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***  HYDROLASE/IMMUNE SYSTEM 30-NOV-15 5F1O  ***

elNémo ID: 21041521351190351

Job options:

ID        	=	 21041521351190351
JOBID     	=	 HYDROLASE/IMMUNE SYSTEM 30-NOV-15 5F1O
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 3
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER    HYDROLASE/IMMUNE SYSTEM                 30-NOV-15   5F1O              
TITLE     HUMAN CD38 IN COMPLEX WITH NANOBODY MU551                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ADP-RIBOSYL CYCLASE/CYCLIC ADP-RIBOSE HYDROLASE 1;         
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: ECTODOMAIN, UNP RESIDUES 46-300;                           
COMPND   5 SYNONYM: CD38;                                                       
COMPND   6 EC: 3.2.2.6;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: NANOBODY MU551;                                            
COMPND  11 CHAIN: B;                                                            
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CD38;                                                          
SOURCE   6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: PICHIA PASTORIS;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: X33;                                       
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PPICZALPHA;                               
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: LAMA GLAMA;                                     
SOURCE  14 ORGANISM_TAXID: 9844;                                                
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PHEN2                                     
KEYWDS    CD38, ADP-RIBOSYL CYCLASE, CYCLIC ADP-RIBOSE, X-CRYSTALLOGRAPHY,      
KEYWDS   2 CALCIUM SIGNALING, NANOBODY, MU551, HYDROLASE-IMMUNE SYSTEM COMPLEX  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.ZHANG,Q.HAO                                                         
REVDAT   1   15-JUN-16 5F1O    0                                                
JRNL        AUTH   T.LI,S.QI,M.UNGER,Y.N.HOU,Q.W.DENG,J.LIU,C.M.LAM,X.W.WANG,   
JRNL        AUTH 2 D.XIN,P.ZHANG,F.KOCH-NOLTE,Q.HAO,H.ZHANG,H.C.LEE,Y.J.ZHAO    
JRNL        TITL   IMMUNO-TARGETING THE MULTIFUNCTIONAL CD38 USING NANOBODY     
JRNL        REF    SCI REP                       V.   6 27055 2016              
JRNL        REFN                   ESSN 2045-2322                               
JRNL        PMID   27251573                                                     
JRNL        DOI    10.1038/SREP27055                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0135                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 22212                          
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) : 0.171                           
REMARK   3   R VALUE            (WORKING SET) : 0.168                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1200                            
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.25                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1257                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 77.02                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1660                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 77                           
REMARK   3   BIN FREE R VALUE                    : 0.2470                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2958                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 207                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.51                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.06000                                              
REMARK   3    B22 (A**2) : 0.94000                                              
REMARK   3    B33 (A**2) : -0.99000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.202         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.131         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.517        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.916                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3035 ; 0.009 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2769 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4112 ; 1.305 ; 1.934       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6382 ; 0.918 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   365 ; 6.191 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   149 ;38.336 ;23.893       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   513 ;13.670 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    21 ;16.052 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   436 ; 0.081 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3435 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   730 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1472 ; 1.071 ; 1.710       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1471 ; 1.071 ; 1.710       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1833 ; 1.374 ; 2.555       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  5804 ; 0.951 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):    71 ;28.620 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  5863 ; 4.490 ; 5.000       
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  : 16                                         
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    49        A    75                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.5710   0.7090 140.2600              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1411 T22:   0.0456                                     
REMARK   3      T33:   0.1952 T12:  -0.0724                                     
REMARK   3      T13:   0.0283 T23:  -0.0428                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5470 L22:   4.8249                                     
REMARK   3      L33:   3.7586 L12:  -3.4546                                     
REMARK   3      L13:  -2.5425 L23:   2.3747                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2082 S12:   0.0536 S13:  -0.3839                       
REMARK   3      S21:   0.1035 S22:  -0.0807 S23:   0.4398                       
REMARK   3      S31:   0.3755 S32:  -0.2170 S33:   0.2889                       
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    76        A    86                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.3820  -3.6850 143.1280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3655 T22:   0.1166                                     
REMARK   3      T33:   0.0877 T12:   0.1355                                     
REMARK   3      T13:   0.0231 T23:  -0.0158                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  15.6626 L22:   9.8890                                     
REMARK   3      L33:  20.1111 L12:  -7.2312                                     
REMARK   3      L13: -15.0367 L23:  13.0357                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7651 S12:  -0.1041 S13:  -0.4645                       
REMARK   3      S21:   0.5954 S22:   0.7248 S23:  -0.2278                       
REMARK   3      S31:   1.0020 S32:   0.7440 S33:   0.0403                       
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    87        A   117                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.5900  10.2120 146.7340              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0661 T22:   0.0616                                     
REMARK   3      T33:   0.1594 T12:   0.0011                                     
REMARK   3      T13:  -0.0118 T23:  -0.0147                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2895 L22:   4.5966                                     
REMARK   3      L33:   2.2978 L12:  -2.6294                                     
REMARK   3      L13:  -1.0833 L23:   1.8580                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1661 S12:  -0.0560 S13:   0.1297                       
REMARK   3      S21:   0.1547 S22:   0.1851 S23:  -0.3294                       
REMARK   3      S31:   0.1144 S32:   0.1964 S33:  -0.0190                       
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   118        A   138                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.0860   7.5980 122.5460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1311 T22:   0.0833                                     
REMARK   3      T33:   0.1049 T12:  -0.0337                                     
REMARK   3      T13:   0.0339 T23:  -0.0078                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1972 L22:   5.0072                                     
REMARK   3      L33:   3.3279 L12:  -1.0800                                     
REMARK   3      L13:  -0.0545 L23:   0.8820                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0304 S12:   0.0644 S13:  -0.0137                       
REMARK   3      S21:  -0.2091 S22:  -0.0255 S23:   0.2206                       
REMARK   3      S31:   0.1714 S32:  -0.1319 S33:  -0.0048                       
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   139        A   161                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.4860   4.4840 132.5600              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1148 T22:   0.0407                                     
REMARK   3      T33:   0.1663 T12:  -0.0350                                     
REMARK   3      T13:   0.0179 T23:  -0.0198                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3887 L22:   1.9012                                     
REMARK   3      L33:   5.3178 L12:  -1.0756                                     
REMARK   3      L13:  -1.3204 L23:   1.7068                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0207 S12:   0.1339 S13:  -0.0532                       
REMARK   3      S21:  -0.1573 S22:  -0.0291 S23:  -0.0324                       
REMARK   3      S31:   0.1592 S32:  -0.0269 S33:   0.0499                       
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   162        A   179                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.6000  14.4570 147.8580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0193 T22:   0.0984                                     
REMARK   3      T33:   0.1958 T12:  -0.0297                                     
REMARK   3      T13:   0.0233 T23:  -0.0742                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2559 L22:   9.6423                                     
REMARK   3      L33:   3.6771 L12:  -1.0899                                     
REMARK   3      L13:  -0.6498 L23:  -0.1619                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1470 S12:   0.0021 S13:  -0.1662                       
REMARK   3      S21:   0.1301 S22:  -0.2632 S23:   0.4209                       
REMARK   3      S31:   0.2130 S32:  -0.5461 S33:   0.4102                       
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   180        A   197                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.3070  15.1520 138.8220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0677 T22:   0.0733                                     
REMARK   3      T33:   0.2042 T12:  -0.0145                                     
REMARK   3      T13:   0.0011 T23:  -0.0182                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5843 L22:   1.4141                                     
REMARK   3      L33:   5.6199 L12:  -1.1807                                     
REMARK   3      L13:  -3.7331 L23:   1.0634                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0200 S12:  -0.1794 S13:   0.3285                       
REMARK   3      S21:  -0.0532 S22:   0.1005 S23:  -0.1711                       
REMARK   3      S31:  -0.0236 S32:   0.1807 S33:  -0.1206                       
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   198        A   225                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.3400  18.7750 123.1530              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0941 T22:   0.1096                                     
REMARK   3      T33:   0.1161 T12:  -0.0396                                     
REMARK   3      T13:   0.0769 T23:  -0.0260                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3301 L22:   1.7194                                     
REMARK   3      L33:   3.6684 L12:  -0.3952                                     
REMARK   3      L13:   2.4746 L23:  -0.5138                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1417 S12:  -0.4272 S13:   0.3473                       
REMARK   3      S21:  -0.0150 S22:  -0.0061 S23:   0.0854                       
REMARK   3      S31:  -0.2883 S32:  -0.3078 S33:  -0.1357                       
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   226        A   236                          
REMARK   3    ORIGIN FOR THE GROUP (A):  36.0120  19.4180 127.8280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0646 T22:   0.1207                                     
REMARK   3      T33:   0.1964 T12:  -0.0561                                     
REMARK   3      T13:  -0.0054 T23:  -0.0711                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  18.7131 L22:   5.2064                                     
REMARK   3      L33:   9.0795 L12:  -8.4470                                     
REMARK   3      L13:  -7.8237 L23:   3.9223                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3957 S12:  -0.3354 S13:   0.0749                       
REMARK   3      S21:   0.1578 S22:   0.3958 S23:  -0.5444                       
REMARK   3      S31:   0.2462 S32:   0.3315 S33:  -0.0001                       
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   237        A   276                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.8300  22.0830 115.4900              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1488 T22:   0.0711                                     
REMARK   3      T33:   0.1032 T12:  -0.0429                                     
REMARK   3      T13:   0.0749 T23:  -0.0186                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7382 L22:   1.7965                                     
REMARK   3      L33:   4.3977 L12:   0.3968                                     
REMARK   3      L13:   1.7848 L23:   0.5111                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0026 S12:   0.1489 S13:   0.0997                       
REMARK   3      S21:  -0.2782 S22:   0.0426 S23:   0.0296                       
REMARK   3      S31:  -0.4504 S32:   0.0320 S33:  -0.0452                       
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   277        A   296                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.8010   4.3420 108.5490              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3429 T22:   0.3167                                     
REMARK   3      T33:   0.0436 T12:  -0.0549                                     
REMARK   3      T13:   0.0045 T23:  -0.0909                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4272 L22:  23.1920                                     
REMARK   3      L33:   6.8898 L12:  -5.6867                                     
REMARK   3      L13:   1.6467 L23:  -6.9865                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1285 S12:   0.1583 S13:  -0.1013                       
REMARK   3      S21:  -0.6687 S22:  -0.2372 S23:   0.3012                       
REMARK   3      S31:   1.0833 S32:  -0.0086 S33:   0.1088                       
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 :   B     1        B    12                          
REMARK   3    ORIGIN FOR THE GROUP (A):  36.2260 -21.9550 111.7910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2289 T22:   0.1701                                     
REMARK   3      T33:   0.0815 T12:  -0.0557                                     
REMARK   3      T13:   0.0772 T23:  -0.0815                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  19.1939 L22:  22.6558                                     
REMARK   3      L33:   3.7733 L12: -16.9435                                     
REMARK   3      L13:   3.7176 L23:  -2.8369                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2212 S12:   0.4675 S13:   0.1630                       
REMARK   3      S21:  -0.3870 S22:  -0.3139 S23:   0.1805                       
REMARK   3      S31:  -0.1180 S32:   0.1229 S33:   0.0926                       
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 :   B    13        B    86                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.6130 -21.7230 122.0540              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2242 T22:   0.0356                                     
REMARK   3      T33:   0.0866 T12:  -0.0243                                     
REMARK   3      T13:   0.0635 T23:  -0.0448                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8012 L22:   4.1999                                     
REMARK   3      L33:   2.1665 L12:  -1.6231                                     
REMARK   3      L13:  -0.6498 L23:   1.0396                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1098 S12:  -0.0021 S13:  -0.1433                       
REMARK   3      S21:   0.3315 S22:   0.0108 S23:   0.1078                       
REMARK   3      S31:   0.3933 S32:   0.0919 S33:   0.0990                       
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    87        B   106                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.1070 -20.7530 121.7010              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2670 T22:   0.0373                                     
REMARK   3      T33:   0.1839 T12:  -0.0344                                     
REMARK   3      T13:   0.0950 T23:  -0.0640                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5766 L22:   6.6178                                     
REMARK   3      L33:   1.6043 L12:  -2.9439                                     
REMARK   3      L13:  -1.3204 L23:   2.5935                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1781 S12:   0.0985 S13:  -0.2593                       
REMARK   3      S21:   0.6459 S22:  -0.1030 S23:   0.4090                       
REMARK   3      S31:   0.3816 S32:  -0.0788 S33:   0.2811                       
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   113                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.8250 -18.0910 127.8450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3887 T22:   0.1109                                     
REMARK   3      T33:   0.4501 T12:  -0.1405                                     
REMARK   3      T13:  -0.0243 T23:  -0.0333                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  48.1826 L22:  14.7575                                     
REMARK   3      L33:  14.0395 L12:  19.3731                                     
REMARK   3      L13:  -7.0420 L23:   6.6874                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.8661 S12:   0.7367 S13:  -0.0871                       
REMARK   3      S21:  -0.9272 S22:  -0.1348 S23:   1.4085                       
REMARK   3      S31:  -0.0086 S32:  -0.6738 S33:   2.0009                       
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   114        B   128                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.2830 -27.2130 114.7870              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3043 T22:   0.0918                                     
REMARK   3      T33:   0.1717 T12:  -0.0732                                     
REMARK   3      T13:   0.0842 T23:  -0.0499                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.3495 L22:   6.3936                                     
REMARK   3      L33:   3.9291 L12:  -4.3596                                     
REMARK   3      L13:  -1.3170 L23:   3.3439                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0732 S12:   0.0994 S13:  -0.4979                       
REMARK   3      S21:   0.1732 S22:  -0.1600 S23:   0.5885                       
REMARK   3      S31:   0.2609 S32:  -0.1294 S33:   0.0867                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 5F1O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-DEC-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000215845.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-NOV-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97852                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24162                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 7.600                              
REMARK 200  R MERGE                    (I) : 0.07400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 13.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1YH3                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.79                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM ACETATE, 0.1M TRIS-HCL,      
REMARK 280  25% PEG4000, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE     
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       16.57050            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       71.62700            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       48.09500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       71.62700            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       16.57050            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       48.09500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     TRP A    46                                                      
REMARK 465     ARG A    47                                                      
REMARK 465     GLN A    48                                                      
REMARK 465     GLY A   246                                                      
REMARK 465     ARG A   247                                                      
REMARK 465     GLU A   248                                                      
REMARK 465     ASP A   249                                                      
REMARK 465     ASP A   293                                                      
REMARK 465     SER A   294                                                      
REMARK 465     SER A   295                                                      
REMARK 465     THR A   297                                                      
REMARK 465     SER A   298                                                      
REMARK 465     GLU A   299                                                      
REMARK 465     ILE A   300                                                      
REMARK 465     GLU B   129                                                      
REMARK 465     PRO B   130                                                      
REMARK 465     LYS B   131                                                      
REMARK 465     THR B   132                                                      
REMARK 465     PRO B   133                                                      
REMARK 465     LYS B   134                                                      
REMARK 465     PRO B   135                                                      
REMARK 465     GLN B   136                                                      
REMARK 465     PRO B   137                                                      
REMARK 465     ALA B   138                                                      
REMARK 465     ALA B   139                                                      
REMARK 465     ALA B   140                                                      
REMARK 465     HIS B   141                                                      
REMARK 465     HIS B   142                                                      
REMARK 465     HIS B   143                                                      
REMARK 465     HIS B   144                                                      
REMARK 465     HIS B   145                                                      
REMARK 465     HIS B   146                                                      
REMARK 465     GLY B   147                                                      
REMARK 465     ALA B   148                                                      
REMARK 465     ALA B   149                                                      
REMARK 465     GLU B   150                                                      
REMARK 465     GLN B   151                                                      
REMARK 465     LYS B   152                                                      
REMARK 465     LEU B   153                                                      
REMARK 465     ILE B   154                                                      
REMARK 465     SER B   155                                                      
REMARK 465     GLU B   156                                                      
REMARK 465     GLU B   157                                                      
REMARK 465     ASP B   158                                                      
REMARK 465     LEU B   159                                                      
REMARK 465     ASN B   160                                                      
REMARK 465     GLY B   161                                                      
REMARK 465     ALA B   162                                                      
REMARK 465     ALA B   163                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ILE A 128       50.37   -150.20                                   
REMARK 500    ASP A 179      -71.49   -105.03                                   
REMARK 500    ASN A 182       58.44    -92.30                                   
REMARK 500    ASP A 202     -118.32     59.62                                   
REMARK 500    VAL A 225      -62.30   -123.29                                   
REMARK 500    SER B  55       16.77     59.76                                   
REMARK 500    ALA B  92      167.51    179.17                                   
REMARK 500    TYR B 104       74.97   -104.96                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 560        DISTANCE =  6.51 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5F1K   RELATED DB: PDB                                   
REMARK 900 HUMAN CD38 IN COMPLEX WITH NANOBODY MU1053                           
REMARK 900 RELATED ID: 5F21   RELATED DB: PDB                                   
REMARK 900 HUMAN CD38 IN COMPLEX WITH NANOBODY MU375                            
DBREF  5F1O A   46   300  UNP    P28907   CD38_HUMAN      46    300             
DBREF  5F1O B    1   163  PDB    5F1O     5F1O             1    163             
SEQADV 5F1O THR A   49  UNP  P28907    GLN    49 ENGINEERED MUTATION            
SEQADV 5F1O ASP A  100  UNP  P28907    ASN   100 ENGINEERED MUTATION            
SEQADV 5F1O ASP A  164  UNP  P28907    ASN   164 ENGINEERED MUTATION            
SEQADV 5F1O ASP A  209  UNP  P28907    ASN   209 ENGINEERED MUTATION            
SEQADV 5F1O ASP A  219  UNP  P28907    ASN   219 ENGINEERED MUTATION            
SEQRES   1 A  255  TRP ARG GLN THR TRP SER GLY PRO GLY THR THR LYS ARG          
SEQRES   2 A  255  PHE PRO GLU THR VAL LEU ALA ARG CYS VAL LYS TYR THR          
SEQRES   3 A  255  GLU ILE HIS PRO GLU MET ARG HIS VAL ASP CYS GLN SER          
SEQRES   4 A  255  VAL TRP ASP ALA PHE LYS GLY ALA PHE ILE SER LYS HIS          
SEQRES   5 A  255  PRO CYS ASP ILE THR GLU GLU ASP TYR GLN PRO LEU MET          
SEQRES   6 A  255  LYS LEU GLY THR GLN THR VAL PRO CYS ASN LYS ILE LEU          
SEQRES   7 A  255  LEU TRP SER ARG ILE LYS ASP LEU ALA HIS GLN PHE THR          
SEQRES   8 A  255  GLN VAL GLN ARG ASP MET PHE THR LEU GLU ASP THR LEU          
SEQRES   9 A  255  LEU GLY TYR LEU ALA ASP ASP LEU THR TRP CYS GLY GLU          
SEQRES  10 A  255  PHE ASP THR SER LYS ILE ASN TYR GLN SER CYS PRO ASP          
SEQRES  11 A  255  TRP ARG LYS ASP CYS SER ASN ASN PRO VAL SER VAL PHE          
SEQRES  12 A  255  TRP LYS THR VAL SER ARG ARG PHE ALA GLU ALA ALA CYS          
SEQRES  13 A  255  ASP VAL VAL HIS VAL MET LEU ASP GLY SER ARG SER LYS          
SEQRES  14 A  255  ILE PHE ASP LYS ASP SER THR PHE GLY SER VAL GLU VAL          
SEQRES  15 A  255  HIS ASN LEU GLN PRO GLU LYS VAL GLN THR LEU GLU ALA          
SEQRES  16 A  255  TRP VAL ILE HIS GLY GLY ARG GLU ASP SER ARG ASP LEU          
SEQRES  17 A  255  CYS GLN ASP PRO THR ILE LYS GLU LEU GLU SER ILE ILE          
SEQRES  18 A  255  SER LYS ARG ASN ILE GLN PHE SER CYS LYS ASN ILE TYR          
SEQRES  19 A  255  ARG PRO ASP LYS PHE LEU GLN CYS VAL LYS ASN PRO GLU          
SEQRES  20 A  255  ASP SER SER CYS THR SER GLU ILE                              
SEQRES   1 B  163  ASP VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 B  163  ALA GLY HIS SER LEU ARG LEU SER CYS VAL GLY SER GLY          
SEQRES   3 B  163  SER ARG PHE ASP ASN TYR ALA MET GLY TRP PHE ARG GLN          
SEQRES   4 B  163  ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA ILE SER          
SEQRES   5 B  163  TRP SER SER GLY THR THR ARG TYR LEU ASP THR VAL LYS          
SEQRES   6 B  163  GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS SER THR          
SEQRES   7 B  163  VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR          
SEQRES   8 B  163  ALA VAL TYR TYR CYS ALA ALA ARG TYR GLN PRO ARG TYR          
SEQRES   9 B  163  TYR ASP SER GLY ASP MET ASP GLY TYR GLU TYR ASP ASN          
SEQRES  10 B  163  TRP GLY GLN GLY THR GLN VAL THR VAL SER SER GLU PRO          
SEQRES  11 B  163  LYS THR PRO LYS PRO GLN PRO ALA ALA ALA HIS HIS HIS          
SEQRES  12 B  163  HIS HIS HIS GLY ALA ALA GLU GLN LYS LEU ILE SER GLU          
SEQRES  13 B  163  GLU ASP LEU ASN GLY ALA ALA                                  
FORMUL   3  HOH   *207(H2 O)                                                    
HELIX    1 AA1 ARG A   58  HIS A   74  1                                  17    
HELIX    2 AA2 PRO A   75  ARG A   78  5                                   4    
HELIX    3 AA3 ASP A   81  ILE A   94  1                                  14    
HELIX    4 AA4 THR A  102  ASP A  105  5                                   4    
HELIX    5 AA5 TYR A  106  THR A  114  1                                   9    
HELIX    6 AA6 ILE A  128  GLN A  139  1                                  12    
HELIX    7 AA7 THR A  144  ASP A  147  5                                   4    
HELIX    8 AA8 THR A  148  ASP A  155  1                                   8    
HELIX    9 AA9 ASN A  183  ALA A  200  1                                  18    
HELIX   10 AB1 SER A  220  VAL A  225  1                                   6    
HELIX   11 AB2 GLU A  226  ASN A  229  5                                   4    
HELIX   12 AB3 ASP A  256  ARG A  269  1                                  14    
HELIX   13 AB4 ARG A  280  ASN A  290  1                                  11    
HELIX   14 AB5 ARG B   28  ASP B   30  5                                   3    
HELIX   15 AB6 ASP B   62  LYS B   65  5                                   4    
HELIX   16 AB7 ASN B   74  LYS B   76  5                                   3    
HELIX   17 AB8 LYS B   87  THR B   91  5                                   5    
HELIX   18 AB9 ASP B  106  GLY B  112  5                                   7    
SHEET    1 AA1 2 GLY A  52  PRO A  53  0                                        
SHEET    2 AA1 2 SER A 172  CYS A 173 -1  O  CYS A 173   N  GLY A  52           
SHEET    1 AA2 4 LEU A 123  SER A 126  0                                        
SHEET    2 AA2 4 ASP A 202  ASP A 209  1  O  HIS A 205   N  LEU A 124           
SHEET    3 AA2 4 VAL A 235  ILE A 243  1  O  ILE A 243   N  LEU A 208           
SHEET    4 AA2 4 GLN A 272  ILE A 278  1  O  LYS A 276   N  VAL A 242           
SHEET    1 AA3 4 VAL B   2  SER B   7  0                                        
SHEET    2 AA3 4 LEU B  18  GLY B  26 -1  O  SER B  25   N  GLN B   3           
SHEET    3 AA3 4 THR B  78  MET B  83 -1  O  LEU B  81   N  LEU B  20           
SHEET    4 AA3 4 PHE B  68  ASP B  73 -1  N  ASP B  73   O  THR B  78           
SHEET    1 AA4 6 GLY B  10  GLN B  13  0                                        
SHEET    2 AA4 6 THR B 122  SER B 127  1  O  THR B 125   N  GLY B  10           
SHEET    3 AA4 6 ALA B  92  TYR B 100 -1  N  TYR B  94   O  THR B 122           
SHEET    4 AA4 6 TYR B  32  GLN B  39 -1  N  PHE B  37   O  TYR B  95           
SHEET    5 AA4 6 GLU B  46  ILE B  51 -1  O  ALA B  49   N  TRP B  36           
SHEET    6 AA4 6 THR B  58  TYR B  60 -1  O  ARG B  59   N  ALA B  50           
SHEET    1 AA5 4 GLY B  10  GLN B  13  0                                        
SHEET    2 AA5 4 THR B 122  SER B 127  1  O  THR B 125   N  GLY B  10           
SHEET    3 AA5 4 ALA B  92  TYR B 100 -1  N  TYR B  94   O  THR B 122           
SHEET    4 AA5 4 ASN B 117  TRP B 118 -1  O  ASN B 117   N  ALA B  98           
SSBOND   1 CYS A   67    CYS A   82                          1555   1555  2.16  
SSBOND   2 CYS A   99    CYS A  180                          1555   1555  2.05  
SSBOND   3 CYS A  119    CYS A  201                          1555   1555  2.05  
SSBOND   4 CYS A  160    CYS A  173                          1555   1555  2.13  
SSBOND   5 CYS A  254    CYS A  275                          1555   1555  2.11  
SSBOND   6 CYS A  287    CYS A  296                          1555   1555  2.05  
SSBOND   7 CYS B   22    CYS B   96                          1555   1555  2.07  
CRYST1   33.141   96.190  143.254  90.00  90.00  90.00 P 21 21 21    4          
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      0.030174  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010396  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006981        0.00000                         
ATOM      1  N   THR A  49       2.941  18.231 150.578  1.00 45.57           N  
ANISOU    1  N   THR A  49     5130   5764   6418    614    589   -876       N  
ATOM      2  CA  THR A  49       2.843  17.551 149.249  1.00 43.67           C  
ANISOU    2  CA  THR A  49     4699   5529   6363    513    430   -800       C  
ATOM      3  C   THR A  49       3.639  18.286 148.161  1.00 40.31           C  
ANISOU    3  C   THR A  49     4294   5017   6005    773    329  -1063       C  
ATOM      4  O   THR A  49       3.447  19.484 147.930  1.00 41.87           O  
ANISOU    4  O   THR A  49     4999   5029   5879    557    -78   -896       O  
ATOM      5  CB  THR A  49       1.365  17.421 148.833  1.00 46.51           C  
ANISOU    5  CB  THR A  49     4667   6120   6881    600    470   -933       C  
ATOM      6  OG1 THR A  49       0.756  16.409 149.639  1.00 50.28           O  
ANISOU    6  OG1 THR A  49     5471   6562   7071    143    783   -931       O  
ATOM      7  CG2 THR A  49       1.196  17.052 147.348  1.00 46.45           C  
ANISOU    7  CG2 THR A  49     4532   6169   6944    756    355  -1040       C  
ATOM      8  N   TRP A  50       4.500  17.546 147.478  1.00 35.97           N  
ANISOU    8  N   TRP A  50     3750   4478   5437    518    181   -706       N  
ATOM      9  CA  TRP A  50       5.253  18.067 146.354  1.00 34.79           C  
ANISOU    9  CA  TRP A  50     3737   4152   5330    652    184   -745       C  
ATOM     10  C   TRP A  50       4.415  17.953 145.080  1.00 36.21           C  
ANISOU   10  C   TRP A  50     3816   4493   5447    786     65   -626       C  
ATOM     11  O   TRP A  50       3.395  17.277 145.065  1.00 38.19           O  
ANISOU   11  O   TRP A  50     3591   5137   5782    762   -415   -843       O  
ATOM     12  CB  TRP A  50       6.547  17.275 146.205  1.00 31.84           C  
ANISOU   12  CB  TRP A  50     3546   3721   4831    376    173   -656       C  
ATOM     13  CG  TRP A  50       7.413  17.309 147.443  1.00 29.82           C  
ANISOU   13  CG  TRP A  50     3280   3343   4707    268    356   -733       C  
ATOM     14  CD1 TRP A  50       7.748  16.250 148.238  1.00 28.72           C  
ANISOU   14  CD1 TRP A  50     3132   3350   4429    149    361   -782       C  
ATOM     15  CD2 TRP A  50       8.038  18.457 148.024  1.00 29.53           C  
ANISOU   15  CD2 TRP A  50     3371   3205   4642    430    414   -885       C  
ATOM     16  NE1 TRP A  50       8.552  16.662 149.267  1.00 28.32           N  
ANISOU   16  NE1 TRP A  50     3160   3227   4371    170    409   -860       N  
ATOM     17  CE2 TRP A  50       8.747  18.012 149.168  1.00 29.08           C  
ANISOU   17  CE2 TRP A  50     3295   3165   4586    279    388   -964       C  
ATOM     18  CE3 TRP A  50       8.097  19.815 147.677  1.00 30.38           C  
ANISOU   18  CE3 TRP A  50     3523   3150   4870    580    441   -888       C  
ATOM     19  CZ2 TRP A  50       9.491  18.886 149.984  1.00 29.68           C  
ANISOU   19  CZ2 TRP A  50     3447   3184   4643    345    375  -1158       C  
ATOM     20  CZ3 TRP A  50       8.836  20.695 148.501  1.00 30.95           C  
ANISOU   20  CZ3 TRP A  50     3594   3032   5131    454    530   -962       C  
ATOM     21  CH2 TRP A  50       9.516  20.222 149.634  1.00 30.80           C  
ANISOU   21  CH2 TRP A  50     3562   3129   5010    323    428  -1226       C  
ATOM     22  N   SER A  51       4.864  18.605 144.014  1.00 36.54           N  
ANISOU   22  N   SER A  51     4026   4465   5391    998    106   -586       N  
ATOM     23  CA  SER A  51       4.147  18.635 142.740  1.00 37.77           C  
ANISOU   23  CA  SER A  51     4157   4710   5484   1274     -4   -575       C  
ATOM     24  C   SER A  51       4.483  17.461 141.817  1.00 37.29           C  
ANISOU   24  C   SER A  51     4063   4699   5406   1183   -218   -602       C  
ATOM     25  O   SER A  51       3.673  17.094 140.969  1.00 40.31           O  
ANISOU   25  O   SER A  51     4577   5296   5440   1573   -685   -621       O  
ATOM     26  CB  SER A  51       4.431  19.945 142.017  1.00 39.68           C  
ANISOU   26  CB  SER A  51     4606   4754   5714   1403     67   -404       C  
ATOM     27  OG  SER A  51       4.055  21.037 142.845  1.00 41.90           O  
ANISOU   27  OG  SER A  51     4832   4950   6138   1487    648   -378       O  
ATOM     28  N   GLY A  52       5.667  16.880 141.980  1.00 34.12           N  
ANISOU   28  N   GLY A  52     3805   4222   4936    865    -87   -576       N  
ATOM     29  CA  GLY A  52       6.114  15.809 141.129  1.00 33.22           C  
ANISOU   29  CA  GLY A  52     3679   4169   4774    813   -279   -561       C  
ATOM     30  C   GLY A  52       5.596  14.450 141.548  1.00 32.29           C  
ANISOU   30  C   GLY A  52     3215   4308   4743    603   -240   -728       C  
ATOM     31  O   GLY A  52       5.094  14.279 142.661  1.00 30.73           O  
ANISOU   31  O   GLY A  52     2438   4318   4917    323   -168   -891       O  
ATOM     32  N   PRO A  53       5.730  13.460 140.650  1.00 33.45           N  
ANISOU   32  N   PRO A  53     3462   4369   4875    520   -346   -855       N  
ATOM     33  CA  PRO A  53       5.387  12.078 141.006  1.00 33.00           C  
ANISOU   33  CA  PRO A  53     3115   4483   4941    263   -330   -901       C  
ATOM     34  C   PRO A  53       6.280  11.505 142.114  1.00 30.35           C  
ANISOU   34  C   PRO A  53     2922   3911   4697      6   -103   -802       C  
ATOM     35  O   PRO A  53       7.450  11.855 142.221  1.00 30.05           O  
ANISOU   35  O   PRO A  53     2957   3645   4816     88   -270   -761       O  
ATOM     36  CB  PRO A  53       5.562  11.309 139.679  1.00 34.41           C  
ANISOU   36  CB  PRO A  53     3339   4656   5076    329   -422  -1081       C  
ATOM     37  CG  PRO A  53       6.466  12.167 138.838  1.00 34.58           C  
ANISOU   37  CG  PRO A  53     3662   4627   4848    609   -367   -836       C  
ATOM     38  CD  PRO A  53       6.154  13.586 139.239  1.00 34.67           C  
ANISOU   38  CD  PRO A  53     3796   4565   4812    742   -438   -671       C  
ATOM     39  N   GLY A  54       5.711  10.641 142.940  1.00 29.75           N  
ANISOU   39  N   GLY A  54     2649   3858   4797   -129   -118   -912       N  
ATOM     40  CA  GLY A  54       6.438  10.009 144.039  1.00 27.57           C  
ANISOU   40  CA  GLY A  54     2454   3428   4593   -287    124   -889       C  
ATOM     41  C   GLY A  54       7.490   9.040 143.535  1.00 25.37           C  
ANISOU   41  C   GLY A  54     2439   3027   4174   -442     76   -795       C  
ATOM     42  O   GLY A  54       7.610   8.811 142.338  1.00 26.06           O  
ANISOU   42  O   GLY A  54     2671   3039   4190   -408    117   -892       O  
ATOM     43  N   THR A  55       8.257   8.480 144.457  1.00 24.02           N  
ANISOU   43  N   THR A  55     2358   2720   4047   -485    242   -741       N  
ATOM     44  CA  THR A  55       9.304   7.520 144.113  1.00 22.93           C  
ANISOU   44  CA  THR A  55     2325   2594   3794   -543    243   -638       C  
ATOM     45  C   THR A  55       8.696   6.340 143.339  1.00 24.05           C  
ANISOU   45  C   THR A  55     2310   2735   4093   -672    277   -762       C  
ATOM     46  O   THR A  55       7.610   5.873 143.675  1.00 25.74           O  
ANISOU   46  O   THR A  55     2325   2972   4481   -716    412   -793       O  
ATOM     47  CB  THR A  55      10.019   7.021 145.387  1.00 21.98           C  
ANISOU   47  CB  THR A  55     2347   2376   3629   -564    440   -549       C  
ATOM     48  OG1 THR A  55      10.620   8.127 146.046  1.00 20.40           O  
ANISOU   48  OG1 THR A  55     2054   2392   3302   -540    400   -399       O  
ATOM     49  CG2 THR A  55      11.076   5.994 145.085  1.00 21.35           C  
ANISOU   49  CG2 THR A  55     2311   2268   3531   -606    460   -425       C  
ATOM     50  N   THR A  56       9.390   5.899 142.293  1.00 23.70           N  
ANISOU   50  N   THR A  56     2325   2681   3997   -666    200   -786       N  
ATOM     51  CA  THR A  56       8.950   4.778 141.454  1.00 25.21           C  
ANISOU   51  CA  THR A  56     2343   2869   4366   -817    160   -971       C  
ATOM     52  C   THR A  56       8.668   3.536 142.305  1.00 26.85           C  
ANISOU   52  C   THR A  56     2601   2889   4711   -965    444   -957       C  
ATOM     53  O   THR A  56       9.484   3.174 143.168  1.00 25.51           O  
ANISOU   53  O   THR A  56     2661   2469   4561  -1126    520   -859       O  
ATOM     54  CB  THR A  56      10.041   4.384 140.429  1.00 24.42           C  
ANISOU   54  CB  THR A  56     2453   2727   4097   -767     63   -951       C  
ATOM     55  OG1 THR A  56      10.567   5.558 139.772  1.00 24.03           O  
ANISOU   55  OG1 THR A  56     2446   2679   4003   -593     78   -899       O  
ATOM     56  CG2 THR A  56       9.494   3.374 139.381  1.00 25.87           C  
ANISOU   56  CG2 THR A  56     2431   2979   4417   -847    -29  -1162       C  
ATOM     57  N   LYS A  57       7.532   2.878 142.054  1.00 30.05           N  
ANISOU   57  N   LYS A  57     2716   3274   5427  -1137    455  -1232       N  
ATOM     58  CA  LYS A  57       7.195   1.630 142.745  1.00 32.78           C  
ANISOU   58  CA  LYS A  57     3096   3371   5985  -1292    849  -1177       C  
ATOM     59  C   LYS A  57       8.362   0.671 142.631  1.00 31.30           C  
ANISOU   59  C   LYS A  57     3038   3091   5761  -1426    903  -1120       C  
ATOM     60  O   LYS A  57       8.907   0.524 141.545  1.00 30.51           O  
ANISOU   60  O   LYS A  57     3011   3051   5530  -1353    620  -1327       O  
ATOM     61  CB  LYS A  57       5.979   0.946 142.107  1.00 37.28           C  
ANISOU   61  CB  LYS A  57     3214   4065   6885  -1561    847  -1558       C  
ATOM     62  CG  LYS A  57       4.672   1.681 142.299  1.00 40.46           C  
ANISOU   62  CG  LYS A  57     3306   4608   7457  -1389    872  -1669       C  
ATOM     63  CD  LYS A  57       3.477   0.778 142.003  1.00 45.94           C  
ANISOU   63  CD  LYS A  57     3578   5277   8598  -1710    892  -2145       C  
ATOM     64  CE  LYS A  57       2.249   1.225 142.794  1.00 49.39           C  
ANISOU   64  CE  LYS A  57     3781   5738   9246  -1587   1208  -2194       C  
ATOM     65  NZ  LYS A  57       2.224   0.758 144.217  1.00 50.90           N  
ANISOU   65  NZ  LYS A  57     4224   5631   9483  -1695   1571  -1905       N  
ATOM     66  N   ARG A  58       8.737   0.034 143.740  1.00 31.54           N  
ANISOU   66  N   ARG A  58     3280   2910   5794  -1456   1186   -938       N  
ATOM     67  CA  ARG A  58       9.812  -0.962 143.764  1.00 32.34           C  
ANISOU   67  CA  ARG A  58     3622   2846   5817  -1313   1338   -709       C  
ATOM     68  C   ARG A  58      11.195  -0.392 143.389  1.00 28.83           C  
ANISOU   68  C   ARG A  58     3409   2547   4997  -1135   1002   -692       C  
ATOM     69  O   ARG A  58      12.040  -1.114 142.841  1.00 28.36           O  
ANISOU   69  O   ARG A  58     3201   2474   5098  -1182    886   -703       O  
ATOM     70  CB  ARG A  58       9.469  -2.165 142.858  1.00 35.74           C  
ANISOU   70  CB  ARG A  58     3999   3099   6479  -1479   1372  -1059       C  
ATOM     71  CG  ARG A  58       8.049  -2.705 143.027  1.00 40.54           C  
ANISOU   71  CG  ARG A  58     4233   3602   7567  -1778   1668  -1173       C  
ATOM     72  CD  ARG A  58       7.866  -4.058 142.350  1.00 44.60           C  
ANISOU   72  CD  ARG A  58     4771   3800   8375  -1942   1824  -1520       C  
ATOM     73  NE  ARG A  58       8.215  -5.156 143.260  1.00 48.55           N  
ANISOU   73  NE  ARG A  58     5616   4012   8817  -1787   2320  -1105       N  
ATOM     74  CZ  ARG A  58       9.332  -5.896 143.236  1.00 48.37           C  
ANISOU   74  CZ  ARG A  58     5754   3862   8759  -1751   2443   -930       C  
ATOM     75  NH1 ARG A  58      10.287  -5.736 142.318  1.00 46.44           N  
ANISOU   75  NH1 ARG A  58     5376   3970   8299  -1923   2025  -1082       N  
ATOM     76  NH2 ARG A  58       9.491  -6.842 144.152  1.00 51.48           N  
ANISOU   76  NH2 ARG A  58     6552   3758   9248  -1701   2848   -669       N  
ATOM     77  N   PHE A  59      11.415   0.887 143.700  1.00 26.76           N  
ANISOU   77  N   PHE A  59     3101   2476   4589  -1010    876   -571       N  
ATOM     78  CA  PHE A  59      12.701   1.556 143.470  1.00 24.43           C  
ANISOU   78  CA  PHE A  59     2975   2247   4060   -852    694   -472       C  
ATOM     79  C   PHE A  59      13.889   0.771 144.042  1.00 23.76           C  
ANISOU   79  C   PHE A  59     3166   1963   3898   -815    789   -310       C  
ATOM     80  O   PHE A  59      14.817   0.453 143.284  1.00 22.49           O  
ANISOU   80  O   PHE A  59     3106   1508   3929   -869    763   -312       O  
ATOM     81  CB  PHE A  59      12.677   3.005 144.010  1.00 23.54           C  
ANISOU   81  CB  PHE A  59     2882   2233   3826   -748    566   -398       C  
ATOM     82  CG  PHE A  59      13.974   3.761 143.820  1.00 22.05           C  
ANISOU   82  CG  PHE A  59     2715   2185   3477   -646    374   -389       C  
ATOM     83  CD1 PHE A  59      14.392   4.132 142.549  1.00 21.28           C  
ANISOU   83  CD1 PHE A  59     2626   2082   3377   -697    235   -433       C  
ATOM     84  CD2 PHE A  59      14.754   4.126 144.914  1.00 21.92           C  
ANISOU   84  CD2 PHE A  59     2804   2212   3312   -528    362   -298       C  
ATOM     85  CE1 PHE A  59      15.580   4.837 142.372  1.00 20.83           C  
ANISOU   85  CE1 PHE A  59     2538   2150   3226   -635    146   -423       C  
ATOM     86  CE2 PHE A  59      15.941   4.829 144.744  1.00 20.64           C  
ANISOU   86  CE2 PHE A  59     2688   2021   3133   -422    206   -307       C  
ATOM     87  CZ  PHE A  59      16.357   5.181 143.476  1.00 20.04           C  
ANISOU   87  CZ  PHE A  59     2535   1971   3108   -521    165   -393       C  
ATOM     88  N   PRO A  60      13.862   0.433 145.350  1.00 25.04           N  
ANISOU   88  N   PRO A  60     3413   2140   3960   -701    984   -162       N  
ATOM     89  CA  PRO A  60      14.981  -0.334 145.903  1.00 26.09           C  
ANISOU   89  CA  PRO A  60     3751   2242   3919   -435   1072     -3       C  
ATOM     90  C   PRO A  60      15.249  -1.631 145.142  1.00 27.43           C  
ANISOU   90  C   PRO A  60     4010   2207   4202   -517   1149    -63       C  
ATOM     91  O   PRO A  60      16.392  -1.920 144.776  1.00 27.25           O  
ANISOU   91  O   PRO A  60     4067   2071   4214   -356   1093   -147       O  
ATOM     92  CB  PRO A  60      14.528  -0.654 147.342  1.00 28.19           C  
ANISOU   92  CB  PRO A  60     4216   2435   4060   -261   1321    126       C  
ATOM     93  CG  PRO A  60      13.413   0.273 147.635  1.00 28.05           C  
ANISOU   93  CG  PRO A  60     4007   2540   4109   -353   1345     58       C  
ATOM     94  CD  PRO A  60      12.751   0.520 146.317  1.00 27.04           C  
ANISOU   94  CD  PRO A  60     3649   2403   4219   -602   1206   -192       C  
ATOM     95  N   GLU A  61      14.198  -2.386 144.870  1.00 29.78           N  
ANISOU   95  N   GLU A  61     4184   2323   4807   -766   1378    -56       N  
ATOM     96  CA  GLU A  61      14.359  -3.683 144.195  1.00 31.75           C  
ANISOU   96  CA  GLU A  61     4568   2411   5083   -824   1538   -190       C  
ATOM     97  C   GLU A  61      14.855  -3.493 142.766  1.00 29.74           C  
ANISOU   97  C   GLU A  61     4096   2296   4906   -927   1241   -270       C  
ATOM     98  O   GLU A  61      15.695  -4.258 142.290  1.00 29.94           O  
ANISOU   98  O   GLU A  61     4330   2110   4934   -907   1271   -247       O  
ATOM     99  CB  GLU A  61      13.051  -4.474 144.202  1.00 35.11           C  
ANISOU   99  CB  GLU A  61     4841   2509   5989  -1104   1881   -256       C  
ATOM    100  CG  GLU A  61      12.661  -4.999 145.584  1.00 39.14           C  
ANISOU  100  CG  GLU A  61     5635   2892   6345   -986   2299     20       C  
ATOM    101  CD  GLU A  61      11.898  -4.010 146.469  1.00 40.88           C  
ANISOU  101  CD  GLU A  61     5869   3139   6523   -825   2390    -36       C  
ATOM    102  OE1 GLU A  61      11.644  -2.839 146.083  1.00 39.35           O  
ANISOU  102  OE1 GLU A  61     5504   3223   6221   -799   2105    -87       O  
ATOM    103  OE2 GLU A  61      11.548  -4.419 147.592  1.00 47.88           O  
ANISOU  103  OE2 GLU A  61     7151   4192   6846   -790   2779    314       O  
ATOM    104  N   THR A  62      14.329  -2.473 142.096  1.00 27.88           N  
ANISOU  104  N   THR A  62     3677   2149   4767  -1051   1093   -463       N  
ATOM    105  CA  THR A  62      14.690  -2.184 140.722  1.00 27.54           C  
ANISOU  105  CA  THR A  62     3598   2283   4582  -1000    787   -568       C  
ATOM    106  C   THR A  62      16.166  -1.774 140.631  1.00 25.59           C  
ANISOU  106  C   THR A  62     3493   2105   4122   -842    627   -482       C  
ATOM    107  O   THR A  62      16.887  -2.255 139.762  1.00 25.46           O  
ANISOU  107  O   THR A  62     3491   2062   4118   -716    523   -546       O  
ATOM    108  CB  THR A  62      13.763  -1.100 140.129  1.00 27.74           C  
ANISOU  108  CB  THR A  62     3383   2482   4674   -999    549   -736       C  
ATOM    109  OG1 THR A  62      12.414  -1.580 140.150  1.00 30.81           O  
ANISOU  109  OG1 THR A  62     3530   2622   5555  -1237    690   -851       O  
ATOM    110  CG2 THR A  62      14.140  -0.740 138.689  1.00 26.95           C  
ANISOU  110  CG2 THR A  62     3279   2518   4443   -985    249   -832       C  
ATOM    111  N   VAL A  63      16.623  -0.924 141.544  1.00 24.63           N  
ANISOU  111  N   VAL A  63     3404   2062   3892   -671    574   -385       N  
ATOM    112  CA  VAL A  63      18.024  -0.473 141.513  1.00 23.66           C  
ANISOU  112  CA  VAL A  63     3320   2112   3559   -531    460   -285       C  
ATOM    113  C   VAL A  63      18.950  -1.662 141.787  1.00 24.52           C  
ANISOU  113  C   VAL A  63     3615   2059   3640   -420    632   -215       C  
ATOM    114  O   VAL A  63      19.952  -1.822 141.113  1.00 22.73           O  
ANISOU  114  O   VAL A  63     3617   1608   3411   -324    556   -219       O  
ATOM    115  CB  VAL A  63      18.309   0.686 142.498  1.00 22.87           C  
ANISOU  115  CB  VAL A  63     3190   2090   3408   -506    401   -203       C  
ATOM    116  CG1 VAL A  63      19.804   0.952 142.638  1.00 22.11           C  
ANISOU  116  CG1 VAL A  63     3146   2075   3181   -298    246   -196       C  
ATOM    117  CG2 VAL A  63      17.597   1.951 142.037  1.00 22.50           C  
ANISOU  117  CG2 VAL A  63     3001   2117   3430   -581    284   -267       C  
ATOM    118  N   LEU A  64      18.606  -2.494 142.766  1.00 26.07           N  
ANISOU  118  N   LEU A  64     4056   2051   3799   -461    824   -196       N  
ATOM    119  CA  LEU A  64      19.464  -3.604 143.117  1.00 28.42           C  
ANISOU  119  CA  LEU A  64     4455   2257   4086   -220    833    -16       C  
ATOM    120  C   LEU A  64      19.553  -4.609 141.945  1.00 28.87           C  
ANISOU  120  C   LEU A  64     4406   2317   4244   -336    902    -94       C  
ATOM    121  O   LEU A  64      20.645  -5.076 141.613  1.00 29.50           O  
ANISOU  121  O   LEU A  64     4485   2543   4180   -210    973   -113       O  
ATOM    122  CB  LEU A  64      18.966  -4.292 144.384  1.00 32.18           C  
ANISOU  122  CB  LEU A  64     5086   2721   4420   -106   1268    170       C  
ATOM    123  CG  LEU A  64      19.976  -5.272 144.993  1.00 35.84           C  
ANISOU  123  CG  LEU A  64     5759   3126   4731    209   1185    448       C  
ATOM    124  CD1 LEU A  64      21.078  -4.524 145.747  1.00 35.84           C  
ANISOU  124  CD1 LEU A  64     5774   3404   4438    399   1018    394       C  
ATOM    125  CD2 LEU A  64      19.269  -6.270 145.905  1.00 40.45           C  
ANISOU  125  CD2 LEU A  64     6504   3594   5269    159   1714    657       C  
ATOM    126  N   ALA A  65      18.413  -4.921 141.316  1.00 28.87           N  
ANISOU  126  N   ALA A  65     4460   1990   4518   -662    954   -219       N  
ATOM    127  CA  ALA A  65      18.394  -5.860 140.193  1.00 28.81           C  
ANISOU  127  CA  ALA A  65     4384   1984   4577   -735   1077   -280       C  
ATOM    128  C   ALA A  65      19.104  -5.310 138.968  1.00 26.62           C  
ANISOU  128  C   ALA A  65     3998   1848   4269   -706    802   -419       C  
ATOM    129  O   ALA A  65      19.712  -6.070 138.241  1.00 27.56           O  
ANISOU  129  O   ALA A  65     4273   1673   4523   -661    954   -382       O  
ATOM    130  CB  ALA A  65      16.968  -6.282 139.848  1.00 30.51           C  
ANISOU  130  CB  ALA A  65     4474   2067   5049   -940   1124   -533       C  
ATOM    131  N   ARG A  66      19.030  -4.003 138.730  1.00 24.54           N  
ANISOU  131  N   ARG A  66     3542   1821   3958   -708    603   -487       N  
ATOM    132  CA  ARG A  66      19.827  -3.378 137.663  1.00 23.66           C  
ANISOU  132  CA  ARG A  66     3533   1823   3634   -606    414   -456       C  
ATOM    133  C   ARG A  66      21.331  -3.504 137.906  1.00 23.36           C  
ANISOU  133  C   ARG A  66     3559   1770   3545   -451    479   -364       C  
ATOM    134  O   ARG A  66      22.104  -3.728 136.962  1.00 22.97           O  
ANISOU  134  O   ARG A  66     3665   1595   3467   -347    419   -508       O  
ATOM    135  CB  ARG A  66      19.490  -1.891 137.535  1.00 22.45           C  
ANISOU  135  CB  ARG A  66     3248   1866   3415   -607    268   -427       C  
ATOM    136  CG  ARG A  66      18.181  -1.683 136.821  1.00 23.05           C  
ANISOU  136  CG  ARG A  66     3208   1983   3567   -713    221   -613       C  
ATOM    137  CD  ARG A  66      17.894  -0.230 136.639  1.00 21.96           C  
ANISOU  137  CD  ARG A  66     2969   2029   3343   -662     92   -583       C  
ATOM    138  NE  ARG A  66      16.640  -0.048 135.943  1.00 22.71           N  
ANISOU  138  NE  ARG A  66     2996   2150   3481   -719    -33   -811       N  
ATOM    139  CZ  ARG A  66      16.162   1.128 135.574  1.00 22.91           C  
ANISOU  139  CZ  ARG A  66     2932   2318   3451   -581   -121   -754       C  
ATOM    140  NH1 ARG A  66      16.840   2.255 135.829  1.00 22.17           N  
ANISOU  140  NH1 ARG A  66     2877   2231   3315   -513    -39   -623       N  
ATOM    141  NH2 ARG A  66      15.005   1.182 134.949  1.00 24.19           N  
ANISOU  141  NH2 ARG A  66     3017   2544   3629   -564   -256   -901       N  
ATOM    142  N   CYS A  67      21.729  -3.329 139.167  1.00 23.33           N  
ANISOU  142  N   CYS A  67     3654   1742   3466   -358    486   -256       N  
ATOM    143  CA  CYS A  67      23.124  -3.426 139.550  1.00 24.70           C  
ANISOU  143  CA  CYS A  67     3740   2017   3629   -180    432   -206       C  
ATOM    144  C   CYS A  67      23.658  -4.850 139.356  1.00 25.26           C  
ANISOU  144  C   CYS A  67     3967   2023   3607   -151    623   -272       C  
ATOM    145  O   CYS A  67      24.767  -5.032 138.882  1.00 23.97           O  
ANISOU  145  O   CYS A  67     3907   1642   3559    -21    508   -382       O  
ATOM    146  CB  CYS A  67      23.332  -2.932 140.997  1.00 26.80           C  
ANISOU  146  CB  CYS A  67     4269   2420   3491    175    585   -212       C  
ATOM    147  SG  CYS A  67      25.062  -2.876 141.519  1.00 30.38           S  
ANISOU  147  SG  CYS A  67     4480   3180   3881    -57    454   -438       S  
ATOM    148  N   VAL A  68      22.840  -5.834 139.719  1.00 26.45           N  
ANISOU  148  N   VAL A  68     4320   1926   3803   -133    814   -162       N  
ATOM    149  CA  VAL A  68      23.163  -7.262 139.585  1.00 27.74           C  
ANISOU  149  CA  VAL A  68     4639   1929   3968    -60    937    -70       C  
ATOM    150  C   VAL A  68      23.320  -7.619 138.095  1.00 27.21           C  
ANISOU  150  C   VAL A  68     4545   1782   4012   -201    900   -173       C  
ATOM    151  O   VAL A  68      24.305  -8.232 137.684  1.00 27.42           O  
ANISOU  151  O   VAL A  68     4767   1705   3945   -182   1098   -170       O  
ATOM    152  CB  VAL A  68      22.079  -8.131 140.296  1.00 29.62           C  
ANISOU  152  CB  VAL A  68     5004   1922   4327    -84   1224     24       C  
ATOM    153  CG1 VAL A  68      22.235  -9.629 140.008  1.00 32.03           C  
ANISOU  153  CG1 VAL A  68     5495   1923   4750   -178   1416    -29       C  
ATOM    154  CG2 VAL A  68      22.131  -7.894 141.802  1.00 30.25           C  
ANISOU  154  CG2 VAL A  68     5193   2047   4250    125   1299    213       C  
ATOM    155  N   LYS A  69      22.360  -7.193 137.290  1.00 26.86           N  
ANISOU  155  N   LYS A  69     4365   1814   4027   -415    814   -342       N  
ATOM    156  CA  LYS A  69      22.415  -7.386 135.838  1.00 27.15           C  
ANISOU  156  CA  LYS A  69     4367   1876   4070   -515    748   -530       C  
ATOM    157  C   LYS A  69      23.645  -6.722 135.174  1.00 25.52           C  
ANISOU  157  C   LYS A  69     4181   1787   3727   -352    633   -556       C  
ATOM    158  O   LYS A  69      24.360  -7.358 134.407  1.00 26.03           O  
ANISOU  158  O   LYS A  69     4293   1673   3922   -238    714   -538       O  
ATOM    159  CB  LYS A  69      21.134  -6.844 135.228  1.00 27.58           C  
ANISOU  159  CB  LYS A  69     4238   1996   4244   -627    626   -719       C  
ATOM    160  CG  LYS A  69      20.993  -7.050 133.736  1.00 29.29           C  
ANISOU  160  CG  LYS A  69     4491   2285   4352   -639    504   -960       C  
ATOM    161  CD  LYS A  69      19.525  -6.974 133.361  1.00 31.38           C  
ANISOU  161  CD  LYS A  69     4519   2615   4786   -781    397  -1194       C  
ATOM    162  CE  LYS A  69      19.339  -6.751 131.883  1.00 33.16           C  
ANISOU  162  CE  LYS A  69     4793   3004   4800   -698    209  -1331       C  
ATOM    163  NZ  LYS A  69      18.024  -7.296 131.463  1.00 37.07           N  
ANISOU  163  NZ  LYS A  69     4940   3532   5611   -821     99  -1608       N  
ATOM    164  N   TYR A  70      23.889  -5.450 135.477  1.00 23.57           N  
ANISOU  164  N   TYR A  70     3815   1714   3427   -337    530   -397       N  
ATOM    165  CA  TYR A  70      25.016  -4.725 134.875  1.00 22.38           C  
ANISOU  165  CA  TYR A  70     3607   1724   3173   -193    466   -426       C  
ATOM    166  C   TYR A  70      26.369  -5.336 135.242  1.00 23.11           C  
ANISOU  166  C   TYR A  70     3722   1743   3313    -44    521   -363       C  
ATOM    167  O   TYR A  70      27.235  -5.489 134.384  1.00 23.08           O  
ANISOU  167  O   TYR A  70     3755   1669   3344     52    522   -471       O  
ATOM    168  CB  TYR A  70      24.994  -3.251 135.290  1.00 20.91           C  
ANISOU  168  CB  TYR A  70     3281   1663   2998   -256    391   -307       C  
ATOM    169  CG  TYR A  70      25.889  -2.364 134.478  1.00 20.22           C  
ANISOU  169  CG  TYR A  70     3113   1646   2922   -122    436   -345       C  
ATOM    170  CD1 TYR A  70      25.378  -1.643 133.406  1.00 20.21           C  
ANISOU  170  CD1 TYR A  70     3153   1695   2829   -162    451   -350       C  
ATOM    171  CD2 TYR A  70      27.238  -2.217 134.791  1.00 20.30           C  
ANISOU  171  CD2 TYR A  70     3091   1603   3016   -112    440   -350       C  
ATOM    172  CE1 TYR A  70      26.185  -0.819 132.655  1.00 20.47           C  
ANISOU  172  CE1 TYR A  70     3188   1661   2925   -123    507   -313       C  
ATOM    173  CE2 TYR A  70      28.060  -1.413 134.028  1.00 20.66           C  
ANISOU  173  CE2 TYR A  70     3058   1689   3101    -97    532   -353       C  
ATOM    174  CZ  TYR A  70      27.518  -0.710 132.970  1.00 20.72           C  
ANISOU  174  CZ  TYR A  70     3128   1716   3029   -136    636   -305       C  
ATOM    175  OH  TYR A  70      28.295   0.113 132.229  1.00 21.79           O  
ANISOU  175  OH  TYR A  70     3157   1815   3304   -119    846   -238       O  
ATOM    176  N   THR A  71      26.551  -5.668 136.516  1.00 23.78           N  
ANISOU  176  N   THR A  71     3926   1739   3371     26    566   -263       N  
ATOM    177  CA  THR A  71      27.824  -6.226 136.984  1.00 25.88           C  
ANISOU  177  CA  THR A  71     4044   2219   3570    207    529   -201       C  
ATOM    178  C   THR A  71      28.066  -7.679 136.518  1.00 28.32           C  
ANISOU  178  C   THR A  71     4555   2262   3940    373    715   -182       C  
ATOM    179  O   THR A  71      29.199  -8.151 136.539  1.00 31.04           O  
ANISOU  179  O   THR A  71     4592   3102   4098    603    999   -116       O  
ATOM    180  CB  THR A  71      27.925  -6.136 138.501  1.00 26.59           C  
ANISOU  180  CB  THR A  71     4162   2348   3590    386    492   -123       C  
ATOM    181  OG1 THR A  71      26.811  -6.803 139.089  1.00 27.19           O  
ANISOU  181  OG1 THR A  71     4353   2286   3691    417    619     97       O  
ATOM    182  CG2 THR A  71      27.945  -4.662 138.950  1.00 25.85           C  
ANISOU  182  CG2 THR A  71     3863   2458   3501    345    343   -277       C  
ATOM    183  N   GLU A  72      26.994  -8.371 136.118  1.00 29.64           N  
ANISOU  183  N   GLU A  72     4786   2311   4162    144    784   -298       N  
ATOM    184  CA  GLU A  72      27.067  -9.690 135.466  1.00 31.59           C  
ANISOU  184  CA  GLU A  72     5286   2364   4349    288    892   -340       C  
ATOM    185  C   GLU A  72      27.514  -9.517 134.025  1.00 30.61           C  
ANISOU  185  C   GLU A  72     5073   2281   4274    190    803   -444       C  
ATOM    186  O   GLU A  72      28.350 -10.268 133.561  1.00 32.70           O  
ANISOU  186  O   GLU A  72     5424   2337   4660    415    759   -555       O  
ATOM    187  CB  GLU A  72      25.700 -10.402 135.517  1.00 33.74           C  
ANISOU  187  CB  GLU A  72     5596   2365   4859     15   1080   -326       C  
ATOM    188  CG  GLU A  72      25.515 -11.631 134.616  1.00 37.40           C  
ANISOU  188  CG  GLU A  72     6300   2577   5332    -23   1189   -595       C  
ATOM    189  CD  GLU A  72      26.470 -12.769 134.943  1.00 40.90           C  
ANISOU  189  CD  GLU A  72     7051   2826   5662    372   1297   -385       C  
ATOM    190  OE1 GLU A  72      26.897 -12.827 136.113  1.00 45.90           O  
ANISOU  190  OE1 GLU A  72     7825   3847   5766    693   1135    133       O  
ATOM    191  OE2 GLU A  72      26.796 -13.603 134.053  1.00 43.80           O  
ANISOU  191  OE2 GLU A  72     8053   2743   5846    100   1387   -634       O  
ATOM    192  N   ILE A  73      26.946  -8.540 133.318  1.00 29.04           N  
ANISOU  192  N   ILE A  73     4792   2199   4042     53    754   -554       N  
ATOM    193  CA  ILE A  73      27.326  -8.265 131.930  1.00 29.16           C  
ANISOU  193  CA  ILE A  73     4825   2315   3938     62    660   -605       C  
ATOM    194  C   ILE A  73      28.780  -7.821 131.790  1.00 29.07           C  
ANISOU  194  C   ILE A  73     4786   2387   3869    137    678   -476       C  
ATOM    195  O   ILE A  73      29.474  -8.272 130.881  1.00 31.04           O  
ANISOU  195  O   ILE A  73     5106   2737   3950    290    709   -626       O  
ATOM    196  CB  ILE A  73      26.399  -7.218 131.278  1.00 28.68           C  
ANISOU  196  CB  ILE A  73     4684   2385   3827     -7    606   -653       C  
ATOM    197  CG1 ILE A  73      24.997  -7.799 131.094  1.00 29.86           C  
ANISOU  197  CG1 ILE A  73     4815   2480   4050   -136    550   -809       C  
ATOM    198  CG2 ILE A  73      26.926  -6.748 129.919  1.00 29.23           C  
ANISOU  198  CG2 ILE A  73     4806   2545   3752    111    630   -685       C  
ATOM    199  CD1 ILE A  73      23.930  -6.733 130.978  1.00 29.35           C  
ANISOU  199  CD1 ILE A  73     4633   2555   3962   -181    438   -860       C  
ATOM    200  N   HIS A  74      29.242  -6.953 132.681  1.00 28.09           N  
ANISOU  200  N   HIS A  74     4622   2300   3750    199    719   -424       N  
ATOM    201  CA  HIS A  74      30.544  -6.287 132.515  1.00 29.21           C  
ANISOU  201  CA  HIS A  74     4491   2696   3909    248    764   -417       C  
ATOM    202  C   HIS A  74      31.597  -6.868 133.437  1.00 30.51           C  
ANISOU  202  C   HIS A  74     4542   2826   4223    378    711   -353       C  
ATOM    203  O   HIS A  74      31.566  -6.590 134.647  1.00 30.93           O  
ANISOU  203  O   HIS A  74     4402   3179   4169    312    579   -264       O  
ATOM    204  CB  HIS A  74      30.384  -4.793 132.782  1.00 28.38           C  
ANISOU  204  CB  HIS A  74     4258   2614   3909     88    773   -298       C  
ATOM    205  CG  HIS A  74      29.533  -4.100 131.773  1.00 28.54           C  
ANISOU  205  CG  HIS A  74     4288   2646   3910     83    703   -387       C  
ATOM    206  ND1 HIS A  74      28.159  -4.082 131.851  1.00 28.65           N  
ANISOU  206  ND1 HIS A  74     4301   2739   3843    141    635   -440       N  
ATOM    207  CD2 HIS A  74      29.856  -3.428 130.642  1.00 30.02           C  
ANISOU  207  CD2 HIS A  74     4479   2861   4064    101    777   -204       C  
ATOM    208  CE1 HIS A  74      27.673  -3.409 130.822  1.00 28.57           C  
ANISOU  208  CE1 HIS A  74     4400   2694   3760     94    694   -405       C  
ATOM    209  NE2 HIS A  74      28.680  -3.001 130.077  1.00 29.54           N  
ANISOU  209  NE2 HIS A  74     4520   2836   3867     91    762   -243       N  
ATOM    210  N   PRO A  75      32.543  -7.661 132.889  1.00 32.43           N  
ANISOU  210  N   PRO A  75     4791   3096   4434    506    862   -414       N  
ATOM    211  CA  PRO A  75      33.478  -8.362 133.772  1.00 34.54           C  
ANISOU  211  CA  PRO A  75     5006   3387   4728    846    796   -374       C  
ATOM    212  C   PRO A  75      34.371  -7.432 134.603  1.00 35.65           C  
ANISOU  212  C   PRO A  75     4892   3786   4867    912    700   -530       C  
ATOM    213  O   PRO A  75      34.736  -7.768 135.724  1.00 36.77           O  
ANISOU  213  O   PRO A  75     5173   3736   5062   1191    532   -409       O  
ATOM    214  CB  PRO A  75      34.306  -9.237 132.812  1.00 35.68           C  
ANISOU  214  CB  PRO A  75     5278   3512   4764    833    951   -437       C  
ATOM    215  CG  PRO A  75      34.106  -8.659 131.460  1.00 35.30           C  
ANISOU  215  CG  PRO A  75     5203   3421   4786    789    939   -457       C  
ATOM    216  CD  PRO A  75      32.765  -7.997 131.468  1.00 33.62           C  
ANISOU  216  CD  PRO A  75     5057   3190   4526    569   1002   -468       C  
ATOM    217  N   GLU A  76      34.701  -6.265 134.064  1.00 42.80           N  
ANISOU  217  N   GLU A  76     5744   5727   4791     -6   1266  -2218       N  
ATOM    218  CA  GLU A  76      35.445  -5.256 134.816  1.00 45.23           C  
ANISOU  218  CA  GLU A  76     5984   5980   5221    -34   1172  -2470       C  
ATOM    219  C   GLU A  76      34.686  -4.699 136.029  1.00 42.47           C  
ANISOU  219  C   GLU A  76     5872   5481   4781    168    886  -2073       C  
ATOM    220  O   GLU A  76      35.309  -4.104 136.881  1.00 44.53           O  
ANISOU  220  O   GLU A  76     5441   6091   5387     50    483  -2016       O  
ATOM    221  CB  GLU A  76      35.938  -4.121 133.892  1.00 49.69           C  
ANISOU  221  CB  GLU A  76     6749   6375   5754   -620   1738  -2520       C  
ATOM    222  CG  GLU A  76      34.868  -3.179 133.316  1.00 51.39           C  
ANISOU  222  CG  GLU A  76     7409   6551   5566   -479   1999  -1814       C  
ATOM    223  CD  GLU A  76      34.052  -3.735 132.136  1.00 52.95           C  
ANISOU  223  CD  GLU A  76     7864   7112   5142   -225   1826  -1638       C  
ATOM    224  OE1 GLU A  76      34.351  -4.828 131.585  1.00 52.20           O  
ANISOU  224  OE1 GLU A  76     7575   7082   5174   -283   1654  -1752       O  
ATOM    225  OE2 GLU A  76      33.080  -3.043 131.754  1.00 60.52           O  
ANISOU  225  OE2 GLU A  76     8393   8736   5864    269   1680   -781       O  
ATOM    226  N   MET A  77      33.361  -4.885 136.104  1.00 39.95           N  
ANISOU  226  N   MET A  77     5876   4995   4306    176    872  -1538       N  
ATOM    227  CA  MET A  77      32.557  -4.420 137.245  1.00 38.67           C  
ANISOU  227  CA  MET A  77     5720   4932   4038    367    646  -1317       C  
ATOM    228  C   MET A  77      32.053  -5.537 138.173  1.00 39.03           C  
ANISOU  228  C   MET A  77     5982   4689   4158    565    537  -1244       C  
ATOM    229  O   MET A  77      31.231  -5.262 139.051  1.00 37.84           O  
ANISOU  229  O   MET A  77     5924   4503   3948    409    547   -877       O  
ATOM    230  CB  MET A  77      31.336  -3.631 136.754  1.00 37.23           C  
ANISOU  230  CB  MET A  77     5904   4678   3563    327    727  -1013       C  
ATOM    231  CG  MET A  77      31.638  -2.487 135.813  1.00 39.84           C  
ANISOU  231  CG  MET A  77     6410   4974   3753    231   1063   -881       C  
ATOM    232  SD  MET A  77      32.569  -1.181 136.605  1.00 42.80           S  
ANISOU  232  SD  MET A  77     6748   4530   4981    -17   1480  -1029       S  
ATOM    233  CE  MET A  77      31.280  -0.379 137.553  1.00 40.54           C  
ANISOU  233  CE  MET A  77     6655   4561   4187    158   1375   -516       C  
ATOM    234  N   ARG A  78      32.526  -6.773 138.018  1.00 42.44           N  
ANISOU  234  N   ARG A  78     6395   5017   4712    982    687  -1411       N  
ATOM    235  CA  ARG A  78      31.999  -7.883 138.837  1.00 45.42           C  
ANISOU  235  CA  ARG A  78     7166   4928   5163   1251    952  -1172       C  
ATOM    236  C   ARG A  78      32.515  -7.839 140.288  1.00 47.08           C  
ANISOU  236  C   ARG A  78     7600   5075   5212   2207    749   -880       C  
ATOM    237  O   ARG A  78      31.965  -8.498 141.152  1.00 48.91           O  
ANISOU  237  O   ARG A  78     8598   4429   5554   2999   1078   -389       O  
ATOM    238  CB  ARG A  78      32.172  -9.266 138.152  1.00 49.85           C  
ANISOU  238  CB  ARG A  78     7915   5092   5933   1339   1495  -1409       C  
ATOM    239  CG  ARG A  78      33.565  -9.861 138.103  1.00 54.11           C  
ANISOU  239  CG  ARG A  78     8280   5848   6431   1903   1404  -1535       C  
ATOM    240  CD  ARG A  78      33.549 -11.334 137.657  1.00 60.52           C  
ANISOU  240  CD  ARG A  78     9560   5855   7580   1727   1834  -1597       C  
ATOM    241  NE  ARG A  78      32.902 -11.590 136.352  1.00 59.92           N  
ANISOU  241  NE  ARG A  78     9152   5953   7663    882   2243  -2201       N  
ATOM    242  CZ  ARG A  78      33.417 -12.286 135.328  1.00 63.10           C  
ANISOU  242  CZ  ARG A  78     9286   6417   8272    734   2626  -2513       C  
ATOM    243  NH1 ARG A  78      34.627 -12.849 135.382  1.00 67.18           N  
ANISOU  243  NH1 ARG A  78     9713   6923   8887   1335   2648  -2337       N  
ATOM    244  NH2 ARG A  78      32.699 -12.438 134.213  1.00 64.01           N  
ANISOU  244  NH2 ARG A  78     8972   6830   8518   -132   2729  -2997       N  
ATOM    245  N   HIS A  79      33.537  -7.019 140.546  1.00 48.82           N  
ANISOU  245  N   HIS A  79     7153   6052   5344   2375    364  -1434       N  
ATOM    246  CA  HIS A  79      33.955  -6.667 141.910  1.00 52.09           C  
ANISOU  246  CA  HIS A  79     7635   6847   5309   3173     -1  -1356       C  
ATOM    247  C   HIS A  79      32.871  -5.942 142.730  1.00 48.69           C  
ANISOU  247  C   HIS A  79     7270   6540   4687   2874     37   -796       C  
ATOM    248  O   HIS A  79      32.810  -6.106 143.948  1.00 52.85           O  
ANISOU  248  O   HIS A  79     7932   7548   4598   3432     13   -732       O  
ATOM    249  CB  HIS A  79      35.244  -5.806 141.889  1.00 55.67           C  
ANISOU  249  CB  HIS A  79     7154   8175   5820   3086   -212  -2122       C  
ATOM    250  CG  HIS A  79      35.051  -4.403 141.381  1.00 55.15           C  
ANISOU  250  CG  HIS A  79     7084   7802   6066   2020     -8  -2263       C  
ATOM    251  ND1 HIS A  79      35.104  -4.075 140.040  1.00 54.60           N  
ANISOU  251  ND1 HIS A  79     7178   7605   5962   1323    224  -2533       N  
ATOM    252  CD2 HIS A  79      34.813  -3.240 142.042  1.00 55.72           C  
ANISOU  252  CD2 HIS A  79     7083   8098   5988   1539   -231  -2725       C  
ATOM    253  CE1 HIS A  79      34.906  -2.774 139.897  1.00 53.76           C  
ANISOU  253  CE1 HIS A  79     6826   7411   6189    675    509  -2441       C  
ATOM    254  NE2 HIS A  79      34.725  -2.244 141.096  1.00 53.97           N  
ANISOU  254  NE2 HIS A  79     6724   7409   6370    719     65  -2793       N  
ATOM    255  N   VAL A  80      32.029  -5.159 142.048  1.00 42.43           N  
ANISOU  255  N   VAL A  80     6485   5317   4317   2027    201   -836       N  
ATOM    256  CA  VAL A  80      31.089  -4.246 142.689  1.00 39.38           C  
ANISOU  256  CA  VAL A  80     6287   4739   3936   1775      8   -685       C  
ATOM    257  C   VAL A  80      30.099  -4.999 143.588  1.00 39.57           C  
ANISOU  257  C   VAL A  80     6923   4397   3715   2157     87   -193       C  
ATOM    258  O   VAL A  80      29.474  -5.972 143.156  1.00 39.37           O  
ANISOU  258  O   VAL A  80     7381   3790   3787   2073    258    269       O  
ATOM    259  CB  VAL A  80      30.325  -3.402 141.632  1.00 36.23           C  
ANISOU  259  CB  VAL A  80     5943   4184   3638   1114    152   -621       C  
ATOM    260  CG1 VAL A  80      29.219  -2.574 142.271  1.00 35.75           C  
ANISOU  260  CG1 VAL A  80     5826   3999   3758   1098     99   -332       C  
ATOM    261  CG2 VAL A  80      31.283  -2.487 140.884  1.00 37.62           C  
ANISOU  261  CG2 VAL A  80     5751   4560   3982    884    321   -892       C  
ATOM    262  N   ASP A  81      29.981  -4.542 144.833  1.00 39.59           N  
ANISOU  262  N   ASP A  81     6814   4490   3739   2611     47   -258       N  
ATOM    263  CA  ASP A  81      29.036  -5.099 145.801  1.00 41.43           C  
ANISOU  263  CA  ASP A  81     7717   4304   3721   2834    334    164       C  
ATOM    264  C   ASP A  81      27.737  -4.312 145.675  1.00 36.96           C  
ANISOU  264  C   ASP A  81     7044   3524   3475   2090    628     25       C  
ATOM    265  O   ASP A  81      27.678  -3.141 146.055  1.00 33.41           O  
ANISOU  265  O   ASP A  81     6181   3601   2911   1868    664    -84       O  
ATOM    266  CB  ASP A  81      29.604  -4.984 147.210  1.00 46.62           C  
ANISOU  266  CB  ASP A  81     8499   5489   3723   3669     87    111       C  
ATOM    267  CG  ASP A  81      28.651  -5.486 148.288  1.00 51.30           C  
ANISOU  267  CG  ASP A  81     9711   5705   4073   3791    565    734       C  
ATOM    268  OD1 ASP A  81      27.517  -5.898 147.990  1.00 49.80           O  
ANISOU  268  OD1 ASP A  81     9925   4934   4063   3418    752   1001       O  
ATOM    269  OD2 ASP A  81      29.048  -5.448 149.469  1.00 59.29           O  
ANISOU  269  OD2 ASP A  81    10932   7566   4029   4190    471   1013       O  
ATOM    270  N   CYS A  82      26.702  -4.960 145.149  1.00 36.04           N  
ANISOU  270  N   CYS A  82     7289   2962   3443   1782    911    105       N  
ATOM    271  CA  CYS A  82      25.476  -4.258 144.800  1.00 34.62           C  
ANISOU  271  CA  CYS A  82     6685   3047   3421   1238    887     15       C  
ATOM    272  C   CYS A  82      24.657  -3.809 146.022  1.00 32.06           C  
ANISOU  272  C   CYS A  82     6360   2572   3247   1238    757    219       C  
ATOM    273  O   CYS A  82      24.004  -2.777 145.975  1.00 27.03           O  
ANISOU  273  O   CYS A  82     5436   2200   2632    748    474   -195       O  
ATOM    274  CB  CYS A  82      24.660  -5.055 143.774  1.00 38.80           C  
ANISOU  274  CB  CYS A  82     6995   3416   4331    575    854   -155       C  
ATOM    275  SG  CYS A  82      25.372  -4.940 142.091  1.00 43.15           S  
ANISOU  275  SG  CYS A  82     7561   4370   4464    793    891   -101       S  
ATOM    276  N   GLN A  83      24.728  -4.552 147.119  1.00 35.54           N  
ANISOU  276  N   GLN A  83     7410   2683   3411   1609   1160    382       N  
ATOM    277  CA  GLN A  83      24.145  -4.094 148.379  1.00 36.75           C  
ANISOU  277  CA  GLN A  83     7933   2670   3359   1679   1299    521       C  
ATOM    278  C   GLN A  83      24.785  -2.774 148.853  1.00 33.24           C  
ANISOU  278  C   GLN A  83     6996   2803   2827   1971    722    583       C  
ATOM    279  O   GLN A  83      24.084  -1.870 149.297  1.00 31.02           O  
ANISOU  279  O   GLN A  83     6269   2601   2917   1462    805    451       O  
ATOM    280  CB  GLN A  83      24.269  -5.173 149.464  1.00 43.44           C  
ANISOU  280  CB  GLN A  83     9696   2938   3869   2373   1861    949       C  
ATOM    281  CG  GLN A  83      23.580  -4.832 150.779  1.00 46.21           C  
ANISOU  281  CG  GLN A  83    10443   3118   3995   2566   2184   1150       C  
ATOM    282  CD  GLN A  83      22.101  -4.511 150.617  1.00 46.32           C  
ANISOU  282  CD  GLN A  83     9971   2908   4720   1613   2489    697       C  
ATOM    283  OE1 GLN A  83      21.622  -3.478 151.085  1.00 45.60           O  
ANISOU  283  OE1 GLN A  83     9037   3460   4827   1605   2523    381       O  
ATOM    284  NE2 GLN A  83      21.377  -5.386 149.934  1.00 49.59           N  
ANISOU  284  NE2 GLN A  83    10543   2983   5314    978   3060    406       N  
ATOM    285  N   SER A  84      26.105  -2.668 148.740  1.00 32.60           N  
ANISOU  285  N   SER A  84     6835   3113   2436   2433    316    544       N  
ATOM    286  CA  SER A  84      26.827  -1.470 149.176  1.00 32.71           C  
ANISOU  286  CA  SER A  84     6233   3780   2414   2414     -9    187       C  
ATOM    287  C   SER A  84      26.479  -0.275 148.291  1.00 28.22           C  
ANISOU  287  C   SER A  84     5166   3194   2359   1661    113     30       C  
ATOM    288  O   SER A  84      26.355   0.840 148.776  1.00 28.36           O  
ANISOU  288  O   SER A  84     4829   3167   2779   1467    200    -60       O  
ATOM    289  CB  SER A  84      28.329  -1.716 149.157  1.00 36.64           C  
ANISOU  289  CB  SER A  84     6350   4951   2621   2852   -427   -207       C  
ATOM    290  OG  SER A  84      28.641  -2.855 149.938  1.00 42.76           O  
ANISOU  290  OG  SER A  84     7313   5854   3077   3821   -424    209       O  
ATOM    291  N   VAL A  85      26.315  -0.535 147.000  1.00 26.27           N  
ANISOU  291  N   VAL A  85     4873   2692   2414   1385     -9     72       N  
ATOM    292  CA  VAL A  85      25.912   0.480 146.042  1.00 25.80           C  
ANISOU  292  CA  VAL A  85     4868   2514   2420   1107    111    119       C  
ATOM    293  C   VAL A  85      24.541   1.037 146.435  1.00 25.43           C  
ANISOU  293  C   VAL A  85     4774   2254   2634   1012     96    321       C  
ATOM    294  O   VAL A  85      24.358   2.270 146.517  1.00 24.31           O  
ANISOU  294  O   VAL A  85     4249   2123   2864    762    265    367       O  
ATOM    295  CB  VAL A  85      25.892  -0.083 144.621  1.00 26.13           C  
ANISOU  295  CB  VAL A  85     5021   2529   2378   1023    151    154       C  
ATOM    296  CG1 VAL A  85      25.204   0.873 143.643  1.00 27.26           C  
ANISOU  296  CG1 VAL A  85     5118   2688   2553   1118    193    296       C  
ATOM    297  CG2 VAL A  85      27.320  -0.349 144.155  1.00 27.51           C  
ANISOU  297  CG2 VAL A  85     4941   2815   2694   1030      0    -56       C  
ATOM    298  N   TRP A  86      23.597   0.131 146.700  1.00 24.34           N  
ANISOU  298  N   TRP A  86     4901   2120   2225   1075    257    459       N  
ATOM    299  CA  TRP A  86      22.266   0.542 147.127  1.00 24.46           C  
ANISOU  299  CA  TRP A  86     4857   2214   2222    934    323    342       C  
ATOM    300  C   TRP A  86      22.328   1.362 148.440  1.00 24.26           C  
ANISOU  300  C   TRP A  86     4760   2072   2382    981    217    268       C  
ATOM    301  O   TRP A  86      21.738   2.435 148.524  1.00 25.02           O  
ANISOU  301  O   TRP A  86     4629   1912   2963    827    384    386       O  
ATOM    302  CB  TRP A  86      21.302  -0.664 147.239  1.00 25.80           C  
ANISOU  302  CB  TRP A  86     5105   2171   2526    816    554    -19       C  
ATOM    303  CG  TRP A  86      20.036  -0.315 147.948  1.00 26.63           C  
ANISOU  303  CG  TRP A  86     5168   2345   2604    607    697   -183       C  
ATOM    304  CD1 TRP A  86      19.604  -0.812 149.128  1.00 28.40           C  
ANISOU  304  CD1 TRP A  86     5705   2177   2908    443   1109   -193       C  
ATOM    305  CD2 TRP A  86      19.074   0.676 147.548  1.00 27.55           C  
ANISOU  305  CD2 TRP A  86     4784   2959   2725    730    494   -343       C  
ATOM    306  NE1 TRP A  86      18.421  -0.212 149.498  1.00 29.52           N  
ANISOU  306  NE1 TRP A  86     5491   2546   3176    274   1122   -418       N  
ATOM    307  CE2 TRP A  86      18.067   0.702 148.541  1.00 29.23           C  
ANISOU  307  CE2 TRP A  86     4974   3070   3062    513    742   -523       C  
ATOM    308  CE3 TRP A  86      18.953   1.525 146.436  1.00 27.86           C  
ANISOU  308  CE3 TRP A  86     4560   3385   2641   1068    255   -291       C  
ATOM    309  CZ2 TRP A  86      16.950   1.562 148.464  1.00 30.89           C  
ANISOU  309  CZ2 TRP A  86     4732   3728   3275    630    577   -828       C  
ATOM    310  CZ3 TRP A  86      17.849   2.368 146.350  1.00 30.54           C  
ANISOU  310  CZ3 TRP A  86     4659   4112   2832   1416     61   -410       C  
ATOM    311  CH2 TRP A  86      16.859   2.383 147.366  1.00 31.89           C  
ANISOU  311  CH2 TRP A  86     4600   4313   3201   1186    217   -729       C  
ATOM    312  N   ASP A  87      23.054   0.868 149.441  1.00 26.56           N  
ANISOU  312  N   ASP A  87     3727   2291   4072    367    641    267       N  
ATOM    313  CA  ASP A  87      23.197   1.591 150.713  1.00 27.31           C  
ANISOU  313  CA  ASP A  87     4009   2436   3930    645    598    325       C  
ATOM    314  C   ASP A  87      23.720   3.015 150.503  1.00 25.34           C  
ANISOU  314  C   ASP A  87     3659   2451   3518    611    300    286       C  
ATOM    315  O   ASP A  87      23.183   3.969 151.071  1.00 24.89           O  
ANISOU  315  O   ASP A  87     3736   2402   3318    525    118    236       O  
ATOM    316  CB  ASP A  87      24.127   0.854 151.688  1.00 29.65           C  
ANISOU  316  CB  ASP A  87     4489   2747   4029    962    554    463       C  
ATOM    317  CG  ASP A  87      23.549  -0.465 152.191  1.00 32.44           C  
ANISOU  317  CG  ASP A  87     5054   2883   4386    939    949    629       C  
ATOM    318  OD1 ASP A  87      22.332  -0.688 152.117  1.00 35.10           O  
ANISOU  318  OD1 ASP A  87     5098   3441   4796    723   1151    854       O  
ATOM    319  OD2 ASP A  87      24.334  -1.305 152.663  1.00 34.93           O  
ANISOU  319  OD2 ASP A  87     5801   3087   4382   1082    930    976       O  
ATOM    320  N   ALA A  88      24.753   3.144 149.679  1.00 23.87           N  
ANISOU  320  N   ALA A  88     3332   2326   3411    624     61    115       N  
ATOM    321  CA  ALA A  88      25.313   4.447 149.337  1.00 23.60           C  
ANISOU  321  CA  ALA A  88     3138   2456   3370    518     22     64       C  
ATOM    322  C   ALA A  88      24.308   5.355 148.603  1.00 22.12           C  
ANISOU  322  C   ALA A  88     2937   2219   3245    362     98     -1       C  
ATOM    323  O   ALA A  88      24.303   6.557 148.829  1.00 22.16           O  
ANISOU  323  O   ALA A  88     2898   2306   3213    554    -14   -301       O  
ATOM    324  CB  ALA A  88      26.574   4.276 148.505  1.00 23.84           C  
ANISOU  324  CB  ALA A  88     3053   2454   3551    591    -20    -96       C  
ATOM    325  N   PHE A  89      23.482   4.765 147.733  1.00 21.42           N  
ANISOU  325  N   PHE A  89     2762   2137   3238    156    324    -18       N  
ATOM    326  CA  PHE A  89      22.491   5.490 146.936  1.00 21.71           C  
ANISOU  326  CA  PHE A  89     2717   2139   3391     58    221    -26       C  
ATOM    327  C   PHE A  89      21.426   6.030 147.881  1.00 22.22           C  
ANISOU  327  C   PHE A  89     2970   2107   3365    146    226   -108       C  
ATOM    328  O   PHE A  89      21.150   7.210 147.897  1.00 20.97           O  
ANISOU  328  O   PHE A  89     2950   2186   2829    442    111   -221       O  
ATOM    329  CB  PHE A  89      21.855   4.557 145.890  1.00 22.64           C  
ANISOU  329  CB  PHE A  89     2852   2237   3510     14    325   -189       C  
ATOM    330  CG  PHE A  89      21.186   5.253 144.723  1.00 23.33           C  
ANISOU  330  CG  PHE A  89     2882   2405   3577     10    188   -216       C  
ATOM    331  CD1 PHE A  89      21.229   4.670 143.461  1.00 24.67           C  
ANISOU  331  CD1 PHE A  89     3166   2461   3746    -61     80   -412       C  
ATOM    332  CD2 PHE A  89      20.500   6.465 144.857  1.00 23.40           C  
ANISOU  332  CD2 PHE A  89     2885   2457   3547      9    218   -218       C  
ATOM    333  CE1 PHE A  89      20.606   5.276 142.367  1.00 25.11           C  
ANISOU  333  CE1 PHE A  89     3170   2634   3737    -48     26   -488       C  
ATOM    334  CE2 PHE A  89      19.883   7.070 143.768  1.00 23.64           C  
ANISOU  334  CE2 PHE A  89     2891   2558   3532      8    132   -289       C  
ATOM    335  CZ  PHE A  89      19.930   6.478 142.523  1.00 24.02           C  
ANISOU  335  CZ  PHE A  89     2936   2658   3532    -54     73   -339       C  
ATOM    336  N   LYS A  90      20.853   5.123 148.660  1.00 24.31           N  
ANISOU  336  N   LYS A  90     3360   2388   3489    127    409     80       N  
ATOM    337  CA  LYS A  90      19.856   5.420 149.653  1.00 25.73           C  
ANISOU  337  CA  LYS A  90     3482   2524   3771    265    487      8       C  
ATOM    338  C   LYS A  90      20.381   6.450 150.686  1.00 25.44           C  
ANISOU  338  C   LYS A  90     3461   2579   3623    317    331    126       C  
ATOM    339  O   LYS A  90      19.667   7.374 151.070  1.00 25.74           O  
ANISOU  339  O   LYS A  90     4102   2410   3268    261    451    -95       O  
ATOM    340  CB  LYS A  90      19.484   4.098 150.326  1.00 28.52           C  
ANISOU  340  CB  LYS A  90     3990   2585   4257     92    682     92       C  
ATOM    341  CG  LYS A  90      18.317   4.143 151.251  1.00 31.35           C  
ANISOU  341  CG  LYS A  90     4292   3022   4596    181    947    194       C  
ATOM    342  CD  LYS A  90      17.975   2.757 151.787  1.00 35.35           C  
ANISOU  342  CD  LYS A  90     5059   3129   5242    166   1153    426       C  
ATOM    343  CE  LYS A  90      19.154   2.122 152.512  1.00 38.10           C  
ANISOU  343  CE  LYS A  90     5389   3644   5444    491   1153    612       C  
ATOM    344  NZ  LYS A  90      18.753   0.944 153.319  1.00 42.88           N  
ANISOU  344  NZ  LYS A  90     6416   3721   6155    576   1464    889       N  
ATOM    345  N   GLY A  91      21.635   6.304 151.101  1.00 25.20           N  
ANISOU  345  N   GLY A  91     3562   2588   3421    286    152    212       N  
ATOM    346  CA  GLY A  91      22.247   7.248 152.022  1.00 25.30           C  
ANISOU  346  CA  GLY A  91     3610   2659   3342    487     98     88       C  
ATOM    347  C   GLY A  91      22.363   8.683 151.508  1.00 23.71           C  
ANISOU  347  C   GLY A  91     3238   2600   3169    584   -169      2       C  
ATOM    348  O   GLY A  91      22.457   9.620 152.302  1.00 24.17           O  
ANISOU  348  O   GLY A  91     3199   2501   3483    501   -430    -57       O  
ATOM    349  N   ALA A  92      22.377   8.870 150.195  1.00 22.02           N  
ANISOU  349  N   ALA A  92     2856   2355   3152    382    -94    -88       N  
ATOM    350  CA  ALA A  92      22.399  10.219 149.615  1.00 21.05           C  
ANISOU  350  CA  ALA A  92     2593   2289   3114    175   -163   -159       C  
ATOM    351  C   ALA A  92      21.152  11.060 149.904  1.00 20.67           C  
ANISOU  351  C   ALA A  92     2538   2237   3077    138   -195   -105       C  
ATOM    352  O   ALA A  92      21.253  12.289 149.976  1.00 20.19           O  
ANISOU  352  O   ALA A  92     2308   2266   3098    133    -25   -383       O  
ATOM    353  CB  ALA A  92      22.635  10.154 148.124  1.00 20.24           C  
ANISOU  353  CB  ALA A  92     2377   2190   3123     91   -138    -97       C  
ATOM    354  N   PHE A  93      19.988  10.424 150.047  1.00 20.11           N  
ANISOU  354  N   PHE A  93     2610   2163   2866    132    -71     63       N  
ATOM    355  CA  PHE A  93      18.719  11.175 150.117  1.00 20.62           C  
ANISOU  355  CA  PHE A  93     2599   2237   2999    114     63   -132       C  
ATOM    356  C   PHE A  93      17.749  10.822 151.255  1.00 21.90           C  
ANISOU  356  C   PHE A  93     2841   2353   3125     95    200    -40       C  
ATOM    357  O   PHE A  93      16.823  11.597 151.517  1.00 22.48           O  
ANISOU  357  O   PHE A  93     2754   2595   3193     97    313    -95       O  
ATOM    358  CB  PHE A  93      17.983  11.100 148.758  1.00 19.92           C  
ANISOU  358  CB  PHE A  93     2415   2107   3044     -9     93   -268       C  
ATOM    359  CG  PHE A  93      17.430   9.734 148.440  1.00 20.31           C  
ANISOU  359  CG  PHE A  93     2431   2040   3244   -103    232   -124       C  
ATOM    360  CD1 PHE A  93      16.126   9.401 148.793  1.00 20.55           C  
ANISOU  360  CD1 PHE A  93     2451   2066   3290    -61    345   -174       C  
ATOM    361  CD2 PHE A  93      18.208   8.780 147.770  1.00 20.20           C  
ANISOU  361  CD2 PHE A  93     2402   2044   3228   -138    260   -156       C  
ATOM    362  CE1 PHE A  93      15.610   8.135 148.519  1.00 21.38           C  
ANISOU  362  CE1 PHE A  93     2439   2172   3512   -195    392   -275       C  
ATOM    363  CE2 PHE A  93      17.691   7.507 147.487  1.00 20.51           C  
ANISOU  363  CE2 PHE A  93     2486   2091   3215   -169    314   -260       C  
ATOM    364  CZ  PHE A  93      16.391   7.183 147.870  1.00 20.92           C  
ANISOU  364  CZ  PHE A  93     2471   2059   3416   -227    327   -300       C  
ATOM    365  N   ILE A  94      17.947   9.690 151.925  1.00 22.77           N  
ANISOU  365  N   ILE A  94     3092   2378   3178    251    228    -16       N  
ATOM    366  CA  ILE A  94      17.081   9.292 153.041  1.00 25.25           C  
ANISOU  366  CA  ILE A  94     3487   2770   3337    361    502     23       C  
ATOM    367  C   ILE A  94      17.321  10.231 154.230  1.00 25.78           C  
ANISOU  367  C   ILE A  94     3597   2783   3413    419    431    -25       C  
ATOM    368  O   ILE A  94      18.442  10.698 154.430  1.00 26.67           O  
ANISOU  368  O   ILE A  94     3795   2844   3492    322    147   -446       O  
ATOM    369  CB  ILE A  94      17.322   7.806 153.413  1.00 27.87           C  
ANISOU  369  CB  ILE A  94     4047   2785   3758    362    791    145       C  
ATOM    370  CG1 ILE A  94      16.649   6.904 152.385  1.00 28.95           C  
ANISOU  370  CG1 ILE A  94     3929   2913   4154     73    717    205       C  
ATOM    371  CG2 ILE A  94      16.819   7.433 154.799  1.00 31.01           C  
ANISOU  371  CG2 ILE A  94     4590   3243   3948    512   1028    293       C  
ATOM    372  CD1 ILE A  94      15.146   7.036 152.305  1.00 30.21           C  
ANISOU  372  CD1 ILE A  94     3917   3018   4541    133    991    179       C  
ATOM    373  N   SER A  95      16.259  10.507 154.990  1.00 26.04           N  
ANISOU  373  N   SER A  95     3780   2751   3363    495    581     82       N  
ATOM    374  CA  SER A  95      16.311  11.393 156.170  1.00 27.48           C  
ANISOU  374  CA  SER A  95     4055   3077   3308    615    429     29       C  
ATOM    375  C   SER A  95      16.822  12.799 155.847  1.00 25.90           C  
ANISOU  375  C   SER A  95     3729   3015   3094    626    213    -82       C  
ATOM    376  O   SER A  95      17.390  13.470 156.692  1.00 28.07           O  
ANISOU  376  O   SER A  95     4363   3088   3213    519    133   -143       O  
ATOM    377  CB  SER A  95      17.120  10.749 157.317  1.00 30.15           C  
ANISOU  377  CB  SER A  95     4564   3499   3389    955    386    149       C  
ATOM    378  OG  SER A  95      16.491   9.562 157.810  1.00 33.71           O  
ANISOU  378  OG  SER A  95     5040   3723   4045    886    666    441       O  
ATOM    379  N   LYS A  96      16.604  13.244 154.623  1.00 23.25           N  
ANISOU  379  N   LYS A  96     3085   2634   3114    426     59   -201       N  
ATOM    380  CA  LYS A  96      17.006  14.560 154.195  1.00 22.92           C  
ANISOU  380  CA  LYS A  96     3071   2580   3058    436   -112   -257       C  
ATOM    381  C   LYS A  96      15.821  15.265 153.540  1.00 21.73           C  
ANISOU  381  C   LYS A  96     2754   2431   3069    268    -24   -347       C  
ATOM    382  O   LYS A  96      15.009  14.639 152.858  1.00 19.81           O  
ANISOU  382  O   LYS A  96     2397   2065   3065    347     89   -169       O  
ATOM    383  CB  LYS A  96      18.176  14.469 153.229  1.00 22.86           C  
ANISOU  383  CB  LYS A  96     2963   2533   3188    409   -144   -321       C  
ATOM    384  CG  LYS A  96      19.491  14.186 153.925  1.00 24.84           C  
ANISOU  384  CG  LYS A  96     3203   2867   3367    555   -321   -325       C  
ATOM    385  CD  LYS A  96      20.592  13.865 152.929  1.00 25.31           C  
ANISOU  385  CD  LYS A  96     3210   3038   3367    370   -275   -391       C  
ATOM    386  CE  LYS A  96      21.834  13.322 153.636  1.00 27.93           C  
ANISOU  386  CE  LYS A  96     3517   3390   3706    599   -442   -352       C  
ATOM    387  NZ  LYS A  96      22.717  12.534 152.725  1.00 28.48           N  
ANISOU  387  NZ  LYS A  96     3552   3339   3929    540   -382   -384       N  
ATOM    388  N   HIS A  97      15.739  16.571 153.768  1.00 21.61           N  
ANISOU  388  N   HIS A  97     2714   2440   3056    344    -66   -435       N  
ATOM    389  CA  HIS A  97      14.800  17.404 153.066  1.00 21.90           C  
ANISOU  389  CA  HIS A  97     2654   2448   3216    271   -156   -466       C  
ATOM    390  C   HIS A  97      15.162  17.348 151.592  1.00 20.61           C  
ANISOU  390  C   HIS A  97     2470   2162   3197    120   -189   -394       C  
ATOM    391  O   HIS A  97      16.308  17.603 151.234  1.00 20.37           O  
ANISOU  391  O   HIS A  97     2536   2457   2747    -24   -217   -592       O  
ATOM    392  CB  HIS A  97      14.854  18.855 153.547  1.00 23.32           C  
ANISOU  392  CB  HIS A  97     2847   2508   3505    340   -188   -566       C  
ATOM    393  CG  HIS A  97      13.658  19.645 153.136  1.00 24.16           C  
ANISOU  393  CG  HIS A  97     2836   2646   3698    337   -198   -470       C  
ATOM    394  ND1 HIS A  97      13.598  20.321 151.945  1.00 24.98           N  
ANISOU  394  ND1 HIS A  97     2746   2916   3829    235   -208   -297       N  
ATOM    395  CD2 HIS A  97      12.452  19.810 153.719  1.00 25.61           C  
ANISOU  395  CD2 HIS A  97     2950   3000   3780    477   -101   -585       C  
ATOM    396  CE1 HIS A  97      12.431  20.921 151.830  1.00 25.17           C  
ANISOU  396  CE1 HIS A  97     2768   2798   3995    280   -195   -455       C  
ATOM    397  NE2 HIS A  97      11.713  20.624 152.894  1.00 26.13           N  
ANISOU  397  NE2 HIS A  97     2941   3102   3884    439   -139   -506       N  
ATOM    398  N   PRO A  98      14.204  16.984 150.738  1.00 19.99           N  
ANISOU  398  N   PRO A  98     2350   2029   3215    158   -173   -326       N  
ATOM    399  CA  PRO A  98      14.505  16.760 149.329  1.00 20.30           C  
ANISOU  399  CA  PRO A  98     2251   2208   3252     62   -135   -369       C  
ATOM    400  C   PRO A  98      14.673  18.005 148.458  1.00 20.54           C  
ANISOU  400  C   PRO A  98     2131   2255   3416     20   -214   -263       C  
ATOM    401  O   PRO A  98      14.716  17.878 147.257  1.00 21.14           O  
ANISOU  401  O   PRO A  98     2179   2320   3531   -111      0   -474       O  
ATOM    402  CB  PRO A  98      13.306  15.901 148.860  1.00 21.08           C  
ANISOU  402  CB  PRO A  98     2257   2360   3389     14    -92   -438       C  
ATOM    403  CG  PRO A  98      12.192  16.332 149.741  1.00 21.43           C  
ANISOU  403  CG  PRO A  98     2256   2417   3469     42    -51   -384       C  
ATOM    404  CD  PRO A  98      12.808  16.641 151.067  1.00 21.17           C  
ANISOU  404  CD  PRO A  98     2430   2294   3319    113     31   -399       C  
ATOM    405  N   CYS A  99      14.702  19.193 149.044  1.00 21.52           N  
ANISOU  405  N   CYS A  99     2329   2336   3509    132   -239   -347       N  
ATOM    406  CA  CYS A  99      15.168  20.424 148.397  1.00 23.49           C  
ANISOU  406  CA  CYS A  99     2668   2393   3864    104   -319   -198       C  
ATOM    407  C   CYS A  99      16.544  20.849 148.916  1.00 22.81           C  
ANISOU  407  C   CYS A  99     2726   2158   3780    110   -334   -319       C  
ATOM    408  O   CYS A  99      17.049  21.895 148.548  1.00 23.00           O  
ANISOU  408  O   CYS A  99     2639   2195   3904   -121   -302   -556       O  
ATOM    409  CB  CYS A  99      14.144  21.560 148.599  1.00 25.56           C  
ANISOU  409  CB  CYS A  99     2986   2531   4193    327   -361   -231       C  
ATOM    410  SG  CYS A  99      12.588  21.190 147.748  1.00 27.52           S  
ANISOU  410  SG  CYS A  99     2983   2829   4642    300   -413   -359       S  
ATOM    411  N   ASP A 100      17.163  20.009 149.736  1.00 22.07           N  
ANISOU  411  N   ASP A 100     2579   2286   3518    216   -362   -531       N  
ATOM    412  CA  ASP A 100      18.450  20.336 150.329  1.00 23.20           C  
ANISOU  412  CA  ASP A 100     2507   2311   3994    104   -338   -529       C  
ATOM    413  C   ASP A 100      19.570  19.355 149.929  1.00 20.94           C  
ANISOU  413  C   ASP A 100     2335   2045   3577    -22   -417   -424       C  
ATOM    414  O   ASP A 100      20.515  19.177 150.692  1.00 21.96           O  
ANISOU  414  O   ASP A 100     2528   2351   3465    382   -408   -449       O  
ATOM    415  CB  ASP A 100      18.289  20.370 151.850  1.00 25.03           C  
ANISOU  415  CB  ASP A 100     2894   2638   3977    254   -459   -639       C  
ATOM    416  CG  ASP A 100      19.468  21.018 152.554  1.00 28.75           C  
ANISOU  416  CG  ASP A 100     3068   3053   4800    142   -645   -840       C  
ATOM    417  OD1 ASP A 100      19.905  22.129 152.112  1.00 30.20           O  
ANISOU  417  OD1 ASP A 100     2893   2740   5840    470   -527   -750       O  
ATOM    418  OD2 ASP A 100      19.947  20.392 153.556  1.00 32.92           O  
ANISOU  418  OD2 ASP A 100     3576   4046   4883    776   -944   -941       O  
ATOM    419  N   ILE A 101      19.504  18.778 148.728  1.00 18.63           N  
ANISOU  419  N   ILE A 101     1875   1794   3409    -42   -300   -228       N  
ATOM    420  CA  ILE A 101      20.476  17.756 148.307  1.00 17.71           C  
ANISOU  420  CA  ILE A 101     1957   1669   3101   -113   -257   -217       C  
ATOM    421  C   ILE A 101      21.611  18.433 147.539  1.00 17.86           C  
ANISOU  421  C   ILE A 101     1948   1551   3284   -142   -242   -218       C  
ATOM    422  O   ILE A 101      21.367  19.348 146.749  1.00 17.74           O  
ANISOU  422  O   ILE A 101     1948   1442   3349   -206    -34   -158       O  
ATOM    423  CB  ILE A 101      19.856  16.665 147.405  1.00 16.69           C  
ANISOU  423  CB  ILE A 101     1866   1603   2869    -89   -197   -101       C  
ATOM    424  CG1 ILE A 101      18.527  16.155 147.963  1.00 16.25           C  
ANISOU  424  CG1 ILE A 101     1812   1627   2732    -56   -243   -133       C  
ATOM    425  CG2 ILE A 101      20.849  15.502 147.203  1.00 16.42           C  
ANISOU  425  CG2 ILE A 101     1816   1618   2805   -106   -193    -97       C  
ATOM    426  CD1 ILE A 101      18.630  15.464 149.308  1.00 16.48           C  
ANISOU  426  CD1 ILE A 101     1897   1681   2681    -24   -221   -179       C  
ATOM    427  N   THR A 102      22.833  17.972 147.763  1.00 18.18           N  
ANISOU  427  N   THR A 102     1902   1598   3405   -183   -294   -290       N  
ATOM    428  CA  THR A 102      24.009  18.513 147.066  1.00 20.06           C  
ANISOU  428  CA  THR A 102     1961   1782   3878   -257   -189   -233       C  
ATOM    429  C   THR A 102      24.829  17.391 146.460  1.00 19.96           C  
ANISOU  429  C   THR A 102     1958   1821   3802   -253   -207   -263       C  
ATOM    430  O   THR A 102      24.598  16.232 146.781  1.00 18.06           O  
ANISOU  430  O   THR A 102     1691   1843   3328    -40   -348   -105       O  
ATOM    431  CB  THR A 102      24.935  19.292 148.017  1.00 21.34           C  
ANISOU  431  CB  THR A 102     1971   1810   4324   -280   -249   -444       C  
ATOM    432  OG1 THR A 102      25.512  18.389 148.956  1.00 21.01           O  
ANISOU  432  OG1 THR A 102     1851   2127   4003   -232   -551   -708       O  
ATOM    433  CG2 THR A 102      24.177  20.366 148.750  1.00 22.00           C  
ANISOU  433  CG2 THR A 102     2058   1856   4443   -255   -301   -549       C  
ATOM    434  N   GLU A 103      25.786  17.746 145.602  1.00 22.13           N  
ANISOU  434  N   GLU A 103     2095   2075   4236   -455    -40   -169       N  
ATOM    435  CA  GLU A 103      26.686  16.750 144.997  1.00 24.54           C  
ANISOU  435  CA  GLU A 103     2337   2386   4599   -260    130   -153       C  
ATOM    436  C   GLU A 103      27.430  15.922 146.063  1.00 24.61           C  
ANISOU  436  C   GLU A 103     2189   2481   4680   -213     -5   -261       C  
ATOM    437  O   GLU A 103      27.600  14.716 145.890  1.00 24.01           O  
ANISOU  437  O   GLU A 103     2083   2498   4538   -118    255   -251       O  
ATOM    438  CB  GLU A 103      27.647  17.389 143.958  1.00 27.76           C  
ANISOU  438  CB  GLU A 103     2681   2663   5202   -459    443    -23       C  
ATOM    439  CG  GLU A 103      26.865  17.931 142.747  1.00 29.63           C  
ANISOU  439  CG  GLU A 103     3157   2789   5310   -362    483    199       C  
ATOM    440  CD  GLU A 103      27.696  18.407 141.552  1.00 33.06           C  
ANISOU  440  CD  GLU A 103     3670   3095   5795   -371    922    336       C  
ATOM    441  OE1 GLU A 103      28.762  17.829 141.231  1.00 36.02           O  
ANISOU  441  OE1 GLU A 103     3565   3401   6717   -456    935     -7       O  
ATOM    442  OE2 GLU A 103      27.257  19.381 140.906  1.00 37.57           O  
ANISOU  442  OE2 GLU A 103     4585   3797   5892   -100    522    605       O  
ATOM    443  N   GLU A 104      27.796  16.554 147.175  1.00 26.34           N  
ANISOU  443  N   GLU A 104     2356   2641   5009   -259   -111   -528       N  
ATOM    444  CA  GLU A 104      28.443  15.868 148.307  1.00 28.49           C  
ANISOU  444  CA  GLU A 104     2629   2986   5209    -64   -388   -600       C  
ATOM    445  C   GLU A 104      27.671  14.670 148.829  1.00 25.21           C  
ANISOU  445  C   GLU A 104     2381   2788   4408     52   -628   -725       C  
ATOM    446  O   GLU A 104      28.269  13.656 149.166  1.00 24.52           O  
ANISOU  446  O   GLU A 104     2267   2789   4260     73   -969  -1008       O  
ATOM    447  CB  GLU A 104      28.654  16.821 149.471  1.00 32.59           C  
ANISOU  447  CB  GLU A 104     3121   3443   5818    -23   -686  -1069       C  
ATOM    448  CG  GLU A 104      29.799  17.790 149.269  1.00 38.34           C  
ANISOU  448  CG  GLU A 104     3376   4123   7068   -335   -430   -994       C  
ATOM    449  CD  GLU A 104      31.117  17.258 149.796  1.00 43.34           C  
ANISOU  449  CD  GLU A 104     3767   4697   8003   -207  -1256  -1522       C  
ATOM    450  OE1 GLU A 104      31.390  16.049 149.625  1.00 49.24           O  
ANISOU  450  OE1 GLU A 104     5252   4807   8648    165   -589  -1148       O  
ATOM    451  OE2 GLU A 104      31.882  18.053 150.383  1.00 52.31           O  
ANISOU  451  OE2 GLU A 104     4584   5957   9334   -822  -1430  -1781       O  
ATOM    452  N   ASP A 105      26.346  14.787 148.893  1.00 23.10           N  
ANISOU  452  N   ASP A 105     2390   2424   3962      4   -469   -619       N  
ATOM    453  CA  ASP A 105      25.495  13.668 149.314  1.00 22.14           C  
ANISOU  453  CA  ASP A 105     2390   2398   3624    112   -462   -467       C  
ATOM    454  C   ASP A 105      25.699  12.400 148.456  1.00 20.81           C  
ANISOU  454  C   ASP A 105     2216   2278   3410     79   -372   -300       C  
ATOM    455  O   ASP A 105      25.535  11.299 148.941  1.00 20.61           O  
ANISOU  455  O   ASP A 105     2265   2112   3451    438   -544   -331       O  
ATOM    456  CB  ASP A 105      24.015  14.060 149.286  1.00 21.34           C  
ANISOU  456  CB  ASP A 105     2383   2254   3469     65   -358   -307       C  
ATOM    457  CG  ASP A 105      23.653  15.073 150.354  1.00 23.35           C  
ANISOU  457  CG  ASP A 105     2832   2479   3558    155   -423   -452       C  
ATOM    458  OD1 ASP A 105      23.977  14.833 151.513  1.00 26.00           O  
ANISOU  458  OD1 ASP A 105     3629   2653   3597    352   -549   -464       O  
ATOM    459  OD2 ASP A 105      23.045  16.114 150.051  1.00 23.81           O  
ANISOU  459  OD2 ASP A 105     2827   2565   3654    329   -153   -548       O  
ATOM    460  N   TYR A 106      26.041  12.574 147.185  1.00 20.06           N  
ANISOU  460  N   TYR A 106     1989   2152   3480    -30   -274   -324       N  
ATOM    461  CA  TYR A 106      26.227  11.460 146.267  1.00 19.76           C  
ANISOU  461  CA  TYR A 106     2044   2166   3297     -7   -174   -232       C  
ATOM    462  C   TYR A 106      27.674  10.943 146.152  1.00 21.41           C  
ANISOU  462  C   TYR A 106     2110   2410   3615    107   -156   -301       C  
ATOM    463  O   TYR A 106      27.925  10.013 145.386  1.00 20.38           O  
ANISOU  463  O   TYR A 106     1985   2288   3468     69   -310   -260       O  
ATOM    464  CB  TYR A 106      25.678  11.841 144.888  1.00 18.57           C  
ANISOU  464  CB  TYR A 106     1852   1979   3222    -49    -11   -151       C  
ATOM    465  CG  TYR A 106      24.184  11.749 144.811  1.00 17.14           C  
ANISOU  465  CG  TYR A 106     1848   1792   2872   -102      1   -144       C  
ATOM    466  CD1 TYR A 106      23.547  10.511 144.812  1.00 16.42           C  
ANISOU  466  CD1 TYR A 106     1768   1733   2736    -32     23   -118       C  
ATOM    467  CD2 TYR A 106      23.387  12.901 144.750  1.00 16.71           C  
ANISOU  467  CD2 TYR A 106     1771   1734   2843   -162    -55   -110       C  
ATOM    468  CE1 TYR A 106      22.172  10.413 144.745  1.00 15.82           C  
ANISOU  468  CE1 TYR A 106     1762   1661   2585   -116     16   -120       C  
ATOM    469  CE2 TYR A 106      22.008  12.812 144.684  1.00 15.62           C  
ANISOU  469  CE2 TYR A 106     1746   1622   2565   -118     19   -153       C  
ATOM    470  CZ  TYR A 106      21.400  11.570 144.679  1.00 15.49           C  
ANISOU  470  CZ  TYR A 106     1709   1647   2526   -132     35   -142       C  
ATOM    471  OH  TYR A 106      20.015  11.482 144.599  1.00 14.85           O  
ANISOU  471  OH  TYR A 106     1734   1415   2490   -238    -62   -287       O  
ATOM    472  N   GLN A 107      28.611  11.507 146.926  1.00 24.15           N  
ANISOU  472  N   GLN A 107     2309   2749   4115    -99   -279   -439       N  
ATOM    473  CA  GLN A 107      30.030  11.108 146.809  1.00 26.59           C  
ANISOU  473  CA  GLN A 107     2437   2988   4678    147   -322   -468       C  
ATOM    474  C   GLN A 107      30.309   9.634 147.107  1.00 24.33           C  
ANISOU  474  C   GLN A 107     2148   2916   4180    122   -370   -621       C  
ATOM    475  O   GLN A 107      31.043   9.008 146.362  1.00 23.63           O  
ANISOU  475  O   GLN A 107     2211   2496   4271     97   -514   -764       O  
ATOM    476  CB  GLN A 107      30.945  12.006 147.644  1.00 30.49           C  
ANISOU  476  CB  GLN A 107     2712   3545   5325     75   -542   -891       C  
ATOM    477  CG  GLN A 107      30.981  13.445 147.145  1.00 34.90           C  
ANISOU  477  CG  GLN A 107     3234   3806   6219   -110   -373   -559       C  
ATOM    478  CD  GLN A 107      31.913  13.643 145.960  1.00 41.26           C  
ANISOU  478  CD  GLN A 107     3944   4865   6865   -473    183   -732       C  
ATOM    479  OE1 GLN A 107      31.837  12.920 144.949  1.00 47.38           O  
ANISOU  479  OE1 GLN A 107     5614   4929   7459  -1063    -34  -1143       O  
ATOM    480  NE2 GLN A 107      32.811  14.634 146.077  1.00 46.27           N  
ANISOU  480  NE2 GLN A 107     4608   4906   8066   -748   -220   -809       N  
ATOM    481  N   PRO A 108      29.748   9.092 148.197  1.00 23.97           N  
ANISOU  481  N   PRO A 108     2316   2763   4029    250   -478   -555       N  
ATOM    482  CA  PRO A 108      29.912   7.657 148.442  1.00 24.26           C  
ANISOU  482  CA  PRO A 108     2454   2855   3908    544   -441   -479       C  
ATOM    483  C   PRO A 108      29.426   6.765 147.293  1.00 23.03           C  
ANISOU  483  C   PRO A 108     2436   2584   3730    439   -232   -339       C  
ATOM    484  O   PRO A 108      30.092   5.795 146.965  1.00 23.73           O  
ANISOU  484  O   PRO A 108     2304   2793   3917    551    -95   -244       O  
ATOM    485  CB  PRO A 108      29.084   7.424 149.704  1.00 24.63           C  
ANISOU  485  CB  PRO A 108     2781   2857   3718    682   -474   -397       C  
ATOM    486  CG  PRO A 108      29.137   8.732 150.424  1.00 25.30           C  
ANISOU  486  CG  PRO A 108     2789   2989   3832    583   -696   -536       C  
ATOM    487  CD  PRO A 108      29.069   9.758 149.325  1.00 24.41           C  
ANISOU  487  CD  PRO A 108     2510   2825   3938    390   -568   -552       C  
ATOM    488  N   LEU A 109      28.285   7.101 146.689  1.00 21.31           N  
ANISOU  488  N   LEU A 109     2347   2261   3485    274   -103   -274       N  
ATOM    489  CA  LEU A 109      27.799   6.408 145.510  1.00 21.09           C  
ANISOU  489  CA  LEU A 109     2288   2310   3412    193    -66   -212       C  
ATOM    490  C   LEU A 109      28.749   6.527 144.305  1.00 22.17           C  
ANISOU  490  C   LEU A 109     2322   2528   3573    177     40   -267       C  
ATOM    491  O   LEU A 109      28.962   5.544 143.595  1.00 22.31           O  
ANISOU  491  O   LEU A 109     2238   2683   3554    348    176   -281       O  
ATOM    492  CB  LEU A 109      26.403   6.890 145.124  1.00 20.02           C  
ANISOU  492  CB  LEU A 109     2213   2168   3224     41     -4   -125       C  
ATOM    493  CG  LEU A 109      25.733   6.183 143.925  1.00 19.68           C  
ANISOU  493  CG  LEU A 109     2209   2112   3156     52     73   -154       C  
ATOM    494  CD1 LEU A 109      25.596   4.684 144.148  1.00 19.98           C  
ANISOU  494  CD1 LEU A 109     2259   2102   3230     68    112   -155       C  
ATOM    495  CD2 LEU A 109      24.367   6.801 143.661  1.00 19.05           C  
ANISOU  495  CD2 LEU A 109     2115   2063   3058    -59     81   -169       C  
ATOM    496  N   MET A 110      29.303   7.716 144.077  1.00 22.93           N  
ANISOU  496  N   MET A 110     2234   2643   3833     42    -14   -320       N  
ATOM    497  CA  MET A 110      30.231   7.923 142.970  1.00 24.94           C  
ANISOU  497  CA  MET A 110     2387   2943   4144     28    235   -385       C  
ATOM    498  C   MET A 110      31.479   7.079 143.158  1.00 25.70           C  
ANISOU  498  C   MET A 110     2435   2885   4443     53    187   -377       C  
ATOM    499  O   MET A 110      31.963   6.492 142.207  1.00 25.44           O  
ANISOU  499  O   MET A 110     2377   2782   4506     73    439   -124       O  
ATOM    500  CB  MET A 110      30.655   9.383 142.832  1.00 26.72           C  
ANISOU  500  CB  MET A 110     2533   3046   4573   -116    291   -359       C  
ATOM    501  CG  MET A 110      29.571  10.386 142.480  1.00 27.31           C  
ANISOU  501  CG  MET A 110     2631   3103   4643    -95    369   -145       C  
ATOM    502  SD  MET A 110      28.736  10.034 140.944  1.00 29.36           S  
ANISOU  502  SD  MET A 110     3128   3378   4647    -26    366   -146       S  
ATOM    503  CE  MET A 110      27.176   9.403 141.568  1.00 27.96           C  
ANISOU  503  CE  MET A 110     3107   3261   4255    -12    257   -191       C  
ATOM    504  N   LYS A 111      31.989   7.006 144.381  1.00 26.44           N  
ANISOU  504  N   LYS A 111     2506   2969   4568    165     58   -510       N  
ATOM    505  CA  LYS A 111      33.148   6.169 144.665  1.00 28.68           C  
ANISOU  505  CA  LYS A 111     2575   3358   4965    368    -29   -659       C  
ATOM    506  C   LYS A 111      32.874   4.694 144.332  1.00 27.99           C  
ANISOU  506  C   LYS A 111     2607   3310   4717    407     13   -584       C  
ATOM    507  O   LYS A 111      33.634   4.080 143.587  1.00 28.81           O  
ANISOU  507  O   LYS A 111     2599   2995   5351    505    -86   -884       O  
ATOM    508  CB  LYS A 111      33.587   6.312 146.111  1.00 30.81           C  
ANISOU  508  CB  LYS A 111     2817   3744   5143    400   -297   -728       C  
ATOM    509  CG  LYS A 111      34.644   5.293 146.526  1.00 34.20           C  
ANISOU  509  CG  LYS A 111     3118   4152   5722    770   -409   -845       C  
ATOM    510  CD  LYS A 111      35.317   5.703 147.822  1.00 38.13           C  
ANISOU  510  CD  LYS A 111     3637   4784   6066    848   -739  -1082       C  
ATOM    511  CE  LYS A 111      34.383   5.568 149.020  1.00 39.44           C  
ANISOU  511  CE  LYS A 111     3972   4990   6022    983   -661   -941       C  
ATOM    512  NZ  LYS A 111      34.399   6.795 149.874  1.00 41.48           N  
ANISOU  512  NZ  LYS A 111     4363   5204   6192    957   -883  -1143       N  
ATOM    513  N   LEU A 112      31.786   4.146 144.859  1.00 26.73           N  
ANISOU  513  N   LEU A 112     2696   3104   4354    407    -40   -508       N  
ATOM    514  CA  LEU A 112      31.433   2.746 144.596  1.00 26.81           C  
ANISOU  514  CA  LEU A 112     2786   3016   4384    562     32   -499       C  
ATOM    515  C   LEU A 112      31.072   2.480 143.139  1.00 26.17           C  
ANISOU  515  C   LEU A 112     2605   3060   4276    372    277   -434       C  
ATOM    516  O   LEU A 112      31.351   1.402 142.632  1.00 28.40           O  
ANISOU  516  O   LEU A 112     3191   3070   4529    446    507   -411       O  
ATOM    517  CB  LEU A 112      30.276   2.285 145.496  1.00 26.14           C  
ANISOU  517  CB  LEU A 112     2957   2788   4186    581    -12   -344       C  
ATOM    518  CG  LEU A 112      30.569   2.225 146.995  1.00 27.76           C  
ANISOU  518  CG  LEU A 112     3233   3038   4276    772   -153   -267       C  
ATOM    519  CD1 LEU A 112      29.346   1.781 147.782  1.00 27.50           C  
ANISOU  519  CD1 LEU A 112     3411   2908   4128    817    -69   -147       C  
ATOM    520  CD2 LEU A 112      31.753   1.306 147.286  1.00 29.93           C  
ANISOU  520  CD2 LEU A 112     3459   3322   4588   1026   -208   -319       C  
ATOM    521  N   GLY A 113      30.458   3.447 142.468  1.00 24.91           N  
ANISOU  521  N   GLY A 113     2351   2958   4154    153    423   -338       N  
ATOM    522  CA  GLY A 113      29.997   3.256 141.089  1.00 26.92           C  
ANISOU  522  CA  GLY A 113     2770   3215   4244    174    317   -493       C  
ATOM    523  C   GLY A 113      30.953   3.714 140.010  1.00 29.13           C  
ANISOU  523  C   GLY A 113     2992   3674   4398    160    521   -505       C  
ATOM    524  O   GLY A 113      30.650   3.585 138.834  1.00 27.74           O  
ANISOU  524  O   GLY A 113     2606   3432   4501   -182    359   -346       O  
ATOM    525  N   THR A 114      32.113   4.232 140.412  1.00 32.96           N  
ANISOU  525  N   THR A 114     3276   4195   5051   -113    403   -703       N  
ATOM    526  CA  THR A 114      33.140   4.721 139.490  1.00 35.91           C  
ANISOU  526  CA  THR A 114     3549   4630   5462      6    726   -507       C  
ATOM    527  C   THR A 114      33.525   3.648 138.491  1.00 35.29           C  
ANISOU  527  C   THR A 114     3218   4606   5585    146    754   -518       C  
ATOM    528  O   THR A 114      33.499   2.451 138.792  1.00 36.01           O  
ANISOU  528  O   THR A 114     2910   4770   6003    663    459   -263       O  
ATOM    529  CB  THR A 114      34.407   5.220 140.240  1.00 40.28           C  
ANISOU  529  CB  THR A 114     3723   5221   6359    -88    374   -478       C  
ATOM    530  OG1 THR A 114      35.261   5.907 139.323  1.00 49.70           O  
ANISOU  530  OG1 THR A 114     5028   6580   7274  -1133    624    -22       O  
ATOM    531  CG2 THR A 114      35.197   4.069 140.863  1.00 40.71           C  
ANISOU  531  CG2 THR A 114     3793   5132   6543    199    411   -637       C  
ATOM    532  N   GLN A 115      33.864   4.083 137.292  1.00 35.61           N  
ANISOU  532  N   GLN A 115     3469   4506   5554    142    815   -591       N  
ATOM    533  CA  GLN A 115      34.042   3.172 136.174  1.00 36.29           C  
ANISOU  533  CA  GLN A 115     3559   4800   5430    325    961   -578       C  
ATOM    534  C   GLN A 115      34.953   3.844 135.159  1.00 37.82           C  
ANISOU  534  C   GLN A 115     3793   4962   5614    341   1175   -475       C  
ATOM    535  O   GLN A 115      34.845   5.035 134.936  1.00 36.63           O  
ANISOU  535  O   GLN A 115     3726   4894   5297      6   1502   -325       O  
ATOM    536  CB  GLN A 115      32.654   2.884 135.603  1.00 34.83           C  
ANISOU  536  CB  GLN A 115     3694   4593   4947    323    921   -666       C  
ATOM    537  CG  GLN A 115      32.569   2.081 134.326  1.00 34.97           C  
ANISOU  537  CG  GLN A 115     3691   4691   4904    499   1115   -738       C  
ATOM    538  CD  GLN A 115      31.133   1.722 133.985  1.00 32.94           C  
ANISOU  538  CD  GLN A 115     3754   4337   4423    553    951   -727       C  
ATOM    539  OE1 GLN A 115      30.195   2.203 134.614  1.00 30.32           O  
ANISOU  539  OE1 GLN A 115     3466   3865   4189    286    912   -434       O  
ATOM    540  NE2 GLN A 115      30.957   0.875 132.997  1.00 34.04           N  
ANISOU  540  NE2 GLN A 115     3807   4672   4453    669    961   -916       N  
ATOM    541  N   THR A 116      35.874   3.087 134.578  1.00 40.46           N  
ANISOU  541  N   THR A 116     3884   5508   5980    467   1290   -662       N  
ATOM    542  CA  THR A 116      36.733   3.632 133.542  1.00 44.59           C  
ANISOU  542  CA  THR A 116     4472   6004   6464    450   1744   -517       C  
ATOM    543  C   THR A 116      36.041   3.321 132.238  1.00 45.75           C  
ANISOU  543  C   THR A 116     4846   6247   6290    617   1843   -702       C  
ATOM    544  O   THR A 116      35.879   2.158 131.880  1.00 47.29           O  
ANISOU  544  O   THR A 116     5433   6360   6175    740   1763   -955       O  
ATOM    545  CB  THR A 116      38.156   3.050 133.578  1.00 47.09           C  
ANISOU  545  CB  THR A 116     4454   6428   7010    505   1775   -718       C  
ATOM    546  OG1 THR A 116      38.655   3.130 134.912  1.00 48.88           O  
ANISOU  546  OG1 THR A 116     3937   7201   7433    146   1271   -493       O  
ATOM    547  CG2 THR A 116      39.091   3.845 132.662  1.00 50.20           C  
ANISOU  547  CG2 THR A 116     4777   6693   7601    427   2166   -637       C  
ATOM    548  N   VAL A 117      35.568   4.374 131.583  1.00 47.47           N  
ANISOU  548  N   VAL A 117     5266   6474   6297    683   1977   -435       N  
ATOM    549  CA  VAL A 117      35.027   4.302 130.238  1.00 49.53           C  
ANISOU  549  CA  VAL A 117     5700   6951   6165    716   2076   -396       C  
ATOM    550  C   VAL A 117      36.164   4.734 129.332  1.00 51.85           C  
ANISOU  550  C   VAL A 117     5948   7264   6488    755   2414   -278       C  
ATOM    551  O   VAL A 117      36.844   5.705 129.642  1.00 50.18           O  
ANISOU  551  O   VAL A 117     5853   7234   5978    624   2531      4       O  
ATOM    552  CB  VAL A 117      33.844   5.281 130.059  1.00 49.65           C  
ANISOU  552  CB  VAL A 117     5900   6958   6004    785   2028   -203       C  
ATOM    553  CG1 VAL A 117      33.267   5.202 128.653  1.00 52.02           C  
ANISOU  553  CG1 VAL A 117     6390   7429   5945    970   2028   -208       C  
ATOM    554  CG2 VAL A 117      32.770   4.991 131.088  1.00 47.69           C  
ANISOU  554  CG2 VAL A 117     5471   6713   5933    666   1709   -220       C  
ATOM    555  N   PRO A 118      36.390   4.011 128.218  1.00 38.11           N  
ANISOU  555  N   PRO A 118     4635   4772   5073    712    -57   -472       N  
ATOM    556  CA  PRO A 118      37.358   4.513 127.232  1.00 38.16           C  
ANISOU  556  CA  PRO A 118     4322   4858   5319    660    -37   -534       C  
ATOM    557  C   PRO A 118      36.962   5.919 126.796  1.00 36.03           C  
ANISOU  557  C   PRO A 118     4045   4695   4949    425     93   -554       C  
ATOM    558  O   PRO A 118      35.914   6.106 126.187  1.00 34.72           O  
ANISOU  558  O   PRO A 118     4042   4370   4780    582    213   -620       O  
ATOM    559  CB  PRO A 118      37.256   3.498 126.087  1.00 37.95           C  
ANISOU  559  CB  PRO A 118     4390   4803   5224    711     92   -472       C  
ATOM    560  CG  PRO A 118      36.827   2.250 126.768  1.00 39.26           C  
ANISOU  560  CG  PRO A 118     4731   4823   5360    723     53   -413       C  
ATOM    561  CD  PRO A 118      35.858   2.696 127.830  1.00 38.02           C  
ANISOU  561  CD  PRO A 118     4694   4674   5078    682    -68   -361       C  
ATOM    562  N   CYS A 119      37.783   6.895 127.168  1.00 37.42           N  
ANISOU  562  N   CYS A 119     3859   4911   5446    365    108   -555       N  
ATOM    563  CA  CYS A 119      37.424   8.309 127.058  1.00 36.86           C  
ANISOU  563  CA  CYS A 119     3917   4828   5259    273    206   -700       C  
ATOM    564  C   CYS A 119      37.173   8.796 125.639  1.00 34.70           C  
ANISOU  564  C   CYS A 119     3585   4434   5161     55    400   -732       C  
ATOM    565  O   CYS A 119      36.517   9.834 125.468  1.00 31.74           O  
ANISOU  565  O   CYS A 119     3270   4194   4594    -99    781  -1071       O  
ATOM    566  CB  CYS A 119      38.478   9.201 127.732  1.00 41.40           C  
ANISOU  566  CB  CYS A 119     4276   5391   6061     80    -20  -1009       C  
ATOM    567  SG  CYS A 119      40.169   9.125 127.094  1.00 48.52           S  
ANISOU  567  SG  CYS A 119     4372   7052   7009    263     56   -884       S  
ATOM    568  N   ASN A 120      37.703   8.073 124.642  1.00 33.58           N  
ANISOU  568  N   ASN A 120     3355   4237   5165    116    536   -530       N  
ATOM    569  CA  ASN A 120      37.444   8.360 123.218  1.00 33.12           C  
ANISOU  569  CA  ASN A 120     3374   4164   5045    -20    814   -504       C  
ATOM    570  C   ASN A 120      36.201   7.698 122.603  1.00 30.70           C  
ANISOU  570  C   ASN A 120     3564   3631   4468     -1    879   -485       C  
ATOM    571  O   ASN A 120      36.025   7.778 121.393  1.00 31.54           O  
ANISOU  571  O   ASN A 120     3889   3649   4444     50   1235   -140       O  
ATOM    572  CB  ASN A 120      38.682   8.026 122.370  1.00 35.76           C  
ANISOU  572  CB  ASN A 120     3609   4581   5394    121    995   -630       C  
ATOM    573  CG  ASN A 120      38.969   6.539 122.300  1.00 37.52           C  
ANISOU  573  CG  ASN A 120     4033   4654   5568    263    935   -630       C  
ATOM    574  OD1 ASN A 120      38.462   5.762 123.104  1.00 37.38           O  
ANISOU  574  OD1 ASN A 120     4237   4692   5274    326    900   -678       O  
ATOM    575  ND2 ASN A 120      39.806   6.137 121.344  1.00 39.33           N  
ANISOU  575  ND2 ASN A 120     4134   5037   5771    339   1074   -621       N  
ATOM    576  N   LYS A 121      35.345   7.071 123.423  1.00 28.92           N  
ANISOU  576  N   LYS A 121     3344   3489   4154     80    696   -523       N  
ATOM    577  CA  LYS A 121      34.150   6.345 122.951  1.00 27.69           C  
ANISOU  577  CA  LYS A 121     3346   3448   3725    108    637   -377       C  
ATOM    578  C   LYS A 121      32.842   6.868 123.553  1.00 25.84           C  
ANISOU  578  C   LYS A 121     3185   3055   3576    -36    530   -339       C  
ATOM    579  O   LYS A 121      31.887   6.099 123.727  1.00 24.22           O  
ANISOU  579  O   LYS A 121     3081   2962   3159    121    732   -229       O  
ATOM    580  CB  LYS A 121      34.248   4.858 123.323  1.00 28.90           C  
ANISOU  580  CB  LYS A 121     3639   3448   3894    219    461   -432       C  
ATOM    581  CG  LYS A 121      35.467   4.132 122.803  1.00 31.32           C  
ANISOU  581  CG  LYS A 121     3783   3846   4270    333    634   -461       C  
ATOM    582  CD  LYS A 121      35.456   4.081 121.300  1.00 32.07           C  
ANISOU  582  CD  LYS A 121     3977   3940   4267    254    742   -438       C  
ATOM    583  CE  LYS A 121      36.667   3.335 120.808  1.00 35.29           C  
ANISOU  583  CE  LYS A 121     4187   4376   4845    417    925   -572       C  
ATOM    584  NZ  LYS A 121      36.462   3.005 119.386  1.00 37.77           N  
ANISOU  584  NZ  LYS A 121     4780   4750   4818    327   1130   -590       N  
ATOM    585  N   ILE A 122      32.793   8.161 123.850  1.00 24.61           N  
ANISOU  585  N   ILE A 122     2943   3021   3387    -86    508   -316       N  
ATOM    586  CA  ILE A 122      31.681   8.731 124.576  1.00 23.52           C  
ANISOU  586  CA  ILE A 122     2923   2833   3179   -144    474   -231       C  
ATOM    587  C   ILE A 122      30.698   9.377 123.609  1.00 22.48           C  
ANISOU  587  C   ILE A 122     2894   2618   3027   -255    615   -146       C  
ATOM    588  O   ILE A 122      31.090  10.154 122.734  1.00 22.48           O  
ANISOU  588  O   ILE A 122     2839   2697   3005   -304    798   -194       O  
ATOM    589  CB  ILE A 122      32.162   9.708 125.681  1.00 24.83           C  
ANISOU  589  CB  ILE A 122     2973   3010   3450   -144    386   -401       C  
ATOM    590  CG1 ILE A 122      32.750   8.874 126.828  1.00 26.11           C  
ANISOU  590  CG1 ILE A 122     3162   3242   3515     16    225   -439       C  
ATOM    591  CG2 ILE A 122      31.011  10.577 126.206  1.00 24.26           C  
ANISOU  591  CG2 ILE A 122     2989   2908   3320   -205    440   -358       C  
ATOM    592  CD1 ILE A 122      33.352   9.675 127.954  1.00 28.56           C  
ANISOU  592  CD1 ILE A 122     3278   3589   3984    -99     39   -612       C  
ATOM    593  N   LEU A 123      29.417   9.046 123.793  1.00 21.80           N  
ANISOU  593  N   LEU A 123     2825   2460   2998   -190    494   -127       N  
ATOM    594  CA  LEU A 123      28.340   9.674 123.050  1.00 20.86           C  
ANISOU  594  CA  LEU A 123     2760   2501   2664   -269    571   -121       C  
ATOM    595  C   LEU A 123      27.447  10.463 124.003  1.00 19.97           C  
ANISOU  595  C   LEU A 123     2627   2260   2699   -272    456   -122       C  
ATOM    596  O   LEU A 123      26.778   9.890 124.891  1.00 18.82           O  
ANISOU  596  O   LEU A 123     2419   2258   2471   -190    375   -216       O  
ATOM    597  CB  LEU A 123      27.526   8.631 122.292  1.00 21.19           C  
ANISOU  597  CB  LEU A 123     2884   2461   2704   -275    507    -98       C  
ATOM    598  CG  LEU A 123      26.353   9.228 121.504  1.00 22.13           C  
ANISOU  598  CG  LEU A 123     3078   2601   2726   -310    377      4       C  
ATOM    599  CD1 LEU A 123      26.820  10.229 120.449  1.00 22.75           C  
ANISOU  599  CD1 LEU A 123     3118   2657   2868   -299    530     44       C  
ATOM    600  CD2 LEU A 123      25.526   8.117 120.873  1.00 22.60           C  
ANISOU  600  CD2 LEU A 123     3303   2535   2748   -296    330    -86       C  
ATOM    601  N   LEU A 124      27.458  11.775 123.822  1.00 19.55           N  
ANISOU  601  N   LEU A 124     2518   2246   2664   -278    499    -84       N  
ATOM    602  CA  LEU A 124      26.505  12.672 124.480  1.00 19.88           C  
ANISOU  602  CA  LEU A 124     2522   2226   2805   -290    465   -180       C  
ATOM    603  C   LEU A 124      25.243  12.791 123.607  1.00 20.28           C  
ANISOU  603  C   LEU A 124     2613   2316   2776   -308    400   -159       C  
ATOM    604  O   LEU A 124      25.267  12.472 122.429  1.00 20.71           O  
ANISOU  604  O   LEU A 124     2576   2565   2729   -343    332   -110       O  
ATOM    605  CB  LEU A 124      27.142  14.047 124.717  1.00 20.22           C  
ANISOU  605  CB  LEU A 124     2521   2178   2984   -269    503   -223       C  
ATOM    606  CG  LEU A 124      28.476  14.038 125.483  1.00 20.64           C  
ANISOU  606  CG  LEU A 124     2511   2249   3080   -302    490   -332       C  
ATOM    607  CD1 LEU A 124      29.051  15.442 125.612  1.00 21.73           C  
ANISOU  607  CD1 LEU A 124     2603   2290   3362   -345    460   -473       C  
ATOM    608  CD2 LEU A 124      28.344  13.385 126.852  1.00 20.84           C  
ANISOU  608  CD2 LEU A 124     2542   2410   2965   -249    379   -430       C  
ATOM    609  N   TRP A 125      24.136  13.222 124.200  1.00 20.49           N  
ANISOU  609  N   TRP A 125     2574   2305   2907   -308    355   -200       N  
ATOM    610  CA  TRP A 125      22.899  13.422 123.443  1.00 21.11           C  
ANISOU  610  CA  TRP A 125     2686   2352   2983   -201    300    -89       C  
ATOM    611  C   TRP A 125      22.024  14.454 124.123  1.00 21.91           C  
ANISOU  611  C   TRP A 125     2649   2492   3183   -173    385   -138       C  
ATOM    612  O   TRP A 125      22.149  14.696 125.325  1.00 20.96           O  
ANISOU  612  O   TRP A 125     2394   2420   3146   -187    401   -141       O  
ATOM    613  CB  TRP A 125      22.146  12.087 123.232  1.00 20.86           C  
ANISOU  613  CB  TRP A 125     2609   2444   2872   -253    258    -70       C  
ATOM    614  CG  TRP A 125      21.754  11.444 124.494  1.00 20.71           C  
ANISOU  614  CG  TRP A 125     2570   2430   2865   -295    358   -148       C  
ATOM    615  CD1 TRP A 125      22.475  10.532 125.202  1.00 20.40           C  
ANISOU  615  CD1 TRP A 125     2570   2389   2789   -255    449   -172       C  
ATOM    616  CD2 TRP A 125      20.572  11.707 125.251  1.00 21.52           C  
ANISOU  616  CD2 TRP A 125     2532   2569   3075   -267    390   -190       C  
ATOM    617  NE1 TRP A 125      21.803  10.189 126.342  1.00 21.67           N  
ANISOU  617  NE1 TRP A 125     2705   2645   2881   -261    523   -101       N  
ATOM    618  CE2 TRP A 125      20.630  10.903 126.404  1.00 22.00           C  
ANISOU  618  CE2 TRP A 125     2605   2707   3045   -303    496   -174       C  
ATOM    619  CE3 TRP A 125      19.471  12.541 125.064  1.00 22.69           C  
ANISOU  619  CE3 TRP A 125     2612   2742   3264   -158    342   -211       C  
ATOM    620  CZ2 TRP A 125      19.624  10.913 127.378  1.00 23.50           C  
ANISOU  620  CZ2 TRP A 125     2658   2931   3338   -298    666   -117       C  
ATOM    621  CZ3 TRP A 125      18.454  12.546 126.020  1.00 24.59           C  
ANISOU  621  CZ3 TRP A 125     2623   3087   3631   -152    506   -170       C  
ATOM    622  CH2 TRP A 125      18.541  11.736 127.168  1.00 24.82           C  
ANISOU  622  CH2 TRP A 125     2701   3135   3593   -187    657   -172       C  
ATOM    623  N   SER A 126      21.154  15.073 123.338  1.00 23.72           N  
ANISOU  623  N   SER A 126     2873   2677   3462    -71    263    -10       N  
ATOM    624  CA  SER A 126      20.236  16.081 123.843  1.00 25.78           C  
ANISOU  624  CA  SER A 126     3122   2791   3880     74    317   -127       C  
ATOM    625  C   SER A 126      18.916  15.931 123.110  1.00 28.16           C  
ANISOU  625  C   SER A 126     3271   3162   4267    140     86    -88       C  
ATOM    626  O   SER A 126      18.885  16.023 121.879  1.00 29.20           O  
ANISOU  626  O   SER A 126     3375   3437   4280    152    365     39       O  
ATOM    627  CB  SER A 126      20.827  17.472 123.629  1.00 26.84           C  
ANISOU  627  CB  SER A 126     3269   2774   4152     67    290   -118       C  
ATOM    628  OG  SER A 126      19.937  18.484 124.055  1.00 29.15           O  
ANISOU  628  OG  SER A 126     3513   2705   4857     71    315   -360       O  
ATOM    629  N   ARG A 127      17.842  15.666 123.865  1.00 30.18           N  
ANISOU  629  N   ARG A 127     3373   3582   4510    165    226    -87       N  
ATOM    630  CA  ARG A 127      16.482  15.507 123.331  1.00 32.31           C  
ANISOU  630  CA  ARG A 127     3367   3950   4960    174    134   -244       C  
ATOM    631  C   ARG A 127      16.327  14.427 122.250  1.00 32.06           C  
ANISOU  631  C   ARG A 127     3403   3838   4938     49     15   -146       C  
ATOM    632  O   ARG A 127      15.455  14.543 121.399  1.00 34.60           O  
ANISOU  632  O   ARG A 127     3685   4263   5196   -126   -241   -309       O  
ATOM    633  CB  ARG A 127      15.962  16.837 122.755  1.00 35.20           C  
ANISOU  633  CB  ARG A 127     3813   4107   5453    392      3   -114       C  
ATOM    634  CG  ARG A 127      16.273  18.100 123.547  1.00 37.74           C  
ANISOU  634  CG  ARG A 127     4178   4316   5842    295      0   -342       C  
ATOM    635  CD  ARG A 127      15.498  18.210 124.841  1.00 40.57           C  
ANISOU  635  CD  ARG A 127     4286   4857   6272    435    316   -480       C  
ATOM    636  NE  ARG A 127      15.805  19.479 125.526  1.00 44.00           N  
ANISOU  636  NE  ARG A 127     4834   4801   7082    514    367   -652       N  
ATOM    637  CZ  ARG A 127      15.200  19.931 126.629  1.00 46.44           C  
ANISOU  637  CZ  ARG A 127     5132   5324   7188    643    465   -767       C  
ATOM    638  NH1 ARG A 127      14.220  19.230 127.213  1.00 47.81           N  
ANISOU  638  NH1 ARG A 127     5082   5772   7310    552    488   -703       N  
ATOM    639  NH2 ARG A 127      15.569  21.105 127.152  1.00 48.51           N  
ANISOU  639  NH2 ARG A 127     5454   5401   7573    462    353   -818       N  
ATOM    640  N   ILE A 128      17.157  13.392 122.271  1.00 29.81           N  
ANISOU  640  N   ILE A 128     3279   3655   4389   -108     -2    -72       N  
ATOM    641  CA  ILE A 128      17.082  12.308 121.278  1.00 30.60           C  
ANISOU  641  CA  ILE A 128     3416   3730   4478    -84   -108   -121       C  
ATOM    642  C   ILE A 128      17.565  10.974 121.891  1.00 29.46           C  
ANISOU  642  C   ILE A 128     3255   3639   4300   -129     -6   -172       C  
ATOM    643  O   ILE A 128      18.365  10.238 121.325  1.00 26.44           O  
ANISOU  643  O   ILE A 128     3148   3147   3750   -242   -150     42       O  
ATOM    644  CB  ILE A 128      17.818  12.700 119.971  1.00 30.56           C  
ANISOU  644  CB  ILE A 128     3679   3687   4244     36   -243    -11       C  
ATOM    645  CG1 ILE A 128      17.570  11.659 118.874  1.00 32.11           C  
ANISOU  645  CG1 ILE A 128     3921   3981   4297    -46   -467    -68       C  
ATOM    646  CG2 ILE A 128      19.306  12.937 120.221  1.00 28.93           C  
ANISOU  646  CG2 ILE A 128     3601   3398   3993    -53     96    -15       C  
ATOM    647  CD1 ILE A 128      17.504  12.248 117.486  1.00 33.84           C  
ANISOU  647  CD1 ILE A 128     4299   4205   4353     47   -595     46       C  
ATOM    648  N   LYS A 129      16.996  10.672 123.052  1.00 31.36           N  
ANISOU  648  N   LYS A 129     3470   3923   4521   -161    198   -120       N  
ATOM    649  CA  LYS A 129      17.399   9.537 123.885  1.00 31.21           C  
ANISOU  649  CA  LYS A 129     3505   3818   4534   -237    319   -140       C  
ATOM    650  C   LYS A 129      17.245   8.207 123.163  1.00 31.16           C  
ANISOU  650  C   LYS A 129     3538   3952   4348   -423    271   -241       C  
ATOM    651  O   LYS A 129      18.184   7.405 123.104  1.00 28.54           O  
ANISOU  651  O   LYS A 129     4025   3321   3495   -414    621     28       O  
ATOM    652  CB  LYS A 129      16.559   9.518 125.164  1.00 32.83           C  
ANISOU  652  CB  LYS A 129     3579   4141   4753   -280    511   -257       C  
ATOM    653  CG  LYS A 129      16.989   8.487 126.184  1.00 33.10           C  
ANISOU  653  CG  LYS A 129     3661   4149   4768   -413    653   -112       C  
ATOM    654  CD  LYS A 129      16.026   8.527 127.343  1.00 34.98           C  
ANISOU  654  CD  LYS A 129     3750   4497   5041   -504    833   -189       C  
ATOM    655  CE  LYS A 129      16.577   7.812 128.544  1.00 35.01           C  
ANISOU  655  CE  LYS A 129     3844   4534   4921   -550    917   -122       C  
ATOM    656  NZ  LYS A 129      15.642   8.056 129.667  1.00 37.88           N  
ANISOU  656  NZ  LYS A 129     4053   5056   5282   -630   1175   -191       N  
ATOM    657  N   ASP A 130      16.029   7.999 122.680  1.00 33.79           N  
ANISOU  657  N   ASP A 130     3508   4361   4969   -502    213   -338       N  
ATOM    658  CA  ASP A 130      15.631   6.907 121.787  1.00 36.45           C  
ANISOU  658  CA  ASP A 130     4054   4535   5257   -472     35   -487       C  
ATOM    659  C   ASP A 130      16.745   6.449 120.835  1.00 32.47           C  
ANISOU  659  C   ASP A 130     3634   3928   4773   -624   -261   -250       C  
ATOM    660  O   ASP A 130      17.274   5.353 120.965  1.00 31.31           O  
ANISOU  660  O   ASP A 130     3495   3780   4619   -785   -264   -257       O  
ATOM    661  CB  ASP A 130      14.356   7.333 120.990  1.00 41.04           C  
ANISOU  661  CB  ASP A 130     4221   5279   6092   -329   -289   -501       C  
ATOM    662  CG  ASP A 130      14.337   8.864 120.626  1.00 43.86           C  
ANISOU  662  CG  ASP A 130     4914   5448   6301   -153    -76   -210       C  
ATOM    663  OD1 ASP A 130      15.024   9.270 119.657  1.00 44.92           O  
ANISOU  663  OD1 ASP A 130     5100   6103   5863    101     62   -564       O  
ATOM    664  OD2 ASP A 130      13.646   9.665 121.320  1.00 47.91           O  
ANISOU  664  OD2 ASP A 130     5036   5900   7266     84    446    -85       O  
ATOM    665  N   LEU A 131      17.128   7.314 119.913  1.00 30.84           N  
ANISOU  665  N   LEU A 131     3411   3915   4389   -431   -407   -303       N  
ATOM    666  CA  LEU A 131      18.049   6.929 118.863  1.00 30.66           C  
ANISOU  666  CA  LEU A 131     3729   3778   4141   -478   -406   -345       C  
ATOM    667  C   LEU A 131      19.488   6.794 119.396  1.00 27.91           C  
ANISOU  667  C   LEU A 131     3679   3299   3624   -409   -189   -333       C  
ATOM    668  O   LEU A 131      20.271   5.972 118.905  1.00 26.72           O  
ANISOU  668  O   LEU A 131     3678   3047   3425   -440   -369   -347       O  
ATOM    669  CB  LEU A 131      17.979   7.945 117.723  1.00 32.04           C  
ANISOU  669  CB  LEU A 131     4071   3948   4152   -324   -543   -291       C  
ATOM    670  CG  LEU A 131      18.680   7.515 116.437  1.00 33.56           C  
ANISOU  670  CG  LEU A 131     4572   4153   4024   -260   -594   -351       C  
ATOM    671  CD1 LEU A 131      17.981   6.308 115.822  1.00 36.02           C  
ANISOU  671  CD1 LEU A 131     4834   4472   4378   -459   -792   -502       C  
ATOM    672  CD2 LEU A 131      18.705   8.654 115.447  1.00 34.98           C  
ANISOU  672  CD2 LEU A 131     4847   4344   4097   -107   -695   -230       C  
ATOM    673  N   ALA A 132      19.838   7.604 120.391  1.00 25.88           N  
ANISOU  673  N   ALA A 132     3327   3185   3319   -434    -11   -193       N  
ATOM    674  CA  ALA A 132      21.165   7.527 120.993  1.00 24.89           C  
ANISOU  674  CA  ALA A 132     3332   2917   3208   -327     71   -146       C  
ATOM    675  C   ALA A 132      21.421   6.127 121.560  1.00 24.21           C  
ANISOU  675  C   ALA A 132     3220   2756   3221   -421    185   -233       C  
ATOM    676  O   ALA A 132      22.464   5.550 121.316  1.00 21.98           O  
ANISOU  676  O   ALA A 132     3183   2253   2915   -385   -153    -97       O  
ATOM    677  CB  ALA A 132      21.335   8.588 122.080  1.00 24.49           C  
ANISOU  677  CB  ALA A 132     3159   2888   3255   -358    192   -184       C  
ATOM    678  N   HIS A 133      20.433   5.588 122.267  1.00 25.12           N  
ANISOU  678  N   HIS A 133     3344   2850   3348   -555    216   -222       N  
ATOM    679  CA  HIS A 133      20.530   4.262 122.874  1.00 25.86           C  
ANISOU  679  CA  HIS A 133     3418   2860   3545   -659    264   -148       C  
ATOM    680  C   HIS A 133      20.395   3.127 121.870  1.00 26.83           C  
ANISOU  680  C   HIS A 133     3575   2929   3690   -801    200   -223       C  
ATOM    681  O   HIS A 133      20.993   2.062 122.065  1.00 26.80           O  
ANISOU  681  O   HIS A 133     3569   2754   3856   -883    273   -407       O  
ATOM    682  CB  HIS A 133      19.511   4.102 124.001  1.00 26.81           C  
ANISOU  682  CB  HIS A 133     3369   3045   3772   -694    387    -74       C  
ATOM    683  CG  HIS A 133      19.810   4.948 125.198  1.00 26.87           C  
ANISOU  683  CG  HIS A 133     3350   3162   3696   -736    543    -72       C  
ATOM    684  ND1 HIS A 133      18.905   5.141 126.222  1.00 28.39           N  
ANISOU  684  ND1 HIS A 133     3341   3455   3989   -667    668   -224       N  
ATOM    685  CD2 HIS A 133      20.920   5.645 125.541  1.00 25.61           C  
ANISOU  685  CD2 HIS A 133     3214   3134   3382   -623    619    -66       C  
ATOM    686  CE1 HIS A 133      19.448   5.920 127.140  1.00 27.49           C  
ANISOU  686  CE1 HIS A 133     3313   3344   3785   -610    694    -95       C  
ATOM    687  NE2 HIS A 133      20.668   6.243 126.746  1.00 25.90           N  
ANISOU  687  NE2 HIS A 133     3290   3141   3407   -620    634    -96       N  
ATOM    688  N   GLN A 134      19.622   3.339 120.809  1.00 27.65           N  
ANISOU  688  N   GLN A 134     3529   3034   3942   -821     21   -278       N  
ATOM    689  CA  GLN A 134      19.620   2.391 119.697  1.00 30.18           C  
ANISOU  689  CA  GLN A 134     4025   3352   4087   -753    -73   -481       C  
ATOM    690  C   GLN A 134      20.989   2.309 119.046  1.00 28.45           C  
ANISOU  690  C   GLN A 134     4075   3092   3641   -646   -127   -438       C  
ATOM    691  O   GLN A 134      21.422   1.229 118.649  1.00 29.97           O  
ANISOU  691  O   GLN A 134     4431   3244   3712   -672     -2   -699       O  
ATOM    692  CB  GLN A 134      18.599   2.774 118.645  1.00 32.97           C  
ANISOU  692  CB  GLN A 134     4342   3727   4457   -671   -407   -513       C  
ATOM    693  CG  GLN A 134      17.175   2.480 119.047  1.00 35.94           C  
ANISOU  693  CG  GLN A 134     4407   4126   5120   -880   -381   -619       C  
ATOM    694  CD  GLN A 134      16.223   2.918 117.966  1.00 40.09           C  
ANISOU  694  CD  GLN A 134     4836   4782   5612   -730   -905   -787       C  
ATOM    695  OE1 GLN A 134      16.247   2.369 116.865  1.00 46.51           O  
ANISOU  695  OE1 GLN A 134     6149   5732   5789   -345  -1189  -1141       O  
ATOM    696  NE2 GLN A 134      15.405   3.928 118.250  1.00 40.96           N  
ANISOU  696  NE2 GLN A 134     4559   5160   5842   -673   -869   -889       N  
ATOM    697  N   PHE A 135      21.666   3.446 118.940  1.00 26.12           N  
ANISOU  697  N   PHE A 135     3826   2969   3129   -479   -119   -380       N  
ATOM    698  CA  PHE A 135      23.004   3.473 118.367  1.00 26.15           C  
ANISOU  698  CA  PHE A 135     3906   2911   3117   -364    -41   -391       C  
ATOM    699  C   PHE A 135      23.984   2.658 119.215  1.00 25.30           C  
ANISOU  699  C   PHE A 135     3858   2644   3109   -353    138   -338       C  
ATOM    700  O   PHE A 135      24.682   1.801 118.676  1.00 25.06           O  
ANISOU  700  O   PHE A 135     3862   2579   3078   -335     80   -343       O  
ATOM    701  CB  PHE A 135      23.510   4.906 118.179  1.00 25.65           C  
ANISOU  701  CB  PHE A 135     3912   2887   2946   -285     72   -241       C  
ATOM    702  CG  PHE A 135      24.944   4.986 117.741  1.00 25.86           C  
ANISOU  702  CG  PHE A 135     3983   2906   2934   -178    153   -183       C  
ATOM    703  CD1 PHE A 135      25.295   4.725 116.429  1.00 27.70           C  
ANISOU  703  CD1 PHE A 135     4356   3149   3019   -164    221   -333       C  
ATOM    704  CD2 PHE A 135      25.940   5.318 118.643  1.00 25.69           C  
ANISOU  704  CD2 PHE A 135     3788   2977   2995   -204    255   -116       C  
ATOM    705  CE1 PHE A 135      26.613   4.791 116.016  1.00 28.36           C  
ANISOU  705  CE1 PHE A 135     4413   3287   3075    -54    302   -340       C  
ATOM    706  CE2 PHE A 135      27.259   5.380 118.240  1.00 26.23           C  
ANISOU  706  CE2 PHE A 135     3931   3117   2918   -160    487    -13       C  
ATOM    707  CZ  PHE A 135      27.596   5.112 116.928  1.00 27.47           C  
ANISOU  707  CZ  PHE A 135     4268   3179   2991   -111    437   -354       C  
ATOM    708  N   THR A 136      24.020   2.917 120.523  1.00 24.19           N  
ANISOU  708  N   THR A 136     3655   2475   3058   -391    259   -195       N  
ATOM    709  CA  THR A 136      24.949   2.213 121.418  1.00 24.61           C  
ANISOU  709  CA  THR A 136     3735   2572   3043   -410    256   -172       C  
ATOM    710  C   THR A 136      24.539   0.763 121.680  1.00 26.11           C  
ANISOU  710  C   THR A 136     4053   2518   3348   -464    199   -280       C  
ATOM    711  O   THR A 136      25.393  -0.054 122.026  1.00 25.80           O  
ANISOU  711  O   THR A 136     4314   2175   3312   -498    112   -417       O  
ATOM    712  CB  THR A 136      25.134   2.933 122.758  1.00 23.93           C  
ANISOU  712  CB  THR A 136     3603   2481   3009   -391    336   -162       C  
ATOM    713  OG1 THR A 136      23.875   3.041 123.425  1.00 24.59           O  
ANISOU  713  OG1 THR A 136     3576   2421   3343   -771    413    -83       O  
ATOM    714  CG2 THR A 136      25.694   4.302 122.530  1.00 23.24           C  
ANISOU  714  CG2 THR A 136     3452   2555   2821   -371    453   -150       C  
ATOM    715  N   GLN A 137      23.254   0.450 121.509  1.00 27.08           N  
ANISOU  715  N   GLN A 137     4041   2672   3575   -546    292   -260       N  
ATOM    716  CA  GLN A 137      22.795  -0.944 121.491  1.00 29.89           C  
ANISOU  716  CA  GLN A 137     4545   2755   4054   -667    171   -326       C  
ATOM    717  C   GLN A 137      23.520  -1.760 120.396  1.00 31.08           C  
ANISOU  717  C   GLN A 137     4839   2835   4132   -573     84   -482       C  
ATOM    718  O   GLN A 137      23.768  -2.948 120.595  1.00 31.67           O  
ANISOU  718  O   GLN A 137     5081   2797   4156   -500    269   -537       O  
ATOM    719  CB  GLN A 137      21.267  -1.002 121.340  1.00 31.64           C  
ANISOU  719  CB  GLN A 137     4569   3014   4439   -733     92   -342       C  
ATOM    720  CG  GLN A 137      20.637  -2.374 121.148  1.00 35.29           C  
ANISOU  720  CG  GLN A 137     5051   3251   5106   -998    160   -394       C  
ATOM    721  CD  GLN A 137      20.705  -3.285 122.370  1.00 37.21           C  
ANISOU  721  CD  GLN A 137     5481   3226   5430   -853    315   -207       C  
ATOM    722  OE1 GLN A 137      20.896  -4.492 122.236  1.00 38.96           O  
ANISOU  722  OE1 GLN A 137     5894   3147   5761  -1042    519   -332       O  
ATOM    723  NE2 GLN A 137      20.515  -2.717 123.562  1.00 37.63           N  
ANISOU  723  NE2 GLN A 137     5370   3590   5338   -791    380   -143       N  
ATOM    724  N   VAL A 138      23.861  -1.118 119.268  1.00 30.95           N  
ANISOU  724  N   VAL A 138     4749   3028   3980   -638     47   -565       N  
ATOM    725  CA  VAL A 138      24.571  -1.767 118.152  1.00 32.52           C  
ANISOU  725  CA  VAL A 138     5086   3154   4114   -445     67   -687       C  
ATOM    726  C   VAL A 138      26.086  -1.560 118.235  1.00 31.63           C  
ANISOU  726  C   VAL A 138     5027   3006   3985   -189     99   -648       C  
ATOM    727  O   VAL A 138      26.858  -2.512 118.098  1.00 33.01           O  
ANISOU  727  O   VAL A 138     5318   3048   4173    -79    322   -750       O  
ATOM    728  CB  VAL A 138      24.081  -1.223 116.782  1.00 33.64           C  
ANISOU  728  CB  VAL A 138     5286   3420   4075   -375    -97   -852       C  
ATOM    729  CG1 VAL A 138      24.872  -1.848 115.631  1.00 35.64           C  
ANISOU  729  CG1 VAL A 138     5691   3665   4183   -202     -9   -937       C  
ATOM    730  CG2 VAL A 138      22.591  -1.503 116.589  1.00 34.82           C  
ANISOU  730  CG2 VAL A 138     5346   3518   4364   -501   -188   -885       C  
ATOM    731  N   GLN A 139      26.486  -0.304 118.402  1.00 31.90           N  
ANISOU  731  N   GLN A 139     4865   3520   3735    200    467   -452       N  
ATOM    732  CA  GLN A 139      27.878   0.090 118.505  1.00 31.98           C  
ANISOU  732  CA  GLN A 139     4851   3592   3708    203    626   -446       C  
ATOM    733  C   GLN A 139      28.292  -0.035 119.967  1.00 30.33           C  
ANISOU  733  C   GLN A 139     4574   3251   3699    169    697   -399       C  
ATOM    734  O   GLN A 139      28.360   0.966 120.705  1.00 28.76           O  
ANISOU  734  O   GLN A 139     4219   3189   3518    213    832   -350       O  
ATOM    735  CB  GLN A 139      28.022   1.535 118.010  1.00 33.30           C  
ANISOU  735  CB  GLN A 139     5022   3749   3880    173    669   -243       C  
ATOM    736  CG  GLN A 139      29.388   2.188 118.180  1.00 34.01           C  
ANISOU  736  CG  GLN A 139     5002   3947   3973     96    853   -283       C  
ATOM    737  CD  GLN A 139      30.208   2.225 116.921  1.00 36.21           C  
ANISOU  737  CD  GLN A 139     5328   4376   4054    228   1035   -288       C  
ATOM    738  OE1 GLN A 139      29.745   2.675 115.873  1.00 37.00           O  
ANISOU  738  OE1 GLN A 139     5556   4322   4180    409   1083   -117       O  
ATOM    739  NE2 GLN A 139      31.457   1.780 117.024  1.00 37.64           N  
ANISOU  739  NE2 GLN A 139     5313   4706   4280    236   1163   -250       N  
ATOM    740  N   ARG A 140      28.595  -1.265 120.373  1.00 29.78           N  
ANISOU  740  N   ARG A 140     4477   3216   3622    237    654   -478       N  
ATOM    741  CA  ARG A 140      28.735  -1.585 121.794  1.00 28.64           C  
ANISOU  741  CA  ARG A 140     4273   2974   3632    190    604   -477       C  
ATOM    742  C   ARG A 140      30.068  -1.214 122.439  1.00 28.38           C  
ANISOU  742  C   ARG A 140     4144   3009   3629    288    676   -461       C  
ATOM    743  O   ARG A 140      30.204  -1.344 123.654  1.00 28.82           O  
ANISOU  743  O   ARG A 140     4295   3014   3640    264    569   -410       O  
ATOM    744  CB  ARG A 140      28.400  -3.058 122.054  1.00 28.52           C  
ANISOU  744  CB  ARG A 140     4371   2897   3568    257    560   -548       C  
ATOM    745  CG  ARG A 140      26.965  -3.356 121.692  1.00 28.11           C  
ANISOU  745  CG  ARG A 140     4467   2728   3482    115    530   -622       C  
ATOM    746  CD  ARG A 140      26.516  -4.743 122.071  1.00 28.33           C  
ANISOU  746  CD  ARG A 140     4651   2655   3456    119    546   -700       C  
ATOM    747  NE  ARG A 140      25.197  -4.995 121.503  1.00 28.49           N  
ANISOU  747  NE  ARG A 140     4721   2635   3468    -53    559   -792       N  
ATOM    748  CZ  ARG A 140      24.544  -6.152 121.544  1.00 29.48           C  
ANISOU  748  CZ  ARG A 140     4974   2646   3579   -145    554   -894       C  
ATOM    749  NH1 ARG A 140      25.073  -7.216 122.138  1.00 30.05           N  
ANISOU  749  NH1 ARG A 140     5257   2534   3623   -119    632   -889       N  
ATOM    750  NH2 ARG A 140      23.344  -6.241 120.979  1.00 30.15           N  
ANISOU  750  NH2 ARG A 140     5096   2744   3612   -331    448  -1058       N  
ATOM    751  N   ASP A 141      31.028  -0.719 121.663  1.00 28.88           N  
ANISOU  751  N   ASP A 141     4118   3196   3659    400    803   -478       N  
ATOM    752  CA  ASP A 141      32.224  -0.124 122.269  1.00 30.21           C  
ANISOU  752  CA  ASP A 141     4084   3531   3862    284    823   -478       C  
ATOM    753  C   ASP A 141      32.004   1.332 122.696  1.00 29.31           C  
ANISOU  753  C   ASP A 141     3829   3527   3778    140    908   -501       C  
ATOM    754  O   ASP A 141      32.897   1.940 123.278  1.00 29.72           O  
ANISOU  754  O   ASP A 141     3873   3500   3917    143   1064   -828       O  
ATOM    755  CB  ASP A 141      33.472  -0.266 121.372  1.00 32.44           C  
ANISOU  755  CB  ASP A 141     4246   4020   4056    315   1006   -575       C  
ATOM    756  CG  ASP A 141      33.332   0.434 120.045  1.00 34.51           C  
ANISOU  756  CG  ASP A 141     4600   4303   4207    215   1072   -377       C  
ATOM    757  OD1 ASP A 141      32.191   0.728 119.623  1.00 35.69           O  
ANISOU  757  OD1 ASP A 141     4474   4499   4585    115   1145   -326       O  
ATOM    758  OD2 ASP A 141      34.373   0.670 119.395  1.00 38.90           O  
ANISOU  758  OD2 ASP A 141     4472   5163   5144   -138   1129   -337       O  
ATOM    759  N   MET A 142      30.830   1.885 122.402  1.00 28.02           N  
ANISOU  759  N   MET A 142     3824   3267   3552      5    848   -426       N  
ATOM    760  CA  MET A 142      30.493   3.234 122.790  1.00 27.64           C  
ANISOU  760  CA  MET A 142     3731   3166   3602   -162    875   -375       C  
ATOM    761  C   MET A 142      29.503   3.288 123.938  1.00 25.23           C  
ANISOU  761  C   MET A 142     3386   2763   3435   -109    656   -318       C  
ATOM    762  O   MET A 142      28.738   2.346 124.162  1.00 23.89           O  
ANISOU  762  O   MET A 142     3290   2755   3032     -1    682   -264       O  
ATOM    763  CB  MET A 142      30.010   4.001 121.579  1.00 29.49           C  
ANISOU  763  CB  MET A 142     4142   3270   3792   -122    843   -246       C  
ATOM    764  CG  MET A 142      31.169   4.173 120.611  1.00 32.93           C  
ANISOU  764  CG  MET A 142     4431   3915   4165    -30   1196   -426       C  
ATOM    765  SD  MET A 142      30.927   5.439 119.404  1.00 37.03           S  
ANISOU  765  SD  MET A 142     5341   4079   4647   -241   1625   -153       S  
ATOM    766  CE  MET A 142      30.790   6.929 120.392  1.00 35.50           C  
ANISOU  766  CE  MET A 142     5037   3990   4458   -436   1329   -160       C  
ATOM    767  N   PHE A 143      29.591   4.382 124.687  1.00 23.93           N  
ANISOU  767  N   PHE A 143     3154   2646   3292   -196    729   -205       N  
ATOM    768  CA  PHE A 143      28.826   4.586 125.903  1.00 22.80           C  
ANISOU  768  CA  PHE A 143     3060   2364   3237   -252    634   -207       C  
ATOM    769  C   PHE A 143      28.193   5.967 125.912  1.00 21.90           C  
ANISOU  769  C   PHE A 143     2965   2315   3040   -319    639   -156       C  
ATOM    770  O   PHE A 143      28.879   7.000 125.739  1.00 22.44           O  
ANISOU  770  O   PHE A 143     3180   2329   3015   -386    577    -34       O  
ATOM    771  CB  PHE A 143      29.729   4.454 127.146  1.00 23.12           C  
ANISOU  771  CB  PHE A 143     2894   2573   3317   -285    623   -283       C  
ATOM    772  CG  PHE A 143      30.296   3.080 127.344  1.00 23.91           C  
ANISOU  772  CG  PHE A 143     2986   2687   3411   -113    559   -370       C  
ATOM    773  CD1 PHE A 143      29.788   2.236 128.324  1.00 23.92           C  
ANISOU  773  CD1 PHE A 143     3067   2611   3409    -48    495   -347       C  
ATOM    774  CD2 PHE A 143      31.334   2.621 126.549  1.00 26.00           C  
ANISOU  774  CD2 PHE A 143     3160   3054   3664     12    691   -420       C  
ATOM    775  CE1 PHE A 143      30.303   0.967 128.511  1.00 24.65           C  
ANISOU  775  CE1 PHE A 143     3132   2729   3504    129    469   -367       C  
ATOM    776  CE2 PHE A 143      31.848   1.337 126.723  1.00 26.97           C  
ANISOU  776  CE2 PHE A 143     3419   3147   3681    163    658   -404       C  
ATOM    777  CZ  PHE A 143      31.327   0.513 127.706  1.00 26.27           C  
ANISOU  777  CZ  PHE A 143     3320   3015   3643    217    592   -419       C  
ATOM    778  N   THR A 144      26.882   5.973 126.110  1.00 20.72           N  
ANISOU  778  N   THR A 144     2912   2039   2921   -278    509   -181       N  
ATOM    779  CA  THR A 144      26.197   7.143 126.657  1.00 19.90           C  
ANISOU  779  CA  THR A 144     2828   1898   2835   -337    491    -86       C  
ATOM    780  C   THR A 144      26.251   7.045 128.171  1.00 18.57           C  
ANISOU  780  C   THR A 144     2504   1728   2824   -350    446   -148       C  
ATOM    781  O   THR A 144      26.634   5.993 128.739  1.00 17.36           O  
ANISOU  781  O   THR A 144     2210   1599   2786   -362    512   -257       O  
ATOM    782  CB  THR A 144      24.712   7.204 126.236  1.00 19.56           C  
ANISOU  782  CB  THR A 144     2883   1814   2733   -260    419    -69       C  
ATOM    783  OG1 THR A 144      23.993   6.118 126.835  1.00 18.04           O  
ANISOU  783  OG1 THR A 144     2589   1779   2484   -255    233   -126       O  
ATOM    784  CG2 THR A 144      24.581   7.154 124.714  1.00 20.61           C  
ANISOU  784  CG2 THR A 144     3133   1970   2726   -169    432    -56       C  
ATOM    785  N   LEU A 145      25.823   8.121 128.822  1.00 18.29           N  
ANISOU  785  N   LEU A 145     2473   1642   2832   -358    434    -97       N  
ATOM    786  CA  LEU A 145      25.758   8.165 130.284  1.00 18.00           C  
ANISOU  786  CA  LEU A 145     2387   1612   2839   -402    417   -127       C  
ATOM    787  C   LEU A 145      24.933   7.016 130.880  1.00 17.50           C  
ANISOU  787  C   LEU A 145     2249   1596   2802   -363    342   -126       C  
ATOM    788  O   LEU A 145      25.309   6.444 131.915  1.00 16.49           O  
ANISOU  788  O   LEU A 145     2094   1420   2748   -407    356   -200       O  
ATOM    789  CB  LEU A 145      25.217   9.509 130.750  1.00 18.19           C  
ANISOU  789  CB  LEU A 145     2477   1591   2841   -433    427   -136       C  
ATOM    790  CG  LEU A 145      25.043   9.696 132.254  1.00 17.63           C  
ANISOU  790  CG  LEU A 145     2336   1529   2833   -451    365   -149       C  
ATOM    791  CD1 LEU A 145      26.383   9.543 132.954  1.00 18.06           C  
ANISOU  791  CD1 LEU A 145     2271   1648   2943   -489    386   -177       C  
ATOM    792  CD2 LEU A 145      24.476  11.097 132.474  1.00 18.07           C  
ANISOU  792  CD2 LEU A 145     2513   1476   2874   -441    413    -70       C  
ATOM    793  N   GLU A 146      23.860   6.634 130.185  1.00 17.94           N  
ANISOU  793  N   GLU A 146     2405   1614   2796   -342    233   -183       N  
ATOM    794  CA  GLU A 146      22.924   5.607 130.687  1.00 17.92           C  
ANISOU  794  CA  GLU A 146     2394   1635   2778   -329    231   -162       C  
ATOM    795  C   GLU A 146      23.442   4.194 130.398  1.00 18.29           C  
ANISOU  795  C   GLU A 146     2509   1617   2823   -371    241   -203       C  
ATOM    796  O   GLU A 146      22.848   3.215 130.843  1.00 18.15           O  
ANISOU  796  O   GLU A 146     2628   1654   2611   -481     55   -164       O  
ATOM    797  CB  GLU A 146      21.536   5.808 130.087  1.00 18.35           C  
ANISOU  797  CB  GLU A 146     2430   1767   2772   -330    190   -212       C  
ATOM    798  CG  GLU A 146      20.929   7.186 130.404  1.00 18.81           C  
ANISOU  798  CG  GLU A 146     2541   1792   2813   -261    168   -134       C  
ATOM    799  CD  GLU A 146      21.453   8.333 129.554  1.00 19.93           C  
ANISOU  799  CD  GLU A 146     2886   1815   2872   -271    259   -101       C  
ATOM    800  OE1 GLU A 146      22.045   8.103 128.468  1.00 20.01           O  
ANISOU  800  OE1 GLU A 146     3009   1795   2797   -426    283    -56       O  
ATOM    801  OE2 GLU A 146      21.257   9.479 129.975  1.00 21.35           O  
ANISOU  801  OE2 GLU A 146     3328   1902   2880   -272    304   -231       O  
ATOM    802  N   ASP A 147      24.550   4.107 129.651  1.00 19.03           N  
ANISOU  802  N   ASP A 147     2572   1756   2900   -292    304   -218       N  
ATOM    803  CA  ASP A 147      25.301   2.869 129.479  1.00 19.52           C  
ANISOU  803  CA  ASP A 147     2660   1807   2947   -216    294   -199       C  
ATOM    804  C   ASP A 147      26.384   2.640 130.538  1.00 19.46           C  
ANISOU  804  C   ASP A 147     2600   1830   2962   -195    311   -244       C  
ATOM    805  O   ASP A 147      26.987   1.564 130.546  1.00 20.92           O  
ANISOU  805  O   ASP A 147     2832   2089   3028     84    368   -224       O  
ATOM    806  CB  ASP A 147      25.921   2.797 128.085  1.00 20.28           C  
ANISOU  806  CB  ASP A 147     2799   1911   2994   -204    380   -221       C  
ATOM    807  CG  ASP A 147      24.874   2.720 126.984  1.00 21.07           C  
ANISOU  807  CG  ASP A 147     3014   2018   2973   -265    309   -250       C  
ATOM    808  OD1 ASP A 147      24.111   1.729 126.994  1.00 22.14           O  
ANISOU  808  OD1 ASP A 147     3251   2074   3084   -390    349   -285       O  
ATOM    809  OD2 ASP A 147      24.814   3.632 126.114  1.00 21.51           O  
ANISOU  809  OD2 ASP A 147     3211   2028   2933   -306    373   -236       O  
ATOM    810  N   THR A 148      26.608   3.607 131.426  1.00 18.46           N  
ANISOU  810  N   THR A 148     2399   1715   2900   -224    353   -169       N  
ATOM    811  CA  THR A 148      27.506   3.439 132.571  1.00 18.94           C  
ANISOU  811  CA  THR A 148     2349   1869   2977   -132    318   -238       C  
ATOM    812  C   THR A 148      26.673   2.840 133.690  1.00 18.73           C  
ANISOU  812  C   THR A 148     2375   1814   2926    -88    298   -238       C  
ATOM    813  O   THR A 148      25.443   2.900 133.639  1.00 17.93           O  
ANISOU  813  O   THR A 148     2371   1620   2819   -204    313   -175       O  
ATOM    814  CB  THR A 148      28.129   4.767 133.062  1.00 19.13           C  
ANISOU  814  CB  THR A 148     2224   1993   3050   -208    306   -273       C  
ATOM    815  OG1 THR A 148      27.120   5.608 133.647  1.00 18.60           O  
ANISOU  815  OG1 THR A 148     2343   1868   2856   -330    400   -305       O  
ATOM    816  CG2 THR A 148      28.824   5.515 131.910  1.00 19.72           C  
ANISOU  816  CG2 THR A 148     2261   2130   3101   -292    404   -329       C  
ATOM    817  N   LEU A 149      27.335   2.261 134.686  1.00 19.43           N  
ANISOU  817  N   LEU A 149     2440   1934   3006     92    258   -275       N  
ATOM    818  CA  LEU A 149      26.643   1.608 135.797  1.00 19.73           C  
ANISOU  818  CA  LEU A 149     2607   1849   3039     98    251   -228       C  
ATOM    819  C   LEU A 149      25.671   2.582 136.479  1.00 19.28           C  
ANISOU  819  C   LEU A 149     2454   1794   3075    -35    239   -271       C  
ATOM    820  O   LEU A 149      24.490   2.290 136.630  1.00 19.20           O  
ANISOU  820  O   LEU A 149     2521   1593   3179    -39    461   -112       O  
ATOM    821  CB  LEU A 149      27.644   1.093 136.828  1.00 20.85           C  
ANISOU  821  CB  LEU A 149     2758   2053   3110    297    208   -256       C  
ATOM    822  CG  LEU A 149      27.054   0.545 138.130  1.00 21.27           C  
ANISOU  822  CG  LEU A 149     2968   2017   3095    362    219   -211       C  
ATOM    823  CD1 LEU A 149      26.102  -0.611 137.875  1.00 21.76           C  
ANISOU  823  CD1 LEU A 149     3268   1838   3158    327    322   -163       C  
ATOM    824  CD2 LEU A 149      28.169   0.096 139.029  1.00 22.85           C  
ANISOU  824  CD2 LEU A 149     3139   2348   3194    621    166   -227       C  
ATOM    825  N   LEU A 150      26.174   3.748 136.848  1.00 19.30           N  
ANISOU  825  N   LEU A 150     2362   1832   3138    -86    201   -249       N  
ATOM    826  CA  LEU A 150      25.390   4.680 137.646  1.00 18.76           C  
ANISOU  826  CA  LEU A 150     2292   1765   3070   -118    162   -193       C  
ATOM    827  C   LEU A 150      24.231   5.204 136.825  1.00 18.00           C  
ANISOU  827  C   LEU A 150     2184   1650   3002   -258    203   -174       C  
ATOM    828  O   LEU A 150      23.124   5.259 137.319  1.00 17.90           O  
ANISOU  828  O   LEU A 150     2232   1568   3002   -343    306   -246       O  
ATOM    829  CB  LEU A 150      26.257   5.813 138.181  1.00 19.20           C  
ANISOU  829  CB  LEU A 150     2230   1932   3132   -143    127   -297       C  
ATOM    830  CG  LEU A 150      27.238   5.407 139.284  1.00 20.57           C  
ANISOU  830  CG  LEU A 150     2310   2214   3289     10     69   -268       C  
ATOM    831  CD1 LEU A 150      28.092   6.607 139.647  1.00 21.47           C  
ANISOU  831  CD1 LEU A 150     2261   2482   3412    -55     16   -451       C  
ATOM    832  CD2 LEU A 150      26.543   4.857 140.525  1.00 20.69           C  
ANISOU  832  CD2 LEU A 150     2393   2288   3179    144     91   -294       C  
ATOM    833  N   GLY A 151      24.490   5.538 135.557  1.00 18.45           N  
ANISOU  833  N   GLY A 151     2268   1755   2986   -300    164   -158       N  
ATOM    834  CA  GLY A 151      23.446   5.972 134.636  1.00 17.65           C  
ANISOU  834  CA  GLY A 151     2191   1602   2913   -344    197   -185       C  
ATOM    835  C   GLY A 151      22.434   4.882 134.374  1.00 17.56           C  
ANISOU  835  C   GLY A 151     2237   1560   2875   -342    176   -160       C  
ATOM    836  O   GLY A 151      21.245   5.162 134.298  1.00 17.18           O  
ANISOU  836  O   GLY A 151     2236   1586   2702   -341    139    -86       O  
ATOM    837  N   TYR A 152      22.896   3.636 134.237  1.00 18.07           N  
ANISOU  837  N   TYR A 152     2379   1579   2906   -320    171   -187       N  
ATOM    838  CA  TYR A 152      21.983   2.501 134.013  1.00 18.47           C  
ANISOU  838  CA  TYR A 152     2514   1571   2931   -363    203   -244       C  
ATOM    839  C   TYR A 152      21.048   2.264 135.198  1.00 18.57           C  
ANISOU  839  C   TYR A 152     2572   1521   2963   -356    269   -346       C  
ATOM    840  O   TYR A 152      19.858   1.998 135.006  1.00 18.84           O  
ANISOU  840  O   TYR A 152     2550   1652   2956   -242    317   -668       O  
ATOM    841  CB  TYR A 152      22.770   1.235 133.681  1.00 18.98           C  
ANISOU  841  CB  TYR A 152     2656   1604   2949   -313    282   -231       C  
ATOM    842  CG  TYR A 152      21.942   0.052 133.308  1.00 19.90           C  
ANISOU  842  CG  TYR A 152     2917   1585   3058   -376    353   -328       C  
ATOM    843  CD1 TYR A 152      21.468  -0.115 132.006  1.00 20.75           C  
ANISOU  843  CD1 TYR A 152     3045   1722   3114   -444    270   -348       C  
ATOM    844  CD2 TYR A 152      21.651  -0.942 134.246  1.00 20.92           C  
ANISOU  844  CD2 TYR A 152     3224   1583   3139   -387    423   -301       C  
ATOM    845  CE1 TYR A 152      20.704  -1.232 131.657  1.00 22.17           C  
ANISOU  845  CE1 TYR A 152     3345   1819   3258   -621    382   -462       C  
ATOM    846  CE2 TYR A 152      20.897  -2.059 133.904  1.00 22.56           C  
ANISOU  846  CE2 TYR A 152     3563   1685   3321   -596    475   -355       C  
ATOM    847  CZ  TYR A 152      20.423  -2.201 132.613  1.00 23.41           C  
ANISOU  847  CZ  TYR A 152     3740   1790   3362   -695    452   -466       C  
ATOM    848  OH  TYR A 152      19.659  -3.319 132.292  1.00 25.60           O  
ANISOU  848  OH  TYR A 152     4048   1919   3759   -898    615   -618       O  
ATOM    849  N   LEU A 153      21.583   2.363 136.410  1.00 18.56           N  
ANISOU  849  N   LEU A 153     2509   1543   3000   -287    228   -301       N  
ATOM    850  CA  LEU A 153      20.795   2.187 137.633  1.00 19.17           C  
ANISOU  850  CA  LEU A 153     2635   1583   3066   -389    272   -172       C  
ATOM    851  C   LEU A 153      19.650   3.183 137.770  1.00 18.84           C  
ANISOU  851  C   LEU A 153     2486   1602   3067   -480    312   -228       C  
ATOM    852  O   LEU A 153      18.575   2.805 138.236  1.00 20.30           O  
ANISOU  852  O   LEU A 153     2565   1795   3350   -706    319   -133       O  
ATOM    853  CB  LEU A 153      21.668   2.341 138.875  1.00 19.43           C  
ANISOU  853  CB  LEU A 153     2717   1612   3052   -290    244   -113       C  
ATOM    854  CG  LEU A 153      22.785   1.341 139.081  1.00 20.55           C  
ANISOU  854  CG  LEU A 153     2935   1709   3163   -122    273    -99       C  
ATOM    855  CD1 LEU A 153      23.499   1.675 140.375  1.00 21.08           C  
ANISOU  855  CD1 LEU A 153     3026   1828   3154    -12    261   -197       C  
ATOM    856  CD2 LEU A 153      22.291  -0.098 139.100  1.00 22.25           C  
ANISOU  856  CD2 LEU A 153     3420   1690   3341   -159    314    -92       C  
ATOM    857  N   ALA A 154      19.867   4.436 137.361  1.00 18.19           N  
ANISOU  857  N   ALA A 154     2312   1595   3004   -451    265   -198       N  
ATOM    858  CA  ALA A 154      18.915   5.508 137.657  1.00 17.79           C  
ANISOU  858  CA  ALA A 154     2206   1607   2945   -437    117   -165       C  
ATOM    859  C   ALA A 154      17.956   5.847 136.530  1.00 17.94           C  
ANISOU  859  C   ALA A 154     2131   1700   2982   -536     45   -293       C  
ATOM    860  O   ALA A 154      16.954   6.514 136.780  1.00 17.20           O  
ANISOU  860  O   ALA A 154     1997   1747   2789   -608   -105   -495       O  
ATOM    861  CB  ALA A 154      19.662   6.767 138.071  1.00 17.25           C  
ANISOU  861  CB  ALA A 154     2069   1629   2855   -393     78   -154       C  
ATOM    862  N   ASP A 155      18.269   5.419 135.307  1.00 18.61           N  
ANISOU  862  N   ASP A 155     2268   1743   3058   -549    121   -378       N  
ATOM    863  CA  ASP A 155      17.542   5.847 134.105  1.00 20.85           C  
ANISOU  863  CA  ASP A 155     2523   2220   3179   -419    -12   -309       C  
ATOM    864  C   ASP A 155      16.037   5.590 134.248  1.00 21.96           C  
ANISOU  864  C   ASP A 155     2579   2588   3176   -527     59   -457       C  
ATOM    865  O   ASP A 155      15.628   4.489 134.645  1.00 21.93           O  
ANISOU  865  O   ASP A 155     2692   2521   3116   -522    256   -573       O  
ATOM    866  CB  ASP A 155      18.089   5.102 132.875  1.00 22.37           C  
ANISOU  866  CB  ASP A 155     2758   2431   3310   -348     58   -392       C  
ATOM    867  CG  ASP A 155      17.645   5.710 131.544  1.00 24.43           C  
ANISOU  867  CG  ASP A 155     3072   2680   3529   -117    -23   -233       C  
ATOM    868  OD1 ASP A 155      17.455   6.930 131.411  1.00 23.78           O  
ANISOU  868  OD1 ASP A 155     2759   2788   3487     55     41    125       O  
ATOM    869  OD2 ASP A 155      17.526   4.936 130.584  1.00 31.44           O  
ANISOU  869  OD2 ASP A 155     4524   3613   3809    -53   -591   -599       O  
ATOM    870  N   ASP A 156      15.240   6.628 133.967  1.00 23.26           N  
ANISOU  870  N   ASP A 156     2771   2803   3262   -380    -67   -419       N  
ATOM    871  CA  ASP A 156      13.766   6.598 134.037  1.00 26.22           C  
ANISOU  871  CA  ASP A 156     2823   3460   3680   -286    -27   -504       C  
ATOM    872  C   ASP A 156      13.165   6.431 135.419  1.00 24.77           C  
ANISOU  872  C   ASP A 156     2588   3208   3616   -372    -91   -630       C  
ATOM    873  O   ASP A 156      11.973   6.210 135.508  1.00 27.58           O  
ANISOU  873  O   ASP A 156     2682   3781   4013   -682   -170   -566       O  
ATOM    874  CB  ASP A 156      13.149   5.501 133.128  1.00 29.97           C  
ANISOU  874  CB  ASP A 156     3283   3876   4229   -611   -172   -737       C  
ATOM    875  CG  ASP A 156      13.303   5.799 131.670  1.00 34.04           C  
ANISOU  875  CG  ASP A 156     4193   4468   4271   -396   -142   -675       C  
ATOM    876  OD1 ASP A 156      13.108   6.967 131.259  1.00 40.91           O  
ANISOU  876  OD1 ASP A 156     5095   5006   5441    172   -309    -51       O  
ATOM    877  OD2 ASP A 156      13.606   4.858 130.926  1.00 39.66           O  
ANISOU  877  OD2 ASP A 156     5379   4406   5282   -523    224  -1001       O  
ATOM    878  N   LEU A 157      13.948   6.530 136.484  1.00 22.72           N  
ANISOU  878  N   LEU A 157     2411   2768   3452   -485     54   -548       N  
ATOM    879  CA  LEU A 157      13.404   6.428 137.839  1.00 22.40           C  
ANISOU  879  CA  LEU A 157     2316   2748   3445   -565     33   -501       C  
ATOM    880  C   LEU A 157      13.303   7.806 138.473  1.00 21.54           C  
ANISOU  880  C   LEU A 157     2231   2737   3215   -421    -30   -436       C  
ATOM    881  O   LEU A 157      13.951   8.749 138.024  1.00 20.08           O  
ANISOU  881  O   LEU A 157     2077   2633   2917   -282   -142   -419       O  
ATOM    882  CB  LEU A 157      14.256   5.499 138.688  1.00 21.69           C  
ANISOU  882  CB  LEU A 157     2364   2521   3356   -711    103   -419       C  
ATOM    883  CG  LEU A 157      14.469   4.100 138.101  1.00 22.70           C  
ANISOU  883  CG  LEU A 157     2578   2557   3489   -772    174   -475       C  
ATOM    884  CD1 LEU A 157      15.412   3.315 138.993  1.00 22.49           C  
ANISOU  884  CD1 LEU A 157     2649   2358   3537   -753    258   -404       C  
ATOM    885  CD2 LEU A 157      13.140   3.341 137.919  1.00 24.28           C  
ANISOU  885  CD2 LEU A 157     2718   2843   3660   -981    241   -631       C  
ATOM    886  N   THR A 158      12.429   7.909 139.472  1.00 22.00           N  
ANISOU  886  N   THR A 158     2201   2812   3344   -423     25   -469       N  
ATOM    887  CA  THR A 158      12.329   9.063 140.356  1.00 21.63           C  
ANISOU  887  CA  THR A 158     2176   2810   3231   -261     40   -400       C  
ATOM    888  C   THR A 158      12.440   8.542 141.766  1.00 21.11           C  
ANISOU  888  C   THR A 158     2094   2670   3255   -312     43   -395       C  
ATOM    889  O   THR A 158      12.004   7.421 142.064  1.00 22.48           O  
ANISOU  889  O   THR A 158     2312   2658   3569   -444    220   -549       O  
ATOM    890  CB  THR A 158      10.970   9.785 140.232  1.00 23.67           C  
ANISOU  890  CB  THR A 158     2300   3282   3410    -48   -120   -488       C  
ATOM    891  OG1 THR A 158      10.711  10.073 138.867  1.00 26.10           O  
ANISOU  891  OG1 THR A 158     2981   3526   3407    154   -267   -724       O  
ATOM    892  CG2 THR A 158      10.969  11.103 140.966  1.00 23.31           C  
ANISOU  892  CG2 THR A 158     2315   3264   3276    117   -212   -411       C  
ATOM    893  N   TRP A 159      12.976   9.375 142.648  1.00 20.09           N  
ANISOU  893  N   TRP A 159     2038   2446   3146   -300     90   -270       N  
ATOM    894  CA  TRP A 159      13.111   9.026 144.051  1.00 19.94           C  
ANISOU  894  CA  TRP A 159     2048   2396   3131   -265    114   -285       C  
ATOM    895  C   TRP A 159      13.281  10.282 144.894  1.00 19.82           C  
ANISOU  895  C   TRP A 159     2031   2356   3143   -113     75   -265       C  
ATOM    896  O   TRP A 159      13.772  11.320 144.404  1.00 18.40           O  
ANISOU  896  O   TRP A 159     1937   2175   2876    122    125   -311       O  
ATOM    897  CB  TRP A 159      14.280   8.072 144.254  1.00 19.05           C  
ANISOU  897  CB  TRP A 159     2136   2065   3034   -343    116   -268       C  
ATOM    898  CG  TRP A 159      15.606   8.674 143.919  1.00 17.76           C  
ANISOU  898  CG  TRP A 159     2106   1734   2905   -239     89   -176       C  
ATOM    899  CD1 TRP A 159      16.444   9.334 144.783  1.00 17.31           C  
ANISOU  899  CD1 TRP A 159     2027   1694   2853   -179     63   -120       C  
ATOM    900  CD2 TRP A 159      16.247   8.699 142.649  1.00 17.52           C  
ANISOU  900  CD2 TRP A 159     2040   1722   2894   -254     48   -194       C  
ATOM    901  NE1 TRP A 159      17.559   9.755 144.128  1.00 16.60           N  
ANISOU  901  NE1 TRP A 159     2019   1471   2815   -209    -21   -120       N  
ATOM    902  CE2 TRP A 159      17.467   9.392 142.814  1.00 17.02           C  
ANISOU  902  CE2 TRP A 159     2024   1607   2833   -207     29   -177       C  
ATOM    903  CE3 TRP A 159      15.917   8.210 141.383  1.00 18.50           C  
ANISOU  903  CE3 TRP A 159     2057   2046   2925   -359     31   -236       C  
ATOM    904  CZ2 TRP A 159      18.354   9.597 141.769  1.00 17.22           C  
ANISOU  904  CZ2 TRP A 159     2052   1617   2871   -311     36   -169       C  
ATOM    905  CZ3 TRP A 159      16.803   8.408 140.341  1.00 18.42           C  
ANISOU  905  CZ3 TRP A 159     2073   2019   2906   -377     13   -179       C  
ATOM    906  CH2 TRP A 159      18.006   9.112 140.535  1.00 17.90           C  
ANISOU  906  CH2 TRP A 159     2048   1877   2876   -302     -8   -186       C  
ATOM    907  N   CYS A 160      12.841  10.178 146.145  1.00 20.91           N  
ANISOU  907  N   CYS A 160     2179   2565   3201   -151    153   -153       N  
ATOM    908  CA  CYS A 160      13.140  11.150 147.179  1.00 22.15           C  
ANISOU  908  CA  CYS A 160     2494   2655   3265    -11    103   -235       C  
ATOM    909  C   CYS A 160      12.794  10.573 148.549  1.00 22.14           C  
ANISOU  909  C   CYS A 160     2401   2651   3359      0    173   -166       C  
ATOM    910  O   CYS A 160      12.098   9.572 148.648  1.00 21.85           O  
ANISOU  910  O   CYS A 160     2453   2640   3209    -23    251   -188       O  
ATOM    911  CB  CYS A 160      12.378  12.471 146.969  1.00 24.00           C  
ANISOU  911  CB  CYS A 160     2737   2913   3466    176    -76   -137       C  
ATOM    912  SG  CYS A 160      10.591  12.335 147.121  1.00 27.16           S  
ANISOU  912  SG  CYS A 160     2786   3741   3789    358    215   -197       S  
ATOM    913  N   GLY A 161      13.290  11.233 149.591  1.00 22.49           N  
ANISOU  913  N   GLY A 161     2494   2701   3349    162    163   -261       N  
ATOM    914  CA  GLY A 161      13.001  10.878 150.974  1.00 23.97           C  
ANISOU  914  CA  GLY A 161     2883   2825   3399     45    205   -129       C  
ATOM    915  C   GLY A 161      12.349  12.060 151.664  1.00 25.30           C  
ANISOU  915  C   GLY A 161     2882   3063   3667    219    289   -164       C  
ATOM    916  O   GLY A 161      11.785  12.943 151.016  1.00 25.06           O  
ANISOU  916  O   GLY A 161     2886   3320   3316    192    416    -50       O  
ATOM    917  N   GLU A 162      12.431  12.090 152.988  1.00 26.41           N  
ANISOU  917  N   GLU A 162     3409   2756   3868   -371    540    -68       N  
ATOM    918  CA  GLU A 162      11.870  13.207 153.754  1.00 28.94           C  
ANISOU  918  CA  GLU A 162     3928   3102   3962   -202    377   -320       C  
ATOM    919  C   GLU A 162      12.689  13.462 154.995  1.00 29.09           C  
ANISOU  919  C   GLU A 162     4169   3034   3848   -108    251   -139       C  
ATOM    920  O   GLU A 162      13.397  12.581 155.472  1.00 27.00           O  
ANISOU  920  O   GLU A 162     4223   2657   3377   -194    380   -263       O  
ATOM    921  CB  GLU A 162      10.391  12.973 154.086  1.00 33.02           C  
ANISOU  921  CB  GLU A 162     4125   3867   4551   -251    867   -398       C  
ATOM    922  CG  GLU A 162      10.106  11.579 154.575  1.00 38.71           C  
ANISOU  922  CG  GLU A 162     5278   4044   5386   -489   1074   -271       C  
ATOM    923  CD  GLU A 162       8.624  11.264 154.720  1.00 44.55           C  
ANISOU  923  CD  GLU A 162     5446   4948   6531   -735   1659  -1185       C  
ATOM    924  OE1 GLU A 162       7.918  12.038 155.402  1.00 51.46           O  
ANISOU  924  OE1 GLU A 162     6556   6493   6502   -509   2456   -833       O  
ATOM    925  OE2 GLU A 162       8.183  10.218 154.171  1.00 56.65           O  
ANISOU  925  OE2 GLU A 162     6932   5420   9170  -2316   1910   -968       O  
ATOM    926  N   PHE A 163      12.587  14.690 155.490  1.00 29.16           N  
ANISOU  926  N   PHE A 163     4230   3043   3806   -112    138   -182       N  
ATOM    927  CA  PHE A 163      13.348  15.136 156.640  1.00 31.88           C  
ANISOU  927  CA  PHE A 163     4947   3157   4009    -27   -283   -245       C  
ATOM    928  C   PHE A 163      13.001  14.365 157.906  1.00 34.70           C  
ANISOU  928  C   PHE A 163     6080   3117   3985     30   -119   -283       C  
ATOM    929  O   PHE A 163      13.902  13.971 158.638  1.00 36.39           O  
ANISOU  929  O   PHE A 163     6536   3206   4083     55   -490   -455       O  
ATOM    930  CB  PHE A 163      13.108  16.624 156.875  1.00 31.70           C  
ANISOU  930  CB  PHE A 163     4991   3178   3874    -36   -357   -304       C  
ATOM    931  CG  PHE A 163      13.994  17.230 157.925  1.00 33.74           C  
ANISOU  931  CG  PHE A 163     5683   3159   3977    111   -753   -306       C  
ATOM    932  CD1 PHE A 163      15.274  17.674 157.605  1.00 33.58           C  
ANISOU  932  CD1 PHE A 163     5437   3158   4162    109  -1253   -177       C  
ATOM    933  CD2 PHE A 163      13.536  17.400 159.231  1.00 37.21           C  
ANISOU  933  CD2 PHE A 163     6578   3677   3882    151   -735   -284       C  
ATOM    934  CE1 PHE A 163      16.079  18.267 158.567  1.00 36.16           C  
ANISOU  934  CE1 PHE A 163     6038   3324   4375    107  -1700    -88       C  
ATOM    935  CE2 PHE A 163      14.340  17.991 160.196  1.00 39.83           C  
ANISOU  935  CE2 PHE A 163     7247   3814   4072    199  -1135   -357       C  
ATOM    936  CZ  PHE A 163      15.614  18.423 159.865  1.00 38.89           C  
ANISOU  936  CZ  PHE A 163     7028   3432   4314    181  -1669   -278       C  
ATOM    937  N   ASP A 164      11.710  14.138 158.145  1.00 37.74           N  
ANISOU  937  N   ASP A 164     6241   3592   4505     74    329   -317       N  
ATOM    938  CA  ASP A 164      11.229  13.577 159.429  1.00 45.22           C  
ANISOU  938  CA  ASP A 164     7826   4594   4759    -21    568     28       C  
ATOM    939  C   ASP A 164      11.679  12.149 159.715  1.00 46.67           C  
ANISOU  939  C   ASP A 164     8415   4517   4800     44    613     19       C  
ATOM    940  O   ASP A 164      11.877  11.799 160.877  1.00 48.16           O  
ANISOU  940  O   ASP A 164     9525   4067   4706    248    907     46       O  
ATOM    941  CB  ASP A 164       9.690  13.548 159.508  1.00 49.62           C  
ANISOU  941  CB  ASP A 164     7935   5379   5540   -247   1246   -243       C  
ATOM    942  CG  ASP A 164       9.058  14.908 159.407  1.00 52.89           C  
ANISOU  942  CG  ASP A 164     8235   5554   6305     25   1227   -529       C  
ATOM    943  OD1 ASP A 164       9.701  15.913 159.786  1.00 56.37           O  
ANISOU  943  OD1 ASP A 164     8893   6188   6337   -415    792   -624       O  
ATOM    944  OD2 ASP A 164       7.893  14.956 158.952  1.00 60.65           O  
ANISOU  944  OD2 ASP A 164     8177   7108   7759   -816    938   -598       O  
ATOM    945  N   THR A 165      11.815  11.333 158.671  1.00 44.81           N  
ANISOU  945  N   THR A 165     7963   4350   4710   -131    614     71       N  
ATOM    946  CA  THR A 165      11.909   9.890 158.842  1.00 44.89           C  
ANISOU  946  CA  THR A 165     7784   4347   4925   -240    948    166       C  
ATOM    947  C   THR A 165      12.964   9.255 157.951  1.00 41.80           C  
ANISOU  947  C   THR A 165     7115   3998   4769   -369    579    320       C  
ATOM    948  O   THR A 165      13.603   9.925 157.151  1.00 39.93           O  
ANISOU  948  O   THR A 165     6175   4021   4972   -550    251    281       O  
ATOM    949  CB  THR A 165      10.528   9.245 158.597  1.00 48.21           C  
ANISOU  949  CB  THR A 165     7804   5007   5504   -498   1376     52       C  
ATOM    950  OG1 THR A 165      10.587   7.836 158.866  1.00 57.39           O  
ANISOU  950  OG1 THR A 165     9298   5107   7399     -5   1581    -33       O  
ATOM    951  CG2 THR A 165      10.025   9.482 157.181  1.00 43.61           C  
ANISOU  951  CG2 THR A 165     6745   4426   5398   -644   1636    -52       C  
ATOM    952  N   SER A 166      13.135   7.947 158.105  1.00 42.32           N  
ANISOU  952  N   SER A 166     7166   4054   4858   -256    830    382       N  
ATOM    953  CA  SER A 166      14.058   7.177 157.284  1.00 40.88           C  
ANISOU  953  CA  SER A 166     6841   3709   4984   -239    621    453       C  
ATOM    954  C   SER A 166      13.345   6.463 156.136  1.00 38.38           C  
ANISOU  954  C   SER A 166     6171   3326   5085   -408    968    388       C  
ATOM    955  O   SER A 166      13.861   5.489 155.614  1.00 41.52           O  
ANISOU  955  O   SER A 166     6160   3794   5820   -166   1328    282       O  
ATOM    956  CB  SER A 166      14.797   6.167 158.165  1.00 43.68           C  
ANISOU  956  CB  SER A 166     7711   3632   5250    -98    598    702       C  
ATOM    957  OG  SER A 166      13.880   5.251 158.732  1.00 46.23           O  
ANISOU  957  OG  SER A 166     8202   3632   5730   -234    959    625       O  
ATOM    958  N   LYS A 167      12.187   6.958 155.720  1.00 35.84           N  
ANISOU  958  N   LYS A 167     5757   3193   4667   -519   1294     10       N  
ATOM    959  CA  LYS A 167      11.355   6.275 154.733  1.00 35.31           C  
ANISOU  959  CA  LYS A 167     5417   3212   4786   -679   1489     18       C  
ATOM    960  C   LYS A 167      11.499   6.900 153.355  1.00 31.43           C  
ANISOU  960  C   LYS A 167     4364   2945   4630   -723   1283   -150       C  
ATOM    961  O   LYS A 167      11.726   8.097 153.215  1.00 30.49           O  
ANISOU  961  O   LYS A 167     4075   2829   4682   -459    909   -191       O  
ATOM    962  CB  LYS A 167       9.887   6.320 155.134  1.00 37.28           C  
ANISOU  962  CB  LYS A 167     5580   3488   5097   -955   1856   -161       C  
ATOM    963  CG  LYS A 167       9.594   5.595 156.426  1.00 41.67           C  
ANISOU  963  CG  LYS A 167     6580   3897   5355   -941   2064     96       C  
ATOM    964  CD  LYS A 167       8.102   5.524 156.691  1.00 44.65           C  
ANISOU  964  CD  LYS A 167     6752   4326   5887  -1163   2548    -84       C  
ATOM    965  CE  LYS A 167       7.792   4.733 157.954  1.00 49.27           C  
ANISOU  965  CE  LYS A 167     7912   4576   6231  -1233   2930    138       C  
ATOM    966  NZ  LYS A 167       7.311   3.353 157.640  1.00 51.83           N  
ANISOU  966  NZ  LYS A 167     8297   4625   6772  -1392   3186      7       N  
ATOM    967  N   ILE A 168      11.343   6.069 152.337  1.00 30.30           N  
ANISOU  967  N   ILE A 168     4190   2735   4586   -869   1516    -81       N  
ATOM    968  CA  ILE A 168      11.275   6.546 150.974  1.00 28.58           C  
ANISOU  968  CA  ILE A 168     3744   2629   4487   -846   1236   -278       C  
ATOM    969  C   ILE A 168       9.889   7.163 150.761  1.00 28.15           C  
ANISOU  969  C   ILE A 168     3500   2788   4407   -990   1366   -563       C  
ATOM    970  O   ILE A 168       8.906   6.630 151.239  1.00 29.73           O  
ANISOU  970  O   ILE A 168     3698   2955   4642  -1278   1457   -778       O  
ATOM    971  CB  ILE A 168      11.615   5.418 149.981  1.00 28.94           C  
ANISOU  971  CB  ILE A 168     3873   2511   4610   -885   1307   -270       C  
ATOM    972  CG1 ILE A 168      13.113   5.093 150.093  1.00 29.03           C  
ANISOU  972  CG1 ILE A 168     3999   2383   4647   -672   1165   -123       C  
ATOM    973  CG2 ILE A 168      11.260   5.816 148.559  1.00 28.08           C  
ANISOU  973  CG2 ILE A 168     3573   2551   4542   -969   1236   -432       C  
ATOM    974  CD1 ILE A 168      13.589   3.908 149.278  1.00 30.26           C  
ANISOU  974  CD1 ILE A 168     4288   2343   4865   -632   1377    -99       C  
ATOM    975  N   ASN A 169       9.826   8.313 150.090  1.00 26.24           N  
ANISOU  975  N   ASN A 169     3069   2791   4110   -825   1095   -671       N  
ATOM    976  CA  ASN A 169       8.545   8.954 149.805  1.00 27.33           C  
ANISOU  976  CA  ASN A 169     2938   3014   4430   -874   1094   -806       C  
ATOM    977  C   ASN A 169       7.970   8.473 148.474  1.00 28.05           C  
ANISOU  977  C   ASN A 169     2880   3121   4656  -1067    970   -878       C  
ATOM    978  O   ASN A 169       8.407   8.921 147.405  1.00 25.35           O  
ANISOU  978  O   ASN A 169     2517   2648   4466   -910    607   -798       O  
ATOM    979  CB  ASN A 169       8.675  10.476 149.799  1.00 26.03           C  
ANISOU  979  CB  ASN A 169     2608   2997   4284   -809    889   -786       C  
ATOM    980  CG  ASN A 169       7.324  11.179 149.758  1.00 28.42           C  
ANISOU  980  CG  ASN A 169     2615   3358   4825   -729    736   -901       C  
ATOM    981  OD1 ASN A 169       6.298  10.590 149.361  1.00 30.55           O  
ANISOU  981  OD1 ASN A 169     2645   3587   5374   -984    871   -830       O  
ATOM    982  ND2 ASN A 169       7.311  12.447 150.165  1.00 27.62           N  
ANISOU  982  ND2 ASN A 169     2367   3409   4718   -602    545   -969       N  
ATOM    983  N   TYR A 170       6.985   7.575 148.555  1.00 30.59           N  
ANISOU  983  N   TYR A 170     3029   3435   5157  -1293   1179   -938       N  
ATOM    984  CA  TYR A 170       6.291   7.051 147.367  1.00 32.08           C  
ANISOU  984  CA  TYR A 170     3107   3534   5544  -1466   1080  -1208       C  
ATOM    985  C   TYR A 170       5.098   7.910 146.932  1.00 33.88           C  
ANISOU  985  C   TYR A 170     2821   4050   5999  -1511    884  -1307       C  
ATOM    986  O   TYR A 170       4.500   7.643 145.893  1.00 35.36           O  
ANISOU  986  O   TYR A 170     2775   4369   6289  -1793    753  -1380       O  
ATOM    987  CB  TYR A 170       5.858   5.597 147.598  1.00 34.39           C  
ANISOU  987  CB  TYR A 170     3480   3616   5970  -1660   1268  -1250       C  
ATOM    988  CG  TYR A 170       7.030   4.642 147.698  1.00 33.03           C  
ANISOU  988  CG  TYR A 170     3669   3236   5642  -1679   1420  -1051       C  
ATOM    989  CD1 TYR A 170       7.696   4.194 146.553  1.00 32.20           C  
ANISOU  989  CD1 TYR A 170     3761   2977   5493  -1607   1260  -1062       C  
ATOM    990  CD2 TYR A 170       7.483   4.196 148.940  1.00 33.42           C  
ANISOU  990  CD2 TYR A 170     3872   3226   5599  -1605   1675   -861       C  
ATOM    991  CE1 TYR A 170       8.770   3.324 146.644  1.00 32.16           C  
ANISOU  991  CE1 TYR A 170     3976   2875   5366  -1511   1540   -878       C  
ATOM    992  CE2 TYR A 170       8.556   3.322 149.041  1.00 33.03           C  
ANISOU  992  CE2 TYR A 170     4186   2948   5415  -1508   1794   -732       C  
ATOM    993  CZ  TYR A 170       9.198   2.900 147.896  1.00 32.32           C  
ANISOU  993  CZ  TYR A 170     4211   2732   5335  -1491   1688   -763       C  
ATOM    994  OH  TYR A 170      10.257   2.047 148.019  1.00 32.49           O  
ANISOU  994  OH  TYR A 170     4458   2496   5391  -1401   2114   -716       O  
ATOM    995  N   GLN A 171       4.785   8.948 147.710  1.00 35.43           N  
ANISOU  995  N   GLN A 171     3011   4250   6199  -1382    920  -1448       N  
ATOM    996  CA  GLN A 171       3.598   9.795 147.495  1.00 38.77           C  
ANISOU  996  CA  GLN A 171     3045   4804   6881  -1282    625  -1447       C  
ATOM    997  C   GLN A 171       3.896  10.901 146.482  1.00 35.74           C  
ANISOU  997  C   GLN A 171     2679   4552   6347  -1055    286  -1643       C  
ATOM    998  O   GLN A 171       3.200  11.032 145.484  1.00 36.31           O  
ANISOU  998  O   GLN A 171     2672   4597   6525   -952    114  -1951       O  
ATOM    999  CB  GLN A 171       3.037  10.308 148.857  1.00 42.71           C  
ANISOU  999  CB  GLN A 171     3441   5533   7253  -1274   1165  -1550       C  
ATOM   1000  CG  GLN A 171       2.728  11.804 149.042  1.00 46.31           C  
ANISOU 1000  CG  GLN A 171     3935   5708   7950  -1025   1065  -1420       C  
ATOM   1001  CD  GLN A 171       3.600  12.503 150.115  1.00 48.98           C  
ANISOU 1001  CD  GLN A 171     4766   6170   7674  -1244    942  -1374       C  
ATOM   1002  OE1 GLN A 171       3.584  12.110 151.289  1.00 58.67           O  
ANISOU 1002  OE1 GLN A 171     7036   7609   7647  -1078   1348  -1335       O  
ATOM   1003  NE2 GLN A 171       4.339  13.548 149.721  1.00 43.22           N  
ANISOU 1003  NE2 GLN A 171     4236   5234   6949   -487    844  -1472       N  
ATOM   1004  N   SER A 172       4.934  11.685 146.743  1.00 32.68           N  
ANISOU 1004  N   SER A 172     2438   4228   5750   -861    357  -1354       N  
ATOM   1005  CA  SER A 172       5.342  12.765 145.841  1.00 31.33           C  
ANISOU 1005  CA  SER A 172     2372   4154   5375   -654    134  -1373       C  
ATOM   1006  C   SER A 172       6.819  13.110 146.036  1.00 28.20           C  
ANISOU 1006  C   SER A 172     2394   3594   4726   -646    129  -1199       C  
ATOM   1007  O   SER A 172       7.418  12.778 147.066  1.00 28.03           O  
ANISOU 1007  O   SER A 172     2119   3723   4805  -1116    -54  -1297       O  
ATOM   1008  CB  SER A 172       4.492  14.016 146.068  1.00 32.11           C  
ANISOU 1008  CB  SER A 172     2187   4385   5626   -579    173  -1489       C  
ATOM   1009  OG  SER A 172       4.744  14.559 147.351  1.00 30.82           O  
ANISOU 1009  OG  SER A 172     1970   4250   5490   -525    556  -1493       O  
ATOM   1010  N   CYS A 173       7.392  13.740 145.018  1.00 26.22           N  
ANISOU 1010  N   CYS A 173     2298   3226   4435   -357    -32  -1226       N  
ATOM   1011  CA  CYS A 173       8.761  14.226 145.046  1.00 25.08           C  
ANISOU 1011  CA  CYS A 173     2284   3131   4114   -328   -160   -998       C  
ATOM   1012  C   CYS A 173       8.826  15.606 144.407  1.00 24.27           C  
ANISOU 1012  C   CYS A 173     2159   3132   3929    -38   -312   -983       C  
ATOM   1013  O   CYS A 173       7.976  15.945 143.581  1.00 23.90           O  
ANISOU 1013  O   CYS A 173     2344   2854   3880     15   -491  -1247       O  
ATOM   1014  CB  CYS A 173       9.710  13.271 144.317  1.00 26.31           C  
ANISOU 1014  CB  CYS A 173     2613   3268   4113   -303     20  -1047       C  
ATOM   1015  SG  CYS A 173       9.955  11.705 145.194  1.00 30.16           S  
ANISOU 1015  SG  CYS A 173     3514   3673   4270   -516    202   -686       S  
ATOM   1016  N   PRO A 174       9.827  16.419 144.798  1.00 22.89           N  
ANISOU 1016  N   PRO A 174     2116   2785   3796      5   -177   -773       N  
ATOM   1017  CA  PRO A 174       9.847  17.760 144.213  1.00 23.32           C  
ANISOU 1017  CA  PRO A 174     2239   2913   3708    142   -291   -628       C  
ATOM   1018  C   PRO A 174      10.010  17.756 142.696  1.00 24.37           C  
ANISOU 1018  C   PRO A 174     2592   2985   3681    368   -345   -661       C  
ATOM   1019  O   PRO A 174      10.836  17.020 142.157  1.00 24.97           O  
ANISOU 1019  O   PRO A 174     2897   2712   3876    492   -196   -431       O  
ATOM   1020  CB  PRO A 174      11.061  18.418 144.872  1.00 22.29           C  
ANISOU 1020  CB  PRO A 174     2111   2678   3677    182   -253   -495       C  
ATOM   1021  CG  PRO A 174      11.204  17.715 146.177  1.00 21.66           C  
ANISOU 1021  CG  PRO A 174     1986   2578   3663     61   -182   -513       C  
ATOM   1022  CD  PRO A 174      10.811  16.287 145.890  1.00 21.78           C  
ANISOU 1022  CD  PRO A 174     1990   2622   3664    -19    -52   -621       C  
ATOM   1023  N   ASP A 175       9.200  18.565 142.026  1.00 25.18           N  
ANISOU 1023  N   ASP A 175     2570   3250   3747    478   -536   -782       N  
ATOM   1024  CA  ASP A 175       9.421  18.900 140.631  1.00 25.77           C  
ANISOU 1024  CA  ASP A 175     2995   3113   3682    580   -689   -746       C  
ATOM   1025  C   ASP A 175      10.505  19.992 140.568  1.00 25.20           C  
ANISOU 1025  C   ASP A 175     3036   2947   3591    670   -655   -623       C  
ATOM   1026  O   ASP A 175      10.471  20.968 141.331  1.00 22.77           O  
ANISOU 1026  O   ASP A 175     2287   2796   3569    817   -905   -570       O  
ATOM   1027  CB  ASP A 175       8.125  19.409 140.007  1.00 27.63           C  
ANISOU 1027  CB  ASP A 175     3199   3492   3806    614  -1032   -887       C  
ATOM   1028  CG  ASP A 175       8.307  19.842 138.588  1.00 29.30           C  
ANISOU 1028  CG  ASP A 175     3768   3607   3758    889  -1235   -776       C  
ATOM   1029  OD1 ASP A 175       8.257  18.979 137.709  1.00 31.55           O  
ANISOU 1029  OD1 ASP A 175     4514   3607   3865    852  -1400   -758       O  
ATOM   1030  OD2 ASP A 175       8.514  21.046 138.346  1.00 29.25           O  
ANISOU 1030  OD2 ASP A 175     3967   3624   3523   1046  -1381   -619       O  
ATOM   1031  N   TRP A 176      11.444  19.829 139.640  1.00 26.73           N  
ANISOU 1031  N   TRP A 176     3605   2948   3603    739   -369   -445       N  
ATOM   1032  CA  TRP A 176      12.571  20.746 139.519  1.00 28.19           C  
ANISOU 1032  CA  TRP A 176     3841   2982   3887    688   -107   -200       C  
ATOM   1033  C   TRP A 176      12.135  22.203 139.270  1.00 28.89           C  
ANISOU 1033  C   TRP A 176     4099   3051   3826    897   -237   -269       C  
ATOM   1034  O   TRP A 176      12.744  23.115 139.794  1.00 27.92           O  
ANISOU 1034  O   TRP A 176     3876   2714   4016    878   -108    -24       O  
ATOM   1035  CB  TRP A 176      13.550  20.275 138.440  1.00 30.71           C  
ANISOU 1035  CB  TRP A 176     4368   3117   4183    915    243   -154       C  
ATOM   1036  CG  TRP A 176      13.091  20.496 137.050  1.00 35.03           C  
ANISOU 1036  CG  TRP A 176     5437   3622   4249   1101     68   -103       C  
ATOM   1037  CD1 TRP A 176      12.365  19.637 136.283  1.00 38.76           C  
ANISOU 1037  CD1 TRP A 176     6393   3857   4476    929   -216   -288       C  
ATOM   1038  CD2 TRP A 176      13.320  21.662 136.246  1.00 38.57           C  
ANISOU 1038  CD2 TRP A 176     6330   3753   4569   1111    284     78       C  
ATOM   1039  NE1 TRP A 176      12.128  20.192 135.048  1.00 42.19           N  
ANISOU 1039  NE1 TRP A 176     7389   4285   4354   1057   -180   -278       N  
ATOM   1040  CE2 TRP A 176      12.697  21.437 134.999  1.00 41.86           C  
ANISOU 1040  CE2 TRP A 176     7217   4185   4500   1221    129    -11       C  
ATOM   1041  CE3 TRP A 176      13.987  22.875 136.463  1.00 40.07           C  
ANISOU 1041  CE3 TRP A 176     6488   3805   4931    976    437    219       C  
ATOM   1042  CZ2 TRP A 176      12.721  22.383 133.961  1.00 45.29           C  
ANISOU 1042  CZ2 TRP A 176     8158   4396   4651   1436    165    136       C  
ATOM   1043  CZ3 TRP A 176      14.008  23.826 135.430  1.00 43.63           C  
ANISOU 1043  CZ3 TRP A 176     7384   4187   5004   1147    391    416       C  
ATOM   1044  CH2 TRP A 176      13.380  23.568 134.195  1.00 45.00           C  
ANISOU 1044  CH2 TRP A 176     7994   4279   4821   1483    385    309       C  
ATOM   1045  N   ARG A 177      11.078  22.396 138.487  1.00 30.79           N  
ANISOU 1045  N   ARG A 177     4387   3427   3882   1121   -423   -291       N  
ATOM   1046  CA  ARG A 177      10.643  23.729 138.073  1.00 33.50           C  
ANISOU 1046  CA  ARG A 177     4994   3519   4212   1218   -623   -226       C  
ATOM   1047  C   ARG A 177       9.683  24.359 139.097  1.00 31.98           C  
ANISOU 1047  C   ARG A 177     4474   3594   4081   1159   -937   -314       C  
ATOM   1048  O   ARG A 177       9.835  25.527 139.478  1.00 32.12           O  
ANISOU 1048  O   ARG A 177     4485   3487   4232   1128  -1143   -190       O  
ATOM   1049  CB  ARG A 177       9.988  23.642 136.677  1.00 37.89           C  
ANISOU 1049  CB  ARG A 177     5893   4163   4337   1345   -947   -376       C  
ATOM   1050  CG  ARG A 177      10.020  24.939 135.878  1.00 41.54           C  
ANISOU 1050  CG  ARG A 177     6775   4393   4615   1476   -915   -175       C  
ATOM   1051  CD  ARG A 177       9.335  24.836 134.515  1.00 46.24           C  
ANISOU 1051  CD  ARG A 177     7803   5103   4660   1761  -1203   -333       C  
ATOM   1052  NE  ARG A 177       8.007  24.236 134.629  1.00 47.82           N  
ANISOU 1052  NE  ARG A 177     7698   5572   4897   1684  -1789   -805       N  
ATOM   1053  CZ  ARG A 177       6.855  24.886 134.827  1.00 50.71           C  
ANISOU 1053  CZ  ARG A 177     7828   5869   5571   2009  -2126   -755       C  
ATOM   1054  NH1 ARG A 177       6.792  26.212 134.911  1.00 52.46           N  
ANISOU 1054  NH1 ARG A 177     8114   5862   5955   2077  -1999   -799       N  
ATOM   1055  NH2 ARG A 177       5.731  24.183 134.926  1.00 53.86           N  
ANISOU 1055  NH2 ARG A 177     7802   6491   6170   1836  -2277   -851       N  
ATOM   1056  N   LYS A 178       8.698  23.580 139.541  1.00 31.44           N  
ANISOU 1056  N   LYS A 178     4028   3797   4119   1186  -1079   -503       N  
ATOM   1057  CA  LYS A 178       7.644  24.085 140.441  1.00 31.33           C  
ANISOU 1057  CA  LYS A 178     3774   3816   4311   1272  -1250   -674       C  
ATOM   1058  C   LYS A 178       8.013  24.092 141.910  1.00 28.61           C  
ANISOU 1058  C   LYS A 178     3176   3513   4179   1093   -945   -645       C  
ATOM   1059  O   LYS A 178       7.511  24.944 142.647  1.00 28.43           O  
ANISOU 1059  O   LYS A 178     3146   3159   4493   1582  -1051   -253       O  
ATOM   1060  CB  LYS A 178       6.361  23.272 140.277  1.00 33.22           C  
ANISOU 1060  CB  LYS A 178     3665   4276   4679   1258  -1375   -793       C  
ATOM   1061  CG  LYS A 178       5.629  23.551 138.983  1.00 36.96           C  
ANISOU 1061  CG  LYS A 178     4368   4752   4923   1428  -1799   -891       C  
ATOM   1062  CD  LYS A 178       4.540  22.523 138.737  1.00 39.66           C  
ANISOU 1062  CD  LYS A 178     4535   5169   5364   1251  -2056  -1161       C  
ATOM   1063  CE  LYS A 178       3.306  23.173 138.151  1.00 44.19           C  
ANISOU 1063  CE  LYS A 178     4900   5913   5975   1497  -2516  -1246       C  
ATOM   1064  NZ  LYS A 178       2.465  22.149 137.487  1.00 48.26           N  
ANISOU 1064  NZ  LYS A 178     5355   6448   6531   1285  -2861  -1465       N  
ATOM   1065  N   ASP A 179       8.849  23.143 142.344  1.00 26.67           N  
ANISOU 1065  N   ASP A 179     2881   3204   4047    896   -687   -668       N  
ATOM   1066  CA  ASP A 179       9.251  23.023 143.765  1.00 26.18           C  
ANISOU 1066  CA  ASP A 179     2694   3210   4043    762   -652   -640       C  
ATOM   1067  C   ASP A 179      10.679  23.508 144.049  1.00 24.62           C  
ANISOU 1067  C   ASP A 179     2761   2846   3745    687   -546   -527       C  
ATOM   1068  O   ASP A 179      10.848  24.574 144.658  1.00 25.03           O  
ANISOU 1068  O   ASP A 179     2824   2850   3833    819   -540   -641       O  
ATOM   1069  CB  ASP A 179       9.042  21.588 144.263  1.00 26.49           C  
ANISOU 1069  CB  ASP A 179     2608   3306   4147    592   -482   -625       C  
ATOM   1070  CG  ASP A 179       7.594  21.128 144.117  1.00 29.17           C  
ANISOU 1070  CG  ASP A 179     2630   3749   4705    525   -435   -816       C  
ATOM   1071  OD1 ASP A 179       6.687  21.913 144.416  1.00 32.63           O  
ANISOU 1071  OD1 ASP A 179     2775   4299   5322    896    -36   -208       O  
ATOM   1072  OD2 ASP A 179       7.345  19.985 143.701  1.00 28.94           O  
ANISOU 1072  OD2 ASP A 179     2456   4109   4429    295   -467  -1096       O  
ATOM   1073  N   CYS A 180      11.688  22.760 143.605  1.00 31.48           N  
ANISOU 1073  N   CYS A 180     3589   3455   4917    793    388     26       N  
ATOM   1074  CA  CYS A 180      13.082  23.105 143.855  1.00 32.43           C  
ANISOU 1074  CA  CYS A 180     3649   3321   5352    625    589   -286       C  
ATOM   1075  C   CYS A 180      14.025  22.318 142.944  1.00 27.99           C  
ANISOU 1075  C   CYS A 180     3128   2915   4591    405    246    -48       C  
ATOM   1076  O   CYS A 180      13.812  21.133 142.667  1.00 24.87           O  
ANISOU 1076  O   CYS A 180     2624   2951   3874    661     83   -196       O  
ATOM   1077  CB  CYS A 180      13.458  22.833 145.313  1.00 35.62           C  
ANISOU 1077  CB  CYS A 180     4143   4018   5372    553    367   -546       C  
ATOM   1078  SG  CYS A 180      13.216  21.101 145.795  1.00 37.03           S  
ANISOU 1078  SG  CYS A 180     4384   4536   5148    310     91    -50       S  
ATOM   1079  N   SER A 181      15.083  22.971 142.501  1.00 27.15           N  
ANISOU 1079  N   SER A 181     3106   2531   4677    554    404   -208       N  
ATOM   1080  CA  SER A 181      16.049  22.324 141.653  1.00 26.26           C  
ANISOU 1080  CA  SER A 181     2911   2514   4552    366    423    -88       C  
ATOM   1081  C   SER A 181      17.046  21.416 142.420  1.00 23.04           C  
ANISOU 1081  C   SER A 181     2407   2212   4134     69    382   -382       C  
ATOM   1082  O   SER A 181      17.600  20.519 141.814  1.00 20.50           O  
ANISOU 1082  O   SER A 181     1916   2164   3707    -51    293   -265       O  
ATOM   1083  CB  SER A 181      16.780  23.365 140.806  1.00 28.65           C  
ANISOU 1083  CB  SER A 181     3428   2387   5069    283    665    -50       C  
ATOM   1084  OG  SER A 181      17.473  24.255 141.639  1.00 31.98           O  
ANISOU 1084  OG  SER A 181     4133   2420   5597     48    829   -449       O  
ATOM   1085  N   ASN A 182      17.247  21.604 143.731  1.00 22.43           N  
ANISOU 1085  N   ASN A 182     2186   2156   4179     46    342   -541       N  
ATOM   1086  CA  ASN A 182      18.195  20.748 144.492  1.00 21.37           C  
ANISOU 1086  CA  ASN A 182     2128   2119   3870   -107    239   -644       C  
ATOM   1087  C   ASN A 182      17.541  19.536 145.137  1.00 19.38           C  
ANISOU 1087  C   ASN A 182     1790   2144   3427    -36     77   -653       C  
ATOM   1088  O   ASN A 182      17.631  19.302 146.338  1.00 18.56           O  
ANISOU 1088  O   ASN A 182     1619   2048   3385   -170    114   -732       O  
ATOM   1089  CB  ASN A 182      19.027  21.552 145.496  1.00 23.18           C  
ANISOU 1089  CB  ASN A 182     2282   2313   4211   -171    255   -968       C  
ATOM   1090  CG  ASN A 182      20.181  22.257 144.825  1.00 25.44           C  
ANISOU 1090  CG  ASN A 182     2536   2394   4735   -376    403   -980       C  
ATOM   1091  OD1 ASN A 182      19.997  23.329 144.282  1.00 28.12           O  
ANISOU 1091  OD1 ASN A 182     2759   2511   5413   -536    428   -621       O  
ATOM   1092  ND2 ASN A 182      21.386  21.650 144.849  1.00 26.04           N  
ANISOU 1092  ND2 ASN A 182     2474   2663   4756   -420    383  -1091       N  
ATOM   1093  N   ASN A 183      16.936  18.736 144.277  1.00 18.14           N  
ANISOU 1093  N   ASN A 183     1713   1951   3228     18     50   -448       N  
ATOM   1094  CA  ASN A 183      16.199  17.561 144.676  1.00 17.33           C  
ANISOU 1094  CA  ASN A 183     1593   2025   2966     21    -19   -409       C  
ATOM   1095  C   ASN A 183      17.021  16.308 144.335  1.00 16.37           C  
ANISOU 1095  C   ASN A 183     1525   1932   2764    -33    -46   -327       C  
ATOM   1096  O   ASN A 183      17.936  16.382 143.525  1.00 15.44           O  
ANISOU 1096  O   ASN A 183     1458   1669   2738    -61    -78   -339       O  
ATOM   1097  CB  ASN A 183      14.833  17.567 143.982  1.00 17.39           C  
ANISOU 1097  CB  ASN A 183     1583   2087   2938     57      3   -297       C  
ATOM   1098  CG  ASN A 183      14.936  17.363 142.492  1.00 17.03           C  
ANISOU 1098  CG  ASN A 183     1556   2016   2898     49    -23   -175       C  
ATOM   1099  OD1 ASN A 183      15.242  16.265 142.023  1.00 16.41           O  
ANISOU 1099  OD1 ASN A 183     1555   1925   2752    -67    -49   -131       O  
ATOM   1100  ND2 ASN A 183      14.719  18.422 141.737  1.00 17.69           N  
ANISOU 1100  ND2 ASN A 183     1624   2036   3060    162     27   -124       N  
ATOM   1101  N   PRO A 184      16.695  15.160 144.952  1.00 16.53           N  
ANISOU 1101  N   PRO A 184     1588   2006   2685    -27    -55   -273       N  
ATOM   1102  CA  PRO A 184      17.550  13.978 144.773  1.00 16.32           C  
ANISOU 1102  CA  PRO A 184     1606   1994   2600    -18    -32   -220       C  
ATOM   1103  C   PRO A 184      17.822  13.571 143.328  1.00 15.62           C  
ANISOU 1103  C   PRO A 184     1561   1789   2583    -69    -56   -196       C  
ATOM   1104  O   PRO A 184      18.965  13.219 143.012  1.00 15.57           O  
ANISOU 1104  O   PRO A 184     1532   1896   2487   -103    -54   -190       O  
ATOM   1105  CB  PRO A 184      16.803  12.886 145.531  1.00 17.01           C  
ANISOU 1105  CB  PRO A 184     1750   2083   2629     -8     31   -133       C  
ATOM   1106  CG  PRO A 184      16.088  13.626 146.610  1.00 17.57           C  
ANISOU 1106  CG  PRO A 184     1760   2282   2632     25     31   -182       C  
ATOM   1107  CD  PRO A 184      15.679  14.934 145.997  1.00 17.26           C  
ANISOU 1107  CD  PRO A 184     1644   2195   2717     12     -2   -284       C  
ATOM   1108  N   VAL A 185      16.806  13.648 142.462  1.00 15.08           N  
ANISOU 1108  N   VAL A 185     1496   1667   2564   -138    -21   -188       N  
ATOM   1109  CA  VAL A 185      16.955  13.235 141.071  1.00 14.98           C  
ANISOU 1109  CA  VAL A 185     1476   1688   2527   -205     10   -137       C  
ATOM   1110  C   VAL A 185      17.802  14.228 140.262  1.00 14.72           C  
ANISOU 1110  C   VAL A 185     1413   1614   2564   -152    -22   -125       C  
ATOM   1111  O   VAL A 185      18.737  13.813 139.573  1.00 14.62           O  
ANISOU 1111  O   VAL A 185     1355   1666   2534   -229     25    -73       O  
ATOM   1112  CB  VAL A 185      15.586  12.993 140.404  1.00 15.70           C  
ANISOU 1112  CB  VAL A 185     1507   1903   2556   -306     24   -198       C  
ATOM   1113  CG1 VAL A 185      15.696  12.789 138.903  1.00 15.99           C  
ANISOU 1113  CG1 VAL A 185     1500   2017   2555   -351     13   -199       C  
ATOM   1114  CG2 VAL A 185      14.897  11.792 141.059  1.00 16.41           C  
ANISOU 1114  CG2 VAL A 185     1642   1962   2627   -431    119   -269       C  
ATOM   1115  N   SER A 186      17.476  15.515 140.315  1.00 14.94           N  
ANISOU 1115  N   SER A 186     1418   1627   2629   -118    -39   -140       N  
ATOM   1116  CA  SER A 186      18.183  16.488 139.488  1.00 15.28           C  
ANISOU 1116  CA  SER A 186     1445   1602   2756    -87      5    -99       C  
ATOM   1117  C   SER A 186      19.665  16.566 139.915  1.00 15.02           C  
ANISOU 1117  C   SER A 186     1438   1490   2777    -46      5   -134       C  
ATOM   1118  O   SER A 186      20.557  16.719 139.087  1.00 15.07           O  
ANISOU 1118  O   SER A 186     1336   1478   2910     73     61   -223       O  
ATOM   1119  CB  SER A 186      17.562  17.883 139.599  1.00 16.42           C  
ANISOU 1119  CB  SER A 186     1575   1689   2973     42     69    -28       C  
ATOM   1120  OG  SER A 186      16.222  17.926 139.120  1.00 17.85           O  
ANISOU 1120  OG  SER A 186     1686   2080   3015    -14    -70      4       O  
ATOM   1121  N   VAL A 187      19.897  16.514 141.219  1.00 14.98           N  
ANISOU 1121  N   VAL A 187     1393   1512   2784    -70    -26   -230       N  
ATOM   1122  CA  VAL A 187      21.250  16.583 141.754  1.00 15.33           C  
ANISOU 1122  CA  VAL A 187     1390   1590   2846   -121    -33   -349       C  
ATOM   1123  C   VAL A 187      22.055  15.337 141.379  1.00 15.06           C  
ANISOU 1123  C   VAL A 187     1377   1585   2760    -87    -77   -283       C  
ATOM   1124  O   VAL A 187      23.241  15.454 141.020  1.00 15.35           O  
ANISOU 1124  O   VAL A 187     1389   1505   2937    -66    -28   -328       O  
ATOM   1125  CB  VAL A 187      21.245  16.854 143.255  1.00 16.01           C  
ANISOU 1125  CB  VAL A 187     1397   1808   2876   -109    -57   -468       C  
ATOM   1126  CG1 VAL A 187      22.650  16.735 143.862  1.00 17.02           C  
ANISOU 1126  CG1 VAL A 187     1408   2104   2953   -129   -102   -620       C  
ATOM   1127  CG2 VAL A 187      20.703  18.240 143.502  1.00 16.76           C  
ANISOU 1127  CG2 VAL A 187     1488   1786   3093   -169     -2   -564       C  
ATOM   1128  N   PHE A 188      21.419  14.173 141.398  1.00 14.55           N  
ANISOU 1128  N   PHE A 188     1373   1556   2597    -54    -47   -168       N  
ATOM   1129  CA  PHE A 188      22.061  12.963 140.886  1.00 14.74           C  
ANISOU 1129  CA  PHE A 188     1487   1537   2574    -41    -19   -138       C  
ATOM   1130  C   PHE A 188      22.518  13.133 139.432  1.00 14.61           C  
ANISOU 1130  C   PHE A 188     1487   1451   2613    -98     25   -119       C  
ATOM   1131  O   PHE A 188      23.681  12.855 139.116  1.00 14.90           O  
ANISOU 1131  O   PHE A 188     1508   1433   2719    -10     19    -97       O  
ATOM   1132  CB  PHE A 188      21.146  11.743 140.973  1.00 14.70           C  
ANISOU 1132  CB  PHE A 188     1581   1495   2509    -40     50    -74       C  
ATOM   1133  CG  PHE A 188      21.702  10.528 140.274  1.00 14.88           C  
ANISOU 1133  CG  PHE A 188     1705   1415   2531    -52    138    -17       C  
ATOM   1134  CD1 PHE A 188      22.530   9.624 140.952  1.00 15.79           C  
ANISOU 1134  CD1 PHE A 188     1840   1551   2607    114    194     23       C  
ATOM   1135  CD2 PHE A 188      21.406  10.291 138.949  1.00 14.58           C  
ANISOU 1135  CD2 PHE A 188     1688   1321   2527   -155    188    -37       C  
ATOM   1136  CE1 PHE A 188      23.030   8.494 140.314  1.00 16.64           C  
ANISOU 1136  CE1 PHE A 188     2060   1538   2724    187    336     87       C  
ATOM   1137  CE2 PHE A 188      21.925   9.182 138.289  1.00 15.39           C  
ANISOU 1137  CE2 PHE A 188     1881   1340   2627   -140    300    -49       C  
ATOM   1138  CZ  PHE A 188      22.730   8.273 138.974  1.00 16.41           C  
ANISOU 1138  CZ  PHE A 188     2087   1407   2741     36    383     14       C  
ATOM   1139  N   TRP A 189      21.610  13.571 138.564  1.00 14.68           N  
ANISOU 1139  N   TRP A 189     1474   1418   2686   -127      5    -91       N  
ATOM   1140  CA  TRP A 189      21.933  13.684 137.140  1.00 15.65           C  
ANISOU 1140  CA  TRP A 189     1647   1583   2714   -132     24    -67       C  
ATOM   1141  C   TRP A 189      22.990  14.748 136.843  1.00 16.44           C  
ANISOU 1141  C   TRP A 189     1688   1641   2915   -173     52    -42       C  
ATOM   1142  O   TRP A 189      23.857  14.539 136.009  1.00 17.09           O  
ANISOU 1142  O   TRP A 189     1688   1755   3050    -96     64   -154       O  
ATOM   1143  CB  TRP A 189      20.683  13.846 136.277  1.00 16.01           C  
ANISOU 1143  CB  TRP A 189     1659   1692   2731   -180      2    -38       C  
ATOM   1144  CG  TRP A 189      19.899  12.589 136.204  1.00 16.30           C  
ANISOU 1144  CG  TRP A 189     1725   1767   2700   -265     41    -89       C  
ATOM   1145  CD1 TRP A 189      18.676  12.361 136.760  1.00 16.49           C  
ANISOU 1145  CD1 TRP A 189     1704   1866   2693   -292     28   -164       C  
ATOM   1146  CD2 TRP A 189      20.288  11.359 135.558  1.00 16.68           C  
ANISOU 1146  CD2 TRP A 189     1826   1820   2692   -320     95   -168       C  
ATOM   1147  NE1 TRP A 189      18.278  11.071 136.504  1.00 17.20           N  
ANISOU 1147  NE1 TRP A 189     1813   1978   2744   -455    108   -229       N  
ATOM   1148  CE2 TRP A 189      19.239  10.431 135.767  1.00 17.35           C  
ANISOU 1148  CE2 TRP A 189     1922   1912   2756   -431    139   -261       C  
ATOM   1149  CE3 TRP A 189      21.422  10.952 134.831  1.00 16.80           C  
ANISOU 1149  CE3 TRP A 189     1879   1792   2711   -312    120   -177       C  
ATOM   1150  CZ2 TRP A 189      19.275   9.116 135.265  1.00 18.37           C  
ANISOU 1150  CZ2 TRP A 189     2124   1994   2860   -553    267   -386       C  
ATOM   1151  CZ3 TRP A 189      21.470   9.640 134.336  1.00 17.65           C  
ANISOU 1151  CZ3 TRP A 189     2068   1840   2796   -359    255   -267       C  
ATOM   1152  CH2 TRP A 189      20.395   8.738 134.552  1.00 18.58           C  
ANISOU 1152  CH2 TRP A 189     2224   1943   2891   -510    319   -404       C  
ATOM   1153  N   LYS A 190      22.936  15.855 137.568  1.00 17.23           N  
ANISOU 1153  N   LYS A 190     1752   1660   3134    -77     96   -110       N  
ATOM   1154  CA  LYS A 190      23.947  16.902 137.492  1.00 18.99           C  
ANISOU 1154  CA  LYS A 190     1883   1878   3454   -230    137   -140       C  
ATOM   1155  C   LYS A 190      25.347  16.393 137.878  1.00 19.01           C  
ANISOU 1155  C   LYS A 190     1832   1955   3434   -237    172   -286       C  
ATOM   1156  O   LYS A 190      26.316  16.690 137.194  1.00 20.00           O  
ANISOU 1156  O   LYS A 190     1864   2056   3676   -447    241   -398       O  
ATOM   1157  CB  LYS A 190      23.508  18.042 138.408  1.00 20.67           C  
ANISOU 1157  CB  LYS A 190     2104   1968   3780   -190    217   -268       C  
ATOM   1158  CG  LYS A 190      24.410  19.236 138.492  1.00 23.34           C  
ANISOU 1158  CG  LYS A 190     2387   2186   4295   -400    349   -396       C  
ATOM   1159  CD  LYS A 190      23.702  20.406 139.196  1.00 25.26           C  
ANISOU 1159  CD  LYS A 190     2680   2296   4622   -300    469   -499       C  
ATOM   1160  CE  LYS A 190      23.524  20.109 140.689  1.00 25.61           C  
ANISOU 1160  CE  LYS A 190     2609   2578   4541   -362    370   -664       C  
ATOM   1161  NZ  LYS A 190      22.956  21.274 141.429  1.00 27.45           N  
ANISOU 1161  NZ  LYS A 190     2910   2595   4922   -369    376   -853       N  
ATOM   1162  N   THR A 191      25.433  15.631 138.970  1.00 18.65           N  
ANISOU 1162  N   THR A 191     1784   1929   3369   -123     83   -351       N  
ATOM   1163  CA  THR A 191      26.693  15.067 139.435  1.00 19.56           C  
ANISOU 1163  CA  THR A 191     1739   2325   3367   -135     18   -401       C  
ATOM   1164  C   THR A 191      27.287  14.035 138.447  1.00 19.28           C  
ANISOU 1164  C   THR A 191     1755   2263   3308    -61     47   -291       C  
ATOM   1165  O   THR A 191      28.443  14.159 138.058  1.00 19.55           O  
ANISOU 1165  O   THR A 191     1691   2283   3452      4     30   -463       O  
ATOM   1166  CB  THR A 191      26.509  14.356 140.786  1.00 20.09           C  
ANISOU 1166  CB  THR A 191     1781   2594   3258      0    -55   -402       C  
ATOM   1167  OG1 THR A 191      25.813  15.221 141.684  1.00 20.85           O  
ANISOU 1167  OG1 THR A 191     1963   2579   3380    -16   -104   -561       O  
ATOM   1168  CG2 THR A 191      27.838  13.965 141.387  1.00 21.41           C  
ANISOU 1168  CG2 THR A 191     1780   3029   3323    104    -76   -483       C  
ATOM   1169  N   VAL A 192      26.494  13.041 138.043  1.00 18.63           N  
ANISOU 1169  N   VAL A 192     1824   2082   3171    -44     59   -156       N  
ATOM   1170  CA  VAL A 192      27.006  11.981 137.166  1.00 19.23           C  
ANISOU 1170  CA  VAL A 192     1924   2186   3194     47     92   -165       C  
ATOM   1171  C   VAL A 192      27.315  12.488 135.767  1.00 19.36           C  
ANISOU 1171  C   VAL A 192     2000   2107   3246    -72    127   -154       C  
ATOM   1172  O   VAL A 192      28.276  12.028 135.157  1.00 20.31           O  
ANISOU 1172  O   VAL A 192     2037   2346   3333     53    132   -181       O  
ATOM   1173  CB  VAL A 192      26.131  10.697 137.078  1.00 19.28           C  
ANISOU 1173  CB  VAL A 192     2141   2022   3160     81    155    -64       C  
ATOM   1174  CG1 VAL A 192      26.048  10.039 138.417  1.00 20.37           C  
ANISOU 1174  CG1 VAL A 192     2325   2217   3194    206    130     -4       C  
ATOM   1175  CG2 VAL A 192      24.728  10.948 136.529  1.00 18.75           C  
ANISOU 1175  CG2 VAL A 192     2111   1905   3108    -81    134   -119       C  
ATOM   1176  N   SER A 193      26.541  13.440 135.259  1.00 19.33           N  
ANISOU 1176  N   SER A 193     1946   2076   3321   -111     52   -234       N  
ATOM   1177  CA  SER A 193      26.810  13.929 133.911  1.00 20.72           C  
ANISOU 1177  CA  SER A 193     2217   2185   3470   -199    160    -83       C  
ATOM   1178  C   SER A 193      28.029  14.868 133.838  1.00 21.32           C  
ANISOU 1178  C   SER A 193     2241   2169   3690   -190    276    -81       C  
ATOM   1179  O   SER A 193      28.758  14.849 132.837  1.00 21.15           O  
ANISOU 1179  O   SER A 193     2377   1990   3669   -277    320   -132       O  
ATOM   1180  CB  SER A 193      25.544  14.490 133.273  1.00 21.86           C  
ANISOU 1180  CB  SER A 193     2394   2360   3549    -97     90    -15       C  
ATOM   1181  OG  SER A 193      25.329  15.802 133.635  1.00 26.42           O  
ANISOU 1181  OG  SER A 193     2992   2441   4606     55     51    -64       O  
ATOM   1182  N   ARG A 194      28.285  15.633 134.905  1.00 21.66           N  
ANISOU 1182  N   ARG A 194     2212   2209   3806   -171    268   -205       N  
ATOM   1183  CA  ARG A 194      29.519  16.416 135.011  1.00 24.10           C  
ANISOU 1183  CA  ARG A 194     2255   2668   4233   -357    415   -280       C  
ATOM   1184  C   ARG A 194      30.750  15.487 134.971  1.00 24.10           C  
ANISOU 1184  C   ARG A 194     2239   2816   4102   -312    370   -400       C  
ATOM   1185  O   ARG A 194      31.663  15.699 134.193  1.00 23.31           O  
ANISOU 1185  O   ARG A 194     2058   2484   4314   -467    300   -303       O  
ATOM   1186  CB  ARG A 194      29.545  17.286 136.297  1.00 25.86           C  
ANISOU 1186  CB  ARG A 194     2448   2855   4520   -414    390   -530       C  
ATOM   1187  CG  ARG A 194      30.739  18.239 136.370  1.00 29.52           C  
ANISOU 1187  CG  ARG A 194     2653   3417   5143   -713    549   -690       C  
ATOM   1188  CD  ARG A 194      30.755  19.200 137.577  1.00 32.09           C  
ANISOU 1188  CD  ARG A 194     2875   3797   5520   -833    597  -1047       C  
ATOM   1189  NE  ARG A 194      30.504  18.491 138.836  1.00 33.19           N  
ANISOU 1189  NE  ARG A 194     3025   4224   5359   -751    296   -952       N  
ATOM   1190  CZ  ARG A 194      31.351  17.641 139.424  1.00 35.51           C  
ANISOU 1190  CZ  ARG A 194     2970   4909   5611   -399    283  -1007       C  
ATOM   1191  NH1 ARG A 194      32.540  17.380 138.906  1.00 37.17           N  
ANISOU 1191  NH1 ARG A 194     2783   5356   5983   -576    343   -951       N  
ATOM   1192  NH2 ARG A 194      30.998  17.024 140.553  1.00 37.90           N  
ANISOU 1192  NH2 ARG A 194     3475   5377   5546   -243    214   -865       N  
ATOM   1193  N   ARG A 195      30.754  14.451 135.798  1.00 24.34           N  
ANISOU 1193  N   ARG A 195     2288   2959   4000   -200    248   -367       N  
ATOM   1194  CA  ARG A 195      31.892  13.508 135.852  1.00 25.96           C  
ANISOU 1194  CA  ARG A 195     2302   3413   4146    -15    218   -435       C  
ATOM   1195  C   ARG A 195      32.147  12.760 134.544  1.00 24.01           C  
ANISOU 1195  C   ARG A 195     2185   2929   4006     15    266   -176       C  
ATOM   1196  O   ARG A 195      33.295  12.549 134.155  1.00 23.69           O  
ANISOU 1196  O   ARG A 195     2248   2906   3843     27    324   -276       O  
ATOM   1197  CB  ARG A 195      31.667  12.483 136.942  1.00 28.19           C  
ANISOU 1197  CB  ARG A 195     2619   3808   4283    164    168   -159       C  
ATOM   1198  CG  ARG A 195      31.846  13.045 138.331  1.00 32.06           C  
ANISOU 1198  CG  ARG A 195     2944   4597   4638     75     57   -620       C  
ATOM   1199  CD  ARG A 195      31.447  11.996 139.354  1.00 35.87           C  
ANISOU 1199  CD  ARG A 195     3579   5134   4916    204     30   -194       C  
ATOM   1200  NE  ARG A 195      31.945  12.325 140.684  1.00 41.62           N  
ANISOU 1200  NE  ARG A 195     4096   6473   5245    399   -332   -476       N  
ATOM   1201  CZ  ARG A 195      33.026  11.812 141.272  1.00 43.21           C  
ANISOU 1201  CZ  ARG A 195     3902   6944   5570    730   -123   -450       C  
ATOM   1202  NH1 ARG A 195      33.796  10.893 140.688  1.00 43.76           N  
ANISOU 1202  NH1 ARG A 195     4178   6872   5574    909     13   -288       N  
ATOM   1203  NH2 ARG A 195      33.329  12.228 142.493  1.00 48.59           N  
ANISOU 1203  NH2 ARG A 195     4714   7722   6026    649   -570   -880       N  
ATOM   1204  N   PHE A 196      31.057  12.348 133.907  1.00 22.39           N  
ANISOU 1204  N   PHE A 196     2207   2601   3700     32    321   -110       N  
ATOM   1205  CA  PHE A 196      31.078  11.725 132.587  1.00 22.66           C  
ANISOU 1205  CA  PHE A 196     2209   2728   3673     48    379   -101       C  
ATOM   1206  C   PHE A 196      31.690  12.666 131.535  1.00 23.36           C  
ANISOU 1206  C   PHE A 196     2253   2822   3798    -53    439    -83       C  
ATOM   1207  O   PHE A 196      32.595  12.275 130.801  1.00 24.39           O  
ANISOU 1207  O   PHE A 196     2456   3178   3632    -75    502   -197       O  
ATOM   1208  CB  PHE A 196      29.658  11.333 132.202  1.00 21.33           C  
ANISOU 1208  CB  PHE A 196     2261   2400   3440    -12    383    -62       C  
ATOM   1209  CG  PHE A 196      29.564  10.431 131.017  1.00 21.33           C  
ANISOU 1209  CG  PHE A 196     2298   2426   3380      1    498    -42       C  
ATOM   1210  CD1 PHE A 196      30.168   9.181 131.031  1.00 21.92           C  
ANISOU 1210  CD1 PHE A 196     2404   2482   3442     92    564    -66       C  
ATOM   1211  CD2 PHE A 196      28.803  10.802 129.903  1.00 21.41           C  
ANISOU 1211  CD2 PHE A 196     2356   2441   3337    -43    484    -59       C  
ATOM   1212  CE1 PHE A 196      30.063   8.336 129.937  1.00 23.02           C  
ANISOU 1212  CE1 PHE A 196     2686   2534   3524     76    602   -133       C  
ATOM   1213  CE2 PHE A 196      28.683   9.956 128.810  1.00 22.37           C  
ANISOU 1213  CE2 PHE A 196     2576   2601   3322    -83    501   -103       C  
ATOM   1214  CZ  PHE A 196      29.320   8.720 128.823  1.00 22.97           C  
ANISOU 1214  CZ  PHE A 196     2679   2620   3428    -25    608   -175       C  
ATOM   1215  N   ALA A 197      31.225  13.903 131.486  1.00 23.53           N  
ANISOU 1215  N   ALA A 197     2246   2705   3989   -187    484   -130       N  
ATOM   1216  CA  ALA A 197      31.799  14.886 130.576  1.00 25.26           C  
ANISOU 1216  CA  ALA A 197     2529   2902   4166   -233    659    -42       C  
ATOM   1217  C   ALA A 197      33.273  15.176 130.907  1.00 26.97           C  
ANISOU 1217  C   ALA A 197     2509   3086   4651   -260    705   -153       C  
ATOM   1218  O   ALA A 197      34.078  15.286 130.001  1.00 26.43           O  
ANISOU 1218  O   ALA A 197     2354   2922   4764   -249    700   -134       O  
ATOM   1219  CB  ALA A 197      30.989  16.174 130.577  1.00 25.49           C  
ANISOU 1219  CB  ALA A 197     2572   2812   4299   -299    669     49       C  
ATOM   1220  N   GLU A 198      33.619  15.272 132.192  1.00 24.91           N  
ANISOU 1220  N   GLU A 198     2740   4027   2697  -1032    283   -408       N  
ATOM   1221  CA  GLU A 198      35.032  15.463 132.598  1.00 27.94           C  
ANISOU 1221  CA  GLU A 198     2831   4659   3124  -1330    258   -395       C  
ATOM   1222  C   GLU A 198      35.937  14.308 132.204  1.00 29.71           C  
ANISOU 1222  C   GLU A 198     3017   4738   3533  -1095    206   -149       C  
ATOM   1223  O   GLU A 198      37.118  14.515 132.008  1.00 33.50           O  
ANISOU 1223  O   GLU A 198     3040   5223   4462   -922    408   -388       O  
ATOM   1224  CB  GLU A 198      35.152  15.693 134.092  1.00 30.73           C  
ANISOU 1224  CB  GLU A 198     3114   5377   3184  -1406    178   -490       C  
ATOM   1225  CG  GLU A 198      34.676  17.073 134.501  1.00 33.18           C  
ANISOU 1225  CG  GLU A 198     3518   5623   3466  -1268    296   -793       C  
ATOM   1226  CD  GLU A 198      34.528  17.246 136.002  1.00 37.88           C  
ANISOU 1226  CD  GLU A 198     4356   6579   3456  -1256     24   -956       C  
ATOM   1227  OE1 GLU A 198      34.530  16.234 136.732  1.00 41.87           O  
ANISOU 1227  OE1 GLU A 198     5031   7256   3619  -1395    227   -423       O  
ATOM   1228  OE2 GLU A 198      34.390  18.406 136.452  1.00 40.30           O  
ANISOU 1228  OE2 GLU A 198     4478   6993   3837  -1420   -711  -1767       O  
ATOM   1229  N   ALA A 199      35.372  13.111 132.079  1.00 30.82           N  
ANISOU 1229  N   ALA A 199     3163   4784   3760  -1194    217     49       N  
ATOM   1230  CA  ALA A 199      36.110  11.909 131.700  1.00 31.80           C  
ANISOU 1230  CA  ALA A 199     3304   4871   3907  -1102    105     44       C  
ATOM   1231  C   ALA A 199      36.442  11.817 130.215  1.00 31.24           C  
ANISOU 1231  C   ALA A 199     3286   4685   3896   -914    109    189       C  
ATOM   1232  O   ALA A 199      37.338  11.061 129.851  1.00 32.17           O  
ANISOU 1232  O   ALA A 199     3316   4667   4239   -947    369    229       O  
ATOM   1233  CB  ALA A 199      35.324  10.669 132.108  1.00 32.98           C  
ANISOU 1233  CB  ALA A 199     3510   4982   4038  -1155    -10    378       C  
ATOM   1234  N   ALA A 200      35.717  12.553 129.367  1.00 29.15           N  
ANISOU 1234  N   ALA A 200     3056   4323   3694   -910    211    -20       N  
ATOM   1235  CA  ALA A 200      35.819  12.397 127.926  1.00 27.80           C  
ANISOU 1235  CA  ALA A 200     3008   3894   3660   -842    109   -169       C  
ATOM   1236  C   ALA A 200      37.129  12.929 127.363  1.00 28.04           C  
ANISOU 1236  C   ALA A 200     2861   3905   3886   -783     68   -256       C  
ATOM   1237  O   ALA A 200      37.740  13.811 127.944  1.00 28.48           O  
ANISOU 1237  O   ALA A 200     2467   4428   3924   -598    -76   -566       O  
ATOM   1238  CB  ALA A 200      34.644  13.076 127.240  1.00 26.61           C  
ANISOU 1238  CB  ALA A 200     2872   3681   3556   -807    347   -236       C  
ATOM   1239  N   CYS A 201      37.542  12.391 126.217  1.00 28.57           N  
ANISOU 1239  N   CYS A 201     3023   4024   3806   -710      6   -244       N  
ATOM   1240  CA  CYS A 201      38.790  12.802 125.565  1.00 31.09           C  
ANISOU 1240  CA  CYS A 201     3337   4444   4031   -676    356   -425       C  
ATOM   1241  C   CYS A 201      38.731  12.566 124.059  1.00 29.65           C  
ANISOU 1241  C   CYS A 201     3053   4185   4025   -531    379   -516       C  
ATOM   1242  O   CYS A 201      37.815  11.915 123.572  1.00 27.25           O  
ANISOU 1242  O   CYS A 201     2789   4356   3208   -368    524   -513       O  
ATOM   1243  CB  CYS A 201      39.975  12.035 126.165  1.00 35.04           C  
ANISOU 1243  CB  CYS A 201     3475   5034   4805   -500    116   -460       C  
ATOM   1244  SG  CYS A 201      40.180  10.379 125.470  1.00 40.56           S  
ANISOU 1244  SG  CYS A 201     4629   5084   5695     71    480   -400       S  
ATOM   1245  N   ASP A 202      39.741  13.078 123.354  1.00 29.87           N  
ANISOU 1245  N   ASP A 202     3076   4175   4097   -534    448   -548       N  
ATOM   1246  CA  ASP A 202      39.876  12.987 121.897  1.00 30.79           C  
ANISOU 1246  CA  ASP A 202     3054   4605   4037   -384    479   -507       C  
ATOM   1247  C   ASP A 202      38.685  13.640 121.163  1.00 28.44           C  
ANISOU 1247  C   ASP A 202     2925   4295   3586   -404    757   -559       C  
ATOM   1248  O   ASP A 202      38.493  14.849 121.292  1.00 29.15           O  
ANISOU 1248  O   ASP A 202     3139   4354   3584   -357    936   -562       O  
ATOM   1249  CB  ASP A 202      40.144  11.538 121.445  1.00 33.29           C  
ANISOU 1249  CB  ASP A 202     3428   4792   4426   -176    240   -746       C  
ATOM   1250  CG  ASP A 202      41.432  10.956 122.018  1.00 37.03           C  
ANISOU 1250  CG  ASP A 202     3410   5465   5195     -2    235   -672       C  
ATOM   1251  OD1 ASP A 202      42.101  11.621 122.848  1.00 37.93           O  
ANISOU 1251  OD1 ASP A 202     3728   6100   4584      0    190   -587       O  
ATOM   1252  OD2 ASP A 202      41.776   9.816 121.616  1.00 41.01           O  
ANISOU 1252  OD2 ASP A 202     3651   5511   6416    320    760   -506       O  
ATOM   1253  N   VAL A 203      37.922  12.870 120.380  1.00 27.76           N  
ANISOU 1253  N   VAL A 203     2915   4096   3537   -266    616   -434       N  
ATOM   1254  CA  VAL A 203      36.690  13.350 119.760  1.00 27.17           C  
ANISOU 1254  CA  VAL A 203     2924   3939   3460   -172    707   -526       C  
ATOM   1255  C   VAL A 203      35.536  12.870 120.629  1.00 26.16           C  
ANISOU 1255  C   VAL A 203     2879   3524   3537   -359    498   -415       C  
ATOM   1256  O   VAL A 203      35.366  11.682 120.844  1.00 24.88           O  
ANISOU 1256  O   VAL A 203     2368   3325   3759   -269    483   -841       O  
ATOM   1257  CB  VAL A 203      36.500  12.842 118.309  1.00 28.50           C  
ANISOU 1257  CB  VAL A 203     3064   4232   3532    -94    555   -593       C  
ATOM   1258  CG1 VAL A 203      35.265  13.474 117.669  1.00 27.54           C  
ANISOU 1258  CG1 VAL A 203     3063   4039   3361    -75    693   -518       C  
ATOM   1259  CG2 VAL A 203      37.740  13.136 117.450  1.00 30.31           C  
ANISOU 1259  CG2 VAL A 203     3193   4788   3535      7    748   -689       C  
ATOM   1260  N   VAL A 204      34.775  13.822 121.158  1.00 26.46           N  
ANISOU 1260  N   VAL A 204     3017   3557   3479   -468    651   -442       N  
ATOM   1261  CA  VAL A 204      33.546  13.541 121.883  1.00 25.45           C  
ANISOU 1261  CA  VAL A 204     2850   3378   3442   -384    471   -344       C  
ATOM   1262  C   VAL A 204      32.440  13.783 120.876  1.00 24.47           C  
ANISOU 1262  C   VAL A 204     2934   3203   3160   -500    487   -344       C  
ATOM   1263  O   VAL A 204      32.497  14.769 120.123  1.00 24.49           O  
ANISOU 1263  O   VAL A 204     3052   3242   3011   -514    737   -352       O  
ATOM   1264  CB  VAL A 204      33.355  14.487 123.078  1.00 25.87           C  
ANISOU 1264  CB  VAL A 204     3066   3513   3249   -661    495   -332       C  
ATOM   1265  CG1 VAL A 204      32.181  14.023 123.922  1.00 26.67           C  
ANISOU 1265  CG1 VAL A 204     3103   3570   3457   -583    530   -268       C  
ATOM   1266  CG2 VAL A 204      34.607  14.519 123.917  1.00 27.06           C  
ANISOU 1266  CG2 VAL A 204     3049   3742   3488   -672    502   -301       C  
ATOM   1267  N   HIS A 205      31.444  12.907 120.871  1.00 23.25           N  
ANISOU 1267  N   HIS A 205     2905   2794   3135   -382    351   -251       N  
ATOM   1268  CA  HIS A 205      30.307  13.028 119.950  1.00 23.51           C  
ANISOU 1268  CA  HIS A 205     2892   2948   3091   -371    410   -298       C  
ATOM   1269  C   HIS A 205      29.032  13.411 120.692  1.00 21.37           C  
ANISOU 1269  C   HIS A 205     2690   2560   2867   -529    315   -155       C  
ATOM   1270  O   HIS A 205      28.839  13.002 121.830  1.00 20.44           O  
ANISOU 1270  O   HIS A 205     2267   2584   2912   -361    289     -7       O  
ATOM   1271  CB  HIS A 205      30.098  11.716 119.211  1.00 25.39           C  
ANISOU 1271  CB  HIS A 205     3267   3094   3284   -258     76   -465       C  
ATOM   1272  CG  HIS A 205      31.339  11.194 118.565  1.00 28.55           C  
ANISOU 1272  CG  HIS A 205     3400   3717   3731   -159    198   -604       C  
ATOM   1273  ND1 HIS A 205      32.262  10.424 119.244  1.00 30.23           N  
ANISOU 1273  ND1 HIS A 205     3586   3783   4116   -116    129   -567       N  
ATOM   1274  CD2 HIS A 205      31.817  11.335 117.308  1.00 30.01           C  
ANISOU 1274  CD2 HIS A 205     3540   4101   3759    -52    272   -677       C  
ATOM   1275  CE1 HIS A 205      33.251  10.105 118.431  1.00 30.76           C  
ANISOU 1275  CE1 HIS A 205     3659   3862   4167      1    164   -751       C  
ATOM   1276  NE2 HIS A 205      33.004  10.643 117.250  1.00 32.19           N  
ANISOU 1276  NE2 HIS A 205     3752   4400   4076    197    153   -822       N  
ATOM   1277  N   VAL A 206      28.182  14.207 120.048  1.00 21.33           N  
ANISOU 1277  N   VAL A 206     2659   2646   2799   -495    393   -113       N  
ATOM   1278  CA  VAL A 206      26.856  14.552 120.589  1.00 21.41           C  
ANISOU 1278  CA  VAL A 206     2692   2694   2746   -484    417   -102       C  
ATOM   1279  C   VAL A 206      25.794  14.365 119.513  1.00 22.21           C  
ANISOU 1279  C   VAL A 206     2760   2840   2836   -396    338    -65       C  
ATOM   1280  O   VAL A 206      25.903  14.935 118.427  1.00 22.04           O  
ANISOU 1280  O   VAL A 206     2605   3094   2676   -422    279   -106       O  
ATOM   1281  CB  VAL A 206      26.781  15.982 121.183  1.00 21.58           C  
ANISOU 1281  CB  VAL A 206     2705   2664   2827   -509    541    -95       C  
ATOM   1282  CG1 VAL A 206      27.154  17.057 120.166  1.00 22.86           C  
ANISOU 1282  CG1 VAL A 206     2890   2837   2957   -463    667     -2       C  
ATOM   1283  CG2 VAL A 206      25.401  16.264 121.774  1.00 21.48           C  
ANISOU 1283  CG2 VAL A 206     2650   2666   2845   -599    511    -65       C  
ATOM   1284  N   MET A 207      24.780  13.557 119.822  1.00 22.31           N  
ANISOU 1284  N   MET A 207     2816   2768   2889   -410    364    -53       N  
ATOM   1285  CA  MET A 207      23.621  13.426 118.966  1.00 23.81           C  
ANISOU 1285  CA  MET A 207     2905   3026   3114   -399    220     56       C  
ATOM   1286  C   MET A 207      22.590  14.530 119.301  1.00 24.38           C  
ANISOU 1286  C   MET A 207     3067   3086   3110   -321    318    125       C  
ATOM   1287  O   MET A 207      22.272  14.777 120.482  1.00 23.93           O  
ANISOU 1287  O   MET A 207     3013   2933   3147   -447    345     79       O  
ATOM   1288  CB  MET A 207      23.034  12.040 119.132  1.00 25.43           C  
ANISOU 1288  CB  MET A 207     3190   3034   3437   -469      4    110       C  
ATOM   1289  CG  MET A 207      22.072  11.643 118.035  1.00 27.85           C  
ANISOU 1289  CG  MET A 207     3478   3447   3657   -426   -248    157       C  
ATOM   1290  SD  MET A 207      21.483   9.943 118.206  1.00 31.18           S  
ANISOU 1290  SD  MET A 207     4171   3319   4357   -392   -821     80       S  
ATOM   1291  CE  MET A 207      22.980   9.030 117.836  1.00 30.51           C  
ANISOU 1291  CE  MET A 207     3797   3512   4280   -544   -724     68       C  
ATOM   1292  N   LEU A 208      22.087  15.190 118.254  1.00 23.77           N  
ANISOU 1292  N   LEU A 208     3002   2977   3052   -305    429    150       N  
ATOM   1293  CA  LEU A 208      21.081  16.248 118.354  1.00 24.14           C  
ANISOU 1293  CA  LEU A 208     2947   3132   3092   -237    464     64       C  
ATOM   1294  C   LEU A 208      19.930  15.995 117.380  1.00 25.47           C  
ANISOU 1294  C   LEU A 208     3057   3324   3295   -180    293    159       C  
ATOM   1295  O   LEU A 208      20.123  15.387 116.311  1.00 25.37           O  
ANISOU 1295  O   LEU A 208     2788   3783   3065   -159      0    126       O  
ATOM   1296  CB  LEU A 208      21.691  17.602 118.027  1.00 24.35           C  
ANISOU 1296  CB  LEU A 208     3056   3037   3157   -107    591     90       C  
ATOM   1297  CG  LEU A 208      22.936  18.054 118.777  1.00 25.02           C  
ANISOU 1297  CG  LEU A 208     3140   3067   3298   -229    624    -15       C  
ATOM   1298  CD1 LEU A 208      23.446  19.340 118.150  1.00 25.82           C  
ANISOU 1298  CD1 LEU A 208     3259   3065   3485   -185    708     14       C  
ATOM   1299  CD2 LEU A 208      22.627  18.258 120.247  1.00 25.97           C  
ANISOU 1299  CD2 LEU A 208     3210   3316   3338   -280    612    -40       C  
ATOM   1300  N   ASP A 209      18.744  16.485 117.753  1.00 25.52           N  
ANISOU 1300  N   ASP A 209     3052   3272   3370   -198    368    290       N  
ATOM   1301  CA  ASP A 209      17.505  16.255 117.008  1.00 27.75           C  
ANISOU 1301  CA  ASP A 209     3166   3708   3667   -186    165    296       C  
ATOM   1302  C   ASP A 209      17.262  17.391 116.018  1.00 27.50           C  
ANISOU 1302  C   ASP A 209     2943   3774   3729    -76     57    308       C  
ATOM   1303  O   ASP A 209      16.865  18.485 116.411  1.00 28.74           O  
ANISOU 1303  O   ASP A 209     3211   3670   4038     19      2    508       O  
ATOM   1304  CB  ASP A 209      16.332  16.130 117.994  1.00 29.62           C  
ANISOU 1304  CB  ASP A 209     3223   4131   3899   -165    263    323       C  
ATOM   1305  CG  ASP A 209      15.018  15.738 117.327  1.00 31.86           C  
ANISOU 1305  CG  ASP A 209     3372   4426   4307   -244     47    446       C  
ATOM   1306  OD1 ASP A 209      14.882  15.823 116.089  1.00 34.26           O  
ANISOU 1306  OD1 ASP A 209     4007   4599   4410   -496   -256    482       O  
ATOM   1307  OD2 ASP A 209      14.096  15.350 118.066  1.00 34.28           O  
ANISOU 1307  OD2 ASP A 209     3418   4868   4739    -94    323    500       O  
ATOM   1308  N   GLY A 210      17.487  17.105 114.740  1.00 27.07           N  
ANISOU 1308  N   GLY A 210     2860   3719   3703     -3    -70    239       N  
ATOM   1309  CA  GLY A 210      17.242  18.044 113.651  1.00 30.04           C  
ANISOU 1309  CA  GLY A 210     3629   3879   3904     68    199    452       C  
ATOM   1310  C   GLY A 210      15.805  18.502 113.401  1.00 32.55           C  
ANISOU 1310  C   GLY A 210     3827   4298   4241    266    -36    586       C  
ATOM   1311  O   GLY A 210      15.613  19.492 112.705  1.00 33.65           O  
ANISOU 1311  O   GLY A 210     4296   4448   4042    358   -300    596       O  
ATOM   1312  N   SER A 211      14.809  17.790 113.951  1.00 34.48           N  
ANISOU 1312  N   SER A 211     3842   4720   4536    118     80    540       N  
ATOM   1313  CA  SER A 211      13.380  18.156 113.821  1.00 35.44           C  
ANISOU 1313  CA  SER A 211     3913   4843   4709    243     -4    676       C  
ATOM   1314  C   SER A 211      12.864  19.168 114.858  1.00 37.53           C  
ANISOU 1314  C   SER A 211     4174   5037   5049    421    179    582       C  
ATOM   1315  O   SER A 211      11.722  19.605 114.761  1.00 39.43           O  
ANISOU 1315  O   SER A 211     4181   5306   5492    496    314    517       O  
ATOM   1316  CB  SER A 211      12.510  16.901 113.938  1.00 35.62           C  
ANISOU 1316  CB  SER A 211     3831   5046   4656    103   -129    681       C  
ATOM   1317  OG  SER A 211      12.435  16.470 115.296  1.00 32.40           O  
ANISOU 1317  OG  SER A 211     3319   4344   4645   -169    104    543       O  
ATOM   1318  N   ARG A 212      13.675  19.510 115.857  1.00 39.05           N  
ANISOU 1318  N   ARG A 212     4476   5190   5168    353     90    417       N  
ATOM   1319  CA  ARG A 212      13.266  20.455 116.909  1.00 40.99           C  
ANISOU 1319  CA  ARG A 212     4589   5534   5448    481    469    339       C  
ATOM   1320  C   ARG A 212      13.376  21.889 116.395  1.00 41.59           C  
ANISOU 1320  C   ARG A 212     4774   5504   5523    879    397    456       C  
ATOM   1321  O   ARG A 212      14.128  22.158 115.456  1.00 40.97           O  
ANISOU 1321  O   ARG A 212     4629   5235   5702    849    464    553       O  
ATOM   1322  CB  ARG A 212      14.180  20.323 118.135  1.00 41.16           C  
ANISOU 1322  CB  ARG A 212     4575   5698   5364    498    587    367       C  
ATOM   1323  CG  ARG A 212      14.225  18.949 118.759  1.00 41.57           C  
ANISOU 1323  CG  ARG A 212     4617   5683   5495    333    526    303       C  
ATOM   1324  CD  ARG A 212      13.009  18.699 119.613  1.00 45.25           C  
ANISOU 1324  CD  ARG A 212     4866   6407   5917    189    705    383       C  
ATOM   1325  NE  ARG A 212      13.060  17.400 120.284  1.00 47.87           N  
ANISOU 1325  NE  ARG A 212     5507   6879   5800    132    666    797       N  
ATOM   1326  CZ  ARG A 212      12.267  17.038 121.295  1.00 46.96           C  
ANISOU 1326  CZ  ARG A 212     4609   7252   5980     42    528    781       C  
ATOM   1327  NH1 ARG A 212      11.358  17.875 121.793  1.00 47.01           N  
ANISOU 1327  NH1 ARG A 212     4695   7458   5707    -18    662    524       N  
ATOM   1328  NH2 ARG A 212      12.395  15.826 121.823  1.00 47.33           N  
ANISOU 1328  NH2 ARG A 212     4705   7241   6037   -290    520    850       N  
ATOM   1329  N   SER A 213      12.650  22.801 117.035  1.00 43.18           N  
ANISOU 1329  N   SER A 213     4805   5851   5749    988    575    364       N  
ATOM   1330  CA  SER A 213      12.748  24.239 116.745  1.00 45.91           C  
ANISOU 1330  CA  SER A 213     5178   5829   6437   1062    464    287       C  
ATOM   1331  C   SER A 213      14.095  24.843 117.165  1.00 44.55           C  
ANISOU 1331  C   SER A 213     5313   5351   6262    983    603    220       C  
ATOM   1332  O   SER A 213      14.543  25.809 116.555  1.00 46.10           O  
ANISOU 1332  O   SER A 213     5879   5275   6361   1072   1044    192       O  
ATOM   1333  CB  SER A 213      11.598  25.003 117.417  1.00 50.28           C  
ANISOU 1333  CB  SER A 213     5616   6474   7011   1387    592     47       C  
ATOM   1334  OG  SER A 213      11.310  24.454 118.691  1.00 54.10           O  
ANISOU 1334  OG  SER A 213     5988   7728   6836   1496   1762   -489       O  
ATOM   1335  N   LYS A 214      14.701  24.300 118.225  1.00 42.78           N  
ANISOU 1335  N   LYS A 214     4922   5213   6118    962    569    -22       N  
ATOM   1336  CA  LYS A 214      16.098  24.570 118.580  1.00 40.83           C  
ANISOU 1336  CA  LYS A 214     4830   4768   5916    852    790    -87       C  
ATOM   1337  C   LYS A 214      16.834  23.235 118.557  1.00 37.63           C  
ANISOU 1337  C   LYS A 214     4559   4481   5258    494    777     64       C  
ATOM   1338  O   LYS A 214      16.639  22.410 119.447  1.00 36.21           O  
ANISOU 1338  O   LYS A 214     4249   4628   4881    798    625     37       O  
ATOM   1339  CB  LYS A 214      16.224  25.178 119.981  1.00 42.05           C  
ANISOU 1339  CB  LYS A 214     4922   4974   6078    835    728   -305       C  
ATOM   1340  CG  LYS A 214      15.611  26.554 120.155  1.00 46.21           C  
ANISOU 1340  CG  LYS A 214     5530   5179   6846   1055    657   -465       C  
ATOM   1341  CD  LYS A 214      16.029  27.140 121.500  1.00 48.32           C  
ANISOU 1341  CD  LYS A 214     5796   5499   7062   1068    627   -760       C  
ATOM   1342  CE  LYS A 214      15.326  28.448 121.809  1.00 52.26           C  
ANISOU 1342  CE  LYS A 214     6172   5883   7801   1497    635   -935       C  
ATOM   1343  NZ  LYS A 214      13.881  28.257 122.102  1.00 54.22           N  
ANISOU 1343  NZ  LYS A 214     6132   6476   7991   1559    498   -929       N  
ATOM   1344  N   ILE A 215      17.671  23.021 117.541  1.00 36.35           N  
ANISOU 1344  N   ILE A 215     4333   4168   5310    477    751    166       N  
ATOM   1345  CA  ILE A 215      18.414  21.768 117.415  1.00 33.07           C  
ANISOU 1345  CA  ILE A 215     4102   3876   4586    211    586    193       C  
ATOM   1346  C   ILE A 215      19.335  21.626 118.629  1.00 32.85           C  
ANISOU 1346  C   ILE A 215     4020   3953   4506    107    614     49       C  
ATOM   1347  O   ILE A 215      19.339  20.590 119.286  1.00 30.60           O  
ANISOU 1347  O   ILE A 215     3475   4104   4048    177     92    -47       O  
ATOM   1348  CB  ILE A 215      19.202  21.681 116.083  1.00 32.91           C  
ANISOU 1348  CB  ILE A 215     4165   3784   4552    192    579    250       C  
ATOM   1349  CG1 ILE A 215      18.219  21.687 114.893  1.00 34.47           C  
ANISOU 1349  CG1 ILE A 215     4295   4131   4669    337    483    533       C  
ATOM   1350  CG2 ILE A 215      20.060  20.416 116.058  1.00 30.92           C  
ANISOU 1350  CG2 ILE A 215     3849   3758   4141     83    589    368       C  
ATOM   1351  CD1 ILE A 215      18.829  21.968 113.529  1.00 34.92           C  
ANISOU 1351  CD1 ILE A 215     4367   4166   4733    358    504    713       C  
ATOM   1352  N   PHE A 216      20.092  22.682 118.917  1.00 33.74           N  
ANISOU 1352  N   PHE A 216     4361   3863   4592     91    693     -3       N  
ATOM   1353  CA  PHE A 216      20.853  22.811 120.167  1.00 32.86           C  
ANISOU 1353  CA  PHE A 216     4105   3754   4624     52    801   -182       C  
ATOM   1354  C   PHE A 216      20.113  23.793 121.073  1.00 35.59           C  
ANISOU 1354  C   PHE A 216     4427   3980   5114    301    829   -394       C  
ATOM   1355  O   PHE A 216      19.718  24.870 120.628  1.00 37.03           O  
ANISOU 1355  O   PHE A 216     4270   4069   5730    619    869   -459       O  
ATOM   1356  CB  PHE A 216      22.278  23.307 119.903  1.00 31.75           C  
ANISOU 1356  CB  PHE A 216     4098   3379   4586     78    836   -271       C  
ATOM   1357  CG  PHE A 216      23.011  23.777 121.143  1.00 31.48           C  
ANISOU 1357  CG  PHE A 216     4053   3303   4603     78    870   -341       C  
ATOM   1358  CD1 PHE A 216      23.465  22.869 122.083  1.00 30.08           C  
ANISOU 1358  CD1 PHE A 216     3859   3342   4226   -198    896   -394       C  
ATOM   1359  CD2 PHE A 216      23.257  25.137 121.357  1.00 33.57           C  
ANISOU 1359  CD2 PHE A 216     4342   3372   5040    -73    721   -469       C  
ATOM   1360  CE1 PHE A 216      24.131  23.295 123.222  1.00 30.56           C  
ANISOU 1360  CE1 PHE A 216     3685   3396   4529   -204    789   -590       C  
ATOM   1361  CE2 PHE A 216      23.934  25.564 122.487  1.00 33.36           C  
ANISOU 1361  CE2 PHE A 216     4361   3233   5081     22    826   -728       C  
ATOM   1362  CZ  PHE A 216      24.370  24.644 123.419  1.00 32.43           C  
ANISOU 1362  CZ  PHE A 216     4134   3398   4789    -42    755   -837       C  
ATOM   1363  N   ASP A 217      19.943  23.410 122.336  1.00 37.07           N  
ANISOU 1363  N   ASP A 217     4618   4348   5116     72    998   -363       N  
ATOM   1364  CA  ASP A 217      19.286  24.237 123.338  1.00 40.84           C  
ANISOU 1364  CA  ASP A 217     4962   4936   5619    560    904   -748       C  
ATOM   1365  C   ASP A 217      20.253  24.454 124.497  1.00 41.38           C  
ANISOU 1365  C   ASP A 217     4840   5259   5621    418   1057  -1083       C  
ATOM   1366  O   ASP A 217      20.684  23.497 125.157  1.00 35.83           O  
ANISOU 1366  O   ASP A 217     3665   5198   4750     25   1021  -1410       O  
ATOM   1367  CB  ASP A 217      18.014  23.549 123.826  1.00 43.55           C  
ANISOU 1367  CB  ASP A 217     4915   5781   5851    524    955   -659       C  
ATOM   1368  CG  ASP A 217      17.320  24.319 124.924  1.00 51.11           C  
ANISOU 1368  CG  ASP A 217     6254   6589   6577    994   1373  -1092       C  
ATOM   1369  OD1 ASP A 217      17.171  25.556 124.793  1.00 57.84           O  
ANISOU 1369  OD1 ASP A 217     7181   6730   8063    840   1351   -238       O  
ATOM   1370  OD2 ASP A 217      16.936  23.687 125.931  1.00 56.65           O  
ANISOU 1370  OD2 ASP A 217     7467   7112   6945    910   1834   -866       O  
ATOM   1371  N   LYS A 218      20.590  25.720 124.728  1.00 44.34           N  
ANISOU 1371  N   LYS A 218     5280   5234   6330    727    993  -1290       N  
ATOM   1372  CA  LYS A 218      21.456  26.134 125.837  1.00 47.45           C  
ANISOU 1372  CA  LYS A 218     5682   5698   6646    561    736  -1466       C  
ATOM   1373  C   LYS A 218      20.935  25.711 127.226  1.00 49.01           C  
ANISOU 1373  C   LYS A 218     5736   6477   6409    670    887  -1881       C  
ATOM   1374  O   LYS A 218      21.729  25.432 128.129  1.00 50.76           O  
ANISOU 1374  O   LYS A 218     5880   7206   6199    600    850  -2059       O  
ATOM   1375  CB  LYS A 218      21.636  27.646 125.800  1.00 52.03           C  
ANISOU 1375  CB  LYS A 218     6532   5643   7594    568    650  -1578       C  
ATOM   1376  CG  LYS A 218      22.771  28.152 126.665  1.00 55.63           C  
ANISOU 1376  CG  LYS A 218     6947   6173   8014    548    372  -1823       C  
ATOM   1377  CD  LYS A 218      22.685  29.654 126.896  1.00 60.60           C  
ANISOU 1377  CD  LYS A 218     7735   6253   9037    690    508  -2216       C  
ATOM   1378  CE  LYS A 218      23.755  30.089 127.887  1.00 64.13           C  
ANISOU 1378  CE  LYS A 218     8081   6765   9519    587    204  -2299       C  
ATOM   1379  NZ  LYS A 218      25.138  29.857 127.356  1.00 63.84           N  
ANISOU 1379  NZ  LYS A 218     8143   6580   9531    300    318  -1885       N  
ATOM   1380  N   ASP A 219      19.615  25.641 127.388  1.00 49.82           N  
ANISOU 1380  N   ASP A 219     5710   6873   6345   1049   1064  -1944       N  
ATOM   1381  CA  ASP A 219      19.015  25.328 128.688  1.00 51.42           C  
ANISOU 1381  CA  ASP A 219     5745   7373   6417    843    925  -1617       C  
ATOM   1382  C   ASP A 219      18.909  23.833 129.035  1.00 48.97           C  
ANISOU 1382  C   ASP A 219     5313   7355   5937    495   1112  -1861       C  
ATOM   1383  O   ASP A 219      18.373  23.493 130.098  1.00 56.30           O  
ANISOU 1383  O   ASP A 219     5671   9339   6380   -113   1046  -1110       O  
ATOM   1384  CB  ASP A 219      17.648  26.006 128.799  1.00 54.37           C  
ANISOU 1384  CB  ASP A 219     5920   7929   6807   1128    976  -1954       C  
ATOM   1385  CG  ASP A 219      17.731  27.506 128.565  1.00 57.04           C  
ANISOU 1385  CG  ASP A 219     6494   7792   7385   1307    772  -2356       C  
ATOM   1386  OD1 ASP A 219      18.353  28.212 129.382  1.00 63.99           O  
ANISOU 1386  OD1 ASP A 219     7906   8535   7871   1131    518  -2616       O  
ATOM   1387  OD2 ASP A 219      17.193  27.984 127.551  1.00 59.72           O  
ANISOU 1387  OD2 ASP A 219     6513   8430   7745   1619    881  -2078       O  
ATOM   1388  N   SER A 220      19.437  22.949 128.189  1.00 41.99           N  
ANISOU 1388  N   SER A 220     4260   6571   5121    140   1080  -1278       N  
ATOM   1389  CA  SER A 220      19.433  21.506 128.454  1.00 41.07           C  
ANISOU 1389  CA  SER A 220     4240   6660   4705    193   1078   -986       C  
ATOM   1390  C   SER A 220      20.648  21.076 129.275  1.00 40.09           C  
ANISOU 1390  C   SER A 220     4422   6490   4320   -181    883   -945       C  
ATOM   1391  O   SER A 220      21.582  21.851 129.449  1.00 41.77           O  
ANISOU 1391  O   SER A 220     4822   6388   4658   -366    788   -786       O  
ATOM   1392  CB  SER A 220      19.443  20.736 127.126  1.00 39.47           C  
ANISOU 1392  CB  SER A 220     4271   6212   4513   -270    874   -698       C  
ATOM   1393  OG  SER A 220      20.636  20.994 126.372  1.00 38.27           O  
ANISOU 1393  OG  SER A 220     3936   6483   4122     -9    723  -1235       O  
ATOM   1394  N   THR A 221      20.645  19.824 129.739  1.00 38.55           N  
ANISOU 1394  N   THR A 221     3836   6640   4170   -312    930   -751       N  
ATOM   1395  CA  THR A 221      21.787  19.232 130.453  1.00 37.81           C  
ANISOU 1395  CA  THR A 221     3782   6543   4040   -398   1034   -668       C  
ATOM   1396  C   THR A 221      23.058  19.331 129.613  1.00 35.43           C  
ANISOU 1396  C   THR A 221     3668   6060   3733   -685    786   -783       C  
ATOM   1397  O   THR A 221      24.123  19.683 130.120  1.00 33.86           O  
ANISOU 1397  O   THR A 221     3719   5509   3636  -1025    978  -1052       O  
ATOM   1398  CB  THR A 221      21.568  17.737 130.785  1.00 38.47           C  
ANISOU 1398  CB  THR A 221     3742   6791   4081   -734    906   -322       C  
ATOM   1399  OG1 THR A 221      20.297  17.566 131.422  1.00 43.96           O  
ANISOU 1399  OG1 THR A 221     3848   7891   4964   -579   1200   -133       O  
ATOM   1400  CG2 THR A 221      22.669  17.200 131.726  1.00 38.01           C  
ANISOU 1400  CG2 THR A 221     3749   6806   3887   -865    953   -233       C  
ATOM   1401  N   PHE A 222      22.930  18.996 128.330  1.00 33.23           N  
ANISOU 1401  N   PHE A 222     3547   5399   3679   -594    972   -734       N  
ATOM   1402  CA  PHE A 222      24.030  19.124 127.406  1.00 29.79           C  
ANISOU 1402  CA  PHE A 222     3342   4469   3506   -469    843   -678       C  
ATOM   1403  C   PHE A 222      24.531  20.571 127.310  1.00 30.18           C  
ANISOU 1403  C   PHE A 222     3487   4353   3624   -402    821   -999       C  
ATOM   1404  O   PHE A 222      25.727  20.821 127.417  1.00 28.64           O  
ANISOU 1404  O   PHE A 222     3483   4101   3298   -667   1211  -1077       O  
ATOM   1405  CB  PHE A 222      23.681  18.606 126.006  1.00 26.82           C  
ANISOU 1405  CB  PHE A 222     2899   3915   3376   -518    774   -375       C  
ATOM   1406  CG  PHE A 222      24.783  18.848 125.019  1.00 25.51           C  
ANISOU 1406  CG  PHE A 222     3081   3444   3168   -447    723   -356       C  
ATOM   1407  CD1 PHE A 222      25.999  18.177 125.145  1.00 24.96           C  
ANISOU 1407  CD1 PHE A 222     2951   3418   3111   -567    807   -311       C  
ATOM   1408  CD2 PHE A 222      24.651  19.797 124.023  1.00 25.66           C  
ANISOU 1408  CD2 PHE A 222     3133   3256   3358   -394    772   -320       C  
ATOM   1409  CE1 PHE A 222      27.039  18.424 124.276  1.00 23.87           C  
ANISOU 1409  CE1 PHE A 222     2981   3070   3017   -575    805   -381       C  
ATOM   1410  CE2 PHE A 222      25.684  20.041 123.147  1.00 24.78           C  
ANISOU 1410  CE2 PHE A 222     3109   2963   3343   -375    777   -395       C  
ATOM   1411  CZ  PHE A 222      26.878  19.360 123.271  1.00 24.46           C  
ANISOU 1411  CZ  PHE A 222     3114   2898   3280   -426    704   -353       C  
ATOM   1412  N   GLY A 223      23.599  21.500 127.114  1.00 32.12           N  
ANISOU 1412  N   GLY A 223     3814   4477   3912   -160    803  -1090       N  
ATOM   1413  CA  GLY A 223      23.920  22.889 126.827  1.00 34.62           C  
ANISOU 1413  CA  GLY A 223     4181   4489   4484   -243    930  -1051       C  
ATOM   1414  C   GLY A 223      24.343  23.761 127.995  1.00 37.86           C  
ANISOU 1414  C   GLY A 223     4719   4905   4758   -120   1005  -1508       C  
ATOM   1415  O   GLY A 223      24.904  24.836 127.780  1.00 42.26           O  
ANISOU 1415  O   GLY A 223     5405   4769   5882   -248   1271  -1930       O  
ATOM   1416  N   SER A 224      24.051  23.324 129.218  1.00 37.14           N  
ANISOU 1416  N   SER A 224     4120   5293   4696     -9   1063  -1584       N  
ATOM   1417  CA  SER A 224      24.391  24.067 130.424  1.00 40.08           C  
ANISOU 1417  CA  SER A 224     4542   5799   4886     28    880  -1848       C  
ATOM   1418  C   SER A 224      25.366  23.360 131.351  1.00 39.33           C  
ANISOU 1418  C   SER A 224     4469   5894   4580   -180    898  -1841       C  
ATOM   1419  O   SER A 224      25.874  23.999 132.243  1.00 43.62           O  
ANISOU 1419  O   SER A 224     4512   7073   4989   -515    380  -1893       O  
ATOM   1420  CB  SER A 224      23.125  24.342 131.233  1.00 43.55           C  
ANISOU 1420  CB  SER A 224     4783   6623   5140    143   1040  -1974       C  
ATOM   1421  OG  SER A 224      22.786  23.197 131.997  1.00 43.04           O  
ANISOU 1421  OG  SER A 224     3932   7336   5085     -5   1432  -1664       O  
ATOM   1422  N   VAL A 225      25.585  22.057 131.199  1.00 37.38           N  
ANISOU 1422  N   VAL A 225     4241   5741   4218   -383    729  -1507       N  
ATOM   1423  CA  VAL A 225      26.476  21.315 132.091  1.00 36.76           C  
ANISOU 1423  CA  VAL A 225     4101   5899   3967   -455    830  -1495       C  
ATOM   1424  C   VAL A 225      27.585  20.619 131.307  1.00 33.99           C  
ANISOU 1424  C   VAL A 225     3852   5454   3609   -761    873  -1239       C  
ATOM   1425  O   VAL A 225      28.752  20.921 131.520  1.00 35.62           O  
ANISOU 1425  O   VAL A 225     3929   6024   3578   -951    883  -1299       O  
ATOM   1426  CB  VAL A 225      25.704  20.319 132.995  1.00 37.20           C  
ANISOU 1426  CB  VAL A 225     3919   6506   3708   -463    871  -1333       C  
ATOM   1427  CG1 VAL A 225      26.654  19.362 133.713  1.00 37.22           C  
ANISOU 1427  CG1 VAL A 225     3941   6612   3587   -605    848  -1118       C  
ATOM   1428  CG2 VAL A 225      24.872  21.082 134.017  1.00 40.34           C  
ANISOU 1428  CG2 VAL A 225     4098   7230   3998   -274    965  -1605       C  
ATOM   1429  N   GLU A 226      27.231  19.694 130.422  1.00 27.69           N  
ANISOU 1429  N   GLU A 226     3009   4040   3469   -889    472   -281       N  
ATOM   1430  CA  GLU A 226      28.230  18.849 129.780  1.00 29.04           C  
ANISOU 1430  CA  GLU A 226     3090   4046   3895   -780    384   -396       C  
ATOM   1431  C   GLU A 226      29.200  19.671 128.922  1.00 26.46           C  
ANISOU 1431  C   GLU A 226     2883   3694   3474   -735     64   -506       C  
ATOM   1432  O   GLU A 226      30.420  19.433 128.949  1.00 25.76           O  
ANISOU 1432  O   GLU A 226     2845   3474   3467   -935     51   -455       O  
ATOM   1433  CB  GLU A 226      27.562  17.708 128.987  1.00 33.93           C  
ANISOU 1433  CB  GLU A 226     3592   4383   4914  -1093    593   -908       C  
ATOM   1434  CG  GLU A 226      26.930  16.665 129.914  1.00 39.37           C  
ANISOU 1434  CG  GLU A 226     4297   4721   5938  -1260   1179   -661       C  
ATOM   1435  CD  GLU A 226      25.998  15.682 129.228  1.00 46.96           C  
ANISOU 1435  CD  GLU A 226     4802   5543   7497  -1812   1251  -1378       C  
ATOM   1436  OE1 GLU A 226      25.105  16.125 128.472  1.00 49.99           O  
ANISOU 1436  OE1 GLU A 226     4793   6615   7584  -2081    934  -1407       O  
ATOM   1437  OE2 GLU A 226      26.136  14.460 129.489  1.00 53.28           O  
ANISOU 1437  OE2 GLU A 226     6196   5226   8822  -1699   1925  -2004       O  
ATOM   1438  N   VAL A 227      28.669  20.678 128.237  1.00 24.65           N  
ANISOU 1438  N   VAL A 227     2516   3768   3079   -761    -64   -662       N  
ATOM   1439  CA  VAL A 227      29.452  21.476 127.301  1.00 24.79           C  
ANISOU 1439  CA  VAL A 227     2515   3782   3121   -656    -57   -628       C  
ATOM   1440  C   VAL A 227      30.519  22.319 128.034  1.00 23.28           C  
ANISOU 1440  C   VAL A 227     2590   3231   3023   -536     10   -624       C  
ATOM   1441  O   VAL A 227      31.601  22.567 127.494  1.00 24.29           O  
ANISOU 1441  O   VAL A 227     2724   3113   3391   -761    189   -961       O  
ATOM   1442  CB  VAL A 227      28.508  22.310 126.377  1.00 27.26           C  
ANISOU 1442  CB  VAL A 227     2823   4443   3091   -350      6   -468       C  
ATOM   1443  CG1 VAL A 227      28.188  23.695 126.937  1.00 28.39           C  
ANISOU 1443  CG1 VAL A 227     3200   4413   3170   -181   -106   -404       C  
ATOM   1444  CG2 VAL A 227      29.079  22.423 125.010  1.00 29.86           C  
ANISOU 1444  CG2 VAL A 227     3251   5014   3079   -113     67   -486       C  
ATOM   1445  N   HIS A 228      30.232  22.716 129.270  1.00 21.67           N  
ANISOU 1445  N   HIS A 228     2323   3079   2829   -577   -169   -495       N  
ATOM   1446  CA  HIS A 228      31.192  23.449 130.087  1.00 21.75           C  
ANISOU 1446  CA  HIS A 228     2365   2889   3010   -372   -294   -647       C  
ATOM   1447  C   HIS A 228      32.126  22.570 130.908  1.00 22.25           C  
ANISOU 1447  C   HIS A 228     2322   3047   3084   -288   -440   -795       C  
ATOM   1448  O   HIS A 228      32.995  23.087 131.611  1.00 22.97           O  
ANISOU 1448  O   HIS A 228     2282   3056   3387   -110   -586  -1005       O  
ATOM   1449  CB  HIS A 228      30.463  24.445 130.999  1.00 22.57           C  
ANISOU 1449  CB  HIS A 228     2340   3121   3114   -215   -370   -764       C  
ATOM   1450  CG  HIS A 228      29.820  25.560 130.247  1.00 23.71           C  
ANISOU 1450  CG  HIS A 228     2588   2982   3438   -164   -211   -646       C  
ATOM   1451  ND1 HIS A 228      30.548  26.595 129.705  1.00 25.79           N  
ANISOU 1451  ND1 HIS A 228     2790   2915   4091   -229     33   -712       N  
ATOM   1452  CD2 HIS A 228      28.525  25.792 129.917  1.00 23.95           C  
ANISOU 1452  CD2 HIS A 228     2659   3180   3258    -17   -200   -439       C  
ATOM   1453  CE1 HIS A 228      29.728  27.433 129.093  1.00 27.52           C  
ANISOU 1453  CE1 HIS A 228     3157   3032   4265    -21    267   -393       C  
ATOM   1454  NE2 HIS A 228      28.497  26.965 129.200  1.00 26.19           N  
ANISOU 1454  NE2 HIS A 228     2944   3333   3675    170     32   -218       N  
ATOM   1455  N   ASN A 229      31.953  21.251 130.824  1.00 21.52           N  
ANISOU 1455  N   ASN A 229     2380   3040   2757   -298   -323   -621       N  
ATOM   1456  CA  ASN A 229      32.750  20.324 131.608  1.00 22.94           C  
ANISOU 1456  CA  ASN A 229     2506   3216   2991    -45   -256   -547       C  
ATOM   1457  C   ASN A 229      33.646  19.395 130.815  1.00 23.26           C  
ANISOU 1457  C   ASN A 229     2371   3216   3249   -121     -7   -390       C  
ATOM   1458  O   ASN A 229      34.377  18.591 131.398  1.00 25.11           O  
ANISOU 1458  O   ASN A 229     2448   3519   3570    252    357   -126       O  
ATOM   1459  CB  ASN A 229      31.821  19.596 132.569  1.00 24.18           C  
ANISOU 1459  CB  ASN A 229     2766   3536   2884    261    -70   -262       C  
ATOM   1460  CG  ASN A 229      31.459  20.477 133.751  1.00 25.28           C  
ANISOU 1460  CG  ASN A 229     2746   4152   2705    568   -289   -353       C  
ATOM   1461  OD1 ASN A 229      32.272  20.685 134.644  1.00 28.73           O  
ANISOU 1461  OD1 ASN A 229     3101   5015   2797    743   -410  -1015       O  
ATOM   1462  ND2 ASN A 229      30.268  21.010 133.746  1.00 24.44           N  
ANISOU 1462  ND2 ASN A 229     2777   3954   2552    606   -318   -434       N  
ATOM   1463  N   LEU A 230      33.609  19.541 129.496  1.00 22.96           N  
ANISOU 1463  N   LEU A 230     2358   3126   3238   -470   -142   -547       N  
ATOM   1464  CA  LEU A 230      34.593  18.939 128.612  1.00 23.96           C  
ANISOU 1464  CA  LEU A 230     2522   3043   3538   -420     20   -611       C  
ATOM   1465  C   LEU A 230      35.895  19.673 128.889  1.00 25.40           C  
ANISOU 1465  C   LEU A 230     2574   3321   3755   -468    -57   -774       C  
ATOM   1466  O   LEU A 230      35.894  20.896 129.008  1.00 26.32           O  
ANISOU 1466  O   LEU A 230     2593   3284   4123   -493   -180   -515       O  
ATOM   1467  CB  LEU A 230      34.182  19.121 127.149  1.00 23.24           C  
ANISOU 1467  CB  LEU A 230     2358   2988   3482   -649    126   -637       C  
ATOM   1468  CG  LEU A 230      32.876  18.452 126.686  1.00 24.05           C  
ANISOU 1468  CG  LEU A 230     2528   3095   3513   -819    194   -781       C  
ATOM   1469  CD1 LEU A 230      32.566  18.797 125.234  1.00 24.79           C  
ANISOU 1469  CD1 LEU A 230     2456   3520   3441   -862    239   -836       C  
ATOM   1470  CD2 LEU A 230      32.873  16.944 126.887  1.00 25.85           C  
ANISOU 1470  CD2 LEU A 230     2790   3034   3996   -806    387   -861       C  
ATOM   1471  N   GLN A 231      36.991  18.941 129.042  1.00 27.47           N  
ANISOU 1471  N   GLN A 231     2817   3693   3926   -152   -145   -876       N  
ATOM   1472  CA  GLN A 231      38.269  19.562 129.382  1.00 31.42           C  
ANISOU 1472  CA  GLN A 231     2915   4312   4710   -261   -323  -1115       C  
ATOM   1473  C   GLN A 231      39.101  19.743 128.108  1.00 31.56           C  
ANISOU 1473  C   GLN A 231     2836   4244   4911   -512   -208  -1121       C  
ATOM   1474  O   GLN A 231      39.393  18.748 127.444  1.00 29.78           O  
ANISOU 1474  O   GLN A 231     2607   4004   4704   -859    130   -894       O  
ATOM   1475  CB  GLN A 231      39.024  18.714 130.411  1.00 36.45           C  
ANISOU 1475  CB  GLN A 231     3474   5294   5079    394   -499   -972       C  
ATOM   1476  CG  GLN A 231      38.116  18.158 131.494  1.00 38.90           C  
ANISOU 1476  CG  GLN A 231     3981   5773   5026    710   -331   -669       C  
ATOM   1477  CD  GLN A 231      38.847  17.711 132.736  1.00 46.19           C  
ANISOU 1477  CD  GLN A 231     5009   7356   5183   1531   -604   -723       C  
ATOM   1478  OE1 GLN A 231      39.422  16.619 132.768  1.00 50.80           O  
ANISOU 1478  OE1 GLN A 231     6035   7661   5606   2048   -349    -76       O  
ATOM   1479  NE2 GLN A 231      38.807  18.535 133.783  1.00 50.68           N  
ANISOU 1479  NE2 GLN A 231     5493   8152   5608   1638   -914  -1299       N  
ATOM   1480  N   PRO A 232      39.478  21.001 127.759  1.00 33.16           N  
ANISOU 1480  N   PRO A 232     2876   4209   5515   -761   -223  -1382       N  
ATOM   1481  CA  PRO A 232      40.327  21.320 126.582  1.00 35.63           C  
ANISOU 1481  CA  PRO A 232     3060   4350   6125  -1024    162  -1312       C  
ATOM   1482  C   PRO A 232      41.628  20.525 126.479  1.00 37.92           C  
ANISOU 1482  C   PRO A 232     2966   4746   6695  -1006    149  -1251       C  
ATOM   1483  O   PRO A 232      42.102  20.253 125.373  1.00 38.97           O  
ANISOU 1483  O   PRO A 232     3544   4642   6619  -1246     39  -1467       O  
ATOM   1484  CB  PRO A 232      40.643  22.801 126.764  1.00 39.07           C  
ANISOU 1484  CB  PRO A 232     3166   4410   7268  -1073    365  -1429       C  
ATOM   1485  CG  PRO A 232      39.502  23.322 127.555  1.00 38.58           C  
ANISOU 1485  CG  PRO A 232     3328   4320   7008   -983    282  -1477       C  
ATOM   1486  CD  PRO A 232      39.086  22.226 128.478  1.00 35.57           C  
ANISOU 1486  CD  PRO A 232     3070   4367   6075   -694    -59  -1590       C  
ATOM   1487  N   GLU A 233      42.209  20.165 127.615  1.00 41.17           N  
ANISOU 1487  N   GLU A 233     3298   5589   6753   -788    -74  -1454       N  
ATOM   1488  CA  GLU A 233      43.357  19.242 127.612  1.00 46.22           C  
ANISOU 1488  CA  GLU A 233     3658   6461   7439   -314   -194  -1731       C  
ATOM   1489  C   GLU A 233      42.930  17.966 126.866  1.00 44.08           C  
ANISOU 1489  C   GLU A 233     3946   5935   6868   -207    181  -1323       C  
ATOM   1490  O   GLU A 233      43.365  17.712 125.729  1.00 47.55           O  
ANISOU 1490  O   GLU A 233     4274   6654   7138   -193    520  -1084       O  
ATOM   1491  CB  GLU A 233      43.859  18.907 129.041  1.00 51.48           C  
ANISOU 1491  CB  GLU A 233     4112   7879   7567    175   -522  -1909       C  
ATOM   1492  CG  GLU A 233      43.970  20.080 130.019  1.00 57.33           C  
ANISOU 1492  CG  GLU A 233     4635   8853   8293    100   -718  -2721       C  
ATOM   1493  CD  GLU A 233      42.683  20.356 130.802  1.00 58.97           C  
ANISOU 1493  CD  GLU A 233     5048   8858   8500    545   -561  -2564       C  
ATOM   1494  OE1 GLU A 233      42.039  19.399 131.298  1.00 62.27           O  
ANISOU 1494  OE1 GLU A 233     5793   9505   8362    243   -597  -2085       O  
ATOM   1495  OE2 GLU A 233      42.307  21.540 130.923  1.00 64.16           O  
ANISOU 1495  OE2 GLU A 233     6335   8779   9261    771    -77  -2370       O  
ATOM   1496  N   LYS A 234      41.991  17.243 127.468  1.00 39.11           N  
ANISOU 1496  N   LYS A 234     3604   5292   5964    127   -176  -1271       N  
ATOM   1497  CA  LYS A 234      41.637  15.899 127.040  1.00 37.24           C  
ANISOU 1497  CA  LYS A 234     3565   4989   5596    191     79   -822       C  
ATOM   1498  C   LYS A 234      40.951  15.872 125.688  1.00 33.17           C  
ANISOU 1498  C   LYS A 234     3207   4200   5195   -100    523   -812       C  
ATOM   1499  O   LYS A 234      41.157  14.942 124.909  1.00 32.60           O  
ANISOU 1499  O   LYS A 234     3106   4233   5044   -149    461   -819       O  
ATOM   1500  CB  LYS A 234      40.691  15.248 128.057  1.00 38.00           C  
ANISOU 1500  CB  LYS A 234     3952   4968   5517    535    319   -614       C  
ATOM   1501  CG  LYS A 234      41.294  15.070 129.423  1.00 42.26           C  
ANISOU 1501  CG  LYS A 234     4489   5924   5641   1112    188   -506       C  
ATOM   1502  CD  LYS A 234      40.242  14.717 130.463  1.00 43.92           C  
ANISOU 1502  CD  LYS A 234     4732   6100   5854   1340    319    -63       C  
ATOM   1503  CE  LYS A 234      39.935  13.232 130.493  1.00 47.24           C  
ANISOU 1503  CE  LYS A 234     5558   5996   6392   1607    875    422       C  
ATOM   1504  NZ  LYS A 234      39.504  12.839 131.857  1.00 51.95           N  
ANISOU 1504  NZ  LYS A 234     6224   6850   6664   2398   1139   1037       N  
ATOM   1505  N   VAL A 235      40.112  16.875 125.444  1.00 29.96           N  
ANISOU 1505  N   VAL A 235     2885   3749   4748   -525    382   -785       N  
ATOM   1506  CA  VAL A 235      39.175  16.858 124.342  1.00 29.57           C  
ANISOU 1506  CA  VAL A 235     2926   3652   4657   -590    408   -886       C  
ATOM   1507  C   VAL A 235      39.675  17.792 123.282  1.00 29.99           C  
ANISOU 1507  C   VAL A 235     2665   3998   4731   -684    464   -826       C  
ATOM   1508  O   VAL A 235      39.767  18.995 123.508  1.00 31.92           O  
ANISOU 1508  O   VAL A 235     2918   3934   5274   -577    297   -619       O  
ATOM   1509  CB  VAL A 235      37.761  17.298 124.770  1.00 28.12           C  
ANISOU 1509  CB  VAL A 235     2876   3453   4354   -596    318   -888       C  
ATOM   1510  CG1 VAL A 235      36.826  17.346 123.572  1.00 28.62           C  
ANISOU 1510  CG1 VAL A 235     2810   3801   4263   -532    440   -962       C  
ATOM   1511  CG2 VAL A 235      37.211  16.329 125.802  1.00 29.53           C  
ANISOU 1511  CG2 VAL A 235     3062   3493   4663   -558    448   -773       C  
ATOM   1512  N   GLN A 236      39.974  17.231 122.122  1.00 30.70           N  
ANISOU 1512  N   GLN A 236     2612   4234   4816   -532    614   -895       N  
ATOM   1513  CA  GLN A 236      40.415  18.019 120.993  1.00 33.01           C  
ANISOU 1513  CA  GLN A 236     2980   4693   4869   -524    746   -748       C  
ATOM   1514  C   GLN A 236      39.196  18.556 120.250  1.00 33.79           C  
ANISOU 1514  C   GLN A 236     3140   5069   4627   -341    847   -586       C  
ATOM   1515  O   GLN A 236      39.177  19.722 119.870  1.00 34.43           O  
ANISOU 1515  O   GLN A 236     3243   5351   4486   -884   1283   -116       O  
ATOM   1516  CB  GLN A 236      41.325  17.176 120.091  1.00 35.10           C  
ANISOU 1516  CB  GLN A 236     3100   5179   5055   -358    871   -846       C  
ATOM   1517  CG  GLN A 236      41.792  17.912 118.853  1.00 38.46           C  
ANISOU 1517  CG  GLN A 236     3411   5916   5284    -75   1166   -516       C  
ATOM   1518  CD  GLN A 236      42.897  17.216 118.102  1.00 40.47           C  
ANISOU 1518  CD  GLN A 236     3472   6443   5460     59   1258   -641       C  
ATOM   1519  OE1 GLN A 236      43.273  16.089 118.412  1.00 40.09           O  
ANISOU 1519  OE1 GLN A 236     3677   6196   5360    -67   1066  -1009       O  
ATOM   1520  NE2 GLN A 236      43.425  17.894 117.095  1.00 43.97           N  
ANISOU 1520  NE2 GLN A 236     3714   7167   5825    289   1628   -249       N  
ATOM   1521  N   THR A 237      38.164  17.718 120.086  1.00 27.84           N  
ANISOU 1521  N   THR A 237     2849   3932   3797   -741    835   -700       N  
ATOM   1522  CA  THR A 237      37.048  18.035 119.196  1.00 27.32           C  
ANISOU 1522  CA  THR A 237     2990   3719   3671   -769    853   -559       C  
ATOM   1523  C   THR A 237      35.683  17.554 119.715  1.00 26.47           C  
ANISOU 1523  C   THR A 237     2979   3409   3668   -663    815   -450       C  
ATOM   1524  O   THR A 237      35.559  16.435 120.228  1.00 26.45           O  
ANISOU 1524  O   THR A 237     2790   3590   3668  -1209    814   -351       O  
ATOM   1525  CB  THR A 237      37.310  17.428 117.793  1.00 28.43           C  
ANISOU 1525  CB  THR A 237     3034   3937   3830   -574    919   -745       C  
ATOM   1526  OG1 THR A 237      38.575  17.895 117.308  1.00 31.27           O  
ANISOU 1526  OG1 THR A 237     3306   4529   4046   -826   1212   -984       O  
ATOM   1527  CG2 THR A 237      36.238  17.834 116.789  1.00 28.17           C  
ANISOU 1527  CG2 THR A 237     3149   3859   3693   -595    965   -632       C  
ATOM   1528  N   LEU A 238      34.676  18.413 119.573  1.00 26.21           N  
ANISOU 1528  N   LEU A 238     3049   3254   3656   -691    709   -493       N  
ATOM   1529  CA  LEU A 238      33.283  18.025 119.744  1.00 25.86           C  
ANISOU 1529  CA  LEU A 238     3068   3259   3496   -612    778   -359       C  
ATOM   1530  C   LEU A 238      32.614  17.899 118.376  1.00 25.47           C  
ANISOU 1530  C   LEU A 238     3028   3123   3525   -576    741   -379       C  
ATOM   1531  O   LEU A 238      32.481  18.900 117.661  1.00 25.63           O  
ANISOU 1531  O   LEU A 238     3006   3289   3443   -430    889   -309       O  
ATOM   1532  CB  LEU A 238      32.514  19.044 120.577  1.00 26.02           C  
ANISOU 1532  CB  LEU A 238     3134   3210   3540   -545    738   -335       C  
ATOM   1533  CG  LEU A 238      31.031  18.641 120.765  1.00 26.17           C  
ANISOU 1533  CG  LEU A 238     3186   3070   3684   -626    737   -242       C  
ATOM   1534  CD1 LEU A 238      30.894  17.476 121.722  1.00 26.33           C  
ANISOU 1534  CD1 LEU A 238     3117   3341   3544   -573    562    -74       C  
ATOM   1535  CD2 LEU A 238      30.185  19.795 121.249  1.00 26.35           C  
ANISOU 1535  CD2 LEU A 238     3204   3327   3478   -498    765   -340       C  
ATOM   1536  N   GLU A 239      32.180  16.685 118.043  1.00 24.12           N  
ANISOU 1536  N   GLU A 239     2721   2992   3450   -405    781   -432       N  
ATOM   1537  CA  GLU A 239      31.479  16.406 116.794  1.00 25.39           C  
ANISOU 1537  CA  GLU A 239     3088   3080   3477   -471    675   -388       C  
ATOM   1538  C   GLU A 239      29.981  16.188 117.039  1.00 24.16           C  
ANISOU 1538  C   GLU A 239     3060   2848   3269   -390    576   -348       C  
ATOM   1539  O   GLU A 239      29.576  15.219 117.710  1.00 23.99           O  
ANISOU 1539  O   GLU A 239     2567   3028   3518   -569    631   -307       O  
ATOM   1540  CB  GLU A 239      32.078  15.175 116.108  1.00 27.85           C  
ANISOU 1540  CB  GLU A 239     3350   3291   3941   -268    622   -592       C  
ATOM   1541  CG  GLU A 239      31.475  14.836 114.752  1.00 29.64           C  
ANISOU 1541  CG  GLU A 239     3653   3592   4014   -393    580   -652       C  
ATOM   1542  CD  GLU A 239      32.212  13.703 114.069  1.00 33.67           C  
ANISOU 1542  CD  GLU A 239     4006   4060   4727   -221    682  -1073       C  
ATOM   1543  OE1 GLU A 239      33.332  13.924 113.567  1.00 39.90           O  
ANISOU 1543  OE1 GLU A 239     4222   5341   5597   -842    979  -1454       O  
ATOM   1544  OE2 GLU A 239      31.676  12.579 114.039  1.00 38.49           O  
ANISOU 1544  OE2 GLU A 239     4491   4225   5909   -419    963  -1423       O  
ATOM   1545  N   ALA A 240      29.175  17.080 116.471  1.00 23.15           N  
ANISOU 1545  N   ALA A 240     3047   2660   3086   -381    773   -329       N  
ATOM   1546  CA  ALA A 240      27.723  16.990 116.527  1.00 23.52           C  
ANISOU 1546  CA  ALA A 240     3051   2715   3167   -414    595   -257       C  
ATOM   1547  C   ALA A 240      27.201  16.141 115.375  1.00 24.35           C  
ANISOU 1547  C   ALA A 240     3198   2760   3290   -458    564   -347       C  
ATOM   1548  O   ALA A 240      27.620  16.330 114.218  1.00 25.54           O  
ANISOU 1548  O   ALA A 240     3130   3281   3292   -765    548   -221       O  
ATOM   1549  CB  ALA A 240      27.103  18.390 116.482  1.00 23.40           C  
ANISOU 1549  CB  ALA A 240     3057   2749   3083   -357    663   -195       C  
ATOM   1550  N   TRP A 241      26.309  15.198 115.699  1.00 24.16           N  
ANISOU 1550  N   TRP A 241     2977   2904   3297   -439    465   -261       N  
ATOM   1551  CA  TRP A 241      25.572  14.410 114.704  1.00 24.68           C  
ANISOU 1551  CA  TRP A 241     3103   2827   3447   -457    399   -345       C  
ATOM   1552  C   TRP A 241      24.127  14.907 114.695  1.00 24.85           C  
ANISOU 1552  C   TRP A 241     3103   2883   3454   -457    238   -215       C  
ATOM   1553  O   TRP A 241      23.368  14.641 115.647  1.00 24.97           O  
ANISOU 1553  O   TRP A 241     2882   2969   3636   -441    280   -280       O  
ATOM   1554  CB  TRP A 241      25.590  12.910 115.030  1.00 25.34           C  
ANISOU 1554  CB  TRP A 241     3205   2795   3625   -510    179   -356       C  
ATOM   1555  CG  TRP A 241      26.924  12.234 115.022  1.00 26.17           C  
ANISOU 1555  CG  TRP A 241     3292   2820   3831   -441    169   -429       C  
ATOM   1556  CD1 TRP A 241      28.085  12.713 114.500  1.00 26.71           C  
ANISOU 1556  CD1 TRP A 241     3389   2867   3891   -329    399   -467       C  
ATOM   1557  CD2 TRP A 241      27.228  10.931 115.543  1.00 27.02           C  
ANISOU 1557  CD2 TRP A 241     3492   2771   4002   -380     11   -506       C  
ATOM   1558  NE1 TRP A 241      29.097  11.811 114.679  1.00 27.77           N  
ANISOU 1558  NE1 TRP A 241     3422   2888   4239   -314     99   -532       N  
ATOM   1559  CE2 TRP A 241      28.603  10.706 115.320  1.00 27.92           C  
ANISOU 1559  CE2 TRP A 241     3537   2857   4213   -309      2   -528       C  
ATOM   1560  CE3 TRP A 241      26.477   9.946 116.197  1.00 27.92           C  
ANISOU 1560  CE3 TRP A 241     3572   2745   4289   -526   -235   -414       C  
ATOM   1561  CZ2 TRP A 241      29.247   9.526 115.708  1.00 29.93           C  
ANISOU 1561  CZ2 TRP A 241     3745   2911   4714   -228   -256   -512       C  
ATOM   1562  CZ3 TRP A 241      27.111   8.771 116.588  1.00 30.62           C  
ANISOU 1562  CZ3 TRP A 241     3916   2891   4827   -458   -301   -210       C  
ATOM   1563  CH2 TRP A 241      28.491   8.571 116.342  1.00 31.71           C  
ANISOU 1563  CH2 TRP A 241     3918   3026   5102   -353   -335   -346       C  
ATOM   1564  N   VAL A 242      23.754  15.654 113.657  1.00 24.05           N  
ANISOU 1564  N   VAL A 242     3113   2879   3146   -458    316   -356       N  
ATOM   1565  CA  VAL A 242      22.402  16.204 113.558  1.00 25.26           C  
ANISOU 1565  CA  VAL A 242     3169   3103   3323   -379    238   -177       C  
ATOM   1566  C   VAL A 242      21.495  15.191 112.858  1.00 25.76           C  
ANISOU 1566  C   VAL A 242     3213   3148   3427   -325    128   -241       C  
ATOM   1567  O   VAL A 242      21.667  14.922 111.679  1.00 26.18           O  
ANISOU 1567  O   VAL A 242     3214   3319   3415   -363    211   -223       O  
ATOM   1568  CB  VAL A 242      22.373  17.558 112.823  1.00 25.78           C  
ANISOU 1568  CB  VAL A 242     3361   3114   3318   -313    313   -183       C  
ATOM   1569  CG1 VAL A 242      20.952  18.127 112.749  1.00 26.61           C  
ANISOU 1569  CG1 VAL A 242     3385   3337   3387   -278    211   -132       C  
ATOM   1570  CG2 VAL A 242      23.283  18.540 113.530  1.00 25.62           C  
ANISOU 1570  CG2 VAL A 242     3357   3116   3260   -312    345   -184       C  
ATOM   1571  N   ILE A 243      20.519  14.660 113.592  1.00 26.43           N  
ANISOU 1571  N   ILE A 243     3152   3302   3585   -467     48    -84       N  
ATOM   1572  CA  ILE A 243      19.639  13.610 113.079  1.00 28.33           C  
ANISOU 1572  CA  ILE A 243     3440   3481   3843   -556    -63   -229       C  
ATOM   1573  C   ILE A 243      18.462  14.238 112.350  1.00 29.14           C  
ANISOU 1573  C   ILE A 243     3403   3692   3976   -586    -89   -113       C  
ATOM   1574  O   ILE A 243      17.731  15.028 112.935  1.00 30.26           O  
ANISOU 1574  O   ILE A 243     3516   3822   4160   -608    256      6       O  
ATOM   1575  CB  ILE A 243      19.098  12.732 114.226  1.00 29.58           C  
ANISOU 1575  CB  ILE A 243     3495   3670   4073   -730   -100    -73       C  
ATOM   1576  CG1 ILE A 243      20.246  12.209 115.115  1.00 29.47           C  
ANISOU 1576  CG1 ILE A 243     3544   3557   4095   -685    -63    -50       C  
ATOM   1577  CG2 ILE A 243      18.268  11.582 113.685  1.00 32.11           C  
ANISOU 1577  CG2 ILE A 243     3616   4037   4546   -943   -261    -83       C  
ATOM   1578  CD1 ILE A 243      21.411  11.570 114.394  1.00 29.78           C  
ANISOU 1578  CD1 ILE A 243     3555   3426   4331   -661   -104   -105       C  
ATOM   1579  N   HIS A 244      18.258  13.876 111.088  1.00 29.60           N  
ANISOU 1579  N   HIS A 244     3677   3647   3922   -549    -83    -47       N  
ATOM   1580  CA  HIS A 244      17.111  14.390 110.322  1.00 32.34           C  
ANISOU 1580  CA  HIS A 244     3767   4326   4194   -398   -278   -167       C  
ATOM   1581  C   HIS A 244      15.873  13.525 110.524  1.00 35.33           C  
ANISOU 1581  C   HIS A 244     4004   4729   4688   -678   -267    -41       C  
ATOM   1582  O   HIS A 244      15.976  12.329 110.790  1.00 33.60           O  
ANISOU 1582  O   HIS A 244     3456   4582   4726   -897   -322   -290       O  
ATOM   1583  CB  HIS A 244      17.451  14.514 108.825  1.00 32.25           C  
ANISOU 1583  CB  HIS A 244     3893   4306   4054   -371   -449   -377       C  
ATOM   1584  CG  HIS A 244      18.432  15.602 108.525  1.00 31.44           C  
ANISOU 1584  CG  HIS A 244     3984   4158   3801   -230   -222   -322       C  
ATOM   1585  ND1 HIS A 244      18.127  16.681 107.721  1.00 32.64           N  
ANISOU 1585  ND1 HIS A 244     4129   4355   3915    -78   -319   -324       N  
ATOM   1586  CD2 HIS A 244      19.706  15.794 108.943  1.00 30.37           C  
ANISOU 1586  CD2 HIS A 244     3936   3865   3738   -196   -138   -252       C  
ATOM   1587  CE1 HIS A 244      19.176  17.479 107.644  1.00 32.18           C  
ANISOU 1587  CE1 HIS A 244     4258   4109   3856    -74   -162   -235       C  
ATOM   1588  NE2 HIS A 244      20.146  16.968 108.383  1.00 30.91           N  
ANISOU 1588  NE2 HIS A 244     4100   3838   3806   -158    -93   -256       N  
ATOM   1589  N   GLY A 245      14.709  14.161 110.408  1.00 40.11           N  
ANISOU 1589  N   GLY A 245     4225   5509   5506   -414   -537    263       N  
ATOM   1590  CA  GLY A 245      13.409  13.504 110.557  1.00 43.99           C  
ANISOU 1590  CA  GLY A 245     4653   6156   5902   -931   -432    164       C  
ATOM   1591  C   GLY A 245      12.478  13.886 109.421  1.00 49.54           C  
ANISOU 1591  C   GLY A 245     5591   7361   5869  -1132   -852    183       C  
ATOM   1592  O   GLY A 245      12.702  13.497 108.270  1.00 59.37           O  
ANISOU 1592  O   GLY A 245     8039   8143   6376  -1497     46   -381       O  
ATOM   1593  N   SER A 250      15.419  17.059 102.443  1.00 49.21           N  
ANISOU 1593  N   SER A 250     6123   7378   5196      6   -721   -185       N  
ATOM   1594  CA  SER A 250      16.226  17.307 103.623  1.00 47.27           C  
ANISOU 1594  CA  SER A 250     6087   6573   5299    -46   -624   -397       C  
ATOM   1595  C   SER A 250      17.598  17.903 103.263  1.00 44.04           C  
ANISOU 1595  C   SER A 250     6186   5973   4572    149   -394   -299       C  
ATOM   1596  O   SER A 250      18.325  17.366 102.424  1.00 42.34           O  
ANISOU 1596  O   SER A 250     5772   5939   4375    256   -599   -120       O  
ATOM   1597  CB  SER A 250      16.394  16.017 104.424  1.00 48.91           C  
ANISOU 1597  CB  SER A 250     6285   6525   5773   -194   -589   -292       C  
ATOM   1598  OG  SER A 250      17.433  15.215 103.890  1.00 56.45           O  
ANISOU 1598  OG  SER A 250     7552   6732   7161     55   -217  -1206       O  
ATOM   1599  N   ARG A 251      17.944  18.992 103.942  1.00 42.11           N  
ANISOU 1599  N   ARG A 251     5776   5772   4451     74   -334    -93       N  
ATOM   1600  CA  ARG A 251      19.075  19.838 103.588  1.00 41.29           C  
ANISOU 1600  CA  ARG A 251     5841   5611   4237    117   -338    -94       C  
ATOM   1601  C   ARG A 251      20.001  20.009 104.758  1.00 37.44           C  
ANISOU 1601  C   ARG A 251     5416   4797   4010    285    -85    -19       C  
ATOM   1602  O   ARG A 251      19.563  19.974 105.891  1.00 33.90           O  
ANISOU 1602  O   ARG A 251     4212   4505   4163    293    -96    288       O  
ATOM   1603  CB  ARG A 251      18.571  21.225 103.225  1.00 43.48           C  
ANISOU 1603  CB  ARG A 251     6375   5716   4430    228   -365     46       C  
ATOM   1604  CG  ARG A 251      17.634  21.250 102.043  1.00 46.37           C  
ANISOU 1604  CG  ARG A 251     6511   6297   4811    267   -640     69       C  
ATOM   1605  CD  ARG A 251      18.333  20.841 100.763  1.00 48.63           C  
ANISOU 1605  CD  ARG A 251     7015   6788   4671    131   -679   -146       C  
ATOM   1606  NE  ARG A 251      17.922  21.758  99.713  1.00 54.12           N  
ANISOU 1606  NE  ARG A 251     8012   7374   5176    119   -713    262       N  
ATOM   1607  CZ  ARG A 251      18.613  22.804  99.254  1.00 55.06           C  
ANISOU 1607  CZ  ARG A 251     8238   7377   5305    -21   -772    324       C  
ATOM   1608  NH1 ARG A 251      19.835  23.109  99.684  1.00 55.35           N  
ANISOU 1608  NH1 ARG A 251     8245   7155   5629   -101   -787     65       N  
ATOM   1609  NH2 ARG A 251      18.068  23.542  98.311  1.00 58.00           N  
ANISOU 1609  NH2 ARG A 251     8932   7437   5666     78   -862    526       N  
ATOM   1610  N   ASP A 252      21.269  20.268 104.457  1.00 36.90           N  
ANISOU 1610  N   ASP A 252     5604   4600   3814     94     36    -42       N  
ATOM   1611  CA  ASP A 252      22.320  20.498 105.455  1.00 36.54           C  
ANISOU 1611  CA  ASP A 252     5289   4670   3923    -83    181    -81       C  
ATOM   1612  C   ASP A 252      21.839  21.407 106.612  1.00 35.38           C  
ANISOU 1612  C   ASP A 252     5121   4423   3896     -7    235    114       C  
ATOM   1613  O   ASP A 252      21.373  22.507 106.365  1.00 35.77           O  
ANISOU 1613  O   ASP A 252     5157   4615   3817     92    366    504       O  
ATOM   1614  CB  ASP A 252      23.528  21.118 104.736  1.00 37.59           C  
ANISOU 1614  CB  ASP A 252     5656   4888   3739   -213    275     54       C  
ATOM   1615  CG  ASP A 252      24.770  21.214 105.605  1.00 37.36           C  
ANISOU 1615  CG  ASP A 252     5519   4932   3744   -255    362    181       C  
ATOM   1616  OD1 ASP A 252      24.725  20.897 106.813  1.00 35.01           O  
ANISOU 1616  OD1 ASP A 252     5122   4487   3691    -90    593     58       O  
ATOM   1617  OD2 ASP A 252      25.815  21.606 105.051  1.00 39.75           O  
ANISOU 1617  OD2 ASP A 252     5721   5502   3881   -360    418    685       O  
ATOM   1618  N   LEU A 253      21.938  20.929 107.857  1.00 34.46           N  
ANISOU 1618  N   LEU A 253     4953   4248   3890     28    361     93       N  
ATOM   1619  CA  LEU A 253      21.487  21.688 109.047  1.00 34.71           C  
ANISOU 1619  CA  LEU A 253     5024   4196   3965     12    229    -23       C  
ATOM   1620  C   LEU A 253      22.636  22.257 109.898  1.00 33.28           C  
ANISOU 1620  C   LEU A 253     4934   3993   3716     99    357     66       C  
ATOM   1621  O   LEU A 253      22.404  22.891 110.931  1.00 30.47           O  
ANISOU 1621  O   LEU A 253     4313   3726   3537    106    741    394       O  
ATOM   1622  CB  LEU A 253      20.565  20.811 109.913  1.00 34.40           C  
ANISOU 1622  CB  LEU A 253     4690   4292   4086    105    263   -129       C  
ATOM   1623  CG  LEU A 253      19.137  20.600 109.387  1.00 36.08           C  
ANISOU 1623  CG  LEU A 253     4873   4582   4251    138    -42    -51       C  
ATOM   1624  CD1 LEU A 253      18.418  19.521 110.181  1.00 36.10           C  
ANISOU 1624  CD1 LEU A 253     4700   4708   4307     63   -128    -32       C  
ATOM   1625  CD2 LEU A 253      18.331  21.896 109.415  1.00 36.74           C  
ANISOU 1625  CD2 LEU A 253     4971   4830   4158    393      2    -58       C  
ATOM   1626  N   CYS A 254      23.868  22.095 109.428  1.00 34.25           N  
ANISOU 1626  N   CYS A 254     5003   4131   3877    106    463    169       N  
ATOM   1627  CA  CYS A 254      25.043  22.495 110.192  1.00 35.38           C  
ANISOU 1627  CA  CYS A 254     5232   4168   4041   -342    478    -28       C  
ATOM   1628  C   CYS A 254      25.288  24.019 110.212  1.00 35.50           C  
ANISOU 1628  C   CYS A 254     5387   4177   3925   -263    512    118       C  
ATOM   1629  O   CYS A 254      26.175  24.479 110.930  1.00 35.50           O  
ANISOU 1629  O   CYS A 254     5764   3942   3779   -616    714   -162       O  
ATOM   1630  CB  CYS A 254      26.278  21.700 109.713  1.00 37.27           C  
ANISOU 1630  CB  CYS A 254     5227   4767   4164   -219    406   -194       C  
ATOM   1631  SG  CYS A 254      26.219  19.950 110.228  1.00 39.64           S  
ANISOU 1631  SG  CYS A 254     5972   4799   4288     75     53   -474       S  
ATOM   1632  N   GLN A 255      24.510  24.797 109.452  1.00 36.54           N  
ANISOU 1632  N   GLN A 255     5677   4263   3941   -273    483    306       N  
ATOM   1633  CA  GLN A 255      24.515  26.253 109.579  1.00 38.56           C  
ANISOU 1633  CA  GLN A 255     5985   4280   4383   -110    328    141       C  
ATOM   1634  C   GLN A 255      23.307  26.783 110.323  1.00 36.43           C  
ANISOU 1634  C   GLN A 255     5913   3834   4093     -4    137    285       C  
ATOM   1635  O   GLN A 255      23.105  27.987 110.357  1.00 35.92           O  
ANISOU 1635  O   GLN A 255     5667   3819   4162    260     37    361       O  
ATOM   1636  CB  GLN A 255      24.608  26.934 108.200  1.00 43.41           C  
ANISOU 1636  CB  GLN A 255     6928   4820   4746   -317    205    580       C  
ATOM   1637  CG  GLN A 255      25.839  26.551 107.397  1.00 46.18           C  
ANISOU 1637  CG  GLN A 255     7260   5328   4959   -456    537    583       C  
ATOM   1638  CD  GLN A 255      27.119  26.708 108.198  1.00 49.59           C  
ANISOU 1638  CD  GLN A 255     7417   5550   5875   -670    250    581       C  
ATOM   1639  OE1 GLN A 255      27.382  27.773 108.758  1.00 54.93           O  
ANISOU 1639  OE1 GLN A 255     8820   5905   6145   -602    398     87       O  
ATOM   1640  NE2 GLN A 255      27.898  25.635 108.298  1.00 51.84           N  
ANISOU 1640  NE2 GLN A 255     7374   5932   6390   -383    407    170       N  
ATOM   1641  N   ASP A 256      22.510  25.906 110.930  1.00 36.03           N  
ANISOU 1641  N   ASP A 256     5590   3991   4109    143    185    269       N  
ATOM   1642  CA  ASP A 256      21.389  26.347 111.776  1.00 36.55           C  
ANISOU 1642  CA  ASP A 256     5555   4057   4274    256    112     33       C  
ATOM   1643  C   ASP A 256      21.901  27.322 112.846  1.00 34.64           C  
ANISOU 1643  C   ASP A 256     5427   3418   4313    322    322     92       C  
ATOM   1644  O   ASP A 256      22.966  27.093 113.421  1.00 31.21           O  
ANISOU 1644  O   ASP A 256     5290   2747   3819   -120    370   -244       O  
ATOM   1645  CB  ASP A 256      20.726  25.142 112.449  1.00 36.37           C  
ANISOU 1645  CB  ASP A 256     5255   4114   4449    287    218     -6       C  
ATOM   1646  CG  ASP A 256      19.527  25.530 113.299  1.00 39.18           C  
ANISOU 1646  CG  ASP A 256     5326   4767   4793    649    183   -222       C  
ATOM   1647  OD1 ASP A 256      18.441  25.731 112.732  1.00 43.74           O  
ANISOU 1647  OD1 ASP A 256     5420   5439   5759   1356     97   -325       O  
ATOM   1648  OD2 ASP A 256      19.667  25.618 114.533  1.00 40.34           O  
ANISOU 1648  OD2 ASP A 256     5441   5068   4814    486    370   -539       O  
ATOM   1649  N   PRO A 257      21.164  28.413 113.104  1.00 35.79           N  
ANISOU 1649  N   PRO A 257     5607   3572   4419    514    144     26       N  
ATOM   1650  CA  PRO A 257      21.601  29.383 114.125  1.00 36.59           C  
ANISOU 1650  CA  PRO A 257     5828   3464   4608    585     78    -54       C  
ATOM   1651  C   PRO A 257      22.013  28.778 115.473  1.00 34.71           C  
ANISOU 1651  C   PRO A 257     5449   3264   4473    543    203   -169       C  
ATOM   1652  O   PRO A 257      23.015  29.192 116.048  1.00 33.58           O  
ANISOU 1652  O   PRO A 257     5590   2660   4508    399    269   -145       O  
ATOM   1653  CB  PRO A 257      20.373  30.282 114.292  1.00 38.54           C  
ANISOU 1653  CB  PRO A 257     6150   3599   4894    892    -59   -145       C  
ATOM   1654  CG  PRO A 257      19.743  30.274 112.945  1.00 39.61           C  
ANISOU 1654  CG  PRO A 257     6287   3747   5015    924   -211     34       C  
ATOM   1655  CD  PRO A 257      19.984  28.905 112.365  1.00 37.89           C  
ANISOU 1655  CD  PRO A 257     5934   3813   4647    743    -80     11       C  
ATOM   1656  N   THR A 258      21.272  27.790 115.956  1.00 34.62           N  
ANISOU 1656  N   THR A 258     5163   3546   4444    524    296   -191       N  
ATOM   1657  CA  THR A 258      21.617  27.148 117.244  1.00 33.83           C  
ANISOU 1657  CA  THR A 258     4869   3686   4298    477    343   -326       C  
ATOM   1658  C   THR A 258      22.905  26.322 117.157  1.00 32.39           C  
ANISOU 1658  C   THR A 258     4746   3352   4206    267    459   -155       C  
ATOM   1659  O   THR A 258      23.660  26.276 118.122  1.00 33.17           O  
ANISOU 1659  O   THR A 258     4981   3388   4234    188    364   -279       O  
ATOM   1660  CB  THR A 258      20.462  26.300 117.833  1.00 33.02           C  
ANISOU 1660  CB  THR A 258     4576   3767   4201    613    413   -419       C  
ATOM   1661  OG1 THR A 258      20.182  25.171 116.999  1.00 30.72           O  
ANISOU 1661  OG1 THR A 258     3897   3640   4134    596    381   -303       O  
ATOM   1662  CG2 THR A 258      19.197  27.148 117.980  1.00 35.63           C  
ANISOU 1662  CG2 THR A 258     4725   4239   4573    839    377   -581       C  
ATOM   1663  N   ILE A 259      23.171  25.699 116.006  1.00 32.92           N  
ANISOU 1663  N   ILE A 259     4892   3527   4087    206    495    -53       N  
ATOM   1664  CA  ILE A 259      24.444  24.981 115.797  1.00 32.52           C  
ANISOU 1664  CA  ILE A 259     4642   3678   4035    -23    634   -103       C  
ATOM   1665  C   ILE A 259      25.603  25.985 115.785  1.00 32.61           C  
ANISOU 1665  C   ILE A 259     4987   3348   4055   -111    622   -211       C  
ATOM   1666  O   ILE A 259      26.659  25.712 116.337  1.00 32.66           O  
ANISOU 1666  O   ILE A 259     4942   3338   4129   -586    448   -313       O  
ATOM   1667  CB  ILE A 259      24.435  24.125 114.507  1.00 33.32           C  
ANISOU 1667  CB  ILE A 259     4763   3814   4083   -113    400   -148       C  
ATOM   1668  CG1 ILE A 259      23.334  23.054 114.552  1.00 33.21           C  
ANISOU 1668  CG1 ILE A 259     4628   3833   4155    -26    414    -56       C  
ATOM   1669  CG2 ILE A 259      25.794  23.468 114.247  1.00 32.75           C  
ANISOU 1669  CG2 ILE A 259     4810   3569   4065   -159    408    -86       C  
ATOM   1670  CD1 ILE A 259      23.495  21.993 115.609  1.00 32.70           C  
ANISOU 1670  CD1 ILE A 259     4475   3830   4119   -103    304   -119       C  
ATOM   1671  N   LYS A 260      25.389  27.149 115.186  1.00 34.00           N  
ANISOU 1671  N   LYS A 260     5425   3526   3965    -78    501    -87       N  
ATOM   1672  CA  LYS A 260      26.383  28.234 115.211  1.00 36.71           C  
ANISOU 1672  CA  LYS A 260     5811   3642   4493   -280    491    -62       C  
ATOM   1673  C   LYS A 260      26.645  28.720 116.644  1.00 36.64           C  
ANISOU 1673  C   LYS A 260     5802   3540   4577   -195    437   -173       C  
ATOM   1674  O   LYS A 260      27.759  29.085 116.980  1.00 35.90           O  
ANISOU 1674  O   LYS A 260     5757   3713   4167   -469    761   -216       O  
ATOM   1675  CB  LYS A 260      25.933  29.420 114.336  1.00 39.46           C  
ANISOU 1675  CB  LYS A 260     6389   3673   4931   -174    419     86       C  
ATOM   1676  CG  LYS A 260      25.679  29.079 112.871  1.00 40.96           C  
ANISOU 1676  CG  LYS A 260     6681   3993   4888   -212    276    336       C  
ATOM   1677  CD  LYS A 260      26.841  29.441 111.962  1.00 43.63           C  
ANISOU 1677  CD  LYS A 260     7056   4259   5263   -527    514    215       C  
ATOM   1678  CE  LYS A 260      28.123  28.738 112.369  1.00 44.32           C  
ANISOU 1678  CE  LYS A 260     7079   4561   5200   -543    488    389       C  
ATOM   1679  NZ  LYS A 260      29.207  28.925 111.366  1.00 48.13           N  
ANISOU 1679  NZ  LYS A 260     7333   5197   5755   -967    698    317       N  
ATOM   1680  N   GLU A 261      25.607  28.723 117.477  1.00 38.46           N  
ANISOU 1680  N   GLU A 261     5890   3905   4815     85    530   -239       N  
ATOM   1681  CA  GLU A 261      25.735  29.072 118.905  1.00 38.74           C  
ANISOU 1681  CA  GLU A 261     6012   3838   4868     24    413   -261       C  
ATOM   1682  C   GLU A 261      26.528  27.992 119.658  1.00 33.43           C  
ANISOU 1682  C   GLU A 261     5230   3435   4034   -313    722   -506       C  
ATOM   1683  O   GLU A 261      27.399  28.313 120.458  1.00 32.67           O  
ANISOU 1683  O   GLU A 261     5367   2890   4154   -603    808   -679       O  
ATOM   1684  CB  GLU A 261      24.352  29.267 119.520  1.00 42.26           C  
ANISOU 1684  CB  GLU A 261     6198   4387   5473    349    625   -455       C  
ATOM   1685  CG  GLU A 261      24.334  29.746 120.966  1.00 47.94           C  
ANISOU 1685  CG  GLU A 261     7084   5221   5910    493    435   -982       C  
ATOM   1686  CD  GLU A 261      22.987  29.514 121.653  1.00 55.76           C  
ANISOU 1686  CD  GLU A 261     7174   7311   6700    882    884  -1167       C  
ATOM   1687  OE1 GLU A 261      21.980  29.216 120.947  1.00 57.98           O  
ANISOU 1687  OE1 GLU A 261     7163   7719   7146    843    889  -1944       O  
ATOM   1688  OE2 GLU A 261      22.943  29.627 122.909  1.00 63.18           O  
ANISOU 1688  OE2 GLU A 261     7908   9096   7000   2358   1736  -2769       O  
ATOM   1689  N   LEU A 262      26.242  26.721 119.391  1.00 30.50           N  
ANISOU 1689  N   LEU A 262     4547   3267   3775   -156    788   -355       N  
ATOM   1690  CA  LEU A 262      27.042  25.629 119.966  1.00 29.67           C  
ANISOU 1690  CA  LEU A 262     4277   3232   3764   -273    696   -494       C  
ATOM   1691  C   LEU A 262      28.525  25.753 119.568  1.00 28.56           C  
ANISOU 1691  C   LEU A 262     4292   2838   3721   -511    700   -430       C  
ATOM   1692  O   LEU A 262      29.405  25.662 120.414  1.00 26.86           O  
ANISOU 1692  O   LEU A 262     3993   2512   3698   -647    812   -604       O  
ATOM   1693  CB  LEU A 262      26.490  24.244 119.564  1.00 28.67           C  
ANISOU 1693  CB  LEU A 262     4035   3146   3711   -296    642   -223       C  
ATOM   1694  CG  LEU A 262      27.287  23.008 120.010  1.00 27.41           C  
ANISOU 1694  CG  LEU A 262     3770   3115   3528   -391    672   -254       C  
ATOM   1695  CD1 LEU A 262      27.502  23.015 121.520  1.00 27.15           C  
ANISOU 1695  CD1 LEU A 262     3644   3189   3480   -350    795   -423       C  
ATOM   1696  CD2 LEU A 262      26.573  21.734 119.585  1.00 26.61           C  
ANISOU 1696  CD2 LEU A 262     3677   3083   3348   -278    680   -367       C  
ATOM   1697  N   GLU A 263      28.777  25.977 118.282  1.00 28.60           N  
ANISOU 1697  N   GLU A 263     4499   2597   3769   -552    810   -545       N  
ATOM   1698  CA  GLU A 263      30.134  26.155 117.765  1.00 30.66           C  
ANISOU 1698  CA  GLU A 263     4656   2998   3995   -749    979   -288       C  
ATOM   1699  C   GLU A 263      30.874  27.270 118.505  1.00 31.16           C  
ANISOU 1699  C   GLU A 263     4824   3235   3778   -810    820   -228       C  
ATOM   1700  O   GLU A 263      32.041  27.113 118.869  1.00 31.05           O  
ANISOU 1700  O   GLU A 263     4690   3145   3961  -1263    879     -4       O  
ATOM   1701  CB  GLU A 263      30.088  26.477 116.267  1.00 33.60           C  
ANISOU 1701  CB  GLU A 263     5218   3501   4048   -713    782   -239       C  
ATOM   1702  CG  GLU A 263      31.463  26.629 115.612  1.00 36.45           C  
ANISOU 1702  CG  GLU A 263     5383   3967   4498   -981   1036   -210       C  
ATOM   1703  CD  GLU A 263      31.393  26.961 114.135  1.00 40.75           C  
ANISOU 1703  CD  GLU A 263     6244   4527   4709   -834    877    250       C  
ATOM   1704  OE1 GLU A 263      30.607  27.839 113.755  1.00 45.04           O  
ANISOU 1704  OE1 GLU A 263     6673   5077   5361   -487    919    336       O  
ATOM   1705  OE2 GLU A 263      32.144  26.357 113.341  1.00 45.90           O  
ANISOU 1705  OE2 GLU A 263     6724   5477   5240   -823   1468    349       O  
ATOM   1706  N   SER A 264      30.179  28.387 118.701  1.00 31.83           N  
ANISOU 1706  N   SER A 264     5101   3092   3900   -743    772   -191       N  
ATOM   1707  CA  SER A 264      30.710  29.540 119.409  1.00 35.20           C  
ANISOU 1707  CA  SER A 264     5556   3326   4490   -857    695   -432       C  
ATOM   1708  C   SER A 264      31.136  29.193 120.846  1.00 35.11           C  
ANISOU 1708  C   SER A 264     5430   3422   4486   -855    743   -464       C  
ATOM   1709  O   SER A 264      32.240  29.556 121.274  1.00 35.86           O  
ANISOU 1709  O   SER A 264     5495   2939   5188  -1122   1065  -1160       O  
ATOM   1710  CB  SER A 264      29.668  30.665 119.391  1.00 38.10           C  
ANISOU 1710  CB  SER A 264     6140   3329   5005   -596    458   -328       C  
ATOM   1711  OG  SER A 264      30.043  31.733 120.224  1.00 43.81           O  
ANISOU 1711  OG  SER A 264     7110   3968   5566   -828    134   -732       O  
ATOM   1712  N   ILE A 265      30.278  28.470 121.568  1.00 34.25           N  
ANISOU 1712  N   ILE A 265     5145   3482   4386   -680    727   -427       N  
ATOM   1713  CA  ILE A 265      30.578  28.029 122.941  1.00 33.58           C  
ANISOU 1713  CA  ILE A 265     5007   3557   4194   -702    776   -613       C  
ATOM   1714  C   ILE A 265      31.820  27.136 122.952  1.00 32.17           C  
ANISOU 1714  C   ILE A 265     4660   3683   3878   -935    795   -511       C  
ATOM   1715  O   ILE A 265      32.775  27.382 123.690  1.00 31.16           O  
ANISOU 1715  O   ILE A 265     4698   3461   3678  -1679    978   -290       O  
ATOM   1716  CB  ILE A 265      29.384  27.264 123.573  1.00 32.62           C  
ANISOU 1716  CB  ILE A 265     4741   3586   4067   -503    776   -682       C  
ATOM   1717  CG1 ILE A 265      28.209  28.223 123.817  1.00 34.66           C  
ANISOU 1717  CG1 ILE A 265     5064   3744   4359   -236    687   -731       C  
ATOM   1718  CG2 ILE A 265      29.790  26.577 124.881  1.00 31.94           C  
ANISOU 1718  CG2 ILE A 265     4459   3675   4001   -537    853   -713       C  
ATOM   1719  CD1 ILE A 265      26.869  27.536 124.030  1.00 34.39           C  
ANISOU 1719  CD1 ILE A 265     4884   3897   4284   -130    477   -702       C  
ATOM   1720  N   ILE A 266      31.792  26.112 122.110  1.00 31.75           N  
ANISOU 1720  N   ILE A 266     4533   3517   4013   -999    992   -502       N  
ATOM   1721  CA  ILE A 266      32.890  25.157 121.993  1.00 33.06           C  
ANISOU 1721  CA  ILE A 266     4463   3875   4222   -898    957   -460       C  
ATOM   1722  C   ILE A 266      34.229  25.835 121.650  1.00 33.49           C  
ANISOU 1722  C   ILE A 266     4677   3788   4258  -1191    854   -393       C  
ATOM   1723  O   ILE A 266      35.240  25.555 122.303  1.00 33.13           O  
ANISOU 1723  O   ILE A 266     4640   3941   4005  -1164    943   -641       O  
ATOM   1724  CB  ILE A 266      32.536  24.070 120.942  1.00 33.54           C  
ANISOU 1724  CB  ILE A 266     4539   3770   4435   -863    786   -510       C  
ATOM   1725  CG1 ILE A 266      31.363  23.221 121.431  1.00 34.24           C  
ANISOU 1725  CG1 ILE A 266     4607   4064   4338   -693    930   -388       C  
ATOM   1726  CG2 ILE A 266      33.722  23.175 120.612  1.00 33.43           C  
ANISOU 1726  CG2 ILE A 266     4340   3988   4373   -870    787   -474       C  
ATOM   1727  CD1 ILE A 266      31.523  22.611 122.810  1.00 35.61           C  
ANISOU 1727  CD1 ILE A 266     4824   4288   4416   -582    224   -521       C  
ATOM   1728  N   SER A 267      34.225  26.711 120.643  1.00 33.40           N  
ANISOU 1728  N   SER A 267     4810   3599   4280  -1218    900   -403       N  
ATOM   1729  CA  SER A 267      35.438  27.452 120.211  1.00 35.00           C  
ANISOU 1729  CA  SER A 267     5005   3958   4332  -1429    965   -413       C  
ATOM   1730  C   SER A 267      35.983  28.344 121.306  1.00 35.38           C  
ANISOU 1730  C   SER A 267     5080   3810   4550  -1564    949   -408       C  
ATOM   1731  O   SER A 267      37.191  28.368 121.557  1.00 36.15           O  
ANISOU 1731  O   SER A 267     4854   3987   4894  -2249   1571   -483       O  
ATOM   1732  CB  SER A 267      35.134  28.335 119.000  1.00 37.02           C  
ANISOU 1732  CB  SER A 267     5544   3981   4538  -1555   1137   -132       C  
ATOM   1733  OG  SER A 267      34.643  27.553 117.929  1.00 40.19           O  
ANISOU 1733  OG  SER A 267     5879   4913   4477  -1696    971   -166       O  
ATOM   1734  N   LYS A 268      35.081  29.063 121.970  1.00 34.13           N  
ANISOU 1734  N   LYS A 268     5229   3358   4381  -1469    732   -418       N  
ATOM   1735  CA  LYS A 268      35.457  29.906 123.092  1.00 35.35           C  
ANISOU 1735  CA  LYS A 268     5311   3693   4425  -1539    749   -582       C  
ATOM   1736  C   LYS A 268      36.125  29.096 124.210  1.00 34.26           C  
ANISOU 1736  C   LYS A 268     4952   3685   4380  -1524    764   -703       C  
ATOM   1737  O   LYS A 268      37.004  29.613 124.893  1.00 36.64           O  
ANISOU 1737  O   LYS A 268     5243   4213   4462  -1675    573   -762       O  
ATOM   1738  CB  LYS A 268      34.258  30.695 123.621  1.00 36.74           C  
ANISOU 1738  CB  LYS A 268     5628   3555   4774  -1263    639   -739       C  
ATOM   1739  CG  LYS A 268      34.566  31.439 124.916  1.00 39.73           C  
ANISOU 1739  CG  LYS A 268     6115   3946   5033  -1310    467   -921       C  
ATOM   1740  CD  LYS A 268      33.588  32.563 125.219  1.00 42.65           C  
ANISOU 1740  CD  LYS A 268     6655   4051   5499  -1061    447  -1062       C  
ATOM   1741  CE  LYS A 268      34.024  33.331 126.457  1.00 44.36           C  
ANISOU 1741  CE  LYS A 268     7032   4149   5674  -1156    433  -1229       C  
ATOM   1742  NZ  LYS A 268      32.936  34.223 126.932  1.00 46.48           N  
ANISOU 1742  NZ  LYS A 268     7488   4217   5952   -947    462  -1404       N  
ATOM   1743  N   ARG A 269      35.739  27.832 124.375  1.00 31.44           N  
ANISOU 1743  N   ARG A 269     4365   3637   3941  -1338    819   -660       N  
ATOM   1744  CA  ARG A 269      36.402  26.943 125.333  1.00 30.92           C  
ANISOU 1744  CA  ARG A 269     4184   3653   3909  -1360    798   -698       C  
ATOM   1745  C   ARG A 269      37.669  26.242 124.800  1.00 31.47           C  
ANISOU 1745  C   ARG A 269     4059   3851   4045  -1422    840   -641       C  
ATOM   1746  O   ARG A 269      38.192  25.364 125.477  1.00 30.08           O  
ANISOU 1746  O   ARG A 269     3396   4005   4029  -1391   1027   -588       O  
ATOM   1747  CB  ARG A 269      35.398  25.915 125.880  1.00 28.97           C  
ANISOU 1747  CB  ARG A 269     3862   3553   3589  -1122    757   -667       C  
ATOM   1748  CG  ARG A 269      34.222  26.569 126.586  1.00 29.53           C  
ANISOU 1748  CG  ARG A 269     4033   3533   3653   -981    751   -677       C  
ATOM   1749  CD  ARG A 269      33.497  25.657 127.555  1.00 28.72           C  
ANISOU 1749  CD  ARG A 269     3737   3655   3517   -913    746   -729       C  
ATOM   1750  NE  ARG A 269      34.392  25.294 128.653  1.00 28.91           N  
ANISOU 1750  NE  ARG A 269     3696   3808   3479   -978    737   -743       N  
ATOM   1751  CZ  ARG A 269      34.869  24.079 128.900  1.00 27.49           C  
ANISOU 1751  CZ  ARG A 269     3418   3795   3231  -1071    800   -650       C  
ATOM   1752  NH1 ARG A 269      34.497  23.033 128.190  1.00 26.69           N  
ANISOU 1752  NH1 ARG A 269     3111   3650   3377   -831    826   -674       N  
ATOM   1753  NH2 ARG A 269      35.704  23.904 129.905  1.00 29.04           N  
ANISOU 1753  NH2 ARG A 269     3335   4048   3651  -1179    617   -561       N  
ATOM   1754  N   ASN A 270      38.176  26.650 123.628  1.00 33.18           N  
ANISOU 1754  N   ASN A 270     4424   4046   4134  -1572    921   -628       N  
ATOM   1755  CA  ASN A 270      39.384  26.073 123.013  1.00 33.96           C  
ANISOU 1755  CA  ASN A 270     4216   4406   4280  -1823   1069   -553       C  
ATOM   1756  C   ASN A 270      39.307  24.586 122.660  1.00 31.87           C  
ANISOU 1756  C   ASN A 270     3703   4351   4053  -1497   1021   -439       C  
ATOM   1757  O   ASN A 270      40.266  23.836 122.822  1.00 29.58           O  
ANISOU 1757  O   ASN A 270     3025   4669   3543  -1788   1101   -357       O  
ATOM   1758  CB  ASN A 270      40.619  26.384 123.856  1.00 37.31           C  
ANISOU 1758  CB  ASN A 270     4591   5029   4553  -1824    714   -622       C  
ATOM   1759  CG  ASN A 270      40.790  27.870 124.087  1.00 42.85           C  
ANISOU 1759  CG  ASN A 270     5860   5164   5254  -2015    645   -746       C  
ATOM   1760  OD1 ASN A 270      40.750  28.670 123.142  1.00 45.84           O  
ANISOU 1760  OD1 ASN A 270     6204   5893   5318  -2142    542   -451       O  
ATOM   1761  ND2 ASN A 270      40.976  28.257 125.341  1.00 46.44           N  
ANISOU 1761  ND2 ASN A 270     6624   5697   5322  -1855    540   -827       N  
ATOM   1762  N   ILE A 271      38.142  24.186 122.156  1.00 31.00           N  
ANISOU 1762  N   ILE A 271     3789   4050   3939  -1416    982   -605       N  
ATOM   1763  CA  ILE A 271      37.903  22.858 121.639  1.00 29.28           C  
ANISOU 1763  CA  ILE A 271     3453   3859   3812  -1261    955   -504       C  
ATOM   1764  C   ILE A 271      37.427  23.078 120.210  1.00 28.60           C  
ANISOU 1764  C   ILE A 271     3371   3708   3785  -1319   1092   -405       C  
ATOM   1765  O   ILE A 271      36.743  24.065 119.930  1.00 28.59           O  
ANISOU 1765  O   ILE A 271     3344   3625   3891  -1281   1009   -680       O  
ATOM   1766  CB  ILE A 271      36.855  22.116 122.513  1.00 28.21           C  
ANISOU 1766  CB  ILE A 271     3302   3755   3659  -1031    953   -551       C  
ATOM   1767  CG1 ILE A 271      37.486  21.761 123.860  1.00 29.05           C  
ANISOU 1767  CG1 ILE A 271     3336   3995   3704  -1073    815   -632       C  
ATOM   1768  CG2 ILE A 271      36.319  20.846 121.829  1.00 26.84           C  
ANISOU 1768  CG2 ILE A 271     3073   3554   3570   -919    990   -475       C  
ATOM   1769  CD1 ILE A 271      36.510  21.300 124.917  1.00 29.09           C  
ANISOU 1769  CD1 ILE A 271     3345   3941   3765  -1055    821   -616       C  
ATOM   1770  N   GLN A 272      37.822  22.181 119.306  1.00 28.70           N  
ANISOU 1770  N   GLN A 272     3089   3990   3823  -1324   1162   -529       N  
ATOM   1771  CA  GLN A 272      37.432  22.265 117.908  1.00 30.08           C  
ANISOU 1771  CA  GLN A 272     3616   4040   3774  -1258   1202   -389       C  
ATOM   1772  C   GLN A 272      35.990  21.762 117.754  1.00 29.17           C  
ANISOU 1772  C   GLN A 272     3533   3795   3753   -938   1146   -364       C  
ATOM   1773  O   GLN A 272      35.530  20.903 118.520  1.00 28.29           O  
ANISOU 1773  O   GLN A 272     3161   3812   3776   -930   1076   -308       O  
ATOM   1774  CB  GLN A 272      38.391  21.436 117.039  1.00 32.22           C  
ANISOU 1774  CB  GLN A 272     3687   4568   3985  -1170   1273   -547       C  
ATOM   1775  CG  GLN A 272      39.848  21.917 117.093  1.00 35.13           C  
ANISOU 1775  CG  GLN A 272     3802   5140   4404  -1356   1176   -659       C  
ATOM   1776  CD  GLN A 272      40.818  21.022 116.345  1.00 38.23           C  
ANISOU 1776  CD  GLN A 272     3946   5813   4766  -1194   1355   -842       C  
ATOM   1777  OE1 GLN A 272      40.426  20.191 115.536  1.00 39.30           O  
ANISOU 1777  OE1 GLN A 272     3895   5774   5262  -1177   1307   -980       O  
ATOM   1778  NE2 GLN A 272      42.102  21.199 116.609  1.00 41.80           N  
ANISOU 1778  NE2 GLN A 272     4110   6453   5318  -1329   1215  -1094       N  
ATOM   1779  N   PHE A 273      35.273  22.305 116.774  1.00 30.34           N  
ANISOU 1779  N   PHE A 273     3881   3862   3782   -890   1077   -274       N  
ATOM   1780  CA  PHE A 273      33.897  21.908 116.529  1.00 29.31           C  
ANISOU 1780  CA  PHE A 273     3958   3538   3640   -956   1022   -338       C  
ATOM   1781  C   PHE A 273      33.756  21.382 115.123  1.00 31.26           C  
ANISOU 1781  C   PHE A 273     4231   3974   3669  -1012   1314   -478       C  
ATOM   1782  O   PHE A 273      34.307  21.960 114.183  1.00 32.68           O  
ANISOU 1782  O   PHE A 273     4293   4221   3901  -1298   1493   -509       O  
ATOM   1783  CB  PHE A 273      32.917  23.063 116.714  1.00 28.87           C  
ANISOU 1783  CB  PHE A 273     3944   3553   3470   -939   1107   -246       C  
ATOM   1784  CG  PHE A 273      31.482  22.655 116.539  1.00 27.81           C  
ANISOU 1784  CG  PHE A 273     3955   3227   3382   -820    871   -281       C  
ATOM   1785  CD1 PHE A 273      30.836  21.923 117.523  1.00 27.31           C  
ANISOU 1785  CD1 PHE A 273     3685   3291   3400   -773    806   -280       C  
ATOM   1786  CD2 PHE A 273      30.785  22.973 115.387  1.00 28.01           C  
ANISOU 1786  CD2 PHE A 273     4032   3153   3456   -749    910   -166       C  
ATOM   1787  CE1 PHE A 273      29.518  21.526 117.372  1.00 26.23           C  
ANISOU 1787  CE1 PHE A 273     3500   3168   3295   -418    851   -346       C  
ATOM   1788  CE2 PHE A 273      29.466  22.579 115.225  1.00 28.13           C  
ANISOU 1788  CE2 PHE A 273     3934   3142   3612   -555    832   -134       C  
ATOM   1789  CZ  PHE A 273      28.829  21.856 116.223  1.00 26.45           C  
ANISOU 1789  CZ  PHE A 273     3695   3075   3279   -309    840   -288       C  
ATOM   1790  N   SER A 274      32.964  20.317 115.002  1.00 29.88           N  
ANISOU 1790  N   SER A 274     3947   3580   3826   -670   1106   -430       N  
ATOM   1791  CA  SER A 274      32.661  19.684 113.747  1.00 31.12           C  
ANISOU 1791  CA  SER A 274     4074   4039   3710   -728    872   -325       C  
ATOM   1792  C   SER A 274      31.202  19.223 113.779  1.00 31.14           C  
ANISOU 1792  C   SER A 274     4132   3940   3760   -689    849   -298       C  
ATOM   1793  O   SER A 274      30.663  18.895 114.843  1.00 31.01           O  
ANISOU 1793  O   SER A 274     4234   3598   3948  -1127    703     37       O  
ATOM   1794  CB  SER A 274      33.624  18.523 113.551  1.00 33.36           C  
ANISOU 1794  CB  SER A 274     4202   4450   4019   -552    900   -554       C  
ATOM   1795  OG  SER A 274      33.163  17.623 112.590  1.00 38.01           O  
ANISOU 1795  OG  SER A 274     4655   5331   4456   -741    725   -921       O  
ATOM   1796  N   CYS A 275      30.556  19.241 112.619  1.00 30.74           N  
ANISOU 1796  N   CYS A 275     4216   3850   3612   -572    907   -518       N  
ATOM   1797  CA  CYS A 275      29.132  18.954 112.520  1.00 31.32           C  
ANISOU 1797  CA  CYS A 275     4234   3976   3687   -548    799   -455       C  
ATOM   1798  C   CYS A 275      28.867  18.065 111.309  1.00 30.38           C  
ANISOU 1798  C   CYS A 275     3968   3918   3654   -452    815   -468       C  
ATOM   1799  O   CYS A 275      29.401  18.304 110.233  1.00 29.51           O  
ANISOU 1799  O   CYS A 275     3926   4240   3046   -280    456   -862       O  
ATOM   1800  CB  CYS A 275      28.320  20.260 112.440  1.00 33.67           C  
ANISOU 1800  CB  CYS A 275     5052   3921   3816   -403    480   -167       C  
ATOM   1801  SG  CYS A 275      26.526  20.025 112.309  1.00 38.08           S  
ANISOU 1801  SG  CYS A 275     5190   5020   4258     97    349   -402       S  
ATOM   1802  N   LYS A 276      28.030  17.056 111.505  1.00 28.70           N  
ANISOU 1802  N   LYS A 276     4061   3378   3463   -245    567   -348       N  
ATOM   1803  CA  LYS A 276      27.689  16.096 110.473  1.00 30.13           C  
ANISOU 1803  CA  LYS A 276     4006   3848   3592   -398    521   -523       C  
ATOM   1804  C   LYS A 276      26.197  15.912 110.460  1.00 28.41           C  
ANISOU 1804  C   LYS A 276     4001   3280   3512   -357    369   -430       C  
ATOM   1805  O   LYS A 276      25.581  15.851 111.525  1.00 28.39           O  
ANISOU 1805  O   LYS A 276     3577   3655   3552   -151    317   -808       O  
ATOM   1806  CB  LYS A 276      28.343  14.749 110.760  1.00 32.23           C  
ANISOU 1806  CB  LYS A 276     4386   3772   4085   -275    594   -846       C  
ATOM   1807  CG  LYS A 276      29.857  14.813 110.831  1.00 36.15           C  
ANISOU 1807  CG  LYS A 276     4506   4611   4619   -310    304   -988       C  
ATOM   1808  CD  LYS A 276      30.516  13.598 110.191  1.00 40.93           C  
ANISOU 1808  CD  LYS A 276     5145   5123   5282     70    479  -1092       C  
ATOM   1809  CE  LYS A 276      32.033  13.742 110.136  1.00 43.64           C  
ANISOU 1809  CE  LYS A 276     5250   5741   5588   -248    687   -972       C  
ATOM   1810  NZ  LYS A 276      32.464  15.003 109.465  1.00 45.44           N  
ANISOU 1810  NZ  LYS A 276     5736   5882   5648   -452    823   -951       N  
ATOM   1811  N   ASN A 277      25.625  15.823 109.262  1.00 35.40           N  
ANISOU 1811  N   ASN A 277     4341   5003   4107   -788  -1129     45       N  
ATOM   1812  CA  ASN A 277      24.235  15.447 109.084  1.00 33.15           C  
ANISOU 1812  CA  ASN A 277     4132   5235   3228   -578   -685   -254       C  
ATOM   1813  C   ASN A 277      24.099  13.937 109.000  1.00 32.00           C  
ANISOU 1813  C   ASN A 277     3939   5239   2980   -449   -393   -460       C  
ATOM   1814  O   ASN A 277      24.860  13.290 108.293  1.00 31.12           O  
ANISOU 1814  O   ASN A 277     3931   4920   2971   -475    -51   -111       O  
ATOM   1815  CB  ASN A 277      23.681  16.039 107.793  1.00 32.26           C  
ANISOU 1815  CB  ASN A 277     3829   5296   3132   -467   -390   -228       C  
ATOM   1816  CG  ASN A 277      23.639  17.543 107.829  1.00 33.16           C  
ANISOU 1816  CG  ASN A 277     4008   5282   3308   -433   -572   -198       C  
ATOM   1817  OD1 ASN A 277      22.671  18.114 108.314  1.00 32.12           O  
ANISOU 1817  OD1 ASN A 277     4518   4572   3113   -354   -197    102       O  
ATOM   1818  ND2 ASN A 277      24.685  18.192 107.325  1.00 34.61           N  
ANISOU 1818  ND2 ASN A 277     3842   5298   4010   -563   -840    -16       N  
ATOM   1819  N   ILE A 278      23.141  13.383 109.736  1.00 31.29           N  
ANISOU 1819  N   ILE A 278     4101   5077   2708   -538   -398   -540       N  
ATOM   1820  CA  ILE A 278      22.673  12.031 109.483  1.00 31.05           C  
ANISOU 1820  CA  ILE A 278     4048   5172   2575   -599   -231   -773       C  
ATOM   1821  C   ILE A 278      21.338  12.220 108.754  1.00 29.22           C  
ANISOU 1821  C   ILE A 278     3951   4604   2544   -573   -120   -616       C  
ATOM   1822  O   ILE A 278      20.298  12.388 109.385  1.00 28.20           O  
ANISOU 1822  O   ILE A 278     3946   3990   2778   -601    -11   -358       O  
ATOM   1823  CB  ILE A 278      22.499  11.198 110.785  1.00 32.47           C  
ANISOU 1823  CB  ILE A 278     4601   5169   2566   -496   -252   -767       C  
ATOM   1824  CG1 ILE A 278      23.735  11.284 111.718  1.00 35.09           C  
ANISOU 1824  CG1 ILE A 278     4921   5247   3163   -555   -619   -648       C  
ATOM   1825  CG2 ILE A 278      22.158   9.755 110.460  1.00 31.68           C  
ANISOU 1825  CG2 ILE A 278     4427   5168   2441   -472   -155   -786       C  
ATOM   1826  CD1 ILE A 278      25.056  10.948 111.055  1.00 37.03           C  
ANISOU 1826  CD1 ILE A 278     4792   5379   3898   -386   -683   -550       C  
ATOM   1827  N   TYR A 279      21.377  12.226 107.427  1.00 29.70           N  
ANISOU 1827  N   TYR A 279     3960   4788   2536   -789   -121   -740       N  
ATOM   1828  CA  TYR A 279      20.171  12.472 106.616  1.00 33.54           C  
ANISOU 1828  CA  TYR A 279     4110   5667   2967   -516   -285   -701       C  
ATOM   1829  C   TYR A 279      19.117  11.344 106.685  1.00 36.85           C  
ANISOU 1829  C   TYR A 279     4422   5961   3615   -814   -575   -813       C  
ATOM   1830  O   TYR A 279      17.923  11.610 106.599  1.00 38.61           O  
ANISOU 1830  O   TYR A 279     4459   5658   4552   -975  -1029   -739       O  
ATOM   1831  CB  TYR A 279      20.533  12.728 105.146  1.00 34.64           C  
ANISOU 1831  CB  TYR A 279     4542   5772   2849   -401   -339   -817       C  
ATOM   1832  CG  TYR A 279      21.328  14.000 104.877  1.00 34.42           C  
ANISOU 1832  CG  TYR A 279     4516   5742   2820   -318   -149   -735       C  
ATOM   1833  CD1 TYR A 279      20.876  15.248 105.323  1.00 33.73           C  
ANISOU 1833  CD1 TYR A 279     4259   5824   2732   -377   -243   -882       C  
ATOM   1834  CD2 TYR A 279      22.505  13.964 104.128  1.00 36.58           C  
ANISOU 1834  CD2 TYR A 279     4715   5872   3313   -121    141   -684       C  
ATOM   1835  CE1 TYR A 279      21.585  16.418 105.049  1.00 33.58           C  
ANISOU 1835  CE1 TYR A 279     4195   5742   2822   -298   -258   -893       C  
ATOM   1836  CE2 TYR A 279      23.222  15.127 103.846  1.00 37.22           C  
ANISOU 1836  CE2 TYR A 279     4835   5963   3343   -131    222   -449       C  
ATOM   1837  CZ  TYR A 279      22.759  16.356 104.314  1.00 35.83           C  
ANISOU 1837  CZ  TYR A 279     4488   5930   3194   -228     58   -436       C  
ATOM   1838  OH  TYR A 279      23.473  17.516 104.055  1.00 37.58           O  
ANISOU 1838  OH  TYR A 279     5352   5523   3403    -18   -129     85       O  
ATOM   1839  N   ARG A 280      19.552  10.100 106.848  1.00 37.55           N  
ANISOU 1839  N   ARG A 280     4822   6022   3423   -749   -572   -697       N  
ATOM   1840  CA  ARG A 280      18.627   8.964 106.929  1.00 41.73           C  
ANISOU 1840  CA  ARG A 280     5186   6367   4301  -1068   -718   -781       C  
ATOM   1841  C   ARG A 280      19.043   8.024 108.083  1.00 41.27           C  
ANISOU 1841  C   ARG A 280     5172   6224   4284   -981   -168   -659       C  
ATOM   1842  O   ARG A 280      19.879   7.132 107.891  1.00 40.27           O  
ANISOU 1842  O   ARG A 280     5483   5525   4291   -989   -528   -347       O  
ATOM   1843  CB  ARG A 280      18.500   8.247 105.580  1.00 46.03           C  
ANISOU 1843  CB  ARG A 280     6258   6568   4663  -1077  -1001  -1127       C  
ATOM   1844  CG  ARG A 280      19.764   8.226 104.751  1.00 47.16           C  
ANISOU 1844  CG  ARG A 280     6836   6733   4350   -766   -731  -1061       C  
ATOM   1845  CD  ARG A 280      19.507   7.876 103.292  1.00 52.64           C  
ANISOU 1845  CD  ARG A 280     8328   7125   4545   -610  -1306   -996       C  
ATOM   1846  NE  ARG A 280      20.794   7.695 102.623  1.00 53.57           N  
ANISOU 1846  NE  ARG A 280     9134   6910   4309    -15   -735   -787       N  
ATOM   1847  CZ  ARG A 280      20.972   7.345 101.355  1.00 57.79           C  
ANISOU 1847  CZ  ARG A 280    10676   6992   4287    290   -939   -890       C  
ATOM   1848  NH1 ARG A 280      19.940   7.140 100.540  1.00 64.35           N  
ANISOU 1848  NH1 ARG A 280    11747   7479   5223      1  -1777  -1342       N  
ATOM   1849  NH2 ARG A 280      22.212   7.214 100.895  1.00 60.20           N  
ANISOU 1849  NH2 ARG A 280    11255   7029   4586   1034   -317   -705       N  
ATOM   1850  N   PRO A 281      18.465   8.249 109.288  1.00 41.75           N  
ANISOU 1850  N   PRO A 281     5169   6259   4435  -1013     60   -580       N  
ATOM   1851  CA  PRO A 281      18.774   7.497 110.518  1.00 42.42           C  
ANISOU 1851  CA  PRO A 281     5399   6292   4424   -804    364   -548       C  
ATOM   1852  C   PRO A 281      18.685   5.972 110.391  1.00 43.71           C  
ANISOU 1852  C   PRO A 281     5656   6259   4693  -1111    199   -478       C  
ATOM   1853  O   PRO A 281      19.541   5.280 110.951  1.00 41.39           O  
ANISOU 1853  O   PRO A 281     6224   5203   4296  -1198    316   -446       O  
ATOM   1854  CB  PRO A 281      17.723   7.989 111.514  1.00 45.27           C  
ANISOU 1854  CB  PRO A 281     5727   6565   4909   -767    892   -361       C  
ATOM   1855  CG  PRO A 281      17.279   9.301 110.999  1.00 44.74           C  
ANISOU 1855  CG  PRO A 281     5300   6705   4992   -647    805   -366       C  
ATOM   1856  CD  PRO A 281      17.395   9.238 109.520  1.00 43.35           C  
ANISOU 1856  CD  PRO A 281     4997   6580   4892   -912    143   -425       C  
ATOM   1857  N   ASP A 282      17.670   5.466 109.682  1.00 45.98           N  
ANISOU 1857  N   ASP A 282     5687   6455   5327  -1345    -29   -420       N  
ATOM   1858  CA  ASP A 282      17.539   4.020 109.437  1.00 49.29           C  
ANISOU 1858  CA  ASP A 282     6273   6571   5882  -1531   -333   -539       C  
ATOM   1859  C   ASP A 282      18.787   3.483 108.752  1.00 47.50           C  
ANISOU 1859  C   ASP A 282     6577   6382   5087  -1372   -549   -805       C  
ATOM   1860  O   ASP A 282      19.428   2.568 109.248  1.00 48.43           O  
ANISOU 1860  O   ASP A 282     6893   6234   5274  -1259   -515   -889       O  
ATOM   1861  CB  ASP A 282      16.323   3.678 108.558  1.00 54.28           C  
ANISOU 1861  CB  ASP A 282     6569   6929   7123  -1990   -876   -430       C  
ATOM   1862  CG  ASP A 282      14.996   3.866 109.271  1.00 59.38           C  
ANISOU 1862  CG  ASP A 282     6467   7392   8702  -1961   -532     31       C  
ATOM   1863  OD1 ASP A 282      14.952   4.509 110.344  1.00 57.86           O  
ANISOU 1863  OD1 ASP A 282     6219   7272   8491  -2031   -397    249       O  
ATOM   1864  OD2 ASP A 282      13.977   3.353 108.747  1.00 67.41           O  
ANISOU 1864  OD2 ASP A 282     6944   8129  10537  -2332  -1278    315       O  
ATOM   1865  N   LYS A 283      19.131   4.072 107.616  1.00 46.98           N  
ANISOU 1865  N   LYS A 283     6765   6243   4840  -1381   -734   -979       N  
ATOM   1866  CA  LYS A 283      20.301   3.640 106.870  1.00 47.55           C  
ANISOU 1866  CA  LYS A 283     7362   6329   4373  -1021   -744  -1243       C  
ATOM   1867  C   LYS A 283      21.557   3.721 107.727  1.00 44.25           C  
ANISOU 1867  C   LYS A 283     7021   6096   3693   -692   -290  -1060       C  
ATOM   1868  O   LYS A 283      22.398   2.829 107.677  1.00 47.19           O  
ANISOU 1868  O   LYS A 283     7446   6195   4289   -406   -351   -960       O  
ATOM   1869  CB  LYS A 283      20.476   4.464 105.594  1.00 49.95           C  
ANISOU 1869  CB  LYS A 283     8054   6566   4358   -886   -978  -1078       C  
ATOM   1870  CG  LYS A 283      21.442   3.868 104.576  1.00 54.81           C  
ANISOU 1870  CG  LYS A 283     9253   7114   4456   -314   -686  -1101       C  
ATOM   1871  CD  LYS A 283      21.088   2.425 104.213  1.00 60.97           C  
ANISOU 1871  CD  LYS A 283    10873   7265   5026   -465  -1132  -1168       C  
ATOM   1872  CE  LYS A 283      21.598   2.008 102.838  1.00 67.83           C  
ANISOU 1872  CE  LYS A 283    12875   7888   5010     99   -934  -1056       C  
ATOM   1873  NZ  LYS A 283      22.990   2.469 102.563  1.00 70.01           N  
ANISOU 1873  NZ  LYS A 283    12906   8328   5364    642    -55   -557       N  
ATOM   1874  N   PHE A 284      21.666   4.786 108.518  1.00 40.34           N  
ANISOU 1874  N   PHE A 284     6233   5969   3124   -648   -115   -830       N  
ATOM   1875  CA  PHE A 284      22.771   4.948 109.455  1.00 39.46           C  
ANISOU 1875  CA  PHE A 284     5921   5796   3273   -493      4   -838       C  
ATOM   1876  C   PHE A 284      22.907   3.762 110.437  1.00 38.65           C  
ANISOU 1876  C   PHE A 284     5959   5330   3396   -618     74   -990       C  
ATOM   1877  O   PHE A 284      23.986   3.203 110.558  1.00 37.61           O  
ANISOU 1877  O   PHE A 284     6586   3915   3786   -384   -153   -950       O  
ATOM   1878  CB  PHE A 284      22.635   6.279 110.213  1.00 38.72           C  
ANISOU 1878  CB  PHE A 284     5657   5684   3367   -485     14   -795       C  
ATOM   1879  CG  PHE A 284      23.653   6.472 111.304  1.00 37.98           C  
ANISOU 1879  CG  PHE A 284     5787   5220   3422   -380   -117   -671       C  
ATOM   1880  CD1 PHE A 284      24.998   6.652 110.990  1.00 39.46           C  
ANISOU 1880  CD1 PHE A 284     5707   5440   3846   -217   -254   -301       C  
ATOM   1881  CD2 PHE A 284      23.267   6.490 112.641  1.00 39.86           C  
ANISOU 1881  CD2 PHE A 284     6369   5391   3384   -358    -89   -541       C  
ATOM   1882  CE1 PHE A 284      25.945   6.840 111.997  1.00 41.86           C  
ANISOU 1882  CE1 PHE A 284     6126   5698   4080   -267   -533   -422       C  
ATOM   1883  CE2 PHE A 284      24.204   6.680 113.653  1.00 42.02           C  
ANISOU 1883  CE2 PHE A 284     6851   5468   3646   -204   -457   -541       C  
ATOM   1884  CZ  PHE A 284      25.548   6.857 113.328  1.00 42.97           C  
ANISOU 1884  CZ  PHE A 284     6711   5687   3927   -131   -736   -307       C  
ATOM   1885  N   LEU A 285      21.829   3.390 111.119  1.00 38.84           N  
ANISOU 1885  N   LEU A 285     6246   5326   3183   -733    250  -1074       N  
ATOM   1886  CA  LEU A 285      21.866   2.252 112.057  1.00 41.15           C  
ANISOU 1886  CA  LEU A 285     6709   5560   3364   -744    392   -883       C  
ATOM   1887  C   LEU A 285      22.120   0.911 111.356  1.00 42.93           C  
ANISOU 1887  C   LEU A 285     7194   5525   3592   -728    202   -931       C  
ATOM   1888  O   LEU A 285      22.856   0.071 111.869  1.00 41.02           O  
ANISOU 1888  O   LEU A 285     7386   4855   3345   -748   -128  -1565       O  
ATOM   1889  CB  LEU A 285      20.571   2.163 112.854  1.00 43.38           C  
ANISOU 1889  CB  LEU A 285     6913   5672   3895   -968    707   -670       C  
ATOM   1890  CG  LEU A 285      20.356   3.210 113.939  1.00 44.61           C  
ANISOU 1890  CG  LEU A 285     7112   5902   3934   -708    991   -630       C  
ATOM   1891  CD1 LEU A 285      19.005   2.974 114.596  1.00 48.51           C  
ANISOU 1891  CD1 LEU A 285     7449   6183   4798   -690   1512   -291       C  
ATOM   1892  CD2 LEU A 285      21.473   3.176 114.980  1.00 45.13           C  
ANISOU 1892  CD2 LEU A 285     7727   5881   3539   -350    869   -678       C  
ATOM   1893  N   GLN A 286      21.498   0.722 110.194  1.00 46.13           N  
ANISOU 1893  N   GLN A 286     7483   6034   4010   -945   -164  -1044       N  
ATOM   1894  CA  GLN A 286      21.738  -0.467 109.353  1.00 49.79           C  
ANISOU 1894  CA  GLN A 286     8531   6170   4213   -829   -109  -1155       C  
ATOM   1895  C   GLN A 286      23.215  -0.601 108.995  1.00 48.77           C  
ANISOU 1895  C   GLN A 286     8693   6136   3699   -495    -29  -1130       C  
ATOM   1896  O   GLN A 286      23.796  -1.684 109.112  1.00 50.84           O  
ANISOU 1896  O   GLN A 286     9655   5914   3747   -411   -338  -1403       O  
ATOM   1897  CB  GLN A 286      20.896  -0.421 108.065  1.00 53.87           C  
ANISOU 1897  CB  GLN A 286     9222   6525   4721   -951   -662  -1122       C  
ATOM   1898  CG  GLN A 286      19.584  -1.208 108.114  1.00 60.99           C  
ANISOU 1898  CG  GLN A 286     9884   7077   6210  -1588   -987   -906       C  
ATOM   1899  CD  GLN A 286      18.492  -0.567 108.979  1.00 63.91           C  
ANISOU 1899  CD  GLN A 286     9304   7939   7038  -1798   -746   -884       C  
ATOM   1900  OE1 GLN A 286      18.763   0.025 110.034  1.00 62.56           O  
ANISOU 1900  OE1 GLN A 286     9275   7770   6724  -2271    -75   -778       O  
ATOM   1901  NE2 GLN A 286      17.238  -0.706 108.540  1.00 69.29           N  
ANISOU 1901  NE2 GLN A 286     9664   8164   8496  -2180  -1437   -623       N  
ATOM   1902  N   CYS A 287      23.817   0.511 108.584  1.00 47.30           N  
ANISOU 1902  N   CYS A 287     8306   6237   3428   -175    183   -698       N  
ATOM   1903  CA  CYS A 287      25.218   0.521 108.169  1.00 48.55           C  
ANISOU 1903  CA  CYS A 287     8457   6527   3460    308    453   -775       C  
ATOM   1904  C   CYS A 287      26.208   0.373 109.320  1.00 45.25           C  
ANISOU 1904  C   CYS A 287     7780   5916   3497    243    720   -584       C  
ATOM   1905  O   CYS A 287      27.294  -0.151 109.114  1.00 45.79           O  
ANISOU 1905  O   CYS A 287     8237   5655   3505    564   1126   -373       O  
ATOM   1906  CB  CYS A 287      25.517   1.756 107.307  1.00 50.53           C  
ANISOU 1906  CB  CYS A 287     8442   6648   4108    519   1004   -573       C  
ATOM   1907  SG  CYS A 287      24.737   1.614 105.671  1.00 58.22           S  
ANISOU 1907  SG  CYS A 287    10231   7424   4466   1180    242   -146       S  
ATOM   1908  N   VAL A 288      25.836   0.802 110.524  1.00 42.03           N  
ANISOU 1908  N   VAL A 288     7270   5313   3384     26    410   -607       N  
ATOM   1909  CA  VAL A 288      26.658   0.542 111.711  1.00 43.37           C  
ANISOU 1909  CA  VAL A 288     7284   5706   3487    107    303   -599       C  
ATOM   1910  C   VAL A 288      26.615  -0.952 112.068  1.00 44.98           C  
ANISOU 1910  C   VAL A 288     7913   5705   3470    267    368   -582       C  
ATOM   1911  O   VAL A 288      27.634  -1.520 112.466  1.00 43.53           O  
ANISOU 1911  O   VAL A 288     8439   4378   3720    386    480   -287       O  
ATOM   1912  CB  VAL A 288      26.217   1.400 112.917  1.00 43.24           C  
ANISOU 1912  CB  VAL A 288     7240   5758   3429    -37    -44   -777       C  
ATOM   1913  CG1 VAL A 288      26.977   1.012 114.182  1.00 45.18           C  
ANISOU 1913  CG1 VAL A 288     7803   5714   3648    188   -255   -626       C  
ATOM   1914  CG2 VAL A 288      26.432   2.887 112.622  1.00 42.50           C  
ANISOU 1914  CG2 VAL A 288     6799   5827   3519   -141   -203   -755       C  
ATOM   1915  N   LYS A 289      25.438  -1.565 111.912  1.00 45.92           N  
ANISOU 1915  N   LYS A 289     8200   5744   3501     22    479   -803       N  
ATOM   1916  CA  LYS A 289      25.211  -2.986 112.224  1.00 48.21           C  
ANISOU 1916  CA  LYS A 289     9102   5696   3518     54    386   -978       C  
ATOM   1917  C   LYS A 289      26.011  -3.871 111.266  1.00 49.48           C  
ANISOU 1917  C   LYS A 289     9719   5844   3236    285    355  -1000       C  
ATOM   1918  O   LYS A 289      26.756  -4.742 111.708  1.00 50.84           O  
ANISOU 1918  O   LYS A 289    10215   5393   3706    535    300  -1391       O  
ATOM   1919  CB  LYS A 289      23.709  -3.319 112.157  1.00 49.70           C  
ANISOU 1919  CB  LYS A 289     9306   5858   3718   -384    275  -1003       C  
ATOM   1920  CG  LYS A 289      23.287  -4.731 112.570  1.00 53.44           C  
ANISOU 1920  CG  LYS A 289    10300   5968   4036   -612    386   -957       C  
ATOM   1921  CD  LYS A 289      23.382  -4.963 114.073  1.00 54.81           C  
ANISOU 1921  CD  LYS A 289    10569   6161   4094   -449    761   -891       C  
ATOM   1922  CE  LYS A 289      22.383  -6.004 114.573  1.00 58.66           C  
ANISOU 1922  CE  LYS A 289    11265   6228   4793   -769    917   -814       C  
ATOM   1923  NZ  LYS A 289      22.634  -7.377 114.050  1.00 61.02           N  
ANISOU 1923  NZ  LYS A 289    12080   6273   4830   -727    739   -850       N  
ATOM   1924  N   ASN A 290      25.865  -3.622 109.968  1.00 49.85           N  
ANISOU 1924  N   ASN A 290     9747   5963   3230    356    445   -958       N  
ATOM   1925  CA  ASN A 290      26.622  -4.331 108.925  1.00 52.72           C  
ANISOU 1925  CA  ASN A 290    10720   5980   3330    815    714   -842       C  
ATOM   1926  C   ASN A 290      27.295  -3.341 107.958  1.00 52.66           C  
ANISOU 1926  C   ASN A 290    10638   6071   3296   1270    988   -701       C  
ATOM   1927  O   ASN A 290      26.662  -2.878 107.014  1.00 53.22           O  
ANISOU 1927  O   ASN A 290    11126   5711   3384   1540    698  -1060       O  
ATOM   1928  CB  ASN A 290      25.708  -5.299 108.170  1.00 54.85           C  
ANISOU 1928  CB  ASN A 290    11917   5894   3028    674    477  -1007       C  
ATOM   1929  CG  ASN A 290      26.487  -6.318 107.331  1.00 60.31           C  
ANISOU 1929  CG  ASN A 290    13393   6052   3469   1262    848   -953       C  
ATOM   1930  OD1 ASN A 290      27.560  -6.027 106.792  1.00 61.04           O  
ANISOU 1930  OD1 ASN A 290    13612   5555   4025   2078   1633   -948       O  
ATOM   1931  ND2 ASN A 290      25.939  -7.523 107.220  1.00 63.86           N  
ANISOU 1931  ND2 ASN A 290    14644   6022   3597   1113    535  -1282       N  
ATOM   1932  N   PRO A 291      28.581  -3.010 108.195  1.00 54.75           N  
ANISOU 1932  N   PRO A 291    10235   6586   3979   1570   1397   -286       N  
ATOM   1933  CA  PRO A 291      29.283  -2.055 107.319  1.00 57.52           C  
ANISOU 1933  CA  PRO A 291    10210   7012   4631   1806   1790    123       C  
ATOM   1934  C   PRO A 291      29.488  -2.438 105.839  1.00 64.22           C  
ANISOU 1934  C   PRO A 291    12026   7616   4757   2374   2359    210       C  
ATOM   1935  O   PRO A 291      29.634  -1.535 105.013  1.00 68.32           O  
ANISOU 1935  O   PRO A 291    12223   8020   5715   2434   2461    776       O  
ATOM   1936  CB  PRO A 291      30.643  -1.887 108.010  1.00 59.08           C  
ANISOU 1936  CB  PRO A 291     9688   7284   5473   2058   1959    559       C  
ATOM   1937  CG  PRO A 291      30.373  -2.171 109.439  1.00 55.60           C  
ANISOU 1937  CG  PRO A 291     9081   6940   5104   1695   1352    131       C  
ATOM   1938  CD  PRO A 291      29.334  -3.253 109.443  1.00 54.47           C  
ANISOU 1938  CD  PRO A 291     9724   6635   4334   1541   1263   -237       C  
ATOM   1939  N   GLU A 292      29.499  -3.728 105.501  1.00 69.72           N  
ANISOU 1939  N   GLU A 292    13543   7660   5285   2701   2593     81       N  
ATOM   1940  CA  GLU A 292      29.806  -4.164 104.122  1.00 76.14           C  
ANISOU 1940  CA  GLU A 292    15756   7833   5341   3498   2999    262       C  
ATOM   1941  C   GLU A 292      28.710  -3.802 103.106  1.00 79.91           C  
ANISOU 1941  C   GLU A 292    16802   8365   5193   3213   2271   -267       C  
ATOM   1942  O   GLU A 292      27.529  -4.092 103.307  1.00 82.12           O  
ANISOU 1942  O   GLU A 292    16933   8639   5629   2138   1364  -1170       O  
ATOM   1943  CB  GLU A 292      30.096  -5.669 104.078  1.00 76.47           C  
ANISOU 1943  CB  GLU A 292    16444   7910   4698   3805   3053    197       C  
ATOM   1944  CG  GLU A 292      31.446  -6.057 104.673  1.00 77.98           C  
ANISOU 1944  CG  GLU A 292    16044   8077   5509   4275   3741    749       C  
ATOM   1945  CD  GLU A 292      31.644  -7.564 104.782  1.00 81.95           C  
ANISOU 1945  CD  GLU A 292    17211   8137   5787   4721   3925    610       C  
ATOM   1946  OE1 GLU A 292      31.094  -8.173 105.728  1.00 81.65           O  
ANISOU 1946  OE1 GLU A 292    16878   7932   6210   3965   3297    741       O  
ATOM   1947  OE2 GLU A 292      32.366  -8.138 103.933  1.00 91.72           O  
ANISOU 1947  OE2 GLU A 292    19038   9602   6208   5379   4629    749       O  
ATOM   1948  N   CYS A 296      26.526  -0.915 101.531  1.00 86.62           N  
ANISOU 1948  N   CYS A 296    17322   9363   6223   2527   1602   -971       N  
ATOM   1949  CA  CYS A 296      25.553   0.106 101.901  1.00 79.37           C  
ANISOU 1949  CA  CYS A 296    16062   8791   5300   1879   1038   -765       C  
ATOM   1950  C   CYS A 296      26.214   1.481 102.005  1.00 77.52           C  
ANISOU 1950  C   CYS A 296    14649   9076   5729   1783   1613   -187       C  
ATOM   1951  O   CYS A 296      26.200   2.259 101.051  1.00 80.41           O  
ANISOU 1951  O   CYS A 296    15084   9355   6113   1576   1176    173       O  
ATOM   1952  CB  CYS A 296      24.872  -0.266 103.227  1.00 73.40           C  
ANISOU 1952  CB  CYS A 296    14415   8492   4978   1075     53   -938       C  
ATOM   1953  SG  CYS A 296      25.796   0.125 104.736  1.00 68.15           S  
ANISOU 1953  SG  CYS A 296    13472   8103   4319   1494    734  -1283       S  
TER    1954      CYS A 296                                                      
ATOM   1955  N   ASP B   1      22.936 -10.830 110.535  1.00 61.91           N  
ANISOU 1955  N   ASP B   1     7355   6330   9836    990   -423  -1105       N  
ATOM   1956  CA  ASP B   1      23.478 -12.112 109.999  1.00 60.22           C  
ANISOU 1956  CA  ASP B   1     7076   6303   9498    862   -499  -1088       C  
ATOM   1957  C   ASP B   1      25.002 -12.019 109.927  1.00 53.80           C  
ANISOU 1957  C   ASP B   1     7080   5501   7859    739   -456   -893       C  
ATOM   1958  O   ASP B   1      25.547 -11.008 109.479  1.00 52.35           O  
ANISOU 1958  O   ASP B   1     7047   5318   7523    801   -518   -937       O  
ATOM   1959  CB  ASP B   1      22.889 -12.416 108.605  1.00 66.34           C  
ANISOU 1959  CB  ASP B   1     7922   7159  10124   1034  -1314  -1286       C  
ATOM   1960  CG  ASP B   1      22.300 -13.820 108.499  1.00 71.96           C  
ANISOU 1960  CG  ASP B   1     8372   7252  11716    890  -1401  -1431       C  
ATOM   1961  OD1 ASP B   1      21.619 -14.265 109.452  1.00 74.52           O  
ANISOU 1961  OD1 ASP B   1     8047   7639  12628    878  -1024  -1222       O  
ATOM   1962  OD2 ASP B   1      22.488 -14.469 107.443  1.00 78.38           O  
ANISOU 1962  OD2 ASP B   1     9227   8817  11734   1482  -1225  -1687       O  
ATOM   1963  N   VAL B   2      25.677 -13.081 110.359  1.00 49.99           N  
ANISOU 1963  N   VAL B   2     6413   5370   7209    538   -235  -1015       N  
ATOM   1964  CA  VAL B   2      27.134 -13.084 110.479  1.00 46.76           C  
ANISOU 1964  CA  VAL B   2     6375   4879   6509    385    -63   -916       C  
ATOM   1965  C   VAL B   2      27.721 -14.349 109.802  1.00 44.18           C  
ANISOU 1965  C   VAL B   2     6111   4902   5770    150    -62   -940       C  
ATOM   1966  O   VAL B   2      27.150 -15.437 109.906  1.00 43.32           O  
ANISOU 1966  O   VAL B   2     5918   4741   5798    220    108  -1783       O  
ATOM   1967  CB  VAL B   2      27.544 -12.909 111.977  1.00 46.35           C  
ANISOU 1967  CB  VAL B   2     6313   4889   6405    317    185   -955       C  
ATOM   1968  CG1 VAL B   2      27.278 -14.161 112.803  1.00 45.50           C  
ANISOU 1968  CG1 VAL B   2     6035   4955   6296    332    524   -998       C  
ATOM   1969  CG2 VAL B   2      28.996 -12.483 112.109  1.00 46.58           C  
ANISOU 1969  CG2 VAL B   2     6505   4819   6373    144    -33  -1020       C  
ATOM   1970  N   GLN B   3      28.846 -14.188 109.102  1.00 42.53           N  
ANISOU 1970  N   GLN B   3     6229   4704   5225    266   -127   -740       N  
ATOM   1971  CA  GLN B   3      29.495 -15.292 108.381  1.00 41.93           C  
ANISOU 1971  CA  GLN B   3     6071   4909   4951    425   -223   -655       C  
ATOM   1972  C   GLN B   3      30.630 -15.732 109.265  1.00 37.11           C  
ANISOU 1972  C   GLN B   3     5686   4269   4145     50    230   -493       C  
ATOM   1973  O   GLN B   3      31.435 -14.896 109.672  1.00 36.39           O  
ANISOU 1973  O   GLN B   3     5767   3994   4063   -101    457   -171       O  
ATOM   1974  CB  GLN B   3      30.057 -14.875 107.004  1.00 46.81           C  
ANISOU 1974  CB  GLN B   3     7146   5706   4931    866    -93   -260       C  
ATOM   1975  CG  GLN B   3      29.365 -13.710 106.319  1.00 52.16           C  
ANISOU 1975  CG  GLN B   3     7977   6280   5560   1306   -294      0       C  
ATOM   1976  CD  GLN B   3      27.865 -13.894 106.234  1.00 54.19           C  
ANISOU 1976  CD  GLN B   3     8052   6488   6049   1434   -906   -536       C  
ATOM   1977  OE1 GLN B   3      27.381 -14.957 105.816  1.00 58.85           O  
ANISOU 1977  OE1 GLN B   3     9289   6768   6302   1277  -1463   -832       O  
ATOM   1978  NE2 GLN B   3      27.115 -12.870 106.637  1.00 54.53           N  
ANISOU 1978  NE2 GLN B   3     8036   6193   6489   1338  -1054   -606       N  
ATOM   1979  N   LEU B   4      30.710 -17.023 109.558  1.00 34.37           N  
ANISOU 1979  N   LEU B   4     5103   4052   3903    -37    143   -899       N  
ATOM   1980  CA  LEU B   4      31.703 -17.536 110.509  1.00 31.71           C  
ANISOU 1980  CA  LEU B   4     4763   3649   3637   -266    422   -801       C  
ATOM   1981  C   LEU B   4      32.731 -18.437 109.818  1.00 31.85           C  
ANISOU 1981  C   LEU B   4     4868   3907   3326   -183    501   -728       C  
ATOM   1982  O   LEU B   4      32.387 -19.209 108.914  1.00 32.10           O  
ANISOU 1982  O   LEU B   4     4820   4251   3123    155    551   -926       O  
ATOM   1983  CB  LEU B   4      30.990 -18.277 111.642  1.00 30.89           C  
ANISOU 1983  CB  LEU B   4     4423   3576   3736   -294    486   -947       C  
ATOM   1984  CG  LEU B   4      30.051 -17.408 112.492  1.00 31.83           C  
ANISOU 1984  CG  LEU B   4     4380   3555   4159   -139    602   -840       C  
ATOM   1985  CD1 LEU B   4      29.278 -18.253 113.484  1.00 33.85           C  
ANISOU 1985  CD1 LEU B   4     4400   3825   4635     -1    973   -702       C  
ATOM   1986  CD2 LEU B   4      30.814 -16.310 113.225  1.00 31.89           C  
ANISOU 1986  CD2 LEU B   4     4694   3548   3873    -35    585   -932       C  
ATOM   1987  N   GLN B   5      33.988 -18.333 110.245  1.00 31.76           N  
ANISOU 1987  N   GLN B   5     4878   3928   3261   -399    586   -535       N  
ATOM   1988  CA  GLN B   5      35.065 -19.137 109.661  1.00 34.30           C  
ANISOU 1988  CA  GLN B   5     5140   4371   3520   -147    769   -423       C  
ATOM   1989  C   GLN B   5      36.048 -19.637 110.731  1.00 31.57           C  
ANISOU 1989  C   GLN B   5     4654   4011   3330   -543    905   -527       C  
ATOM   1990  O   GLN B   5      36.795 -18.855 111.297  1.00 31.52           O  
ANISOU 1990  O   GLN B   5     4833   3825   3318   -602   1204   -692       O  
ATOM   1991  CB  GLN B   5      35.771 -18.320 108.569  1.00 40.00           C  
ANISOU 1991  CB  GLN B   5     5941   5153   4103    -31   1098    211       C  
ATOM   1992  CG  GLN B   5      36.616 -19.128 107.613  1.00 45.53           C  
ANISOU 1992  CG  GLN B   5     6825   6156   4317    586   1436    300       C  
ATOM   1993  CD  GLN B   5      35.817 -20.181 106.841  1.00 50.13           C  
ANISOU 1993  CD  GLN B   5     7921   6893   4233    831    670   -183       C  
ATOM   1994  OE1 GLN B   5      35.184 -19.882 105.820  1.00 58.88           O  
ANISOU 1994  OE1 GLN B   5     9551   8690   4130   1596    149   -587       O  
ATOM   1995  NE2 GLN B   5      35.849 -21.424 107.327  1.00 48.96           N  
ANISOU 1995  NE2 GLN B   5     7901   6439   4261    774    512   -732       N  
ATOM   1996  N   GLU B   6      36.024 -20.949 110.999  1.00 30.28           N  
ANISOU 1996  N   GLU B   6     4665   3924   2914   -369    736   -796       N  
ATOM   1997  CA  GLU B   6      36.894 -21.587 111.998  1.00 28.49           C  
ANISOU 1997  CA  GLU B   6     4289   3725   2809   -546    868   -770       C  
ATOM   1998  C   GLU B   6      38.245 -21.915 111.403  1.00 29.08           C  
ANISOU 1998  C   GLU B   6     4317   3837   2894   -475    931   -616       C  
ATOM   1999  O   GLU B   6      38.362 -22.078 110.204  1.00 31.65           O  
ANISOU 1999  O   GLU B   6     4395   4738   2890     68   1092   -441       O  
ATOM   2000  CB  GLU B   6      36.312 -22.915 112.513  1.00 27.68           C  
ANISOU 2000  CB  GLU B   6     4209   3611   2694   -543    822   -957       C  
ATOM   2001  CG  GLU B   6      34.917 -22.854 113.090  1.00 28.80           C  
ANISOU 2001  CG  GLU B   6     4162   3630   3150   -556    879   -853       C  
ATOM   2002  CD  GLU B   6      33.823 -23.057 112.070  1.00 29.91           C  
ANISOU 2002  CD  GLU B   6     4212   3591   3560   -531    695  -1032       C  
ATOM   2003  OE1 GLU B   6      34.076 -22.830 110.872  1.00 32.06           O  
ANISOU 2003  OE1 GLU B   6     4323   4217   3640   -433    714   -738       O  
ATOM   2004  OE2 GLU B   6      32.693 -23.435 112.459  1.00 31.11           O  
ANISOU 2004  OE2 GLU B   6     4279   3204   4338   -450    914   -826       O  
ATOM   2005  N   SER B   7      39.252 -22.031 112.262  1.00 29.02           N  
ANISOU 2005  N   SER B   7     4227   3670   3129   -601    871   -651       N  
ATOM   2006  CA  SER B   7      40.538 -22.627 111.909  1.00 30.29           C  
ANISOU 2006  CA  SER B   7     4162   3969   3377   -590    970   -485       C  
ATOM   2007  C   SER B   7      41.252 -23.079 113.181  1.00 29.32           C  
ANISOU 2007  C   SER B   7     3956   3706   3476   -637    825   -679       C  
ATOM   2008  O   SER B   7      40.730 -22.903 114.282  1.00 28.05           O  
ANISOU 2008  O   SER B   7     3990   3364   3303   -234    603   -696       O  
ATOM   2009  CB  SER B   7      41.403 -21.640 111.128  1.00 34.99           C  
ANISOU 2009  CB  SER B   7     4407   4373   4513   -591   1256     66       C  
ATOM   2010  OG  SER B   7      41.735 -20.530 111.936  1.00 38.57           O  
ANISOU 2010  OG  SER B   7     4696   4195   5764   -618    898   -130       O  
ATOM   2011  N   GLY B   8      42.437 -23.664 113.026  1.00 30.25           N  
ANISOU 2011  N   GLY B   8     3910   3769   3811   -645    844   -655       N  
ATOM   2012  CA  GLY B   8      43.270 -24.049 114.160  1.00 31.31           C  
ANISOU 2012  CA  GLY B   8     3932   3862   4100   -600    536   -862       C  
ATOM   2013  C   GLY B   8      43.119 -25.498 114.563  1.00 29.51           C  
ANISOU 2013  C   GLY B   8     4028   3832   3353   -442    553  -1007       C  
ATOM   2014  O   GLY B   8      43.821 -25.964 115.463  1.00 30.96           O  
ANISOU 2014  O   GLY B   8     4160   4084   3519   -287    249  -1263       O  
ATOM   2015  N   GLY B   9      42.221 -26.230 113.904  1.00 28.37           N  
ANISOU 2015  N   GLY B   9     3962   3877   2938   -520    771   -936       N  
ATOM   2016  CA  GLY B   9      42.144 -27.690 114.089  1.00 28.91           C  
ANISOU 2016  CA  GLY B   9     4189   3895   2899   -335    792   -921       C  
ATOM   2017  C   GLY B   9      43.424 -28.369 113.645  1.00 30.32           C  
ANISOU 2017  C   GLY B   9     4226   4155   3136   -240    815   -974       C  
ATOM   2018  O   GLY B   9      44.297 -27.740 113.043  1.00 31.23           O  
ANISOU 2018  O   GLY B   9     4123   4381   3360   -312    762   -828       O  
ATOM   2019  N   GLY B  10      43.544 -29.654 113.951  1.00 32.09           N  
ANISOU 2019  N   GLY B  10     4524   4194   3472   -125    713   -951       N  
ATOM   2020  CA  GLY B  10      44.737 -30.406 113.562  1.00 33.56           C  
ANISOU 2020  CA  GLY B  10     4609   4512   3630     18    778  -1042       C  
ATOM   2021  C   GLY B  10      44.817 -31.795 114.155  1.00 33.96           C  
ANISOU 2021  C   GLY B  10     4746   4433   3721     75    648  -1116       C  
ATOM   2022  O   GLY B  10      43.883 -32.265 114.812  1.00 32.65           O  
ANISOU 2022  O   GLY B  10     4890   4077   3437    126    599  -1055       O  
ATOM   2023  N   LEU B  11      45.948 -32.444 113.892  1.00 36.03           N  
ANISOU 2023  N   LEU B  11     4872   4764   4051    277    664  -1180       N  
ATOM   2024  CA  LEU B  11      46.298 -33.736 114.471  1.00 38.26           C  
ANISOU 2024  CA  LEU B  11     5197   4793   4548    422    509  -1143       C  
ATOM   2025  C   LEU B  11      47.262 -33.470 115.622  1.00 39.17           C  
ANISOU 2025  C   LEU B  11     5267   4818   4798    403    365  -1225       C  
ATOM   2026  O   LEU B  11      48.335 -32.926 115.394  1.00 40.04           O  
ANISOU 2026  O   LEU B  11     5037   4849   5326    529    431  -1571       O  
ATOM   2027  CB  LEU B  11      46.980 -34.628 113.422  1.00 40.60           C  
ANISOU 2027  CB  LEU B  11     5425   5127   4873    677    475  -1405       C  
ATOM   2028  CG  LEU B  11      47.498 -36.005 113.872  1.00 42.93           C  
ANISOU 2028  CG  LEU B  11     5674   5203   5433    841    322  -1408       C  
ATOM   2029  CD1 LEU B  11      46.352 -36.992 114.006  1.00 44.56           C  
ANISOU 2029  CD1 LEU B  11     5960   4923   6046    752    106  -1404       C  
ATOM   2030  CD2 LEU B  11      48.540 -36.537 112.896  1.00 45.94           C  
ANISOU 2030  CD2 LEU B  11     5940   5736   5778   1279    302  -1715       C  
ATOM   2031  N   VAL B  12      46.885 -33.863 116.839  1.00 41.38           N  
ANISOU 2031  N   VAL B  12     5898   5002   4822    656    353   -963       N  
ATOM   2032  CA  VAL B  12      47.760 -33.742 118.012  1.00 45.94           C  
ANISOU 2032  CA  VAL B  12     6413   5836   5203   1013   -137   -953       C  
ATOM   2033  C   VAL B  12      47.757 -34.994 118.882  1.00 49.80           C  
ANISOU 2033  C   VAL B  12     7284   6244   5393   1377     61   -599       C  
ATOM   2034  O   VAL B  12      46.833 -35.806 118.823  1.00 48.12           O  
ANISOU 2034  O   VAL B  12     7210   6196   4877   1377    273     -5       O  
ATOM   2035  CB  VAL B  12      47.396 -32.530 118.901  1.00 47.92           C  
ANISOU 2035  CB  VAL B  12     6937   6169   5100   1289   -307  -1064       C  
ATOM   2036  CG1 VAL B  12      47.791 -31.228 118.216  1.00 47.84           C  
ANISOU 2036  CG1 VAL B  12     6544   6138   5494    837   -472  -1262       C  
ATOM   2037  CG2 VAL B  12      45.916 -32.528 119.272  1.00 47.41           C  
ANISOU 2037  CG2 VAL B  12     7190   6194   4628   1366    146   -658       C  
ATOM   2038  N   GLN B  13      48.811 -35.133 119.686  1.00 47.33           N  
ANISOU 2038  N   GLN B  13     7644   4976   5361   2025    226   -574       N  
ATOM   2039  CA  GLN B  13      48.932 -36.250 120.627  1.00 50.48           C  
ANISOU 2039  CA  GLN B  13     8447   5084   5649   2299    187   -471       C  
ATOM   2040  C   GLN B  13      48.053 -35.988 121.832  1.00 49.53           C  
ANISOU 2040  C   GLN B  13     8378   4929   5509   2324    101   -412       C  
ATOM   2041  O   GLN B  13      47.860 -34.837 122.213  1.00 47.53           O  
ANISOU 2041  O   GLN B  13     7960   4958   5140   2756   -343   -276       O  
ATOM   2042  CB  GLN B  13      50.389 -36.449 121.082  1.00 53.70           C  
ANISOU 2042  CB  GLN B  13     8640   5524   6239   2556   -104   -618       C  
ATOM   2043  CG  GLN B  13      51.219 -37.307 120.151  1.00 57.01           C  
ANISOU 2043  CG  GLN B  13     8868   6041   6751   2870    179   -583       C  
ATOM   2044  CD  GLN B  13      50.944 -38.797 120.328  1.00 62.04           C  
ANISOU 2044  CD  GLN B  13     9798   6073   7701   2878    141   -488       C  
ATOM   2045  OE1 GLN B  13      49.801 -39.253 120.218  1.00 66.02           O  
ANISOU 2045  OE1 GLN B  13     9842   7005   8238   2634    483   -694       O  
ATOM   2046  NE2 GLN B  13      51.994 -39.566 120.601  1.00 65.72           N  
ANISOU 2046  NE2 GLN B  13    10089   6560   8319   3162   -115   -361       N  
ATOM   2047  N   ALA B  14      47.534 -37.056 122.433  1.00 50.98           N  
ANISOU 2047  N   ALA B  14     8858   4863   5648   2378    201   -322       N  
ATOM   2048  CA  ALA B  14      46.794 -36.947 123.693  1.00 51.88           C  
ANISOU 2048  CA  ALA B  14     9319   4855   5536   2281    251   -296       C  
ATOM   2049  C   ALA B  14      47.651 -36.250 124.747  1.00 53.08           C  
ANISOU 2049  C   ALA B  14     9303   5220   5641   2447      8   -287       C  
ATOM   2050  O   ALA B  14      48.860 -36.486 124.835  1.00 53.53           O  
ANISOU 2050  O   ALA B  14     9461   5332   5543   2904   -269   -596       O  
ATOM   2051  CB  ALA B  14      46.362 -38.317 124.188  1.00 53.65           C  
ANISOU 2051  CB  ALA B  14     9954   4788   5641   2333    432   -265       C  
ATOM   2052  N   GLY B  15      47.019 -35.369 125.519  1.00 53.34           N  
ANISOU 2052  N   GLY B  15     9531   5143   5590   2231     92   -362       N  
ATOM   2053  CA  GLY B  15      47.708 -34.572 126.529  1.00 54.77           C  
ANISOU 2053  CA  GLY B  15     9588   5540   5680   2374   -286   -336       C  
ATOM   2054  C   GLY B  15      48.207 -33.220 126.046  1.00 53.87           C  
ANISOU 2054  C   GLY B  15     9155   5595   5718   2177   -469   -414       C  
ATOM   2055  O   GLY B  15      48.528 -32.368 126.870  1.00 53.93           O  
ANISOU 2055  O   GLY B  15     9140   6223   5127   2250   -992   -315       O  
ATOM   2056  N   HIS B  16      48.261 -33.009 124.727  1.00 51.76           N  
ANISOU 2056  N   HIS B  16     8551   5411   5702   2117   -192   -512       N  
ATOM   2057  CA  HIS B  16      48.786 -31.761 124.160  1.00 51.07           C  
ANISOU 2057  CA  HIS B  16     8036   5556   5811   2052   -401   -445       C  
ATOM   2058  C   HIS B  16      47.668 -30.720 124.008  1.00 47.34           C  
ANISOU 2058  C   HIS B  16     7500   5181   5305   1681   -176   -633       C  
ATOM   2059  O   HIS B  16      46.526 -30.976 124.400  1.00 44.57           O  
ANISOU 2059  O   HIS B  16     7480   5120   4335   1748   -292   -679       O  
ATOM   2060  CB  HIS B  16      49.501 -32.034 122.826  1.00 52.24           C  
ANISOU 2060  CB  HIS B  16     8002   5713   6134   2159   -195   -644       C  
ATOM   2061  CG  HIS B  16      50.851 -32.663 122.982  1.00 56.82           C  
ANISOU 2061  CG  HIS B  16     8145   6381   7061   2369   -417   -539       C  
ATOM   2062  ND1 HIS B  16      51.074 -33.783 123.757  1.00 58.97           N  
ANISOU 2062  ND1 HIS B  16     8758   6634   7014   2553   -461   -432       N  
ATOM   2063  CD2 HIS B  16      52.050 -32.333 122.446  1.00 58.61           C  
ANISOU 2063  CD2 HIS B  16     8044   6680   7545   2355   -370   -596       C  
ATOM   2064  CE1 HIS B  16      52.353 -34.109 123.700  1.00 60.80           C  
ANISOU 2064  CE1 HIS B  16     8889   6768   7445   2897   -559   -637       C  
ATOM   2065  NE2 HIS B  16      52.967 -33.245 122.912  1.00 61.31           N  
ANISOU 2065  NE2 HIS B  16     8418   6963   7914   2783   -354   -730       N  
ATOM   2066  N   SER B  17      48.021 -29.547 123.468  1.00 46.20           N  
ANISOU 2066  N   SER B  17     7035   5189   5329   1670   -331   -579       N  
ATOM   2067  CA  SER B  17      47.101 -28.426 123.277  1.00 43.92           C  
ANISOU 2067  CA  SER B  17     6679   4936   5073   1405   -183   -576       C  
ATOM   2068  C   SER B  17      46.879 -28.061 121.812  1.00 41.42           C  
ANISOU 2068  C   SER B  17     6100   4667   4968   1110    -36   -651       C  
ATOM   2069  O   SER B  17      47.738 -28.303 120.962  1.00 40.34           O  
ANISOU 2069  O   SER B  17     5801   4470   5057    780    -90   -643       O  
ATOM   2070  CB  SER B  17      47.642 -27.186 123.986  1.00 45.64           C  
ANISOU 2070  CB  SER B  17     6614   5265   5462   1321   -477   -721       C  
ATOM   2071  OG  SER B  17      47.607 -27.364 125.382  1.00 50.73           O  
ANISOU 2071  OG  SER B  17     7568   6141   5565   1471   -601   -655       O  
ATOM   2072  N   LEU B  18      45.708 -27.489 121.543  1.00 38.99           N  
ANISOU 2072  N   LEU B  18     5935   4458   4418    980    116   -642       N  
ATOM   2073  CA  LEU B  18      45.405 -26.785 120.292  1.00 37.86           C  
ANISOU 2073  CA  LEU B  18     5595   4108   4680    911    243   -512       C  
ATOM   2074  C   LEU B  18      44.543 -25.605 120.661  1.00 35.35           C  
ANISOU 2074  C   LEU B  18     5525   3806   4098    619    354   -627       C  
ATOM   2075  O   LEU B  18      43.703 -25.719 121.547  1.00 34.02           O  
ANISOU 2075  O   LEU B  18     5549   3449   3928    905    342   -353       O  
ATOM   2076  CB  LEU B  18      44.568 -27.627 119.317  1.00 37.79           C  
ANISOU 2076  CB  LEU B  18     5673   4049   4634    812    376   -593       C  
ATOM   2077  CG  LEU B  18      45.153 -28.714 118.431  1.00 39.08           C  
ANISOU 2077  CG  LEU B  18     5939   4288   4620    854    469   -624       C  
ATOM   2078  CD1 LEU B  18      44.008 -29.503 117.801  1.00 38.02           C  
ANISOU 2078  CD1 LEU B  18     5979   4057   4407    935    462   -593       C  
ATOM   2079  CD2 LEU B  18      46.073 -28.130 117.370  1.00 39.42           C  
ANISOU 2079  CD2 LEU B  18     5863   4436   4677    852    468   -476       C  
ATOM   2080  N   ARG B  19      44.716 -24.506 119.935  1.00 34.57           N  
ANISOU 2080  N   ARG B  19     5305   3827   4003    538    241   -594       N  
ATOM   2081  CA  ARG B  19      43.885 -23.322 120.085  1.00 34.21           C  
ANISOU 2081  CA  ARG B  19     4922   3905   4170    486    306   -526       C  
ATOM   2082  C   ARG B  19      43.060 -23.140 118.815  1.00 32.42           C  
ANISOU 2082  C   ARG B  19     4673   3747   3895    342    580   -624       C  
ATOM   2083  O   ARG B  19      43.622 -22.911 117.750  1.00 30.52           O  
ANISOU 2083  O   ARG B  19     3915   3811   3867    663    607   -896       O  
ATOM   2084  CB  ARG B  19      44.780 -22.105 120.296  1.00 36.46           C  
ANISOU 2084  CB  ARG B  19     5039   4223   4589    312    180   -689       C  
ATOM   2085  CG  ARG B  19      44.056 -20.807 120.647  1.00 38.18           C  
ANISOU 2085  CG  ARG B  19     5299   4317   4887    428    268   -578       C  
ATOM   2086  CD  ARG B  19      45.077 -19.690 120.795  1.00 40.87           C  
ANISOU 2086  CD  ARG B  19     5456   4711   5361    176    165   -839       C  
ATOM   2087  NE  ARG B  19      44.487 -18.368 121.009  1.00 43.87           N  
ANISOU 2087  NE  ARG B  19     5972   4908   5788    449    139   -719       N  
ATOM   2088  CZ  ARG B  19      44.015 -17.903 122.172  1.00 45.63           C  
ANISOU 2088  CZ  ARG B  19     6146   5359   5831    510    222   -639       C  
ATOM   2089  NH1 ARG B  19      43.993 -18.658 123.272  1.00 46.94           N  
ANISOU 2089  NH1 ARG B  19     6669   5588   5577    480   -332   -725       N  
ATOM   2090  NH2 ARG B  19      43.529 -16.662 122.231  1.00 47.08           N  
ANISOU 2090  NH2 ARG B  19     6588   5064   6235    171    131   -910       N  
ATOM   2091  N   LEU B  20      41.735 -23.234 118.921  1.00 30.81           N  
ANISOU 2091  N   LEU B  20     4672   3337   3696    273    455   -526       N  
ATOM   2092  CA  LEU B  20      40.858 -22.941 117.789  1.00 30.04           C  
ANISOU 2092  CA  LEU B  20     4600   3313   3499    186    572   -523       C  
ATOM   2093  C   LEU B  20      40.502 -21.454 117.755  1.00 29.87           C  
ANISOU 2093  C   LEU B  20     4618   3193   3537    -37    568   -492       C  
ATOM   2094  O   LEU B  20      40.395 -20.812 118.804  1.00 28.83           O  
ANISOU 2094  O   LEU B  20     4379   2952   3620   -323    468   -515       O  
ATOM   2095  CB  LEU B  20      39.582 -23.785 117.845  1.00 30.04           C  
ANISOU 2095  CB  LEU B  20     4765   3157   3489     99    576   -496       C  
ATOM   2096  CG  LEU B  20      39.739 -25.282 118.137  1.00 30.53           C  
ANISOU 2096  CG  LEU B  20     4886   3202   3510    181    523   -452       C  
ATOM   2097  CD1 LEU B  20      38.402 -25.986 117.985  1.00 30.32           C  
ANISOU 2097  CD1 LEU B  20     5071   3022   3426     30    497   -415       C  
ATOM   2098  CD2 LEU B  20      40.792 -25.933 117.256  1.00 31.40           C  
ANISOU 2098  CD2 LEU B  20     5057   3270   3601    309    452   -703       C  
ATOM   2099  N   SER B  21      40.321 -20.932 116.540  1.00 29.21           N  
ANISOU 2099  N   SER B  21     4329   3258   3509      1    637   -522       N  
ATOM   2100  CA  SER B  21      39.856 -19.572 116.283  1.00 29.90           C  
ANISOU 2100  CA  SER B  21     4433   3314   3614     27    651   -406       C  
ATOM   2101  C   SER B  21      38.662 -19.598 115.350  1.00 30.61           C  
ANISOU 2101  C   SER B  21     4384   3369   3877     49    603   -408       C  
ATOM   2102  O   SER B  21      38.527 -20.495 114.518  1.00 32.92           O  
ANISOU 2102  O   SER B  21     4478   3770   4258    342    400   -710       O  
ATOM   2103  CB  SER B  21      40.934 -18.753 115.592  1.00 31.51           C  
ANISOU 2103  CB  SER B  21     4489   3437   4044    -38    746   -342       C  
ATOM   2104  OG  SER B  21      42.052 -18.613 116.425  1.00 34.74           O  
ANISOU 2104  OG  SER B  21     4822   3631   4746   -214    424   -357       O  
ATOM   2105  N   CYS B  22      37.827 -18.579 115.460  1.00 28.81           N  
ANISOU 2105  N   CYS B  22     4215   3095   3636   -168    698   -386       N  
ATOM   2106  CA  CYS B  22      36.727 -18.378 114.541  1.00 29.04           C  
ANISOU 2106  CA  CYS B  22     4463   3149   3420   -141    630   -500       C  
ATOM   2107  C   CYS B  22      36.558 -16.885 114.313  1.00 29.09           C  
ANISOU 2107  C   CYS B  22     4457   3262   3330    -18    684   -325       C  
ATOM   2108  O   CYS B  22      36.298 -16.133 115.273  1.00 29.37           O  
ANISOU 2108  O   CYS B  22     4578   3079   3503    -45    306   -560       O  
ATOM   2109  CB  CYS B  22      35.460 -18.973 115.136  1.00 30.01           C  
ANISOU 2109  CB  CYS B  22     4583   3225   3594   -326    569   -322       C  
ATOM   2110  SG  CYS B  22      33.921 -18.559 114.300  1.00 33.46           S  
ANISOU 2110  SG  CYS B  22     4726   3597   4390   -244    349     41       S  
ATOM   2111  N   VAL B  23      36.717 -16.467 113.058  1.00 29.54           N  
ANISOU 2111  N   VAL B  23     4818   3242   3163    151    756   -490       N  
ATOM   2112  CA  VAL B  23      36.552 -15.073 112.638  1.00 28.95           C  
ANISOU 2112  CA  VAL B  23     4470   3248   3279     68    833   -332       C  
ATOM   2113  C   VAL B  23      35.154 -14.870 112.065  1.00 28.80           C  
ANISOU 2113  C   VAL B  23     4574   3183   3185    123    722   -379       C  
ATOM   2114  O   VAL B  23      34.685 -15.683 111.264  1.00 29.02           O  
ANISOU 2114  O   VAL B  23     5109   2651   3266    411    682   -377       O  
ATOM   2115  CB  VAL B  23      37.573 -14.671 111.553  1.00 30.05           C  
ANISOU 2115  CB  VAL B  23     4672   3312   3432    115    954   -130       C  
ATOM   2116  CG1 VAL B  23      37.494 -13.172 111.264  1.00 29.45           C  
ANISOU 2116  CG1 VAL B  23     4636   3275   3277    -24   1009    -62       C  
ATOM   2117  CG2 VAL B  23      38.981 -15.063 111.982  1.00 31.00           C  
ANISOU 2117  CG2 VAL B  23     4586   3475   3715     47    982   -218       C  
ATOM   2118  N   GLY B  24      34.500 -13.782 112.471  1.00 28.24           N  
ANISOU 2118  N   GLY B  24     4530   2879   3317    -52    627   -382       N  
ATOM   2119  CA  GLY B  24      33.191 -13.400 111.938  1.00 28.87           C  
ANISOU 2119  CA  GLY B  24     4658   3149   3162    100    531   -463       C  
ATOM   2120  C   GLY B  24      33.304 -12.201 111.014  1.00 31.99           C  
ANISOU 2120  C   GLY B  24     5301   3618   3236    215    661   -162       C  
ATOM   2121  O   GLY B  24      34.190 -11.364 111.194  1.00 34.38           O  
ANISOU 2121  O   GLY B  24     5625   3684   3754     66    441    314       O  
ATOM   2122  N   SER B  25      32.414 -12.120 110.026  1.00 33.02           N  
ANISOU 2122  N   SER B  25     5347   3740   3457    241    538   -376       N  
ATOM   2123  CA  SER B  25      32.280 -10.948 109.151  1.00 34.91           C  
ANISOU 2123  CA  SER B  25     5798   3918   3547    499    573   -266       C  
ATOM   2124  C   SER B  25      30.799 -10.727 108.887  1.00 35.54           C  
ANISOU 2124  C   SER B  25     5924   4144   3434    550    242   -433       C  
ATOM   2125  O   SER B  25      29.976 -11.545 109.290  1.00 37.14           O  
ANISOU 2125  O   SER B  25     6051   4139   3918    269     43   -617       O  
ATOM   2126  CB  SER B  25      33.079 -11.115 107.852  1.00 37.54           C  
ANISOU 2126  CB  SER B  25     6323   4274   3665    569    804   -137       C  
ATOM   2127  OG  SER B  25      32.741 -12.312 107.171  1.00 39.82           O  
ANISOU 2127  OG  SER B  25     7007   4533   3588    844   1218   -634       O  
ATOM   2128  N   GLY B  26      30.460  -9.613 108.248  1.00 36.64           N  
ANISOU 2128  N   GLY B  26     6254   4300   3365    726    383   -343       N  
ATOM   2129  CA  GLY B  26      29.065  -9.171 108.130  1.00 38.63           C  
ANISOU 2129  CA  GLY B  26     6303   4679   3693    806     81   -414       C  
ATOM   2130  C   GLY B  26      28.705  -8.311 109.335  1.00 38.79           C  
ANISOU 2130  C   GLY B  26     6182   4400   4155    634    450   -453       C  
ATOM   2131  O   GLY B  26      29.403  -7.342 109.639  1.00 40.53           O  
ANISOU 2131  O   GLY B  26     6426   4268   4705    484    506   -329       O  
ATOM   2132  N   SER B  27      27.636  -8.679 110.042  1.00 37.42           N  
ANISOU 2132  N   SER B  27     5854   4384   3980    669    186   -598       N  
ATOM   2133  CA  SER B  27      27.183  -7.923 111.203  1.00 34.49           C  
ANISOU 2133  CA  SER B  27     5347   3886   3871    627     88   -453       C  
ATOM   2134  C   SER B  27      28.243  -7.866 112.299  1.00 32.79           C  
ANISOU 2134  C   SER B  27     5234   3605   3617    440    332   -354       C  
ATOM   2135  O   SER B  27      29.143  -8.715 112.355  1.00 34.42           O  
ANISOU 2135  O   SER B  27     5752   3429   3896    579    526      5       O  
ATOM   2136  CB  SER B  27      25.885  -8.498 111.751  1.00 34.00           C  
ANISOU 2136  CB  SER B  27     5226   3919   3772    583    -52   -565       C  
ATOM   2137  OG  SER B  27      24.849  -8.368 110.793  1.00 36.09           O  
ANISOU 2137  OG  SER B  27     5557   4178   3977    588   -348   -972       O  
ATOM   2138  N   ARG B  28      28.148  -6.836 113.141  1.00 30.47           N  
ANISOU 2138  N   ARG B  28     4792   3328   3456    366    275   -165       N  
ATOM   2139  CA  ARG B  28      29.133  -6.572 114.186  1.00 28.42           C  
ANISOU 2139  CA  ARG B  28     4541   2900   3356    145    485   -187       C  
ATOM   2140  C   ARG B  28      29.252  -7.757 115.122  1.00 27.11           C  
ANISOU 2140  C   ARG B  28     4204   2809   3287     34    410   -289       C  
ATOM   2141  O   ARG B  28      28.238  -8.213 115.656  1.00 25.53           O  
ANISOU 2141  O   ARG B  28     4018   2582   3097    330    412   -219       O  
ATOM   2142  CB  ARG B  28      28.741  -5.337 115.008  1.00 28.03           C  
ANISOU 2142  CB  ARG B  28     4420   2932   3298     92    543   -189       C  
ATOM   2143  CG  ARG B  28      29.083  -4.000 114.357  1.00 28.35           C  
ANISOU 2143  CG  ARG B  28     4619   2779   3372    399    550    -99       C  
ATOM   2144  CD  ARG B  28      28.714  -2.868 115.292  1.00 28.10           C  
ANISOU 2144  CD  ARG B  28     4595   2741   3338    290    649    -52       C  
ATOM   2145  NE  ARG B  28      29.543  -2.796 116.488  1.00 26.53           N  
ANISOU 2145  NE  ARG B  28     4312   2434   3333    168    763   -254       N  
ATOM   2146  CZ  ARG B  28      30.681  -2.110 116.613  1.00 27.70           C  
ANISOU 2146  CZ  ARG B  28     4428   2572   3525     25    804    -57       C  
ATOM   2147  NH1 ARG B  28      31.201  -1.420 115.611  1.00 30.18           N  
ANISOU 2147  NH1 ARG B  28     4733   3098   3634     63    912    167       N  
ATOM   2148  NH2 ARG B  28      31.323  -2.109 117.775  1.00 27.86           N  
ANISOU 2148  NH2 ARG B  28     4333   2555   3695   -113    676     25       N  
ATOM   2149  N   PHE B  29      30.489  -8.231 115.314  1.00 26.58           N  
ANISOU 2149  N   PHE B  29     4085   2682   3331    -50    554   -426       N  
ATOM   2150  CA  PHE B  29      30.787  -9.395 116.166  1.00 26.30           C  
ANISOU 2150  CA  PHE B  29     4033   2810   3147   -127    567   -376       C  
ATOM   2151  C   PHE B  29      30.316  -9.200 117.601  1.00 26.34           C  
ANISOU 2151  C   PHE B  29     4013   2761   3233   -199    622   -415       C  
ATOM   2152  O   PHE B  29      29.847 -10.151 118.235  1.00 27.76           O  
ANISOU 2152  O   PHE B  29     4182   3079   3287   -262   1259   -506       O  
ATOM   2153  CB  PHE B  29      32.296  -9.670 116.173  1.00 26.38           C  
ANISOU 2153  CB  PHE B  29     3996   2785   3240   -305    709   -389       C  
ATOM   2154  CG  PHE B  29      32.665 -11.081 116.491  1.00 26.50           C  
ANISOU 2154  CG  PHE B  29     4034   2920   3113    -74    678   -311       C  
ATOM   2155  CD1 PHE B  29      32.381 -12.110 115.591  1.00 28.28           C  
ANISOU 2155  CD1 PHE B  29     4257   3043   3443   -186    313   -368       C  
ATOM   2156  CD2 PHE B  29      33.362 -11.383 117.647  1.00 26.91           C  
ANISOU 2156  CD2 PHE B  29     4096   2964   3161   -128    543   -525       C  
ATOM   2157  CE1 PHE B  29      32.751 -13.420 115.878  1.00 29.23           C  
ANISOU 2157  CE1 PHE B  29     4529   3109   3466    -80    289   -421       C  
ATOM   2158  CE2 PHE B  29      33.725 -12.687 117.949  1.00 27.80           C  
ANISOU 2158  CE2 PHE B  29     4319   2940   3302   -151    491   -423       C  
ATOM   2159  CZ  PHE B  29      33.425 -13.709 117.064  1.00 28.71           C  
ANISOU 2159  CZ  PHE B  29     4483   3031   3393   -250    293   -421       C  
ATOM   2160  N   ASP B  30      30.428  -7.967 118.097  1.00 26.19           N  
ANISOU 2160  N   ASP B  30     3940   2721   3288   -323    564   -397       N  
ATOM   2161  CA  ASP B  30      30.066  -7.647 119.474  1.00 25.86           C  
ANISOU 2161  CA  ASP B  30     3849   2657   3318   -209    612   -366       C  
ATOM   2162  C   ASP B  30      28.561  -7.623 119.733  1.00 25.79           C  
ANISOU 2162  C   ASP B  30     3835   2699   3265   -286    557   -473       C  
ATOM   2163  O   ASP B  30      28.157  -7.383 120.859  1.00 26.98           O  
ANISOU 2163  O   ASP B  30     3942   2954   3355     98    666   -477       O  
ATOM   2164  CB  ASP B  30      30.730  -6.330 119.945  1.00 26.53           C  
ANISOU 2164  CB  ASP B  30     4005   2694   3380   -289    660   -404       C  
ATOM   2165  CG  ASP B  30      30.185  -5.068 119.247  1.00 28.11           C  
ANISOU 2165  CG  ASP B  30     4235   2733   3710   -154    585   -408       C  
ATOM   2166  OD1 ASP B  30      29.274  -5.126 118.388  1.00 28.47           O  
ANISOU 2166  OD1 ASP B  30     4343   2820   3655    250    515   -603       O  
ATOM   2167  OD2 ASP B  30      30.700  -3.979 119.572  1.00 28.88           O  
ANISOU 2167  OD2 ASP B  30     4340   2565   4065   -116    828   -440       O  
ATOM   2168  N   ASN B  31      27.745  -7.832 118.698  1.00 25.30           N  
ANISOU 2168  N   ASN B  31     3851   2506   3256   -149    519   -571       N  
ATOM   2169  CA  ASN B  31      26.313  -8.081 118.864  1.00 25.89           C  
ANISOU 2169  CA  ASN B  31     3775   2743   3317    -10    455   -654       C  
ATOM   2170  C   ASN B  31      25.948  -9.552 119.114  1.00 25.82           C  
ANISOU 2170  C   ASN B  31     3683   2830   3294   -197    400   -751       C  
ATOM   2171  O   ASN B  31      24.781  -9.849 119.338  1.00 27.94           O  
ANISOU 2171  O   ASN B  31     3634   3380   3599   -179    350   -900       O  
ATOM   2172  CB  ASN B  31      25.526  -7.568 117.650  1.00 26.93           C  
ANISOU 2172  CB  ASN B  31     3885   2933   3413     -2    304   -708       C  
ATOM   2173  CG  ASN B  31      25.478  -6.054 117.562  1.00 27.98           C  
ANISOU 2173  CG  ASN B  31     4094   2990   3545    129    385   -468       C  
ATOM   2174  OD1 ASN B  31      24.492  -5.508 117.086  1.00 31.19           O  
ANISOU 2174  OD1 ASN B  31     4259   3527   4064    415    316   -453       O  
ATOM   2175  ND2 ASN B  31      26.531  -5.371 118.012  1.00 27.38           N  
ANISOU 2175  ND2 ASN B  31     4102   2669   3631     39    483   -251       N  
ATOM   2176  N   TYR B  32      26.923 -10.465 119.100  1.00 25.49           N  
ANISOU 2176  N   TYR B  32     3638   2732   3315   -257    430   -802       N  
ATOM   2177  CA  TYR B  32      26.635 -11.905 119.144  1.00 25.93           C  
ANISOU 2177  CA  TYR B  32     3679   2775   3398   -302    419   -753       C  
ATOM   2178  C   TYR B  32      27.257 -12.623 120.335  1.00 24.88           C  
ANISOU 2178  C   TYR B  32     3682   2515   3256   -325    617   -770       C  
ATOM   2179  O   TYR B  32      28.435 -12.415 120.661  1.00 26.30           O  
ANISOU 2179  O   TYR B  32     3709   2695   3588   -364    582   -607       O  
ATOM   2180  CB  TYR B  32      27.082 -12.571 117.821  1.00 26.67           C  
ANISOU 2180  CB  TYR B  32     3801   2918   3415   -146    449   -726       C  
ATOM   2181  CG  TYR B  32      26.282 -12.038 116.667  1.00 27.27           C  
ANISOU 2181  CG  TYR B  32     3812   3099   3448    -78    371   -753       C  
ATOM   2182  CD1 TYR B  32      25.084 -12.632 116.282  1.00 28.76           C  
ANISOU 2182  CD1 TYR B  32     3938   3345   3643   -123    260   -958       C  
ATOM   2183  CD2 TYR B  32      26.674 -10.882 116.030  1.00 28.16           C  
ANISOU 2183  CD2 TYR B  32     3965   3190   3543    -21    351   -582       C  
ATOM   2184  CE1 TYR B  32      24.311 -12.094 115.255  1.00 31.32           C  
ANISOU 2184  CE1 TYR B  32     4241   3774   3884    -31     95   -766       C  
ATOM   2185  CE2 TYR B  32      25.924 -10.329 115.007  1.00 30.33           C  
ANISOU 2185  CE2 TYR B  32     4393   3462   3666      1     29   -668       C  
ATOM   2186  CZ  TYR B  32      24.742 -10.928 114.622  1.00 32.31           C  
ANISOU 2186  CZ  TYR B  32     4416   3698   4160    -13   -112   -684       C  
ATOM   2187  OH  TYR B  32      24.026 -10.365 113.590  1.00 35.15           O  
ANISOU 2187  OH  TYR B  32     5035   3738   4579    149   -419   -488       O  
ATOM   2188  N   ALA B  33      26.441 -13.450 120.988  1.00 24.55           N  
ANISOU 2188  N   ALA B  33     3516   2467   3343   -372    639   -920       N  
ATOM   2189  CA  ALA B  33      26.935 -14.520 121.838  1.00 25.79           C  
ANISOU 2189  CA  ALA B  33     3774   2673   3352   -534    704   -649       C  
ATOM   2190  C   ALA B  33      27.537 -15.600 120.939  1.00 25.96           C  
ANISOU 2190  C   ALA B  33     3855   2521   3488   -547    655   -649       C  
ATOM   2191  O   ALA B  33      26.932 -15.977 119.941  1.00 27.78           O  
ANISOU 2191  O   ALA B  33     4208   2607   3741   -329    392   -884       O  
ATOM   2192  CB  ALA B  33      25.807 -15.103 122.669  1.00 27.09           C  
ANISOU 2192  CB  ALA B  33     3812   2798   3681   -598    878   -762       C  
ATOM   2193  N   MET B  34      28.730 -16.079 121.281  1.00 26.56           N  
ANISOU 2193  N   MET B  34     3894   2688   3507   -511    636   -544       N  
ATOM   2194  CA  MET B  34      29.434 -17.066 120.454  1.00 27.90           C  
ANISOU 2194  CA  MET B  34     4267   2919   3414   -509    693   -637       C  
ATOM   2195  C   MET B  34      29.504 -18.417 121.150  1.00 29.14           C  
ANISOU 2195  C   MET B  34     4583   2858   3629   -387    626   -612       C  
ATOM   2196  O   MET B  34      29.663 -18.475 122.358  1.00 29.16           O  
ANISOU 2196  O   MET B  34     4756   2744   3578   -341    811   -673       O  
ATOM   2197  CB  MET B  34      30.850 -16.577 120.116  1.00 28.05           C  
ANISOU 2197  CB  MET B  34     4151   3122   3381   -536    527   -601       C  
ATOM   2198  CG  MET B  34      30.884 -15.288 119.299  1.00 28.69           C  
ANISOU 2198  CG  MET B  34     4241   3119   3540   -392    639   -529       C  
ATOM   2199  SD  MET B  34      30.032 -15.389 117.706  1.00 30.33           S  
ANISOU 2199  SD  MET B  34     4498   3275   3751   -213    454   -507       S  
ATOM   2200  CE  MET B  34      31.056 -16.605 116.883  1.00 29.95           C  
ANISOU 2200  CE  MET B  34     4458   3392   3527   -260    443   -595       C  
ATOM   2201  N   GLY B  35      29.387 -19.490 120.373  1.00 29.40           N  
ANISOU 2201  N   GLY B  35     4513   2917   3737   -492    429   -650       N  
ATOM   2202  CA  GLY B  35      29.406 -20.855 120.900  1.00 29.74           C  
ANISOU 2202  CA  GLY B  35     4576   2909   3814   -563    787   -670       C  
ATOM   2203  C   GLY B  35      30.287 -21.780 120.082  1.00 29.80           C  
ANISOU 2203  C   GLY B  35     4671   2920   3728   -398    711   -575       C  
ATOM   2204  O   GLY B  35      30.375 -21.655 118.861  1.00 29.83           O  
ANISOU 2204  O   GLY B  35     4745   2904   3684   -279    506   -489       O  
ATOM   2205  N   TRP B  36      30.958 -22.697 120.766  1.00 28.87           N  
ANISOU 2205  N   TRP B  36     4684   2666   3619   -489    885   -550       N  
ATOM   2206  CA  TRP B  36      31.661 -23.785 120.118  1.00 28.70           C  
ANISOU 2206  CA  TRP B  36     4744   2589   3570   -515    788   -631       C  
ATOM   2207  C   TRP B  36      30.869 -25.068 120.371  1.00 29.19           C  
ANISOU 2207  C   TRP B  36     4816   2600   3674   -596    936   -710       C  
ATOM   2208  O   TRP B  36      30.427 -25.315 121.499  1.00 28.04           O  
ANISOU 2208  O   TRP B  36     4997   1979   3676   -937    911   -747       O  
ATOM   2209  CB  TRP B  36      33.084 -23.913 120.654  1.00 28.90           C  
ANISOU 2209  CB  TRP B  36     4814   2635   3530   -324    770   -771       C  
ATOM   2210  CG  TRP B  36      34.005 -22.881 120.145  1.00 28.89           C  
ANISOU 2210  CG  TRP B  36     4709   2755   3510   -270    728   -599       C  
ATOM   2211  CD1 TRP B  36      34.359 -21.719 120.775  1.00 28.57           C  
ANISOU 2211  CD1 TRP B  36     4563   2790   3502   -364    710   -528       C  
ATOM   2212  CD2 TRP B  36      34.697 -22.883 118.894  1.00 29.26           C  
ANISOU 2212  CD2 TRP B  36     4748   2894   3476   -274    676   -616       C  
ATOM   2213  NE1 TRP B  36      35.227 -21.003 119.993  1.00 28.19           N  
ANISOU 2213  NE1 TRP B  36     4544   2754   3410   -372    714   -574       N  
ATOM   2214  CE2 TRP B  36      35.462 -21.696 118.838  1.00 28.13           C  
ANISOU 2214  CE2 TRP B  36     4631   2805   3251   -208    531   -482       C  
ATOM   2215  CE3 TRP B  36      34.755 -23.777 117.814  1.00 30.61           C  
ANISOU 2215  CE3 TRP B  36     4978   3099   3551   -292    699   -688       C  
ATOM   2216  CZ2 TRP B  36      36.279 -21.376 117.749  1.00 27.86           C  
ANISOU 2216  CZ2 TRP B  36     4426   2815   3343    -27    574   -510       C  
ATOM   2217  CZ3 TRP B  36      35.564 -23.459 116.729  1.00 30.54           C  
ANISOU 2217  CZ3 TRP B  36     4982   3142   3478   -189    661   -561       C  
ATOM   2218  CH2 TRP B  36      36.311 -22.258 116.705  1.00 29.59           C  
ANISOU 2218  CH2 TRP B  36     4709   3130   3404   -101    588   -651       C  
ATOM   2219  N   PHE B  37      30.653 -25.831 119.300  1.00 29.11           N  
ANISOU 2219  N   PHE B  37     4763   2531   3765   -500   1016   -826       N  
ATOM   2220  CA  PHE B  37      30.049 -27.160 119.343  1.00 31.02           C  
ANISOU 2220  CA  PHE B  37     5089   2621   4075   -641   1037   -842       C  
ATOM   2221  C   PHE B  37      31.004 -28.138 118.674  1.00 31.13           C  
ANISOU 2221  C   PHE B  37     5151   2567   4109   -566    968   -768       C  
ATOM   2222  O   PHE B  37      31.950 -27.739 117.986  1.00 30.02           O  
ANISOU 2222  O   PHE B  37     5055   2681   3670   -264   1004   -866       O  
ATOM   2223  CB  PHE B  37      28.728 -27.199 118.577  1.00 32.55           C  
ANISOU 2223  CB  PHE B  37     5047   2796   4522   -799    966   -967       C  
ATOM   2224  CG  PHE B  37      27.630 -26.383 119.197  1.00 33.81           C  
ANISOU 2224  CG  PHE B  37     5067   2933   4847   -787   1061   -966       C  
ATOM   2225  CD1 PHE B  37      26.558 -27.002 119.841  1.00 35.42           C  
ANISOU 2225  CD1 PHE B  37     5323   2995   5138   -929   1240  -1007       C  
ATOM   2226  CD2 PHE B  37      27.638 -24.992 119.104  1.00 32.97           C  
ANISOU 2226  CD2 PHE B  37     4996   2922   4609   -868    955  -1066       C  
ATOM   2227  CE1 PHE B  37      25.536 -26.249 120.402  1.00 36.09           C  
ANISOU 2227  CE1 PHE B  37     5128   3134   5449  -1011   1289  -1025       C  
ATOM   2228  CE2 PHE B  37      26.614 -24.236 119.658  1.00 33.97           C  
ANISOU 2228  CE2 PHE B  37     4810   3065   5032   -867   1036   -875       C  
ATOM   2229  CZ  PHE B  37      25.563 -24.861 120.310  1.00 35.06           C  
ANISOU 2229  CZ  PHE B  37     4957   3151   5212   -995   1210   -999       C  
ATOM   2230  N   ARG B  38      30.749 -29.423 118.858  1.00 31.92           N  
ANISOU 2230  N   ARG B  38     5404   2523   4198   -676   1044   -981       N  
ATOM   2231  CA  ARG B  38      31.532 -30.425 118.192  1.00 32.20           C  
ANISOU 2231  CA  ARG B  38     5516   2486   4232   -537    973   -960       C  
ATOM   2232  C   ARG B  38      30.672 -31.633 117.855  1.00 34.95           C  
ANISOU 2232  C   ARG B  38     5748   2681   4849   -751   1116  -1065       C  
ATOM   2233  O   ARG B  38      29.681 -31.902 118.528  1.00 35.17           O  
ANISOU 2233  O   ARG B  38     5840   2540   4980   -731   1352  -1327       O  
ATOM   2234  CB  ARG B  38      32.737 -30.817 119.036  1.00 31.10           C  
ANISOU 2234  CB  ARG B  38     5647   2179   3988   -473   1021   -900       C  
ATOM   2235  CG  ARG B  38      32.409 -31.606 120.282  1.00 32.88           C  
ANISOU 2235  CG  ARG B  38     5999   2346   4145   -415   1237   -830       C  
ATOM   2236  CD  ARG B  38      33.657 -31.861 121.103  1.00 32.97           C  
ANISOU 2236  CD  ARG B  38     6220   2271   4035   -179   1226   -671       C  
ATOM   2237  NE  ARG B  38      33.329 -32.525 122.360  1.00 34.12           N  
ANISOU 2237  NE  ARG B  38     6670   1922   4371   -244   1418   -510       N  
ATOM   2238  CZ  ARG B  38      34.199 -32.792 123.334  1.00 36.59           C  
ANISOU 2238  CZ  ARG B  38     7004   2594   4305   -167   1362   -310       C  
ATOM   2239  NH1 ARG B  38      35.484 -32.458 123.230  1.00 36.49           N  
ANISOU 2239  NH1 ARG B  38     6898   2787   4179     10   1292   -153       N  
ATOM   2240  NH2 ARG B  38      33.777 -33.408 124.430  1.00 39.67           N  
ANISOU 2240  NH2 ARG B  38     7535   2984   4553   -331   1626   -175       N  
ATOM   2241  N   GLN B  39      31.081 -32.347 116.809  1.00 37.01           N  
ANISOU 2241  N   GLN B  39     6195   3067   4800   -618    992  -1269       N  
ATOM   2242  CA  GLN B  39      30.408 -33.557 116.371  1.00 40.63           C  
ANISOU 2242  CA  GLN B  39     6706   3089   5639   -762   1084  -1375       C  
ATOM   2243  C   GLN B  39      31.479 -34.579 116.032  1.00 42.42           C  
ANISOU 2243  C   GLN B  39     7045   3372   5698   -461   1102  -1354       C  
ATOM   2244  O   GLN B  39      32.273 -34.365 115.114  1.00 39.37           O  
ANISOU 2244  O   GLN B  39     7000   3116   4842   -124    860  -2106       O  
ATOM   2245  CB  GLN B  39      29.524 -33.261 115.158  1.00 42.37           C  
ANISOU 2245  CB  GLN B  39     6690   3528   5878   -730    848  -1556       C  
ATOM   2246  CG  GLN B  39      28.774 -34.469 114.610  1.00 46.86           C  
ANISOU 2246  CG  GLN B  39     7140   3854   6810  -1073    830  -1716       C  
ATOM   2247  CD  GLN B  39      27.594 -34.075 113.727  1.00 50.04           C  
ANISOU 2247  CD  GLN B  39     7271   4321   7420  -1135    429  -1767       C  
ATOM   2248  OE1 GLN B  39      27.619 -33.043 113.056  1.00 50.95           O  
ANISOU 2248  OE1 GLN B  39     7151   4745   7460  -1339   -271  -1456       O  
ATOM   2249  NE2 GLN B  39      26.553 -34.890 113.734  1.00 53.14           N  
ANISOU 2249  NE2 GLN B  39     7602   4412   8177  -1386    378  -2008       N  
ATOM   2250  N   ALA B  40      31.531 -35.657 116.814  1.00 45.87           N  
ANISOU 2250  N   ALA B  40     7750   3303   6372   -741   1288  -1153       N  
ATOM   2251  CA  ALA B  40      32.404 -36.795 116.528  1.00 48.51           C  
ANISOU 2251  CA  ALA B  40     8195   3705   6531   -359   1304  -1232       C  
ATOM   2252  C   ALA B  40      31.736 -37.623 115.434  1.00 52.34           C  
ANISOU 2252  C   ALA B  40     8535   4104   7244   -580   1193  -1658       C  
ATOM   2253  O   ALA B  40      30.516 -37.502 115.241  1.00 51.71           O  
ANISOU 2253  O   ALA B  40     8283   3817   7544   -546   1813  -2340       O  
ATOM   2254  CB  ALA B  40      32.616 -37.632 117.781  1.00 50.74           C  
ANISOU 2254  CB  ALA B  40     8618   3737   6923   -387   1280   -905       C  
ATOM   2255  N   PRO B  41      32.519 -38.464 114.710  1.00 54.48           N  
ANISOU 2255  N   PRO B  41     8975   4237   7487   -293   1230  -1653       N  
ATOM   2256  CA  PRO B  41      31.951 -39.210 113.583  1.00 56.04           C  
ANISOU 2256  CA  PRO B  41     9258   4259   7774   -480   1071  -1794       C  
ATOM   2257  C   PRO B  41      30.877 -40.198 114.036  1.00 57.55           C  
ANISOU 2257  C   PRO B  41     9592   4042   8229   -624   1225  -1939       C  
ATOM   2258  O   PRO B  41      31.080 -40.920 115.019  1.00 57.36           O  
ANISOU 2258  O   PRO B  41    10642   2714   8438   -993   1373  -2098       O  
ATOM   2259  CB  PRO B  41      33.163 -39.962 112.994  1.00 57.26           C  
ANISOU 2259  CB  PRO B  41     9436   4657   7662   -278   1077  -1765       C  
ATOM   2260  CG  PRO B  41      34.372 -39.314 113.587  1.00 54.82           C  
ANISOU 2260  CG  PRO B  41     9373   4261   7193   -142   1073  -1567       C  
ATOM   2261  CD  PRO B  41      33.936 -38.815 114.928  1.00 53.77           C  
ANISOU 2261  CD  PRO B  41     9067   4264   7100   -200   1212  -1259       C  
ATOM   2262  N   GLY B  42      29.739 -40.195 113.343  1.00 58.51           N  
ANISOU 2262  N   GLY B  42     9629   3943   8656   -697   1047  -2323       N  
ATOM   2263  CA  GLY B  42      28.607 -41.059 113.691  1.00 63.98           C  
ANISOU 2263  CA  GLY B  42     9952   4735   9621  -1151   1197  -2209       C  
ATOM   2264  C   GLY B  42      27.907 -40.768 115.015  1.00 63.96           C  
ANISOU 2264  C   GLY B  42     9898   4600   9801  -1651   1685  -1852       C  
ATOM   2265  O   GLY B  42      27.132 -41.594 115.488  1.00 73.15           O  
ANISOU 2265  O   GLY B  42    10704   5295  11793  -1808   1429  -1207       O  
ATOM   2266  N   LYS B  43      28.167 -39.602 115.604  1.00 63.94           N  
ANISOU 2266  N   LYS B  43     9958   4798   9536  -1350   1538  -1952       N  
ATOM   2267  CA  LYS B  43      27.565 -39.179 116.873  1.00 63.54           C  
ANISOU 2267  CA  LYS B  43     9868   4758   9516  -1360   1711  -1509       C  
ATOM   2268  C   LYS B  43      26.838 -37.856 116.651  1.00 60.93           C  
ANISOU 2268  C   LYS B  43     9318   4561   9270  -1522   1592  -1933       C  
ATOM   2269  O   LYS B  43      26.972 -37.230 115.595  1.00 58.26           O  
ANISOU 2269  O   LYS B  43     9383   3574   9179  -1592    768  -2112       O  
ATOM   2270  CB  LYS B  43      28.647 -39.020 117.951  1.00 63.31           C  
ANISOU 2270  CB  LYS B  43    10052   4833   9170  -1323   1746  -1328       C  
ATOM   2271  CG  LYS B  43      29.037 -40.317 118.663  1.00 65.47           C  
ANISOU 2271  CG  LYS B  43    10566   4755   9555  -1156   1978  -1299       C  
ATOM   2272  CD  LYS B  43      27.976 -40.825 119.640  1.00 68.71           C  
ANISOU 2272  CD  LYS B  43    11031   4980  10094  -1329   2317  -1246       C  
ATOM   2273  CE  LYS B  43      27.552 -39.761 120.651  1.00 68.72           C  
ANISOU 2273  CE  LYS B  43    10886   5036  10187  -1349   2470  -1206       C  
ATOM   2274  NZ  LYS B  43      26.955 -40.314 121.897  1.00 72.16           N  
ANISOU 2274  NZ  LYS B  43    11427   5345  10643  -1438   2899  -1023       N  
ATOM   2275  N   GLU B  44      26.067 -37.435 117.645  1.00 60.88           N  
ANISOU 2275  N   GLU B  44     9393   4342   9397  -1676   1736  -1935       N  
ATOM   2276  CA  GLU B  44      25.293 -36.199 117.534  1.00 60.68           C  
ANISOU 2276  CA  GLU B  44     8792   4776   9486  -1572   1567  -1815       C  
ATOM   2277  C   GLU B  44      26.093 -34.953 117.963  1.00 55.53           C  
ANISOU 2277  C   GLU B  44     8403   4384   8311  -1098   1504  -1776       C  
ATOM   2278  O   GLU B  44      27.014 -35.025 118.783  1.00 52.31           O  
ANISOU 2278  O   GLU B  44     8506   3643   7727   -888   1643  -2750       O  
ATOM   2279  CB  GLU B  44      23.991 -36.314 118.330  1.00 64.67           C  
ANISOU 2279  CB  GLU B  44     9023   5301  10245  -1671   1907  -1754       C  
ATOM   2280  CG  GLU B  44      22.948 -35.273 117.928  1.00 64.76           C  
ANISOU 2280  CG  GLU B  44     8729   5454  10421  -1664   1727  -2093       C  
ATOM   2281  CD  GLU B  44      21.524 -35.766 118.069  1.00 68.77           C  
ANISOU 2281  CD  GLU B  44     9022   5590  11516  -2165   1859  -2183       C  
ATOM   2282  OE1 GLU B  44      21.215 -36.865 117.548  1.00 72.89           O  
ANISOU 2282  OE1 GLU B  44    10001   5734  11960  -2081   1961  -2531       O  
ATOM   2283  OE2 GLU B  44      20.714 -35.038 118.688  1.00 71.15           O  
ANISOU 2283  OE2 GLU B  44     8942   5725  12366  -1800   1679  -2029       O  
ATOM   2284  N   ARG B  45      25.737 -33.815 117.383  1.00 53.55           N  
ANISOU 2284  N   ARG B  45     8130   4262   7954  -1322   1347  -1859       N  
ATOM   2285  CA  ARG B  45      26.415 -32.557 117.681  1.00 50.84           C  
ANISOU 2285  CA  ARG B  45     7457   4405   7455  -1214   1248  -1718       C  
ATOM   2286  C   ARG B  45      26.187 -32.215 119.152  1.00 49.56           C  
ANISOU 2286  C   ARG B  45     7189   4083   7558  -1090   1493  -1723       C  
ATOM   2287  O   ARG B  45      25.087 -32.419 119.663  1.00 52.93           O  
ANISOU 2287  O   ARG B  45     7242   4496   8373   -867   1859  -1760       O  
ATOM   2288  CB  ARG B  45      25.893 -31.450 116.770  1.00 51.49           C  
ANISOU 2288  CB  ARG B  45     7395   4413   7753  -1041   1026  -1781       C  
ATOM   2289  CG  ARG B  45      26.790 -30.224 116.699  1.00 51.41           C  
ANISOU 2289  CG  ARG B  45     7174   4796   7562  -1098    805  -1516       C  
ATOM   2290  CD  ARG B  45      26.254 -29.224 115.687  1.00 53.50           C  
ANISOU 2290  CD  ARG B  45     7405   5176   7745   -900    464  -1509       C  
ATOM   2291  NE  ARG B  45      24.882 -28.809 116.011  1.00 56.89           N  
ANISOU 2291  NE  ARG B  45     7483   5864   8266   -876    744  -1552       N  
ATOM   2292  CZ  ARG B  45      24.100 -28.060 115.229  1.00 57.37           C  
ANISOU 2292  CZ  ARG B  45     7372   6057   8367   -896    507  -1780       C  
ATOM   2293  NH1 ARG B  45      24.531 -27.595 114.055  1.00 56.35           N  
ANISOU 2293  NH1 ARG B  45     7477   5821   8111   -865    363  -1938       N  
ATOM   2294  NH2 ARG B  45      22.870 -27.753 115.638  1.00 59.95           N  
ANISOU 2294  NH2 ARG B  45     7206   6464   9106  -1323    672  -2047       N  
ATOM   2295  N   GLU B  46      27.236 -31.766 119.840  1.00 45.95           N  
ANISOU 2295  N   GLU B  46     7061   3536   6861   -981   1658  -1450       N  
ATOM   2296  CA  GLU B  46      27.129 -31.382 121.248  1.00 44.91           C  
ANISOU 2296  CA  GLU B  46     7038   3365   6660  -1203   1698  -1030       C  
ATOM   2297  C   GLU B  46      27.797 -30.045 121.539  1.00 40.85           C  
ANISOU 2297  C   GLU B  46     6528   3157   5834   -956   1697   -898       C  
ATOM   2298  O   GLU B  46      28.788 -29.661 120.909  1.00 35.73           O  
ANISOU 2298  O   GLU B  46     6280   2069   5226   -785   1503  -1327       O  
ATOM   2299  CB  GLU B  46      27.698 -32.462 122.182  1.00 47.67           C  
ANISOU 2299  CB  GLU B  46     7697   3511   6902  -1183   1946   -649       C  
ATOM   2300  CG  GLU B  46      29.209 -32.423 122.421  1.00 47.43           C  
ANISOU 2300  CG  GLU B  46     7734   3672   6613   -916   1852   -574       C  
ATOM   2301  CD  GLU B  46      29.717 -33.586 123.260  1.00 51.34           C  
ANISOU 2301  CD  GLU B  46     8512   3944   7050   -677   1922   -266       C  
ATOM   2302  OE1 GLU B  46      28.941 -34.144 124.071  1.00 55.51           O  
ANISOU 2302  OE1 GLU B  46     9181   4268   7639   -742   2400   -173       O  
ATOM   2303  OE2 GLU B  46      30.906 -33.940 123.124  1.00 51.87           O  
ANISOU 2303  OE2 GLU B  46     8459   4058   7191   -688   2150    936       O  
ATOM   2304  N   PHE B  47      27.237 -29.382 122.541  1.00 39.70           N  
ANISOU 2304  N   PHE B  47     6420   2940   5723  -1127   1852   -665       N  
ATOM   2305  CA  PHE B  47      27.691 -28.102 123.044  1.00 37.29           C  
ANISOU 2305  CA  PHE B  47     6076   2957   5133   -858   1645   -714       C  
ATOM   2306  C   PHE B  47      29.015 -28.251 123.781  1.00 35.33           C  
ANISOU 2306  C   PHE B  47     6150   2633   4638   -687   1785   -566       C  
ATOM   2307  O   PHE B  47      29.185 -29.192 124.543  1.00 36.57           O  
ANISOU 2307  O   PHE B  47     6538   2578   4779   -894   2445   -364       O  
ATOM   2308  CB  PHE B  47      26.627 -27.559 123.994  1.00 38.63           C  
ANISOU 2308  CB  PHE B  47     6141   3138   5396   -915   1831   -703       C  
ATOM   2309  CG  PHE B  47      26.998 -26.261 124.643  1.00 37.96           C  
ANISOU 2309  CG  PHE B  47     6233   3004   5185   -682   1782   -688       C  
ATOM   2310  CD1 PHE B  47      26.869 -25.071 123.948  1.00 36.13           C  
ANISOU 2310  CD1 PHE B  47     5866   3025   4835   -884   1761   -732       C  
ATOM   2311  CD2 PHE B  47      27.476 -26.233 125.955  1.00 39.06           C  
ANISOU 2311  CD2 PHE B  47     6711   3032   5095   -529   1824   -589       C  
ATOM   2312  CE1 PHE B  47      27.205 -23.867 124.542  1.00 35.78           C  
ANISOU 2312  CE1 PHE B  47     5783   3052   4758  -1116   1593   -580       C  
ATOM   2313  CE2 PHE B  47      27.822 -25.030 126.555  1.00 38.64           C  
ANISOU 2313  CE2 PHE B  47     6713   3079   4886   -750   1672   -394       C  
ATOM   2314  CZ  PHE B  47      27.683 -23.846 125.847  1.00 36.39           C  
ANISOU 2314  CZ  PHE B  47     6210   2961   4654   -897   1662   -495       C  
ATOM   2315  N   VAL B  48      29.940 -27.315 123.561  1.00 33.20           N  
ANISOU 2315  N   VAL B  48     5804   2504   4303   -561   1475   -586       N  
ATOM   2316  CA  VAL B  48      31.252 -27.348 124.216  1.00 33.01           C  
ANISOU 2316  CA  VAL B  48     5998   2509   4034   -393   1357   -421       C  
ATOM   2317  C   VAL B  48      31.462 -26.141 125.126  1.00 33.11           C  
ANISOU 2317  C   VAL B  48     6166   2600   3811   -414   1261   -332       C  
ATOM   2318  O   VAL B  48      31.784 -26.293 126.312  1.00 33.61           O  
ANISOU 2318  O   VAL B  48     6570   2433   3764   -447   1265   -251       O  
ATOM   2319  CB  VAL B  48      32.394 -27.417 123.187  1.00 32.07           C  
ANISOU 2319  CB  VAL B  48     5719   2495   3971   -347   1146   -381       C  
ATOM   2320  CG1 VAL B  48      33.749 -27.375 123.887  1.00 32.10           C  
ANISOU 2320  CG1 VAL B  48     5859   2547   3787   -257   1044   -296       C  
ATOM   2321  CG2 VAL B  48      32.259 -28.686 122.342  1.00 33.69           C  
ANISOU 2321  CG2 VAL B  48     6012   2789   3996   -213   1160   -583       C  
ATOM   2322  N   ALA B  49      31.324 -24.944 124.561  1.00 31.09           N  
ANISOU 2322  N   ALA B  49     5624   2529   3657   -489   1270   -447       N  
ATOM   2323  CA  ALA B  49      31.486 -23.728 125.334  1.00 29.69           C  
ANISOU 2323  CA  ALA B  49     5338   2474   3467   -416   1186   -346       C  
ATOM   2324  C   ALA B  49      30.775 -22.559 124.671  1.00 28.56           C  
ANISOU 2324  C   ALA B  49     5002   2507   3340   -465   1107   -450       C  
ATOM   2325  O   ALA B  49      30.561 -22.574 123.464  1.00 28.45           O  
ANISOU 2325  O   ALA B  49     4985   2463   3360   -626   1018   -988       O  
ATOM   2326  CB  ALA B  49      32.968 -23.428 125.531  1.00 28.98           C  
ANISOU 2326  CB  ALA B  49     5275   2461   3275   -209   1025   -311       C  
ATOM   2327  N   ALA B  50      30.397 -21.563 125.475  1.00 27.93           N  
ANISOU 2327  N   ALA B  50     5019   2332   3259   -540   1205   -313       N  
ATOM   2328  CA  ALA B  50      29.800 -20.332 124.966  1.00 26.53           C  
ANISOU 2328  CA  ALA B  50     4465   2351   3264   -461   1130   -540       C  
ATOM   2329  C   ALA B  50      30.254 -19.113 125.770  1.00 26.32           C  
ANISOU 2329  C   ALA B  50     4516   2391   3090   -397    898   -445       C  
ATOM   2330  O   ALA B  50      30.676 -19.238 126.917  1.00 27.65           O  
ANISOU 2330  O   ALA B  50     4694   2580   3229   -244    728   -439       O  
ATOM   2331  CB  ALA B  50      28.293 -20.433 124.962  1.00 26.69           C  
ANISOU 2331  CB  ALA B  50     4466   2236   3436   -738   1206   -581       C  
ATOM   2332  N   ILE B  51      30.131 -17.940 125.156  1.00 25.08           N  
ANISOU 2332  N   ILE B  51     4260   2346   2921   -590    877   -471       N  
ATOM   2333  CA  ILE B  51      30.546 -16.681 125.756  1.00 24.77           C  
ANISOU 2333  CA  ILE B  51     4167   2333   2912   -468    784   -464       C  
ATOM   2334  C   ILE B  51      29.640 -15.516 125.304  1.00 24.14           C  
ANISOU 2334  C   ILE B  51     4041   2241   2887   -534    825   -552       C  
ATOM   2335  O   ILE B  51      29.317 -15.383 124.120  1.00 23.85           O  
ANISOU 2335  O   ILE B  51     3948   2197   2915   -817    726   -586       O  
ATOM   2336  CB  ILE B  51      32.041 -16.416 125.446  1.00 24.48           C  
ANISOU 2336  CB  ILE B  51     4107   2373   2821   -427    659   -443       C  
ATOM   2337  CG1 ILE B  51      32.549 -15.174 126.188  1.00 24.84           C  
ANISOU 2337  CG1 ILE B  51     4185   2366   2886   -283    572   -555       C  
ATOM   2338  CG2 ILE B  51      32.292 -16.325 123.944  1.00 23.33           C  
ANISOU 2338  CG2 ILE B  51     3836   2220   2807   -471    638   -501       C  
ATOM   2339  CD1 ILE B  51      34.064 -15.084 126.238  1.00 25.24           C  
ANISOU 2339  CD1 ILE B  51     4224   2485   2879   -350    474   -535       C  
ATOM   2340  N   SER B  52      29.217 -14.686 126.254  1.00 24.62           N  
ANISOU 2340  N   SER B  52     4158   2368   2827   -384    864   -552       N  
ATOM   2341  CA  SER B  52      28.417 -13.496 125.948  1.00 24.42           C  
ANISOU 2341  CA  SER B  52     3987   2405   2886   -406    883   -532       C  
ATOM   2342  C   SER B  52      29.224 -12.480 125.150  1.00 23.54           C  
ANISOU 2342  C   SER B  52     3766   2210   2967   -435    716   -618       C  
ATOM   2343  O   SER B  52      30.439 -12.584 125.072  1.00 24.11           O  
ANISOU 2343  O   SER B  52     3779   2421   2960   -331    568   -780       O  
ATOM   2344  CB  SER B  52      27.907 -12.845 127.229  1.00 24.69           C  
ANISOU 2344  CB  SER B  52     4133   2192   3054   -332    961   -581       C  
ATOM   2345  OG  SER B  52      28.978 -12.357 128.013  1.00 24.53           O  
ANISOU 2345  OG  SER B  52     4137   2027   3153   -136    947   -830       O  
ATOM   2346  N   TRP B  53      28.545 -11.501 124.560  1.00 23.89           N  
ANISOU 2346  N   TRP B  53     3729   2372   2972   -379    723   -522       N  
ATOM   2347  CA  TRP B  53      29.215 -10.450 123.772  1.00 23.71           C  
ANISOU 2347  CA  TRP B  53     3642   2429   2936   -403    670   -524       C  
ATOM   2348  C   TRP B  53      30.322  -9.741 124.549  1.00 24.10           C  
ANISOU 2348  C   TRP B  53     3739   2415   3003   -419    680   -591       C  
ATOM   2349  O   TRP B  53      31.387  -9.456 124.010  1.00 23.63           O  
ANISOU 2349  O   TRP B  53     3799   2160   3018   -323    882   -855       O  
ATOM   2350  CB  TRP B  53      28.195  -9.420 123.225  1.00 24.11           C  
ANISOU 2350  CB  TRP B  53     3693   2369   3096   -411    695   -541       C  
ATOM   2351  CG  TRP B  53      27.649  -8.453 124.216  1.00 23.90           C  
ANISOU 2351  CG  TRP B  53     3665   2350   3063   -353    728   -503       C  
ATOM   2352  CD1 TRP B  53      26.497  -8.573 124.939  1.00 24.56           C  
ANISOU 2352  CD1 TRP B  53     3735   2376   3218   -261    846   -590       C  
ATOM   2353  CD2 TRP B  53      28.247  -7.220 124.610  1.00 24.12           C  
ANISOU 2353  CD2 TRP B  53     3689   2315   3158   -266    709   -585       C  
ATOM   2354  NE1 TRP B  53      26.353  -7.493 125.775  1.00 24.62           N  
ANISOU 2354  NE1 TRP B  53     3904   2315   3135   -308    931   -556       N  
ATOM   2355  CE2 TRP B  53      27.411  -6.645 125.588  1.00 24.63           C  
ANISOU 2355  CE2 TRP B  53     3771   2463   3122   -331    750   -675       C  
ATOM   2356  CE3 TRP B  53      29.419  -6.545 124.237  1.00 24.25           C  
ANISOU 2356  CE3 TRP B  53     3784   2301   3126   -329    676   -542       C  
ATOM   2357  CZ2 TRP B  53      27.702  -5.416 126.187  1.00 25.55           C  
ANISOU 2357  CZ2 TRP B  53     3988   2365   3355   -267    798   -670       C  
ATOM   2358  CZ3 TRP B  53      29.713  -5.334 124.839  1.00 24.83           C  
ANISOU 2358  CZ3 TRP B  53     3904   2301   3227   -344    656   -546       C  
ATOM   2359  CH2 TRP B  53      28.851  -4.777 125.802  1.00 25.20           C  
ANISOU 2359  CH2 TRP B  53     4017   2333   3226   -303    661   -616       C  
ATOM   2360  N   SER B  54      30.038  -9.489 125.831  1.00 25.49           N  
ANISOU 2360  N   SER B  54     3980   2692   3011   -323    634   -644       N  
ATOM   2361  CA  SER B  54      30.877  -8.737 126.743  1.00 24.86           C  
ANISOU 2361  CA  SER B  54     4106   2271   3067   -372    655   -645       C  
ATOM   2362  C   SER B  54      31.941  -9.571 127.455  1.00 25.63           C  
ANISOU 2362  C   SER B  54     4184   2535   3016   -410    490   -670       C  
ATOM   2363  O   SER B  54      32.694  -9.031 128.260  1.00 26.40           O  
ANISOU 2363  O   SER B  54     4471   2374   3184   -434    584  -1071       O  
ATOM   2364  CB  SER B  54      29.955  -8.150 127.811  1.00 25.42           C  
ANISOU 2364  CB  SER B  54     4264   2421   2971   -363    652   -629       C  
ATOM   2365  OG  SER B  54      29.132  -9.168 128.394  1.00 24.66           O  
ANISOU 2365  OG  SER B  54     4278   2320   2769   -271    862   -754       O  
ATOM   2366  N   SER B  55      31.979 -10.886 127.192  1.00 25.96           N  
ANISOU 2366  N   SER B  55     4284   2528   3048   -288    553   -619       N  
ATOM   2367  CA  SER B  55      32.766 -11.842 127.972  1.00 26.89           C  
ANISOU 2367  CA  SER B  55     4477   2717   3021   -194    419   -609       C  
ATOM   2368  C   SER B  55      32.382 -11.902 129.473  1.00 28.48           C  
ANISOU 2368  C   SER B  55     4845   2897   3079   -111    539   -597       C  
ATOM   2369  O   SER B  55      33.125 -12.448 130.296  1.00 29.15           O  
ANISOU 2369  O   SER B  55     5149   3139   2789   -203    490   -505       O  
ATOM   2370  CB  SER B  55      34.274 -11.580 127.786  1.00 27.32           C  
ANISOU 2370  CB  SER B  55     4498   2799   3081   -383    281   -610       C  
ATOM   2371  OG  SER B  55      34.604 -11.443 126.411  1.00 27.22           O  
ANISOU 2371  OG  SER B  55     4168   3002   3173   -567    261   -449       O  
ATOM   2372  N   GLY B  56      31.210 -11.379 129.825  1.00 29.07           N  
ANISOU 2372  N   GLY B  56     4903   2996   3146   -165    612   -717       N  
ATOM   2373  CA  GLY B  56      30.771 -11.352 131.209  1.00 30.32           C  
ANISOU 2373  CA  GLY B  56     5308   3046   3164   -127    748   -741       C  
ATOM   2374  C   GLY B  56      30.286 -12.703 131.661  1.00 31.49           C  
ANISOU 2374  C   GLY B  56     5707   2992   3265     83    907   -625       C  
ATOM   2375  O   GLY B  56      30.358 -13.022 132.841  1.00 34.62           O  
ANISOU 2375  O   GLY B  56     6486   3447   3219    511    632   -797       O  
ATOM   2376  N   THR B  57      29.778 -13.494 130.717  1.00 30.69           N  
ANISOU 2376  N   THR B  57     5383   2938   3337    -91   1148   -632       N  
ATOM   2377  CA  THR B  57      29.210 -14.794 131.010  1.00 31.70           C  
ANISOU 2377  CA  THR B  57     5642   3021   3379   -188   1250   -468       C  
ATOM   2378  C   THR B  57      29.797 -15.862 130.083  1.00 30.57           C  
ANISOU 2378  C   THR B  57     5380   2959   3275   -305   1214   -403       C  
ATOM   2379  O   THR B  57      29.853 -15.674 128.870  1.00 27.51           O  
ANISOU 2379  O   THR B  57     4931   2264   3254   -599   1020   -418       O  
ATOM   2380  CB  THR B  57      27.694 -14.739 130.801  1.00 32.16           C  
ANISOU 2380  CB  THR B  57     5600   3074   3544   -208   1430   -410       C  
ATOM   2381  OG1 THR B  57      27.172 -13.547 131.415  1.00 32.89           O  
ANISOU 2381  OG1 THR B  57     5814   3278   3402   -139   1473   -474       O  
ATOM   2382  CG2 THR B  57      27.020 -15.968 131.380  1.00 33.66           C  
ANISOU 2382  CG2 THR B  57     5954   3142   3692   -248   1787   -444       C  
ATOM   2383  N   THR B  58      30.228 -16.973 130.672  1.00 32.30           N  
ANISOU 2383  N   THR B  58     5764   3125   3383   -155   1198   -327       N  
ATOM   2384  CA  THR B  58      30.622 -18.158 129.931  1.00 33.29           C  
ANISOU 2384  CA  THR B  58     5999   3087   3561   -166   1081   -419       C  
ATOM   2385  C   THR B  58      29.831 -19.370 130.423  1.00 35.20           C  
ANISOU 2385  C   THR B  58     6517   3187   3669   -166   1464   -246       C  
ATOM   2386  O   THR B  58      29.300 -19.366 131.536  1.00 35.25           O  
ANISOU 2386  O   THR B  58     7023   2878   3490     59   1454   -652       O  
ATOM   2387  CB  THR B  58      32.129 -18.446 130.057  1.00 33.62           C  
ANISOU 2387  CB  THR B  58     6094   3216   3464    -71    868   -402       C  
ATOM   2388  OG1 THR B  58      32.479 -18.635 131.430  1.00 37.31           O  
ANISOU 2388  OG1 THR B  58     7404   3459   3312     56    724   -801       O  
ATOM   2389  CG2 THR B  58      32.939 -17.311 129.487  1.00 33.02           C  
ANISOU 2389  CG2 THR B  58     5823   3170   3554     11    756   -366       C  
ATOM   2390  N   ARG B  59      29.731 -20.377 129.556  1.00 36.10           N  
ANISOU 2390  N   ARG B  59     6643   3201   3870   -213   1434   -357       N  
ATOM   2391  CA  ARG B  59      29.140 -21.679 129.888  1.00 37.82           C  
ANISOU 2391  CA  ARG B  59     6860   3336   4172   -263   1723   -301       C  
ATOM   2392  C   ARG B  59      30.015 -22.769 129.276  1.00 37.26           C  
ANISOU 2392  C   ARG B  59     6858   3214   4083   -254   1636   -170       C  
ATOM   2393  O   ARG B  59      30.565 -22.584 128.186  1.00 34.68           O  
ANISOU 2393  O   ARG B  59     6559   2802   3813    -85   1411   -254       O  
ATOM   2394  CB  ARG B  59      27.718 -21.800 129.339  1.00 39.77           C  
ANISOU 2394  CB  ARG B  59     6774   3665   4668   -504   1830   -360       C  
ATOM   2395  CG  ARG B  59      26.705 -20.843 129.954  1.00 42.09           C  
ANISOU 2395  CG  ARG B  59     7035   3841   5116   -332   1915   -375       C  
ATOM   2396  CD  ARG B  59      26.285 -21.276 131.353  1.00 45.13           C  
ANISOU 2396  CD  ARG B  59     7623   4098   5426   -431   2271   -150       C  
ATOM   2397  NE  ARG B  59      25.267 -20.387 131.914  1.00 47.73           N  
ANISOU 2397  NE  ARG B  59     7933   4501   5700   -333   2406   -368       N  
ATOM   2398  CZ  ARG B  59      25.497 -19.276 132.620  1.00 47.98           C  
ANISOU 2398  CZ  ARG B  59     8067   4320   5841   -360   2303   -227       C  
ATOM   2399  NH1 ARG B  59      26.731 -18.861 132.897  1.00 48.92           N  
ANISOU 2399  NH1 ARG B  59     8122   4485   5977   -262   1998   -291       N  
ATOM   2400  NH2 ARG B  59      24.466 -18.568 133.066  1.00 50.59           N  
ANISOU 2400  NH2 ARG B  59     8241   4825   6153   -242   2570   -226       N  
ATOM   2401  N   TYR B  60      30.140 -23.896 129.977  1.00 38.58           N  
ANISOU 2401  N   TYR B  60     7273   3264   4121   -118   1764   -125       N  
ATOM   2402  CA  TYR B  60      30.978 -25.008 129.539  1.00 38.27           C  
ANISOU 2402  CA  TYR B  60     7264   3125   4152   -120   1572    -79       C  
ATOM   2403  C   TYR B  60      30.258 -26.345 129.698  1.00 39.66           C  
ANISOU 2403  C   TYR B  60     7505   3104   4458   -188   1954   -118       C  
ATOM   2404  O   TYR B  60      29.539 -26.558 130.676  1.00 41.37           O  
ANISOU 2404  O   TYR B  60     7955   3156   4604     16   2277   -220       O  
ATOM   2405  CB  TYR B  60      32.270 -25.056 130.357  1.00 38.34           C  
ANISOU 2405  CB  TYR B  60     7437   3183   3946     87   1494     20       C  
ATOM   2406  CG  TYR B  60      33.223 -23.933 130.083  1.00 36.47           C  
ANISOU 2406  CG  TYR B  60     7027   3132   3697    189   1226   -162       C  
ATOM   2407  CD1 TYR B  60      34.082 -23.979 128.982  1.00 35.00           C  
ANISOU 2407  CD1 TYR B  60     6630   3051   3617    202    995   -249       C  
ATOM   2408  CD2 TYR B  60      33.278 -22.816 130.923  1.00 36.28           C  
ANISOU 2408  CD2 TYR B  60     7017   3268   3500    197   1134   -168       C  
ATOM   2409  CE1 TYR B  60      34.972 -22.948 128.727  1.00 33.81           C  
ANISOU 2409  CE1 TYR B  60     6425   3014   3405    251    772   -241       C  
ATOM   2410  CE2 TYR B  60      34.158 -21.778 130.672  1.00 34.87           C  
ANISOU 2410  CE2 TYR B  60     6795   3141   3312    202    883   -397       C  
ATOM   2411  CZ  TYR B  60      35.001 -21.849 129.580  1.00 33.90           C  
ANISOU 2411  CZ  TYR B  60     6400   3171   3307    198    719   -320       C  
ATOM   2412  OH  TYR B  60      35.878 -20.829 129.326  1.00 33.37           O  
ANISOU 2412  OH  TYR B  60     6472   3059   3144    286    871   -398       O  
ATOM   2413  N   LEU B  61      30.468 -27.239 128.734  1.00 38.56           N  
ANISOU 2413  N   LEU B  61     7217   2962   4469   -309   1974   -115       N  
ATOM   2414  CA  LEU B  61      30.170 -28.670 128.914  1.00 40.71           C  
ANISOU 2414  CA  LEU B  61     7774   2961   4730   -341   2161    -86       C  
ATOM   2415  C   LEU B  61      30.973 -29.197 130.104  1.00 42.23           C  
ANISOU 2415  C   LEU B  61     8465   2806   4774     76   2158    -13       C  
ATOM   2416  O   LEU B  61      32.164 -28.890 130.241  1.00 40.20           O  
ANISOU 2416  O   LEU B  61     8274   2622   4376    386   2377    270       O  
ATOM   2417  CB  LEU B  61      30.528 -29.462 127.652  1.00 39.83           C  
ANISOU 2417  CB  LEU B  61     7537   2854   4742   -452   1976   -159       C  
ATOM   2418  CG  LEU B  61      30.378 -30.992 127.681  1.00 41.66           C  
ANISOU 2418  CG  LEU B  61     7938   2865   5024   -351   2151   -140       C  
ATOM   2419  CD1 LEU B  61      28.918 -31.408 127.824  1.00 42.31           C  
ANISOU 2419  CD1 LEU B  61     8092   2688   5293   -583   2508   -142       C  
ATOM   2420  CD2 LEU B  61      30.996 -31.588 126.425  1.00 41.67           C  
ANISOU 2420  CD2 LEU B  61     7786   2915   5130   -294   2112   -163       C  
ATOM   2421  N   ASP B  62      30.313 -29.971 130.963  1.00 45.44           N  
ANISOU 2421  N   ASP B  62     9236   2780   5247    -62   2528     43       N  
ATOM   2422  CA  ASP B  62      30.932 -30.493 132.184  1.00 51.18           C  
ANISOU 2422  CA  ASP B  62    10215   3817   5414    226   2427    386       C  
ATOM   2423  C   ASP B  62      32.296 -31.155 131.936  1.00 50.86           C  
ANISOU 2423  C   ASP B  62    10195   4034   5093    299   2261    445       C  
ATOM   2424  O   ASP B  62      33.293 -30.817 132.579  1.00 50.24           O  
ANISOU 2424  O   ASP B  62    10527   4194   4366     20   2132   1176       O  
ATOM   2425  CB  ASP B  62      30.000 -31.510 132.850  1.00 57.05           C  
ANISOU 2425  CB  ASP B  62    10988   4311   6374    -94   3101    485       C  
ATOM   2426  CG  ASP B  62      30.408 -31.822 134.266  1.00 63.74           C  
ANISOU 2426  CG  ASP B  62    12300   5193   6722    261   2598    509       C  
ATOM   2427  OD1 ASP B  62      30.576 -30.854 135.046  1.00 69.95           O  
ANISOU 2427  OD1 ASP B  62    12908   5186   8482    409   2749   -266       O  
ATOM   2428  OD2 ASP B  62      30.544 -33.024 134.612  1.00 72.94           O  
ANISOU 2428  OD2 ASP B  62    13633   4692   9385    916   2333   -353       O  
ATOM   2429  N   THR B  63      32.330 -32.070 130.974  1.00 51.34           N  
ANISOU 2429  N   THR B  63    10090   3869   5545    357   2340    282       N  
ATOM   2430  CA  THR B  63      33.535 -32.845 130.665  1.00 50.91           C  
ANISOU 2430  CA  THR B  63    10197   3725   5418    461   2116    312       C  
ATOM   2431  C   THR B  63      34.724 -32.045 130.087  1.00 48.74           C  
ANISOU 2431  C   THR B  63     9688   3784   5045    655   1843    267       C  
ATOM   2432  O   THR B  63      35.810 -32.613 129.940  1.00 49.98           O  
ANISOU 2432  O   THR B  63     9937   3750   5302   1021   1393     40       O  
ATOM   2433  CB  THR B  63      33.209 -33.988 129.691  1.00 50.78           C  
ANISOU 2433  CB  THR B  63    10209   3546   5540    361   2289    306       C  
ATOM   2434  OG1 THR B  63      32.593 -33.448 128.522  1.00 47.83           O  
ANISOU 2434  OG1 THR B  63     9478   2879   5814   -106   2049    226       O  
ATOM   2435  CG2 THR B  63      32.265 -34.989 130.334  1.00 54.38           C  
ANISOU 2435  CG2 THR B  63    10835   3651   6173    205   2655    423       C  
ATOM   2436  N   VAL B  64      34.534 -30.764 129.751  1.00 46.40           N  
ANISOU 2436  N   VAL B  64     9156   3679   4793    577   1810    188       N  
ATOM   2437  CA  VAL B  64      35.658 -29.901 129.317  1.00 45.00           C  
ANISOU 2437  CA  VAL B  64     8757   3723   4617    553   1277     49       C  
ATOM   2438  C   VAL B  64      36.101 -28.823 130.321  1.00 46.36           C  
ANISOU 2438  C   VAL B  64     9022   4017   4574    606   1267   -133       C  
ATOM   2439  O   VAL B  64      37.076 -28.112 130.047  1.00 45.15           O  
ANISOU 2439  O   VAL B  64     9077   3659   4416    715   1265     16       O  
ATOM   2440  CB  VAL B  64      35.392 -29.225 127.949  1.00 42.06           C  
ANISOU 2440  CB  VAL B  64     8013   3528   4437    348   1331    -93       C  
ATOM   2441  CG1 VAL B  64      35.008 -30.263 126.903  1.00 41.69           C  
ANISOU 2441  CG1 VAL B  64     8021   3166   4652    278   1516    -80       C  
ATOM   2442  CG2 VAL B  64      34.329 -28.126 128.028  1.00 40.76           C  
ANISOU 2442  CG2 VAL B  64     7762   3421   4303    170   1411   -171       C  
ATOM   2443  N   LYS B  65      35.405 -28.690 131.455  1.00 49.33           N  
ANISOU 2443  N   LYS B  65     9551   4504   4685    615   1571     60       N  
ATOM   2444  CA  LYS B  65      35.766 -27.683 132.484  1.00 49.86           C  
ANISOU 2444  CA  LYS B  65     9705   4552   4685    826   1216     32       C  
ATOM   2445  C   LYS B  65      37.173 -27.909 133.026  1.00 49.48           C  
ANISOU 2445  C   LYS B  65     9934   4577   4286   1040   1015   -159       C  
ATOM   2446  O   LYS B  65      37.545 -29.037 133.334  1.00 53.61           O  
ANISOU 2446  O   LYS B  65    10787   4811   4769   1254   1237     83       O  
ATOM   2447  CB  LYS B  65      34.807 -27.721 133.675  1.00 52.98           C  
ANISOU 2447  CB  LYS B  65    10370   4851   4908    849   1576    -24       C  
ATOM   2448  CG  LYS B  65      33.447 -27.086 133.441  1.00 54.53           C  
ANISOU 2448  CG  LYS B  65    10284   4960   5475    757   1649    226       C  
ATOM   2449  CD  LYS B  65      32.753 -26.768 134.773  1.00 57.94           C  
ANISOU 2449  CD  LYS B  65    11155   5361   5499    770   1788    114       C  
ATOM   2450  CE  LYS B  65      31.306 -27.259 134.823  1.00 60.26           C  
ANISOU 2450  CE  LYS B  65    11280   5540   6074    636   2212    294       C  
ATOM   2451  NZ  LYS B  65      30.421 -26.596 133.818  1.00 58.31           N  
ANISOU 2451  NZ  LYS B  65    10770   5112   6272    466   2219    290       N  
ATOM   2452  N   GLY B  66      37.949 -26.835 133.138  1.00 47.44           N  
ANISOU 2452  N   GLY B  66     9471   4480   4071   1281    755   -236       N  
ATOM   2453  CA  GLY B  66      39.334 -26.922 133.609  1.00 48.71           C  
ANISOU 2453  CA  GLY B  66     9735   4566   4206   1547    350   -157       C  
ATOM   2454  C   GLY B  66      40.311 -27.482 132.587  1.00 48.46           C  
ANISOU 2454  C   GLY B  66     9419   4781   4210   1411    189   -322       C  
ATOM   2455  O   GLY B  66      41.472 -27.752 132.911  1.00 49.21           O  
ANISOU 2455  O   GLY B  66     9590   4963   4143   1253   -354   -868       O  
ATOM   2456  N   ARG B  67      39.834 -27.690 131.361  1.00 46.17           N  
ANISOU 2456  N   ARG B  67     8937   4423   4181   1308    363   -292       N  
ATOM   2457  CA  ARG B  67      40.676 -28.106 130.240  1.00 44.35           C  
ANISOU 2457  CA  ARG B  67     8485   4257   4107   1166    310   -113       C  
ATOM   2458  C   ARG B  67      40.565 -27.106 129.108  1.00 40.17           C  
ANISOU 2458  C   ARG B  67     7528   3779   3956   1081    217   -343       C  
ATOM   2459  O   ARG B  67      41.578 -26.732 128.534  1.00 40.27           O  
ANISOU 2459  O   ARG B  67     7529   3812   3960    885     93   -508       O  
ATOM   2460  CB  ARG B  67      40.302 -29.520 129.758  1.00 45.11           C  
ANISOU 2460  CB  ARG B  67     8737   4171   4231   1152    470   -106       C  
ATOM   2461  CG  ARG B  67      40.672 -30.607 130.752  1.00 47.81           C  
ANISOU 2461  CG  ARG B  67     9379   4392   4392   1536    471    -20       C  
ATOM   2462  CD  ARG B  67      40.635 -32.015 130.160  1.00 49.24           C  
ANISOU 2462  CD  ARG B  67     9703   4420   4586   1500    647    -39       C  
ATOM   2463  NE  ARG B  67      39.340 -32.338 129.546  1.00 48.34           N  
ANISOU 2463  NE  ARG B  67     9558   4148   4661   1214    951   -116       N  
ATOM   2464  CZ  ARG B  67      39.116 -32.591 128.251  1.00 47.59           C  
ANISOU 2464  CZ  ARG B  67     9248   4165   4666   1058    886     73       C  
ATOM   2465  NH1 ARG B  67      40.103 -32.592 127.348  1.00 47.42           N  
ANISOU 2465  NH1 ARG B  67     8960   4301   4756   1090    741     23       N  
ATOM   2466  NH2 ARG B  67      37.872 -32.871 127.854  1.00 46.84           N  
ANISOU 2466  NH2 ARG B  67     9236   3870   4690    719   1131    283       N  
ATOM   2467  N   PHE B  68      39.342 -26.705 128.767  1.00 38.08           N  
ANISOU 2467  N   PHE B  68     7241   3640   3587    807    536   -158       N  
ATOM   2468  CA  PHE B  68      39.088 -25.764 127.674  1.00 35.51           C  
ANISOU 2468  CA  PHE B  68     6604   3366   3520    651    405   -311       C  
ATOM   2469  C   PHE B  68      38.728 -24.384 128.227  1.00 34.74           C  
ANISOU 2469  C   PHE B  68     6485   3307   3406    488    495   -293       C  
ATOM   2470  O   PHE B  68      38.041 -24.291 129.238  1.00 34.62           O  
ANISOU 2470  O   PHE B  68     7053   3234   2867    271    399   -123       O  
ATOM   2471  CB  PHE B  68      37.915 -26.255 126.813  1.00 33.97           C  
ANISOU 2471  CB  PHE B  68     6344   3094   3469    474    687   -225       C  
ATOM   2472  CG  PHE B  68      38.166 -27.539 126.047  1.00 34.19           C  
ANISOU 2472  CG  PHE B  68     6412   3071   3506    472    692   -247       C  
ATOM   2473  CD1 PHE B  68      39.308 -28.336 126.229  1.00 35.03           C  
ANISOU 2473  CD1 PHE B  68     6679   3152   3476    666    586   -205       C  
ATOM   2474  CD2 PHE B  68      37.200 -27.982 125.150  1.00 33.73           C  
ANISOU 2474  CD2 PHE B  68     6296   2956   3562    339    838   -297       C  
ATOM   2475  CE1 PHE B  68      39.481 -29.511 125.509  1.00 35.04           C  
ANISOU 2475  CE1 PHE B  68     6730   3029   3553    624    626   -128       C  
ATOM   2476  CE2 PHE B  68      37.371 -29.165 124.438  1.00 33.89           C  
ANISOU 2476  CE2 PHE B  68     6332   2879   3665    264    888   -292       C  
ATOM   2477  CZ  PHE B  68      38.512 -29.928 124.617  1.00 34.11           C  
ANISOU 2477  CZ  PHE B  68     6650   2841   3466    491    786   -206       C  
ATOM   2478  N   THR B  69      39.166 -23.320 127.549  1.00 33.54           N  
ANISOU 2478  N   THR B  69     6075   3222   3446    502    302   -324       N  
ATOM   2479  CA  THR B  69      38.780 -21.937 127.912  1.00 31.76           C  
ANISOU 2479  CA  THR B  69     5660   3161   3246    419    207   -343       C  
ATOM   2480  C   THR B  69      38.268 -21.217 126.674  1.00 29.16           C  
ANISOU 2480  C   THR B  69     5176   2836   3065    225    360   -447       C  
ATOM   2481  O   THR B  69      38.964 -21.156 125.678  1.00 29.37           O  
ANISOU 2481  O   THR B  69     5354   2878   2927    349    341   -737       O  
ATOM   2482  CB  THR B  69      39.968 -21.128 128.468  1.00 31.79           C  
ANISOU 2482  CB  THR B  69     5704   3239   3134    608    -18   -457       C  
ATOM   2483  OG1 THR B  69      40.695 -21.929 129.383  1.00 34.18           O  
ANISOU 2483  OG1 THR B  69     6067   3913   3007    970   -274   -610       O  
ATOM   2484  CG2 THR B  69      39.501 -19.850 129.180  1.00 31.87           C  
ANISOU 2484  CG2 THR B  69     5724   3312   3072    491    -57   -592       C  
ATOM   2485  N   ILE B  70      37.061 -20.667 126.749  1.00 28.12           N  
ANISOU 2485  N   ILE B  70     5018   2836   2829     46    358   -358       N  
ATOM   2486  CA  ILE B  70      36.537 -19.805 125.699  1.00 26.28           C  
ANISOU 2486  CA  ILE B  70     4572   2586   2827    -45    473   -435       C  
ATOM   2487  C   ILE B  70      36.874 -18.346 126.005  1.00 26.29           C  
ANISOU 2487  C   ILE B  70     4443   2675   2867    -45    324   -542       C  
ATOM   2488  O   ILE B  70      36.881 -17.934 127.158  1.00 26.79           O  
ANISOU 2488  O   ILE B  70     4630   2600   2948    -28    277   -601       O  
ATOM   2489  CB  ILE B  70      35.020 -20.005 125.476  1.00 25.57           C  
ANISOU 2489  CB  ILE B  70     4545   2356   2811   -101    542   -488       C  
ATOM   2490  CG1 ILE B  70      34.587 -19.384 124.150  1.00 24.41           C  
ANISOU 2490  CG1 ILE B  70     4178   2279   2816   -153    586   -512       C  
ATOM   2491  CG2 ILE B  70      34.187 -19.442 126.625  1.00 26.57           C  
ANISOU 2491  CG2 ILE B  70     4744   2528   2822   -176    624   -540       C  
ATOM   2492  CD1 ILE B  70      33.202 -19.817 123.675  1.00 24.29           C  
ANISOU 2492  CD1 ILE B  70     4224   2131   2872   -285    657   -616       C  
ATOM   2493  N   SER B  71      37.149 -17.585 124.953  1.00 25.84           N  
ANISOU 2493  N   SER B  71     4191   2673   2952    -94    414   -550       N  
ATOM   2494  CA  SER B  71      37.415 -16.160 125.045  1.00 26.29           C  
ANISOU 2494  CA  SER B  71     4242   2719   3026   -101    241   -599       C  
ATOM   2495  C   SER B  71      37.153 -15.516 123.697  1.00 25.87           C  
ANISOU 2495  C   SER B  71     4087   2685   3056   -186    346   -532       C  
ATOM   2496  O   SER B  71      36.873 -16.200 122.714  1.00 25.02           O  
ANISOU 2496  O   SER B  71     4262   2228   3016     30    597   -514       O  
ATOM   2497  CB  SER B  71      38.854 -15.902 125.491  1.00 27.42           C  
ANISOU 2497  CB  SER B  71     4261   2889   3265   -160    151   -596       C  
ATOM   2498  OG  SER B  71      39.784 -16.405 124.550  1.00 28.22           O  
ANISOU 2498  OG  SER B  71     4415   2899   3406   -141    166   -828       O  
ATOM   2499  N   ARG B  72      37.228 -14.197 123.657  1.00 25.79           N  
ANISOU 2499  N   ARG B  72     3929   2689   3178   -360    265   -587       N  
ATOM   2500  CA  ARG B  72      36.990 -13.469 122.422  1.00 26.03           C  
ANISOU 2500  CA  ARG B  72     3898   2776   3213   -382    324   -541       C  
ATOM   2501  C   ARG B  72      37.709 -12.138 122.400  1.00 27.45           C  
ANISOU 2501  C   ARG B  72     4126   2776   3526   -451    297   -484       C  
ATOM   2502  O   ARG B  72      38.111 -11.612 123.441  1.00 27.69           O  
ANISOU 2502  O   ARG B  72     4223   2957   3341   -218    224   -436       O  
ATOM   2503  CB  ARG B  72      35.489 -13.257 122.210  1.00 25.82           C  
ANISOU 2503  CB  ARG B  72     3915   2760   3133   -284    393   -457       C  
ATOM   2504  CG  ARG B  72      34.802 -12.432 123.285  1.00 26.40           C  
ANISOU 2504  CG  ARG B  72     4009   2776   3244   -317    498   -480       C  
ATOM   2505  CD  ARG B  72      33.283 -12.608 123.230  1.00 26.08           C  
ANISOU 2505  CD  ARG B  72     4012   2816   3081   -355    428   -526       C  
ATOM   2506  NE  ARG B  72      32.705 -11.984 122.048  1.00 24.73           N  
ANISOU 2506  NE  ARG B  72     3802   2577   3014   -350    618   -467       N  
ATOM   2507  CZ  ARG B  72      31.505 -12.249 121.537  1.00 24.73           C  
ANISOU 2507  CZ  ARG B  72     3758   2478   3161   -304    692   -582       C  
ATOM   2508  NH1 ARG B  72      31.108 -11.607 120.441  1.00 25.75           N  
ANISOU 2508  NH1 ARG B  72     3859   2710   3214   -132    511   -701       N  
ATOM   2509  NH2 ARG B  72      30.687 -13.130 122.098  1.00 25.06           N  
ANISOU 2509  NH2 ARG B  72     3823   2475   3221   -249    848   -634       N  
ATOM   2510  N   ASP B  73      37.873 -11.619 121.189  1.00 27.82           N  
ANISOU 2510  N   ASP B  73     4078   2949   3541   -495    498   -499       N  
ATOM   2511  CA  ASP B  73      38.401 -10.284 120.957  1.00 28.46           C  
ANISOU 2511  CA  ASP B  73     4003   2966   3845   -560    435   -444       C  
ATOM   2512  C   ASP B  73      37.496  -9.644 119.925  1.00 26.80           C  
ANISOU 2512  C   ASP B  73     3788   2623   3771   -650    603   -437       C  
ATOM   2513  O   ASP B  73      37.587  -9.959 118.733  1.00 25.00           O  
ANISOU 2513  O   ASP B  73     3636   2115   3746   -706    726   -313       O  
ATOM   2514  CB  ASP B  73      39.849 -10.367 120.457  1.00 31.01           C  
ANISOU 2514  CB  ASP B  73     4084   3315   4382   -477    549   -439       C  
ATOM   2515  CG  ASP B  73      40.538  -9.000 120.381  1.00 34.85           C  
ANISOU 2515  CG  ASP B  73     4341   3476   5423   -701    418   -608       C  
ATOM   2516  OD1 ASP B  73      39.867  -7.950 120.354  1.00 36.76           O  
ANISOU 2516  OD1 ASP B  73     4466   3432   6068   -710    -14   -402       O  
ATOM   2517  OD2 ASP B  73      41.778  -8.983 120.336  1.00 40.65           O  
ANISOU 2517  OD2 ASP B  73     4365   4502   6576   -874    319   -525       O  
ATOM   2518  N   ASN B  74      36.618  -8.753 120.389  1.00 27.28           N  
ANISOU 2518  N   ASN B  74     3805   2810   3749   -600    565   -543       N  
ATOM   2519  CA  ASN B  74      35.615  -8.142 119.524  1.00 27.41           C  
ANISOU 2519  CA  ASN B  74     3996   2771   3647   -495    619   -389       C  
ATOM   2520  C   ASN B  74      36.177  -7.201 118.488  1.00 28.41           C  
ANISOU 2520  C   ASN B  74     4176   2761   3857   -486    674   -284       C  
ATOM   2521  O   ASN B  74      35.665  -7.161 117.380  1.00 30.76           O  
ANISOU 2521  O   ASN B  74     5023   2873   3789   -581    459   -243       O  
ATOM   2522  CB  ASN B  74      34.515  -7.447 120.331  1.00 26.98           C  
ANISOU 2522  CB  ASN B  74     4128   2649   3474   -469    553   -443       C  
ATOM   2523  CG  ASN B  74      33.569  -8.431 120.993  1.00 27.22           C  
ANISOU 2523  CG  ASN B  74     4018   2825   3500   -551    575   -501       C  
ATOM   2524  OD1 ASN B  74      33.434  -9.579 120.565  1.00 27.43           O  
ANISOU 2524  OD1 ASN B  74     4241   2713   3465   -336    668   -401       O  
ATOM   2525  ND2 ASN B  74      32.914  -7.989 122.048  1.00 27.82           N  
ANISOU 2525  ND2 ASN B  74     3974   2773   3822   -443    696   -580       N  
ATOM   2526  N   ALA B  75      37.230  -6.461 118.824  1.00 29.79           N  
ANISOU 2526  N   ALA B  75     4096   2937   4283   -521    867   -471       N  
ATOM   2527  CA  ALA B  75      37.905  -5.612 117.833  1.00 31.39           C  
ANISOU 2527  CA  ALA B  75     4432   2983   4512   -463   1000   -251       C  
ATOM   2528  C   ALA B  75      38.489  -6.423 116.662  1.00 32.75           C  
ANISOU 2528  C   ALA B  75     4806   3272   4365   -339   1255    -53       C  
ATOM   2529  O   ALA B  75      38.572  -5.908 115.562  1.00 33.09           O  
ANISOU 2529  O   ALA B  75     4717   3344   4510    -60   1931     85       O  
ATOM   2530  CB  ALA B  75      38.992  -4.773 118.493  1.00 32.84           C  
ANISOU 2530  CB  ALA B  75     4414   3121   4941   -690   1122   -259       C  
ATOM   2531  N   LYS B  76      38.880  -7.682 116.899  1.00 32.90           N  
ANISOU 2531  N   LYS B  76     4688   3263   4547   -333   1179   -197       N  
ATOM   2532  CA  LYS B  76      39.331  -8.579 115.812  1.00 32.77           C  
ANISOU 2532  CA  LYS B  76     4586   3318   4548   -483   1142   -212       C  
ATOM   2533  C   LYS B  76      38.243  -9.520 115.302  1.00 30.40           C  
ANISOU 2533  C   LYS B  76     4365   3118   4064   -305   1141   -114       C  
ATOM   2534  O   LYS B  76      38.530 -10.423 114.523  1.00 29.24           O  
ANISOU 2534  O   LYS B  76     4456   3266   3387   -737   1306    -30       O  
ATOM   2535  CB  LYS B  76      40.545  -9.398 116.254  1.00 34.72           C  
ANISOU 2535  CB  LYS B  76     4568   3709   4913   -352   1071   -193       C  
ATOM   2536  CG  LYS B  76      41.777  -8.548 116.479  1.00 37.93           C  
ANISOU 2536  CG  LYS B  76     4819   4008   5583   -607   1170   -272       C  
ATOM   2537  CD  LYS B  76      42.922  -9.405 116.970  1.00 40.83           C  
ANISOU 2537  CD  LYS B  76     4912   4634   5965   -421    941   -327       C  
ATOM   2538  CE  LYS B  76      44.109  -8.547 117.350  1.00 44.78           C  
ANISOU 2538  CE  LYS B  76     5091   5032   6892   -668   1044   -440       C  
ATOM   2539  NZ  LYS B  76      45.094  -9.378 118.097  1.00 47.13           N  
ANISOU 2539  NZ  LYS B  76     5133   5531   7241   -403    984   -405       N  
ATOM   2540  N   SER B  77      37.007  -9.320 115.745  1.00 28.35           N  
ANISOU 2540  N   SER B  77     4222   2726   3820   -358    973     15       N  
ATOM   2541  CA  SER B  77      35.891 -10.160 115.344  1.00 28.10           C  
ANISOU 2541  CA  SER B  77     4241   2948   3485   -224    735   -211       C  
ATOM   2542  C   SER B  77      36.198 -11.668 115.487  1.00 27.39           C  
ANISOU 2542  C   SER B  77     4152   2925   3329   -264    640   -223       C  
ATOM   2543  O   SER B  77      35.817 -12.459 114.636  1.00 27.64           O  
ANISOU 2543  O   SER B  77     4473   2974   3054    -21    640   -232       O  
ATOM   2544  CB  SER B  77      35.490  -9.827 113.902  1.00 28.97           C  
ANISOU 2544  CB  SER B  77     4438   3076   3491   -154    858    -40       C  
ATOM   2545  OG  SER B  77      35.123  -8.470 113.779  1.00 29.04           O  
ANISOU 2545  OG  SER B  77     4727   2930   3376   -229    583   -517       O  
ATOM   2546  N   THR B  78      36.889 -12.048 116.561  1.00 25.90           N  
ANISOU 2546  N   THR B  78     3885   2687   3266   -353    722   -264       N  
ATOM   2547  CA  THR B  78      37.384 -13.404 116.721  1.00 25.28           C  
ANISOU 2547  CA  THR B  78     3743   2701   3159   -299    644   -357       C  
ATOM   2548  C   THR B  78      37.017 -13.996 118.079  1.00 24.50           C  
ANISOU 2548  C   THR B  78     3612   2580   3113   -221    495   -369       C  
ATOM   2549  O   THR B  78      37.043 -13.309 119.106  1.00 25.91           O  
ANISOU 2549  O   THR B  78     4060   2620   3164   -281    394   -379       O  
ATOM   2550  CB  THR B  78      38.908 -13.473 116.512  1.00 26.38           C  
ANISOU 2550  CB  THR B  78     3778   2768   3475   -402    702   -266       C  
ATOM   2551  OG1 THR B  78      39.246 -12.938 115.225  1.00 27.54           O  
ANISOU 2551  OG1 THR B  78     4227   3000   3235   -441    681   -441       O  
ATOM   2552  CG2 THR B  78      39.426 -14.920 116.589  1.00 26.92           C  
ANISOU 2552  CG2 THR B  78     3866   2892   3470   -202    783   -377       C  
ATOM   2553  N   VAL B  79      36.681 -15.282 118.064  1.00 23.60           N  
ANISOU 2553  N   VAL B  79     3560   2559   2845   -205    453   -404       N  
ATOM   2554  CA  VAL B  79      36.441 -16.056 119.268  1.00 23.33           C  
ANISOU 2554  CA  VAL B  79     3585   2499   2778   -287    509   -481       C  
ATOM   2555  C   VAL B  79      37.409 -17.230 119.270  1.00 24.72           C  
ANISOU 2555  C   VAL B  79     3858   2568   2964   -167    445   -439       C  
ATOM   2556  O   VAL B  79      37.728 -17.792 118.203  1.00 24.93           O  
ANISOU 2556  O   VAL B  79     4060   2533   2877   -243    583   -284       O  
ATOM   2557  CB  VAL B  79      34.967 -16.492 119.393  1.00 23.02           C  
ANISOU 2557  CB  VAL B  79     3593   2351   2801   -298    463   -433       C  
ATOM   2558  CG1 VAL B  79      34.526 -17.405 118.253  1.00 23.25           C  
ANISOU 2558  CG1 VAL B  79     3697   2484   2651   -200    641   -509       C  
ATOM   2559  CG2 VAL B  79      34.691 -17.141 120.749  1.00 23.31           C  
ANISOU 2559  CG2 VAL B  79     3691   2388   2777   -311    483   -491       C  
ATOM   2560  N   TYR B  80      37.882 -17.584 120.468  1.00 24.74           N  
ANISOU 2560  N   TYR B  80     3881   2642   2875   -196    383   -600       N  
ATOM   2561  CA  TYR B  80      38.902 -18.603 120.645  1.00 25.46           C  
ANISOU 2561  CA  TYR B  80     3988   2683   3001    -79    451   -522       C  
ATOM   2562  C   TYR B  80      38.412 -19.724 121.537  1.00 26.27           C  
ANISOU 2562  C   TYR B  80     4122   2794   3065    -80    409   -455       C  
ATOM   2563  O   TYR B  80      37.603 -19.500 122.454  1.00 26.52           O  
ANISOU 2563  O   TYR B  80     4032   2798   3246     13    340   -713       O  
ATOM   2564  CB  TYR B  80      40.175 -18.011 121.251  1.00 26.60           C  
ANISOU 2564  CB  TYR B  80     4025   2837   3243    -34    329   -559       C  
ATOM   2565  CG  TYR B  80      40.726 -16.827 120.486  1.00 28.82           C  
ANISOU 2565  CG  TYR B  80     4160   3078   3712   -190    471   -470       C  
ATOM   2566  CD1 TYR B  80      41.547 -17.007 119.365  1.00 29.95           C  
ANISOU 2566  CD1 TYR B  80     4202   3309   3869   -191    578   -484       C  
ATOM   2567  CD2 TYR B  80      40.424 -15.518 120.874  1.00 29.39           C  
ANISOU 2567  CD2 TYR B  80     4343   3069   3754   -296    321   -575       C  
ATOM   2568  CE1 TYR B  80      42.045 -15.919 118.664  1.00 30.93           C  
ANISOU 2568  CE1 TYR B  80     4220   3360   4170   -256    654   -449       C  
ATOM   2569  CE2 TYR B  80      40.919 -14.430 120.169  1.00 29.20           C  
ANISOU 2569  CE2 TYR B  80     4032   3069   3994   -502    391   -677       C  
ATOM   2570  CZ  TYR B  80      41.725 -14.638 119.079  1.00 31.03           C  
ANISOU 2570  CZ  TYR B  80     4142   3400   4246   -329    583   -623       C  
ATOM   2571  OH  TYR B  80      42.210 -13.564 118.392  1.00 35.77           O  
ANISOU 2571  OH  TYR B  80     4891   3458   5241   -220    869   -336       O  
ATOM   2572  N   LEU B  81      38.922 -20.926 121.272  1.00 26.65           N  
ANISOU 2572  N   LEU B  81     4403   2711   3012   -146    496   -530       N  
ATOM   2573  CA  LEU B  81      38.776 -22.053 122.174  1.00 27.19           C  
ANISOU 2573  CA  LEU B  81     4550   2756   3024     85    427   -484       C  
ATOM   2574  C   LEU B  81      40.150 -22.646 122.415  1.00 28.16           C  
ANISOU 2574  C   LEU B  81     4649   2850   3201    216    328   -558       C  
ATOM   2575  O   LEU B  81      40.708 -23.311 121.543  1.00 28.13           O  
ANISOU 2575  O   LEU B  81     4985   2706   2995    104     55   -809       O  
ATOM   2576  CB  LEU B  81      37.823 -23.090 121.585  1.00 27.47           C  
ANISOU 2576  CB  LEU B  81     4619   2695   3123     25    548   -479       C  
ATOM   2577  CG  LEU B  81      37.380 -24.185 122.550  1.00 29.04           C  
ANISOU 2577  CG  LEU B  81     5005   2759   3270     28    649   -422       C  
ATOM   2578  CD1 LEU B  81      36.507 -23.614 123.659  1.00 29.03           C  
ANISOU 2578  CD1 LEU B  81     5106   2783   3140    -45    651   -422       C  
ATOM   2579  CD2 LEU B  81      36.640 -25.280 121.792  1.00 29.52           C  
ANISOU 2579  CD2 LEU B  81     5033   2903   3278    -59    638   -438       C  
ATOM   2580  N   GLN B  82      40.711 -22.365 123.591  1.00 29.32           N  
ANISOU 2580  N   GLN B  82     4891   2975   3271    252    232   -631       N  
ATOM   2581  CA  GLN B  82      42.001 -22.909 123.987  1.00 31.89           C  
ANISOU 2581  CA  GLN B  82     5084   3398   3634    512     86   -565       C  
ATOM   2582  C   GLN B  82      41.740 -24.266 124.600  1.00 34.08           C  
ANISOU 2582  C   GLN B  82     5749   3467   3732    547     73   -439       C  
ATOM   2583  O   GLN B  82      41.143 -24.334 125.668  1.00 35.23           O  
ANISOU 2583  O   GLN B  82     5983   3454   3947    861    281   -531       O  
ATOM   2584  CB  GLN B  82      42.679 -22.000 125.024  1.00 33.92           C  
ANISOU 2584  CB  GLN B  82     5150   3743   3994    533    -91   -733       C  
ATOM   2585  CG  GLN B  82      44.030 -22.506 125.529  1.00 35.31           C  
ANISOU 2585  CG  GLN B  82     5374   3958   4083    680   -295   -682       C  
ATOM   2586  CD  GLN B  82      45.057 -22.613 124.411  1.00 35.86           C  
ANISOU 2586  CD  GLN B  82     5162   4088   4372    769   -247   -806       C  
ATOM   2587  OE1 GLN B  82      45.117 -21.766 123.515  1.00 35.41           O  
ANISOU 2587  OE1 GLN B  82     4835   4390   4229    612    -66   -801       O  
ATOM   2588  NE2 GLN B  82      45.868 -23.642 124.463  1.00 37.92           N  
ANISOU 2588  NE2 GLN B  82     5571   4360   4474   1069   -266   -769       N  
ATOM   2589  N   MET B  83      42.189 -25.332 123.934  1.00 35.59           N  
ANISOU 2589  N   MET B  83     6000   3662   3857    720    323   -449       N  
ATOM   2590  CA  MET B  83      41.930 -26.710 124.372  1.00 36.55           C  
ANISOU 2590  CA  MET B  83     6263   3681   3942    729    281   -429       C  
ATOM   2591  C   MET B  83      43.204 -27.359 124.895  1.00 38.19           C  
ANISOU 2591  C   MET B  83     6561   3780   4169    916     94   -448       C  
ATOM   2592  O   MET B  83      44.097 -27.695 124.121  1.00 39.14           O  
ANISOU 2592  O   MET B  83     6562   3943   4366    659    332   -316       O  
ATOM   2593  CB  MET B  83      41.376 -27.539 123.218  1.00 36.55           C  
ANISOU 2593  CB  MET B  83     6287   3599   4001    651    365   -461       C  
ATOM   2594  CG  MET B  83      40.079 -27.017 122.627  1.00 36.57           C  
ANISOU 2594  CG  MET B  83     6028   3748   4116    546    504   -396       C  
ATOM   2595  SD  MET B  83      39.399 -28.126 121.368  1.00 39.29           S  
ANISOU 2595  SD  MET B  83     6183   4230   4513    217    687   -733       S  
ATOM   2596  CE  MET B  83      40.732 -28.178 120.177  1.00 37.92           C  
ANISOU 2596  CE  MET B  83     6278   3984   4145    495    555   -550       C  
ATOM   2597  N   ASN B  84      43.281 -27.526 126.213  1.00 39.94           N  
ANISOU 2597  N   ASN B  84     6862   4131   4179   1119     14   -442       N  
ATOM   2598  CA  ASN B  84      44.425 -28.153 126.864  1.00 42.15           C  
ANISOU 2598  CA  ASN B  84     7233   4399   4382   1361   -193   -431       C  
ATOM   2599  C   ASN B  84      44.095 -29.563 127.296  1.00 42.68           C  
ANISOU 2599  C   ASN B  84     7768   4360   4087   1474   -146   -414       C  
ATOM   2600  O   ASN B  84      42.920 -29.936 127.384  1.00 41.43           O  
ANISOU 2600  O   ASN B  84     7863   4410   3468   1370   -133   -353       O  
ATOM   2601  CB  ASN B  84      44.852 -27.346 128.094  1.00 43.57           C  
ANISOU 2601  CB  ASN B  84     7433   4626   4494   1418   -403   -486       C  
ATOM   2602  CG  ASN B  84      45.292 -25.941 127.745  1.00 43.36           C  
ANISOU 2602  CG  ASN B  84     7162   4662   4648   1279   -437   -584       C  
ATOM   2603  OD1 ASN B  84      45.943 -25.717 126.733  1.00 43.31           O  
ANISOU 2603  OD1 ASN B  84     6719   4511   5223    811   -298   -410       O  
ATOM   2604  ND2 ASN B  84      44.941 -24.989 128.585  1.00 43.97           N  
ANISOU 2604  ND2 ASN B  84     7349   4751   4604   1188   -569   -658       N  
ATOM   2605  N   SER B  85      45.149 -30.330 127.570  1.00 45.34           N  
ANISOU 2605  N   SER B  85     8048   4659   4517   1745   -260   -429       N  
ATOM   2606  CA  SER B  85      45.046 -31.706 128.069  1.00 47.86           C  
ANISOU 2606  CA  SER B  85     8731   4717   4734   1924   -110   -278       C  
ATOM   2607  C   SER B  85      44.075 -32.527 127.227  1.00 47.00           C  
ANISOU 2607  C   SER B  85     8620   4579   4656   1655    171   -126       C  
ATOM   2608  O   SER B  85      43.198 -33.209 127.755  1.00 48.01           O  
ANISOU 2608  O   SER B  85     9223   4908   4110   1667    442    190       O  
ATOM   2609  CB  SER B  85      44.626 -31.708 129.545  1.00 49.71           C  
ANISOU 2609  CB  SER B  85     9313   4856   4716   2069   -130   -175       C  
ATOM   2610  OG  SER B  85      45.568 -31.014 130.341  1.00 52.17           O  
ANISOU 2610  OG  SER B  85     9206   5512   5102   2239   -497   -254       O  
ATOM   2611  N   LEU B  86      44.234 -32.443 125.908  1.00 45.31           N  
ANISOU 2611  N   LEU B  86     8213   4349   4651   1583    141   -232       N  
ATOM   2612  CA  LEU B  86      43.311 -33.094 124.993  1.00 44.13           C  
ANISOU 2612  CA  LEU B  86     8141   4054   4570   1438    387   -228       C  
ATOM   2613  C   LEU B  86      43.333 -34.610 125.167  1.00 46.39           C  
ANISOU 2613  C   LEU B  86     8684   4108   4831   1683    473    -18       C  
ATOM   2614  O   LEU B  86      44.384 -35.199 125.433  1.00 46.39           O  
ANISOU 2614  O   LEU B  86     9145   3966   4513   1912    233    278       O  
ATOM   2615  CB  LEU B  86      43.636 -32.737 123.543  1.00 42.94           C  
ANISOU 2615  CB  LEU B  86     7728   3964   4623   1239    395   -290       C  
ATOM   2616  CG  LEU B  86      43.170 -31.359 123.075  1.00 40.58           C  
ANISOU 2616  CG  LEU B  86     7068   3987   4360   1116    323   -265       C  
ATOM   2617  CD1 LEU B  86      43.886 -30.994 121.793  1.00 39.11           C  
ANISOU 2617  CD1 LEU B  86     6721   3906   4231   1248    227   -369       C  
ATOM   2618  CD2 LEU B  86      41.665 -31.326 122.887  1.00 39.71           C  
ANISOU 2618  CD2 LEU B  86     7066   3830   4191    915    409   -294       C  
ATOM   2619  N   LYS B  87      42.154 -35.209 125.016  1.00 51.57           N  
ANISOU 2619  N   LYS B  87    10272   4042   5277   1895   -121   -599       N  
ATOM   2620  CA  LYS B  87      41.953 -36.643 125.122  1.00 53.55           C  
ANISOU 2620  CA  LYS B  87    10948   4082   5314   1944    -26   -502       C  
ATOM   2621  C   LYS B  87      41.487 -37.175 123.773  1.00 50.42           C  
ANISOU 2621  C   LYS B  87    10229   3834   5093   1603    342   -342       C  
ATOM   2622  O   LYS B  87      40.925 -36.415 122.984  1.00 46.22           O  
ANISOU 2622  O   LYS B  87     9233   3915   4412   1236    394   -546       O  
ATOM   2623  CB  LYS B  87      40.859 -36.938 126.144  1.00 56.95           C  
ANISOU 2623  CB  LYS B  87    11851   4322   5464   1910    455   -376       C  
ATOM   2624  CG  LYS B  87      41.159 -36.504 127.565  1.00 60.24           C  
ANISOU 2624  CG  LYS B  87    12801   4538   5548   2391    152   -489       C  
ATOM   2625  CD  LYS B  87      39.937 -36.718 128.446  1.00 63.02           C  
ANISOU 2625  CD  LYS B  87    13601   4675   5668   2398    698   -190       C  
ATOM   2626  CE  LYS B  87      39.953 -35.819 129.664  1.00 65.95           C  
ANISOU 2626  CE  LYS B  87    14360   4998   5696   2629    488   -262       C  
ATOM   2627  NZ  LYS B  87      40.963 -36.258 130.662  1.00 71.48           N  
ANISOU 2627  NZ  LYS B  87    15342   5630   6187   3224     -9   -245       N  
ATOM   2628  N   PRO B  88      41.664 -38.490 123.522  1.00 52.17           N  
ANISOU 2628  N   PRO B  88    10585   3913   5321   1710    411   -427       N  
ATOM   2629  CA  PRO B  88      41.147 -39.086 122.271  1.00 50.37           C  
ANISOU 2629  CA  PRO B  88    10037   3783   5316   1288    546   -250       C  
ATOM   2630  C   PRO B  88      39.651 -38.810 122.042  1.00 48.22           C  
ANISOU 2630  C   PRO B  88     9751   3383   5186    951   1031   -386       C  
ATOM   2631  O   PRO B  88      39.250 -38.535 120.911  1.00 46.57           O  
ANISOU 2631  O   PRO B  88     9327   3049   5316    463    729   -611       O  
ATOM   2632  CB  PRO B  88      41.418 -40.588 122.441  1.00 52.92           C  
ANISOU 2632  CB  PRO B  88    10698   3855   5555   1564    761   -318       C  
ATOM   2633  CG  PRO B  88      42.484 -40.676 123.484  1.00 55.48           C  
ANISOU 2633  CG  PRO B  88    11367   4107   5605   1896    444   -385       C  
ATOM   2634  CD  PRO B  88      42.264 -39.510 124.405  1.00 55.32           C  
ANISOU 2634  CD  PRO B  88    11447   4141   5429   2075    320   -336       C  
ATOM   2635  N   GLU B  89      38.856 -38.835 123.112  1.00 49.00           N  
ANISOU 2635  N   GLU B  89    10196   3177   5244   1095   1260    -71       N  
ATOM   2636  CA  GLU B  89      37.421 -38.512 123.036  1.00 48.71           C  
ANISOU 2636  CA  GLU B  89    10061   3164   5282    898   1614   -227       C  
ATOM   2637  C   GLU B  89      37.081 -37.051 122.670  1.00 45.09           C  
ANISOU 2637  C   GLU B  89     9181   3166   4783    678   1419   -220       C  
ATOM   2638  O   GLU B  89      35.912 -36.732 122.460  1.00 44.84           O  
ANISOU 2638  O   GLU B  89     8893   3519   4623    528   1818   -278       O  
ATOM   2639  CB  GLU B  89      36.697 -38.889 124.340  1.00 52.47           C  
ANISOU 2639  CB  GLU B  89    11047   3411   5476   1097   2042    -91       C  
ATOM   2640  CG  GLU B  89      37.187 -38.165 125.597  1.00 55.57           C  
ANISOU 2640  CG  GLU B  89    11677   3953   5483   1225   1719    -76       C  
ATOM   2641  CD  GLU B  89      37.961 -39.066 126.558  1.00 59.43           C  
ANISOU 2641  CD  GLU B  89    12717   4122   5742   1754   1849    116       C  
ATOM   2642  OE1 GLU B  89      38.741 -39.942 126.094  1.00 56.79           O  
ANISOU 2642  OE1 GLU B  89    12754   3503   5318   1790   1715    259       O  
ATOM   2643  OE2 GLU B  89      37.783 -38.878 127.787  1.00 66.23           O  
ANISOU 2643  OE2 GLU B  89    13928   5556   5680   1481   1981    220       O  
ATOM   2644  N   ASP B  90      38.082 -36.169 122.611  1.00 43.74           N  
ANISOU 2644  N   ASP B  90     8949   3111   4558    798   1063   -291       N  
ATOM   2645  CA  ASP B  90      37.898 -34.810 122.063  1.00 41.32           C  
ANISOU 2645  CA  ASP B  90     8191   2995   4513    739    925   -425       C  
ATOM   2646  C   ASP B  90      37.988 -34.757 120.538  1.00 39.02           C  
ANISOU 2646  C   ASP B  90     7552   2771   4500    653    941   -427       C  
ATOM   2647  O   ASP B  90      37.874 -33.685 119.957  1.00 38.23           O  
ANISOU 2647  O   ASP B  90     7069   2692   4762    731   1028   -453       O  
ATOM   2648  CB  ASP B  90      38.922 -33.835 122.666  1.00 41.81           C  
ANISOU 2648  CB  ASP B  90     8170   3202   4514    851    569   -411       C  
ATOM   2649  CG  ASP B  90      38.775 -33.687 124.175  1.00 44.20           C  
ANISOU 2649  CG  ASP B  90     8754   3544   4496   1141    632   -409       C  
ATOM   2650  OD1 ASP B  90      37.636 -33.548 124.649  1.00 43.77           O  
ANISOU 2650  OD1 ASP B  90     9107   3739   3782    780   1091   -313       O  
ATOM   2651  OD2 ASP B  90      39.803 -33.695 124.887  1.00 46.16           O  
ANISOU 2651  OD2 ASP B  90     9423   3927   4186   1248    244   -420       O  
ATOM   2652  N   THR B  91      38.213 -35.901 119.891  1.00 38.34           N  
ANISOU 2652  N   THR B  91     7552   2728   4285    403    920   -386       N  
ATOM   2653  CA  THR B  91      38.260 -35.979 118.437  1.00 35.07           C  
ANISOU 2653  CA  THR B  91     6537   2510   4275    339    929   -618       C  
ATOM   2654  C   THR B  91      36.895 -35.650 117.846  1.00 33.50           C  
ANISOU 2654  C   THR B  91     6265   2295   4165    132   1139   -607       C  
ATOM   2655  O   THR B  91      35.897 -36.262 118.208  1.00 35.00           O  
ANISOU 2655  O   THR B  91     6584   2171   4540    -16   1521   -876       O  
ATOM   2656  CB  THR B  91      38.723 -37.375 117.998  1.00 35.06           C  
ANISOU 2656  CB  THR B  91     6708   2396   4215    412    929   -425       C  
ATOM   2657  OG1 THR B  91      40.056 -37.566 118.477  1.00 36.26           O  
ANISOU 2657  OG1 THR B  91     6953   2731   4091    556    671   -344       O  
ATOM   2658  CG2 THR B  91      38.704 -37.537 116.470  1.00 33.03           C  
ANISOU 2658  CG2 THR B  91     6159   2158   4232    282    900   -590       C  
ATOM   2659  N   ALA B  92      36.863 -34.679 116.944  1.00 31.34           N  
ANISOU 2659  N   ALA B  92     5677   2080   4149     90    965   -704       N  
ATOM   2660  CA  ALA B  92      35.604 -34.216 116.352  1.00 31.38           C  
ANISOU 2660  CA  ALA B  92     5455   2255   4209    -68   1026   -740       C  
ATOM   2661  C   ALA B  92      35.877 -33.087 115.372  1.00 29.75           C  
ANISOU 2661  C   ALA B  92     5045   2402   3856    -20    879   -763       C  
ATOM   2662  O   ALA B  92      36.981 -32.537 115.334  1.00 29.94           O  
ANISOU 2662  O   ALA B  92     4984   2634   3757    -15    794   -853       O  
ATOM   2663  CB  ALA B  92      34.638 -33.729 117.449  1.00 31.51           C  
ANISOU 2663  CB  ALA B  92     5612   2165   4194   -173   1151   -681       C  
ATOM   2664  N   VAL B  93      34.864 -32.754 114.581  1.00 29.46           N  
ANISOU 2664  N   VAL B  93     4828   2357   4007    -79    894   -907       N  
ATOM   2665  CA  VAL B  93      34.822 -31.492 113.852  1.00 28.61           C  
ANISOU 2665  CA  VAL B  93     4601   2423   3845    -43    776   -859       C  
ATOM   2666  C   VAL B  93      34.286 -30.463 114.851  1.00 28.33           C  
ANISOU 2666  C   VAL B  93     4540   2393   3830   -124    727   -882       C  
ATOM   2667  O   VAL B  93      33.244 -30.700 115.465  1.00 28.95           O  
ANISOU 2667  O   VAL B  93     4885   2771   3343    -88    961  -1187       O  
ATOM   2668  CB  VAL B  93      33.868 -31.563 112.649  1.00 29.28           C  
ANISOU 2668  CB  VAL B  93     4555   2516   4050    -23    693  -1018       C  
ATOM   2669  CG1 VAL B  93      33.826 -30.226 111.905  1.00 29.15           C  
ANISOU 2669  CG1 VAL B  93     4501   2635   3936     29    587   -974       C  
ATOM   2670  CG2 VAL B  93      34.283 -32.687 111.705  1.00 29.95           C  
ANISOU 2670  CG2 VAL B  93     4686   2591   4100    -36    667  -1089       C  
ATOM   2671  N   TYR B  94      34.982 -29.346 115.026  1.00 27.12           N  
ANISOU 2671  N   TYR B  94     4425   2237   3640    -38    649   -681       N  
ATOM   2672  CA  TYR B  94      34.527 -28.305 115.951  1.00 27.42           C  
ANISOU 2672  CA  TYR B  94     4439   2311   3666    -60    711   -687       C  
ATOM   2673  C   TYR B  94      33.895 -27.180 115.146  1.00 27.55           C  
ANISOU 2673  C   TYR B  94     4382   2389   3694   -146    601   -665       C  
ATOM   2674  O   TYR B  94      34.481 -26.701 114.173  1.00 26.28           O  
ANISOU 2674  O   TYR B  94     4194   2195   3596    -50    676   -856       O  
ATOM   2675  CB  TYR B  94      35.667 -27.778 116.830  1.00 26.95           C  
ANISOU 2675  CB  TYR B  94     4482   2157   3598     27    636   -608       C  
ATOM   2676  CG  TYR B  94      36.027 -28.721 117.957  1.00 28.64           C  
ANISOU 2676  CG  TYR B  94     5047   2214   3620     47    579   -583       C  
ATOM   2677  CD1 TYR B  94      35.827 -28.368 119.286  1.00 29.14           C  
ANISOU 2677  CD1 TYR B  94     5347   2068   3656     57    610   -628       C  
ATOM   2678  CD2 TYR B  94      36.530 -30.011 117.690  1.00 29.62           C  
ANISOU 2678  CD2 TYR B  94     5191   2316   3746    208    594   -559       C  
ATOM   2679  CE1 TYR B  94      36.161 -29.243 120.320  1.00 30.66           C  
ANISOU 2679  CE1 TYR B  94     5762   2179   3706    164    669   -540       C  
ATOM   2680  CE2 TYR B  94      36.849 -30.890 118.709  1.00 30.20           C  
ANISOU 2680  CE2 TYR B  94     5546   2113   3816    133    682   -508       C  
ATOM   2681  CZ  TYR B  94      36.669 -30.506 120.021  1.00 31.38           C  
ANISOU 2681  CZ  TYR B  94     5842   2260   3821    310    781   -474       C  
ATOM   2682  OH  TYR B  94      36.989 -31.373 121.040  1.00 33.39           O  
ANISOU 2682  OH  TYR B  94     6420   2380   3886    453    902   -390       O  
ATOM   2683  N   TYR B  95      32.690 -26.785 115.557  1.00 29.11           N  
ANISOU 2683  N   TYR B  95     4433   2719   3905   -167    671   -871       N  
ATOM   2684  CA  TYR B  95      31.896 -25.786 114.856  1.00 30.16           C  
ANISOU 2684  CA  TYR B  95     4605   2745   4107   -129    603   -822       C  
ATOM   2685  C   TYR B  95      31.715 -24.581 115.748  1.00 30.52           C  
ANISOU 2685  C   TYR B  95     4682   2803   4108    -52    596   -822       C  
ATOM   2686  O   TYR B  95      31.437 -24.704 116.940  1.00 30.04           O  
ANISOU 2686  O   TYR B  95     4966   2388   4057   -215    563  -1012       O  
ATOM   2687  CB  TYR B  95      30.514 -26.329 114.474  1.00 32.06           C  
ANISOU 2687  CB  TYR B  95     4625   3117   4439   -167    557  -1035       C  
ATOM   2688  CG  TYR B  95      30.523 -27.461 113.446  1.00 33.11           C  
ANISOU 2688  CG  TYR B  95     4682   3188   4710    -79    594  -1232       C  
ATOM   2689  CD1 TYR B  95      30.495 -27.185 112.077  1.00 34.19           C  
ANISOU 2689  CD1 TYR B  95     4881   3382   4726     19    564  -1281       C  
ATOM   2690  CD2 TYR B  95      30.522 -28.793 113.846  1.00 34.82           C  
ANISOU 2690  CD2 TYR B  95     5095   3188   4944   -201    852  -1229       C  
ATOM   2691  CE1 TYR B  95      30.484 -28.202 111.131  1.00 36.07           C  
ANISOU 2691  CE1 TYR B  95     5173   3617   4914     -8    509  -1456       C  
ATOM   2692  CE2 TYR B  95      30.513 -29.828 112.908  1.00 36.65           C  
ANISOU 2692  CE2 TYR B  95     5332   3402   5189   -273    557  -1414       C  
ATOM   2693  CZ  TYR B  95      30.498 -29.523 111.554  1.00 37.46           C  
ANISOU 2693  CZ  TYR B  95     5356   3660   5216    -68    672  -1354       C  
ATOM   2694  OH  TYR B  95      30.479 -30.524 110.620  1.00 42.29           O  
ANISOU 2694  OH  TYR B  95     6148   3992   5927    115    911  -1747       O  
ATOM   2695  N   CYS B  96      31.841 -23.425 115.120  1.00 30.36           N  
ANISOU 2695  N   CYS B  96     4447   2978   4110   -362    529   -701       N  
ATOM   2696  CA  CYS B  96      31.638 -22.126 115.721  1.00 31.35           C  
ANISOU 2696  CA  CYS B  96     4525   3102   4283    -73    473   -712       C  
ATOM   2697  C   CYS B  96      30.232 -21.671 115.343  1.00 29.82           C  
ANISOU 2697  C   CYS B  96     4340   2844   4143   -221    656   -780       C  
ATOM   2698  O   CYS B  96      29.816 -21.846 114.195  1.00 28.41           O  
ANISOU 2698  O   CYS B  96     3780   2919   4092    130    760   -825       O  
ATOM   2699  CB  CYS B  96      32.685 -21.180 115.122  1.00 34.83           C  
ANISOU 2699  CB  CYS B  96     4744   3769   4719   -261    482   -300       C  
ATOM   2700  SG  CYS B  96      32.508 -19.448 115.516  1.00 40.90           S  
ANISOU 2700  SG  CYS B  96     5099   3971   6468   -597    773   -248       S  
ATOM   2701  N   ALA B  97      29.500 -21.106 116.302  1.00 29.59           N  
ANISOU 2701  N   ALA B  97     4381   2754   4106   -299    533   -921       N  
ATOM   2702  CA  ALA B  97      28.127 -20.614 116.066  1.00 30.73           C  
ANISOU 2702  CA  ALA B  97     4374   3038   4261   -172    588  -1012       C  
ATOM   2703  C   ALA B  97      27.862 -19.280 116.752  1.00 30.36           C  
ANISOU 2703  C   ALA B  97     4375   2947   4213   -246    591   -953       C  
ATOM   2704  O   ALA B  97      28.518 -18.944 117.729  1.00 29.37           O  
ANISOU 2704  O   ALA B  97     4471   2784   3903   -143    659   -639       O  
ATOM   2705  CB  ALA B  97      27.096 -21.647 116.507  1.00 31.22           C  
ANISOU 2705  CB  ALA B  97     4337   2953   4571   -241    653  -1270       C  
ATOM   2706  N   ALA B  98      26.897 -18.530 116.225  1.00 31.77           N  
ANISOU 2706  N   ALA B  98     4477   3278   4315   -120    390  -1173       N  
ATOM   2707  CA  ALA B  98      26.528 -17.207 116.756  1.00 32.11           C  
ANISOU 2707  CA  ALA B  98     4476   3310   4413    -82    588  -1077       C  
ATOM   2708  C   ALA B  98      25.024 -17.077 116.948  1.00 33.00           C  
ANISOU 2708  C   ALA B  98     4382   3432   4722   -198    392  -1267       C  
ATOM   2709  O   ALA B  98      24.240 -17.709 116.252  1.00 35.81           O  
ANISOU 2709  O   ALA B  98     4686   4020   4900   -346    322  -1588       O  
ATOM   2710  CB  ALA B  98      27.029 -16.094 115.852  1.00 31.65           C  
ANISOU 2710  CB  ALA B  98     4470   3443   4112      2    539  -1024       C  
ATOM   2711  N   ARG B  99      24.654 -16.244 117.912  1.00 32.49           N  
ANISOU 2711  N   ARG B  99     4450   3237   4657   -318    626  -1083       N  
ATOM   2712  CA  ARG B  99      23.269 -15.971 118.267  1.00 35.04           C  
ANISOU 2712  CA  ARG B  99     4480   3556   5278   -187    542  -1419       C  
ATOM   2713  C   ARG B  99      23.206 -14.504 118.680  1.00 32.79           C  
ANISOU 2713  C   ARG B  99     4209   3488   4761   -165    464  -1304       C  
ATOM   2714  O   ARG B  99      24.001 -14.075 119.525  1.00 28.37           O  
ANISOU 2714  O   ARG B  99     3927   2357   4495    -90    809  -1371       O  
ATOM   2715  CB  ARG B  99      22.864 -16.876 119.439  1.00 38.18           C  
ANISOU 2715  CB  ARG B  99     4939   3767   5799   -437    839  -1254       C  
ATOM   2716  CG  ARG B  99      21.380 -17.128 119.596  1.00 42.64           C  
ANISOU 2716  CG  ARG B  99     5036   4389   6776   -536   1032  -1581       C  
ATOM   2717  CD  ARG B  99      20.710 -16.025 120.375  1.00 45.12           C  
ANISOU 2717  CD  ARG B  99     5643   4635   6865   -465   1061  -1790       C  
ATOM   2718  NE  ARG B  99      19.322 -16.327 120.721  1.00 49.85           N  
ANISOU 2718  NE  ARG B  99     5859   5196   7883   -698   1320  -1811       N  
ATOM   2719  CZ  ARG B  99      18.534 -15.522 121.434  1.00 53.72           C  
ANISOU 2719  CZ  ARG B  99     6089   5488   8834   -501   1475  -2079       C  
ATOM   2720  NH1 ARG B  99      18.986 -14.351 121.896  1.00 56.07           N  
ANISOU 2720  NH1 ARG B  99     6737   5370   9197   -672   1515  -1996       N  
ATOM   2721  NH2 ARG B  99      17.286 -15.891 121.695  1.00 57.70           N  
ANISOU 2721  NH2 ARG B  99     6364   5540  10017   -969   1642  -2083       N  
ATOM   2722  N   TYR B 100      22.286 -13.741 118.082  1.00 33.52           N  
ANISOU 2722  N   TYR B 100     4336   3574   4825     44    418  -1458       N  
ATOM   2723  CA  TYR B 100      22.110 -12.337 118.458  1.00 32.51           C  
ANISOU 2723  CA  TYR B 100     4178   3480   4694    -81    367  -1374       C  
ATOM   2724  C   TYR B 100      21.770 -12.253 119.942  1.00 31.76           C  
ANISOU 2724  C   TYR B 100     3992   3336   4735   -233    495  -1259       C  
ATOM   2725  O   TYR B 100      20.944 -13.016 120.440  1.00 33.93           O  
ANISOU 2725  O   TYR B 100     3880   3744   5266   -437    512  -1259       O  
ATOM   2726  CB  TYR B 100      21.019 -11.610 117.650  1.00 33.80           C  
ANISOU 2726  CB  TYR B 100     4269   3677   4894    135    262  -1559       C  
ATOM   2727  CG  TYR B 100      20.836 -10.183 118.165  1.00 33.71           C  
ANISOU 2727  CG  TYR B 100     4315   3642   4852    133    316  -1489       C  
ATOM   2728  CD1 TYR B 100      21.745  -9.173 117.824  1.00 33.33           C  
ANISOU 2728  CD1 TYR B 100     4439   3670   4554    180    277  -1239       C  
ATOM   2729  CD2 TYR B 100      19.810  -9.862 119.065  1.00 33.90           C  
ANISOU 2729  CD2 TYR B 100     4071   3648   5160    -21    374  -1581       C  
ATOM   2730  CE1 TYR B 100      21.603  -7.869 118.325  1.00 32.67           C  
ANISOU 2730  CE1 TYR B 100     4417   3655   4338    216    299  -1169       C  
ATOM   2731  CE2 TYR B 100      19.667  -8.572 119.570  1.00 33.46           C  
ANISOU 2731  CE2 TYR B 100     4077   3696   4937     99    403  -1548       C  
ATOM   2732  CZ  TYR B 100      20.563  -7.578 119.196  1.00 32.51           C  
ANISOU 2732  CZ  TYR B 100     4231   3543   4578    253    284  -1228       C  
ATOM   2733  OH  TYR B 100      20.434  -6.300 119.700  1.00 32.66           O  
ANISOU 2733  OH  TYR B 100     4579   3553   4274    230   -119  -1187       O  
ATOM   2734  N   GLN B 101      22.419 -11.319 120.632  1.00 29.98           N  
ANISOU 2734  N   GLN B 101     4075   2957   4360   -225    621  -1041       N  
ATOM   2735  CA  GLN B 101      22.255 -11.128 122.065  1.00 29.61           C  
ANISOU 2735  CA  GLN B 101     4060   2817   4371   -412    851   -985       C  
ATOM   2736  C   GLN B 101      22.108  -9.627 122.326  1.00 28.61           C  
ANISOU 2736  C   GLN B 101     3895   2803   4172   -326    881   -917       C  
ATOM   2737  O   GLN B 101      22.915  -8.848 121.827  1.00 26.60           O  
ANISOU 2737  O   GLN B 101     3725   2459   3921    -76    869   -946       O  
ATOM   2738  CB  GLN B 101      23.493 -11.665 122.799  1.00 28.93           C  
ANISOU 2738  CB  GLN B 101     4184   2695   4111   -433    916   -812       C  
ATOM   2739  CG  GLN B 101      23.395 -11.610 124.316  1.00 29.45           C  
ANISOU 2739  CG  GLN B 101     4462   2631   4096   -508   1056   -813       C  
ATOM   2740  CD  GLN B 101      24.558 -12.299 124.987  1.00 29.10           C  
ANISOU 2740  CD  GLN B 101     4592   2542   3922   -494   1095   -734       C  
ATOM   2741  OE1 GLN B 101      25.705 -11.963 124.734  1.00 29.01           O  
ANISOU 2741  OE1 GLN B 101     4799   2124   4099   -846    942   -765       O  
ATOM   2742  NE2 GLN B 101      24.274 -13.271 125.842  1.00 31.76           N  
ANISOU 2742  NE2 GLN B 101     5057   2736   4275   -649   1214   -553       N  
ATOM   2743  N   PRO B 102      21.091  -9.211 123.105  1.00 29.41           N  
ANISOU 2743  N   PRO B 102     3996   2841   4335   -463    981  -1083       N  
ATOM   2744  CA  PRO B 102      21.023  -7.794 123.481  1.00 28.38           C  
ANISOU 2744  CA  PRO B 102     3889   2777   4117   -270    885   -961       C  
ATOM   2745  C   PRO B 102      22.252  -7.311 124.263  1.00 27.13           C  
ANISOU 2745  C   PRO B 102     3945   2514   3848   -269    897   -812       C  
ATOM   2746  O   PRO B 102      22.910  -8.102 124.950  1.00 27.10           O  
ANISOU 2746  O   PRO B 102     4163   2582   3548   -194    988   -805       O  
ATOM   2747  CB  PRO B 102      19.792  -7.725 124.384  1.00 29.55           C  
ANISOU 2747  CB  PRO B 102     3975   2846   4404   -446   1099  -1098       C  
ATOM   2748  CG  PRO B 102      18.971  -8.899 124.009  1.00 31.53           C  
ANISOU 2748  CG  PRO B 102     4104   2991   4886   -493   1171  -1355       C  
ATOM   2749  CD  PRO B 102      19.948  -9.971 123.645  1.00 30.99           C  
ANISOU 2749  CD  PRO B 102     4026   2939   4808   -525   1140  -1212       C  
ATOM   2750  N   ARG B 103      22.539  -6.015 124.181  1.00 25.76           N  
ANISOU 2750  N   ARG B 103     3629   2583   3574   -309    813   -641       N  
ATOM   2751  CA  ARG B 103      23.593  -5.432 125.001  1.00 24.72           C  
ANISOU 2751  CA  ARG B 103     3795   2278   3318   -301    845   -662       C  
ATOM   2752  C   ARG B 103      23.349  -5.729 126.483  1.00 24.79           C  
ANISOU 2752  C   ARG B 103     3992   2085   3342   -337    849   -627       C  
ATOM   2753  O   ARG B 103      24.267  -6.168 127.184  1.00 24.10           O  
ANISOU 2753  O   ARG B 103     4109   1682   3363   -407    754   -690       O  
ATOM   2754  CB  ARG B 103      23.712  -3.936 124.762  1.00 24.31           C  
ANISOU 2754  CB  ARG B 103     3697   2297   3241   -213    671   -534       C  
ATOM   2755  CG  ARG B 103      24.856  -3.291 125.536  1.00 23.94           C  
ANISOU 2755  CG  ARG B 103     3716   2193   3186   -255    632   -401       C  
ATOM   2756  CD  ARG B 103      25.116  -1.855 125.132  1.00 23.19           C  
ANISOU 2756  CD  ARG B 103     3589   2134   3085   -169    618   -386       C  
ATOM   2757  NE  ARG B 103      26.236  -1.286 125.892  1.00 23.09           N  
ANISOU 2757  NE  ARG B 103     3754   1846   3172   -163    583   -511       N  
ATOM   2758  CZ  ARG B 103      27.101  -0.361 125.446  1.00 23.98           C  
ANISOU 2758  CZ  ARG B 103     3628   2162   3321   -200    634   -403       C  
ATOM   2759  NH1 ARG B 103      27.028   0.138 124.213  1.00 24.07           N  
ANISOU 2759  NH1 ARG B 103     3587   2107   3451    -64    687   -251       N  
ATOM   2760  NH2 ARG B 103      28.065   0.080 126.250  1.00 24.91           N  
ANISOU 2760  NH2 ARG B 103     3639   2233   3592   -261    539   -417       N  
ATOM   2761  N   TYR B 104      22.105  -5.520 126.926  1.00 25.30           N  
ANISOU 2761  N   TYR B 104     4088   2039   3484   -325   1027   -638       N  
ATOM   2762  CA  TYR B 104      21.704  -5.749 128.305  1.00 26.86           C  
ANISOU 2762  CA  TYR B 104     4428   2198   3578   -358   1194   -578       C  
ATOM   2763  C   TYR B 104      20.884  -7.036 128.392  1.00 28.82           C  
ANISOU 2763  C   TYR B 104     4512   2363   4074   -504   1448   -761       C  
ATOM   2764  O   TYR B 104      19.667  -7.005 128.525  1.00 30.27           O  
ANISOU 2764  O   TYR B 104     4576   2388   4536   -380   1780   -835       O  
ATOM   2765  CB  TYR B 104      20.970  -4.515 128.869  1.00 26.67           C  
ANISOU 2765  CB  TYR B 104     4400   2182   3552   -417   1211   -592       C  
ATOM   2766  CG  TYR B 104      21.883  -3.310 128.848  1.00 25.80           C  
ANISOU 2766  CG  TYR B 104     4318   2166   3317   -370   1012   -516       C  
ATOM   2767  CD1 TYR B 104      22.901  -3.174 129.795  1.00 25.49           C  
ANISOU 2767  CD1 TYR B 104     4528   2010   3144   -240    947   -492       C  
ATOM   2768  CD2 TYR B 104      21.785  -2.351 127.833  1.00 24.91           C  
ANISOU 2768  CD2 TYR B 104     4005   2144   3317   -287    888   -556       C  
ATOM   2769  CE1 TYR B 104      23.770  -2.093 129.765  1.00 25.27           C  
ANISOU 2769  CE1 TYR B 104     4376   2164   3060   -247    806   -448       C  
ATOM   2770  CE2 TYR B 104      22.651  -1.263 127.789  1.00 24.23           C  
ANISOU 2770  CE2 TYR B 104     3834   2147   3222   -203    842   -474       C  
ATOM   2771  CZ  TYR B 104      23.636  -1.137 128.761  1.00 24.49           C  
ANISOU 2771  CZ  TYR B 104     4180   2063   3062   -215    738   -510       C  
ATOM   2772  OH  TYR B 104      24.506  -0.090 128.713  1.00 23.93           O  
ANISOU 2772  OH  TYR B 104     4230   2049   2810   -206    664   -456       O  
ATOM   2773  N   TYR B 105      21.591  -8.164 128.298  1.00 28.98           N  
ANISOU 2773  N   TYR B 105     4755   2351   3902   -423   1492   -587       N  
ATOM   2774  CA  TYR B 105      20.989  -9.498 128.357  1.00 31.07           C  
ANISOU 2774  CA  TYR B 105     5057   2390   4358   -495   1631   -838       C  
ATOM   2775  C   TYR B 105      20.746  -9.955 129.810  1.00 34.12           C  
ANISOU 2775  C   TYR B 105     5793   2684   4484   -371   2070   -765       C  
ATOM   2776  O   TYR B 105      21.435  -9.493 130.722  1.00 33.51           O  
ANISOU 2776  O   TYR B 105     6034   2482   4216   -111   2143   -882       O  
ATOM   2777  CB  TYR B 105      21.881 -10.532 127.621  1.00 29.74           C  
ANISOU 2777  CB  TYR B 105     4805   2425   4070   -479   1518   -746       C  
ATOM   2778  CG  TYR B 105      23.264 -10.758 128.229  1.00 28.12           C  
ANISOU 2778  CG  TYR B 105     4963   2128   3593   -413   1469   -645       C  
ATOM   2779  CD1 TYR B 105      23.455 -11.646 129.291  1.00 29.46           C  
ANISOU 2779  CD1 TYR B 105     5421   2052   3721   -330   1587   -558       C  
ATOM   2780  CD2 TYR B 105      24.375 -10.097 127.727  1.00 25.91           C  
ANISOU 2780  CD2 TYR B 105     4659   1878   3306   -356   1118   -720       C  
ATOM   2781  CE1 TYR B 105      24.715 -11.847 129.842  1.00 29.77           C  
ANISOU 2781  CE1 TYR B 105     5676   2069   3563   -249   1389   -462       C  
ATOM   2782  CE2 TYR B 105      25.639 -10.290 128.265  1.00 25.69           C  
ANISOU 2782  CE2 TYR B 105     4847   1870   3041   -186   1039   -619       C  
ATOM   2783  CZ  TYR B 105      25.814 -11.159 129.314  1.00 27.42           C  
ANISOU 2783  CZ  TYR B 105     5288   1939   3191    -66   1113   -518       C  
ATOM   2784  OH  TYR B 105      27.078 -11.318 129.837  1.00 27.45           O  
ANISOU 2784  OH  TYR B 105     5392   2019   3017    187   1041   -676       O  
ATOM   2785  N   ASP B 106      19.778 -10.857 130.007  1.00 38.78           N  
ANISOU 2785  N   ASP B 106     6367   2819   5546   -724   2234   -929       N  
ATOM   2786  CA  ASP B 106      19.628 -11.604 131.279  1.00 44.66           C  
ANISOU 2786  CA  ASP B 106     7660   3468   5839   -620   2646   -613       C  
ATOM   2787  C   ASP B 106      20.506 -12.838 131.177  1.00 45.00           C  
ANISOU 2787  C   ASP B 106     7969   3159   5970   -691   2724   -444       C  
ATOM   2788  O   ASP B 106      20.442 -13.529 130.182  1.00 46.62           O  
ANISOU 2788  O   ASP B 106     8377   3072   6262   -953   2497   -479       O  
ATOM   2789  CB  ASP B 106      18.193 -12.087 131.507  1.00 50.09           C  
ANISOU 2789  CB  ASP B 106     7919   4082   7031   -814   3207   -876       C  
ATOM   2790  CG  ASP B 106      17.164 -11.004 131.297  1.00 52.82           C  
ANISOU 2790  CG  ASP B 106     7954   4519   7596   -710   2578   -846       C  
ATOM   2791  OD1 ASP B 106      17.295  -9.907 131.893  1.00 59.49           O  
ANISOU 2791  OD1 ASP B 106     9448   4668   8487  -1452   2067   -870       O  
ATOM   2792  OD2 ASP B 106      16.209 -11.266 130.537  1.00 59.31           O  
ANISOU 2792  OD2 ASP B 106     7803   6366   8366  -1321   2649   -899       O  
ATOM   2793  N   SER B 107      21.310 -13.133 132.190  1.00 62.01           N  
ANISOU 2793  N   SER B 107     7113   5737  10708  -1376   -867  -2540       N  
ATOM   2794  CA  SER B 107      22.233 -14.277 132.107  1.00 58.00           C  
ANISOU 2794  CA  SER B 107     6888   6153   8995  -1191   -426  -1380       C  
ATOM   2795  C   SER B 107      21.496 -15.626 132.033  1.00 56.73           C  
ANISOU 2795  C   SER B 107     6931   6053   8571  -1059   -227  -1367       C  
ATOM   2796  O   SER B 107      22.018 -16.580 131.447  1.00 55.59           O  
ANISOU 2796  O   SER B 107     7964   5427   7730   -846   -463   -828       O  
ATOM   2797  CB  SER B 107      23.212 -14.280 133.278  1.00 60.79           C  
ANISOU 2797  CB  SER B 107     6917   7900   8281  -1635    -13  -1460       C  
ATOM   2798  OG  SER B 107      24.264 -15.199 133.044  1.00 60.24           O  
ANISOU 2798  OG  SER B 107     6867   8386   7635  -1296    416   -116       O  
ATOM   2799  N   GLY B 108      20.298 -15.684 132.626  1.00 58.90           N  
ANISOU 2799  N   GLY B 108     6802   6635   8941  -1238    -70  -2087       N  
ATOM   2800  CA  GLY B 108      19.404 -16.817 132.504  1.00 60.15           C  
ANISOU 2800  CA  GLY B 108     6867   6685   9301  -1328    542  -1893       C  
ATOM   2801  C   GLY B 108      19.194 -17.270 131.070  1.00 59.65           C  
ANISOU 2801  C   GLY B 108     7457   5874   9332  -1042    121  -1627       C  
ATOM   2802  O   GLY B 108      19.300 -18.457 130.782  1.00 59.30           O  
ANISOU 2802  O   GLY B 108     8155   5666   8708  -2171    285  -1570       O  
ATOM   2803  N   ASP B 109      18.956 -16.318 130.167  1.00 61.40           N  
ANISOU 2803  N   ASP B 109     7483   5588  10258   -358   -632  -1747       N  
ATOM   2804  CA  ASP B 109      18.675 -16.623 128.752  1.00 63.07           C  
ANISOU 2804  CA  ASP B 109     7731   5851  10382   -681  -1332  -1259       C  
ATOM   2805  C   ASP B 109      19.850 -17.274 127.973  1.00 61.17           C  
ANISOU 2805  C   ASP B 109     8050   5967   9222   -827  -1120   -827       C  
ATOM   2806  O   ASP B 109      19.639 -17.856 126.913  1.00 66.25           O  
ANISOU 2806  O   ASP B 109     9176   6863   9134   -577  -1123  -1092       O  
ATOM   2807  CB  ASP B 109      18.175 -15.362 128.027  1.00 68.90           C  
ANISOU 2807  CB  ASP B 109     8274   5859  12046   -698  -2316  -1008       C  
ATOM   2808  CG  ASP B 109      16.853 -14.826 128.605  1.00 75.95           C  
ANISOU 2808  CG  ASP B 109     8100   6538  14218   -486  -2539  -1883       C  
ATOM   2809  OD1 ASP B 109      16.617 -13.600 128.525  1.00 84.83           O  
ANISOU 2809  OD1 ASP B 109     8706   6659  16865   -277  -3252  -1688       O  
ATOM   2810  OD2 ASP B 109      16.049 -15.616 129.148  1.00 73.16           O  
ANISOU 2810  OD2 ASP B 109     7784   5850  14161   -640  -2170  -2923       O  
ATOM   2811  N   MET B 110      21.066 -17.178 128.515  1.00 55.58           N  
ANISOU 2811  N   MET B 110     7645   4819   8652  -1102   -571   -324       N  
ATOM   2812  CA  MET B 110      22.247 -17.907 128.022  1.00 52.25           C  
ANISOU 2812  CA  MET B 110     7634   4642   7575  -1528     27      3       C  
ATOM   2813  C   MET B 110      22.117 -19.453 127.977  1.00 54.97           C  
ANISOU 2813  C   MET B 110     7810   4674   8400  -1353   1135    -65       C  
ATOM   2814  O   MET B 110      22.882 -20.111 127.282  1.00 58.81           O  
ANISOU 2814  O   MET B 110     8801   3543   9999  -1288   1560   -416       O  
ATOM   2815  CB  MET B 110      23.452 -17.553 128.895  1.00 49.54           C  
ANISOU 2815  CB  MET B 110     7287   4373   7162  -1477    227    681       C  
ATOM   2816  CG  MET B 110      24.799 -17.731 128.233  1.00 48.86           C  
ANISOU 2816  CG  MET B 110     7493   4199   6871  -1597    421   1167       C  
ATOM   2817  SD  MET B 110      25.425 -16.234 127.420  1.00 48.53           S  
ANISOU 2817  SD  MET B 110     7746   4253   6437  -1731   -367   1625       S  
ATOM   2818  CE  MET B 110      26.754 -16.995 126.499  1.00 49.72           C  
ANISOU 2818  CE  MET B 110     7928   4814   6147  -2542    159   1015       C  
ATOM   2819  N   ASP B 111      21.183 -20.035 128.719  1.00 56.95           N  
ANISOU 2819  N   ASP B 111     7641   4861   9135  -1376   1399    -23       N  
ATOM   2820  CA  ASP B 111      20.991 -21.490 128.711  1.00 62.06           C  
ANISOU 2820  CA  ASP B 111     8314   4920  10345  -1305   2366   -453       C  
ATOM   2821  C   ASP B 111      20.114 -21.994 127.564  1.00 65.72           C  
ANISOU 2821  C   ASP B 111     8550   5455  10962  -1805   2613  -1410       C  
ATOM   2822  O   ASP B 111      20.229 -23.158 127.170  1.00 71.30           O  
ANISOU 2822  O   ASP B 111     9052   5266  12772  -1826   3631  -1418       O  
ATOM   2823  CB  ASP B 111      20.386 -21.954 130.038  1.00 66.70           C  
ANISOU 2823  CB  ASP B 111     8564   5646  11131  -1632   2801    187       C  
ATOM   2824  CG  ASP B 111      21.253 -21.598 131.237  1.00 70.35           C  
ANISOU 2824  CG  ASP B 111     8684   7334  10709  -1006   2414   1144       C  
ATOM   2825  OD1 ASP B 111      20.687 -21.101 132.233  1.00 75.83           O  
ANISOU 2825  OD1 ASP B 111     9459   8845  10506   -852   2149    538       O  
ATOM   2826  OD2 ASP B 111      22.490 -21.803 131.186  1.00 72.08           O  
ANISOU 2826  OD2 ASP B 111     8904   7699  10783    -77   2758   2043       O  
ATOM   2827  N   GLY B 112      19.240 -21.134 127.037  1.00 65.45           N  
ANISOU 2827  N   GLY B 112     8569   5949  10347  -1988   1621  -1902       N  
ATOM   2828  CA  GLY B 112      18.229 -21.550 126.053  1.00 69.89           C  
ANISOU 2828  CA  GLY B 112     8905   7052  10597  -2697   1867  -2717       C  
ATOM   2829  C   GLY B 112      18.463 -21.119 124.614  1.00 72.29           C  
ANISOU 2829  C   GLY B 112     8945   8369  10153  -3543   1227  -2959       C  
ATOM   2830  O   GLY B 112      17.546 -21.225 123.792  1.00 77.69           O  
ANISOU 2830  O   GLY B 112     9376   9735  10405  -4308    984  -3585       O  
ATOM   2831  N   TYR B 113      19.673 -20.646 124.301  1.00 68.89           N  
ANISOU 2831  N   TYR B 113     9069   7882   9221  -3590   1017  -2405       N  
ATOM   2832  CA  TYR B 113      19.991 -20.190 122.942  1.00 74.51           C  
ANISOU 2832  CA  TYR B 113     9751   9656   8903  -4716    435  -2365       C  
ATOM   2833  C   TYR B 113      19.995 -21.330 121.890  1.00 82.25           C  
ANISOU 2833  C   TYR B 113    10140  11567   9541  -6045   1494  -3710       C  
ATOM   2834  O   TYR B 113      20.686 -22.346 122.039  1.00 81.86           O  
ANISOU 2834  O   TYR B 113     9779  10717  10606  -6315   3188  -4602       O  
ATOM   2835  CB  TYR B 113      21.337 -19.428 122.900  1.00 71.51           C  
ANISOU 2835  CB  TYR B 113     9821   9200   8147  -4629     30  -1576       C  
ATOM   2836  CG  TYR B 113      21.381 -18.052 123.577  1.00 68.14           C  
ANISOU 2836  CG  TYR B 113     9663   8181   8043  -3800  -1219   -492       C  
ATOM   2837  CD1 TYR B 113      22.598 -17.513 123.997  1.00 64.48           C  
ANISOU 2837  CD1 TYR B 113     9291   7376   7830  -3599   -923    -18       C  
ATOM   2838  CD2 TYR B 113      20.219 -17.283 123.797  1.00 70.50           C  
ANISOU 2838  CD2 TYR B 113     9699   8424   8662  -3285  -2304     -8       C  
ATOM   2839  CE1 TYR B 113      22.664 -16.262 124.609  1.00 62.70           C  
ANISOU 2839  CE1 TYR B 113     9211   6423   8187  -3098  -1519    804       C  
ATOM   2840  CE2 TYR B 113      20.283 -16.030 124.406  1.00 69.87           C  
ANISOU 2840  CE2 TYR B 113     9528   7565   9453  -2661  -3002    607       C  
ATOM   2841  CZ  TYR B 113      21.503 -15.523 124.812  1.00 65.75           C  
ANISOU 2841  CZ  TYR B 113     9309   6399   9273  -2716  -2433    950       C  
ATOM   2842  OH  TYR B 113      21.562 -14.286 125.430  1.00 61.96           O  
ANISOU 2842  OH  TYR B 113     8163   5356  10022  -3138  -2369   1783       O  
ATOM   2843  N   GLU B 114      19.167 -21.150 120.860  1.00 57.27           N  
ANISOU 2843  N   GLU B 114     6338   6771   8649   -950   2316  -1962       N  
ATOM   2844  CA  GLU B 114      19.283 -21.854 119.597  1.00 55.18           C  
ANISOU 2844  CA  GLU B 114     5973   6353   8638  -1023   2065  -1920       C  
ATOM   2845  C   GLU B 114      20.191 -20.959 118.736  1.00 51.51           C  
ANISOU 2845  C   GLU B 114     5627   5885   8058   -687   1698  -1908       C  
ATOM   2846  O   GLU B 114      19.847 -19.814 118.446  1.00 54.00           O  
ANISOU 2846  O   GLU B 114     5981   5983   8553   -626   1508  -1771       O  
ATOM   2847  CB  GLU B 114      17.896 -22.037 118.951  1.00 58.61           C  
ANISOU 2847  CB  GLU B 114     5915   6837   9514  -1052   1940  -2337       C  
ATOM   2848  CG  GLU B 114      16.874 -22.769 119.835  1.00 63.20           C  
ANISOU 2848  CG  GLU B 114     6196   7426  10391  -1307   2400  -2354       C  
ATOM   2849  CD  GLU B 114      15.547 -23.123 119.132  1.00 67.36           C  
ANISOU 2849  CD  GLU B 114     6198   7885  11509  -1299   2241  -2870       C  
ATOM   2850  OE1 GLU B 114      15.155 -22.428 118.166  1.00 66.49           O  
ANISOU 2850  OE1 GLU B 114     5915   8200  11146  -1159   1382  -3477       O  
ATOM   2851  OE2 GLU B 114      14.870 -24.104 119.542  1.00 68.97           O  
ANISOU 2851  OE2 GLU B 114     6191   7803  12212  -1457   2620  -3177       O  
ATOM   2852  N   TYR B 115      21.361 -21.468 118.362  1.00 46.78           N  
ANISOU 2852  N   TYR B 115     5473   5125   7175   -904   1530  -1726       N  
ATOM   2853  CA  TYR B 115      22.332 -20.705 117.568  1.00 43.48           C  
ANISOU 2853  CA  TYR B 115     5309   4791   6420   -642   1226  -1659       C  
ATOM   2854  C   TYR B 115      22.016 -20.854 116.081  1.00 43.87           C  
ANISOU 2854  C   TYR B 115     5284   4859   6523   -503    990  -1581       C  
ATOM   2855  O   TYR B 115      21.895 -21.979 115.590  1.00 44.42           O  
ANISOU 2855  O   TYR B 115     5402   4993   6481   -858    952  -1656       O  
ATOM   2856  CB  TYR B 115      23.750 -21.181 117.879  1.00 40.69           C  
ANISOU 2856  CB  TYR B 115     5227   4382   5851   -801   1421  -1351       C  
ATOM   2857  CG  TYR B 115      24.240 -20.776 119.260  1.00 40.34           C  
ANISOU 2857  CG  TYR B 115     5226   4491   5608   -723   1572  -1189       C  
ATOM   2858  CD1 TYR B 115      25.101 -19.688 119.421  1.00 39.04           C  
ANISOU 2858  CD1 TYR B 115     5156   4323   5353   -590   1406  -1153       C  
ATOM   2859  CD2 TYR B 115      23.820 -21.458 120.413  1.00 42.56           C  
ANISOU 2859  CD2 TYR B 115     5682   4632   5856   -853   1716  -1033       C  
ATOM   2860  CE1 TYR B 115      25.544 -19.299 120.677  1.00 39.99           C  
ANISOU 2860  CE1 TYR B 115     5315   4606   5272   -565   1540  -1232       C  
ATOM   2861  CE2 TYR B 115      24.261 -21.076 121.679  1.00 43.10           C  
ANISOU 2861  CE2 TYR B 115     5907   4872   5597   -705   1972  -1040       C  
ATOM   2862  CZ  TYR B 115      25.128 -19.999 121.805  1.00 42.48           C  
ANISOU 2862  CZ  TYR B 115     5616   5090   5431   -658   1698  -1071       C  
ATOM   2863  OH  TYR B 115      25.568 -19.590 123.051  1.00 45.02           O  
ANISOU 2863  OH  TYR B 115     5786   5922   5395   -280   1252   -782       O  
ATOM   2864  N   ASP B 116      21.894 -19.733 115.364  1.00 43.36           N  
ANISOU 2864  N   ASP B 116     5014   4895   6565   -165    753  -1620       N  
ATOM   2865  CA  ASP B 116      21.398 -19.748 113.962  1.00 46.03           C  
ANISOU 2865  CA  ASP B 116     5443   5307   6737     65    430  -1791       C  
ATOM   2866  C   ASP B 116      22.392 -19.297 112.880  1.00 44.90           C  
ANISOU 2866  C   ASP B 116     5613   5217   6227    287    206  -1570       C  
ATOM   2867  O   ASP B 116      22.015 -19.185 111.716  1.00 47.12           O  
ANISOU 2867  O   ASP B 116     5954   5655   6294    830      4  -1795       O  
ATOM   2868  CB  ASP B 116      20.066 -18.974 113.834  1.00 49.88           C  
ANISOU 2868  CB  ASP B 116     5675   5859   7418    370    191  -1930       C  
ATOM   2869  CG  ASP B 116      20.140 -17.553 114.382  1.00 51.30           C  
ANISOU 2869  CG  ASP B 116     5968   5720   7802    407    135  -1804       C  
ATOM   2870  OD1 ASP B 116      21.078 -17.244 115.154  1.00 51.69           O  
ANISOU 2870  OD1 ASP B 116     6106   5672   7860    124     -5  -1190       O  
ATOM   2871  OD2 ASP B 116      19.244 -16.747 114.049  1.00 54.52           O  
ANISOU 2871  OD2 ASP B 116     5932   6242   8541    614    -74  -2064       O  
ATOM   2872  N   ASN B 117      23.643 -19.034 113.255  1.00 41.93           N  
ANISOU 2872  N   ASN B 117     5565   4635   5729    147    466  -1454       N  
ATOM   2873  CA  ASN B 117      24.714 -18.781 112.287  1.00 41.46           C  
ANISOU 2873  CA  ASN B 117     5702   4536   5514    393    381  -1089       C  
ATOM   2874  C   ASN B 117      25.803 -19.804 112.591  1.00 38.76           C  
ANISOU 2874  C   ASN B 117     5718   4079   4930    124    312   -965       C  
ATOM   2875  O   ASN B 117      26.185 -19.946 113.756  1.00 36.26           O  
ANISOU 2875  O   ASN B 117     6089   3035   4654   -279    479  -1105       O  
ATOM   2876  CB  ASN B 117      25.294 -17.366 112.408  1.00 41.57           C  
ANISOU 2876  CB  ASN B 117     5913   4349   5530    446    525   -662       C  
ATOM   2877  CG  ASN B 117      24.242 -16.278 112.306  1.00 44.80           C  
ANISOU 2877  CG  ASN B 117     6135   4815   6071    733    367   -561       C  
ATOM   2878  OD1 ASN B 117      23.995 -15.744 111.229  1.00 46.95           O  
ANISOU 2878  OD1 ASN B 117     6341   5451   6047   1069    525   -383       O  
ATOM   2879  ND2 ASN B 117      23.631 -15.923 113.443  1.00 45.80           N  
ANISOU 2879  ND2 ASN B 117     6236   4826   6339    546    431   -907       N  
ATOM   2880  N   TRP B 118      26.276 -20.516 111.562  1.00 37.53           N  
ANISOU 2880  N   TRP B 118     5368   4190   4699    218    266   -859       N  
ATOM   2881  CA  TRP B 118      27.219 -21.619 111.742  1.00 35.27           C  
ANISOU 2881  CA  TRP B 118     5192   3854   4352    -30    460   -865       C  
ATOM   2882  C   TRP B 118      28.383 -21.507 110.778  1.00 34.15           C  
ANISOU 2882  C   TRP B 118     5329   3619   4027     62    417   -654       C  
ATOM   2883  O   TRP B 118      28.199 -21.088 109.643  1.00 36.10           O  
ANISOU 2883  O   TRP B 118     5470   4299   3946    279    376   -704       O  
ATOM   2884  CB  TRP B 118      26.509 -22.954 111.533  1.00 36.59           C  
ANISOU 2884  CB  TRP B 118     5043   4137   4720   -131    326  -1093       C  
ATOM   2885  CG  TRP B 118      25.496 -23.202 112.579  1.00 37.49           C  
ANISOU 2885  CG  TRP B 118     5037   4154   5050   -268    479  -1200       C  
ATOM   2886  CD1 TRP B 118      24.214 -22.743 112.600  1.00 39.03           C  
ANISOU 2886  CD1 TRP B 118     5040   4302   5487   -195    377  -1446       C  
ATOM   2887  CD2 TRP B 118      25.680 -23.951 113.779  1.00 36.68           C  
ANISOU 2887  CD2 TRP B 118     4915   3975   5047   -573    648  -1182       C  
ATOM   2888  NE1 TRP B 118      23.583 -23.158 113.743  1.00 39.79           N  
ANISOU 2888  NE1 TRP B 118     4969   4329   5818   -460    562  -1495       N  
ATOM   2889  CE2 TRP B 118      24.458 -23.909 114.485  1.00 38.08           C  
ANISOU 2889  CE2 TRP B 118     4889   4038   5540   -675    769  -1352       C  
ATOM   2890  CE3 TRP B 118      26.755 -24.669 114.324  1.00 34.92           C  
ANISOU 2890  CE3 TRP B 118     4845   3629   4793   -771    784   -987       C  
ATOM   2891  CZ2 TRP B 118      24.282 -24.552 115.716  1.00 37.97           C  
ANISOU 2891  CZ2 TRP B 118     4866   3830   5731   -911   1098  -1299       C  
ATOM   2892  CZ3 TRP B 118      26.580 -25.302 115.549  1.00 34.93           C  
ANISOU 2892  CZ3 TRP B 118     4826   3453   4992  -1008    999   -903       C  
ATOM   2893  CH2 TRP B 118      25.353 -25.232 116.233  1.00 36.64           C  
ANISOU 2893  CH2 TRP B 118     4959   3607   5355   -988   1223  -1072       C  
ATOM   2894  N   GLY B 119      29.575 -21.864 111.248  1.00 31.61           N  
ANISOU 2894  N   GLY B 119     5159   3131   3718   -189    573   -511       N  
ATOM   2895  CA  GLY B 119      30.746 -22.004 110.379  1.00 33.05           C  
ANISOU 2895  CA  GLY B 119     5370   3601   3586    -30    637   -299       C  
ATOM   2896  C   GLY B 119      30.786 -23.400 109.788  1.00 33.46           C  
ANISOU 2896  C   GLY B 119     5448   3800   3464     36    420   -537       C  
ATOM   2897  O   GLY B 119      29.938 -24.220 110.101  1.00 32.64           O  
ANISOU 2897  O   GLY B 119     5173   3685   3543    -20    396  -1226       O  
ATOM   2898  N   GLN B 120      31.767 -23.674 108.937  1.00 35.02           N  
ANISOU 2898  N   GLN B 120     5558   4222   3527    181    468   -447       N  
ATOM   2899  CA  GLN B 120      31.852 -24.982 108.243  1.00 36.68           C  
ANISOU 2899  CA  GLN B 120     5742   4482   3712    255    263   -722       C  
ATOM   2900  C   GLN B 120      32.597 -26.050 109.033  1.00 34.73           C  
ANISOU 2900  C   GLN B 120     5439   4063   3691    -31    330   -820       C  
ATOM   2901  O   GLN B 120      32.481 -27.227 108.720  1.00 36.37           O  
ANISOU 2901  O   GLN B 120     5362   4205   4251    -54    223  -1131       O  
ATOM   2902  CB  GLN B 120      32.472 -24.827 106.856  1.00 40.10           C  
ANISOU 2902  CB  GLN B 120     6297   5232   3707    561    403   -640       C  
ATOM   2903  CG  GLN B 120      31.530 -24.196 105.835  1.00 44.37           C  
ANISOU 2903  CG  GLN B 120     6777   6060   4020    991    164   -573       C  
ATOM   2904  CD  GLN B 120      30.517 -25.191 105.295  1.00 47.96           C  
ANISOU 2904  CD  GLN B 120     6967   6758   4495   1051   -244  -1087       C  
ATOM   2905  OE1 GLN B 120      29.377 -25.241 105.753  1.00 51.35           O  
ANISOU 2905  OE1 GLN B 120     7085   7446   4978    740    -82   -900       O  
ATOM   2906  NE2 GLN B 120      30.936 -26.003 104.326  1.00 50.80           N  
ANISOU 2906  NE2 GLN B 120     7349   7317   4635   1372   -348  -1304       N  
ATOM   2907  N   GLY B 121      33.389 -25.632 110.018  1.00 32.28           N  
ANISOU 2907  N   GLY B 121     5247   3627   3389   -139    549   -608       N  
ATOM   2908  CA  GLY B 121      34.000 -26.524 111.000  1.00 30.58           C  
ANISOU 2908  CA  GLY B 121     5042   3260   3314   -381    629   -642       C  
ATOM   2909  C   GLY B 121      35.509 -26.643 110.831  1.00 29.94           C  
ANISOU 2909  C   GLY B 121     5038   3254   3081   -408    667   -575       C  
ATOM   2910  O   GLY B 121      36.049 -26.320 109.777  1.00 30.20           O  
ANISOU 2910  O   GLY B 121     5122   3425   2925   -340    807   -881       O  
ATOM   2911  N   THR B 122      36.189 -27.090 111.884  1.00 29.12           N  
ANISOU 2911  N   THR B 122     4941   3014   3106   -469    718   -534       N  
ATOM   2912  CA  THR B 122      37.620 -27.414 111.812  1.00 29.56           C  
ANISOU 2912  CA  THR B 122     4961   3097   3171   -394    668   -586       C  
ATOM   2913  C   THR B 122      37.856 -28.782 112.447  1.00 29.05           C  
ANISOU 2913  C   THR B 122     4897   3046   3094   -345    551   -714       C  
ATOM   2914  O   THR B 122      37.341 -29.064 113.523  1.00 28.35           O  
ANISOU 2914  O   THR B 122     4877   2718   3175   -495    552   -718       O  
ATOM   2915  CB  THR B 122      38.503 -26.313 112.445  1.00 30.00           C  
ANISOU 2915  CB  THR B 122     4960   3257   3181   -491    705   -566       C  
ATOM   2916  OG1 THR B 122      39.889 -26.587 112.175  1.00 31.34           O  
ANISOU 2916  OG1 THR B 122     5173   3369   3364    -17    726   -805       O  
ATOM   2917  CG2 THR B 122      38.281 -26.166 113.956  1.00 29.89           C  
ANISOU 2917  CG2 THR B 122     4977   3156   3224   -464    808   -585       C  
ATOM   2918  N   GLN B 123      38.607 -29.635 111.751  1.00 29.61           N  
ANISOU 2918  N   GLN B 123     4943   3074   3232   -280    502   -823       N  
ATOM   2919  CA  GLN B 123      38.817 -31.010 112.181  1.00 30.04           C  
ANISOU 2919  CA  GLN B 123     5065   3012   3337   -237    393   -940       C  
ATOM   2920  C   GLN B 123      39.886 -31.086 113.235  1.00 29.11           C  
ANISOU 2920  C   GLN B 123     5097   2756   3206   -159    422  -1004       C  
ATOM   2921  O   GLN B 123      41.006 -30.638 113.013  1.00 28.21           O  
ANISOU 2921  O   GLN B 123     4996   2656   3065    -80    304  -1230       O  
ATOM   2922  CB  GLN B 123      39.241 -31.894 111.009  1.00 31.59           C  
ANISOU 2922  CB  GLN B 123     5202   3284   3516   -161    333  -1183       C  
ATOM   2923  CG  GLN B 123      38.137 -32.075 109.990  1.00 32.94           C  
ANISOU 2923  CG  GLN B 123     5244   3529   3743    -77    239  -1310       C  
ATOM   2924  CD  GLN B 123      38.636 -32.678 108.697  1.00 34.83           C  
ANISOU 2924  CD  GLN B 123     5475   3964   3793    -19    189  -1518       C  
ATOM   2925  OE1 GLN B 123      39.471 -32.101 108.025  1.00 34.51           O  
ANISOU 2925  OE1 GLN B 123     5343   4439   3328    233    395  -1513       O  
ATOM   2926  NE2 GLN B 123      38.121 -33.841 108.348  1.00 38.36           N  
ANISOU 2926  NE2 GLN B 123     6153   4017   4402     19     31  -1879       N  
ATOM   2927  N   VAL B 124      39.527 -31.683 114.364  1.00 30.07           N  
ANISOU 2927  N   VAL B 124     5288   2731   3403   -118    401   -776       N  
ATOM   2928  CA  VAL B 124      40.446 -31.987 115.447  1.00 31.71           C  
ANISOU 2928  CA  VAL B 124     5517   3039   3492     62    302   -697       C  
ATOM   2929  C   VAL B 124      40.534 -33.504 115.599  1.00 34.05           C  
ANISOU 2929  C   VAL B 124     5918   3064   3954    175    213   -642       C  
ATOM   2930  O   VAL B 124      39.520 -34.181 115.806  1.00 34.31           O  
ANISOU 2930  O   VAL B 124     6166   2673   4194    161    331   -438       O  
ATOM   2931  CB  VAL B 124      39.967 -31.396 116.780  1.00 32.04           C  
ANISOU 2931  CB  VAL B 124     5700   3121   3351    100    350   -535       C  
ATOM   2932  CG1 VAL B 124      40.925 -31.763 117.909  1.00 34.31           C  
ANISOU 2932  CG1 VAL B 124     6067   3540   3429    453    283   -440       C  
ATOM   2933  CG2 VAL B 124      39.843 -29.885 116.670  1.00 30.67           C  
ANISOU 2933  CG2 VAL B 124     5388   3112   3152    -86    467   -530       C  
ATOM   2934  N   THR B 125      41.756 -34.017 115.504  1.00 35.42           N  
ANISOU 2934  N   THR B 125     6081   3295   4082    414    133   -901       N  
ATOM   2935  CA  THR B 125      42.035 -35.421 115.746  1.00 38.15           C  
ANISOU 2935  CA  THR B 125     6565   3404   4524    592     56   -706       C  
ATOM   2936  C   THR B 125      43.079 -35.508 116.841  1.00 39.92           C  
ANISOU 2936  C   THR B 125     6935   3747   4484    972    -63   -706       C  
ATOM   2937  O   THR B 125      44.136 -34.870 116.752  1.00 38.60           O  
ANISOU 2937  O   THR B 125     6779   3768   4119   1073   -205   -879       O  
ATOM   2938  CB  THR B 125      42.531 -36.097 114.458  1.00 38.81           C  
ANISOU 2938  CB  THR B 125     6495   3470   4779    626    -64  -1023       C  
ATOM   2939  OG1 THR B 125      41.585 -35.853 113.412  1.00 38.31           O  
ANISOU 2939  OG1 THR B 125     6288   3601   4666    333    -11  -1148       O  
ATOM   2940  CG2 THR B 125      42.680 -37.600 114.647  1.00 42.32           C  
ANISOU 2940  CG2 THR B 125     7051   3520   5505    744   -138   -915       C  
ATOM   2941  N   VAL B 126      42.763 -36.281 117.882  1.00 43.03           N  
ANISOU 2941  N   VAL B 126     7594   3920   4834   1160     57   -371       N  
ATOM   2942  CA  VAL B 126      43.656 -36.510 119.014  1.00 46.61           C  
ANISOU 2942  CA  VAL B 126     8201   4553   4952   1568   -170   -200       C  
ATOM   2943  C   VAL B 126      44.035 -37.980 118.972  1.00 49.72           C  
ANISOU 2943  C   VAL B 126     8915   4627   5348   1794   -209    -60       C  
ATOM   2944  O   VAL B 126      43.159 -38.831 118.997  1.00 50.84           O  
ANISOU 2944  O   VAL B 126     9359   4275   5679   1746      1    236       O  
ATOM   2945  CB  VAL B 126      42.973 -36.202 120.368  1.00 48.33           C  
ANISOU 2945  CB  VAL B 126     8694   4813   4854   1693    -37    141       C  
ATOM   2946  CG1 VAL B 126      43.948 -36.434 121.516  1.00 52.49           C  
ANISOU 2946  CG1 VAL B 126     9363   5611   4968   2220   -288    153       C  
ATOM   2947  CG2 VAL B 126      42.429 -34.778 120.400  1.00 45.18           C  
ANISOU 2947  CG2 VAL B 126     8068   4725   4371   1443     16    -77       C  
ATOM   2948  N   SER B 127      45.333 -38.262 118.902  1.00 52.52           N  
ANISOU 2948  N   SER B 127     9003   5246   5706   2113   -555   -273       N  
ATOM   2949  CA  SER B 127      45.848 -39.629 118.797  1.00 58.32           C  
ANISOU 2949  CA  SER B 127     9845   5452   6860   2437   -588   -324       C  
ATOM   2950  C   SER B 127      46.498 -40.077 120.103  1.00 64.17           C  
ANISOU 2950  C   SER B 127    10790   6403   7188   3071   -816     -3       C  
ATOM   2951  O   SER B 127      46.666 -39.279 121.024  1.00 66.31           O  
ANISOU 2951  O   SER B 127    10990   7161   7043   3047   -932   -175       O  
ATOM   2952  CB  SER B 127      46.891 -39.693 117.688  1.00 58.13           C  
ANISOU 2952  CB  SER B 127     9450   5691   6944   2360   -764   -835       C  
ATOM   2953  OG  SER B 127      48.045 -38.950 118.058  1.00 59.90           O  
ANISOU 2953  OG  SER B 127     9181   6525   7054   2554  -1029  -1205       O  
ATOM   2954  N   SER B 128      46.875 -41.351 120.168  1.00 69.21           N  
ANISOU 2954  N   SER B 128    11724   6487   8085   3313   -870     96       N  
ATOM   2955  CA  SER B 128      47.624 -41.884 121.311  1.00 75.02           C  
ANISOU 2955  CA  SER B 128    12716   7371   8415   4016  -1043    373       C  
ATOM   2956  C   SER B 128      48.378 -43.163 120.947  1.00 79.12           C  
ANISOU 2956  C   SER B 128    13279   7389   9391   4271  -1178    243       C  
ATOM   2957  O   SER B 128      49.316 -43.136 120.148  1.00 76.54           O  
ANISOU 2957  O   SER B 128    12732   6789   9558   4014  -1429   -305       O  
ATOM   2958  CB  SER B 128      46.681 -42.149 122.485  1.00 79.24           C  
ANISOU 2958  CB  SER B 128    13652   7732   8723   4181   -618   1024       C  
ATOM   2959  OG  SER B 128      45.664 -43.063 122.113  1.00 81.82           O  
ANISOU 2959  OG  SER B 128    14043   7385   9658   3770   -111   1255       O  
TER    2960      SER B 128                                                      
HETATM 2961  O   HOH A 401      11.425  -4.688 140.426  1.00 42.88           O  
ANISOU 2961  O   HOH A 401     6532   5563   4195  -1437     54   -315       O  
HETATM 2962  O   HOH A 402      20.094  20.762 123.087  1.00 37.73           O  
ANISOU 2962  O   HOH A 402     5752   3355   5226    369    876    350       O  
HETATM 2963  O   HOH A 403      22.613  17.887 151.757  1.00 32.98           O  
ANISOU 2963  O   HOH A 403     5427   3576   3527   1289   -557   -413       O  
HETATM 2964  O   HOH A 404      18.267  -2.845 130.258  1.00 27.93           O  
ANISOU 2964  O   HOH A 404     4488   1531   4590   -876    512   -923       O  
HETATM 2965  O   HOH A 405       8.869  13.390 140.794  1.00 34.49           O  
ANISOU 2965  O   HOH A 405     3214   5531   4357    875    407   -394       O  
HETATM 2966  O   HOH A 406       8.955   6.358 137.977  1.00 42.27           O  
ANISOU 2966  O   HOH A 406     5055   5371   5632  -1885  -1575   -679       O  
HETATM 2967  O   HOH A 407      17.619  -3.889 133.719  1.00 43.49           O  
ANISOU 2967  O   HOH A 407     6113   4956   5453  -1642    -35   -786       O  
HETATM 2968  O   HOH A 408      12.023  14.824 141.590  1.00 29.08           O  
ANISOU 2968  O   HOH A 408     2512   3228   5308   2186   -449    283       O  
HETATM 2969  O   HOH A 409      33.079   0.700 140.615  1.00 32.55           O  
ANISOU 2969  O   HOH A 409     4152   2777   5438    514   1200  -1481       O  
HETATM 2970  O   HOH A 410      25.563  10.452 127.086  1.00 15.36           O  
ANISOU 2970  O   HOH A 410     1990   1562   2282   -192    264   -141       O  
HETATM 2971  O   HOH A 411       5.013   5.866 143.906  1.00 38.61           O  
ANISOU 2971  O   HOH A 411     3339   4834   6496  -1241    397     58       O  
HETATM 2972  O   HOH A 412      27.081  23.349 106.527  1.00 38.43           O  
ANISOU 2972  O   HOH A 412     5705   5846   3048  -3102   -239    677       O  
HETATM 2973  O   HOH A 413      15.146  14.154 114.094  1.00 42.83           O  
ANISOU 2973  O   HOH A 413     3383   7591   5296   2132   -916    558       O  
HETATM 2974  O   HOH A 414      16.010   9.471 136.577  1.00 23.42           O  
ANISOU 2974  O   HOH A 414     1787   3125   3987  -1030    364   -506       O  
HETATM 2975  O   HOH A 415      19.026  -8.599 138.227  1.00 31.68           O  
ANISOU 2975  O   HOH A 415     5318   1266   5453    748    837  -1062       O  
HETATM 2976  O   HOH A 416      29.578  31.719 122.813  1.00 44.19           O  
ANISOU 2976  O   HOH A 416     7031   5950   3807  -2017   -238   -206       O  
HETATM 2977  O   HOH A 417      15.527   4.461 128.937  1.00 34.02           O  
ANISOU 2977  O   HOH A 417     3894   4887   4144   -352     12   -617       O  
HETATM 2978  O   HOH A 418      25.857  26.435 133.248  1.00 42.12           O  
ANISOU 2978  O   HOH A 418     3796   3675   8534  -2186    535  -1071       O  
HETATM 2979  O   HOH A 419      36.133  14.395 137.735  1.00 53.48           O  
ANISOU 2979  O   HOH A 419     6684   6334   7299   -289    807   -751       O  
HETATM 2980  O   HOH A 420      41.015  21.238 122.899  1.00 30.44           O  
ANISOU 2980  O   HOH A 420     3005   4632   3928   -247   -695    241       O  
HETATM 2981  O   HOH A 421      43.156  14.925 123.182  1.00 33.40           O  
ANISOU 2981  O   HOH A 421     2442   6109   4139    394   1613     31       O  
HETATM 2982  O   HOH A 422      33.833  25.492 132.322  1.00 26.89           O  
ANISOU 2982  O   HOH A 422     2887   4066   3262   -584    690   -817       O  
HETATM 2983  O   HOH A 423      35.064   0.890 124.418  1.00 32.85           O  
ANISOU 2983  O   HOH A 423     3696   4374   4412    741    268    -53       O  
HETATM 2984  O   HOH A 424      12.425   7.013 160.611  1.00 50.74           O  
ANISOU 2984  O   HOH A 424     9830   4349   5099    705   2248   1051       O  
HETATM 2985  O   HOH A 425      22.554   1.080 124.666  1.00 27.25           O  
ANISOU 2985  O   HOH A 425     4022   2766   3565   -892    796  -1096       O  
HETATM 2986  O   HOH A 426      10.961   1.460 150.528  1.00 40.25           O  
ANISOU 2986  O   HOH A 426     4036   4471   6787   -113    620    622       O  
HETATM 2987  O   HOH A 427      12.276  11.742 137.472  1.00 53.09           O  
ANISOU 2987  O   HOH A 427     6388   6167   7614  -1317  -2333   1625       O  
HETATM 2988  O   HOH A 428      22.063  24.707 107.741  1.00 33.04           O  
ANISOU 2988  O   HOH A 428     5229   4738   2586    419   -831    917       O  
HETATM 2989  O   HOH A 429      39.473  10.198 131.369  1.00 39.13           O  
ANISOU 2989  O   HOH A 429     4618   4618   5630   1876   1007     42       O  
HETATM 2990  O   HOH A 430      19.761  -4.291 125.604  1.00 30.07           O  
ANISOU 2990  O   HOH A 430     4642   2771   4010   -895    422   -962       O  
HETATM 2991  O   HOH A 431      13.532   9.767 154.308  1.00 24.64           O  
ANISOU 2991  O   HOH A 431     2655   3007   3699    905   -239    232       O  
HETATM 2992  O   HOH A 432       9.484  14.350 150.962  1.00 29.92           O  
ANISOU 2992  O   HOH A 432     3241   3370   4755     59    439    163       O  
HETATM 2993  O   HOH A 433       7.109  23.746 146.357  1.00 41.66           O  
ANISOU 2993  O   HOH A 433     3613   6398   5818    706    288   -148       O  
HETATM 2994  O   HOH A 434      38.872   1.965 118.741  1.00 48.91           O  
ANISOU 2994  O   HOH A 434     5637   4965   7979   -427   2221    679       O  
HETATM 2995  O   HOH A 435      15.194  10.024 160.136  1.00 39.37           O  
ANISOU 2995  O   HOH A 435     4277   4704   5974  -1220    452    -88       O  
HETATM 2996  O   HOH A 436      21.009   9.791 154.579  1.00 28.33           O  
ANISOU 2996  O   HOH A 436     4349   2787   3626   -282    638   -492       O  
HETATM 2997  O   HOH A 437      29.390   4.277 136.542  1.00 20.28           O  
ANISOU 2997  O   HOH A 437     2360   2277   3066    336    -76   -452       O  
HETATM 2998  O   HOH A 438      23.604  11.443 106.099  1.00 38.83           O  
ANISOU 2998  O   HOH A 438     4689   4648   5415    535     80   1011       O  
HETATM 2999  O   HOH A 439      31.066  14.527 141.995  1.00 46.74           O  
ANISOU 2999  O   HOH A 439     4966   5805   6985  -2104    377    196       O  
HETATM 3000  O   HOH A 440      18.243  18.206 119.965  1.00 26.61           O  
ANISOU 3000  O   HOH A 440     3125   4033   2951   1291   1153   -500       O  
HETATM 3001  O   HOH A 441      10.154  20.244 121.258  1.00 52.97           O  
ANISOU 3001  O   HOH A 441     6670   6371   7083   -137   -585    840       O  
HETATM 3002  O   HOH A 442      29.911  29.971 115.291  1.00 39.34           O  
ANISOU 3002  O   HOH A 442     5185   4884   4879   -460    633    302       O  
HETATM 3003  O   HOH A 443      28.124  -7.655 141.314  1.00 39.26           O  
ANISOU 3003  O   HOH A 443     6811   3956   4147    707   -169   -103       O  
HETATM 3004  O   HOH A 444      15.079  13.342 150.358  1.00 16.22           O  
ANISOU 3004  O   HOH A 444     2084   1357   2721   -548    313     90       O  
HETATM 3005  O   HOH A 445      17.159  24.964 115.390  1.00 34.25           O  
ANISOU 3005  O   HOH A 445     4462   3312   5240    641    420     91       O  
HETATM 3006  O   HOH A 446      25.780  10.579 151.563  1.00 31.80           O  
ANISOU 3006  O   HOH A 446     4581   4358   3144    685    -49   -502       O  
HETATM 3007  O   HOH A 447      15.181  12.379 124.176  1.00 43.07           O  
ANISOU 3007  O   HOH A 447     3574   6404   6385    216   1232   -755       O  
HETATM 3008  O   HOH A 448      25.951  -9.845 139.162  1.00 39.28           O  
ANISOU 3008  O   HOH A 448     6737   4215   3973   -472    151    697       O  
HETATM 3009  O   HOH A 449      31.941  -2.536 125.411  1.00 39.41           O  
ANISOU 3009  O   HOH A 449     3443   4783   6745    673    864   -224       O  
HETATM 3010  O   HOH A 450      25.656  -7.657 147.000  1.00 46.86           O  
ANISOU 3010  O   HOH A 450     6708   3231   7864     71    942   -730       O  
HETATM 3011  O   HOH A 451      36.565  24.026 115.060  1.00 52.53           O  
ANISOU 3011  O   HOH A 451     7081   7494   5384  -2500    580   -250       O  
HETATM 3012  O   HOH A 452      16.229   6.667 107.665  1.00 39.86           O  
ANISOU 3012  O   HOH A 452     3392   6041   5712   -399   -807    196       O  
HETATM 3013  O   HOH A 453      30.671 -10.183 135.042  1.00 34.96           O  
ANISOU 3013  O   HOH A 453     3821   4966   4493    981    270  -1140       O  
HETATM 3014  O   HOH A 454      36.722  16.054 129.190  1.00 22.80           O  
ANISOU 3014  O   HOH A 454     1888   3305   3469    346    731    234       O  
HETATM 3015  O   HOH A 455      16.841  -0.621 152.081  1.00 45.56           O  
ANISOU 3015  O   HOH A 455     6377   6017   4918    736   2412  -1099       O  
HETATM 3016  O   HOH A 456      25.969   8.732 148.003  1.00 20.14           O  
ANISOU 3016  O   HOH A 456     2673   1941   3036    479    -93   -500       O  
HETATM 3017  O   HOH A 457      18.415   1.286 132.753  1.00 26.23           O  
ANISOU 3017  O   HOH A 457     3909   2593   3463   -403     12  -1055       O  
HETATM 3018  O   HOH A 458      17.686  25.652 110.067  1.00 47.02           O  
ANISOU 3018  O   HOH A 458     5653   5667   6545   -139   -558     39       O  
HETATM 3019  O   HOH A 459      10.978   3.352 152.768  1.00 35.64           O  
ANISOU 3019  O   HOH A 459     5563   3009   4966  -1368    838   -429       O  
HETATM 3020  O   HOH A 460      34.811  10.355 123.342  1.00 22.70           O  
ANISOU 3020  O   HOH A 460     3359   2499   2764    235     22    235       O  
HETATM 3021  O   HOH A 461       8.212   4.345 152.660  1.00 42.44           O  
ANISOU 3021  O   HOH A 461     5794   5431   4898  -1693   1041   -301       O  
HETATM 3022  O   HOH A 462      33.915  -0.394 116.869  1.00 49.17           O  
ANISOU 3022  O   HOH A 462     5538   4990   8152  -1881    698   -770       O  
HETATM 3023  O   HOH A 463      27.828   1.566 151.026  1.00 28.69           O  
ANISOU 3023  O   HOH A 463     3868   2850   4181    841    313   -625       O  
HETATM 3024  O   HOH A 464      22.125   9.040 106.712  1.00 36.78           O  
ANISOU 3024  O   HOH A 464     5923   3651   4398   -733   -366   -959       O  
HETATM 3025  O   HOH A 465      16.074  -6.797 143.377  1.00 32.29           O  
ANISOU 3025  O   HOH A 465     5798   1506   4963   -267   -216   1158       O  
HETATM 3026  O   HOH A 466      39.297   3.100 123.260  1.00 47.09           O  
ANISOU 3026  O   HOH A 466     4157   5765   7970    731    527   -808       O  
HETATM 3027  O   HOH A 467      29.508  -9.726 140.619  1.00 45.79           O  
ANISOU 3027  O   HOH A 467     5519   4405   7473   1877    693    643       O  
HETATM 3028  O   HOH A 468      33.752  13.871 148.600  1.00 59.10           O  
ANISOU 3028  O   HOH A 468     7929   7139   7386  -1554   -729    -97       O  
HETATM 3029  O   HOH A 469       5.517   6.984 150.870  1.00 31.21           O  
ANISOU 3029  O   HOH A 469     2148   4526   5182   -374    528   -970       O  
HETATM 3030  O   HOH A 470      20.921  24.784 142.067  1.00 43.27           O  
ANISOU 3030  O   HOH A 470     5053   5537   5850   -652   1597   3049       O  
HETATM 3031  O   HOH A 471      32.093   7.897 139.778  1.00 42.69           O  
ANISOU 3031  O   HOH A 471     6071   6106   4043   -662   -268    812       O  
HETATM 3032  O   HOH A 472      19.303  -0.560 118.201  1.00 40.52           O  
ANISOU 3032  O   HOH A 472     5358   4981   5056   -628  -1736   -251       O  
HETATM 3033  O   HOH A 473      13.855  13.984 143.515  1.00 18.25           O  
ANISOU 3033  O   HOH A 473     2006   2168   2759   -814    363    235       O  
HETATM 3034  O   HOH A 474      31.420  -2.278 145.690  1.00 35.95           O  
ANISOU 3034  O   HOH A 474     3855   3289   6514    -68   -907   -497       O  
HETATM 3035  O   HOH A 475      33.100  27.526 130.465  1.00 32.48           O  
ANISOU 3035  O   HOH A 475     3105   5362   3874  -1059    277  -1314       O  
HETATM 3036  O   HOH A 476      18.553   9.529 131.282  1.00 38.44           O  
ANISOU 3036  O   HOH A 476     5993   3793   4819   1744     58    850       O  
HETATM 3037  O   HOH A 477       5.472  10.589 153.462  1.00 53.46           O  
ANISOU 3037  O   HOH A 477     8129   6202   5978   -930   1292   1250       O  
HETATM 3038  O   HOH A 478      28.441   7.225 135.556  1.00 28.91           O  
ANISOU 3038  O   HOH A 478     3892   3195   3895    343   -953  -1051       O  
HETATM 3039  O   HOH A 479      20.097  13.199 157.490  1.00 48.63           O  
ANISOU 3039  O   HOH A 479     8122   4142   6210  -1377  -1364   -146       O  
HETATM 3040  O   HOH A 480      18.212   7.329 158.131  1.00 60.43           O  
ANISOU 3040  O   HOH A 480     9369   6280   7309   3034   -219  -2990       O  
HETATM 3041  O   HOH A 481      16.154   4.532 125.833  1.00 33.92           O  
ANISOU 3041  O   HOH A 481     2617   4160   6111   -296    -49  -1721       O  
HETATM 3042  O   HOH A 482      14.973  24.140 113.588  1.00 49.73           O  
ANISOU 3042  O   HOH A 482     4765   4764   9364   -773   -228    200       O  
HETATM 3043  O   HOH A 483       0.760   9.682 144.879  1.00 36.88           O  
ANISOU 3043  O   HOH A 483     2539   4803   6670  -2168  -1489    -55       O  
HETATM 3044  O   HOH A 484       6.123   7.643 140.198  1.00 36.35           O  
ANISOU 3044  O   HOH A 484     3504   4232   6073     -7  -1171   -698       O  
HETATM 3045  O   HOH A 485      27.053  19.139 106.037  1.00 29.06           O  
ANISOU 3045  O   HOH A 485     3440   4228   3370    587   1085    816       O  
HETATM 3046  O   HOH A 486      33.481  -1.493 129.376  1.00 44.83           O  
ANISOU 3046  O   HOH A 486     5094   5863   6073   1383    341  -2038       O  
HETATM 3047  O   HOH A 487      19.998  27.374 122.017  1.00 49.51           O  
ANISOU 3047  O   HOH A 487     6629   4488   7696   1231   1731  -2906       O  
HETATM 3048  O   HOH A 488      35.433  12.271 136.075  1.00 37.14           O  
ANISOU 3048  O   HOH A 488     4293   4459   5359    477   -387    657       O  
HETATM 3049  O   HOH A 489      40.021  15.519 116.534  1.00 38.85           O  
ANISOU 3049  O   HOH A 489     3411   4931   6416   -614   1511    434       O  
HETATM 3050  O   HOH A 490      32.936  -0.515 144.104  1.00 36.39           O  
ANISOU 3050  O   HOH A 490     6319   3240   4265   2065    278   1097       O  
HETATM 3051  O   HOH A 491      22.311   3.998 153.827  1.00 35.30           O  
ANISOU 3051  O   HOH A 491     5512   2837   5061     82    715     92       O  
HETATM 3052  O   HOH A 492      20.077  17.818 136.447  1.00 36.19           O  
ANISOU 3052  O   HOH A 492     4485   4461   4801   -682   -279     46       O  
HETATM 3053  O   HOH A 493      15.683  21.419 122.000  1.00 51.89           O  
ANISOU 3053  O   HOH A 493     7814   5900   6002  -4322  -2133   1784       O  
HETATM 3054  O   HOH A 494      28.760  24.429 112.252  1.00 48.33           O  
ANISOU 3054  O   HOH A 494     5951   8225   4185     -7   1514     58       O  
HETATM 3055  O   HOH A 495      42.427  18.988 113.799  1.00 42.23           O  
ANISOU 3055  O   HOH A 495     5264   4661   6117    521   -492  -1009       O  
HETATM 3056  O   HOH A 496      22.400  12.053 129.238  1.00 28.19           O  
ANISOU 3056  O   HOH A 496     2847   2776   5086      7   -551   -865       O  
HETATM 3057  O   HOH A 497      17.814  15.986 126.769  1.00 30.34           O  
ANISOU 3057  O   HOH A 497     2723   5521   3282  -1065     84    470       O  
HETATM 3058  O   HOH A 498      31.937  20.689 110.488  1.00 34.56           O  
ANISOU 3058  O   HOH A 498     4836   5187   3106  -1816   -170   1703       O  
HETATM 3059  O   HOH A 499      31.115   4.694 149.473  1.00 34.96           O  
ANISOU 3059  O   HOH A 499     3700   3967   5615   1450   -638   -779       O  
HETATM 3060  O   HOH A 500      42.629  13.482 119.569  1.00 44.52           O  
ANISOU 3060  O   HOH A 500     7326   4914   4673    444    -90    325       O  
HETATM 3061  O   HOH A 501      17.763  18.082 155.249  1.00 23.50           O  
ANISOU 3061  O   HOH A 501     3400   2500   3028    279   -256    233       O  
HETATM 3062  O   HOH A 502      21.964  23.925 103.869  1.00 34.90           O  
ANISOU 3062  O   HOH A 502     5442   4448   3371     74   1071    371       O  
HETATM 3063  O   HOH A 503      36.365  20.041 133.085  1.00 37.71           O  
ANISOU 3063  O   HOH A 503     4847   5240   4239   -890  -1365   -626       O  
HETATM 3064  O   HOH A 504      25.467   7.805 151.246  1.00 25.48           O  
ANISOU 3064  O   HOH A 504     3044   3440   3197    -74   -587    480       O  
HETATM 3065  O   HOH A 505      19.771   0.025 124.402  1.00 40.43           O  
ANISOU 3065  O   HOH A 505     4968   4141   6249   -766    738   1727       O  
HETATM 3066  O   HOH A 506      15.971   9.500 133.918  1.00 29.00           O  
ANISOU 3066  O   HOH A 506     3701   3325   3990   1104   -645   -257       O  
HETATM 3067  O   HOH A 507       9.014  27.444 141.585  1.00 20.30           O  
ANISOU 3067  O   HOH A 507     2259   1664   3787    402   -203    578       O  
HETATM 3068  O   HOH A 508      29.730   9.495 135.700  1.00 34.02           O  
ANISOU 3068  O   HOH A 508     4168   4109   4649   -267    376   -121       O  
HETATM 3069  O   HOH A 509      14.650  -2.230 135.616  1.00 33.40           O  
ANISOU 3069  O   HOH A 509     5033   3093   4562  -1618    339   -266       O  
HETATM 3070  O   HOH A 510      38.617  31.999 124.120  1.00 49.25           O  
ANISOU 3070  O   HOH A 510     5846   4634   8233   -681     -2    454       O  
HETATM 3071  O   HOH A 511      24.467  13.313 127.295  1.00 27.58           O  
ANISOU 3071  O   HOH A 511     2845   4483   3149    216   -175   -999       O  
HETATM 3072  O   HOH A 512      24.858 -12.364 138.245  1.00 37.12           O  
ANISOU 3072  O   HOH A 512     5334   3419   5350    449   -320  -1000       O  
HETATM 3073  O   HOH A 513      19.565  20.999 156.462  1.00 48.11           O  
ANISOU 3073  O   HOH A 513     7127   6094   5055   1806    130   -197       O  
HETATM 3074  O   HOH A 514      13.069  22.768 120.474  1.00 42.57           O  
ANISOU 3074  O   HOH A 514     4906   6348   4920    208    417   -345       O  
HETATM 3075  O   HOH A 515      10.926  16.806 154.113  1.00 25.54           O  
ANISOU 3075  O   HOH A 515     3472   2467   3762    434   1291   1017       O  
HETATM 3076  O   HOH A 516      22.508   9.914 103.849  1.00 51.08           O  
ANISOU 3076  O   HOH A 516     6603   5942   6860   2049   -591   -255       O  
HETATM 3077  O   HOH A 517       2.811   9.607 142.654  1.00 49.63           O  
ANISOU 3077  O   HOH A 517     5394   5372   8089    110  -2266  -1765       O  
HETATM 3078  O   HOH A 518      13.825  15.789 139.284  1.00 34.93           O  
ANISOU 3078  O   HOH A 518     4569   4017   4682    965  -1232     87       O  
HETATM 3079  O   HOH A 519      19.785   2.678 130.438  1.00 26.25           O  
ANISOU 3079  O   HOH A 519     3359   1668   4945   -107    535   -578       O  
HETATM 3080  O   HOH A 520      17.988  -4.562 123.775  1.00 47.93           O  
ANISOU 3080  O   HOH A 520     8530   4669   5013    336    313  -1163       O  
HETATM 3081  O   HOH A 521      17.432  -1.049 132.025  1.00 34.65           O  
ANISOU 3081  O   HOH A 521     5269   3324   4571  -1670     31  -1411       O  
HETATM 3082  O   HOH A 522      38.143  12.324 134.747  1.00 44.46           O  
ANISOU 3082  O   HOH A 522     3911   6930   6050   1075   -855    730       O  
HETATM 3083  O   HOH A 523      16.374  21.784 131.992  1.00 58.50           O  
ANISOU 3083  O   HOH A 523     7663   7469   7094   -322    334     49       O  
HETATM 3084  O   HOH A 524      17.690  18.572 129.052  1.00 50.17           O  
ANISOU 3084  O   HOH A 524     3289   8318   7456  -1151   2241   1751       O  
HETATM 3085  O   HOH A 525      17.386  -5.299 135.995  1.00 41.48           O  
ANISOU 3085  O   HOH A 525     6629   4535   4593   -470    225  -1187       O  
HETATM 3086  O   HOH A 526      15.748   2.370 131.883  1.00 46.92           O  
ANISOU 3086  O   HOH A 526     7374   6379   4072  -1948   2500  -1913       O  
HETATM 3087  O   HOH A 527      22.130  22.098 155.485  1.00 48.63           O  
ANISOU 3087  O   HOH A 527     7932   6383   4159   1778    578    709       O  
HETATM 3088  O   HOH A 528      18.856   1.981 127.714  1.00 38.37           O  
ANISOU 3088  O   HOH A 528     5251   4846   4481   -956    200  -1272       O  
HETATM 3089  O   HOH A 529      18.409  -8.029 142.923  1.00 43.10           O  
ANISOU 3089  O   HOH A 529     5283   3554   7539  -1235    957    312       O  
HETATM 3090  O   HOH A 530      35.429  14.196 140.499  1.00 52.73           O  
ANISOU 3090  O   HOH A 530     5061   9202   5772    615   1083  -1595       O  
HETATM 3091  O   HOH A 531      31.201  16.242 106.372  1.00 52.51           O  
ANISOU 3091  O   HOH A 531     6058   6569   7325   2135    892   -810       O  
HETATM 3092  O   HOH A 532      28.128  11.829 152.282  1.00 43.95           O  
ANISOU 3092  O   HOH A 532     4580   5310   6808    780   1248  -1979       O  
HETATM 3093  O   HOH A 533      31.937   8.788 134.192  1.00 43.61           O  
ANISOU 3093  O   HOH A 533     4953   4373   7240   1363   -390    648       O  
HETATM 3094  O   HOH A 534      19.721  26.134 108.516  1.00 45.63           O  
ANISOU 3094  O   HOH A 534     5693   7108   4535    436  -1257    -68       O  
HETATM 3095  O   HOH A 535      30.942  23.555 111.191  1.00 54.15           O  
ANISOU 3095  O   HOH A 535     4537   7938   8099    895    588    299       O  
HETATM 3096  O   HOH A 536      30.845  34.146 123.800  1.00 41.87           O  
ANISOU 3096  O   HOH A 536     3928   4964   7013     13   -111    110       O  
HETATM 3097  O   HOH A 537      20.236   7.860 156.233  1.00 45.31           O  
ANISOU 3097  O   HOH A 537     7289   3069   6858   -558    460  -2598       O  
HETATM 3098  O   HOH A 538      20.082  23.827 138.873  1.00 50.07           O  
ANISOU 3098  O   HOH A 538     5792   6427   6803  -1477   1272    444       O  
HETATM 3099  O   HOH A 539      17.036  -8.049 136.309  1.00 44.83           O  
ANISOU 3099  O   HOH A 539     7036   4426   5570  -1254   1130  -1806       O  
HETATM 3100  O   HOH A 540      27.492  14.492 153.074  1.00 61.24           O  
ANISOU 3100  O   HOH A 540     8162   6924   8181    227   1782  -2706       O  
HETATM 3101  O   HOH A 541      32.542  30.516 116.403  1.00 58.72           O  
ANISOU 3101  O   HOH A 541     7329  10120   4862  -2395   -252    956       O  
HETATM 3102  O   HOH A 542      32.167  -2.193 148.283  1.00 51.50           O  
ANISOU 3102  O   HOH A 542     7182   5133   7253   1534   1575  -1474       O  
HETATM 3103  O   HOH A 543      31.164   6.778 135.996  1.00 47.44           O  
ANISOU 3103  O   HOH A 543     6966   4577   6481   -954   1205  -2696       O  
HETATM 3104  O   HOH A 544      21.333  19.675 134.710  1.00 50.67           O  
ANISOU 3104  O   HOH A 544     5141   8188   5921  -1966   -587   -705       O  
HETATM 3105  O   HOH A 545       3.344   7.112 141.975  1.00 51.71           O  
ANISOU 3105  O   HOH A 545     5115   9018   5515   -284   -623  -1338       O  
HETATM 3106  O   HOH A 546      34.807   3.606 152.572  1.00 49.48           O  
ANISOU 3106  O   HOH A 546     6039   5445   7313   -511   2224     25       O  
HETATM 3107  O   HOH A 547      33.086   2.818 150.260  1.00 55.83           O  
ANISOU 3107  O   HOH A 547     6666   6834   7711   1544    418   -690       O  
HETATM 3108  O   HOH A 548      17.721  16.441 135.432  1.00 46.09           O  
ANISOU 3108  O   HOH A 548     4882   6864   5766   -498    -56   1608       O  
HETATM 3109  O   HOH A 549       9.662  18.346 155.996  1.00 47.30           O  
ANISOU 3109  O   HOH A 549     5195   5868   6905  -1224   2024  -3117       O  
HETATM 3110  O   HOH A 550      34.304  -1.189 125.990  1.00 44.78           O  
ANISOU 3110  O   HOH A 550     5581   4539   6892    436    792    952       O  
HETATM 3111  O   HOH A 551      25.438 -16.694 137.564  1.00 61.06           O  
ANISOU 3111  O   HOH A 551     6911   5907  10380  -1742  -2140   -995       O  
HETATM 3112  O   HOH A 552      15.988  16.583 130.548  1.00 55.22           O  
ANISOU 3112  O   HOH A 552     6306   8938   5735    -39  -1513   -655       O  
HETATM 3113  O   HOH A 553      37.569   0.777 123.165  1.00 42.55           O  
ANISOU 3113  O   HOH A 553     5468   5070   5627    870    999   -476       O  
HETATM 3114  O   HOH A 554      17.908  -9.558 140.546  1.00 38.16           O  
ANISOU 3114  O   HOH A 554     6998   2241   5259     10    -77    718       O  
HETATM 3115  O   HOH A 555      15.471  -7.032 146.112  1.00 37.08           O  
ANISOU 3115  O   HOH A 555     5146   3572   5368   -173   -205  -1044       O  
HETATM 3116  O   HOH A 556      17.427  -0.863 120.477  1.00 48.40           O  
ANISOU 3116  O   HOH A 556     7527   5554   5306   -547   -898    834       O  
HETATM 3117  O   HOH A 557      29.379   3.932 151.374  1.00 45.06           O  
ANISOU 3117  O   HOH A 557     6147   4718   6256   1067  -1013  -1772       O  
HETATM 3118  O   HOH A 558      25.199 -10.558 141.951  1.00 52.76           O  
ANISOU 3118  O   HOH A 558     6706   7946   5393   2164    700  -3034       O  
HETATM 3119  O   HOH A 559      19.979  -9.206 144.897  1.00 44.35           O  
ANISOU 3119  O   HOH A 559     6536   5388   4926   -239   1763   -464       O  
HETATM 3120  O   HOH A 560      34.581  -0.673 148.224  1.00 57.68           O  
ANISOU 3120  O   HOH A 560     7657   8723   5536    697    233   1754       O  
HETATM 3121  O   HOH B 201      43.382 -13.978 116.230  1.00 37.96           O  
ANISOU 3121  O   HOH B 201     5889   4141   4390  -1981   1114    504       O  
HETATM 3122  O   HOH B 202      41.998 -23.959 128.546  1.00 33.44           O  
ANISOU 3122  O   HOH B 202     5587   2773   4342    678     11   -720       O  
HETATM 3123  O   HOH B 203      37.560 -16.664 129.274  1.00 41.25           O  
ANISOU 3123  O   HOH B 203     6447   4300   4923    650    900  -3203       O  
HETATM 3124  O   HOH B 204      35.914 -18.842 130.943  1.00 33.69           O  
ANISOU 3124  O   HOH B 204     5678   3434   3688   1348   -214    131       O  
HETATM 3125  O   HOH B 205      35.642 -23.813 108.320  1.00 45.38           O  
ANISOU 3125  O   HOH B 205     7189   5802   4249   -290   -408    980       O  
HETATM 3126  O   HOH B 206      40.529 -18.875 125.013  1.00 30.25           O  
ANISOU 3126  O   HOH B 206     4561   3152   3779   -175   -728   -560       O  
HETATM 3127  O   HOH B 207      37.198  -6.978 113.157  1.00 34.69           O  
ANISOU 3127  O   HOH B 207     4916   3865   4396   -845    415   -625       O  
HETATM 3128  O   HOH B 208      33.980  -9.359 124.931  1.00 24.14           O  
ANISOU 3128  O   HOH B 208     3328   2388   3456   -527    897  -1362       O  
HETATM 3129  O   HOH B 209      43.638 -20.750 116.216  1.00 34.53           O  
ANISOU 3129  O   HOH B 209     4048   4152   4917    195   1267   -271       O  
HETATM 3130  O   HOH B 210      32.850  -3.987 121.170  1.00 29.73           O  
ANISOU 3130  O   HOH B 210     3838   2643   4814   -585     25  -1304       O  
HETATM 3131  O   HOH B 211      20.782 -14.663 115.818  1.00 37.61           O  
ANISOU 3131  O   HOH B 211     4896   3507   5884    286  -2050  -1322       O  
HETATM 3132  O   HOH B 212      28.773 -18.743 108.476  1.00 35.14           O  
ANISOU 3132  O   HOH B 212     3799   5360   4189  -1011   -120  -1226       O  
HETATM 3133  O   HOH B 213      47.778 -29.748 127.285  1.00 44.04           O  
ANISOU 3133  O   HOH B 213     6735   5897   4102    571    101   -527       O  
HETATM 3134  O   HOH B 214      36.896 -12.870 126.200  1.00 27.29           O  
ANISOU 3134  O   HOH B 214     4242   2905   3220   -296    322  -1176       O  
HETATM 3135  O   HOH B 215      36.234 -10.047 109.984  1.00 43.20           O  
ANISOU 3135  O   HOH B 215     7428   4491   4492     68   1304    924       O  
HETATM 3136  O   HOH B 216      33.084 -21.812 107.435  1.00 44.12           O  
ANISOU 3136  O   HOH B 216     5700   5723   5338    430   1221  -1668       O  
HETATM 3137  O   HOH B 217      27.019  -1.165 128.697  1.00 22.05           O  
ANISOU 3137  O   HOH B 217     3704   1957   2715  -1183    379     83       O  
HETATM 3138  O   HOH B 218      32.540  -7.626 113.459  1.00 37.72           O  
ANISOU 3138  O   HOH B 218     4716   5533   4082   1006   2019    766       O  
HETATM 3139  O   HOH B 219      31.406 -10.247 112.549  1.00 42.47           O  
ANISOU 3139  O   HOH B 219     5317   6108   4709   -104    309    748       O  
HETATM 3140  O   HOH B 220      24.960 -30.481 123.633  1.00 37.31           O  
ANISOU 3140  O   HOH B 220     4793   3691   5689  -1109   2314  -1204       O  
HETATM 3141  O   HOH B 221      32.018 -35.384 121.055  1.00 51.98           O  
ANISOU 3141  O   HOH B 221     7667   5424   6657    776    831  -1999       O  
HETATM 3142  O   HOH B 222      41.791 -13.296 114.170  1.00 41.89           O  
ANISOU 3142  O   HOH B 222     4703   4286   6925   1119    634  -1172       O  
HETATM 3143  O   HOH B 223      44.064 -20.637 113.539  1.00 37.76           O  
ANISOU 3143  O   HOH B 223     6163   3728   4456   -577     48     64       O  
HETATM 3144  O   HOH B 224      29.489 -23.498 132.702  1.00 46.18           O  
ANISOU 3144  O   HOH B 224     7500   5066   4980  -1212   1963   1180       O  
HETATM 3145  O   HOH B 225      18.235 -11.426 127.659  1.00 36.91           O  
ANISOU 3145  O   HOH B 225     5259   3274   5488  -1272    -28   -300       O  
HETATM 3146  O   HOH B 226      26.961 -33.810 126.104  1.00 48.19           O  
ANISOU 3146  O   HOH B 226     6867   4719   6721    255   1400   -433       O  
HETATM 3147  O   HOH B 227      38.476  -9.277 125.071  1.00 44.27           O  
ANISOU 3147  O   HOH B 227     6102   4778   5940  -1500   -503   -362       O  
HETATM 3148  O   HOH B 228      26.248 -16.419 134.733  1.00 47.75           O  
ANISOU 3148  O   HOH B 228     6642   4105   7395   -859   1491     31       O  
HETATM 3149  O   HOH B 229      38.194  -6.144 121.913  1.00 43.80           O  
ANISOU 3149  O   HOH B 229     6609   4479   5551   -296   -793   1437       O  
HETATM 3150  O   HOH B 230      43.898 -16.647 115.318  1.00 42.13           O  
ANISOU 3150  O   HOH B 230     5506   2664   7836  -1134   -750    -11       O  
HETATM 3151  O   HOH B 231      20.867 -14.329 112.282  1.00 57.32           O  
ANISOU 3151  O   HOH B 231     5441   7207   9130    726   2502    496       O  
HETATM 3152  O   HOH B 232      29.869 -35.540 119.254  1.00 41.97           O  
ANISOU 3152  O   HOH B 232     6414   2838   6692  -1273   2216    -42       O  
HETATM 3153  O   HOH B 233      32.924  -6.085 117.011  1.00 32.58           O  
ANISOU 3153  O   HOH B 233     4720   4705   2951   -522   1329   -683       O  
HETATM 3154  O   HOH B 234      30.003 -16.886 133.638  1.00 31.80           O  
ANISOU 3154  O   HOH B 234     6907   1940   3234   -258   2061  -1037       O  
HETATM 3155  O   HOH B 235      38.460  -2.940 115.294  1.00 48.81           O  
ANISOU 3155  O   HOH B 235     5337   6774   6433   -733     22    673       O  
HETATM 3156  O   HOH B 236      44.086 -28.671 131.757  1.00 43.16           O  
ANISOU 3156  O   HOH B 236     5371   5882   5143    780   -810   -556       O  
HETATM 3157  O   HOH B 237      34.187 -14.983 108.368  1.00 39.45           O  
ANISOU 3157  O   HOH B 237     5609   4056   5324   1132   1083   -879       O  
HETATM 3158  O   HOH B 238      38.426 -34.638 113.012  1.00 40.73           O  
ANISOU 3158  O   HOH B 238     5900   3797   5776   1290     38  -1881       O  
HETATM 3159  O   HOH B 239      45.120 -26.245 131.381  1.00 60.59           O  
ANISOU 3159  O   HOH B 239     8913   9115   4993   -421      6    650       O  
HETATM 3160  O   HOH B 240      34.792 -14.734 131.490  1.00 53.34           O  
ANISOU 3160  O   HOH B 240     8002   3420   8843    492   1251   -918       O  
HETATM 3161  O   HOH B 241      36.239  -8.551 123.447  1.00 35.59           O  
ANISOU 3161  O   HOH B 241     4187   4257   5076    384   2224  -1842       O  
HETATM 3162  O   HOH B 242      33.590  -5.118 123.212  1.00 39.57           O  
ANISOU 3162  O   HOH B 242     5766   5117   4152   -506    913  -1329       O  
HETATM 3163  O   HOH B 243      35.022  -4.016 119.461  1.00 43.52           O  
ANISOU 3163  O   HOH B 243     5769   5777   4987   1388   -413   -329       O  
HETATM 3164  O   HOH B 244      42.414 -18.783 126.851  1.00 43.93           O  
ANISOU 3164  O   HOH B 244     6364   4369   5958    364    536   -792       O  
HETATM 3165  O   HOH B 245      33.353  -4.717 114.936  1.00 44.87           O  
ANISOU 3165  O   HOH B 245     7058   2064   7924    164    514  -1486       O  
HETATM 3166  O   HOH B 246      37.002 -14.120 128.596  1.00 44.32           O  
ANISOU 3166  O   HOH B 246     5562   6500   4776   1259     20  -1860       O  
HETATM 3167  O   HOH B 247      18.055  -2.701 127.669  1.00 38.31           O  
ANISOU 3167  O   HOH B 247     4735   3661   6158   -163   -642   -368       O  
CONECT  147  275                                                                
CONECT  275  147                                                                
CONECT  410 1078                                                                
CONECT  567 1244                                                                
CONECT  912 1015                                                                
CONECT 1015  912                                                                
CONECT 1078  410                                                                
CONECT 1244  567                                                                
CONECT 1631 1801                                                                
CONECT 1801 1631                                                                
CONECT 1907 1953                                                                
CONECT 1953 1907                                                                
CONECT 2110 2700                                                                
CONECT 2700 2110                                                                
MASTER      622    0    0   18   20    0    0    6 3165    2   14   33          
END                                                                             



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