862       C  
ATOM   5403  CD  GLU B  92      44.769  48.467  68.986  1.00 96.71           C  
ANISOU 5403  CD  GLU B  92    17807   8071  10865   2456  -1932   -947       C  
ATOM   5404  OE1 GLU B  92      45.547  48.765  69.917  1.00 98.26           O  
ANISOU 5404  OE1 GLU B  92    18324   8132  10878   2264  -1857  -1010       O  
ATOM   5405  OE2 GLU B  92      43.991  49.328  68.507  1.00100.10           O  
ANISOU 5405  OE2 GLU B  92    18512   8249  11272   2847  -2114   -949       O  
ATOM   5406  N   LYS B  93      47.895  43.476  68.049  1.00 75.84           N  
ANISOU 5406  N   LYS B  93    13432   6788   8595    729  -1444   -683       N  
ATOM   5407  CA  LYS B  93      49.308  43.474  67.653  1.00 74.17           C  
ANISOU 5407  CA  LYS B  93    13368   6580   8233    241  -1487   -609       C  
ATOM   5408  C   LYS B  93      49.719  42.393  66.666  1.00 72.21           C  
ANISOU 5408  C   LYS B  93    12767   6595   8074     -5  -1441   -530       C  
ATOM   5409  O   LYS B  93      49.000  41.422  66.389  1.00 70.12           O  
ANISOU 5409  O   LYS B  93    12117   6531   7993    146  -1362   -532       O  
ATOM   5410  CB  LYS B  93      50.179  43.219  68.874  1.00 73.88           C  
ANISOU 5410  CB  LYS B  93    13307   6637   8129     58  -1342   -642       C  
ATOM   5411  CG  LYS B  93      50.424  44.307  69.870  1.00 73.76           C  
ANISOU 5411  CG  LYS B  93    13763   6346   7917     76  -1395   -695       C  
ATOM   5412  CD  LYS B  93      51.315  43.683  70.881  1.00 73.11           C  
ANISOU 5412  CD  LYS B  93    13513   6454   7810   -167  -1250   -694       C  
ATOM   5413  CE  LYS B  93      52.476  44.549  71.291  1.00 77.67           C  
ANISOU 5413  CE  LYS B  93    14531   6862   8121   -543  -1370   -640       C  
ATOM   5414  NZ  LYS B  93      52.126  45.552  72.374  1.00 79.13           N  
ANISOU 5414  NZ  LYS B  93    15206   6722   8137   -362  -1408   -734       N  
ATOM   5415  N   GLN B  94      50.943  42.547  66.194  1.00 72.37           N  
ANISOU 5415  N   GLN B  94    12931   6626   7938   -408  -1483   -456       N  
ATOM   5416  CA  GLN B  94      51.533  41.627  65.225  1.00 71.13           C  
ANISOU 5416  CA  GLN B  94    12510   6705   7810   -655  -1422   -387       C  
ATOM   5417  C   GLN B  94      52.455  40.681  65.946  1.00 69.24           C  
ANISOU 5417  C   GLN B  94    11966   6740   7601   -818  -1227   -389       C  
ATOM   5418  O   GLN B  94      53.088  41.094  66.917  1.00 71.04           O  
ANISOU 5418  O   GLN B  94    12316   6941   7735   -927  -1208   -396       O  
ATOM   5419  CB  GLN B  94      52.342  42.426  64.218  1.00 72.54           C  
ANISOU 5419  CB  GLN B  94    13024   6765   7773   -999  -1575   -295       C  
ATOM   5420  CG  GLN B  94      51.525  43.305  63.290  1.00 75.49           C  
ANISOU 5420  CG  GLN B  94    13729   6856   8097   -880  -1803   -271       C  
ATOM   5421  CD  GLN B  94      52.432  44.005  62.307  1.00 81.65           C  
ANISOU 5421  CD  GLN B  94    14846   7545   8634  -1292  -1944   -170       C  
ATOM   5422  OE1 GLN B  94      53.563  43.537  62.093  1.00 82.90           O  
ANISOU 5422  OE1 GLN B  94    14848   7946   8705  -1636  -1826   -115       O  
ATOM   5423  NE2 GLN B  94      51.968  45.127  61.703  1.00 79.00           N  
ANISOU 5423  NE2 GLN B  94    14971   6874   8173  -1261  -2198   -138       N  
ATOM   5424  N   GLU B  95      52.492  39.411  65.532  1.00 67.85           N  
ANISOU 5424  N   GLU B  95    11422   6809   7547   -818  -1096   -382       N  
ATOM   5425  CA  GLU B  95      53.518  38.474  65.984  1.00 66.53           C  
ANISOU 5425  CA  GLU B  95    10985   6903   7390   -977   -931   -366       C  
ATOM   5426  C   GLU B  95      54.837  39.011  65.420  1.00 68.58           C  
ANISOU 5426  C   GLU B  95    11388   7219   7450  -1343   -969   -273       C  
ATOM   5427  O   GLU B  95      54.846  39.635  64.349  1.00 70.42           O  
ANISOU 5427  O   GLU B  95    11843   7343   7570  -1474  -1085   -225       O  
ATOM   5428  CB  GLU B  95      53.267  37.083  65.395  1.00 65.42           C  
ANISOU 5428  CB  GLU B  95    10526   6953   7378   -895   -815   -374       C  
ATOM   5429  CG  GLU B  95      52.224  36.151  66.106  1.00 65.07           C  
ANISOU 5429  CG  GLU B  95    10237   6967   7518   -625   -736   -441       C  
ATOM   5430  CD  GLU B  95      52.382  35.983  67.663  1.00 70.27           C  
ANISOU 5430  CD  GLU B  95    10799   7683   8218   -559   -642   -488       C  
ATOM   5431  OE1 GLU B  95      51.437  35.383  68.267  1.00 69.41           O  
ANISOU 5431  OE1 GLU B  95    10525   7615   8232   -358   -587   -539       O  
ATOM   5432  OE2 GLU B  95      53.411  36.444  68.284  1.00 69.88           O  
ANISOU 5432  OE2 GLU B  95    10841   7647   8064   -730   -633   -465       O  
ATOM   5433  N   PRO B  96      55.964  38.830  66.125  1.00 68.55           N  
ANISOU 5433  N   PRO B  96    11265   7397   7382  -1535   -889   -232       N  
ATOM   5434  CA  PRO B  96      56.262  38.243  67.420  1.00 67.31           C  
ANISOU 5434  CA  PRO B  96    10902   7369   7304  -1473   -785   -258       C  
ATOM   5435  C   PRO B  96      55.816  39.058  68.614  1.00 67.58           C  
ANISOU 5435  C   PRO B  96    11181   7189   7309  -1392   -861   -308       C  
ATOM   5436  O   PRO B  96      55.786  38.513  69.721  1.00 66.52           O  
ANISOU 5436  O   PRO B  96    10892   7129   7253  -1295   -774   -349       O  
ATOM   5437  CB  PRO B  96      57.796  38.186  67.420  1.00 67.71           C  
ANISOU 5437  CB  PRO B  96    10830   7673   7223  -1800   -746   -148       C  
ATOM   5438  CG  PRO B  96      58.210  39.353  66.611  1.00 69.48           C  
ANISOU 5438  CG  PRO B  96    11366   7795   7239  -2089   -887    -67       C  
ATOM   5439  CD  PRO B  96      57.201  39.295  65.469  1.00 70.34           C  
ANISOU 5439  CD  PRO B  96    11566   7749   7410  -1909   -918   -120       C  
ATOM   5440  N   GLU B  97      55.501  40.347  68.442  1.00 69.08           N  
ANISOU 5440  N   GLU B  97    11785   7099   7365  -1430  -1023   -308       N  
ATOM   5441  CA  GLU B  97      55.259  41.165  69.654  1.00 69.93           C  
ANISOU 5441  CA  GLU B  97    12191   6988   7392  -1367  -1083   -359       C  
ATOM   5442  C   GLU B  97      54.022  40.663  70.418  1.00 67.74           C  
ANISOU 5442  C   GLU B  97    11769   6672   7296   -958   -976   -483       C  
ATOM   5443  O   GLU B  97      53.945  40.792  71.598  1.00 66.76           O  
ANISOU 5443  O   GLU B  97    11724   6495   7148   -894   -934   -535       O  
ATOM   5444  CB  GLU B  97      55.142  42.678  69.381  1.00 72.79           C  
ANISOU 5444  CB  GLU B  97    13107   7005   7545  -1455  -1292   -343       C  
ATOM   5445  CG  GLU B  97      56.351  43.363  68.735  1.00 77.26           C  
ANISOU 5445  CG  GLU B  97    13892   7590   7872  -1929  -1427   -205       C  
ATOM   5446  CD  GLU B  97      56.393  43.246  67.175  1.00 83.44           C  
ANISOU 5446  CD  GLU B  97    14605   8445   8652  -2028  -1461   -144       C  
ATOM   5447  OE1 GLU B  97      55.424  42.764  66.508  1.00 80.74           O  
ANISOU 5447  OE1 GLU B  97    14116   8080   8479  -1731  -1423   -206       O  
ATOM   5448  OE2 GLU B  97      57.451  43.610  66.622  1.00 86.72           O  
ANISOU 5448  OE2 GLU B  97    15103   8969   8876  -2441  -1525    -22       O  
ATOM   5449  N   ARG B  98      53.052  40.098  69.729  1.00 66.49           N  
ANISOU 5449  N   ARG B  98    11406   6556   7302   -710   -936   -521       N  
ATOM   5450  CA  ARG B  98      51.870  39.648  70.394  1.00 66.71           C  
ANISOU 5450  CA  ARG B  98    11266   6599   7483   -364   -839   -614       C  
ATOM   5451  C   ARG B  98      52.204  38.604  71.479  1.00 67.12           C  
ANISOU 5451  C   ARG B  98    11032   6863   7606   -394   -679   -636       C  
ATOM   5452  O   ARG B  98      51.870  38.790  72.675  1.00 68.46           O  
ANISOU 5452  O   ARG B  98    11276   6978   7758   -273   -618   -705       O  
ATOM   5453  CB  ARG B  98      50.986  39.048  69.374  1.00 65.32           C  
ANISOU 5453  CB  ARG B  98    10864   6499   7453   -199   -842   -608       C  
ATOM   5454  CG  ARG B  98      49.550  38.989  69.713  1.00 64.96           C  
ANISOU 5454  CG  ARG B  98    10706   6441   7535    163   -809   -675       C  
ATOM   5455  CD  ARG B  98      49.192  37.670  69.184  1.00 67.76           C  
ANISOU 5455  CD  ARG B  98    10681   7028   8036    161   -740   -645       C  
ATOM   5456  NE  ARG B  98      48.092  37.640  68.245  1.00 69.54           N  
ANISOU 5456  NE  ARG B  98    10819   7250   8354    332   -830   -618       N  
ATOM   5457  CZ  ARG B  98      47.847  36.605  67.459  1.00 64.14           C  
ANISOU 5457  CZ  ARG B  98     9899   6718   7751    262   -826   -569       C  
ATOM   5458  NH1 ARG B  98      48.657  35.560  67.478  1.00 59.01           N  
ANISOU 5458  NH1 ARG B  98     9111   6212   7099     63   -726   -555       N  
ATOM   5459  NH2 ARG B  98      46.814  36.647  66.642  1.00 63.74           N  
ANISOU 5459  NH2 ARG B  98     9783   6663   7771    395   -938   -527       N  
ATOM   5460  N   ASN B  99      52.862  37.526  71.056  1.00 66.00           N  
ANISOU 5460  N   ASN B  99    10600   6949   7529   -543   -614   -580       N  
ATOM   5461  CA  ASN B  99      53.270  36.424  71.915  1.00 65.13           C  
ANISOU 5461  CA  ASN B  99    10227   7037   7484   -578   -491   -583       C  
ATOM   5462  C   ASN B  99      54.082  36.928  73.039  1.00 66.22           C  
ANISOU 5462  C   ASN B  99    10523   7138   7499   -740   -507   -569       C  
ATOM   5463  O   ASN B  99      53.911  36.464  74.160  1.00 66.25           O  
ANISOU 5463  O   ASN B  99    10449   7188   7534   -678   -428   -611       O  
ATOM   5464  CB  ASN B  99      54.094  35.377  71.119  1.00 65.23           C  
ANISOU 5464  CB  ASN B  99     9988   7261   7537   -712   -445   -515       C  
ATOM   5465  CG  ASN B  99      54.355  34.090  71.916  1.00 64.64           C  
ANISOU 5465  CG  ASN B  99     9653   7364   7545   -684   -335   -521       C  
ATOM   5466  OD1 ASN B  99      53.416  33.485  72.454  1.00 64.80           O  
ANISOU 5466  OD1 ASN B  99     9574   7389   7657   -517   -278   -580       O  
ATOM   5467  ND2 ASN B  99      55.623  33.687  72.010  1.00 61.55           N  
ANISOU 5467  ND2 ASN B  99     9150   7129   7108   -850   -315   -450       N  
ATOM   5468  N   GLU B 100      54.963  37.899  72.769  1.00 67.97           N  
ANISOU 5468  N   GLU B 100    10993   7275   7556   -984   -622   -500       N  
ATOM   5469  CA  GLU B 100      55.737  38.534  73.864  1.00 69.52           C  
ANISOU 5469  CA  GLU B 100    11410   7410   7594  -1193   -679   -468       C  
ATOM   5470  C   GLU B 100      54.856  39.122  74.971  1.00 69.70           C  
ANISOU 5470  C   GLU B 100    11702   7208   7572   -995   -662   -578       C  
ATOM   5471  O   GLU B 100      55.061  38.884  76.150  1.00 69.47           O  
ANISOU 5471  O   GLU B 100    11678   7207   7510  -1036   -614   -596       O  
ATOM   5472  CB  GLU B 100      56.695  39.611  73.335  1.00 71.54           C  
ANISOU 5472  CB  GLU B 100    11949   7590   7644  -1526   -836   -363       C  
ATOM   5473  CG  GLU B 100      57.986  39.046  72.716  1.00 74.66           C  
ANISOU 5473  CG  GLU B 100    12050   8296   8024  -1809   -827   -227       C  
ATOM   5474  CD  GLU B 100      58.639  37.984  73.608  1.00 78.31           C  
ANISOU 5474  CD  GLU B 100    12176   9012   8566  -1838   -736   -190       C  
ATOM   5475  OE1 GLU B 100      58.883  38.292  74.791  1.00 84.19           O  
ANISOU 5475  OE1 GLU B 100    13068   9694   9226  -1941   -785   -181       O  
ATOM   5476  OE2 GLU B 100      58.900  36.848  73.150  1.00 75.80           O  
ANISOU 5476  OE2 GLU B 100    11485   8934   8380  -1752   -628   -171       O  
ATOM   5477  N   CYS B 101      53.872  39.879  74.533  1.00 70.47           N  
ANISOU 5477  N   CYS B 101    12022   7091   7663   -765   -700   -650       N  
ATOM   5478  CA  CYS B 101      52.918  40.543  75.344  1.00 72.34           C  
ANISOU 5478  CA  CYS B 101    12524   7111   7851   -495   -669   -765       C  
ATOM   5479  C   CYS B 101      52.127  39.525  76.134  1.00 71.30           C  
ANISOU 5479  C   CYS B 101    12066   7153   7872   -265   -484   -843       C  
ATOM   5480  O   CYS B 101      51.815  39.754  77.317  1.00 71.28           O  
ANISOU 5480  O   CYS B 101    12220   7072   7792   -168   -407   -921       O  
ATOM   5481  CB  CYS B 101      51.977  41.302  74.430  1.00 73.88           C  
ANISOU 5481  CB  CYS B 101    12895   7115   8063   -237   -745   -805       C  
ATOM   5482  SG  CYS B 101      50.739  42.217  75.327  1.00 81.53           S  
ANISOU 5482  SG  CYS B 101    14195   7821   8963    192   -695   -954       S  
ATOM   5483  N   PHE B 102      51.813  38.403  75.469  1.00 69.51           N  
ANISOU 5483  N   PHE B 102    11420   7156   7834   -204   -417   -817       N  
ATOM   5484  CA  PHE B 102      51.039  37.342  76.068  1.00 69.12           C  
ANISOU 5484  CA  PHE B 102    11054   7291   7919    -38   -264   -868       C  
ATOM   5485  C   PHE B 102      51.877  36.668  77.106  1.00 69.06           C  
ANISOU 5485  C   PHE B 102    10975   7393   7871   -245   -213   -843       C  
ATOM   5486  O   PHE B 102      51.402  36.398  78.195  1.00 71.32           O  
ANISOU 5486  O   PHE B 102    11245   7709   8144   -157   -107   -907       O  
ATOM   5487  CB  PHE B 102      50.631  36.316  75.052  1.00 68.24           C  
ANISOU 5487  CB  PHE B 102    10590   7362   7975      8   -246   -828       C  
ATOM   5488  CG  PHE B 102      49.291  36.546  74.465  1.00 70.87           C  
ANISOU 5488  CG  PHE B 102    10852   7678   8396    289   -246   -865       C  
ATOM   5489  CD1 PHE B 102      48.188  36.817  75.280  1.00 71.50           C  
ANISOU 5489  CD1 PHE B 102    10920   7761   8485    560   -147   -949       C  
ATOM   5490  CD2 PHE B 102      49.105  36.444  73.087  1.00 71.69           C  
ANISOU 5490  CD2 PHE B 102    10877   7793   8570    288   -341   -808       C  
ATOM   5491  CE1 PHE B 102      46.923  37.024  74.738  1.00 69.82           C  
ANISOU 5491  CE1 PHE B 102    10581   7585   8363    844   -152   -963       C  
ATOM   5492  CE2 PHE B 102      47.820  36.660  72.538  1.00 72.18           C  
ANISOU 5492  CE2 PHE B 102    10850   7857   8718    547   -370   -820       C  
ATOM   5493  CZ  PHE B 102      46.741  36.946  73.368  1.00 70.00           C  
ANISOU 5493  CZ  PHE B 102    10521   7611   8465    830   -279   -891       C  
ATOM   5494  N   LEU B 103      53.132  36.393  76.784  1.00 68.14           N  
ANISOU 5494  N   LEU B 103    10807   7356   7727   -517   -289   -743       N  
ATOM   5495  CA  LEU B 103      54.058  35.883  77.793  1.00 67.74           C  
ANISOU 5495  CA  LEU B 103    10712   7404   7624   -722   -282   -695       C  
ATOM   5496  C   LEU B 103      54.198  36.697  79.076  1.00 69.13           C  
ANISOU 5496  C   LEU B 103    11224   7417   7626   -799   -300   -732       C  
ATOM   5497  O   LEU B 103      54.364  36.144  80.150  1.00 68.80           O  
ANISOU 5497  O   LEU B 103    11137   7440   7563   -860   -251   -737       O  
ATOM   5498  CB  LEU B 103      55.443  35.654  77.192  1.00 67.33           C  
ANISOU 5498  CB  LEU B 103    10543   7489   7550   -985   -371   -565       C  
ATOM   5499  CG  LEU B 103      55.524  34.477  76.216  1.00 65.14           C  
ANISOU 5499  CG  LEU B 103     9917   7407   7425   -918   -319   -530       C  
ATOM   5500  CD1 LEU B 103      56.993  34.040  76.146  1.00 65.47           C  
ANISOU 5500  CD1 LEU B 103     9797   7644   7435  -1139   -362   -407       C  
ATOM   5501  CD2 LEU B 103      54.609  33.316  76.591  1.00 59.93           C  
ANISOU 5501  CD2 LEU B 103     9056   6819   6895   -723   -210   -595       C  
ATOM   5502  N   SER B 104      54.143  38.014  78.985  1.00 71.24           N  
ANISOU 5502  N   SER B 104    11877   7446   7743   -807   -383   -758       N  
ATOM   5503  CA  SER B 104      54.471  38.792  80.179  1.00 73.24           C  
ANISOU 5503  CA  SER B 104    12523   7519   7786   -938   -425   -780       C  
ATOM   5504  C   SER B 104      53.326  38.882  81.164  1.00 73.16           C  
ANISOU 5504  C   SER B 104    12639   7409   7750   -652   -271   -927       C  
ATOM   5505  O   SER B 104      53.437  39.603  82.119  1.00 75.44           O  
ANISOU 5505  O   SER B 104    13317   7506   7840   -710   -286   -971       O  
ATOM   5506  CB  SER B 104      54.909  40.186  79.809  1.00 74.52           C  
ANISOU 5506  CB  SER B 104    13142   7426   7747  -1088   -591   -747       C  
ATOM   5507  OG  SER B 104      53.840  40.770  79.100  1.00 78.20           O  
ANISOU 5507  OG  SER B 104    13728   7729   8254   -765   -565   -841       O  
ATOM   5508  N   HIS B 105      52.237  38.160  80.938  1.00 71.56           N  
ANISOU 5508  N   HIS B 105    12119   7349   7723   -363   -123   -996       N  
ATOM   5509  CA  HIS B 105      51.082  38.256  81.839  1.00 72.00           C  
ANISOU 5509  CA  HIS B 105    12240   7370   7745    -78     52  -1131       C  
ATOM   5510  C   HIS B 105      50.959  36.963  82.595  1.00 70.06           C  
ANISOU 5510  C   HIS B 105    11674   7364   7580   -142    172  -1124       C  
ATOM   5511  O   HIS B 105      49.964  36.729  83.284  1.00 69.39           O  
ANISOU 5511  O   HIS B 105    11521   7352   7492     59    344  -1217       O  
ATOM   5512  CB  HIS B 105      49.770  38.620  81.109  1.00 73.16           C  
ANISOU 5512  CB  HIS B 105    12300   7504   7992    316    125  -1209       C  
ATOM   5513  CG  HIS B 105      49.644  40.080  80.808  1.00 76.85           C  
ANISOU 5513  CG  HIS B 105    13226   7657   8315    465     31  -1259       C  
ATOM   5514  ND1 HIS B 105      50.019  40.629  79.600  1.00 75.62           N  
ANISOU 5514  ND1 HIS B 105    13171   7385   8176    398   -146  -1188       N  
ATOM   5515  CD2 HIS B 105      49.228  41.121  81.581  1.00 82.99           C  
ANISOU 5515  CD2 HIS B 105    14448   8184   8900    669     81  -1373       C  
ATOM   5516  CE1 HIS B 105      49.826  41.937  79.631  1.00 79.87           C  
ANISOU 5516  CE1 HIS B 105    14201   7604   8542    545   -223  -1249       C  
ATOM   5517  NE2 HIS B 105      49.335  42.263  80.818  1.00 82.94           N  
ANISOU 5517  NE2 HIS B 105    14815   7896   8801    734    -84  -1367       N  
ATOM   5518  N   LYS B 106      51.982  36.115  82.451  1.00 67.99           N  
ANISOU 5518  N   LYS B 106    11217   7237   7378   -417     80  -1008       N  
ATOM   5519  CA  LYS B 106      52.128  34.993  83.356  1.00 67.21           C  
ANISOU 5519  CA  LYS B 106    10938   7298   7300   -534    142   -987       C  
ATOM   5520  C   LYS B 106      52.276  35.450  84.814  1.00 69.66           C  
ANISOU 5520  C   LYS B 106    11584   7482   7403   -634    178  -1037       C  
ATOM   5521  O   LYS B 106      53.161  36.223  85.196  1.00 70.60           O  
ANISOU 5521  O   LYS B 106    12027   7439   7358   -840     53   -996       O  
ATOM   5522  CB  LYS B 106      53.262  34.046  82.928  1.00 65.68           C  
ANISOU 5522  CB  LYS B 106    10502   7253   7199   -761     22   -851       C  
ATOM   5523  CG  LYS B 106      52.818  32.836  82.008  1.00 61.81           C  
ANISOU 5523  CG  LYS B 106     9625   6952   6909   -649     64   -827       C  
ATOM   5524  CD  LYS B 106      53.950  32.298  81.092  1.00 59.15           C  
ANISOU 5524  CD  LYS B 106     9112   6712   6652   -780    -52   -709       C  
ATOM   5525  CE  LYS B 106      53.605  30.874  80.659  1.00 61.03           C  
ANISOU 5525  CE  LYS B 106     9064   7099   7026   -703     -9   -693       C  
ATOM   5526  NZ  LYS B 106      54.538  30.093  79.740  1.00 58.97           N  
ANISOU 5526  NZ  LYS B 106     8618   6944   6843   -747    -78   -602       N  
ATOM   5527  N   ASP B 107      51.373  34.966  85.634  1.00 60.24           N  
ANISOU 5527  N   ASP B 107     7677   7826   7385    926   -470   -837       N  
ATOM   5528  CA  ASP B 107      51.334  35.345  87.033  1.00 60.76           C  
ANISOU 5528  CA  ASP B 107     7777   7893   7414    891   -328  -1065       C  
ATOM   5529  C   ASP B 107      51.953  34.246  87.904  1.00 59.09           C  
ANISOU 5529  C   ASP B 107     7623   7904   6924    756   -350  -1101       C  
ATOM   5530  O   ASP B 107      51.381  33.181  88.049  1.00 56.99           O  
ANISOU 5530  O   ASP B 107     7300   7785   6569    764   -338  -1041       O  
ATOM   5531  CB  ASP B 107      49.879  35.530  87.411  1.00 62.38           C  
ANISOU 5531  CB  ASP B 107     7857   8052   7791   1017   -181  -1144       C  
ATOM   5532  CG  ASP B 107      49.705  36.249  88.729  1.00 69.48           C  
ANISOU 5532  CG  ASP B 107     8834   8878   8686    984     52  -1428       C  
ATOM   5533  OD1 ASP B 107      50.533  36.042  89.669  1.00 70.90           O  
ANISOU 5533  OD1 ASP B 107     9187   9173   8578    815     63  -1557       O  
ATOM   5534  OD2 ASP B 107      48.720  37.041  88.830  1.00 75.71           O  
ANISOU 5534  OD2 ASP B 107     9514   9478   9777   1120    223  -1527       O  
ATOM   5535  N   ASP B 108      53.110  34.520  88.512  1.00 60.48           N  
ANISOU 5535  N   ASP B 108     7903   8085   6990    621   -408  -1180       N  
ATOM   5536  CA  ASP B 108      53.742  33.553  89.412  1.00 61.04           C  
ANISOU 5536  CA  ASP B 108     8026   8345   6822    488   -497  -1170       C  
ATOM   5537  C   ASP B 108      53.072  33.528  90.806  1.00 63.82           C  
ANISOU 5537  C   ASP B 108     8505   8789   6955    413   -370  -1342       C  
ATOM   5538  O   ASP B 108      53.408  32.711  91.664  1.00 64.95           O  
ANISOU 5538  O   ASP B 108     8734   9096   6849    286   -452  -1304       O  
ATOM   5539  CB  ASP B 108      55.228  33.836  89.571  1.00 61.69           C  
ANISOU 5539  CB  ASP B 108     8136   8402   6902    351   -662  -1166       C  
ATOM   5540  CG  ASP B 108      55.952  33.817  88.278  1.00 62.68           C  
ANISOU 5540  CG  ASP B 108     8149   8436   7229    393   -706  -1015       C  
ATOM   5541  OD1 ASP B 108      56.184  32.706  87.746  1.00 62.23           O  
ANISOU 5541  OD1 ASP B 108     8006   8460   7179    420   -743   -863       O  
ATOM   5542  OD2 ASP B 108      56.265  34.929  87.788  1.00 64.08           O  
ANISOU 5542  OD2 ASP B 108     8346   8440   7562    387   -671  -1059       O  
ATOM   5543  N   SER B 109      52.145  34.426  91.051  1.00 65.04           N  
ANISOU 5543  N   SER B 109     8681   8822   7208    481   -153  -1525       N  
ATOM   5544  CA  SER B 109      51.433  34.330  92.293  1.00 68.13           C  
ANISOU 5544  CA  SER B 109     9203   9296   7387    401     57  -1707       C  
ATOM   5545  C   SER B 109      49.927  34.511  92.121  1.00 67.98           C  
ANISOU 5545  C   SER B 109     9032   9192   7606    567    340  -1774       C  
ATOM   5546  O   SER B 109      49.378  35.516  92.516  1.00 69.13           O  
ANISOU 5546  O   SER B 109     9204   9170   7893    609    583  -2005       O  
ATOM   5547  CB  SER B 109      51.967  35.347  93.271  1.00 71.18           C  
ANISOU 5547  CB  SER B 109     9826   9607   7613    238    110  -1977       C  
ATOM   5548  OG  SER B 109      51.318  35.086  94.475  1.00 77.74           O  
ANISOU 5548  OG  SER B 109    10838  10549   8149    119    338  -2146       O  
ATOM   5549  N   PRO B 110      49.271  33.515  91.520  1.00 66.80           N  
ANISOU 5549  N   PRO B 110     8698   9137   7545    655    307  -1576       N  
ATOM   5550  CA  PRO B 110      47.873  33.633  91.090  1.00 68.00           C  
ANISOU 5550  CA  PRO B 110     8610   9198   8030    824    484  -1575       C  
ATOM   5551  C   PRO B 110      46.801  33.581  92.182  1.00 71.92           C  
ANISOU 5551  C   PRO B 110     9096   9719   8513    794    864  -1771       C  
ATOM   5552  O   PRO B 110      45.700  34.086  91.916  1.00 75.85           O  
ANISOU 5552  O   PRO B 110     9351  10061   9406    955   1054  -1829       O  
ATOM   5553  CB  PRO B 110      47.759  32.548  90.028  1.00 64.45           C  
ANISOU 5553  CB  PRO B 110     8005   8847   7637    869    256  -1303       C  
ATOM   5554  CG  PRO B 110      48.747  31.554  90.406  1.00 62.47           C  
ANISOU 5554  CG  PRO B 110     7915   8771   7051    715    118  -1214       C  
ATOM   5555  CD  PRO B 110      49.846  32.213  91.161  1.00 63.15           C  
ANISOU 5555  CD  PRO B 110     8221   8845   6928    596     81  -1341       C  
ATOM   5556  N   ASP B 111      47.124  33.073  93.404  1.00 73.12           N  
ANISOU 5556  N   ASP B 111     9506  10040   8236    586    985  -1869       N  
ATOM   5557  CA  ASP B 111      46.085  32.855  94.435  1.00 77.33           C  
ANISOU 5557  CA  ASP B 111    10067  10623   8693    515   1405  -2038       C  
ATOM   5558  C   ASP B 111      44.769  32.108  94.079  1.00 77.41           C  
ANISOU 5558  C   ASP B 111     9746  10653   9013    618   1571  -1923       C  
ATOM   5559  O   ASP B 111      43.688  32.531  94.487  1.00 80.59           O  
ANISOU 5559  O   ASP B 111     9997  10950   9673    678   1972  -2106       O  
ATOM   5560  CB  ASP B 111      45.738  34.187  95.111  1.00 81.51           C  
ANISOU 5560  CB  ASP B 111    10693  10952   9324    528   1772  -2400       C  
ATOM   5561  CG  ASP B 111      45.133  34.002  96.489  1.00 89.47           C  
ANISOU 5561  CG  ASP B 111    11919  12047  10028    342   2240  -2642       C  
ATOM   5562  OD1 ASP B 111      44.233  33.148  96.634  1.00 94.31           O  
ANISOU 5562  OD1 ASP B 111    12373  12758  10700    338   2445  -2550       O  
ATOM   5563  OD2 ASP B 111      45.557  34.710  97.426  1.00 92.26           O  
ANISOU 5563  OD2 ASP B 111    12621  12366  10066    172   2415  -2931       O  
ATOM   5564  N   LEU B 112      44.862  30.932  93.614  1.00 75.29           N  
ANISOU 5564  N   LEU B 112     9405  10527   8676    584   1341  -1666       N  
ATOM   5565  CA  LEU B 112      43.742  30.060  93.390  1.00 75.83           C  
ANISOU 5565  CA  LEU B 112     9200  10637   8973    610   1462  -1553       C  
ATOM   5566  C   LEU B 112      43.458  29.185  94.642  1.00 78.82           C  
ANISOU 5566  C   LEU B 112     9774  11179   8996    388   1760  -1577       C  
ATOM   5567  O   LEU B 112      44.255  29.203  95.578  1.00 79.68           O  
ANISOU 5567  O   LEU B 112    10259  11385   8630    211   1777  -1639       O  
ATOM   5568  CB  LEU B 112      44.062  29.250  92.128  1.00 71.46           C  
ANISOU 5568  CB  LEU B 112     8509  10120   8523    665   1040  -1278       C  
ATOM   5569  CG  LEU B 112      44.334  30.076  90.871  1.00 67.76           C  
ANISOU 5569  CG  LEU B 112     7913   9506   8327    840    759  -1224       C  
ATOM   5570  CD1 LEU B 112      44.938  29.181  89.835  1.00 64.47           C  
ANISOU 5570  CD1 LEU B 112     7510   9156   7831    815    401  -1000       C  
ATOM   5571  CD2 LEU B 112      43.089  30.709  90.304  1.00 67.32           C  
ANISOU 5571  CD2 LEU B 112     7499   9291   8787   1013    836  -1243       C  
ATOM   5572  N   PRO B 113      42.323  28.445  94.678  1.00 80.96           N  
ANISOU 5572  N   PRO B 113     9797  11474   9488    370   1984  -1515       N  
ATOM   5573  CA  PRO B 113      41.974  27.714  95.902  1.00 84.55           C  
ANISOU 5573  CA  PRO B 113    10457  12060   9608    139   2339  -1536       C  
ATOM   5574  C   PRO B 113      42.855  26.508  96.215  1.00 83.38           C  
ANISOU 5574  C   PRO B 113    10604  12075   9000    -51   2067  -1279       C  
ATOM   5575  O   PRO B 113      43.163  25.687  95.316  1.00 79.15           O  
ANISOU 5575  O   PRO B 113     9933  11542   8597      3   1707  -1044       O  
ATOM   5576  CB  PRO B 113      40.522  27.240  95.641  1.00 86.27           C  
ANISOU 5576  CB  PRO B 113    10245  12226  10309    185   2614  -1507       C  
ATOM   5577  CG  PRO B 113      39.996  28.160  94.662  1.00 85.48           C  
ANISOU 5577  CG  PRO B 113     9751  11944  10785    444   2522  -1579       C  
ATOM   5578  CD  PRO B 113      41.183  28.450  93.742  1.00 82.06           C  
ANISOU 5578  CD  PRO B 113     9455  11499  10225    541   1985  -1461       C  
ATOM   5579  N   LYS B 114      43.212  26.394  97.501  1.00 86.62           N  
ANISOU 5579  N   LYS B 114    11427  12603   8882   -284   2253  -1326       N  
ATOM   5580  CA  LYS B 114      43.998  25.253  97.984  1.00 87.28           C  
ANISOU 5580  CA  LYS B 114    11805  12822   8536   -480   1998  -1042       C  
ATOM   5581  C   LYS B 114      43.308  23.948  97.574  1.00 87.18           C  
ANISOU 5581  C   LYS B 114    11557  12803   8766   -498   2014   -799       C  
ATOM   5582  O   LYS B 114      42.103  23.800  97.741  1.00 88.87           O  
ANISOU 5582  O   LYS B 114    11568  12993   9205   -528   2416   -874       O  
ATOM   5583  CB  LYS B 114      44.346  25.371  99.474  1.00 91.08           C  
ANISOU 5583  CB  LYS B 114    12796  13436   8376   -767   2186  -1110       C  
ATOM   5584  CG  LYS B 114      45.331  26.490  99.815  1.00 92.00           C  
ANISOU 5584  CG  LYS B 114    13191  13559   8207   -796   2010  -1309       C  
ATOM   5585  CD  LYS B 114      46.689  26.281  99.097  1.00 90.86           C  
ANISOU 5585  CD  LYS B 114    13011  13408   8106   -703   1382  -1083       C  
ATOM   5586  CE  LYS B 114      47.845  26.803  99.936  1.00 94.06           C  
ANISOU 5586  CE  LYS B 114    13823  13897   8020   -898   1125  -1132       C  
ATOM   5587  NZ  LYS B 114      47.711  26.502 101.427  1.00 97.96           N  
ANISOU 5587  NZ  LYS B 114    14808  14553   7861  -1246   1318  -1129       N  
ATOM   5588  N   LEU B 115      44.110  23.068  96.953  1.00 85.09           N  
ANISOU 5588  N   LEU B 115    11282  12528   8521   -468   1576   -532       N  
ATOM   5589  CA  LEU B 115      43.774  21.678  96.617  1.00 84.86           C  
ANISOU 5589  CA  LEU B 115    11122  12466   8653   -524   1509   -276       C  
ATOM   5590  C   LEU B 115      43.666  20.723  97.818  1.00 88.09           C  
ANISOU 5590  C   LEU B 115    11833  12954   8682   -794   1686    -71       C  
ATOM   5591  O   LEU B 115      44.654  20.100  98.250  1.00 87.42           O  
ANISOU 5591  O   LEU B 115    12027  12898   8292   -895   1394    176       O  
ATOM   5592  CB  LEU B 115      44.900  21.127  95.739  1.00 81.37           C  
ANISOU 5592  CB  LEU B 115    10660  11957   8299   -421   1021    -89       C  
ATOM   5593  CG  LEU B 115      45.149  21.860  94.421  1.00 81.06           C  
ANISOU 5593  CG  LEU B 115    10378  11834   8585   -191    807   -224       C  
ATOM   5594  CD1 LEU B 115      46.398  21.382  93.538  1.00 75.69           C  
ANISOU 5594  CD1 LEU B 115     9705  11076   7977   -102    397    -79       C  
ATOM   5595  CD2 LEU B 115      43.818  21.780  93.627  1.00 83.36           C  
ANISOU 5595  CD2 LEU B 115    10310  12063   9300   -122    964   -304       C  
ATOM   5596  N   LYS B 116      42.463  20.604  98.349  1.00 91.59           N  
ANISOU 5596  N   LYS B 116    12207  13417   9177   -916   2163   -149       N  
ATOM   5597  CA  LYS B 116      42.193  19.638  99.408  1.00 95.66           C  
ANISOU 5597  CA  LYS B 116    12998  13990   9357  -1199   2391     69       C  
ATOM   5598  C   LYS B 116      41.513  18.391  98.825  1.00 95.73           C  
ANISOU 5598  C   LYS B 116    12720  13886   9769  -1225   2401    275       C  
ATOM   5599  O   LYS B 116      40.317  18.421  98.528  1.00 96.93           O  
ANISOU 5599  O   LYS B 116    12523  13991  10316  -1214   2732    142       O  
ATOM   5600  CB  LYS B 116      41.380  20.315 100.527  1.00100.39           C  
ANISOU 5600  CB  LYS B 116    13780  14683   9680  -1376   2995   -166       C  
ATOM   5601  CG  LYS B 116      39.900  20.632 100.217  1.00101.56           C  
ANISOU 5601  CG  LYS B 116    13473  14755  10358  -1305   3506   -401       C  
ATOM   5602  CD  LYS B 116      39.741  21.739  99.182  1.00 93.93           C  
ANISOU 5602  CD  LYS B 116    12107  13695   9888   -989   3385   -666       C  
ATOM   5603  CE  LYS B 116      38.724  21.312  98.127  1.00 93.09           C  
ANISOU 5603  CE  LYS B 116    11422  13470  10477   -860   3376   -630       C  
ATOM   5604  NZ  LYS B 116      39.168  21.663  96.744  1.00 84.27           N  
ANISOU 5604  NZ  LYS B 116    10044  12273   9701   -594   2854   -630       N  
ATOM   5605  N   PRO B 117      42.299  17.310  98.577  1.00 95.02           N  
ANISOU 5605  N   PRO B 117    12732  13718   9654  -1248   2012    590       N  
ATOM   5606  CA  PRO B 117      41.719  16.087  97.954  1.00 94.47           C  
ANISOU 5606  CA  PRO B 117    12408  13494   9991  -1286   1999    761       C  
ATOM   5607  C   PRO B 117      40.773  15.356  98.896  1.00 98.47           C  
ANISOU 5607  C   PRO B 117    13011  14009  10395  -1569   2445    903       C  
ATOM   5608  O   PRO B 117      41.017  15.339 100.088  1.00101.61           O  
ANISOU 5608  O   PRO B 117    13821  14511  10276  -1770   2605   1032       O  
ATOM   5609  CB  PRO B 117      42.956  15.213  97.662  1.00 92.74           C  
ANISOU 5609  CB  PRO B 117    12347  13159   9731  -1242   1520   1047       C  
ATOM   5610  CG  PRO B 117      44.044  15.737  98.607  1.00 94.06           C  
ANISOU 5610  CG  PRO B 117    12920  13455   9362  -1289   1343   1139       C  
ATOM   5611  CD  PRO B 117      43.780  17.231  98.655  1.00 93.34           C  
ANISOU 5611  CD  PRO B 117    12787  13509   9168  -1201   1533    768       C  
ATOM   5612  N   ASP B 118      39.679  14.817  98.356  1.00 98.91           N  
ANISOU 5612  N   ASP B 118    12692  13960  10930  -1606   2647    869       N  
ATOM   5613  CA  ASP B 118      38.785  13.884  99.078  1.00102.96           C  
ANISOU 5613  CA  ASP B 118    13235  14426  11459  -1894   3054   1050       C  
ATOM   5614  C   ASP B 118      38.985  12.524  98.411  1.00101.50           C  
ANISOU 5614  C   ASP B 118    12962  14024  11580  -1929   2747   1308       C  
ATOM   5615  O   ASP B 118      38.875  12.411  97.181  1.00 98.26           O  
ANISOU 5615  O   ASP B 118    12208  13502  11624  -1772   2487   1183       O  
ATOM   5616  CB  ASP B 118      37.302  14.318  99.036  1.00105.20           C  
ANISOU 5616  CB  ASP B 118    13100  14729  12142  -1941   3569    799       C  
ATOM   5617  CG  ASP B 118      36.348  13.254  99.620  1.00110.58           C  
ANISOU 5617  CG  ASP B 118    13736  15329  12950  -2253   3995    992       C  
ATOM   5618  OD1 ASP B 118      36.779  12.464 100.477  1.00114.66           O  
ANISOU 5618  OD1 ASP B 118    14689  15833  13043  -2476   4039   1303       O  
ATOM   5619  OD2 ASP B 118      35.156  13.191  99.239  1.00111.21           O  
ANISOU 5619  OD2 ASP B 118    13337  15345  13574  -2293   4278    859       O  
ATOM   5620  N   PRO B 119      39.341  11.503  99.208  1.00103.94           N  
ANISOU 5620  N   PRO B 119    13619  14254  11620  -2141   2754   1673       N  
ATOM   5621  CA  PRO B 119      39.622  10.183  98.631  1.00103.22           C  
ANISOU 5621  CA  PRO B 119    13475  13897  11846  -2167   2475   1922       C  
ATOM   5622  C   PRO B 119      38.458   9.643  97.800  1.00103.30           C  
ANISOU 5622  C   PRO B 119    13032  13761  12458  -2235   2634   1789       C  
ATOM   5623  O   PRO B 119      38.620   9.456  96.589  1.00 99.99           O  
ANISOU 5623  O   PRO B 119    12364  13212  12417  -2081   2313   1654       O  
ATOM   5624  CB  PRO B 119      39.901   9.296  99.866  1.00108.11           C  
ANISOU 5624  CB  PRO B 119    14543  14461  12072  -2435   2577   2361       C  
ATOM   5625  CG  PRO B 119      39.519  10.147 101.087  1.00111.17           C  
ANISOU 5625  CG  PRO B 119    15211  15120  11907  -2608   3003   2295       C  
ATOM   5626  CD  PRO B 119      39.694  11.563 100.639  1.00107.57           C  
ANISOU 5626  CD  PRO B 119    14594  14849  11428  -2355   2937   1887       C  
ATOM   5627  N   ASN B 120      37.303   9.420  98.441  1.00107.45           N  
ANISOU 5627  N   ASN B 120    13458  14309  13060  -2486   3131   1815       N  
ATOM   5628  CA  ASN B 120      36.136   8.852  97.767  1.00108.60           C  
ANISOU 5628  CA  ASN B 120    13144  14309  13811  -2604   3284   1718       C  
ATOM   5629  C   ASN B 120      35.812   9.551  96.448  1.00104.85           C  
ANISOU 5629  C   ASN B 120    12211  13863  13766  -2374   3025   1368       C  
ATOM   5630  O   ASN B 120      35.639   8.875  95.432  1.00104.02           O  
ANISOU 5630  O   ASN B 120    11878  13576  14070  -2386   2754   1330       O  
ATOM   5631  CB  ASN B 120      34.903   8.775  98.684  1.00114.13           C  
ANISOU 5631  CB  ASN B 120    13736  15064  14566  -2891   3928   1746       C  
ATOM   5632  CG  ASN B 120      34.887   7.511  99.551  1.00119.42           C  
ANISOU 5632  CG  ASN B 120    14734  15570  15071  -3214   4136   2154       C  
ATOM   5633  OD1 ASN B 120      35.849   7.215 100.261  1.00121.01           O  
ANISOU 5633  OD1 ASN B 120    15448  15769  14762  -3249   3990   2450       O  
ATOM   5634  ND2 ASN B 120      33.786   6.767  99.500  1.00124.42           N  
ANISOU 5634  ND2 ASN B 120    15062  16053  16160  -3466   4457   2197       N  
ATOM   5635  N   THR B 121      35.786  10.887  96.441  1.00102.87           N  
ANISOU 5635  N   THR B 121    11866  13819  13400  -2179   3076   1121       N  
ATOM   5636  CA  THR B 121      35.297  11.625  95.254  1.00100.09           C  
ANISOU 5636  CA  THR B 121    11056  13491  13481  -1986   2856    831       C  
ATOM   5637  C   THR B 121      36.333  11.790  94.167  1.00 94.83           C  
ANISOU 5637  C   THR B 121    10486  12788  12758  -1756   2296    765       C  
ATOM   5638  O   THR B 121      36.008  12.241  93.070  1.00 93.28           O  
ANISOU 5638  O   THR B 121     9977  12590  12873  -1632   2040    574       O  
ATOM   5639  CB  THR B 121      34.689  12.992  95.593  1.00100.77           C  
ANISOU 5639  CB  THR B 121    10925  13753  13610  -1864   3166    594       C  
ATOM   5640  OG1 THR B 121      35.709  13.828  96.151  1.00 99.07           O  
ANISOU 5640  OG1 THR B 121    11115  13675  12853  -1715   3130    561       O  
ATOM   5641  CG2 THR B 121      33.503  12.840  96.572  1.00106.08           C  
ANISOU 5641  CG2 THR B 121    11421  14441  14445  -2104   3817    605       C  
ATOM   5642  N   LEU B 122      37.581  11.451  94.469  1.00 92.96           N  
ANISOU 5642  N   LEU B 122    10673  12517  12132  -1706   2107    934       N  
ATOM   5643  CA  LEU B 122      38.607  11.465  93.435  1.00 88.96           C  
ANISOU 5643  CA  LEU B 122    10247  11936  11618  -1511   1642    875       C  
ATOM   5644  C   LEU B 122      38.492  10.155  92.700  1.00 90.13           C  
ANISOU 5644  C   LEU B 122    10329  11830  12088  -1641   1482    945       C  
ATOM   5645  O   LEU B 122      38.574  10.145  91.461  1.00 88.51           O  
ANISOU 5645  O   LEU B 122     9987  11550  12092  -1564   1188    770       O  
ATOM   5646  CB  LEU B 122      40.022  11.614  93.986  1.00 86.42           C  
ANISOU 5646  CB  LEU B 122    10331  11645  10859  -1395   1485   1023       C  
ATOM   5647  CG  LEU B 122      40.473  12.884  94.705  1.00 84.82           C  
ANISOU 5647  CG  LEU B 122    10298  11670  10260  -1278   1559    946       C  
ATOM   5648  CD1 LEU B 122      41.916  12.736  95.234  1.00 80.87           C  
ANISOU 5648  CD1 LEU B 122    10180  11160   9389  -1222   1317   1154       C  
ATOM   5649  CD2 LEU B 122      40.314  14.137  93.845  1.00 80.33           C  
ANISOU 5649  CD2 LEU B 122     9491  11206   9827  -1066   1449    645       C  
ATOM   5650  N   CYS B 123      38.285   9.059  93.443  1.00 93.34           N  
ANISOU 5650  N   CYS B 123    10858  12087  12520  -1863   1683   1192       N  
ATOM   5651  CA  CYS B 123      38.164   7.742  92.797  1.00 95.29           C  
ANISOU 5651  CA  CYS B 123    11058  12035  13113  -2010   1561   1252       C  
ATOM   5652  C   CYS B 123      36.879   7.632  91.999  1.00 96.62           C  
ANISOU 5652  C   CYS B 123    10809  12176  13728  -2157   1580   1044       C  
ATOM   5653  O   CYS B 123      36.809   6.829  91.067  1.00 97.57           O  
ANISOU 5653  O   CYS B 123    10863  12078  14132  -2249   1370    961       O  
ATOM   5654  CB  CYS B 123      38.246   6.571  93.773  1.00 99.13           C  
ANISOU 5654  CB  CYS B 123    11779  12322  13563  -2221   1759   1604       C  
ATOM   5655  SG  CYS B 123      39.923   6.051  94.310  1.00100.77           S  
ANISOU 5655  SG  CYS B 123    12449  12373  13468  -2083   1526   1932       S  
ATOM   5656  N   ASP B 124      35.872   8.429  92.359  1.00 97.33           N  
ANISOU 5656  N   ASP B 124    10609  12467  13906  -2190   1826    953       N  
ATOM   5657  CA  ASP B 124      34.654   8.503  91.562  1.00 98.64           C  
ANISOU 5657  CA  ASP B 124    10297  12628  14553  -2299   1771    764       C  
ATOM   5658  C   ASP B 124      35.068   8.997  90.203  1.00 94.24           C  
ANISOU 5658  C   ASP B 124     9696  12095  14018  -2121   1295    545       C  
ATOM   5659  O   ASP B 124      35.057   8.248  89.221  1.00 93.24           O  
ANISOU 5659  O   ASP B 124     9553  11791  14081  -2235   1013    460       O  
ATOM   5660  CB  ASP B 124      33.598   9.436  92.194  1.00101.48           C  
ANISOU 5660  CB  ASP B 124    10310  13186  15064  -2301   2133    698       C  
ATOM   5661  CG  ASP B 124      33.030   8.878  93.488  1.00106.26           C  
ANISOU 5661  CG  ASP B 124    10954  13760  15660  -2545   2681    894       C  
ATOM   5662  OD1 ASP B 124      33.537   7.818  93.910  1.00108.32           O  
ANISOU 5662  OD1 ASP B 124    11548  13854  15753  -2694   2718   1124       O  
ATOM   5663  OD2 ASP B 124      32.090   9.474  94.091  1.00110.53           O  
ANISOU 5663  OD2 ASP B 124    11204  14420  16375  -2595   3098    831       O  
ATOM   5664  N   GLU B 125      35.492  10.249  90.179  1.00 91.17           N  
ANISOU 5664  N   GLU B 125     9341  11908  13391  -1863   1226    452       N  
ATOM   5665  CA  GLU B 125      36.046  10.855  88.970  1.00 87.61           C  
ANISOU 5665  CA  GLU B 125     8927  11496  12863  -1682    804    280       C  
ATOM   5666  C   GLU B 125      37.114  10.041  88.256  1.00 85.83           C  
ANISOU 5666  C   GLU B 125     9036  11088  12489  -1681    552    268       C  
ATOM   5667  O   GLU B 125      37.223  10.135  87.033  1.00 85.45           O  
ANISOU 5667  O   GLU B 125     8980  11010  12479  -1668    225     99       O  
ATOM   5668  CB  GLU B 125      36.528  12.252  89.260  1.00 84.85           C  
ANISOU 5668  CB  GLU B 125     8641  11351  12248  -1413    829    228       C  
ATOM   5669  CG  GLU B 125      35.368  13.237  89.326  1.00 86.33           C  
ANISOU 5669  CG  GLU B 125     8396  11668  12736  -1368    943    135       C  
ATOM   5670  CD  GLU B 125      35.609  14.353  90.314  1.00 84.16           C  
ANISOU 5670  CD  GLU B 125     8204  11544  12228  -1190   1245    119       C  
ATOM   5671  OE1 GLU B 125      36.789  14.683  90.523  1.00 80.58           O  
ANISOU 5671  OE1 GLU B 125     8123  11135  11360  -1052   1174    138       O  
ATOM   5672  OE2 GLU B 125      34.625  14.898  90.876  1.00 85.84           O  
ANISOU 5672  OE2 GLU B 125     8101  11815  12700  -1200   1566     70       O  
ATOM   5673  N   PHE B 126      37.879   9.231  88.985  1.00 85.70           N  
ANISOU 5673  N   PHE B 126     9312  10930  12321  -1708    705    449       N  
ATOM   5674  CA  PHE B 126      38.936   8.433  88.336  1.00 84.39           C  
ANISOU 5674  CA  PHE B 126     9423  10535  12107  -1680    517    431       C  
ATOM   5675  C   PHE B 126      38.487   7.120  87.674  1.00 87.32           C  
ANISOU 5675  C   PHE B 126     9759  10614  12803  -1932    458    368       C  
ATOM   5676  O   PHE B 126      38.969   6.801  86.585  1.00 87.16           O  
ANISOU 5676  O   PHE B 126     9863  10450  12802  -1930    246    181       O  
ATOM   5677  CB  PHE B 126      40.122   8.144  89.275  1.00 83.25           C  
ANISOU 5677  CB  PHE B 126     9590  10315  11724  -1561    621    669       C  
ATOM   5678  CG  PHE B 126      41.114   7.199  88.693  1.00 80.08           C  
ANISOU 5678  CG  PHE B 126     9397   9612  11417  -1531    493    669       C  
ATOM   5679  CD1 PHE B 126      42.070   7.643  87.834  1.00 76.92           C  
ANISOU 5679  CD1 PHE B 126     9104   9210  10911  -1344    309    499       C  
ATOM   5680  CD2 PHE B 126      41.051   5.855  88.960  1.00 84.66           C  
ANISOU 5680  CD2 PHE B 126    10051   9878  12240  -1699    591    824       C  
ATOM   5681  CE1 PHE B 126      42.982   6.795  87.283  1.00 76.91           C  
ANISOU 5681  CE1 PHE B 126     9267   8905  11049  -1307    262    463       C  
ATOM   5682  CE2 PHE B 126      41.966   4.979  88.392  1.00 84.09           C  
ANISOU 5682  CE2 PHE B 126    10145   9471  12333  -1651    511    796       C  
ATOM   5683  CZ  PHE B 126      42.931   5.461  87.561  1.00 79.68           C  
ANISOU 5683  CZ  PHE B 126     9677   8922  11676  -1450    365    602       C  
ATOM   5684  N   LYS B 127      37.670   6.327  88.378  1.00 90.66           N  
ANISOU 5684  N   LYS B 127    10063  10926  13459  -2161    682    523       N  
ATOM   5685  CA  LYS B 127      37.017   5.128  87.825  1.00 94.06           C  
ANISOU 5685  CA  LYS B 127    10404  11076  14259  -2453    646    453       C  
ATOM   5686  C   LYS B 127      36.074   5.476  86.665  1.00 95.33           C  
ANISOU 5686  C   LYS B 127    10276  11330  14616  -2585    372    175       C  
ATOM   5687  O   LYS B 127      35.907   4.679  85.738  1.00 97.01           O  
ANISOU 5687  O   LYS B 127    10524  11324  15010  -2786    187      0       O  
ATOM   5688  CB  LYS B 127      36.207   4.367  88.907  1.00 97.85           C  
ANISOU 5688  CB  LYS B 127    10768  11449  14961  -2695    980    702       C  
ATOM   5689  CG  LYS B 127      36.960   3.236  89.636  1.00 98.38           C  
ANISOU 5689  CG  LYS B 127    11155  11204  15021  -2739   1141    984       C  
ATOM   5690  CD  LYS B 127      36.447   3.042  91.069  1.00101.49           C  
ANISOU 5690  CD  LYS B 127    11545  11645  15371  -2880   1517   1320       C  
ATOM   5691  CE  LYS B 127      35.539   1.825  91.190  1.00106.61           C  
ANISOU 5691  CE  LYS B 127    12066  11999  16442  -3240   1698   1417       C  
ATOM   5692  NZ  LYS B 127      34.494   1.990  92.235  1.00110.26           N  
ANISOU 5692  NZ  LYS B 127    12335  12615  16942  -3439   2098   1594       N  
ATOM   5693  N   ALA B 128      35.454   6.661  86.736  1.00 94.83           N  
ANISOU 5693  N   ALA B 128     9933  11571  14528  -2482    336    142       N  
ATOM   5694  CA  ALA B 128      34.455   7.105  85.752  1.00 95.68           C  
ANISOU 5694  CA  ALA B 128     9700  11786  14870  -2597     28    -46       C  
ATOM   5695  C   ALA B 128      35.093   7.534  84.428  1.00 93.08           C  
ANISOU 5695  C   ALA B 128     9583  11493  14292  -2502   -380   -261       C  
ATOM   5696  O   ALA B 128      34.584   7.175  83.372  1.00 95.63           O  
ANISOU 5696  O   ALA B 128     9843  11745  14748  -2724   -699   -434       O  
ATOM   5697  CB  ALA B 128      33.607   8.228  86.318  1.00 95.93           C  
ANISOU 5697  CB  ALA B 128     9335  12077  15039  -2489    153     16       C  
ATOM   5698  N   ASP B 129      36.203   8.273  84.487  1.00 88.34           N  
ANISOU 5698  N   ASP B 129     9252  10998  13317  -2209   -365   -251       N  
ATOM   5699  CA  ASP B 129      36.794   8.898  83.291  1.00 85.96           C  
ANISOU 5699  CA  ASP B 129     9145  10769  12747  -2108   -693   -432       C  
ATOM   5700  C   ASP B 129      38.305   9.234  83.479  1.00 81.80           C  
ANISOU 5700  C   ASP B 129     8982  10239  11861  -1834   -571   -408       C  
ATOM   5701  O   ASP B 129      38.685  10.375  83.767  1.00 78.86           O  
ANISOU 5701  O   ASP B 129     8601  10067  11295  -1594   -559   -352       O  
ATOM   5702  CB  ASP B 129      35.937  10.128  82.875  1.00 86.17           C  
ANISOU 5702  CB  ASP B 129     8846  11048  12847  -2048   -954   -447       C  
ATOM   5703  CG  ASP B 129      36.384  10.775  81.551  1.00 84.67           C  
ANISOU 5703  CG  ASP B 129     8868  10935  12367  -2003  -1341   -596       C  
ATOM   5704  OD1 ASP B 129      37.456  10.415  81.027  1.00 83.05           O  
ANISOU 5704  OD1 ASP B 129     9071  10619  11867  -1984  -1330   -711       O  
ATOM   5705  OD2 ASP B 129      35.660  11.669  81.036  1.00 85.36           O  
ANISOU 5705  OD2 ASP B 129     8710  11183  12541  -1988  -1644   -582       O  
ATOM   5706  N   GLU B 130      39.145   8.220  83.296  1.00 82.29           N  
ANISOU 5706  N   GLU B 130     9334  10039  11893  -1881   -481   -458       N  
ATOM   5707  CA  GLU B 130      40.612   8.363  83.353  1.00 80.60           C  
ANISOU 5707  CA  GLU B 130     9417   9763  11446  -1647   -382   -445       C  
ATOM   5708  C   GLU B 130      41.171   9.621  82.655  1.00 77.88           C  
ANISOU 5708  C   GLU B 130     9163   9629  10800  -1460   -547   -551       C  
ATOM   5709  O   GLU B 130      42.059  10.334  83.202  1.00 74.95           O  
ANISOU 5709  O   GLU B 130     8862   9356  10259  -1215   -451   -447       O  
ATOM   5710  CB  GLU B 130      41.333   7.107  82.796  1.00 82.48           C  
ANISOU 5710  CB  GLU B 130     9918   9638  11784  -1747   -307   -576       C  
ATOM   5711  CG  GLU B 130      41.856   6.062  83.831  1.00 85.50           C  
ANISOU 5711  CG  GLU B 130    10360   9744  12381  -1714    -54   -352       C  
ATOM   5712  CD  GLU B 130      42.344   4.738  83.159  1.00 91.38           C  
ANISOU 5712  CD  GLU B 130    11314  10056  13352  -1840     28   -520       C  
ATOM   5713  OE1 GLU B 130      43.174   4.820  82.209  1.00 92.66           O  
ANISOU 5713  OE1 GLU B 130    11680  10125  13400  -1770     18   -758       O  
ATOM   5714  OE2 GLU B 130      41.906   3.619  83.567  1.00 90.97           O  
ANISOU 5714  OE2 GLU B 130    11231   9730  13603  -2019    140   -429       O  
ATOM   5715  N   LYS B 131      40.683   9.918  81.454  1.00 78.80           N  
ANISOU 5715  N   LYS B 131     9296   9810  10835  -1594   -816   -740       N  
ATOM   5716  CA  LYS B 131      41.395  10.963  80.725  1.00 76.31           C  
ANISOU 5716  CA  LYS B 131     9151   9633  10209  -1439   -939   -820       C  
ATOM   5717  C   LYS B 131      40.993  12.394  81.087  1.00 73.54           C  
ANISOU 5717  C   LYS B 131     8582   9562   9799  -1260  -1045   -690       C  
ATOM   5718  O   LYS B 131      41.819  13.276  81.059  1.00 70.81           O  
ANISOU 5718  O   LYS B 131     8355   9305   9245  -1060  -1019   -671       O  
ATOM   5719  CB  LYS B 131      41.511  10.669  79.222  1.00 78.72           C  
ANISOU 5719  CB  LYS B 131     9733   9852  10324  -1642  -1133  -1078       C  
ATOM   5720  CG  LYS B 131      43.006  10.789  78.766  1.00 79.74           C  
ANISOU 5720  CG  LYS B 131    10201   9883  10212  -1495   -948  -1190       C  
ATOM   5721  CD  LYS B 131      43.981   9.989  79.703  1.00 78.49           C  
ANISOU 5721  CD  LYS B 131    10064   9495  10265  -1340   -604  -1103       C  
ATOM   5722  CE  LYS B 131      45.426   9.972  79.192  1.00 77.23           C  
ANISOU 5722  CE  LYS B 131    10162   9185   9995  -1212   -402  -1232       C  
ATOM   5723  NZ  LYS B 131      46.198   8.762  79.671  1.00 78.71           N  
ANISOU 5723  NZ  LYS B 131    10387   9023  10495  -1160   -125  -1218       N  
ATOM   5724  N   LYS B 132      39.756  12.611  81.514  1.00 74.76           N  
ANISOU 5724  N   LYS B 132     8393   9821  10192  -1325  -1117   -601       N  
ATOM   5725  CA  LYS B 132      39.380  13.945  81.952  1.00 73.72           C  
ANISOU 5725  CA  LYS B 132     8032   9896  10082  -1131  -1147   -493       C  
ATOM   5726  C   LYS B 132      40.134  14.236  83.220  1.00 72.21           C  
ANISOU 5726  C   LYS B 132     7894   9736   9805   -923   -819   -380       C  
ATOM   5727  O   LYS B 132      40.673  15.311  83.372  1.00 70.45           O  
ANISOU 5727  O   LYS B 132     7722   9622   9421   -722   -808   -359       O  
ATOM   5728  CB  LYS B 132      37.919  14.017  82.246  1.00 75.82           C  
ANISOU 5728  CB  LYS B 132     7870  10224  10714  -1236  -1211   -431       C  
ATOM   5729  CG  LYS B 132      37.502  15.337  82.725  1.00 74.49           C  
ANISOU 5729  CG  LYS B 132     7441  10211  10651  -1026  -1181   -345       C  
ATOM   5730  CD  LYS B 132      36.203  15.676  82.109  1.00 75.57           C  
ANISOU 5730  CD  LYS B 132     7193  10393  11127  -1126  -1494   -327       C  
ATOM   5731  CE  LYS B 132      35.203  14.710  82.638  1.00 78.83           C  
ANISOU 5731  CE  LYS B 132     7299  10735  11917  -1338  -1352   -306       C  
ATOM   5732  NZ  LYS B 132      34.111  15.520  83.178  1.00 85.81           N  
ANISOU 5732  NZ  LYS B 132     7676  11694  13233  -1241  -1269   -226       N  
ATOM   5733  N   PHE B 133      40.157  13.240  84.107  1.00 73.12           N  
ANISOU 5733  N   PHE B 133     8017   9740  10024  -1003   -576   -299       N  
ATOM   5734  CA  PHE B 133      40.890  13.233  85.362  1.00 72.15           C  
ANISOU 5734  CA  PHE B 133     8005   9623   9784   -876   -306   -156       C  
ATOM   5735  C   PHE B 133      42.417  13.495  85.144  1.00 69.41           C  
ANISOU 5735  C   PHE B 133     7948   9239   9184   -704   -335   -173       C  
ATOM   5736  O   PHE B 133      43.047  14.289  85.870  1.00 67.25           O  
ANISOU 5736  O   PHE B 133     7731   9075   8746   -538   -256    -99       O  
ATOM   5737  CB  PHE B 133      40.576  11.881  86.029  1.00 75.29           C  
ANISOU 5737  CB  PHE B 133     8397   9852  10357  -1059   -123    -43       C  
ATOM   5738  CG  PHE B 133      41.168  11.676  87.419  1.00 77.12           C  
ANISOU 5738  CG  PHE B 133     8762  10079  10459   -996    122    169       C  
ATOM   5739  CD1 PHE B 133      40.450  12.044  88.558  1.00 80.72           C  
ANISOU 5739  CD1 PHE B 133     9090  10674  10905  -1030    358    280       C  
ATOM   5740  CD2 PHE B 133      42.411  11.038  87.577  1.00 74.57           C  
ANISOU 5740  CD2 PHE B 133     8696   9591  10048   -929    118    265       C  
ATOM   5741  CE1 PHE B 133      40.975  11.839  89.846  1.00 81.38           C  
ANISOU 5741  CE1 PHE B 133     9368  10769  10783  -1025    557    489       C  
ATOM   5742  CE2 PHE B 133      42.951  10.823  88.843  1.00 76.35           C  
ANISOU 5742  CE2 PHE B 133     9055   9812  10143   -897    257    508       C  
ATOM   5743  CZ  PHE B 133      42.230  11.219  89.988  1.00 81.27           C  
ANISOU 5743  CZ  PHE B 133     9619  10607  10654   -964    462    626       C  
ATOM   5744  N   TRP B 134      43.003  12.864  84.121  1.00 69.49           N  
ANISOU 5744  N   TRP B 134     8136   9086   9181   -760   -434   -294       N  
ATOM   5745  CA  TRP B 134      44.437  13.061  83.791  1.00 66.56           C  
ANISOU 5745  CA  TRP B 134     7989   8648   8652   -609   -418   -333       C  
ATOM   5746  C   TRP B 134      44.621  14.489  83.325  1.00 64.49           C  
ANISOU 5746  C   TRP B 134     7729   8577   8195   -477   -540   -392       C  
ATOM   5747  O   TRP B 134      45.593  15.113  83.706  1.00 62.72           O  
ANISOU 5747  O   TRP B 134     7579   8395   7856   -314   -484   -343       O  
ATOM   5748  CB  TRP B 134      44.885  12.014  82.771  1.00 67.78           C  
ANISOU 5748  CB  TRP B 134     8324   8553   8875   -727   -413   -494       C  
ATOM   5749  CG  TRP B 134      46.292  12.084  82.191  1.00 67.77           C  
ANISOU 5749  CG  TRP B 134     8525   8434   8791   -605   -336   -588       C  
ATOM   5750  CD1 TRP B 134      47.424  11.419  82.646  1.00 69.37           C  
ANISOU 5750  CD1 TRP B 134     8783   8423   9151   -495   -173   -509       C  
ATOM   5751  CD2 TRP B 134      46.697  12.778  81.004  1.00 66.80           C  
ANISOU 5751  CD2 TRP B 134     8559   8366   8455   -602   -401   -771       C  
ATOM   5752  NE1 TRP B 134      48.500  11.690  81.838  1.00 67.43           N  
ANISOU 5752  NE1 TRP B 134     8672   8099   8851   -410    -97   -654       N  
ATOM   5753  CE2 TRP B 134      48.089  12.522  80.821  1.00 68.43           C  
ANISOU 5753  CE2 TRP B 134     8893   8393   8713   -487   -212   -821       C  
ATOM   5754  CE3 TRP B 134      46.025  13.606  80.082  1.00 65.98           C  
ANISOU 5754  CE3 TRP B 134     8497   8437   8136   -690   -609   -870       C  
ATOM   5755  CZ2 TRP B 134      48.823  13.065  79.738  1.00 66.51           C  
ANISOU 5755  CZ2 TRP B 134     8837   8148   8286   -478   -157   -997       C  
ATOM   5756  CZ3 TRP B 134      46.753  14.135  78.989  1.00 65.73           C  
ANISOU 5756  CZ3 TRP B 134     8701   8406   7867   -692   -606  -1014       C  
ATOM   5757  CH2 TRP B 134      48.138  13.870  78.843  1.00 66.28           C  
ANISOU 5757  CH2 TRP B 134     8912   8306   7968   -593   -347  -1087       C  
ATOM   5758  N   GLY B 135      43.660  15.017  82.553  1.00 65.26           N  
ANISOU 5758  N   GLY B 135     7728   8777   8289   -557   -730   -471       N  
ATOM   5759  CA  GLY B 135      43.674  16.418  82.092  1.00 63.53           C  
ANISOU 5759  CA  GLY B 135     7496   8713   7930   -437   -876   -485       C  
ATOM   5760  C   GLY B 135      43.561  17.453  83.181  1.00 62.81           C  
ANISOU 5760  C   GLY B 135     7248   8757   7861   -264   -775   -381       C  
ATOM   5761  O   GLY B 135      44.394  18.351  83.313  1.00 61.27           O  
ANISOU 5761  O   GLY B 135     7149   8608   7523   -113   -747   -373       O  
ATOM   5762  N   LYS B 136      42.514  17.302  83.987  1.00 65.28           N  
ANISOU 5762  N   LYS B 136     7322   9117   8366   -308   -686   -320       N  
ATOM   5763  CA  LYS B 136      42.245  18.132  85.150  1.00 64.40           C  
ANISOU 5763  CA  LYS B 136     7074   9112   8283   -188   -502   -261       C  
ATOM   5764  C   LYS B 136      43.472  18.296  86.047  1.00 61.46           C  
ANISOU 5764  C   LYS B 136     6917   8752   7685    -86   -349   -213       C  
ATOM   5765  O   LYS B 136      43.722  19.360  86.525  1.00 59.41           O  
ANISOU 5765  O   LYS B 136     6666   8573   7334     36   -294   -228       O  
ATOM   5766  CB  LYS B 136      41.073  17.580  85.965  1.00 66.30           C  
ANISOU 5766  CB  LYS B 136     7074   9364   8753   -305   -321   -211       C  
ATOM   5767  CG  LYS B 136      40.335  18.728  86.700  1.00 69.73           C  
ANISOU 5767  CG  LYS B 136     7281   9902   9312   -193   -153   -227       C  
ATOM   5768  CD  LYS B 136      39.173  19.240  85.846  1.00 75.24           C  
ANISOU 5768  CD  LYS B 136     7640  10602  10345   -190   -359   -258       C  
ATOM   5769  CE  LYS B 136      38.568  20.594  86.337  1.00 78.85           C  
ANISOU 5769  CE  LYS B 136     7850  11101  11010    -16   -217   -293       C  
ATOM   5770  NZ  LYS B 136      37.838  20.541  87.674  1.00 80.61           N  
ANISOU 5770  NZ  LYS B 136     7889  11347  11391    -48    231   -315       N  
ATOM   5771  N   TYR B 137      44.202  17.223  86.301  1.00 62.43           N  
ANISOU 5771  N   TYR B 137     7196   8772   7755   -148   -299   -145       N  
ATOM   5772  CA  TYR B 137      45.503  17.340  86.940  1.00 62.09           C  
ANISOU 5772  CA  TYR B 137     7334   8719   7540    -55   -258    -73       C  
ATOM   5773  C   TYR B 137      46.397  18.297  86.139  1.00 60.98           C  
ANISOU 5773  C   TYR B 137     7277   8591   7302     72   -381   -165       C  
ATOM   5774  O   TYR B 137      46.839  19.306  86.693  1.00 60.85           O  
ANISOU 5774  O   TYR B 137     7290   8664   7167    169   -363   -164       O  
ATOM   5775  CB  TYR B 137      46.214  16.000  87.028  1.00 62.80           C  
ANISOU 5775  CB  TYR B 137     7537   8632   7692   -115   -244     28       C  
ATOM   5776  CG  TYR B 137      47.481  16.112  87.818  1.00 60.28           C  
ANISOU 5776  CG  TYR B 137     7341   8302   7259    -25   -255    155       C  
ATOM   5777  CD1 TYR B 137      47.447  16.202  89.213  1.00 60.18           C  
ANISOU 5777  CD1 TYR B 137     7385   8387   7094    -59   -188    312       C  
ATOM   5778  CD2 TYR B 137      48.718  16.161  87.178  1.00 58.34           C  
ANISOU 5778  CD2 TYR B 137     7159   7954   7055     73   -334    119       C  
ATOM   5779  CE1 TYR B 137      48.620  16.336  89.969  1.00 58.86           C  
ANISOU 5779  CE1 TYR B 137     7337   8225   6802     -7   -282    452       C  
ATOM   5780  CE2 TYR B 137      49.898  16.267  87.901  1.00 57.01           C  
ANISOU 5780  CE2 TYR B 137     7042   7766   6853    150   -393    255       C  
ATOM   5781  CZ  TYR B 137      49.855  16.378  89.288  1.00 60.62           C  
ANISOU 5781  CZ  TYR B 137     7556   8334   7144    107   -409    429       C  
ATOM   5782  OH  TYR B 137      51.052  16.500  89.987  1.00 63.14           O  
ANISOU 5782  OH  TYR B 137     7928   8642   7419    156   -550    582       O  
ATOM   5783  N   LEU B 138      46.653  18.027  84.850  1.00 60.14           N  
ANISOU 5783  N   LEU B 138     7232   8391   7226     45   -483   -256       N  
ATOM   5784  CA  LEU B 138      47.534  18.943  84.120  1.00 58.17           C  
ANISOU 5784  CA  LEU B 138     7086   8151   6867    140   -547   -324       C  
ATOM   5785  C   LEU B 138      46.999  20.342  84.286  1.00 58.09           C  
ANISOU 5785  C   LEU B 138     6989   8272   6812    224   -599   -335       C  
ATOM   5786  O   LEU B 138      47.763  21.263  84.606  1.00 58.51           O  
ANISOU 5786  O   LEU B 138     7093   8356   6783    324   -581   -334       O  
ATOM   5787  CB  LEU B 138      47.670  18.622  82.646  1.00 58.43           C  
ANISOU 5787  CB  LEU B 138     7243   8092   6867     60   -619   -439       C  
ATOM   5788  CG  LEU B 138      48.188  17.246  82.312  1.00 57.65           C  
ANISOU 5788  CG  LEU B 138     7244   7806   6856    -26   -520   -488       C  
ATOM   5789  CD1 LEU B 138      48.238  17.162  80.835  1.00 56.86           C  
ANISOU 5789  CD1 LEU B 138     7322   7643   6640   -136   -563   -650       C  
ATOM   5790  CD2 LEU B 138      49.523  17.019  82.888  1.00 56.11           C  
ANISOU 5790  CD2 LEU B 138     7071   7511   6739     84   -396   -423       C  
ATOM   5791  N   TYR B 139      45.692  20.505  84.094  1.00 59.14           N  
ANISOU 5791  N   TYR B 139     6964   8456   7053    182   -664   -345       N  
ATOM   5792  CA  TYR B 139      45.033  21.809  84.299  1.00 58.53           C  
ANISOU 5792  CA  TYR B 139     6744   8453   7043    284   -689   -350       C  
ATOM   5793  C   TYR B 139      45.483  22.532  85.590  1.00 57.79           C  
ANISOU 5793  C   TYR B 139     6670   8409   6879    381   -507   -355       C  
ATOM   5794  O   TYR B 139      45.912  23.694  85.548  1.00 56.04           O  
ANISOU 5794  O   TYR B 139     6490   8186   6614    484   -526   -391       O  
ATOM   5795  CB  TYR B 139      43.529  21.632  84.271  1.00 59.78           C  
ANISOU 5795  CB  TYR B 139     6641   8635   7438    225   -729   -337       C  
ATOM   5796  CG  TYR B 139      42.707  22.885  84.558  1.00 63.13           C  
ANISOU 5796  CG  TYR B 139     6840   9086   8059    351   -711   -342       C  
ATOM   5797  CD1 TYR B 139      42.751  24.001  83.705  1.00 63.40           C  
ANISOU 5797  CD1 TYR B 139     6878   9088   8124    452   -913   -322       C  
ATOM   5798  CD2 TYR B 139      41.837  22.939  85.644  1.00 63.70           C  
ANISOU 5798  CD2 TYR B 139     6693   9188   8321    363   -468   -363       C  
ATOM   5799  CE1 TYR B 139      41.993  25.145  83.969  1.00 64.89           C  
ANISOU 5799  CE1 TYR B 139     6833   9243   8580    591   -889   -317       C  
ATOM   5800  CE2 TYR B 139      41.072  24.084  85.901  1.00 64.24           C  
ANISOU 5800  CE2 TYR B 139     6526   9234   8649    495   -392   -398       C  
ATOM   5801  CZ  TYR B 139      41.165  25.180  85.070  1.00 66.00           C  
ANISOU 5801  CZ  TYR B 139     6732   9394   8951    623   -613   -373       C  
ATOM   5802  OH  TYR B 139      40.405  26.319  85.313  1.00 69.31           O  
ANISOU 5802  OH  TYR B 139     6892   9734   9709    777   -536   -398       O  
ATOM   5803  N   GLU B 140      45.439  21.833  86.724  1.00 58.64           N  
ANISOU 5803  N   GLU B 140     6786   8549   6944    319   -339   -316       N  
ATOM   5804  CA  GLU B 140      45.405  22.532  88.002  1.00 60.23           C  
ANISOU 5804  CA  GLU B 140     7008   8822   7056    352   -154   -346       C  
ATOM   5805  C   GLU B 140      46.813  22.843  88.452  1.00 59.87           C  
ANISOU 5805  C   GLU B 140     7173   8783   6793    379   -197   -331       C  
ATOM   5806  O   GLU B 140      47.022  23.729  89.260  1.00 61.16           O  
ANISOU 5806  O   GLU B 140     7406   8992   6838    403   -111   -398       O  
ATOM   5807  CB  GLU B 140      44.629  21.739  89.042  1.00 62.14           C  
ANISOU 5807  CB  GLU B 140     7200   9109   7301    235     60   -297       C  
ATOM   5808  CG  GLU B 140      43.090  21.705  88.802  1.00 66.62           C  
ANISOU 5808  CG  GLU B 140     7474   9672   8168    209    156   -335       C  
ATOM   5809  CD  GLU B 140      42.279  22.960  89.300  1.00 69.64           C  
ANISOU 5809  CD  GLU B 140     7684  10074   8701    306    362   -460       C  
ATOM   5810  OE1 GLU B 140      42.788  24.101  89.382  1.00 69.66           O  
ANISOU 5810  OE1 GLU B 140     7773  10065   8629    423    357   -549       O  
ATOM   5811  OE2 GLU B 140      41.072  22.807  89.581  1.00 76.02           O  
ANISOU 5811  OE2 GLU B 140     8237  10880   9768    264    553   -482       O  
ATOM   5812  N   ILE B 141      47.777  22.103  87.926  1.00 58.41           N  
ANISOU 5812  N   ILE B 141     7074   8533   6588    363   -324   -258       N  
ATOM   5813  CA  ILE B 141      49.129  22.312  88.243  1.00 56.86           C  
ANISOU 5813  CA  ILE B 141     7001   8321   6283    388   -397   -222       C  
ATOM   5814  C   ILE B 141      49.605  23.330  87.292  1.00 56.23           C  
ANISOU 5814  C   ILE B 141     6921   8201   6243    473   -471   -310       C  
ATOM   5815  O   ILE B 141      50.499  24.079  87.630  1.00 57.05           O  
ANISOU 5815  O   ILE B 141     7088   8308   6282    500   -507   -332       O  
ATOM   5816  CB  ILE B 141      50.031  21.073  87.937  1.00 57.00           C  
ANISOU 5816  CB  ILE B 141     7051   8228   6377    361   -470   -107       C  
ATOM   5817  CG1 ILE B 141      49.614  19.802  88.698  1.00 59.49           C  
ANISOU 5817  CG1 ILE B 141     7378   8523   6703    266   -419     35       C  
ATOM   5818  CG2 ILE B 141      51.445  21.372  88.375  1.00 58.02           C  
ANISOU 5818  CG2 ILE B 141     7236   8338   6472    393   -569    -48       C  
ATOM   5819  CD1 ILE B 141      49.155  20.031  90.136  1.00 60.30           C  
ANISOU 5819  CD1 ILE B 141     7556   8755   6598    187   -334     97       C  
ATOM   5820  N   ALA B 142      49.118  23.328  86.045  1.00 55.74           N  
ANISOU 5820  N   ALA B 142     6813   8090   6276    489   -519   -347       N  
ATOM   5821  CA  ALA B 142      49.701  24.283  85.102  1.00 54.29           C  
ANISOU 5821  CA  ALA B 142     6684   7857   6087    544   -586   -391       C  
ATOM   5822  C   ALA B 142      49.247  25.730  85.359  1.00 54.88           C  
ANISOU 5822  C   ALA B 142     6720   7949   6183    621   -582   -445       C  
ATOM   5823  O   ALA B 142      50.034  26.633  85.207  1.00 54.96           O  
ANISOU 5823  O   ALA B 142     6797   7913   6172    657   -599   -469       O  
ATOM   5824  CB  ALA B 142      49.440  23.905  83.752  1.00 54.40           C  
ANISOU 5824  CB  ALA B 142     6735   7819   6117    501   -656   -398       C  
ATOM   5825  N   ARG B 143      48.003  25.923  85.796  1.00 55.66           N  
ANISOU 5825  N   ARG B 143     6691   8086   6372    643   -528   -469       N  
ATOM   5826  CA  ARG B 143      47.455  27.223  86.023  1.00 56.00           C  
ANISOU 5826  CA  ARG B 143     6660   8092   6524    736   -483   -535       C  
ATOM   5827  C   ARG B 143      48.020  27.792  87.302  1.00 57.37           C  
ANISOU 5827  C   ARG B 143     6929   8288   6580    730   -339   -632       C  
ATOM   5828  O   ARG B 143      47.980  29.003  87.518  1.00 57.59           O  
ANISOU 5828  O   ARG B 143     6961   8243   6677    797   -282   -727       O  
ATOM   5829  CB  ARG B 143      45.948  27.144  86.137  1.00 57.68           C  
ANISOU 5829  CB  ARG B 143     6651   8315   6950    763   -428   -540       C  
ATOM   5830  CG  ARG B 143      45.391  26.377  87.324  1.00 58.27           C  
ANISOU 5830  CG  ARG B 143     6669   8474   6997    689   -212   -575       C  
ATOM   5831  CD  ARG B 143      43.967  25.921  86.969  1.00 61.91           C  
ANISOU 5831  CD  ARG B 143     6860   8932   7731    677   -214   -538       C  
ATOM   5832  NE  ARG B 143      43.094  27.088  86.875  1.00 65.03           N  
ANISOU 5832  NE  ARG B 143     7036   9241   8431    811   -174   -589       N  
ATOM   5833  CZ  ARG B 143      42.201  27.463  87.794  1.00 66.82           C  
ANISOU 5833  CZ  ARG B 143     7078   9447   8863    851    118   -692       C  
ATOM   5834  NH1 ARG B 143      41.965  26.745  88.893  1.00 62.03           N  
ANISOU 5834  NH1 ARG B 143     6504   8928   8135    735    404   -746       N  
ATOM   5835  NH2 ARG B 143      41.498  28.556  87.572  1.00 70.21           N  
ANISOU 5835  NH2 ARG B 143     7281   9744   9650   1003    139   -730       N  
ATOM   5836  N   ARG B 144      48.557  26.920  88.151  1.00 56.62           N  
ANISOU 5836  N   ARG B 144     6929   8277   6306    633   -301   -603       N  
ATOM   5837  CA  ARG B 144      49.108  27.378  89.398  1.00 57.25           C  
ANISOU 5837  CA  ARG B 144     7148   8402   6202    574   -223   -682       C  
ATOM   5838  C   ARG B 144      50.612  27.596  89.279  1.00 56.00           C  
ANISOU 5838  C   ARG B 144     7095   8216   5967    547   -388   -648       C  
ATOM   5839  O   ARG B 144      51.223  28.251  90.093  1.00 56.87           O  
ANISOU 5839  O   ARG B 144     7320   8340   5948    488   -399   -726       O  
ATOM   5840  CB  ARG B 144      48.759  26.401  90.562  1.00 58.89           C  
ANISOU 5840  CB  ARG B 144     7425   8723   6229    453   -109   -633       C  
ATOM   5841  CG  ARG B 144      47.366  26.623  91.144  1.00 58.19           C  
ANISOU 5841  CG  ARG B 144     7253   8658   6198    449    166   -741       C  
ATOM   5842  CD  ARG B 144      46.944  25.494  92.062  1.00 59.36           C  
ANISOU 5842  CD  ARG B 144     7467   8905   6180    305    301   -649       C  
ATOM   5843  NE  ARG B 144      45.612  25.718  92.610  1.00 61.63           N  
ANISOU 5843  NE  ARG B 144     7647   9206   6562    288    635   -767       N  
ATOM   5844  CZ  ARG B 144      44.467  25.504  91.949  1.00 62.53           C  
ANISOU 5844  CZ  ARG B 144     7470   9271   7019    356    712   -760       C  
ATOM   5845  NH1 ARG B 144      44.474  25.056  90.709  1.00 60.41           N  
ANISOU 5845  NH1 ARG B 144     7049   8951   6952    422    455   -650       N  
ATOM   5846  NH2 ARG B 144      43.301  25.767  92.519  1.00 65.72           N  
ANISOU 5846  NH2 ARG B 144     7728   9668   7576    345   1053   -877       N  
ATOM   5847  N   HIS B 145      51.212  27.054  88.249  1.00 54.70           N  
ANISOU 5847  N   HIS B 145     6886   8000   5897    572   -503   -548       N  
ATOM   5848  CA  HIS B 145      52.665  27.179  88.069  1.00 53.83           C  
ANISOU 5848  CA  HIS B 145     6811   7842   5802    548   -617   -510       C  
ATOM   5849  C   HIS B 145      52.865  27.394  86.551  1.00 52.21           C  
ANISOU 5849  C   HIS B 145     6570   7534   5733    605   -621   -497       C  
ATOM   5850  O   HIS B 145      53.173  26.478  85.850  1.00 51.27           O  
ANISOU 5850  O   HIS B 145     6432   7383   5667    595   -622   -434       O  
ATOM   5851  CB  HIS B 145      53.368  25.894  88.497  1.00 52.88           C  
ANISOU 5851  CB  HIS B 145     6678   7745   5669    491   -701   -371       C  
ATOM   5852  CG  HIS B 145      53.174  25.536  89.930  1.00 56.46           C  
ANISOU 5852  CG  HIS B 145     7222   8306   5925    398   -727   -324       C  
ATOM   5853  ND1 HIS B 145      54.180  25.650  90.859  1.00 58.96           N  
ANISOU 5853  ND1 HIS B 145     7608   8657   6136    308   -894   -266       N  
ATOM   5854  CD2 HIS B 145      52.105  25.024  90.599  1.00 57.19           C  
ANISOU 5854  CD2 HIS B 145     7364   8479   5889    350   -613   -309       C  
ATOM   5855  CE1 HIS B 145      53.728  25.273  92.048  1.00 56.60           C  
ANISOU 5855  CE1 HIS B 145     7451   8468   5585    198   -891   -216       C  
ATOM   5856  NE2 HIS B 145      52.477  24.893  91.917  1.00 56.55           N  
ANISOU 5856  NE2 HIS B 145     7433   8486   5567    224   -686   -247       N  
ATOM   5857  N   PRO B 146      52.698  28.626  86.063  1.00 52.60           N  
ANISOU 5857  N   PRO B 146     6642   7516   5829    649   -607   -558       N  
ATOM   5858  CA  PRO B 146      52.755  28.992  84.657  1.00 51.48           C  
ANISOU 5858  CA  PRO B 146     6529   7284   5748    673   -619   -518       C  
ATOM   5859  C   PRO B 146      54.107  28.745  83.921  1.00 51.88           C  
ANISOU 5859  C   PRO B 146     6614   7266   5831    619   -589   -482       C  
ATOM   5860  O   PRO B 146      54.173  28.919  82.716  1.00 51.47           O  
ANISOU 5860  O   PRO B 146     6643   7149   5764    600   -557   -449       O  
ATOM   5861  CB  PRO B 146      52.445  30.453  84.699  1.00 52.13           C  
ANISOU 5861  CB  PRO B 146     6630   7280   5895    725   -618   -568       C  
ATOM   5862  CG  PRO B 146      53.104  30.912  86.023  1.00 53.85           C  
ANISOU 5862  CG  PRO B 146     6864   7514   6082    681   -593   -674       C  
ATOM   5863  CD  PRO B 146      52.837  29.802  86.955  1.00 53.87           C  
ANISOU 5863  CD  PRO B 146     6845   7655   5969    642   -588   -668       C  
ATOM   5864  N   TYR B 147      55.156  28.308  84.617  1.00 52.19           N  
ANISOU 5864  N   TYR B 147     6590   7314   5927    583   -596   -476       N  
ATOM   5865  CA  TYR B 147      56.412  27.939  83.974  1.00 52.11           C  
ANISOU 5865  CA  TYR B 147     6534   7215   6050    547   -522   -447       C  
ATOM   5866  C   TYR B 147      56.744  26.510  84.132  1.00 52.17           C  
ANISOU 5866  C   TYR B 147     6458   7217   6146    550   -504   -398       C  
ATOM   5867  O   TYR B 147      57.856  26.112  83.797  1.00 52.74           O  
ANISOU 5867  O   TYR B 147     6433   7190   6416    539   -422   -380       O  
ATOM   5868  CB  TYR B 147      57.558  28.705  84.598  1.00 53.39           C  
ANISOU 5868  CB  TYR B 147     6613   7336   6339    504   -576   -458       C  
ATOM   5869  CG  TYR B 147      57.432  30.165  84.307  1.00 56.52           C  
ANISOU 5869  CG  TYR B 147     7095   7669   6711    489   -558   -512       C  
ATOM   5870  CD1 TYR B 147      56.747  30.995  85.176  1.00 57.16           C  
ANISOU 5870  CD1 TYR B 147     7230   7783   6705    503   -636   -585       C  
ATOM   5871  CD2 TYR B 147      57.953  30.720  83.101  1.00 56.57           C  
ANISOU 5871  CD2 TYR B 147     7153   7556   6786    453   -422   -490       C  
ATOM   5872  CE1 TYR B 147      56.629  32.366  84.893  1.00 60.30           C  
ANISOU 5872  CE1 TYR B 147     7699   8064   7147    503   -607   -633       C  
ATOM   5873  CE2 TYR B 147      57.821  32.055  82.814  1.00 55.45           C  
ANISOU 5873  CE2 TYR B 147     7102   7320   6646    437   -415   -498       C  
ATOM   5874  CZ  TYR B 147      57.158  32.866  83.714  1.00 59.85           C  
ANISOU 5874  CZ  TYR B 147     7682   7882   7176    474   -519   -568       C  
ATOM   5875  OH  TYR B 147      57.014  34.191  83.472  1.00 66.37           O  
ANISOU 5875  OH  TYR B 147     8587   8564   8067    472   -503   -580       O  
ATOM   5876  N   PHE B 148      55.813  25.716  84.657  1.00 55.43           N  
ANISOU 5876  N   PHE B 148     6473   7523   7063    339    228    176       N  
ATOM   5877  CA  PHE B 148      56.152  24.342  84.937  1.00 55.54           C  
ANISOU 5877  CA  PHE B 148     6489   7527   7087    339    215    227       C  
ATOM   5878  C   PHE B 148      56.678  23.642  83.669  1.00 56.26           C  
ANISOU 5878  C   PHE B 148     6616   7553   7205    336    150    195       C  
ATOM   5879  O   PHE B 148      56.162  23.826  82.561  1.00 57.19           O  
ANISOU 5879  O   PHE B 148     6754   7616   7359    296     99    162       O  
ATOM   5880  CB  PHE B 148      54.973  23.618  85.524  1.00 56.47           C  
ANISOU 5880  CB  PHE B 148     6558   7614   7285    316    253    297       C  
ATOM   5881  CG  PHE B 148      55.342  22.335  86.239  1.00 57.38           C  
ANISOU 5881  CG  PHE B 148     6698   7718   7385    310    255    370       C  
ATOM   5882  CD1 PHE B 148      55.675  21.197  85.528  1.00 52.46           C  
ANISOU 5882  CD1 PHE B 148     6107   7011   6814    317    200    383       C  
ATOM   5883  CD2 PHE B 148      55.330  22.271  87.628  1.00 55.35           C  
ANISOU 5883  CD2 PHE B 148     6456   7519   7056    285    318    427       C  
ATOM   5884  CE1 PHE B 148      55.986  20.070  86.148  1.00 54.11           C  
ANISOU 5884  CE1 PHE B 148     6344   7184   7033    325    198    460       C  
ATOM   5885  CE2 PHE B 148      55.659  21.129  88.233  1.00 58.05           C  
ANISOU 5885  CE2 PHE B 148     6829   7840   7388    273    294    515       C  
ATOM   5886  CZ  PHE B 148      56.005  20.009  87.492  1.00 57.15           C  
ANISOU 5886  CZ  PHE B 148     6729   7630   7355    306    230    538       C  
ATOM   5887  N   TYR B 149      57.763  22.903  83.813  1.00 56.66           N  
ANISOU 5887  N   TYR B 149     6684   7606   7237    373    157    206       N  
ATOM   5888  CA  TYR B 149      58.295  22.100  82.722  1.00 56.96           C  
ANISOU 5888  CA  TYR B 149     6772   7558   7314    380    150    163       C  
ATOM   5889  C   TYR B 149      57.228  21.229  82.069  1.00 56.46           C  
ANISOU 5889  C   TYR B 149     6757   7379   7317    320    124    170       C  
ATOM   5890  O   TYR B 149      56.772  20.281  82.664  1.00 57.09           O  
ANISOU 5890  O   TYR B 149     6830   7411   7449    320    131    239       O  
ATOM   5891  CB  TYR B 149      59.330  21.167  83.309  1.00 58.72           C  
ANISOU 5891  CB  TYR B 149     6968   7770   7571    456    178    217       C  
ATOM   5892  CG  TYR B 149      60.379  20.697  82.351  1.00 59.31           C  
ANISOU 5892  CG  TYR B 149     7066   7781   7686    501    225    154       C  
ATOM   5893  CD1 TYR B 149      60.546  21.291  81.088  1.00 54.98           C  
ANISOU 5893  CD1 TYR B 149     6582   7219   7090    450    247     40       C  
ATOM   5894  CD2 TYR B 149      61.241  19.675  82.743  1.00 59.38           C  
ANISOU 5894  CD2 TYR B 149     7034   7739   7789    597    258    218       C  
ATOM   5895  CE1 TYR B 149      61.577  20.856  80.244  1.00 57.91           C  
ANISOU 5895  CE1 TYR B 149     6979   7530   7492    485    336    -32       C  
ATOM   5896  CE2 TYR B 149      62.229  19.223  81.930  1.00 60.94           C  
ANISOU 5896  CE2 TYR B 149     7232   7866   8058    661    343    159       C  
ATOM   5897  CZ  TYR B 149      62.400  19.796  80.691  1.00 61.96           C  
ANISOU 5897  CZ  TYR B 149     7429   7985   8127    603    399     24       C  
ATOM   5898  OH  TYR B 149      63.414  19.266  79.954  1.00 64.60           O  
ANISOU 5898  OH  TYR B 149     7765   8240   8541    669    526    -41       O  
ATOM   5899  N   ALA B 150      56.848  21.525  80.841  1.00 55.90           N  
ANISOU 5899  N   ALA B 150     6750   7260   7230    244     81    109       N  
ATOM   5900  CA  ALA B 150      55.678  20.865  80.290  1.00 57.01           C  
ANISOU 5900  CA  ALA B 150     6930   7312   7418    144     20    137       C  
ATOM   5901  C   ALA B 150      55.878  19.339  80.098  1.00 57.82           C  
ANISOU 5901  C   ALA B 150     7130   7284   7553    129     59    134       C  
ATOM   5902  O   ALA B 150      55.045  18.568  80.544  1.00 58.95           O  
ANISOU 5902  O   ALA B 150     7261   7383   7753     88     39    206       O  
ATOM   5903  CB  ALA B 150      55.201  21.562  79.031  1.00 56.28           C  
ANISOU 5903  CB  ALA B 150     6896   7202   7286     35    -72     99       C  
ATOM   5904  N   PRO B 151      56.985  18.911  79.465  1.00 57.62           N  
ANISOU 5904  N   PRO B 151     7201   7188   7503    165    134     50       N  
ATOM   5905  CA  PRO B 151      57.070  17.460  79.349  1.00 59.72           C  
ANISOU 5905  CA  PRO B 151     7571   7295   7824    164    190     49       C  
ATOM   5906  C   PRO B 151      57.120  16.713  80.685  1.00 60.05           C  
ANISOU 5906  C   PRO B 151     7534   7332   7951    261    209    162       C  
ATOM   5907  O   PRO B 151      56.593  15.558  80.770  1.00 61.92           O  
ANISOU 5907  O   PRO B 151     7852   7437   8237    214    211    202       O  
ATOM   5908  CB  PRO B 151      58.344  17.209  78.487  1.00 59.88           C  
ANISOU 5908  CB  PRO B 151     7689   7232   7831    215    314    -69       C  
ATOM   5909  CG  PRO B 151      58.996  18.496  78.273  1.00 56.23           C  
ANISOU 5909  CG  PRO B 151     7154   6909   7301    239    315   -115       C  
ATOM   5910  CD  PRO B 151      58.089  19.603  78.765  1.00 57.03           C  
ANISOU 5910  CD  PRO B 151     7157   7148   7364    193    189    -47       C  
ATOM   5911  N   GLU B 152      57.672  17.349  81.709  1.00 58.72           N  
ANISOU 5911  N   GLU B 152     7232   7296   7781    360    210    220       N  
ATOM   5912  CA  GLU B 152      57.840  16.667  82.992  1.00 60.47           C  
ANISOU 5912  CA  GLU B 152     7402   7518   8055    429    212    343       C  
ATOM   5913  C   GLU B 152      56.520  16.505  83.661  1.00 60.58           C  
ANISOU 5913  C   GLU B 152     7401   7553   8063    335    168    421       C  
ATOM   5914  O   GLU B 152      56.326  15.547  84.415  1.00 61.96           O  
ANISOU 5914  O   GLU B 152     7598   7664   8279    335    169    517       O  
ATOM   5915  CB  GLU B 152      58.738  17.420  83.963  1.00 61.48           C  
ANISOU 5915  CB  GLU B 152     7414   7795   8149    513    202    398       C  
ATOM   5916  CG  GLU B 152      59.399  16.518  85.014  1.00 65.84           C  
ANISOU 5916  CG  GLU B 152     7936   8315   8766    594    189    533       C  
ATOM   5917  CD  GLU B 152      60.174  15.361  84.374  1.00 72.69           C  
ANISOU 5917  CD  GLU B 152     8850   9002   9769    694    248    523       C  
ATOM   5918  OE1 GLU B 152      61.410  15.543  84.139  1.00 76.51           O  
ANISOU 5918  OE1 GLU B 152     9254   9506  10309    801    284    508       O  
ATOM   5919  OE2 GLU B 152      59.554  14.285  84.075  1.00 74.61           O  
ANISOU 5919  OE2 GLU B 152     9207   9072  10067    662    272    525       O  
ATOM   5920  N   LEU B 153      55.608  17.436  83.346  1.00 58.47           N  
ANISOU 5920  N   LEU B 153     7089   7367   7760    255    135    387       N  
ATOM   5921  CA  LEU B 153      54.292  17.455  83.875  1.00 56.81           C  
ANISOU 5921  CA  LEU B 153     6821   7192   7573    169    116    455       C  
ATOM   5922  C   LEU B 153      53.485  16.331  83.297  1.00 58.61           C  
ANISOU 5922  C   LEU B 153     7128   7288   7853     57     80    477       C  
ATOM   5923  O   LEU B 153      52.793  15.665  84.019  1.00 61.10           O  
ANISOU 5923  O   LEU B 153     7427   7586   8201      2     88    564       O  
ATOM   5924  CB  LEU B 153      53.658  18.806  83.636  1.00 55.38           C  
ANISOU 5924  CB  LEU B 153     6546   7114   7381    145     96    423       C  
ATOM   5925  CG  LEU B 153      52.242  18.979  84.173  1.00 55.21           C  
ANISOU 5925  CG  LEU B 153     6414   7137   7427     76    105    496       C  
ATOM   5926  CD1 LEU B 153      52.151  18.646  85.659  1.00 54.59           C  
ANISOU 5926  CD1 LEU B 153     6309   7106   7328     90    194    570       C  
ATOM   5927  CD2 LEU B 153      51.699  20.371  83.927  1.00 52.05           C  
ANISOU 5927  CD2 LEU B 153     5907   6811   7057     91     99    472       C  
ATOM   5928  N   LEU B 154      53.583  16.042  82.018  1.00 59.57           N  
ANISOU 5928  N   LEU B 154     7360   7308   7964     -3     47    399       N  
ATOM   5929  CA  LEU B 154      52.892  14.829  81.517  1.00 60.81           C  
ANISOU 5929  CA  LEU B 154     7640   7316   8148   -139     14    418       C  
ATOM   5930  C   LEU B 154      53.303  13.570  82.273  1.00 61.59           C  
ANISOU 5930  C   LEU B 154     7817   7295   8288    -87     75    475       C  
ATOM   5931  O   LEU B 154      52.445  12.711  82.604  1.00 61.50           O  
ANISOU 5931  O   LEU B 154     7842   7219   8308   -198     51    553       O  
ATOM   5932  CB  LEU B 154      53.132  14.612  80.016  1.00 61.52           C  
ANISOU 5932  CB  LEU B 154     7905   7287   8183   -231     -8    305       C  
ATOM   5933  CG  LEU B 154      52.648  15.772  79.136  1.00 61.05           C  
ANISOU 5933  CG  LEU B 154     7799   7324   8073   -320   -107    273       C  
ATOM   5934  CD1 LEU B 154      53.212  15.647  77.746  1.00 60.33           C  
ANISOU 5934  CD1 LEU B 154     7915   7125   7884   -404   -100    148       C  
ATOM   5935  CD2 LEU B 154      51.127  15.830  79.116  1.00 58.17           C  
ANISOU 5935  CD2 LEU B 154     7335   7005   7760   -480   -235    378       C  
ATOM   5936  N   TYR B 155      54.617  13.459  82.527  1.00 61.40           N  
ANISOU 5936  N   TYR B 155     7812   7240   8276     76    144    452       N  
ATOM   5937  CA  TYR B 155      55.141  12.392  83.383  1.00 61.29           C  
ANISOU 5937  CA  TYR B 155     7842   7120   8325    159    182    543       C  
ATOM   5938  C   TYR B 155      54.388  12.329  84.714  1.00 61.49           C  
ANISOU 5938  C   TYR B 155     7784   7240   8341    109    148    682       C  
ATOM   5939  O   TYR B 155      53.861  11.289  85.063  1.00 63.11           O  
ANISOU 5939  O   TYR B 155     8071   7333   8577     33    141    760       O  
ATOM   5940  CB  TYR B 155      56.639  12.552  83.620  1.00 61.13           C  
ANISOU 5940  CB  TYR B 155     7774   7108   8345    350    233    538       C  
ATOM   5941  CG  TYR B 155      57.128  11.658  84.706  1.00 61.59           C  
ANISOU 5941  CG  TYR B 155     7830   7094   8478    439    228    683       C  
ATOM   5942  CD1 TYR B 155      57.211  10.278  84.518  1.00 64.54           C  
ANISOU 5942  CD1 TYR B 155     8347   7226   8947    456    265    713       C  
ATOM   5943  CD2 TYR B 155      57.473  12.176  85.941  1.00 61.36           C  
ANISOU 5943  CD2 TYR B 155     7679   7223   8412    486    177    799       C  
ATOM   5944  CE1 TYR B 155      57.621   9.426  85.567  1.00 68.31           C  
ANISOU 5944  CE1 TYR B 155     8828   7620   9505    536    236    878       C  
ATOM   5945  CE2 TYR B 155      57.879  11.343  86.991  1.00 65.09           C  
ANISOU 5945  CE2 TYR B 155     8163   7634   8937    539    136    965       C  
ATOM   5946  CZ  TYR B 155      57.950   9.975  86.799  1.00 68.21           C  
ANISOU 5946  CZ  TYR B 155     8682   7787   9448    572    159   1013       C  
ATOM   5947  OH  TYR B 155      58.373   9.168  87.831  1.00 72.24           O  
ANISOU 5947  OH  TYR B 155     9205   8223  10021    628     98   1200       O  
ATOM   5948  N   TYR B 156      54.317  13.435  85.456  1.00 60.28           N  
ANISOU 5948  N   TYR B 156     7490   7281   8132    134    144    707       N  
ATOM   5949  CA  TYR B 156      53.599  13.435  86.749  1.00 60.43           C  
ANISOU 5949  CA  TYR B 156     7451   7391   8118     68    152    821       C  
ATOM   5950  C   TYR B 156      52.143  13.098  86.623  1.00 61.53           C  
ANISOU 5950  C   TYR B 156     7577   7516   8287    -95    148    849       C  
ATOM   5951  O   TYR B 156      51.569  12.516  87.546  1.00 62.24           O  
ANISOU 5951  O   TYR B 156     7675   7605   8369   -176    170    952       O  
ATOM   5952  CB  TYR B 156      53.680  14.766  87.468  1.00 59.30           C  
ANISOU 5952  CB  TYR B 156     7193   7441   7899     99    181    811       C  
ATOM   5953  CG  TYR B 156      55.044  15.066  87.999  1.00 59.97           C  
ANISOU 5953  CG  TYR B 156     7278   7575   7935    214    167    834       C  
ATOM   5954  CD1 TYR B 156      55.765  14.108  88.669  1.00 63.03           C  
ANISOU 5954  CD1 TYR B 156     7724   7887   8339    257    131    950       C  
ATOM   5955  CD2 TYR B 156      55.627  16.301  87.796  1.00 59.40           C  
ANISOU 5955  CD2 TYR B 156     7141   7618   7808    272    173    754       C  
ATOM   5956  CE1 TYR B 156      57.040  14.374  89.137  1.00 65.35           C  
ANISOU 5956  CE1 TYR B 156     7985   8236   8610    353     87   1001       C  
ATOM   5957  CE2 TYR B 156      56.859  16.569  88.268  1.00 61.16           C  
ANISOU 5957  CE2 TYR B 156     7350   7899   7990    349    143    788       C  
ATOM   5958  CZ  TYR B 156      57.564  15.598  88.926  1.00 62.23           C  
ANISOU 5958  CZ  TYR B 156     7516   7972   8155    389     94    917       C  
ATOM   5959  OH  TYR B 156      58.793  15.864  89.410  1.00 66.20           O  
ANISOU 5959  OH  TYR B 156     7974