CNRS Nantes University UFIP UFIP
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***  3S0A  ***

elNémo ID: 22060800352216411

Job options:

ID        	=	 22060800352216411
JOBID     	=	 3S0A
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 3S0A

HEADER    TRANSPORT PROTEIN                       13-MAY-11   3S0A              
TITLE     APIS MELLIFERA OBP14, NATIVE APO-PROTEIN                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: OBP14;                                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 18-135;                                       
COMPND   5 SYNONYM: ODORANT BINDING PROTEIN 14;                                 
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: APIS MELLIFERA;                                 
SOURCE   3 ORGANISM_COMMON: HONEYBEE;                                           
SOURCE   4 ORGANISM_TAXID: 7460;                                                
SOURCE   5 GENE: NP_001035313;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET-5 B(+)                            
KEYWDS    ALL HELICAL PROTEIN, UNKNOWN ODORANT MOLECULES, ANTENNAE, TRANSPORT   
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.SPINELLI,A.LAGARDE,I.IOVINELLA,M.TEGONI,P.PELOSI,C.CAMBILLAU        
REVDAT   2   11-JAN-12 3S0A    1       JRNL                                     
REVDAT   1   30-NOV-11 3S0A    0                                                
JRNL        AUTH   S.SPINELLI,A.LAGARDE,I.IOVINELLA,P.LEGRAND,M.TEGONI,         
JRNL        AUTH 2 P.PELOSI,C.CAMBILLAU                                         
JRNL        TITL   CRYSTAL STRUCTURE OF APIS MELLIFERA OBP14, A C-MINUS         
JRNL        TITL 2 ODORANT-BINDING PROTEIN, AND ITS COMPLEXES WITH ODORANT      
JRNL        TITL 3 MOLECULES.                                                   
JRNL        REF    INSECT BIOCHEM.MOL.BIOL.      V.  42    41 2012              
JRNL        REFN                   ISSN 0965-1748                               
JRNL        PMID   22075131                                                     
JRNL        DOI    10.1016/J.IBMB.2011.10.005                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 1.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.19                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 36080                          
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) : 0.156                           
REMARK   3   R VALUE            (WORKING SET) : 0.155                           
REMARK   3   FREE R VALUE                     : 0.178                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1900                            
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) : 1.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.18                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2290                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.17                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2780                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 128                          
REMARK   3   BIN FREE R VALUE                    : 0.3120                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 943                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 174                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 10.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 8.41                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.27000                                              
REMARK   3    B22 (A**2) : -0.62000                                             
REMARK   3    B33 (A**2) : 0.35000                                              
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): 0.039         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.038         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.024         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.142         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.972                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.957                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1025 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):   700 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1398 ; 1.481 ; 1.990       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  1772 ; 0.939 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   142 ; 5.165 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    43 ;39.520 ;27.907       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   228 ;11.282 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     1 ;11.590 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   172 ; 0.091 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1114 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   159 ; 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):   633 ; 1.196 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   251 ; 0.385 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1053 ; 1.938 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   392 ; 3.043 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   332 ; 4.680 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  1725 ; 1.132 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A    10                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.0760   3.6486  29.3747              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0774 T22:   0.0085                                     
REMARK   3      T33:   0.0100 T12:   0.0003                                     
REMARK   3      T13:   0.0154 T23:  -0.0037                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.3470 L22:   2.2944                                     
REMARK   3      L33:   2.7862 L12:   0.6833                                     
REMARK   3      L13:   0.8573 L23:   0.9768                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0657 S12:   0.0239 S13:   0.0535                       
REMARK   3      S21:   0.2585 S22:  -0.0641 S23:   0.0081                       
REMARK   3      S31:   0.2291 S32:  -0.0502 S33:  -0.0016                       
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    11        A    20                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.2693  16.6159  24.6320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0295 T22:   0.0265                                     
REMARK   3      T33:   0.0278 T12:  -0.0023                                     
REMARK   3      T13:   0.0031 T23:   0.0066                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0020 L22:   2.7770                                     
REMARK   3      L33:   0.3918 L12:  -0.3908                                     
REMARK   3      L13:  -0.0735 L23:  -0.6290                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0090 S12:   0.0082 S13:   0.0355                       
REMARK   3      S21:   0.0166 S22:   0.0151 S23:  -0.0600                       
REMARK   3      S31:   0.0316 S32:   0.0454 S33:  -0.0061                       
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    21        A    30                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.1875  25.1344  31.7697              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0192 T22:   0.0266                                     
REMARK   3      T33:   0.0364 T12:   0.0011                                     
REMARK   3      T13:  -0.0118 T23:   0.0038                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1607 L22:   1.7587                                     
REMARK   3      L33:   2.4276 L12:   0.6420                                     
REMARK   3      L13:   0.1966 L23:  -0.1157                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0310 S12:   0.0043 S13:  -0.0158                       
REMARK   3      S21:   0.0705 S22:  -0.0402 S23:  -0.1415                       
REMARK   3      S31:  -0.0695 S32:   0.0876 S33:   0.0092                       
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    31        A    40                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.5744  24.2945  36.1154              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0566 T22:   0.0219                                     
REMARK   3      T33:   0.0579 T12:   0.0042                                     
REMARK   3      T13:  -0.0028 T23:  -0.0142                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8408 L22:   0.3201                                     
REMARK   3      L33:   1.0361 L12:  -0.1701                                     
REMARK   3      L13:   0.9860 L23:  -1.0043                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0156 S12:  -0.1472 S13:   0.1476                       
REMARK   3      S21:   0.1215 S22:   0.0034 S23:   0.0491                       
REMARK   3      S31:  -0.0796 S32:   0.0050 S33:   0.0122                       
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    41        A    50                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.6784  24.3429  26.3656              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0214 T22:   0.0225                                     
REMARK   3      T33:   0.0454 T12:  -0.0092                                     
REMARK   3      T13:  -0.0081 T23:   0.0264                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4060 L22:   0.9172                                     
REMARK   3      L33:   0.4988 L12:  -0.0935                                     
REMARK   3      L13:   0.3538 L23:   0.7148                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0610 S12:   0.0391 S13:   0.0712                       
REMARK   3      S21:  -0.0144 S22:   0.0547 S23:   0.0488                       
REMARK   3      S31:  -0.0087 S32:   0.0235 S33:   0.0063                       
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    51        A    60                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.3997  15.0005  21.3281              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0255 T22:   0.0038                                     
REMARK   3      T33:   0.0749 T12:  -0.0127                                     
REMARK   3      T13:  -0.0303 T23:   0.0051                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1937 L22:  -0.3164                                     
REMARK   3      L33:   1.9743 L12:   0.1999                                     
REMARK   3      L13:   0.9796 L23:  -0.4571                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0067 S12:   0.0290 S13:  -0.1629                       
REMARK   3      S21:  -0.0674 S22:   0.0189 S23:   0.0262                       
REMARK   3      S31:   0.1007 S32:  -0.0519 S33:  -0.0256                       
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    61        A    70                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.1393  11.0066  27.0680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0405 T22:   0.0775                                     
REMARK   3      T33:   0.0146 T12:  -0.0413                                     
REMARK   3      T13:  -0.0079 T23:   0.0255                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3598 L22:   3.4179                                     
REMARK   3      L33:   4.1940 L12:   0.8691                                     
REMARK   3      L13:   3.6595 L23:  -2.2502                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2216 S12:  -0.3623 S13:   0.0800                       
REMARK   3      S21:  -0.1807 S22:   0.1599 S23:   0.2098                       
REMARK   3      S31:   0.4486 S32:  -0.5681 S33:  -0.3814                       
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    71        A    80                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.8845   3.0878  37.3525              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0494 T22:   0.0480                                     
REMARK   3      T33:   0.0126 T12:  -0.0233                                     
REMARK   3      T13:   0.0192 T23:  -0.0133                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6201 L22:   0.5004                                     
REMARK   3      L33:   1.8780 L12:   0.5827                                     
REMARK   3      L13:  -1.6413 L23:   0.0233                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1759 S12:  -0.0839 S13:  -0.0687                       
REMARK   3      S21:  -0.0684 S22:   0.1459 S23:  -0.1023                       
REMARK   3      S31:   0.1498 S32:  -0.0629 S33:   0.0300                       
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    81        A    90                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.5470  10.9796  37.3931              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0185 T22:   0.0437                                     
REMARK   3      T33:   0.0370 T12:  -0.0031                                     
REMARK   3      T13:   0.0020 T23:   0.0235                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.5537 L22:   3.9922                                     
REMARK   3      L33:   2.0320 L12:  -0.4567                                     
REMARK   3      L13:   0.5005 L23:  -2.1334                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0001 S12:  -0.0392 S13:   0.0671                       
REMARK   3      S21:  -0.0821 S22:   0.0504 S23:   0.0872                       
REMARK   3      S31:   0.0884 S32:  -0.1081 S33:  -0.0503                       
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    91        A   100                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.1501  25.5966  29.0126              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0210 T22:   0.0400                                     
REMARK   3      T33:   0.0852 T12:   0.0085                                     
REMARK   3      T13:  -0.0174 T23:   0.0516                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0873 L22:   0.4444                                     
REMARK   3      L33:   1.7911 L12:   0.5537                                     
REMARK   3      L13:  -0.5580 L23:  -0.4601                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0321 S12:   0.0006 S13:   0.0563                       
REMARK   3      S21:  -0.0929 S22:   0.0559 S23:   0.1479                       
REMARK   3      S31:   0.0184 S32:  -0.1324 S33:  -0.0880                       
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   101        A   109                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.4710  19.2953  36.9108              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0180 T22:   0.0310                                     
REMARK   3      T33:   0.0409 T12:  -0.0049                                     
REMARK   3      T13:   0.0152 T23:   0.0217                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.3429 L22:   2.0393                                     
REMARK   3      L33:   3.2317 L12:   0.0243                                     
REMARK   3      L13:   0.0968 L23:  -1.0686                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0262 S12:  -0.0174 S13:   0.0632                       
REMARK   3      S21:   0.0668 S22:  -0.0360 S23:   0.0813                       
REMARK   3      S31:   0.0515 S32:  -0.0630 S33:   0.0098                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   110        A   119                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.3636  10.0182  38.8647              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0650 T22:   0.0308                                     
REMARK   3      T33:   0.0051 T12:   0.0142                                     
REMARK   3      T13:  -0.0093 T23:   0.0139                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5462 L22:   0.6778                                     
REMARK   3      L33:   0.3442 L12:  -0.2646                                     
REMARK   3      L13:   0.6123 L23:  -0.2323                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0337 S12:   0.0096 S13:  -0.0190                       
REMARK   3      S21:  -0.0090 S22:  -0.0139 S23:   0.0040                       
REMARK   3      S31:   0.0844 S32:   0.0278 S33:  -0.0198                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS                   
REMARK   3  U VALUES      : RESIDUAL ONLY                                       
REMARK   4                                                                      
REMARK   4 3S0A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAY-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB065598.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-FEB-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 1                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8265                             
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37980                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.100                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : 0.04500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 18.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.50000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3RZS                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8-1.9 M  TRI-SODIUM CITRATE, 25 MM     
REMARK 280  CHES, PH 9.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K       
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       16.20500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       43.19000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       18.99500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       43.19000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       16.20500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       18.99500            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   210     O    HOH A   246              1.67            
REMARK 500   O    HOH A   172     O    HOH A   173              1.91            
REMARK 500   O    HOH A   144     O    HOH A   146              2.19            
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 126        DISTANCE =  6.00 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3RZS   RELATED DB: PDB                                   
REMARK 900 APIS MELLIFERA OBP14 IN COMPLEX WITH TA6BR14                         
REMARK 900 RELATED ID: 3S0B   RELATED DB: PDB                                   
REMARK 900 APIS MELLIFERA OBP14 IN COMPLEX WITH THE FLUORESCENT PROBE           
REMARK 900 1-N-PHENYLNAPHTHYLAMINE                                              
REMARK 900 RELATED ID: 3S0D   RELATED DB: PDB                                   
REMARK 900 APIS MELLIFERA OBP 14 IN COMPLEX WITH THE CITRUS ODORANT             
REMARK 900 CITRALVA                                                             
REMARK 900 RELATED ID: 3S0E   RELATED DB: PDB                                   
REMARK 900 APIS MELLIFERA OBP14 IN COMPLEX WITH THE ODORANT EUGENOL             
REMARK 900 RELATED ID: 3S0F   RELATED DB: PDB                                   
REMARK 900 APIS MELLIFERA OBP14, NATIVE APO, CRYSTAL FORM 2                     
REMARK 900 RELATED ID: 3S0G   RELATED DB: PDB                                   
REMARK 900 APIS MELLIFERA OBP 14 DOUBLE MUTANT GLN44CYS, HIS97CYS               
DBREF  3S0A A    2   119  UNP    Q1W640   Q1W640_APIME    18    135             
SEQADV 3S0A MET A    1  UNP  Q1W640              INITIATING METHIONINE          
SEQRES   1 A  119  MET THR ILE GLU GLU LEU LYS THR ARG LEU HIS THR GLU          
SEQRES   2 A  119  GLN SER VAL CYS LYS THR GLU THR GLY ILE ASP GLN GLN          
SEQRES   3 A  119  LYS ALA ASN ASP VAL ILE GLU GLY ASN ILE ASP VAL GLU          
SEQRES   4 A  119  ASP LYS LYS VAL GLN LEU TYR CYS GLU CYS ILE LEU LYS          
SEQRES   5 A  119  ASN PHE ASN ILE LEU ASP LYS ASN ASN VAL PHE LYS PRO          
SEQRES   6 A  119  GLN GLY ILE LYS ALA VAL MET GLU LEU LEU ILE ASP GLU          
SEQRES   7 A  119  ASN SER VAL LYS GLN LEU VAL SER ASP CYS SER THR ILE          
SEQRES   8 A  119  SER GLU GLU ASN PRO HIS LEU LYS ALA SER LYS LEU VAL          
SEQRES   9 A  119  GLN CYS VAL SER LYS TYR LYS THR MET LYS SER VAL ASP          
SEQRES  10 A  119  PHE LEU                                                      
FORMUL   2  HOH   *174(H2 O)                                                    
HELIX    1   1 THR A    2  GLY A   22  1                                  21    
HELIX    2   2 ASP A   24  GLU A   33  1                                  10    
HELIX    3   3 ASP A   40  PHE A   54  1                                  15    
HELIX    4   4 LYS A   64  GLU A   73  1                                  10    
HELIX    5   5 ASP A   77  SER A   89  1                                  13    
HELIX    6   6 ASN A   95  LYS A  109  1                                  15    
HELIX    7   7 THR A  112  ASP A  117  1                                   6    
SSBOND   1 CYS A   17    CYS A   49                          1555   1555  2.06  
SSBOND   2 CYS A   88    CYS A  106                          1555   1555  2.02  
CRYST1   32.410   37.990   86.380  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      0.030855  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.026323  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011577        0.00000                         
ATOM      1  N   MET A   1      10.739  -2.256  28.043  1.00 17.55           N  
ANISOU    1  N   MET A   1     2181   2106   2378    -99    -83     37       N  
ATOM      2  CA AMET A   1      11.812  -1.226  28.089  0.50 16.67           C  
ANISOU    2  CA AMET A   1     2105   2093   2136    -51    -54     29       C  
ATOM      3  CA BMET A   1      11.809  -1.229  28.100  0.50 16.03           C  
ANISOU    3  CA BMET A   1     2041   1999   2049    -71    -44     53       C  
ATOM      4  C   MET A   1      12.429  -1.301  29.462  1.00 15.02           C  
ANISOU    4  C   MET A   1     1934   1888   1884    -58    -34     -6       C  
ATOM      5  O   MET A   1      11.738  -1.135  30.470  1.00 16.30           O  
ANISOU    5  O   MET A   1     2023   2174   1995    -57     27    226       O  
ATOM      6  CB AMET A   1      11.269   0.179  27.825  0.50 17.46           C  
ANISOU    6  CB AMET A   1     2205   2193   2233     21    -63    -28       C  
ATOM      7  CB BMET A   1      11.242   0.159  27.884  0.50 16.44           C  
ANISOU    7  CB BMET A   1     2086   2046   2112    -40    -42     11       C  
ATOM      8  CG AMET A   1      12.338   1.144  27.334  0.50 18.68           C  
ANISOU    8  CG AMET A   1     2269   2366   2462     49    -54    -64       C  
ATOM      9  CG BMET A   1      12.258   1.260  28.084  0.50 15.37           C  
ANISOU    9  CG BMET A   1     2000   1865   1975    -92     -8    100       C  
ATOM     10  SD AMET A   1      12.123   2.876  27.781  0.50 20.24           S  
ANISOU   10  SD AMET A   1     2409   2596   2684    140   -252   -283       S  
ATOM     11  SD BMET A   1      11.502   2.852  27.794  0.50 17.86           S  
ANISOU   11  SD BMET A   1     2014   1949   2823   -241     51    174       S  
ATOM     12  CE AMET A   1      10.963   3.457  26.556  0.50 15.74           C  
ANISOU   12  CE AMET A   1     2111   2495   1374      9    271   -370       C  
ATOM     13  CE BMET A   1      12.782   3.704  26.900  0.50 13.71           C  
ANISOU   13  CE BMET A   1     2044   1503   1661   -857   -436    385       C  
ATOM     14  N   THR A   2      13.719  -1.566  29.502  1.00 11.92           N  
ANISOU   14  N   THR A   2     1724   1402   1400   -229      6     63       N  
ATOM     15  CA  THR A   2      14.361  -1.752  30.776  1.00 10.56           C  
ANISOU   15  CA  THR A   2     1554   1257   1199   -237     -7     78       C  
ATOM     16  C   THR A   2      14.629  -0.369  31.397  1.00  9.90           C  
ANISOU   16  C   THR A   2     1482   1149   1128   -200     46     60       C  
ATOM     17  O   THR A   2      14.598   0.692  30.730  1.00 10.06           O  
ANISOU   17  O   THR A   2     1520   1224   1077   -311    -59     78       O  
ATOM     18  CB  THR A   2      15.678  -2.499  30.635  1.00 10.62           C  
ANISOU   18  CB  THR A   2     1631   1210   1193   -243     67    118       C  
ATOM     19  OG1 THR A   2      16.608  -1.663  29.938  1.00 11.16           O  
ANISOU   19  OG1 THR A   2     1611   1190   1440   -191     70    216       O  
ATOM     20  CG2 THR A   2      15.487  -3.840  29.902  1.00 11.58           C  
ANISOU   20  CG2 THR A   2     1726   1238   1434   -320     95     45       C  
ATOM     21  N   ILE A   3      14.910  -0.366  32.695  1.00  9.78           N  
ANISOU   21  N   ILE A   3     1459   1117   1140   -201     29    110       N  
ATOM     22  CA AILE A   3      15.268   0.875  33.370  0.50  9.85           C  
ANISOU   22  CA AILE A   3     1436   1242   1063   -103     41     54       C  
ATOM     23  CA BILE A   3      15.262   0.869  33.367  0.50  9.89           C  
ANISOU   23  CA BILE A   3     1421   1240   1095    -99     33     67       C  
ATOM     24  C   ILE A   3      16.509   1.477  32.728  1.00  9.69           C  
ANISOU   24  C   ILE A   3     1419   1192   1069    -31     16     94       C  
ATOM     25  O   ILE A   3      16.580   2.694  32.558  1.00  9.12           O  
ANISOU   25  O   ILE A   3     1502    962   1001    -78     -3    106       O  
ATOM     26  CB AILE A   3      15.520   0.641  34.869  0.50 10.19           C  
ANISOU   26  CB AILE A   3     1459   1348   1064    -78     36    102       C  
ATOM     27  CB BILE A   3      15.438   0.621  34.882  0.50 10.16           C  
ANISOU   27  CB BILE A   3     1428   1336   1095    -87     27    119       C  
ATOM     28  CG1AILE A   3      14.215   0.332  35.608  0.50 11.33           C  
ANISOU   28  CG1AILE A   3     1523   1580   1203    -64    154     14       C  
ATOM     29  CG1BILE A   3      15.628   1.944  35.618  0.50 10.50           C  
ANISOU   29  CG1BILE A   3     1363   1442   1181   -151    -82     16       C  
ATOM     30  CG2AILE A   3      16.174   1.854  35.490  0.50 10.07           C  
ANISOU   30  CG2AILE A   3     1482   1391    951   -133    -21     56       C  
ATOM     31  CG2BILE A   3      16.587  -0.358  35.166  0.50 11.72           C  
ANISOU   31  CG2BILE A   3     1525   1550   1376     31     95    165       C  
ATOM     32  CD1AILE A   3      13.148   1.341  35.418  0.50 11.60           C  
ANISOU   32  CD1AILE A   3     1478   2063    866     94     87     60       C  
ATOM     33  CD1BILE A   3      14.482   2.855  35.434  0.50 12.40           C  
ANISOU   33  CD1BILE A   3     1525   1745   1441     39   -173    -10       C  
ATOM     34  N   GLU A   4      17.472   0.633  32.347  1.00 10.49           N  
ANISOU   34  N   GLU A   4     1555   1216   1212     40    -12     73       N  
ATOM     35  CA  GLU A   4      18.694   1.153  31.739  1.00 11.41           C  
ANISOU   35  CA  GLU A   4     1539   1325   1471    140      5     94       C  
ATOM     36  C   GLU A   4      18.374   1.768  30.372  1.00  9.90           C  
ANISOU   36  C   GLU A   4     1413   1133   1213     61     73     16       C  
ATOM     37  O   GLU A   4      18.937   2.794  30.027  1.00  9.81           O  
ANISOU   37  O   GLU A   4     1150   1190   1388     58     46     68       O  
ATOM     38  CB  GLU A   4      19.806   0.089  31.655  1.00 13.15           C  
ANISOU   38  CB  GLU A   4     1704   1501   1789    173     55     83       C  
ATOM     39  CG  GLU A   4      20.461  -0.248  33.001  1.00 18.12           C  
ANISOU   39  CG  GLU A   4     2134   2426   2324    282   -102    213       C  
ATOM     40  CD  GLU A   4      21.154   0.926  33.682  1.00 22.89           C  
ANISOU   40  CD  GLU A   4     2815   3020   2859    197   -122    123       C  
ATOM     41  OE1 GLU A   4      21.982   1.620  33.045  1.00 26.46           O  
ANISOU   41  OE1 GLU A   4     3053   3646   3354     84    -14    279       O  
ATOM     42  OE2 GLU A   4      20.888   1.141  34.890  1.00 26.76           O  
ANISOU   42  OE2 GLU A   4     3354   3793   3017    246    -34    -63       O  
ATOM     43  N   GLU A   5      17.460   1.159  29.615  1.00  8.48           N  
ANISOU   43  N   GLU A   5     1252    884   1083     66    125     88       N  
ATOM     44  CA  GLU A   5      17.039   1.755  28.346  1.00  8.15           C  
ANISOU   44  CA  GLU A   5     1225    934    937      4     93    -28       C  
ATOM     45  C   GLU A   5      16.325   3.086  28.540  1.00  6.89           C  
ANISOU   45  C   GLU A   5     1058    774    785     -3    140    -24       C  
ATOM     46  O   GLU A   5      16.540   4.006  27.756  1.00  7.27           O  
ANISOU   46  O   GLU A   5     1198    753    809    -23    159     45       O  
ATOM     47  CB  GLU A   5      16.181   0.780  27.567  1.00  8.65           C  
ANISOU   47  CB  GLU A   5     1272    890   1123    -64     79    -28       C  
ATOM     48  CG  GLU A   5      17.005  -0.382  26.983  1.00 10.42           C  
ANISOU   48  CG  GLU A   5     1707    985   1265    -54    239   -127       C  
ATOM     49  CD  GLU A   5      16.210  -1.615  26.661  1.00 11.47           C  
ANISOU   49  CD  GLU A   5     1949    936   1470     18    223   -193       C  
ATOM     50  OE1 GLU A   5      14.965  -1.641  26.835  1.00 12.08           O  
ANISOU   50  OE1 GLU A   5     2063   1187   1337   -343     60   -159       O  
ATOM     51  OE2 GLU A   5      16.865  -2.557  26.181  1.00 17.89           O  
ANISOU   51  OE2 GLU A   5     2822   1347   2626     16    537   -516       O  
ATOM     52  N   LEU A   6      15.483   3.189  29.566  1.00  6.69           N  
ANISOU   52  N   LEU A   6      931    712    896    -98    119     84       N  
ATOM     53  CA  LEU A   6      14.810   4.448  29.855  1.00  6.72           C  
ANISOU   53  CA  LEU A   6      908    812    834    -75     71     64       C  
ATOM     54  C   LEU A   6      15.806   5.513  30.263  1.00  6.01           C  
ANISOU   54  C   LEU A   6      805    768    707      7     60    -25       C  
ATOM     55  O   LEU A   6      15.682   6.654  29.821  1.00  6.23           O  
ANISOU   55  O   LEU A   6      897    712    759      1     52    -59       O  
ATOM     56  CB  LEU A   6      13.721   4.268  30.925  1.00  7.29           C  
ANISOU   56  CB  LEU A   6      958   1003    806    -76    121    102       C  
ATOM     57  CG  LEU A   6      13.011   5.563  31.347  1.00  8.69           C  
ANISOU   57  CG  LEU A   6     1009   1220   1072    -77    149     43       C  
ATOM     58  CD1 LEU A   6      12.227   6.165  30.192  1.00  9.79           C  
ANISOU   58  CD1 LEU A   6     1102   1262   1353     48     78     34       C  
ATOM     59  CD2 LEU A   6      12.088   5.282  32.531  1.00  9.71           C  
ANISOU   59  CD2 LEU A   6      858   1593   1236   -112     77   -133       C  
ATOM     60  N   LYS A   7      16.797   5.164  31.092  1.00  6.69           N  
ANISOU   60  N   LYS A   7      978    733    829     22    -43    100       N  
ATOM     61  CA  LYS A   7      17.814   6.133  31.454  1.00  7.03           C  
ANISOU   61  CA  LYS A   7      944    848    878     60    -45     28       C  
ATOM     62  C   LYS A   7      18.461   6.703  30.204  1.00  6.75           C  
ANISOU   62  C   LYS A   7      943    795    824    -15    -19     46       C  
ATOM     63  O   LYS A   7      18.680   7.897  30.094  1.00  7.15           O  
ANISOU   63  O   LYS A   7     1014    843    860     80    -34     62       O  
ATOM     64  CB  LYS A   7      18.904   5.494  32.319  1.00  7.63           C  
ANISOU   64  CB  LYS A   7      991   1038    869    124   -118     74       C  
ATOM     65  CG  LYS A   7      18.531   5.159  33.730  1.00  9.63           C  
ANISOU   65  CG  LYS A   7     1315   1241   1100    190   -222    101       C  
ATOM     66  CD  LYS A   7      19.735   4.544  34.454  1.00 13.92           C  
ANISOU   66  CD  LYS A   7     1619   1932   1737    295   -241    153       C  
ATOM     67  CE  LYS A   7      19.362   3.834  35.748  1.00 15.59           C  
ANISOU   67  CE  LYS A   7     1685   2185   2051    327   -111    294       C  
ATOM     68  NZ  LYS A   7      20.592   3.258  36.357  1.00 18.68           N  
ANISOU   68  NZ  LYS A   7     1731   2666   2701    578   -213    506       N  
ATOM     69  N   THR A   8      18.837   5.812  29.289  1.00  6.75           N  
ANISOU   69  N   THR A   8      949    771    845     41   -114     51       N  
ATOM     70  CA  THR A   8      19.507   6.189  28.065  1.00  7.00           C  
ANISOU   70  CA  THR A   8      843    848    967    145      2     11       C  
ATOM     71  C   THR A   8      18.609   7.051  27.169  1.00  5.96           C  
ANISOU   71  C   THR A   8      774    671    817     -1     42    -72       C  
ATOM     72  O   THR A   8      19.059   8.063  26.636  1.00  6.34           O  
ANISOU   72  O   THR A   8      775    755    879     14    -10     39       O  
ATOM     73  CB  THR A   8      19.991   4.914  27.359  1.00  8.06           C  
ANISOU   73  CB  THR A   8      890    997   1173    201     32     58       C  
ATOM     74  OG1 THR A   8      20.852   4.182  28.234  1.00 10.49           O  
ANISOU   74  OG1 THR A   8     1356   1331   1296    509    -67     21       O  
ATOM     75  CG2 THR A   8      20.742   5.255  26.109  1.00  9.54           C  
ANISOU   75  CG2 THR A   8     1047   1233   1345    237    112     98       C  
ATOM     76  N   ARG A   9      17.355   6.635  27.019  1.00  4.68           N  
ANISOU   76  N   ARG A   9      634    503    638     -5     72    -34       N  
ATOM     77  CA  ARG A   9      16.415   7.390  26.219  1.00  5.09           C  
ANISOU   77  CA  ARG A   9      666    613    654     -6     80     22       C  
ATOM     78  C   ARG A   9      16.231   8.790  26.765  1.00  4.34           C  
ANISOU   78  C   ARG A   9      609    595    444     44     -6    -46       C  
ATOM     79  O   ARG A   9      16.161   9.760  26.011  1.00  4.63           O  
ANISOU   79  O   ARG A   9      588    641    530     21     -6      2       O  
ATOM     80  CB  ARG A   9      15.086   6.643  26.164  1.00  5.43           C  
ANISOU   80  CB  ARG A   9      748    620    695    -30     57     22       C  
ATOM     81  CG  ARG A   9      13.939   7.355  25.469  1.00  4.92           C  
ANISOU   81  CG  ARG A   9      664    583    620   -110    109    -10       C  
ATOM     82  CD  ARG A   9      14.145   7.507  23.978  1.00  5.43           C  
ANISOU   82  CD  ARG A   9      671    676    716     31     91   -101       C  
ATOM     83  NE  ARG A   9      13.036   8.216  23.359  1.00  5.25           N  
ANISOU   83  NE  ARG A   9      587    712    695    -21    100    -90       N  
ATOM     84  CZ  ARG A   9      11.864   7.681  23.068  1.00  6.09           C  
ANISOU   84  CZ  ARG A   9      533    707   1074     79    219      0       C  
ATOM     85  NH1 ARG A   9      11.627   6.400  23.252  1.00  7.97           N  
ANISOU   85  NH1 ARG A   9      596    885   1544     71    -68     24       N  
ATOM     86  NH2 ARG A   9      10.912   8.441  22.553  1.00  7.53           N  
ANISOU   86  NH2 ARG A   9      728    884   1248     63   -103    -30       N  
ATOM     87  N   LEU A  10      16.119   8.906  28.076  1.00  4.67           N  
ANISOU   87  N   LEU A  10      656    591    527    -29      8     49       N  
ATOM     88  CA  LEU A  10      15.990  10.222  28.701  1.00  4.61           C  
ANISOU   88  CA  LEU A  10      618    622    512      7    -55    -52       C  
ATOM     89  C   LEU A  10      17.199  11.098  28.402  1.00  4.57           C  
ANISOU   89  C   LEU A  10      597    679    459     20    -80    -77       C  
ATOM     90  O   LEU A  10      17.041  12.244  28.056  1.00  4.46           O  
ANISOU   90  O   LEU A  10      549    638    506     22     19    -36       O  
ATOM     91  CB  LEU A  10      15.762  10.091  30.205  1.00  5.53           C  
ANISOU   91  CB  LEU A  10      702    790    610    -15     12    -57       C  
ATOM     92  CG  LEU A  10      14.373   9.665  30.647  1.00  6.11           C  
ANISOU   92  CG  LEU A  10      857    834    630    -22     58    -92       C  
ATOM     93  CD1 LEU A  10      14.407   9.263  32.106  1.00  7.71           C  
ANISOU   93  CD1 LEU A  10     1069   1262    596   -247    282      8       C  
ATOM     94  CD2 LEU A  10      13.360  10.767  30.402  1.00  8.40           C  
ANISOU   94  CD2 LEU A  10      949   1268    975     83    145     81       C  
ATOM     95  N   HIS A  11      18.397  10.548  28.540  1.00  4.41           N  
ANISOU   95  N   HIS A  11      683    484    506     59    -53     28       N  
ATOM     96  CA  HIS A  11      19.568  11.324  28.230  1.00  5.03           C  
ANISOU   96  CA  HIS A  11      739    614    555    -34    -81    -92       C  
ATOM     97  C   HIS A  11      19.559  11.783  26.768  1.00  4.83           C  
ANISOU   97  C   HIS A  11      660    597    576    111   -109    -81       C  
ATOM     98  O   HIS A  11      19.933  12.909  26.484  1.00  4.97           O  
ANISOU   98  O   HIS A  11      606    654    626    -29      1    -27       O  
ATOM     99  CB  HIS A  11      20.842  10.529  28.511  1.00  6.07           C  
ANISOU   99  CB  HIS A  11      850    718    737    -28     27    -86       C  
ATOM    100  CG  HIS A  11      21.131  10.292  29.961  1.00  9.55           C  
ANISOU  100  CG  HIS A  11     1124   1296   1207     37     80     89       C  
ATOM    101  ND1 HIS A  11      20.613  11.011  31.025  1.00 12.40           N  
ANISOU  101  ND1 HIS A  11     1555   1885   1268     80   -311    413       N  
ATOM    102  CD2 HIS A  11      21.977   9.390  30.496  1.00  9.95           C  
ANISOU  102  CD2 HIS A  11     1050   1332   1396    348     88    268       C  
ATOM    103  CE1 HIS A  11      21.113  10.526  32.150  1.00 10.20           C  
ANISOU  103  CE1 HIS A  11     1323   1640    911    272     84     81       C  
ATOM    104  NE2 HIS A  11      21.948   9.550  31.856  1.00 14.46           N  
ANISOU  104  NE2 HIS A  11     1847   2148   1497    231    -47    190       N  
ATOM    105  N   THR A  12      19.154  10.906  25.853  1.00  4.62           N  
ANISOU  105  N   THR A  12      599    555    601      6     68    -55       N  
ATOM    106  CA  THR A  12      19.084  11.238  24.456  1.00  4.54           C  
ANISOU  106  CA  THR A  12      585    586    551     46     19    -56       C  
ATOM    107  C   THR A  12      18.101  12.361  24.195  1.00  4.61           C  
ANISOU  107  C   THR A  12      635    507    610     34     70    -77       C  
ATOM    108  O   THR A  12      18.427  13.315  23.489  1.00  4.63           O  
ANISOU  108  O   THR A  12      575    579    605     28     87    -21       O  
ATOM    109  CB  THR A  12      18.792   9.988  23.613  1.00  4.50           C  
ANISOU  109  CB  THR A  12      512    594    601    111     76    -43       C  
ATOM    110  OG1 THR A  12      19.966   9.181  23.695  1.00  5.26           O  
ANISOU  110  OG1 THR A  12      580    714    702     95    -17   -167       O  
ATOM    111  CG2 THR A  12      18.501  10.330  22.163  1.00  5.70           C  
ANISOU  111  CG2 THR A  12      763    836    565    -40    -54   -121       C  
ATOM    112  N   GLU A  13      16.897  12.260  24.748  1.00  3.91           N  
ANISOU  112  N   GLU A  13      572    442    470     20     80     21       N  
ATOM    113  CA  GLU A  13      15.910  13.286  24.519  1.00  3.81           C  
ANISOU  113  CA  GLU A  13      513    499    433     30     36    -69       C  
ATOM    114  C   GLU A  13      16.293  14.593  25.176  1.00  3.94           C  
ANISOU  114  C   GLU A  13      515    452    528     18     34    -41       C  
ATOM    115  O   GLU A  13      16.024  15.665  24.630  1.00  4.60           O  
ANISOU  115  O   GLU A  13      670    498    577     20     21    -31       O  
ATOM    116  CB  GLU A  13      14.498  12.844  24.935  1.00  4.44           C  
ANISOU  116  CB  GLU A  13      575    585    525     -6     83    -65       C  
ATOM    117  CG  GLU A  13      13.964  11.600  24.241  1.00  5.24           C  
ANISOU  117  CG  GLU A  13      636    632    721    -63    -23     27       C  
ATOM    118  CD  GLU A  13      13.798  11.660  22.722  1.00  5.09           C  
ANISOU  118  CD  GLU A  13      524    628    781      1     54    -45       C  
ATOM    119  OE1 GLU A  13      14.244  12.636  22.083  1.00  6.57           O  
ANISOU  119  OE1 GLU A  13      784    947    765   -193      8    -50       O  
ATOM    120  OE2 GLU A  13      13.204  10.684  22.212  1.00  6.34           O  
ANISOU  120  OE2 GLU A  13      776    812    821    -38    -24    -57       O  
ATOM    121  N   GLN A  14      16.885  14.538  26.365  1.00  3.52           N  
ANISOU  121  N   GLN A  14      507    364    464    -10     24    -30       N  
ATOM    122  CA  GLN A  14      17.410  15.726  27.001  1.00  4.08           C  
ANISOU  122  CA  GLN A  14      624    397    525      8    -17    -31       C  
ATOM    123  C   GLN A  14      18.412  16.421  26.100  1.00  4.76           C  
ANISOU  123  C   GLN A  14      636    523    650      8    -19    -22       C  
ATOM    124  O   GLN A  14      18.410  17.645  25.970  1.00  5.29           O  
ANISOU  124  O   GLN A  14      734    566    707    -54     38     12       O  
ATOM    125  CB  GLN A  14      18.047  15.337  28.328  1.00  4.32           C  
ANISOU  125  CB  GLN A  14      638    430    573     -8    -88   -113       C  
ATOM    126  CG  GLN A  14      17.025  15.000  29.398  1.00  4.25           C  
ANISOU  126  CG  GLN A  14      596    578    438    -30   -135   -114       C  
ATOM    127  CD  GLN A  14      17.564  14.126  30.516  1.00  5.00           C  
ANISOU  127  CD  GLN A  14      737    637    524    -76    -22   -156       C  
ATOM    128  OE1 GLN A  14      18.751  13.880  30.591  1.00  6.52           O  
ANISOU  128  OE1 GLN A  14      887    986    603    203     12    -27       O  
ATOM    129  NE2 GLN A  14      16.682  13.646  31.369  1.00  5.63           N  
ANISOU  129  NE2 GLN A  14      863    639    637    -58     37   -107       N  
ATOM    130  N   SER A  15      19.285  15.647  25.468  1.00  5.08           N  
ANISOU  130  N   SER A  15      633    600    696    -13     -6      3       N  
ATOM    131  CA ASER A  15      20.296  16.215  24.583  0.50  5.36           C  
ANISOU  131  CA ASER A  15      654    730    649    -52     22     23       C  
ATOM    132  CA BSER A  15      20.298  16.223  24.595  0.50  5.92           C  
ANISOU  132  CA BSER A  15      727    802    719    -42      5     13       C  
ATOM    133  C   SER A  15      19.684  16.870  23.355  1.00  5.28           C  
ANISOU  133  C   SER A  15      682    645    679    -92     81     24       C  
ATOM    134  O   SER A  15      20.001  18.012  23.039  1.00  5.74           O  
ANISOU  134  O   SER A  15      780    669    732    -42     14     31       O  
ATOM    135  CB ASER A  15      21.281  15.137  24.142  0.50  5.91           C  
ANISOU  135  CB ASER A  15      666    845    732    -56     46    111       C  
ATOM    136  CB BSER A  15      21.321  15.149  24.221  0.50  6.74           C  
ANISOU  136  CB BSER A  15      776    949    836    -36     45     73       C  
ATOM    137  OG ASER A  15      22.165  15.673  23.174  0.50  6.76           O  
ANISOU  137  OG ASER A  15      723   1000    846     -6    242    250       O  
ATOM    138  OG BSER A  15      22.015  14.704  25.378  0.50 11.01           O  
ANISOU  138  OG BSER A  15     1284   1613   1287     84    -24    139       O  
ATOM    139  N   VAL A  16      18.805  16.149  22.663  1.00  4.91           N  
ANISOU  139  N   VAL A  16      637    559    666    -39     53    -37       N  
ATOM    140  CA  VAL A  16      18.254  16.709  21.439  1.00  5.83           C  
ANISOU  140  CA  VAL A  16      813    676    725    -24      2     34       C  
ATOM    141  C   VAL A  16      17.321  17.897  21.743  1.00  5.05           C  
ANISOU  141  C   VAL A  16      711    653    553    -24     28     26       C  
ATOM    142  O   VAL A  16      17.272  18.848  20.971  1.00  5.30           O  
ANISOU  142  O   VAL A  16      737    648    627    -77     74    113       O  
ATOM    143  CB  VAL A  16      17.614  15.665  20.495  1.00  7.34           C  
ANISOU  143  CB  VAL A  16      865    933    991    104    -77    -50       C  
ATOM    144  CG1 VAL A  16      18.611  14.559  20.133  1.00  9.85           C  
ANISOU  144  CG1 VAL A  16     1234   1160   1349     70     -9   -260       C  
ATOM    145  CG2 VAL A  16      16.422  15.114  21.060  1.00  7.97           C  
ANISOU  145  CG2 VAL A  16     1032   1162    833     24    -38    108       C  
ATOM    146  N   CYS A  17      16.618  17.857  22.864  1.00  4.38           N  
ANISOU  146  N   CYS A  17      553    608    501      3    -38    111       N  
ATOM    147  CA  CYS A  17      15.766  18.964  23.214  1.00  4.28           C  
ANISOU  147  CA  CYS A  17      434    630    562     -1      7     80       C  
ATOM    148  C   CYS A  17      16.552  20.182  23.686  1.00  4.33           C  
ANISOU  148  C   CYS A  17      521    534    588      4     41     56       C  
ATOM    149  O   CYS A  17      16.112  21.317  23.463  1.00  5.10           O  
ANISOU  149  O   CYS A  17      622    566    748     -7      7     76       O  
ATOM    150  CB  CYS A  17      14.705  18.526  24.212  1.00  5.17           C  
ANISOU  150  CB  CYS A  17      593    643    727     -8     67     59       C  
ATOM    151  SG  CYS A  17      13.487  17.403  23.483  1.00  5.76           S  
ANISOU  151  SG  CYS A  17      641    796    748    -43    -53     26       S  
ATOM    152  N   LYS A  18      17.702  19.988  24.306  1.00  4.78           N  
ANISOU  152  N   LYS A  18      693    490    629     49    -67     38       N  
ATOM    153  CA  LYS A  18      18.547  21.112  24.646  1.00  5.28           C  
ANISOU  153  CA  LYS A  18      687    654    664    -11    -10    -37       C  
ATOM    154  C   LYS A  18      18.985  21.831  23.360  1.00  5.42           C  
ANISOU  154  C   LYS A  18      687    612    760     46    -45    -25       C  
ATOM    155  O   LYS A  18      18.941  23.047  23.280  1.00  5.77           O  
ANISOU  155  O   LYS A  18      730    650    810    -18    -84    -18       O  
ATOM    156  CB  LYS A  18      19.730  20.668  25.496  1.00  6.05           C  
ANISOU  156  CB  LYS A  18      816    739    741    -34   -131     59       C  
ATOM    157  CG  LYS A  18      20.604  21.832  25.904  1.00  7.52           C  
ANISOU  157  CG  LYS A  18      783   1084    989    -78     46     -6       C  
ATOM    158  CD  LYS A  18      21.736  21.441  26.825  1.00 11.14           C  
ANISOU  158  CD  LYS A  18     1376   1551   1303   -173   -240    -63       C  
ATOM    159  CE  LYS A  18      22.627  22.636  27.169  1.00 12.93           C  
ANISOU  159  CE  LYS A  18     1501   1633   1779   -117   -206    -62       C  
ATOM    160  NZ  LYS A  18      23.348  23.131  25.981  1.00 17.32           N  
ANISOU  160  NZ  LYS A  18     2526   2158   1897   -107    -34    -34       N  
ATOM    161  N   THR A  19      19.419  21.065  22.355  1.00  5.69           N  
ANISOU  161  N   THR A  19      708    710    742     76      8     26       N  
ATOM    162  CA ATHR A  19      19.858  21.594  21.073  0.50  6.33           C  
ANISOU  162  CA ATHR A  19      796    810    797     -1     80      1       C  
ATOM    163  CA BTHR A  19      19.867  21.736  21.139  0.50  6.01           C  
ANISOU  163  CA BTHR A  19      692    750    839     18     73    -19       C  
ATOM    164  C   THR A  19      18.714  22.273  20.301  1.00  5.83           C  
ANISOU  164  C   THR A  19      700    716    797     54    139     39       C  
ATOM    165  O   THR A  19      18.901  23.260  19.617  1.00  6.08           O  
ANISOU  165  O   THR A  19      780    590    939    -18    128     57       O  
ATOM    166  CB ATHR A  19      20.486  20.417  20.270  0.50  6.92           C  
ANISOU  166  CB ATHR A  19      867    872    890    -15    135    -41       C  
ATOM    167  CB BTHR A  19      20.878  20.922  20.314  0.50  6.19           C  
ANISOU  167  CB BTHR A  19      575    823    951     82    106     41       C  
ATOM    168  OG1ATHR A  19      21.555  19.847  21.041  0.50  9.31           O  
ANISOU  168  OG1ATHR A  19     1102   1130   1306    -85    180    238       O  
ATOM    169  OG1BTHR A  19      20.341  19.640  20.007  0.50  7.06           O  
ANISOU  169  OG1BTHR A  19      780    734   1169    101    296    -95       O  
ATOM    170  CG2ATHR A  19      21.003  20.863  18.955  0.50  8.32           C  
ANISOU  170  CG2ATHR A  19     1347   1042    772     39     65     34       C  
ATOM    171  CG2BTHR A  19      22.173  20.759  21.087  0.50  8.56           C  
ANISOU  171  CG2BTHR A  19      666   1083   1503    146   -180   -182       C  
ATOM    172  N   GLU A  20      17.520  21.698  20.374  1.00  4.60           N  
ANISOU  172  N   GLU A  20      658    510    578    -73     54     34       N  
ATOM    173  CA  GLU A  20      16.381  22.254  19.669  1.00  4.66           C  
ANISOU  173  CA  GLU A  20      716    589    463    -68     51      5       C  
ATOM    174  C   GLU A  20      15.975  23.607  20.238  1.00  4.09           C  
ANISOU  174  C   GLU A  20      534    501    520   -115      2     58       C  
ATOM    175  O   GLU A  20      15.474  24.450  19.487  1.00  5.00           O  
ANISOU  175  O   GLU A  20      701    670    527     20    -12     91       O  
ATOM    176  CB  GLU A  20      15.223  21.266  19.714  1.00  5.29           C  
ANISOU  176  CB  GLU A  20      809    579    622    -68    -30    -67       C  
ATOM    177  CG  GLU A  20      13.994  21.778  18.986  1.00  6.85           C  
ANISOU  177  CG  GLU A  20      999    845    758    -37    -91    -92       C  
ATOM    178  CD  GLU A  20      12.833  20.822  18.981  1.00  7.01           C  
ANISOU  178  CD  GLU A  20      909    839    915     73    -85   -131       C  
ATOM    179  OE1 GLU A  20      13.011  19.654  18.654  1.00  8.75           O  
ANISOU  179  OE1 GLU A  20     1097    935   1290     89    -79   -325       O  
ATOM    180  OE2 GLU A  20      11.707  21.244  19.270  1.00 12.23           O  
ANISOU  180  OE2 GLU A  20     1132   1071   2442   -116    342   -438       O  
ATOM    181  N   THR A  21      16.107  23.772  21.549  1.00  4.17           N  
ANISOU  181  N   THR A  21      497    602    483     43     16    102       N  
ATOM    182  CA  THR A  21      15.532  24.923  22.243  1.00  4.81           C  
ANISOU  182  CA  THR A  21      674    624    527     53     86     81       C  
ATOM    183  C   THR A  21      16.564  25.978  22.594  1.00  5.09           C  
ANISOU  183  C   THR A  21      764    585    584     83     93    128       C  
ATOM    184  O   THR A  21      16.193  27.120  22.831  1.00  6.34           O  
ANISOU  184  O   THR A  21      963    711    736    142    -74     23       O  
ATOM    185  CB  THR A  21      14.812  24.498  23.528  1.00  5.43           C  
ANISOU  185  CB  THR A  21      861    686    515    122     80     47       C  
ATOM    186  OG1 THR A  21      15.770  23.935  24.463  1.00  5.91           O  
ANISOU  186  OG1 THR A  21      890    849    505     57     -1     23       O  
ATOM    187  CG2 THR A  21      13.730  23.492  23.219  1.00  6.63           C  
ANISOU  187  CG2 THR A  21      666    952    899    110     85    265       C  
ATOM    188  N   GLY A  22      17.848  25.611  22.663  1.00  5.05           N  
ANISOU  188  N   GLY A  22      682    641    596     -5    -15    -10       N  
ATOM    189  CA  GLY A  22      18.847  26.543  23.151  1.00  5.56           C  
ANISOU  189  CA  GLY A  22      737    722    651    -80      9     83       C  
ATOM    190  C   GLY A  22      18.781  26.845  24.632  1.00  5.69           C  
ANISOU  190  C   GLY A  22      656    806    698    -55     22     11       C  
ATOM    191  O   GLY A  22      19.377  27.832  25.068  1.00  6.85           O  
ANISOU  191  O   GLY A  22      783    922    897   -248    -57     -8       O  
ATOM    192  N   ILE A  23      18.076  26.039  25.412  1.00  5.64           N  
ANISOU  192  N   ILE A  23      821    746    574    -54    -14     18       N  
ATOM    193  CA  ILE A  23      18.004  26.252  26.841  1.00  5.91           C  
ANISOU  193  CA  ILE A  23      777    824    641    -20    -45     39       C  
ATOM    194  C   ILE A  23      19.403  26.193  27.454  1.00  6.01           C  
ANISOU  194  C   ILE A  23      773    782    728     -6     19    -23       C  
ATOM    195  O   ILE A  23      20.222  25.352  27.079  1.00  6.93           O  
ANISOU  195  O   ILE A  23      849    952    832     64     -7    -52       O  
ATOM    196  CB  ILE A  23      17.038  25.230  27.483  1.00  5.72           C  
ANISOU  196  CB  ILE A  23      687    815    667    -31    -89     38       C  
ATOM    197  CG1 ILE A  23      16.739  25.567  28.942  1.00  5.45           C  
ANISOU  197  CG1 ILE A  23      602    843    625    -56     81   -109       C  
ATOM    198  CG2 ILE A  23      17.536  23.803  27.363  1.00  6.69           C  
ANISOU  198  CG2 ILE A  23     1021    866    654      0      5     11       C  
ATOM    199  CD1 ILE A  23      15.645  24.729  29.541  1.00  7.93           C  
ANISOU  199  CD1 ILE A  23      778   1214   1021   -250    -69     45       C  
ATOM    200  N   ASP A  24      19.639  27.029  28.460  1.00  5.94           N  
ANISOU  200  N   ASP A  24      683    830    741    -48    -74    -41       N  
ATOM    201  CA  ASP A  24      20.889  26.948  29.241  1.00  7.01           C  
ANISOU  201  CA  ASP A  24      858    976    827    -66   -118    -34       C  
ATOM    202  C   ASP A  24      20.976  25.582  29.908  1.00  6.37           C  
ANISOU  202  C   ASP A  24      775    852    792     13    -84   -148       C  
ATOM    203  O   ASP A  24      19.978  25.053  30.408  1.00  6.31           O  
ANISOU  203  O   ASP A  24      727    947    720    -82   -104    -48       O  
ATOM    204  CB  ASP A  24      20.885  27.968  30.403  1.00  8.61           C  
ANISOU  204  CB  ASP A  24     1151   1140    977   -103   -288    -50       C  
ATOM    205  CG  ASP A  24      21.037  29.396  29.981  1.00 11.10           C  
ANISOU  205  CG  ASP A  24     1450   1450   1315     -1   -267   -145       C  
ATOM    206  OD1 ASP A  24      21.407  29.674  28.827  1.00 13.76           O  
ANISOU  206  OD1 ASP A  24     1931   1397   1899   -399   -137    259       O  
ATOM    207  OD2 ASP A  24      20.784  30.243  30.880  1.00 13.45           O  
ANISOU  207  OD2 ASP A  24     2150   1502   1459     96   -453   -261       O  
ATOM    208  N   GLN A  25      22.192  25.045  30.036  1.00  7.03           N  
ANISOU  208  N   GLN A  25      794   1050    824     19    -15   -157       N  
ATOM    209  CA  GLN A  25      22.378  23.791  30.748  1.00  7.52           C  
ANISOU  209  CA  GLN A  25      853   1040    962    134    -65   -154       C  
ATOM    210  C   GLN A  25      21.859  23.873  32.175  1.00  6.76           C  
ANISOU  210  C   GLN A  25      764    904    897    101    -84   -114       C  
ATOM    211  O   GLN A  25      21.283  22.917  32.662  1.00  6.96           O  
ANISOU  211  O   GLN A  25      817    876    947    157   -122     -8       O  
ATOM    212  CB  GLN A  25      23.840  23.343  30.794  1.00  8.71           C  
ANISOU  212  CB  GLN A  25      990   1216   1101    212     -9   -229       C  
ATOM    213  CG  GLN A  25      24.032  21.977  31.564  1.00 11.77           C  
ANISOU  213  CG  GLN A  25     1423   1699   1348    196    125   -101       C  
ATOM    214  CD  GLN A  25      23.509  20.787  30.771  1.00 14.34           C  
ANISOU  214  CD  GLN A  25     1802   1904   1741    190    181   -218       C  
ATOM    215  OE1 GLN A  25      22.558  20.091  31.162  1.00 15.39           O  
ANISOU  215  OE1 GLN A  25     2023   2070   1753    154    236   -260       O  
ATOM    216  NE2 GLN A  25      24.117  20.564  29.625  1.00 16.42           N  
ANISOU  216  NE2 GLN A  25     2364   2355   1520    117    216   -553       N  
ATOM    217  N   GLN A  26      22.050  25.007  32.851  1.00  6.19           N  
ANISOU  217  N   GLN A  26      719    813    820     56    -87    -43       N  
ATOM    218  CA  GLN A  26      21.593  25.132  34.221  1.00  6.60           C  
ANISOU  218  CA  GLN A  26      797    914    796    -52   -139     -7       C  
ATOM    219  C   GLN A  26      20.076  24.921  34.304  1.00  6.07           C  
ANISOU  219  C   GLN A  26      763    765    778    -97    -59    -31       C  
ATOM    220  O   GLN A  26      19.572  24.256  35.218  1.00  6.38           O  
ANISOU  220  O   GLN A  26      813    868    743     -6   -117    -23       O  
ATOM    221  CB  GLN A  26      21.923  26.517  34.745  1.00  8.46           C  
ANISOU  221  CB  GLN A  26     1044   1139   1030    -31    -31   -218       C  
ATOM    222  CG  GLN A  26      21.361  26.789  36.118  1.00 11.47           C  
ANISOU  222  CG  GLN A  26     1347   1760   1249    -81     20   -385       C  
ATOM    223  CD  GLN A  26      21.979  25.921  37.158  1.00 15.67           C  
ANISOU  223  CD  GLN A  26     1899   2383   1672     51    -26   -192       C  
ATOM    224  OE1 GLN A  26      23.201  25.907  37.314  1.00 19.09           O  
ANISOU  224  OE1 GLN A  26     1957   3276   2019    103   -287     43       O  
ATOM    225  NE2 GLN A  26      21.155  25.188  37.895  1.00 18.42           N  
ANISOU  225  NE2 GLN A  26     2209   2924   1865   -202   -391    133       N  
ATOM    226  N   LYS A  27      19.343  25.539  33.376  1.00  5.48           N  
ANISOU  226  N   LYS A  27      695    680    707    -27    -32     28       N  
ATOM    227  CA  LYS A  27      17.893  25.430  33.405  1.00  5.24           C  
ANISOU  227  CA  LYS A  27      680    631    679    -35     34     57       C  
ATOM    228  C   LYS A  27      17.432  24.039  33.003  1.00  5.42           C  
ANISOU  228  C   LYS A  27      734    650    675     17     -8     28       C  
ATOM    229  O   LYS A  27      16.447  23.525  33.569  1.00  6.27           O  
ANISOU  229  O   LYS A  27      769    768    844     50     41     93       O  
ATOM    230  CB  LYS A  27      17.255  26.516  32.550  1.00  5.66           C  
ANISOU  230  CB  LYS A  27      753    677    720    -40    -12      8       C  
ATOM    231  CG  LYS A  27      17.516  27.895  33.071  1.00  6.92           C  
ANISOU  231  CG  LYS A  27      818    772   1039    -17     20    -41       C  
ATOM    232  CD  LYS A  27      16.872  28.971  32.217  1.00  7.82           C  
ANISOU  232  CD  LYS A  27     1016    862   1092     49     27    -47       C  
ATOM    233  CE  LYS A  27      17.137  30.357  32.809  1.00  9.24           C  
ANISOU  233  CE  LYS A  27     1122    837   1551    186     75    -92       C  
ATOM    234  NZ  LYS A  27      16.551  31.432  31.994  1.00 11.36           N  
ANISOU  234  NZ  LYS A  27     1578    967   1772    166   -189     31       N  
ATOM    235  N   ALA A  28      18.095  23.412  32.030  1.00  5.41           N  
ANISOU  235  N   ALA A  28      696    713    643    -34     37    -20       N  
ATOM    236  CA  ALA A  28      17.795  22.016  31.732  1.00  5.57           C  
ANISOU  236  CA  ALA A  28      747    661    707    -45    -85      3       C  
ATOM    237  C   ALA A  28      18.013  21.151  32.957  1.00  5.57           C  
ANISOU  237  C   ALA A  28      675    670    770     -2    -73    -26       C  
ATOM    238  O   ALA A  28      17.188  20.300  33.252  1.00  5.62           O  
ANISOU  238  O   ALA A  28      729    677    729     35    -24     14       O  
ATOM    239  CB  ALA A  28      18.634  21.530  30.555  1.00  6.73           C  
ANISOU  239  CB  ALA A  28      841    886    828     27     25    -78       C  
ATOM    240  N   ASN A  29      19.120  21.374  33.658  1.00  5.95           N  
ANISOU  240  N   ASN A  29      692    714    855     26   -121     32       N  
ATOM    241  CA  ASN A  29      19.383  20.613  34.892  1.00  6.22           C  
ANISOU  241  CA  ASN A  29      789    723    849    -27    -84     93       C  
ATOM    242  C   ASN A  29      18.300  20.821  35.929  1.00  6.40           C  
ANISOU  242  C   ASN A  29      905    782    743     -1    -93    -27       C  
ATOM    243  O   ASN A  29      17.916  19.881  36.607  1.00  6.31           O  
ANISOU  243  O   ASN A  29      865    803    729    -17    -96     46       O  
ATOM    244  CB  ASN A  29      20.698  20.997  35.551  1.00  7.45           C  
ANISOU  244  CB  ASN A  29      945    923    960    -37   -234    126       C  
ATOM    245  CG  ASN A  29      21.879  20.595  34.810  1.00  9.32           C  
ANISOU  245  CG  ASN A  29     1131   1348   1062   -101   -197    251       C  
ATOM    246  OD1 ASN A  29      22.987  21.073  35.143  1.00 13.44           O  
ANISOU  246  OD1 ASN A  29     1115   1807   2182   -270   -153    232       O  
ATOM    247  ND2 ASN A  29      21.741  19.722  33.866  1.00  8.02           N  
ANISOU  247  ND2 ASN A  29      617   1208   1221    -54    271    254       N  
ATOM    248  N   ASP A  30      17.823  22.051  36.064  1.00  6.45           N  
ANISOU  248  N   ASP A  30      951    681    818      7    -91     49       N  
ATOM    249  CA  ASP A  30      16.742  22.332  36.989  1.00  6.72           C  
ANISOU  249  CA  ASP A  30     1006    697    849     -6    -56     19       C  
ATOM    250  C   ASP A  30      15.511  21.496  36.633  1.00  5.97           C  
ANISOU  250  C   ASP A  30      886    652    730    130     -4    -41       C  
ATOM    251  O   ASP A  30      14.895  20.888  37.502  1.00  6.40           O  
ANISOU  251  O   ASP A  30      888    774    766     82    -11     45       O  
ATOM    252  CB  ASP A  30      16.368  23.820  36.967  1.00  7.48           C  
ANISOU  252  CB  ASP A  30     1066    757   1017    -44     21   -107       C  
ATOM    253  CG  ASP A  30      17.426  24.730  37.536  1.00 11.45           C  
ANISOU  253  CG  ASP A  30     1553   1253   1542   -145     70   -201       C  
ATOM    254  OD1 ASP A  30      18.288  24.264  38.305  1.00 14.06           O  
ANISOU  254  OD1 ASP A  30     1832   1599   1908   -314   -501   -663       O  
ATOM    255  OD2 ASP A  30      17.403  25.930  37.182  1.00 13.52           O  
ANISOU  255  OD2 ASP A  30     1778   1226   2133    -92     92   -428       O  
ATOM    256  N   VAL A  31      15.137  21.490  35.356  1.00  4.97           N  
ANISOU  256  N   VAL A  31      679    641    567     97    -99     94       N  
ATOM    257  CA  VAL A  31      13.999  20.695  34.905  1.00  5.06           C  
ANISOU  257  CA  VAL A  31      679    630    614     55    -60     58       C  
ATOM    258  C   VAL A  31      14.236  19.216  35.203  1.00  5.13           C  
ANISOU  258  C   VAL A  31      633    651    662     29    -69     71       C  
ATOM    259  O   VAL A  31      13.362  18.522  35.733  1.00  5.30           O  
ANISOU  259  O   VAL A  31      635    774    604     32   -122    160       O  
ATOM    260  CB  VAL A  31      13.713  20.912  33.414  1.00  4.74           C  
ANISOU  260  CB  VAL A  31      576    641    584    110    -57     35       C  
ATOM    261  CG1 VAL A  31      12.696  19.915  32.910  1.00  6.41           C  
ANISOU  261  CG1 VAL A  31      753   1013    668    -78    -99     38       C  
ATOM    262  CG2 VAL A  31      13.276  22.336  33.134  1.00  5.67           C  
ANISOU  262  CG2 VAL A  31      632    752    771    123     13    180       C  
ATOM    263  N   ILE A  32      15.422  18.722  34.864  1.00  4.75           N  
ANISOU  263  N   ILE A  32      678    487    637     41    -93     83       N  
ATOM    264  CA  ILE A  32      15.757  17.330  35.103  1.00  4.93           C  
ANISOU  264  CA  ILE A  32      697    526    648     14    -46     27       C  
ATOM    265  C   ILE A  32      15.643  16.957  36.578  1.00  4.96           C  
ANISOU  265  C   ILE A  32      639    544    700    -20   -125     77       C  
ATOM    266  O   ILE A  32      15.158  15.893  36.908  1.00  5.26           O  
ANISOU  266  O   ILE A  32      705    560    731     -5    -27    112       O  
ATOM    267  CB  ILE A  32      17.150  17.034  34.486  1.00  4.44           C  
ANISOU  267  CB  ILE A  32      615    481    588    -86    -69     50       C  
ATOM    268  CG1 ILE A  32      17.091  17.125  32.963  1.00  4.94           C  
ANISOU  268  CG1 ILE A  32      705    623    548    -82    -69   -148       C  
ATOM    269  CG2 ILE A  32      17.680  15.684  34.893  1.00  6.37           C  
ANISOU  269  CG2 ILE A  32      836    727    855    136     80    200       C  
ATOM    270  CD1 ILE A  32      18.454  17.208  32.289  1.00  6.34           C  
ANISOU  270  CD1 ILE A  32      869    780    760    -14    180    -48       C  
ATOM    271  N   GLU A  33      16.041  17.859  37.454  1.00  5.32           N  
ANISOU  271  N   GLU A  33      800    575    643     27   -119     56       N  
ATOM    272  CA  GLU A  33      15.939  17.650  38.901  1.00  6.18           C  
ANISOU  272  CA  GLU A  33      925    800    621    -23   -177     68       C  
ATOM    273  C   GLU A  33      14.559  17.908  39.477  1.00  6.53           C  
ANISOU  273  C   GLU A  33      999    791    688     22   -112     90       C  
ATOM    274  O   GLU A  33      14.340  17.691  40.660  1.00  7.46           O  
ANISOU  274  O   GLU A  33     1087    977    768    -44     19    111       O  
ATOM    275  CB  GLU A  33      16.942  18.541  39.623  1.00  8.03           C  
ANISOU  275  CB  GLU A  33     1161   1238    651      8   -217    147       C  
ATOM    276  CG  GLU A  33      18.325  18.073  39.349  1.00 11.10           C  
ANISOU  276  CG  GLU A  33     1404   1520   1293     56   -331     29       C  
ATOM    277  CD  GLU A  33      19.423  18.982  39.833  1.00 14.59           C  
ANISOU  277  CD  GLU A  33     1761   2045   1735   -154   -437     78       C  
ATOM    278  OE1 GLU A  33      19.116  20.003  40.493  1.00 14.98           O  
ANISOU  278  OE1 GLU A  33     1995   1934   1761   -393   -661    -60       O  
ATOM    279  OE2 GLU A  33      20.619  18.640  39.558  1.00 16.47           O  
ANISOU  279  OE2 GLU A  33     1769   2363   2124   -190   -227    217       O  
ATOM    280  N   GLY A  34      13.613  18.328  38.650  1.00  6.07           N  
ANISOU  280  N   GLY A  34      844    744    715     67      4    136       N  
ATOM    281  CA  GLY A  34      12.216  18.501  39.052  1.00  6.47           C  
ANISOU  281  CA  GLY A  34      869    766    823     15     16    116       C  
ATOM    282  C   GLY A  34      11.857  19.887  39.562  1.00  7.70           C  
ANISOU  282  C   GLY A  34     1123    862    937     73     80    164       C  
ATOM    283  O   GLY A  34      10.822  20.049  40.188  1.00  9.61           O  
ANISOU  283  O   GLY A  34     1278   1063   1308    213    305     86       O  
ATOM    284  N   ASN A  35      12.700  20.886  39.319  1.00  7.24           N  
ANISOU  284  N   ASN A  35      987    816    948     77    -11     82       N  
ATOM    285  CA  ASN A  35      12.411  22.266  39.704  1.00  8.07           C  
ANISOU  285  CA  ASN A  35     1185    860   1021     26    -43    110       C  
ATOM    286  C   ASN A  35      12.146  23.051  38.452  1.00  8.18           C  
ANISOU  286  C   ASN A  35     1125    982    999     19    -47    165       C  
ATOM    287  O   ASN A  35      13.074  23.540  37.785  1.00  9.09           O  
ANISOU  287  O   ASN A  35     1053   1080   1318     38    -98    449       O  
ATOM    288  CB  ASN A  35      13.566  22.794  40.495  1.00  8.67           C  
ANISOU  288  CB  ASN A  35     1240   1062    992     78    -91     94       C  
ATOM    289  CG  ASN A  35      13.737  22.007  41.748  1.00 10.33           C  
ANISOU  289  CG  ASN A  35     1527   1196   1199    203   -157    169       C  
ATOM    290  OD1 ASN A  35      12.788  21.883  42.519  1.00 12.30           O  
ANISOU  290  OD1 ASN A  35     1721   1554   1398    305   -159    461       O  
ATOM    291  ND2 ASN A  35      14.907  21.388  41.929  1.00 12.62           N  
ANISOU  291  ND2 ASN A  35     1628   1703   1462    445   -162    128       N  
ATOM    292  N   ILE A  36      10.863  23.123  38.116  1.00  8.73           N  
ANISOU  292  N   ILE A  36     1019   1198   1098     50      7    146       N  
ATOM    293  CA AILE A  36      10.423  23.699  36.845  0.50  8.84           C  
ANISOU  293  CA AILE A  36     1061   1168   1128     15    -14    153       C  
ATOM    294  CA BILE A  36      10.444  23.677  36.837  0.50  9.04           C  
ANISOU  294  CA BILE A  36     1099   1196   1137     47     -7    150       C  
ATOM    295  C   ILE A  36      10.001  25.139  37.039  1.00  8.97           C  
ANISOU  295  C   ILE A  36     1070   1189   1149     21    -24    117       C  
ATOM    296  O   ILE A  36       9.077  25.416  37.784  1.00 10.32           O  
ANISOU  296  O   ILE A  36     1232   1325   1364     58     61     70       O  
ATOM    297  CB AILE A  36       9.190  22.970  36.244  0.50  8.40           C  
ANISOU  297  CB AILE A  36      914   1072   1205     41     -2    124       C  
ATOM    298  CB BILE A  36       9.305  22.820  36.159  0.50  8.72           C  
ANISOU  298  CB BILE A  36      992   1132   1189     68     11    107       C  
ATOM    299  CG1AILE A  36       9.330  21.463  36.379  0.50  7.55           C  
ANISOU  299  CG1AILE A  36      868    945   1056    -90     31    147       C  
ATOM    300  CG1BILE A  36       9.832  21.460  35.634  0.50  9.14           C  
ANISOU  300  CG1BILE A  36     1124   1081   1266     -9     -7    121       C  
ATOM    301  CG2AILE A  36       8.993  23.381  34.786  0.50  8.22           C  
ANISOU  301  CG2AILE A  36      921   1036   1166   -117    -27    126       C  
ATOM    302  CG2BILE A  36       8.689  23.595  34.999  0.50  8.26           C  
ANISOU  302  CG2BILE A  36      945   1127   1066    144    100    114       C  
ATOM    303  CD1AILE A  36      10.673  20.956  35.999  0.50  9.10           C  
ANISOU  303  CD1AILE A  36      965   1218   1274    115    142    189       C  
ATOM    304  CD1BILE A  36      10.089  20.376  36.684  0.50  7.82           C  
ANISOU  304  CD1BILE A  36      984    774   1211   -102    121     17       C  
ATOM    305  N   ASP A  37      10.686  26.064  36.374  1.00  8.63           N  
ANISOU  305  N   ASP A  37     1059   1015   1203     64   -102    119       N  
ATOM    306  CA  ASP A  37      10.286  27.467  36.352  1.00  9.12           C  
ANISOU  306  CA  ASP A  37     1201   1037   1227     72   -110     43       C  
ATOM    307  C   ASP A  37       9.286  27.591  35.209  1.00  8.39           C  
ANISOU  307  C   ASP A  37     1107    960   1120    126   -119     48       C  
ATOM    308  O   ASP A  37       9.660  27.775  34.048  1.00  7.87           O  
ANISOU  308  O   ASP A  37      791    950   1247    189    -67    134       O  
ATOM    309  CB  ASP A  37      11.516  28.338  36.123  1.00 10.55           C  
ANISOU  309  CB  ASP A  37     1431   1226   1350    -31   -122     71       C  
ATOM    310  CG  ASP A  37      11.196  29.820  36.076  1.00 14.73           C  
ANISOU  310  CG  ASP A  37     2008   1499   2089    -84    -49    -18       C  
ATOM    311  OD1 ASP A  37      12.155  30.606  35.940  1.00 18.70           O  
ANISOU  311  OD1 ASP A  37     2755   1612   2735   -491   -165    158       O  
ATOM    312  OD2 ASP A  37      10.003  30.190  36.134  1.00 18.38           O  
ANISOU  312  OD2 ASP A  37     2582   1701   2697    139    134    -12       O  
ATOM    313  N   VAL A  38       8.008  27.399  35.544  1.00  8.02           N  
ANISOU  313  N   VAL A  38     1060    830   1157     67    -96     17       N  
ATOM    314  CA  VAL A  38       6.999  27.135  34.530  1.00  8.42           C  
ANISOU  314  CA  VAL A  38     1043   1001   1155     74    -12    123       C  
ATOM    315  C   VAL A  38       6.805  28.319  33.572  1.00  7.18           C  
ANISOU  315  C   VAL A  38      881    767   1079    118     59    118       C  
ATOM    316  O   VAL A  38       6.408  28.092  32.442  1.00  7.87           O  
ANISOU  316  O   VAL A  38     1041    896   1053     30      0    169       O  
ATOM    317  CB  VAL A  38       5.630  26.715  35.150  1.00  8.87           C  
ANISOU  317  CB  VAL A  38     1028   1055   1287    130     37    138       C  
ATOM    318  CG1 VAL A  38       5.751  25.383  35.906  1.00  9.75           C  
ANISOU  318  CG1 VAL A  38     1140   1251   1312    136    -65    251       C  
ATOM    319  CG2 VAL A  38       5.040  27.820  36.045  1.00 10.56           C  
ANISOU  319  CG2 VAL A  38     1163   1351   1496    115     42    -89       C  
ATOM    320  N   GLU A  39       7.149  29.539  33.996  1.00  8.18           N  
ANISOU  320  N   GLU A  39      992    994   1121     28    -26    114       N  
ATOM    321  CA  GLU A  39       6.964  30.746  33.173  1.00  8.51           C  
ANISOU  321  CA  GLU A  39     1071    879   1283    171     24     89       C  
ATOM    322  C   GLU A  39       8.107  31.033  32.206  1.00  9.11           C  
ANISOU  322  C   GLU A  39     1059   1066   1334    120     19    114       C  
ATOM    323  O   GLU A  39       7.994  31.923  31.378  1.00 10.15           O  
ANISOU  323  O   GLU A  39     1223   1060   1571     54     86    228       O  
ATOM    324  CB  GLU A  39       6.740  31.983  34.058  1.00  9.70           C  
ANISOU  324  CB  GLU A  39     1291   1025   1368    194     30    -54       C  
ATOM    325  CG  GLU A  39       5.542  31.891  34.996  1.00 12.49           C  
ANISOU  325  CG  GLU A  39     1681   1286   1778    252    124    -24       C  
ATOM    326  CD  GLU A  39       4.200  31.940  34.290  1.00 16.98           C  
ANISOU  326  CD  GLU A  39     2196   2063   2192      6    -48   -185       C  
ATOM    327  OE1 GLU A  39       4.110  32.464  33.156  1.00 19.30           O  
ANISOU  327  OE1 GLU A  39     2210   2591   2533    375   -202    213       O  
ATOM    328  OE2 GLU A  39       3.210  31.475  34.899  1.00 19.79           O  
ANISOU  328  OE2 GLU A  39     2346   2607   2565     96    336   -290       O  
ATOM    329  N   ASP A  40       9.204  30.295  32.309  1.00  8.14           N  
ANISOU  329  N   ASP A  40      979    870   1243     69    -49     88       N  
ATOM    330  CA  ASP A  40      10.396  30.583  31.521  1.00  8.35           C  
ANISOU  330  CA  ASP A  40     1008    947   1216     21    -59     86       C  
ATOM    331  C   ASP A  40      10.183  30.003  30.121  1.00  8.22           C  
ANISOU  331  C   ASP A  40      987    961   1174     77    -34     81       C  
ATOM    332  O   ASP A  40       9.848  28.819  29.984  1.00  8.07           O  
ANISOU  332  O   ASP A  40     1010    831   1224     46    -92     82       O  
ATOM    333  CB  ASP A  40      11.602  29.980  32.246  1.00  8.65           C  
ANISOU  333  CB  ASP A  40     1060   1001   1224      7   -112    -26       C  
ATOM    334  CG  ASP A  40      12.920  30.190  31.527  1.00  9.54           C  
ANISOU  334  CG  ASP A  40     1099    984   1538   -143     48    -59       C  
ATOM    335  OD1 ASP A  40      13.815  30.895  32.087  1.00 13.08           O  
ANISOU  335  OD1 ASP A  40     1321   1679   1970   -376    133   -325       O  
ATOM    336  OD2 ASP A  40      13.117  29.603  30.445  1.00  9.61           O  
ANISOU  336  OD2 ASP A  40     1002   1293   1354   -153    -76    131       O  
ATOM    337  N   LYS A  41      10.364  30.825  29.092  1.00  8.41           N  
ANISOU  337  N   LYS A  41     1101    810   1281     56     -3     57       N  
ATOM    338  CA ALYS A  41      10.064  30.432  27.710  0.50  8.27           C  
ANISOU  338  CA ALYS A  41     1017    889   1234     86    -52    100       C  
ATOM    339  CA BLYS A  41      10.039  30.427  27.739  0.50  8.97           C  
ANISOU  339  CA BLYS A  41     1121    981   1306     75    -46     75       C  
ATOM    340  C   LYS A  41      10.854  29.210  27.260  1.00  7.71           C  
ANISOU  340  C   LYS A  41      955    816   1156     53    -32    137       C  
ATOM    341  O   LYS A  41      10.279  28.282  26.698  1.00  7.53           O  
ANISOU  341  O   LYS A  41      839    957   1064   -120    -29     58       O  
ATOM    342  CB ALYS A  41      10.301  31.594  26.721  0.50  9.00           C  
ANISOU  342  CB ALYS A  41     1134    996   1288    101    -78    141       C  
ATOM    343  CB BLYS A  41      10.196  31.615  26.778  0.50 10.13           C  
ANISOU  343  CB BLYS A  41     1308   1153   1388     72    -76    121       C  
ATOM    344  CG ALYS A  41      10.070  31.234  25.220  0.50  9.84           C  
ANISOU  344  CG ALYS A  41     1252   1116   1367    139    -41    172       C  
ATOM    345  CG BLYS A  41       9.343  32.862  27.110  0.50 14.57           C  
ANISOU  345  CG BLYS A  41     1907   1659   1967    139    -13    -60       C  
ATOM    346  CD ALYS A  41      10.437  32.378  24.274  0.50 13.42           C  
ANISOU  346  CD ALYS A  41     1768   1644   1685    -25      6    346       C  
ATOM    347  CD BLYS A  41       7.854  32.556  27.201  0.50 17.56           C  
ANISOU  347  CD BLYS A  41     2152   2137   2381     88    -19    -55       C  
ATOM    348  CE ALYS A  41      10.609  31.895  22.823  0.50 16.00           C  
ANISOU  348  CE ALYS A  41     2088   2070   1919    -72     44    202       C  
ATOM    349  CE BLYS A  41       7.433  32.361  28.635  0.50 18.98           C  
ANISOU  349  CE BLYS A  41     2326   2414   2469     57     21    -40       C  
ATOM    350  NZ ALYS A  41       9.335  31.775  22.066  0.50 17.14           N  
ANISOU  350  NZ ALYS A  41     2252   2226   2033   -176      7    282       N  
ATOM    351  NZ BLYS A  41       6.011  32.745  28.901  0.50 20.67           N  
ANISOU  351  NZ BLYS A  41     2575   2574   2705    223     -2   -111       N  
ATOM    352  N   LYS A  42      12.182  29.211  27.449  1.00  7.28           N  
ANISOU  352  N   LYS A  42      822    836   1107   -161    -23     19       N  
ATOM    353  CA  LYS A  42      12.963  28.052  27.001  1.00  6.63           C  
ANISOU  353  CA  LYS A  42      791    823    904    -59    -50     65       C  
ATOM    354  C   LYS A  42      12.670  26.819  27.865  1.00  5.85           C  
ANISOU  354  C   LYS A  42      707    721    794     -6    -24     21       C  
ATOM    355  O   LYS A  42      12.747  25.730  27.364  1.00  6.55           O  
ANISOU  355  O   LYS A  42      809    755    923   -127    -97     23       O  
ATOM    356  CB  LYS A  42      14.450  28.375  26.796  1.00  7.23           C  
ANISOU  356  CB  LYS A  42      936    820    989    -64     68     54       C  
ATOM    357  CG  LYS A  42      14.688  29.186  25.489  1.00  8.16           C  
ANISOU  357  CG  LYS A  42     1140    972    989     17     96     -1       C  
ATOM    358  CD  LYS A  42      16.127  29.564  25.295  1.00  5.18           C  
ANISOU  358  CD  LYS A  42      763    742    463     94     53   -170       C  
ATOM    359  CE  LYS A  42      16.341  30.187  23.946  1.00  6.25           C  
ANISOU  359  CE  LYS A  42     1108    672    591     74    -21   -139       C  
ATOM    360  NZ  LYS A  42      17.647  30.918  23.793  1.00 10.84           N  
ANISOU  360  NZ  LYS A  42     1289   1844    984   -294     57    -32       N  
ATOM    361  N   VAL A  43      12.388  27.005  29.145  1.00  6.18           N  
ANISOU  361  N   VAL A  43      801    629    917    -26    -16    -10       N  
ATOM    362  CA  VAL A  43      11.951  25.876  29.970  1.00  6.00           C  
ANISOU  362  CA  VAL A  43      778    608    891     36     45    -31       C  
ATOM    363  C   VAL A  43      10.684  25.264  29.377  1.00  5.39           C  
ANISOU  363  C   VAL A  43      672    564    809     32     36    -18       C  
ATOM    364  O   VAL A  43      10.571  24.044  29.261  1.00  5.07           O  
ANISOU  364  O   VAL A  43      647    552    727     25      4     -8       O  
ATOM    365  CB  VAL A  43      11.744  26.273  31.436  1.00  5.76           C  
ANISOU  365  CB  VAL A  43      607    721    860     49     21    -55       C  
ATOM    366  CG1 VAL A  43      10.991  25.210  32.216  1.00  7.09           C  
ANISOU  366  CG1 VAL A  43      813    811   1069    -54     43    -61       C  
ATOM    367  CG2 VAL A  43      13.093  26.572  32.094  1.00  7.47           C  
ANISOU  367  CG2 VAL A  43      873    971    994     58   -132   -178       C  
ATOM    368  N   GLN A  44       9.724  26.109  29.020  1.00  5.35           N  
ANISOU  368  N   GLN A  44      700    584    747     37     27    -63       N  
ATOM    369  CA  GLN A  44       8.495  25.634  28.383  1.00  5.35           C  
ANISOU  369  CA  GLN A  44      638    631    763     -2     14    -23       C  
ATOM    370  C   GLN A  44       8.806  24.859  27.121  1.00  4.79           C  
ANISOU  370  C   GLN A  44      509    674    637     34     34     17       C  
ATOM    371  O   GLN A  44       8.264  23.777  26.902  1.00  4.98           O  
ANISOU  371  O   GLN A  44      597    660    633      9    103     49       O  
ATOM    372  CB  GLN A  44       7.573  26.796  28.027  1.00  5.56           C  
ANISOU  372  CB  GLN A  44      670    650    790     52      9    -37       C  
ATOM    373  CG  GLN A  44       6.956  27.453  29.236  1.00  6.19           C  
ANISOU  373  CG  GLN A  44      897    631    823     49    -63    -14       C  
ATOM    374  CD  GLN A  44       6.306  28.769  28.956  1.00  7.35           C  
ANISOU  374  CD  GLN A  44      984    967    842    143    -72    -14       C  
ATOM    375  OE1 GLN A  44       6.260  29.214  27.819  1.00  8.67           O  
ANISOU  375  OE1 GLN A  44     1231   1006   1058    196    -76     74       O  
ATOM    376  NE2 GLN A  44       5.792  29.395  30.010  1.00  8.63           N  
ANISOU  376  NE2 GLN A  44     1371    740   1169    317    175    106       N  
ATOM    377  N   LEU A  45       9.659  25.422  26.271  1.00  4.97           N  
ANISOU  377  N   LEU A  45      602    618    667     28     26     29       N  
ATOM    378  CA  LEU A  45       9.991  24.772  25.014  1.00  4.73           C  
ANISOU  378  CA  LEU A  45      540    714    542     38     39     57       C  
ATOM    379  C   LEU A  45      10.702  23.436  25.262  1.00  4.61           C  
ANISOU  379  C   LEU A  45      547    641    561     51     13     16       C  
ATOM    380  O   LEU A  45      10.456  22.456  24.573  1.00  5.19           O  
ANISOU  380  O   LEU A  45      581    713    675     13    -48     61       O  
ATOM    381  CB  LEU A  45      10.864  25.674  24.168  1.00  5.30           C  
ANISOU  381  CB  LEU A  45      532    787    693      2     47     35       C  
ATOM    382  CG  LEU A  45      10.184  26.920  23.591  1.00  6.38           C  
ANISOU  382  CG  LEU A  45      770    887    767    144    151    109       C  
ATOM    383  CD1 LEU A  45      11.212  27.859  22.985  1.00  8.89           C  
ANISOU  383  CD1 LEU A  45     1117   1295    964    -52    295    104       C  
ATOM    384  CD2 LEU A  45       9.143  26.509  22.564  1.00 10.00           C  
ANISOU  384  CD2 LEU A  45     1332   1191   1277     80   -297    291       C  
ATOM    385  N   TYR A  46      11.592  23.404  26.253  1.00  4.63           N  
ANISOU  385  N   TYR A  46      537    653    567     -6    -36     21       N  
ATOM    386  CA  TYR A  46      12.314  22.170  26.565  1.00  4.31           C  
ANISOU  386  CA  TYR A  46      510    620    505     40     -5      2       C  
ATOM    387  C   TYR A  46      11.346  21.093  27.066  1.00  4.42           C  
ANISOU  387  C   TYR A  46      508    604    567     54    -43    -36       C  
ATOM    388  O   TYR A  46      11.400  19.953  26.639  1.00  4.73           O  
ANISOU  388  O   TYR A  46      476    696    625    -30    -40    -29       O  
ATOM    389  CB  TYR A  46      13.388  22.507  27.600  1.00  4.55           C  
ANISOU  389  CB  TYR A  46      576    653    500     83    122    -23       C  
ATOM    390  CG  TYR A  46      14.260  21.383  28.037  1.00  4.52           C  
ANISOU  390  CG  TYR A  46      521    664    529    -84      2     33       C  
ATOM    391  CD1 TYR A  46      15.286  20.900  27.231  1.00  5.04           C  
ANISOU  391  CD1 TYR A  46      646    778    492     29    -30     15       C  
ATOM    392  CD2 TYR A  46      14.105  20.821  29.298  1.00  5.55           C  
ANISOU  392  CD2 TYR A  46      792    646    670     73    183     33       C  
ATOM    393  CE1 TYR A  46      16.126  19.874  27.671  1.00  4.94           C  
ANISOU  393  CE1 TYR A  46      640    710    524    -17    117   -159       C  
ATOM    394  CE2 TYR A  46      14.956  19.835  29.750  1.00  5.94           C  
ANISOU  394  CE2 TYR A  46     1077    790    388    110     13     57       C  
ATOM    395  CZ  TYR A  46      15.965  19.385  28.953  1.00  4.66           C  
ANISOU  395  CZ  TYR A  46      640    539    590      7   -127     -3       C  
ATOM    396  OH  TYR A  46      16.788  18.387  29.445  1.00  5.91           O  
ANISOU  396  OH  TYR A  46     1032    584    630     56   -212   -146       O  
ATOM    397  N   CYS A  47      10.444  21.487  27.963  1.00  4.87           N  
ANISOU  397  N   CYS A  47      541    687    622    -43     22      7       N  
ATOM    398  CA  CYS A  47       9.421  20.560  28.457  1.00  5.11           C  
ANISOU  398  CA  CYS A  47      640    673    627    -32     -9     60       C  
ATOM    399  C   CYS A  47       8.526  20.052  27.327  1.00  4.62           C  
ANISOU  399  C   CYS A  47      509    617    629      7     69     10       C  
ATOM    400  O   CYS A  47       8.250  18.855  27.230  1.00  5.37           O  
ANISOU  400  O   CYS A  47      641    666    731    -62     35     98       O  
ATOM    401  CB  CYS A  47       8.584  21.246  29.534  1.00  5.27           C  
ANISOU  401  CB  CYS A  47      688    800    512     -2     11     -4       C  
ATOM    402  SG  CYS A  47       9.439  21.512  31.090  1.00  5.44           S  
ANISOU  402  SG  CYS A  47      649    778    637      2     25     10       S  
ATOM    403  N   GLU A  48       8.072  20.959  26.480  1.00  4.75           N  
ANISOU  403  N   GLU A  48      581    640    580    -58     75      4       N  
ATOM    404  CA  GLU A  48       7.271  20.592  25.327  1.00  5.43           C  
ANISOU  404  CA  GLU A  48      571    724    765     -1    -50    -43       C  
ATOM    405  C   GLU A  48       7.991  19.589  24.444  1.00  5.16           C  
ANISOU  405  C   GLU A  48      613    668    677      8   -150     -4       C  
ATOM    406  O   GLU A  48       7.412  18.630  23.971  1.00  5.66           O  
ANISOU  406  O   GLU A  48      658    649    841    -76    -38    -14       O  
ATOM    407  CB  GLU A  48       6.910  21.839  24.541  1.00  6.07           C  
ANISOU  407  CB  GLU A  48      748    781    776      2   -155    -42       C  
ATOM    408  CG  GLU A  48       6.044  21.569  23.308  1.00  6.48           C  
ANISOU  408  CG  GLU A  48      756    751    953     27   -177   -167       C  
ATOM    409  CD  GLU A  48       5.870  22.768  22.410  1.00  8.06           C  
ANISOU  409  CD  GLU A  48      942    943   1176    135   -315   -110       C  
ATOM    410  OE1 GLU A  48       6.826  23.528  22.192  1.00  9.14           O  
ANISOU  410  OE1 GLU A  48     1121   1245   1105    -18   -102    290       O  
ATOM    411  OE2 GLU A  48       4.749  22.972  21.911  1.00 10.75           O  
ANISOU  411  OE2 GLU A  48     1146   1255   1683   -104   -406    222       O  
ATOM    412  N   CYS A  49       9.264  19.853  24.185  1.00  4.62           N  
ANISOU  412  N   CYS A  49      526    581    647     -8    -10    -69       N  
ATOM    413  CA  CYS A  49      10.049  18.992  23.333  1.00  4.79           C  
ANISOU  413  CA  CYS A  49      614    603    602    -17    -12    -70       C  
ATOM    414  C   CYS A  49      10.170  17.582  23.883  1.00  5.30           C  
ANISOU  414  C   CYS A  49      673    698    640    -26    -22    -85       C  
ATOM    415  O   CYS A  49      10.005  16.588  23.174  1.00  6.31           O  
ANISOU  415  O   CYS A  49      777    681    937     17    -16    -36       O  
ATOM    416  CB  CYS A  49      11.414  19.624  23.103  1.00  5.41           C  
ANISOU  416  CB  CYS A  49      810    534    709     82     47    -19       C  
ATOM    417  SG  CYS A  49      12.579  18.661  22.125  1.00  6.14           S  
ANISOU  417  SG  CYS A  49      840    805    687    -10     62    -38       S  
ATOM    418  N   ILE A  50      10.454  17.472  25.165  1.00  5.04           N  
ANISOU  418  N   ILE A  50      543    637    734     -2     11     17       N  
ATOM    419  CA AILE A  50      10.578  16.153  25.760  0.50  5.94           C  
ANISOU  419  CA AILE A  50      692    761    804    -35     26    126       C  
ATOM    420  CA BILE A  50      10.580  16.145  25.760  0.50  6.38           C  
ANISOU  420  CA BILE A  50      742    793    889     -5    -12    115       C  
ATOM    421  C   ILE A  50       9.233  15.404  25.677  1.00  6.15           C  
ANISOU  421  C   ILE A  50      751    748    835    -52     24    107       C  
ATOM    422  O   ILE A  50       9.175  14.233  25.307  1.00  6.73           O  
ANISOU  422  O   ILE A  50      810    674   1069     -4    -22    121       O  
ATOM    423  CB AILE A  50      11.126  16.287  27.177  0.50  6.26           C  
ANISOU  423  CB AILE A  50      729    779    867    -84    -19    181       C  
ATOM    424  CB BILE A  50      11.059  16.182  27.214  0.50  7.14           C  
ANISOU  424  CB BILE A  50      817    904    991    -20    -58    151       C  
ATOM    425  CG1AILE A  50      12.648  16.538  27.097  0.50  5.48           C  
ANISOU  425  CG1AILE A  50      679    827    575    -34    110     15       C  
ATOM    426  CG1BILE A  50      12.371  16.981  27.359  0.50  7.85           C  
ANISOU  426  CG1BILE A  50      912    781   1287     92   -145    131       C  
ATOM    427  CG2AILE A  50      10.731  15.083  28.079  0.50  6.58           C  
ANISOU  427  CG2AILE A  50      689    818    992    -71    158    333       C  
ATOM    428  CG2BILE A  50      11.249  14.737  27.718  0.50  7.49           C  
ANISOU  428  CG2BILE A  50      863    964   1017    102    -35    142       C  
ATOM    429  CD1AILE A  50      13.173  17.011  28.424  0.50  4.72           C  
ANISOU  429  CD1AILE A  50      742    788    262    -49      8    -70       C  
ATOM    430  CD1BILE A  50      13.566  16.105  27.433  0.50  9.80           C  
ANISOU  430  CD1BILE A  50      974   1371   1379    285    134    -47       C  
ATOM    431  N   LEU A  51       8.140  16.083  25.989  1.00  7.01           N  
ANISOU  431  N   LEU A  51      865    860    939    -27     59     98       N  
ATOM    432  CA  LEU A  51       6.827  15.443  25.898  1.00  7.05           C  
ANISOU  432  CA  LEU A  51      935    767    975    -84     82    199       C  
ATOM    433  C   LEU A  51       6.490  15.023  24.476  1.00  7.41           C  
ANISOU  433  C   LEU A  51      770    981   1065    -28     92     91       C  
ATOM    434  O   LEU A  51       5.929  13.952  24.266  1.00  8.03           O  
ANISOU  434  O   LEU A  51      849    977   1222   -225    111     24       O  
ATOM    435  CB  LEU A  51       5.758  16.394  26.396  1.00  7.91           C  
ANISOU  435  CB  LEU A  51     1001   1043    958    -33    108     86       C  
ATOM    436  CG  LEU A  51       5.810  16.653  27.891  1.00  8.98           C  
ANISOU  436  CG  LEU A  51     1032   1214   1163   -177    214    101       C  
ATOM    437  CD1 LEU A  51       4.923  17.843  28.269  1.00 11.16           C  
ANISOU  437  CD1 LEU A  51     1168   1588   1482     36    311    222       C  
ATOM    438  CD2 LEU A  51       5.427  15.458  28.719  1.00 13.75           C  
ANISOU  438  CD2 LEU A  51     2035   1745   1443   -469    500    397       C  
ATOM    439  N   LYS A  52       6.764  15.864  23.506  1.00  7.04           N  
ANISOU  439  N   LYS A  52      892    797    984      0    -13     30       N  
ATOM    440  CA  LYS A  52       6.489  15.526  22.103  1.00  7.69           C  
ANISOU  440  CA  LYS A  52      838   1046   1035     33    -97    -87       C  
ATOM    441  C   LYS A  52       7.352  14.370  21.627  1.00  7.81           C  
ANISOU  441  C   LYS A  52      895    927   1145     10   -108   -104       C  
ATOM    442  O   LYS A  52       6.893  13.495  20.857  1.00  8.68           O  
ANISOU  442  O   LYS A  52     1020   1012   1265     11   -127   -177       O  
ATOM    443  CB  LYS A  52       6.662  16.724  21.200  1.00  8.21           C  
ANISOU  443  CB  LYS A  52      990   1021   1108    103    -32    -54       C  
ATOM    444  CG  LYS A  52       5.484  17.692  21.221  1.00  7.83           C  
ANISOU  444  CG  LYS A  52      986   1034    955     15    -92    -82       C  
ATOM    445  CD  LYS A  52       5.607  18.827  20.226  1.00 10.42           C  
ANISOU  445  CD  LYS A  52     1543   1190   1225     59   -107     24       C  
ATOM    446  CE  LYS A  52       4.417  19.772  20.375  1.00 11.71           C  
ANISOU  446  CE  LYS A  52     1535   1330   1583    108   -460     41       C  
ATOM    447  NZ  LYS A  52       4.444  20.889  19.388  1.00 13.93           N  
ANISOU  447  NZ  LYS A  52     1930   1557   1805    134   -305    168       N  
ATOM    448  N   ASN A  53       8.601  14.325  22.088  1.00  7.70           N  
ANISOU  448  N   ASN A  53      880    909   1137     40    -25   -100       N  
ATOM    449  CA  ASN A  53       9.484  13.265  21.636  1.00  8.23           C  
ANISOU  449  CA  ASN A  53     1007    931   1189     63    -20      5       C  
ATOM    450  C   ASN A  53       9.119  11.907  22.210  1.00  8.88           C  
ANISOU  450  C   ASN A  53     1034   1029   1311     51     -9    -38       C  
ATOM    451  O   ASN A  53       9.456  10.870  21.626  1.00 10.00           O  
ANISOU  451  O   ASN A  53     1221    994   1584     48     56    -94       O  
ATOM    452  CB  ASN A  53      10.939  13.599  21.890  1.00  8.20           C  
ANISOU  452  CB  ASN A  53      956   1012   1148     50     16    -52       C  
ATOM    453  CG  ASN A  53      11.453  14.701  20.980  1.00  8.67           C  
ANISOU  453  CG  ASN A  53     1036   1156   1100     78    -81    136       C  
ATOM    454  OD1 ASN A  53      10.689  15.316  20.223  1.00 11.67           O  
ANISOU  454  OD1 ASN A  53     1352   1686   1393    102   -194     71       O  
ATOM    455  ND2 ASN A  53      12.743  15.001  21.078  1.00  8.35           N  
ANISOU  455  ND2 ASN A  53     1113   1190    869     68   -136      0       N  
ATOM    456  N   PHE A  54       8.419  11.904  23.334  1.00  8.63           N  
ANISOU  456  N   PHE A  54     1129    872   1278     47     -2     26       N  
ATOM    457  CA  PHE A  54       7.812  10.698  23.892  1.00 10.06           C  
ANISOU  457  CA  PHE A  54     1279   1101   1441     25    -14     95       C  
ATOM    458  C   PHE A  54       6.369  10.488  23.388  1.00 11.15           C  
ANISOU  458  C   PHE A  54     1334   1249   1653    -36    -58    186       C  
ATOM    459  O   PHE A  54       5.708   9.554  23.834  1.00 12.79           O  
ANISOU  459  O   PHE A  54     1430   1332   2094   -137   -115    307       O  
ATOM    460  CB  PHE A  54       7.823  10.776  25.419  1.00  9.29           C  
ANISOU  460  CB  PHE A  54     1085   1023   1420     85    116     71       C  
ATOM    461  CG  PHE A  54       9.136  10.342  26.056  1.00  8.26           C  
ANISOU  461  CG  PHE A  54     1119   1013   1003     54    273     61       C  
ATOM    462  CD1 PHE A  54       9.343   9.011  26.362  1.00  9.37           C  
ANISOU  462  CD1 PHE A  54     1243   1181   1135    208    435    -42       C  
ATOM    463  CD2 PHE A  54      10.131  11.260  26.378  1.00 10.07           C  
ANISOU  463  CD2 PHE A  54     1180   1305   1341    174    242    193       C  
ATOM    464  CE1 PHE A  54      10.520   8.601  26.942  1.00  8.86           C  
ANISOU  464  CE1 PHE A  54     1394   1081    888    201    343    154       C  
ATOM    465  CE2 PHE A  54      11.316  10.854  26.971  1.00  8.64           C  
ANISOU  465  CE2 PHE A  54     1167   1382    731    127    365    245       C  
ATOM    466  CZ  PHE A  54      11.498   9.505  27.259  1.00  7.31           C  
ANISOU  466  CZ  PHE A  54     1043   1279    456    366    315   -111       C  
ATOM    467  N   ASN A  55       5.887  11.338  22.478  1.00 10.92           N  
ANISOU  467  N   ASN A  55     1304   1247   1597    -52    -73      2       N  
ATOM    468  CA  ASN A  55       4.559  11.208  21.850  1.00 11.46           C  
ANISOU  468  CA  ASN A  55     1393   1432   1526    -93    -45   -110       C  
ATOM    469  C   ASN A  55       3.426  11.393  22.837  1.00 11.03           C  
ANISOU  469  C   ASN A  55     1354   1365   1472   -189     12    -15       C  
ATOM    470  O   ASN A  55       2.265  11.053  22.536  1.00 11.51           O  
ANISOU  470  O   ASN A  55     1354   1559   1458   -249    -29     94       O  
ATOM    471  CB  ASN A  55       4.463   9.926  21.001  1.00 11.91           C  
ANISOU  471  CB  ASN A  55     1406   1548   1569   -119    -18   -185       C  
ATOM    472  CG  ASN A  55       5.519   9.920  19.916  1.00 14.24           C  
ANISOU  472  CG  ASN A  55     1730   1921   1758    -54     46   -372       C  
ATOM    473  OD1 ASN A  55       5.533  10.814  19.070  1.00 15.38           O  
ANISOU  473  OD1 ASN A  55     2151   2392   1299   -169    253   -696       O  
ATOM    474  ND2 ASN A  55       6.450   8.971  19.978  1.00 16.99           N  
ANISOU  474  ND2 ASN A  55     1862   2326   2267    124     79   -408       N  
ATOM    475  N   ILE A  56       3.743  11.993  23.978  1.00 11.30           N  
ANISOU  475  N   ILE A  56     1240   1535   1516   -117      1     27       N  
ATOM    476  CA  ILE A  56       2.752  12.375  24.981  1.00 11.33           C  
ANISOU  476  CA  ILE A  56     1392   1453   1458   -164     69    122       C  
ATOM    477  C   ILE A  56       1.961  13.635  24.610  1.00 11.36           C  
ANISOU  477  C   ILE A  56     1285   1504   1524   -111     19     37       C  
ATOM    478  O   ILE A  56       0.824  13.818  25.027  1.00 13.03           O  
ANISOU  478  O   ILE A  56     1476   1862   1611    -43    181    157       O  
ATOM    479  CB  ILE A  56       3.444  12.520  26.344  1.00 12.00           C  
ANISOU  479  CB  ILE A  56     1471   1560   1525   -202      8    194       C  
ATOM    480  CG1 ILE A  56       3.968  11.174  26.834  1.00 13.89           C  
ANISOU  480  CG1 ILE A  56     1670   1990   1617    -35     69    318       C  
ATOM    481  CG2 ILE A  56       2.556  13.155  27.400  1.00 13.38           C  
ANISOU  481  CG2 ILE A  56     1582   1698   1803    -84     26    181       C  
ATOM    482  CD1 ILE A  56       4.885  11.315  28.002  1.00 14.84           C  
ANISOU  482  CD1 ILE A  56     1752   2285   1598    -68     -4    570       C  
ATOM    483  N   LEU A  57       2.594  14.523  23.869  1.00 10.59           N  
ANISOU  483  N   LEU A  57     1241   1359   1421   -147    -41    -17       N  
ATOM    484  CA  LEU A  57       1.900  15.568  23.154  1.00  9.89           C  
ANISOU  484  CA  LEU A  57     1123   1402   1230   -121   -113      2       C  
ATOM    485  C   LEU A  57       2.059  15.225  21.689  1.00 10.25           C  
ANISOU  485  C   LEU A  57     1258   1416   1220    -67   -176    -36       C  
ATOM    486  O   LEU A  57       3.169  14.875  21.274  1.00 11.18           O  
ANISOU  486  O   LEU A  57     1412   1485   1349    -18   -261    -45       O  
ATOM    487  CB  LEU A  57       2.527  16.942  23.413  1.00 10.30           C  
ANISOU  487  CB  LEU A  57     1314   1369   1229   -102     33     40       C  
ATOM    488  CG  LEU A  57       2.364  17.500  24.825  1.00  9.74           C  
ANISOU  488  CG  LEU A  57      991   1459   1249   -110     -7    -47       C  
ATOM    489  CD1 LEU A  57       3.206  18.740  24.961  1.00 10.93           C  
ANISOU  489  CD1 LEU A  57     1372   1318   1460   -159    -96    118       C  
ATOM    490  CD2 LEU A  57       0.911  17.821  25.111  1.00 12.25           C  
ANISOU  490  CD2 LEU A  57     1356   1660   1637    -50    233      3       C  
ATOM    491  N   ASP A  58       0.982  15.314  20.896  1.00  9.91           N  
ANISOU  491  N   ASP A  58     1180   1404   1179    -30   -203      0       N  
ATOM    492  CA  ASP A  58       1.147  15.171  19.450  1.00 10.62           C  
ANISOU  492  CA  ASP A  58     1379   1430   1227     34   -147     14       C  
ATOM    493  C   ASP A  58       1.685  16.486  18.910  1.00 10.81           C  
ANISOU  493  C   ASP A  58     1426   1342   1339     54   -102     -1       C  
ATOM    494  O   ASP A  58       1.958  17.433  19.666  1.00 10.50           O  
ANISOU  494  O   ASP A  58     1285   1337   1367   -114   -168     85       O  
ATOM    495  CB  ASP A  58      -0.127  14.651  18.725  1.00 11.31           C  
ANISOU  495  CB  ASP A  58     1503   1507   1287      6   -206     23       C  
ATOM    496  CG  ASP A  58      -1.203  15.709  18.509  1.00 11.92           C  
ANISOU  496  CG  ASP A  58     1661   1499   1367   -109   -177    -40       C  
ATOM    497  OD1 ASP A  58      -1.039  16.880  18.871  1.00 11.85           O  
ANISOU  497  OD1 ASP A  58     1486   1393   1621     81   -341     10       O  
ATOM    498  OD2 ASP A  58      -2.251  15.335  17.926  1.00 14.63           O  
ANISOU  498  OD2 ASP A  58     1658   1745   2153   -250   -273     74       O  
ATOM    499  N   LYS A  59       1.913  16.542  17.605  1.00 11.36           N  
ANISOU  499  N   LYS A  59     1548   1412   1354     43   -105      8       N  
ATOM    500  CA  LYS A  59       2.548  17.709  17.005  1.00 12.34           C  
ANISOU  500  CA  LYS A  59     1639   1528   1522     10    -54     55       C  
ATOM    501  C   LYS A  59       1.726  18.990  17.181  1.00 12.36           C  
ANISOU  501  C   LYS A  59     1548   1503   1641    -34    -13     58       C  
ATOM    502  O   LYS A  59       2.293  20.072  17.144  1.00 13.77           O  
ANISOU  502  O   LYS A  59     1714   1573   1943   -107     20     49       O  
ATOM    503  CB  LYS A  59       2.857  17.446  15.525  1.00 13.46           C  
ANISOU  503  CB  LYS A  59     1902   1628   1584     -4    -15     67       C  
ATOM    504  CG  LYS A  59       1.630  17.335  14.638  1.00 14.85           C  
ANISOU  504  CG  LYS A  59     2170   1813   1658      1    -19    106       C  
ATOM    505  CD  LYS A  59       2.015  16.989  13.200  1.00 18.48           C  
ANISOU  505  CD  LYS A  59     2844   2214   1962     39     73     32       C  
ATOM    506  CE  LYS A  59       0.784  16.838  12.331  1.00 20.52           C  
ANISOU  506  CE  LYS A  59     2970   2447   2377    -65    -30     89       C  
ATOM    507  NZ  LYS A  59       1.101  16.585  10.886  1.00 22.60           N  
ANISOU  507  NZ  LYS A  59     3590   2518   2476   -197    -26   -155       N  
ATOM    508  N   ASN A  60       0.411  18.850  17.368  1.00 12.37           N  
ANISOU  508  N   ASN A  60     1468   1519   1712     19    -58     60       N  
ATOM    509  CA  ASN A  60      -0.510  19.961  17.640  1.00 12.58           C  
ANISOU  509  CA  ASN A  60     1515   1550   1716     59    -62     66       C  
ATOM    510  C   ASN A  60      -0.827  20.165  19.115  1.00 12.98           C  
ANISOU  510  C   ASN A  60     1499   1625   1805     64    -41     28       C  
ATOM    511  O   ASN A  60      -1.793  20.852  19.456  1.00 13.88           O  
ANISOU  511  O   ASN A  60     1575   1805   1890    128     67     13       O  
ATOM    512  CB  ASN A  60      -1.824  19.744  16.876  1.00 12.82           C  
ANISOU  512  CB  ASN A  60     1561   1568   1739    106    -84     69       C  
ATOM    513  CG  ASN A  60      -1.636  19.688  15.359  1.00 14.64           C  
ANISOU  513  CG  ASN A  60     1919   1787   1855     65   -156    -85       C  
ATOM    514  OD1 ASN A  60      -2.278  18.876  14.670  1.00 17.37           O  
ANISOU  514  OD1 ASN A  60     2441   2224   1934    124   -346   -364       O  
ATOM    515  ND2 ASN A  60      -0.797  20.557  14.833  1.00 14.85           N  
ANISOU  515  ND2 ASN A  60     1891   2080   1670    205   -368    285       N  
ATOM    516  N   ASN A  61       0.002  19.590  19.989  1.00 12.60           N  
ANISOU  516  N   ASN A  61     1456   1572   1758     28    -25     11       N  
ATOM    517  CA  ASN A  61      -0.110  19.741  21.456  1.00 12.89           C  
ANISOU  517  CA  ASN A  61     1487   1657   1751    -16      5     20       C  
ATOM    518  C   ASN A  61      -1.351  19.096  22.041  1.00 14.06           C  
ANISOU  518  C   ASN A  61     1660   1872   1807   -104     89    -45       C  
ATOM    519  O   ASN A  61      -1.772  19.458  23.136  1.00 15.46           O  
ANISOU  519  O   ASN A  61     1861   2164   1847   -258    296    -56       O  
ATOM    520  CB  ASN A  61       0.037  21.203  21.919  1.00 13.15           C  
ANISOU  520  CB  ASN A  61     1555   1704   1736     50     43    -55       C  
ATOM    521  CG  ASN A  61       1.426  21.727  21.704  1.00 12.30           C  
ANISOU  521  CG  ASN A  61     1502   1543   1626    123     15     27       C  
ATOM    522  OD1 ASN A  61       2.213  21.844  22.655  1.00 15.68           O  
ANISOU  522  OD1 ASN A  61     1763   2073   2119    -14    -14   -296       O  
ATOM    523  ND2 ASN A  61       1.770  22.001  20.452  1.00 12.59           N  
ANISOU  523  ND2 ASN A  61     1696   1502   1586    -73     18   -163       N  
ATOM    524  N   VAL A  62      -1.888  18.092  21.354  1.00 13.99           N  
ANISOU  524  N   VAL A  62     1608   1899   1806   -153     77    -21       N  
ATOM    525  CA  VAL A  62      -2.945  17.277  21.928  1.00 14.24           C  
ANISOU  525  CA  VAL A  62     1644   1894   1871   -123     35     15       C  
ATOM    526  C   VAL A  62      -2.294  16.318  22.917  1.00 14.18           C  
ANISOU  526  C   VAL A  62     1679   1886   1821    -83     57     50       C  
ATOM    527  O   VAL A  62      -1.339  15.584  22.591  1.00 13.35           O  
ANISOU  527  O   VAL A  62     1563   1777   1729    -54   -112     81       O  
ATOM    528  CB  VAL A  62      -3.749  16.506  20.869  1.00 13.76           C  
ANISOU  528  CB  VAL A  62     1473   1951   1802   -161    -15     -2       C  
ATOM    529  CG1 VAL A  62      -4.828  15.627  21.528  1.00 14.49           C  
ANISOU  529  CG1 VAL A  62     1485   2090   1931   -114    183    136       C  
ATOM    530  CG2 VAL A  62      -4.390  17.489  19.870  1.00 14.43           C  
ANISOU  530  CG2 VAL A  62     1494   1973   2013    155    -21      8       C  
ATOM    531  N   PHE A  63      -2.790  16.366  24.147  1.00 15.02           N  
ANISOU  531  N   PHE A  63     1876   1940   1891    -17     90     88       N  
ATOM    532  CA  PHE A  63      -2.238  15.606  25.248  1.00 15.92           C  
ANISOU  532  CA  PHE A  63     1958   2049   2038    -64     -5     20       C  
ATOM    533  C   PHE A  63      -2.788  14.166  25.250  1.00 15.19           C  
ANISOU  533  C   PHE A  63     1766   1994   2010   -138     66     -3       C  
ATOM    534  O   PHE A  63      -4.003  13.944  25.109  1.00 15.72           O  
ANISOU  534  O   PHE A  63     1709   2179   2084   -168     60     35       O  
ATOM    535  CB  PHE A  63      -2.544  16.335  26.555  1.00 16.60           C  
ANISOU  535  CB  PHE A  63     2062   2078   2167   -122     73    -39       C  
ATOM    536  CG  PHE A  63      -2.209  15.550  27.778  1.00 19.24           C  
ANISOU  536  CG  PHE A  63     2536   2301   2472    -86    -63     28       C  
ATOM    537  CD1 PHE A  63      -0.908  15.186  28.050  1.00 21.42           C  
ANISOU  537  CD1 PHE A  63     2759   2716   2661   -107    -86     16       C  
ATOM    538  CD2 PHE A  63      -3.200  15.172  28.663  1.00 22.00           C  
ANISOU  538  CD2 PHE A  63     2875   2792   2691     -6     72     11       C  
ATOM    539  CE1 PHE A  63      -0.601  14.463  29.183  1.00 23.48           C  
ANISOU  539  CE1 PHE A  63     3170   2802   2948   -113    -33    139       C  
ATOM    540  CE2 PHE A  63      -2.898  14.445  29.784  1.00 23.81           C  
ANISOU  540  CE2 PHE A  63     3161   2985   2898    -18     36     98       C  
ATOM    541  CZ  PHE A  63      -1.602  14.098  30.052  1.00 23.61           C  
ANISOU  541  CZ  PHE A  63     3119   3032   2819     -3     28      9       C  
ATOM    542  N   LYS A  64      -1.886  13.200  25.433  1.00 14.54           N  
ANISOU  542  N   LYS A  64     1672   1888   1965   -183     38     36       N  
ATOM    543  CA  LYS A  64      -2.175  11.765  25.401  1.00 15.96           C  
ANISOU  543  CA  LYS A  64     1928   1993   2141   -120      6    -43       C  
ATOM    544  C   LYS A  64      -1.780  11.121  26.737  1.00 16.36           C  
ANISOU  544  C   LYS A  64     1901   2106   2209   -128    -59    -82       C  
ATOM    545  O   LYS A  64      -0.627  10.703  26.925  1.00 16.55           O  
ANISOU  545  O   LYS A  64     1806   1991   2489   -130    -99   -259       O  
ATOM    546  CB  LYS A  64      -1.349  11.084  24.314  1.00 16.21           C  
ANISOU  546  CB  LYS A  64     2004   2067   2086    -76      1     -8       C  
ATOM    547  CG  LYS A  64      -1.397  11.726  22.958  1.00 18.18           C  
ANISOU  547  CG  LYS A  64     2392   2269   2245     10     57    -64       C  
ATOM    548  CD  LYS A  64      -2.721  11.490  22.288  1.00 17.83           C  
ANISOU  548  CD  LYS A  64     2195   2343   2236     46    183   -133       C  
ATOM    549  CE  LYS A  64      -2.710  12.099  20.881  1.00 16.36           C  
ANISOU  549  CE  LYS A  64     2087   2155   1973      1    132   -383       C  
ATOM    550  NZ  LYS A  64      -2.005  11.294  19.818  1.00 15.88           N  
ANISOU  550  NZ  LYS A  64     1895   2057   2081    355    210   -300       N  
ATOM    551  N   PRO A  65      -2.731  10.988  27.670  1.00 18.04           N  
ANISOU  551  N   PRO A  65     2187   2386   2281    -38     -3    -24       N  
ATOM    552  CA  PRO A  65      -2.420  10.371  28.973  1.00 18.62           C  
ANISOU  552  CA  PRO A  65     2281   2477   2317    -41    -39     -1       C  
ATOM    553  C   PRO A  65      -1.771   8.976  28.923  1.00 18.72           C  
ANISOU  553  C   PRO A  65     2295   2521   2295    -31    -56    -27       C  
ATOM    554  O   PRO A  65      -0.950   8.658  29.774  1.00 18.86           O  
ANISOU  554  O   PRO A  65     2199   2703   2262    -23   -115    -31       O  
ATOM    555  CB  PRO A  65      -3.782  10.290  29.666  1.00 19.45           C  
ANISOU  555  CB  PRO A  65     2385   2574   2429     10    -14     10       C  
ATOM    556  CG  PRO A  65      -4.646  11.289  28.969  1.00 19.59           C  
ANISOU  556  CG  PRO A  65     2459   2556   2429     16     -3     46       C  
ATOM    557  CD  PRO A  65      -4.130  11.446  27.579  1.00 18.13           C  
ANISOU  557  CD  PRO A  65     2169   2434   2285    -14    -40      1       C  
ATOM    558  N   GLN A  66      -2.131   8.146  27.948  1.00 18.38           N  
ANISOU  558  N   GLN A  66     2300   2401   2283    -74    -94    -60       N  
ATOM    559  CA  GLN A  66      -1.547   6.804  27.831  1.00 18.58           C  
ANISOU  559  CA  GLN A  66     2393   2376   2289    -34   -101    -37       C  
ATOM    560  C   GLN A  66      -0.025   6.817  27.663  1.00 17.25           C  
ANISOU  560  C   GLN A  66     2298   2152   2101    -19    -91    -61       C  
ATOM    561  O   GLN A  66       0.653   5.892  28.103  1.00 17.37           O  
ANISOU  561  O   GLN A  66     2490   2023   2087     19   -180    -70       O  
ATOM    562  CB  GLN A  66      -2.199   6.029  26.671  1.00 19.53           C  
ANISOU  562  CB  GLN A  66     2534   2452   2432    -31   -125    -68       C  
ATOM    563  CG  GLN A  66      -1.844   4.522  26.609  1.00 22.98           C  
ANISOU  563  CG  GLN A  66     2979   2738   3015     99     -6    -57       C  
ATOM    564  CD  GLN A  66      -2.383   3.724  27.786  1.00 24.75           C  
ANISOU  564  CD  GLN A  66     3283   2962   3158     85    -22    -46       C  
ATOM    565  OE1 GLN A  66      -3.575   3.773  28.093  1.00 28.47           O  
ANISOU  565  OE1 GLN A  66     3393   3621   3802    190     14   -179       O  
ATOM    566  NE2 GLN A  66      -1.512   2.969  28.438  1.00 25.15           N  
ANISOU  566  NE2 GLN A  66     3181   3034   3337    194   -239   -394       N  
ATOM    567  N   GLY A  67       0.515   7.869  27.047  1.00 15.40           N  
ANISOU  567  N   GLY A  67     2160   2016   1673     30    -92     -6       N  
ATOM    568  CA  GLY A  67       1.950   8.015  26.893  1.00 15.06           C  
ANISOU  568  CA  GLY A  67     2115   1944   1660     84     71     62       C  
ATOM    569  C   GLY A  67       2.630   8.174  28.227  1.00 14.68           C  
ANISOU  569  C   GLY A  67     1975   1960   1643     61    112     95       C  
ATOM    570  O   GLY A  67       3.733   7.681  28.427  1.00 15.71           O  
ANISOU  570  O   GLY A  67     2200   2133   1637    247    278    113       O  
ATOM    571  N   ILE A  68       1.989   8.899  29.142  1.00 13.27           N  
ANISOU  571  N   ILE A  68     1799   1641   1602     62     45     58       N  
ATOM    572  CA  ILE A  68       2.531   9.040  30.482  1.00 13.26           C  
ANISOU  572  CA  ILE A  68     1767   1695   1573     35    -55      5       C  
ATOM    573  C   ILE A  68       2.484   7.703  31.208  1.00 12.37           C  
ANISOU  573  C   ILE A  68     1676   1631   1392     -3    -65     -1       C  
ATOM    574  O   ILE A  68       3.449   7.324  31.846  1.00 11.35           O  
ANISOU  574  O   ILE A  68     1497   1346   1467     30    -81     52       O  
ATOM    575  CB  ILE A  68       1.770  10.091  31.314  1.00 14.13           C  
ANISOU  575  CB  ILE A  68     1890   1858   1617    110   -188   -129       C  
ATOM    576  CG1 ILE A  68       1.998  11.485  30.759  1.00 16.50           C  
ANISOU  576  CG1 ILE A  68     2319   2114   1835    247    -99    -48       C  
ATOM    577  CG2 ILE A  68       2.250  10.082  32.764  1.00 16.12           C  
ANISOU  577  CG2 ILE A  68     2067   2245   1812    211   -335    -65       C  
ATOM    578  CD1 ILE A  68       1.215  12.576  31.517  1.00 18.54           C  
ANISOU  578  CD1 ILE A  68     2514   2282   2248    560    -94   -221       C  
ATOM    579  N   LYS A  69       1.370   6.984  31.091  1.00 13.10           N  
ANISOU  579  N   LYS A  69     1757   1703   1514    -37     -4    158       N  
ATOM    580  CA  LYS A  69       1.246   5.675  31.742  1.00 14.28           C  
ANISOU  580  CA  LYS A  69     1893   1797   1736    -90      8    148       C  
ATOM    581  C   LYS A  69       2.329   4.710  31.296  1.00 14.39           C  
ANISOU  581  C   LYS A  69     1899   1780   1789    -93    -75    116       C  
ATOM    582  O   LYS A  69       2.926   4.016  32.134  1.00 14.96           O  
ANISOU  582  O   LYS A  69     2005   1757   1918    -93   -189    215       O  
ATOM    583  CB  LYS A  69      -0.099   5.039  31.443  1.00 15.02           C  
ANISOU  583  CB  LYS A  69     1970   1903   1834   -146     74    159       C  
ATOM    584  CG  LYS A  69      -1.288   5.784  31.975  1.00 18.42           C  
ANISOU  584  CG  LYS A  69     2360   2235   2401     54     84    -11       C  
ATOM    585  CD  LYS A  69      -2.557   4.908  31.905  1.00 22.61           C  
ANISOU  585  CD  LYS A  69     2746   2783   3062   -136     91    -92       C  
ATOM    586  CE  LYS A  69      -3.747   5.706  31.376  1.00 25.08           C  
ANISOU  586  CE  LYS A  69     3046   3092   3389    -29     25    -78       C  
ATOM    587  NZ  LYS A  69      -4.957   4.868  31.145  1.00 26.94           N  
ANISOU  587  NZ  LYS A  69     3133   3378   3723    -56      5   -104       N  
ATOM    588  N   ALA A  70       2.593   4.664  29.995  1.00 15.48           N  
ANISOU  588  N   ALA A  70     2021   1930   1930    -28   -138    -52       N  
ATOM    589  CA  ALA A  70       3.579   3.732  29.448  1.00 16.15           C  
ANISOU  589  CA  ALA A  70     2110   2012   2015     32    -87    -69       C  
ATOM    590  C   ALA A  70       4.938   3.917  30.090  1.00 15.77           C  
ANISOU  590  C   ALA A  70     2088   1923   1979     26    -44    -47       C  
ATOM    591  O   ALA A  70       5.597   2.943  30.423  1.00 17.70           O  
ANISOU  591  O   ALA A  70     2272   2149   2301    138    -70   -104       O  
ATOM    592  CB  ALA A  70       3.692   3.887  27.932  1.00 16.88           C  
ANISOU  592  CB  ALA A  70     2196   2180   2037     71    -94   -155       C  
ATOM    593  N   VAL A  71       5.361   5.166  30.260  1.00 13.40           N  
ANISOU  593  N   VAL A  71     1887   1614   1589     25    -47      0       N  
ATOM    594  CA  VAL A  71       6.657   5.440  30.873  1.00 12.13           C  
ANISOU  594  CA  VAL A  71     1684   1500   1425     35     63    117       C  
ATOM    595  C   VAL A  71       6.613   5.228  32.415  1.00  9.78           C  
ANISOU  595  C   VAL A  71     1342   1143   1230     12    -10    110       C  
ATOM    596  O   VAL A  71       7.492   4.575  32.998  1.00  9.82           O  
ANISOU  596  O   VAL A  71     1367   1211   1153     89    -94     91       O  
ATOM    597  CB  VAL A  71       7.179   6.865  30.527  1.00 12.76           C  
ANISOU  597  CB  VAL A  71     1761   1602   1483     70    139    164       C  
ATOM    598  CG1 VAL A  71       8.472   7.115  31.251  1.00 14.14           C  
ANISOU  598  CG1 VAL A  71     1819   1701   1853     79     69    310       C  
ATOM    599  CG2 VAL A  71       7.384   7.035  29.016  1.00 14.94           C  
ANISOU  599  CG2 VAL A  71     2124   2014   1538    216    259    354       C  
ATOM    600  N   MET A  72       5.606   5.786  33.072  1.00  8.74           N  
ANISOU  600  N   MET A  72     1244    997   1078    -69    -73    157       N  
ATOM    601  CA  MET A  72       5.585   5.815  34.525  1.00  8.81           C  
ANISOU  601  CA  MET A  72     1184   1087   1076    -49   -106    130       C  
ATOM    602  C   MET A  72       5.353   4.447  35.141  1.00  9.44           C  
ANISOU  602  C   MET A  72     1251   1117   1219      0   -120     59       C  
ATOM    603  O   MET A  72       5.786   4.202  36.262  1.00  9.70           O  
ANISOU  603  O   MET A  72     1271   1270   1143     14   -138    110       O  
ATOM    604  CB  MET A  72       4.602   6.865  35.032  1.00  8.73           C  
ANISOU  604  CB  MET A  72     1090   1126   1099    -39    -22    119       C  
ATOM    605  CG  MET A  72       4.921   8.302  34.597  1.00  9.42           C  
ANISOU  605  CG  MET A  72     1312   1198   1066    -31   -102     36       C  
ATOM    606  SD  MET A  72       6.576   8.872  35.027  1.00 11.27           S  
ANISOU  606  SD  MET A  72     1356   1252   1672     54   -208      8       S  
ATOM    607  CE  MET A  72       6.394   8.647  36.732  1.00 11.55           C  
ANISOU  607  CE  MET A  72      923   1968   1495    125   -422    138       C  
ATOM    608  N   GLU A  73       4.701   3.533  34.420  1.00 10.46           N  
ANISOU  608  N   GLU A  73     1407   1123   1444    -54   -142    100       N  
ATOM    609  CA AGLU A  73       4.509   2.208  35.000  0.50 10.83           C  
ANISOU  609  CA AGLU A  73     1424   1228   1460    -77    -75    100       C  
ATOM    610  CA BGLU A  73       4.509   2.119  34.821  0.50 11.08           C  
ANISOU  610  CA BGLU A  73     1470   1255   1483    -47    -87    110       C  
ATOM    611  C   GLU A  73       5.845   1.430  35.094  1.00 10.46           C  
ANISOU  611  C   GLU A  73     1372   1175   1426    -81     -2     98       C  
ATOM    612  O   GLU A  73       5.910   0.420  35.797  1.00 11.23           O  
ANISOU  612  O   GLU A  73     1483   1245   1539    -64    -10    248       O  
ATOM    613  CB AGLU A  73       3.399   1.434  34.289  0.50 11.03           C  
ANISOU  613  CB AGLU A  73     1434   1236   1521    -81    -54     79       C  
ATOM    614  CB BGLU A  73       3.744   1.310  33.733  0.50 11.52           C  
ANISOU  614  CB BGLU A  73     1530   1307   1538     -7    -84    120       C  
ATOM    615  CG AGLU A  73       1.997   1.955  34.622  0.50 12.17           C  
ANISOU  615  CG AGLU A  73     1488   1431   1704   -103   -128    -91       C  
ATOM    616  CG BGLU A  73       4.586   0.875  32.517  0.50 13.13           C  
ANISOU  616  CG BGLU A  73     1748   1651   1590     85   -159     24       C  
ATOM    617  CD AGLU A  73       0.893   1.180  33.936  0.50 13.51           C  
ANISOU  617  CD AGLU A  73     1621   1642   1869    -34   -233   -298       C  
ATOM    618  CD BGLU A  73       3.846  -0.009  31.496  0.50 14.51           C  
ANISOU  618  CD BGLU A  73     2064   1986   1464    123   -260     21       C  
ATOM    619  OE1AGLU A  73      -0.269   1.305  34.381  0.50 14.24           O  
ANISOU  619  OE1AGLU A  73     1762   1686   1962    243   -103   -395       O  
ATOM    620  OE1BGLU A  73       2.598  -0.035  31.482  0.50 15.60           O  
ANISOU  620  OE1BGLU A  73     2176   2287   1462    204   -508     43       O  
ATOM    621  OE2AGLU A  73       1.187   0.451  32.958  0.50 15.79           O  
ANISOU  621  OE2AGLU A  73     1699   2131   2170    121   -242   -648       O  
ATOM    622  OE2BGLU A  73       4.540  -0.683  30.703  0.50 14.95           O  
ANISOU  622  OE2BGLU A  73     2064   2233   1380    320   -544      8       O  
ATOM    623  N   LEU A  74       6.922   1.933  34.481  1.00 10.76           N  
ANISOU  623  N   LEU A  74     1469   1285   1332    -30     13    -15       N  
ATOM    624  CA  LEU A  74       8.243   1.364  34.694  1.00 10.52           C  
ANISOU  624  CA  LEU A  74     1463   1186   1348     -6     34    -38       C  
ATOM    625  C   LEU A  74       8.872   1.798  36.023  1.00 10.97           C  
ANISOU  625  C   LEU A  74     1420   1298   1447      2    -63    -17       C  
ATOM    626  O   LEU A  74       9.840   1.197  36.487  1.00 11.40           O  
ANISOU  626  O   LEU A  74     1464   1250   1615    138    -41    -66       O  
ATOM    627  CB  LEU A  74       9.183   1.776  33.559  1.00 11.71           C  
ANISOU  627  CB  LEU A  74     1624   1265   1558      7     80    -20       C  
ATOM    628  CG  LEU A  74       8.747   1.470  32.135  1.00 14.37           C  
ANISOU  628  CG  LEU A  74     2085   1611   1762    -59     41    -28       C  
ATOM    629  CD1 LEU A  74       9.796   2.014  31.160  1.00 15.08           C  
ANISOU  629  CD1 LEU A  74     2251   1610   1866   -147    209    -37       C  
ATOM    630  CD2 LEU A  74       8.548  -0.023  31.929  1.00 15.47           C  
ANISOU  630  CD2 LEU A  74     2414   1593   1872   -144     53   -179       C  
ATOM    631  N   LEU A  75       8.334   2.863  36.615  1.00  9.39           N  
ANISOU  631  N   LEU A  75     1124   1103   1338    -50     24      9       N  
ATOM    632  CA  LEU A  75       8.958   3.566  37.739  1.00  9.27           C  
ANISOU  632  CA  LEU A  75     1168   1169   1184     -6     67     12       C  
ATOM    633  C   LEU A  75       8.191   3.510  39.052  1.00  9.77           C  
ANISOU  633  C   LEU A  75     1239   1206   1265    -59     49     83       C  
ATOM    634  O   LEU A  75       8.806   3.549  40.108  1.00 11.77           O  
ANISOU  634  O   LEU A  75     1488   1674   1310    -40    -11     34       O  
ATOM    635  CB  LEU A  75       9.137   5.028  37.347  1.00  8.71           C  
ANISOU  635  CB  LEU A  75     1066   1121   1121    -30    106    -42       C  
ATOM    636  CG  LEU A  75      10.002   5.269  36.106  1.00  9.26           C  
ANISOU  636  CG  LEU A  75     1331   1092   1095      0      8    -67       C  
ATOM    637  CD1 LEU A  75       9.994   6.721  35.711  1.00 10.01           C  
ANISOU  637  CD1 LEU A  75     1416   1011   1375     10    216    -14       C  
ATOM    638  CD2 LEU A  75      11.413   4.783  36.350  1.00 10.52           C  
ANISOU  638  CD2 LEU A  75     1230   1447   1317    120    188    155       C  
ATOM    639  N   ILE A  76       6.868   3.483  39.001  1.00  9.38           N  
ANISOU  639  N   ILE A  76     1249   1111   1203    -63     66    125       N  
ATOM    640  CA  ILE A  76       6.048   3.508  40.208  1.00  9.51           C  
ANISOU  640  CA  ILE A  76     1221   1098   1292     -5    118    156       C  
ATOM    641  C   ILE A  76       4.940   2.508  40.015  1.00  9.02           C  
ANISOU  641  C   ILE A  76     1220   1018   1188     20    116    182       C  
ATOM    642  O   ILE A  76       4.664   2.051  38.915  1.00  9.25           O  
ANISOU  642  O   ILE A  76     1211   1002   1299    -16    136    106       O  
ATOM    643  CB  ILE A  76       5.496   4.938  40.502  1.00 10.30           C  
ANISOU  643  CB  ILE A  76     1346   1202   1365    -66    173     42       C  
ATOM    644  CG1 ILE A  76       4.546   5.419  39.410  1.00 11.17           C  
ANISOU  644  CG1 ILE A  76     1529   1133   1581     20    254     91       C  
ATOM    645  CG2 ILE A  76       6.640   5.923  40.673  1.00 12.14           C  
ANISOU  645  CG2 ILE A  76     1473   1232   1906   -178    179     41       C  
ATOM    646  CD1 ILE A  76       3.994   6.817  39.635  1.00 14.08           C  
ANISOU  646  CD1 ILE A  76     2087   1334   1927    303    463    121       C  
ATOM    647  N   ASP A  77       4.273   2.184  41.107  1.00  8.80           N  
ANISOU  647  N   ASP A  77     1152   1125   1067     12     85    200       N  
ATOM    648  CA  ASP A  77       3.247   1.153  41.090  1.00  9.52           C  
ANISOU  648  CA  ASP A  77     1261   1091   1265     -3     92    182       C  
ATOM    649  C   ASP A  77       2.011   1.574  40.270  1.00  9.22           C  
ANISOU  649  C   ASP A  77     1274   1099   1127     42    188    210       C  
ATOM    650  O   ASP A  77       1.741   2.759  40.085  1.00  8.98           O  
ANISOU  650  O   ASP A  77     1195    967   1249     60    252    216       O  
ATOM    651  CB  ASP A  77       2.848   0.809  42.525  1.00  9.25           C  
ANISOU  651  CB  ASP A  77     1243   1050   1220     37     24    365       C  
ATOM    652  CG  ASP A  77       2.118   1.942  43.196  1.00  9.66           C  
ANISOU  652  CG  ASP A  77     1360   1162   1145     17     29    251       C  
ATOM    653  OD1 ASP A  77       2.782   2.857  43.708  1.00 10.43           O  
ANISOU  653  OD1 ASP A  77     1612   1155   1192    -68   -175    512       O  
ATOM    654  OD2 ASP A  77       0.873   1.920  43.198  1.00  9.71           O  
ANISOU  654  OD2 ASP A  77     1186   1109   1392     37     15    487       O  
ATOM    655  N   GLU A  78       1.237   0.593  39.825  1.00  9.59           N  
ANISOU  655  N   GLU A  78     1350   1108   1183     75     88    144       N  
ATOM    656  CA  GLU A  78       0.119   0.811  38.914  1.00 10.72           C  
ANISOU  656  CA  GLU A  78     1400   1308   1365     54     49    117       C  
ATOM    657  C   GLU A  78      -0.903   1.802  39.475  1.00  9.31           C  
ANISOU  657  C   GLU A  78     1321   1140   1074     73     72    117       C  
ATOM    658  O   GLU A  78      -1.379   2.684  38.754  1.00  9.61           O  
ANISOU  658  O   GLU A  78     1394   1190   1067    258    -61    139       O  
ATOM    659  CB  GLU A  78      -0.556  -0.528  38.592  1.00 12.88           C  
ANISOU  659  CB  GLU A  78     1597   1591   1706     73    -39    -60       C  
ATOM    660  CG  GLU A  78      -1.654  -0.448  37.562  1.00 17.43           C  
ANISOU  660  CG  GLU A  78     2087   2237   2295     68   -224    -63       C  
ATOM    661  CD  GLU A  78      -2.439  -1.748  37.444  1.00 23.65           C  
ANISOU  661  CD  GLU A  78     2950   2681   3352    -87   -418   -204       C  
ATOM    662  OE1 GLU A  78      -1.904  -2.816  37.820  1.00 28.25           O  
ANISOU  662  OE1 GLU A  78     3558   3033   4139    143   -541   -216       O  
ATOM    663  OE2 GLU A  78      -3.601  -1.694  36.991  1.00 28.47           O  
ANISOU  663  OE2 GLU A  78     3329   3377   4109    -51   -745   -351       O  
ATOM    664  N   ASN A  79      -1.265   1.673  40.738  1.00  7.78           N  
ANISOU  664  N   ASN A  79     1110    940    905     80     82    103       N  
ATOM    665  CA  ASN A  79      -2.260   2.578  41.277  1.00  7.74           C  
ANISOU  665  CA  ASN A  79     1063    937    940     10     45     58       C  
ATOM    666  C   ASN A  79      -1.747   4.003  41.355  1.00  7.87           C  
ANISOU  666  C   ASN A  79     1077   1022    890     18     70    102       C  
ATOM    667  O   ASN A  79      -2.505   4.933  41.135  1.00  7.93           O  
ANISOU  667  O   ASN A  79      945   1077    991    100      0    280       O  
ATOM    668  CB  ASN A  79      -2.772   2.105  42.630  1.00  7.31           C  
ANISOU  668  CB  ASN A  79     1040    859    876   -116     48     79       C  
ATOM    669  CG  ASN A  79      -3.482   0.758  42.557  1.00  8.14           C  
ANISOU  669  CG  ASN A  79     1111   1005    976   -274   -126   -227       C  
ATOM    670  OD1 ASN A  79      -4.010   0.369  41.513  1.00 12.35           O  
ANISOU  670  OD1 ASN A  79     1703   1762   1227   -496   -236   -215       O  
ATOM    671  ND2 ASN A  79      -3.460   0.033  43.652  1.00  8.89           N  
ANISOU  671  ND2 ASN A  79     1327    920   1129   -164     34    -94       N  
ATOM    672  N   SER A  80      -0.472   4.174  41.684  1.00  7.26           N  
ANISOU  672  N   SER A  80     1011    940    804     -6     46    157       N  
ATOM    673  CA  SER A  80       0.134   5.496  41.708  1.00  7.63           C  
ANISOU  673  CA  SER A  80      992   1010    895    -72     -3    160       C  
ATOM    674  C   SER A  80       0.130   6.112  40.318  1.00  7.74           C  
ANISOU  674  C   SER A  80     1082    971    889      7    -68     79       C  
ATOM    675  O   SER A  80      -0.081   7.307  40.186  1.00  8.27           O  
ANISOU  675  O   SER A  80     1228    935    979    -33   -175    270       O  
ATOM    676  CB  SER A  80       1.553   5.457  42.292  1.00  7.81           C  
ANISOU  676  CB  SER A  80      995   1014    956    -38     41    246       C  
ATOM    677  OG  SER A  80       1.511   5.110  43.673  1.00  8.08           O  
ANISOU  677  OG  SER A  80     1153   1088    827   -284     37    375       O  
ATOM    678  N   VAL A  81       0.375   5.319  39.281  1.00  8.29           N  
ANISOU  678  N   VAL A  81     1085   1138    927   -121     26     94       N  
ATOM    679  CA  VAL A  81       0.311   5.831  37.902  1.00  9.41           C  
ANISOU  679  CA  VAL A  81     1245   1340    989    -60    -47     30       C  
ATOM    680  C   VAL A  81      -1.105   6.339  37.585  1.00  8.44           C  
ANISOU  680  C   VAL A  81     1115   1214    876    -73     59     55       C  
ATOM    681  O   VAL A  81      -1.276   7.413  37.002  1.00  8.44           O  
ANISOU  681  O   VAL A  81     1129   1171    907    -31    -50     33       O  
ATOM    682  CB  VAL A  81       0.750   4.764  36.873  1.00  9.30           C  
ANISOU  682  CB  VAL A  81     1104   1560    869     10    162     98       C  
ATOM    683  CG1 VAL A  81       0.558   5.274  35.459  1.00 11.60           C  
ANISOU  683  CG1 VAL A  81     1483   1864   1058    144    169     97       C  
ATOM    684  CG2 VAL A  81       2.188   4.345  37.103  1.00 11.84           C  
ANISOU  684  CG2 VAL A  81     1123   1980   1392    129    141    303       C  
ATOM    685  N   LYS A  82      -2.125   5.575  37.970  1.00  8.76           N  
ANISOU  685  N   LYS A  82     1142   1134   1052    -74     37     55       N  
ATOM    686  CA  LYS A  82      -3.513   6.044  37.776  1.00 10.41           C  
ANISOU  686  CA  LYS A  82     1309   1416   1227    -26     15    129       C  
ATOM    687  C   LYS A  82      -3.761   7.377  38.483  1.00  9.99           C  
ANISOU  687  C   LYS A  82     1148   1412   1233     29     35    112       C  
ATOM    688  O   LYS A  82      -4.389   8.292  37.937  1.00  9.67           O  
ANISOU  688  O   LYS A  82     1014   1498   1161    -44    -38     62       O  
ATOM    689  CB  LYS A  82      -4.507   5.012  38.300  1.00 12.09           C  
ANISOU  689  CB  LYS A  82     1459   1671   1460    -51    125    126       C  
ATOM    690  CG  LYS A  82      -4.589   3.714  37.520  1.00 18.39           C  
ANISOU  690  CG  LYS A  82     2359   2225   2402     74     62    -27       C  
ATOM    691  CD  LYS A  82      -5.658   2.822  38.159  1.00 23.88           C  
ANISOU  691  CD  LYS A  82     2909   2862   3301   -175     78     17       C  
ATOM    692  CE  LYS A  82      -5.692   1.402  37.596  1.00 27.75           C  
ANISOU  692  CE  LYS A  82     3513   3211   3819    -47     63    -49       C  
ATOM    693  NZ  LYS A  82      -6.521   0.513  38.471  1.00 30.46           N  
ANISOU  693  NZ  LYS A  82     3746   3657   4167    -85    182     99       N  
ATOM    694  N   GLN A  83      -3.255   7.491  39.719  1.00  9.82           N  
ANISOU  694  N   GLN A  83     1264   1359   1105     58     89     57       N  
ATOM    695  CA  GLN A  83      -3.357   8.727  40.515  1.00 10.65           C  
ANISOU  695  CA  GLN A  83     1357   1418   1269      4    143    -14       C  
ATOM    696  C   GLN A  83      -2.674   9.887  39.871  1.00  9.69           C  
ANISOU  696  C   GLN A  83     1329   1334   1018     74     -6    -81       C  
ATOM    697  O   GLN A  83      -3.217  10.984  39.833  1.00 10.47           O  
ANISOU  697  O   GLN A  83     1255   1350   1373     90    -88   -137       O  
ATOM    698  CB  GLN A  83      -2.785   8.520  41.934  1.00 11.92           C  
ANISOU  698  CB  GLN A  83     1511   1627   1392     -5    165    -97       C  
ATOM    699  CG  GLN A  83      -3.608   7.590  42.816  1.00 11.92           C  
ANISOU  699  CG  GLN A  83     1467   1710   1352   -353    207   -159       C  
ATOM    700  CD  GLN A  83      -4.965   8.150  43.172  1.00 14.16           C  
ANISOU  700  CD  GLN A  83     1790   1838   1752   -174    424   -357       C  
ATOM    701  OE1 GLN A  83      -5.126   9.352  43.354  1.00 16.84           O  
ANISOU  701  OE1 GLN A  83     1998   1960   2439   -186    971   -677       O  
ATOM    702  NE2 GLN A  83      -5.960   7.276  43.249  1.00 14.09           N  
ANISOU  702  NE2 GLN A  83     1941   2098   1315   -446    508   -105       N  
ATOM    703  N   LEU A  84      -1.479   9.637  39.357  1.00  9.74           N  
ANISOU  703  N   LEU A  84     1211   1228   1259    114    -87   -296       N  
ATOM    704  CA  LEU A  84      -0.728  10.628  38.620  1.00 10.31           C  
ANISOU  704  CA  LEU A  84     1344   1181   1392     43    -52   -241       C  
ATOM    705  C   LEU A  84      -1.514  11.123  37.422  1.00 10.19           C  
ANISOU  705  C   LEU A  84     1315   1163   1391    -22     38    -93       C  
ATOM    706  O   LEU A  84      -1.629  12.321  37.205  1.00 11.34           O  
ANISOU  706  O   LEU A  84     1306   1230   1770     -1     44    -41       O  
ATOM    707  CB  LEU A  84       0.616  10.035  38.147  1.00 10.11           C  
ANISOU  707  CB  LEU A  84     1215   1256   1367    -45   -120   -276       C  
ATOM    708  CG  LEU A  84       1.562  10.888  37.289  1.00 11.64           C  
ANISOU  708  CG  LEU A  84     1354   1378   1688    -65     95   -443       C  
ATOM    709  CD1 LEU A  84       2.945  10.257  37.286  1.00 13.22           C  
ANISOU  709  CD1 LEU A  84     1251   1734   2036    -76    391   -761       C  
ATOM    710  CD2 LEU A  84       1.090  11.067  35.885  1.00 12.55           C  
ANISOU  710  CD2 LEU A  84     1606   1519   1643   -344    290   -160       C  
ATOM    711  N   VAL A  85      -2.071  10.202  36.643  1.00  9.92           N  
ANISOU  711  N   VAL A  85     1275   1177   1316    -47    -10    -21       N  
ATOM    712  CA  VAL A  85      -2.806  10.589  35.462  1.00 10.26           C  
ANISOU  712  CA  VAL A  85     1406   1302   1191   -193     17     94       C  
ATOM    713  C   VAL A  85      -4.018  11.436  35.847  1.00 10.52           C  
ANISOU  713  C   VAL A  85     1436   1342   1217    -96    -78    131       C  
ATOM    714  O   VAL A  85      -4.253  12.482  35.237  1.00 11.61           O  
ANISOU  714  O   VAL A  85     1472   1337   1600    -83    -15    266       O  
ATOM    715  CB  VAL A  85      -3.210   9.361  34.619  1.00 10.59           C  
ANISOU  715  CB  VAL A  85     1508   1423   1092   -124    -72      6       C  
ATOM    716  CG1 VAL A  85      -4.212   9.728  33.532  1.00 13.33           C  
ANISOU  716  CG1 VAL A  85     1752   1923   1386   -195   -178     21       C  
ATOM    717  CG2 VAL A  85      -1.987   8.727  33.992  1.00 12.09           C  
ANISOU  717  CG2 VAL A  85     1753   1591   1247   -177    110    -47       C  
ATOM    718  N   SER A  86      -4.745  11.051  36.891  1.00 10.96           N  
ANISOU  718  N   SER A  86     1429   1431   1303    -34   -121    127       N  
ATOM    719  CA  SER A  86      -5.895  11.838  37.312  1.00 11.72           C  
ANISOU  719  CA  SER A  86     1481   1561   1409     38    -86     94       C  
ATOM    720  C   SER A  86      -5.464  13.220  37.822  1.00 11.91           C  
ANISOU  720  C   SER A  86     1483   1504   1537    124    -96     73       C  
ATOM    721  O   SER A  86      -6.141  14.230  37.583  1.00 14.40           O  
ANISOU  721  O   SER A  86     1715   1719   2036    266   -218     90       O  
ATOM    722  CB  SER A  86      -6.660  11.095  38.385  1.00 12.49           C  
ANISOU  722  CB  SER A  86     1658   1596   1490    -29    -55     86       C  
ATOM    723  OG  SER A  86      -7.206   9.904  37.858  1.00 15.72           O  
ANISOU  723  OG  SER A  86     2034   2120   1816   -168    -30    -81       O  
ATOM    724  N   ASP A  87      -4.337  13.264  38.521  1.00 11.01           N  
ANISOU  724  N   ASP A  87     1344   1381   1456     75     39     97       N  
ATOM    725  CA  ASP A  87      -3.799  14.498  39.083  1.00 11.11           C  
ANISOU  725  CA  ASP A  87     1350   1422   1448     97     42     26       C  
ATOM    726  C   ASP A  87      -3.343  15.473  37.994  1.00 11.48           C  
ANISOU  726  C   ASP A  87     1518   1351   1491    193     34     95       C  
ATOM    727  O   ASP A  87      -3.589  16.687  38.088  1.00 13.83           O  
ANISOU  727  O   ASP A  87     2003   1467   1785    227    187    161       O  
ATOM    728  CB  ASP A  87      -2.613  14.141  40.006  1.00 10.40           C  
ANISOU  728  CB  ASP A  87     1307   1276   1369     64     36     -7       C  
ATOM    729  CG  ASP A  87      -2.095  15.317  40.842  1.00 10.37           C  
ANISOU  729  CG  ASP A  87     1486   1221   1232    130      7    -13       C  
ATOM    730  OD1 ASP A  87      -2.779  16.349  40.990  1.00 15.90           O  
ANISOU  730  OD1 ASP A  87     2064   1769   2207    435   -313   -183       O  
ATOM    731  OD2 ASP A  87      -0.963  15.167  41.364  1.00  9.80           O  
ANISOU  731  OD2 ASP A  87     1405   1205   1111     33    122     14       O  
ATOM    732  N   CYS A  88      -2.673  14.955  36.965  1.00 11.95           N  
ANISOU  732  N   CYS A  88     1514   1431   1595    -58    149     84       N  
ATOM    733  CA  CYS A  88      -1.944  15.789  36.009  1.00 11.63           C  
ANISOU  733  CA  CYS A  88     1514   1453   1449    -11     77    117       C  
ATOM    734  C   CYS A  88      -2.566  15.932  34.622  1.00 12.85           C  
ANISOU  734  C   CYS A  88     1671   1588   1622    -16     41    147       C  
ATOM    735  O   CYS A  88      -2.007  16.676  33.797  1.00 14.95           O  
ANISOU  735  O   CYS A  88     1862   1886   1932     56     30    349       O  
ATOM    736  CB  CYS A  88      -0.532  15.224  35.820  1.00 10.92           C  
ANISOU  736  CB  CYS A  88     1558   1355   1234   -139    204     69       C  
ATOM    737  SG  CYS A  88       0.498  15.108  37.289  1.00 10.56           S  
ANISOU  737  SG  CYS A  88     1330   1416   1264      4    -76    188       S  
ATOM    738  N   SER A  89      -3.710  15.292  34.335  1.00 13.80           N  
ANISOU  738  N   SER A  89     1711   1686   1843     39    -21     77       N  
ATOM    739  CA ASER A  89      -4.190  15.250  32.932  0.50 14.45           C  
ANISOU  739  CA ASER A  89     1805   1798   1885     37      0     48       C  
ATOM    740  CA BSER A  89      -4.261  15.207  32.956  0.50 13.86           C  
ANISOU  740  CA BSER A  89     1767   1713   1786     57    -19     57       C  
ATOM    741  C   SER A  89      -5.064  16.416  32.453  1.00 14.20           C  
ANISOU  741  C   SER A  89     1790   1779   1823     46     -9     39       C  
ATOM    742  O   SER A  89      -5.323  16.540  31.252  1.00 14.86           O  
ANISOU  742  O   SER A  89     1885   1755   2005     -4     58     60       O  
ATOM    743  CB ASER A  89      -4.942  13.956  32.654  0.50 15.05           C  
ANISOU  743  CB ASER A  89     1897   1870   1951     42    -40     18       C  
ATOM    744  CB BSER A  89      -5.158  13.960  32.803  0.50 14.15           C  
ANISOU  744  CB BSER A  89     1809   1750   1816     81    -54     23       C  
ATOM    745  OG ASER A  89      -6.146  13.945  33.374  0.50 16.72           O  
ANISOU  745  OG ASER A  89     1943   2154   2255    -34     72     39       O  
ATOM    746  OG BSER A  89      -4.398  12.775  32.608  0.50 12.64           O  
ANISOU  746  OG BSER A  89     1799   1598   1405    215   -145     84       O  
ATOM    747  N   THR A  90      -5.518  17.251  33.372  1.00 13.90           N  
ANISOU  747  N   THR A  90     1785   1660   1835     23     57     -1       N  
ATOM    748  CA  THR A  90      -6.417  18.345  33.031  1.00 14.28           C  
ANISOU  748  CA  THR A  90     1784   1688   1952      7     37    -11       C  
ATOM    749  C   THR A  90      -6.000  19.625  33.763  1.00 13.49           C  
ANISOU  749  C   THR A  90     1604   1607   1914    -43     -2    -31       C  
ATOM    750  O   THR A  90      -6.795  20.309  34.413  1.00 13.38           O  
ANISOU  750  O   THR A  90     1442   1627   2013      6     17     73       O  
ATOM    751  CB  THR A  90      -7.861  17.983  33.359  1.00 14.36           C  
ANISOU  751  CB  THR A  90     1776   1746   1933    -48     50    -50       C  
ATOM    752  OG1 THR A  90      -7.941  17.548  34.720  1.00 15.27           O  
ANISOU  752  OG1 THR A  90     1968   1851   1980     54    229    124       O  
ATOM    753  CG2 THR A  90      -8.367  16.873  32.427  1.00 15.76           C  
ANISOU  753  CG2 THR A  90     2151   1697   2139     64     13   -197       C  
ATOM    754  N   ILE A  91      -4.717  19.929  33.664  1.00 13.87           N  
ANISOU  754  N   ILE A  91     1583   1664   2023    -24     55   -105       N  
ATOM    755  CA  ILE A  91      -4.181  21.145  34.251  1.00 13.57           C  
ANISOU  755  CA  ILE A  91     1406   1751   1998   -110     76   -119       C  
ATOM    756  C   ILE A  91      -4.918  22.310  33.622  1.00 12.55           C  
ANISOU  756  C   ILE A  91     1187   1845   1735    -93     43    -22       C  
ATOM    757  O   ILE A  91      -5.155  22.382  32.391  1.00 13.97           O  
ANISOU  757  O   ILE A  91     1417   1986   1902    -62     -4    -41       O  
ATOM    758  CB  ILE A  91      -2.660  21.207  34.047  1.00 14.25           C  
ANISOU  758  CB  ILE A  91     1398   1876   2140      3    111   -193       C  
ATOM    759  CG1 ILE A  91      -2.001  20.116  34.879  1.00 15.43           C  
ANISOU  759  CG1 ILE A  91     1617   1852   2393     76    224   -213       C  
ATOM    760  CG2 ILE A  91      -2.085  22.562  34.423  1.00 15.40           C  
ANISOU  760  CG2 ILE A  91     1413   1979   2456   -215     37   -112       C  
ATOM    761  CD1 ILE A  91      -0.528  19.926  34.585  1.00 16.58           C  
ANISOU  761  CD1 ILE A  91     1403   2123   2773    152     66   -360       C  
ATOM    762  N   SER A  92      -5.289  23.258  34.444  1.00 11.84           N  
ANISOU  762  N   SER A  92     1275   1611   1611    -54     14     97       N  
ATOM    763  CA ASER A  92      -6.117  24.345  33.946  0.50 12.78           C  
ANISOU  763  CA ASER A  92     1500   1669   1685    -48     21     94       C  
ATOM    764  CA BSER A  92      -6.115  24.356  33.971  0.50 12.54           C  
ANISOU  764  CA BSER A  92     1485   1633   1645    -35     40    111       C  
ATOM    765  C   SER A  92      -5.207  25.406  33.340  1.00 12.41           C  
ANISOU  765  C   SER A  92     1459   1617   1637   -100     59     81       C  
ATOM    766  O   SER A  92      -4.843  26.348  34.013  1.00 14.74           O  
ANISOU  766  O   SER A  92     1763   1979   1856   -288    175     -2       O  
ATOM    767  CB ASER A  92      -6.996  24.917  35.060  0.50 13.40           C  
ANISOU  767  CB ASER A  92     1614   1740   1736    -51     56     87       C  
ATOM    768  CB BSER A  92      -6.924  24.949  35.134  0.50 13.13           C  
ANISOU  768  CB BSER A  92     1610   1700   1676    -29     60    101       C  
ATOM    769  OG ASER A  92      -6.212  25.335  36.160  0.50 15.10           O  
ANISOU  769  OG ASER A  92     1872   1941   1923    -53    -67    -72       O  
ATOM    770  OG BSER A  92      -7.823  23.999  35.687  0.50 13.13           O  
ANISOU  770  OG BSER A  92     1701   1637   1648     23    137     82       O  
ATOM    771  N   GLU A  93      -4.863  25.228  32.053  1.00 11.56           N  
ANISOU  771  N   GLU A  93     1316   1414   1659    -23     -8    130       N  
ATOM    772  CA  GLU A  93      -3.965  26.162  31.339  1.00 11.50           C  
ANISOU  772  CA  GLU A  93     1372   1386   1609     19     32     96       C  
ATOM    773  C   GLU A  93      -4.243  26.179  29.834  1.00 12.35           C  
ANISOU  773  C   GLU A  93     1530   1492   1668    139    -51    137       C  
ATOM    774  O   GLU A  93      -4.176  25.146  29.181  1.00 15.63           O  
ANISOU  774  O   GLU A  93     2214   1821   1901    354   -238     79       O  
ATOM    775  CB  GLU A  93      -2.495  25.753  31.606  1.00 11.65           C  
ANISOU  775  CB  GLU A  93     1282   1467   1675    -17    108     20       C  
ATOM    776  CG  GLU A  93      -1.483  26.648  30.943  1.00 11.61           C  
ANISOU  776  CG  GLU A  93     1240   1544   1626     17     58     84       C  
ATOM    777  CD  GLU A  93      -1.697  28.094  31.290  1.00 12.42           C  
ANISOU  777  CD  GLU A  93     1365   1683   1669      5    183      8       C  
ATOM    778  OE1 GLU A  93      -1.622  28.412  32.498  1.00 12.45           O  
ANISOU  778  OE1 GLU A  93     1563   1328   1838    320    208   -226       O  
ATOM    779  OE2 GLU A  93      -1.937  28.902  30.371  1.00 13.46           O  
ANISOU  779  OE2 GLU A  93     1643   1497   1975     96    238    -41       O  
ATOM    780  N   GLU A  94      -4.578  27.346  29.277  1.00 11.67           N  
ANISOU  780  N   GLU A  94     1154   1556   1724    124    199    205       N  
ATOM    781  CA  GLU A  94      -4.907  27.462  27.845  1.00 12.32           C  
ANISOU  781  CA  GLU A  94     1131   1839   1711     22    161    125       C  
ATOM    782  C   GLU A  94      -3.701  27.626  26.908  1.00 11.71           C  
ANISOU  782  C   GLU A  94     1093   1845   1511     -4    141     29       C  
ATOM    783  O   GLU A  94      -3.769  27.275  25.711  1.00 13.63           O  
ANISOU  783  O   GLU A  94     1211   2368   1599      3    -18    -70       O  
ATOM    784  CB  GLU A  94      -5.880  28.639  27.623  1.00 13.18           C  
ANISOU  784  CB  GLU A  94     1170   1957   1878    107    156    197       C  
ATOM    785  CG  GLU A  94      -7.154  28.565  28.474  1.00 16.43           C  
ANISOU  785  CG  GLU A  94     1433   2487   2321    157    229    121       C  
ATOM    786  CD  GLU A  94      -7.819  27.242  28.303  1.00 17.75           C  
ANISOU  786  CD  GLU A  94     1156   2986   2600     60    -91   -115       C  
ATOM    787  OE1 GLU A  94      -8.109  26.877  27.144  1.00 24.00           O  
ANISOU  787  OE1 GLU A  94     2325   4138   2655    174    -38   -286       O  
ATOM    788  OE2 GLU A  94      -8.001  26.538  29.304  1.00 17.60           O  
ANISOU  788  OE2 GLU A  94      921   3428   2337   -297    246   -220       O  
ATOM    789  N   ASN A  95      -2.619  28.175  27.442  1.00  9.77           N  
ANISOU  789  N   ASN A  95     1021   1355   1335     79     70    137       N  
ATOM    790  CA  ASN A  95      -1.422  28.436  26.666  1.00  9.26           C  
ANISOU  790  CA  ASN A  95     1171   1183   1163     63    140    105       C  
ATOM    791  C   ASN A  95      -0.660  27.122  26.561  1.00  8.06           C  
ANISOU  791  C   ASN A  95      834   1092   1137    102      6    139       C  
ATOM    792  O   ASN A  95      -0.237  26.581  27.603  1.00  8.43           O  
ANISOU  792  O   ASN A  95      956   1210   1035    218    190    141       O  
ATOM    793  CB  ASN A  95      -0.588  29.465  27.414  1.00  9.15           C  
ANISOU  793  CB  ASN A  95     1210   1092   1175    103     90     65       C  
ATOM    794  CG  ASN A  95       0.749  29.754  26.761  1.00 10.55           C  
ANISOU  794  CG  ASN A  95     1497   1112   1397   -149    350     29       C  
ATOM    795  OD1 ASN A  95       1.315  28.939  26.022  1.00 11.32           O  
ANISOU  795  OD1 ASN A  95     1569   1177   1553   -108    492    -48       O  
ATOM    796  ND2 ASN A  95       1.271  30.917  27.048  1.00 14.38           N  
ANISOU  796  ND2 ASN A  95     2037   1361   2062   -261    613   -505       N  
ATOM    797  N   PRO A  96      -0.506  26.564  25.341  1.00  8.97           N  
ANISOU  797  N   PRO A  96     1032   1183   1193     12    -52     86       N  
ATOM    798  CA  PRO A  96       0.105  25.239  25.247  1.00  8.89           C  
ANISOU  798  CA  PRO A  96      951   1209   1215     47     -6     42       C  
ATOM    799  C   PRO A  96       1.516  25.141  25.826  1.00  7.91           C  
ANISOU  799  C   PRO A  96      854   1080   1071    -36     -2     51       C  
ATOM    800  O   PRO A  96       1.924  24.080  26.285  1.00  7.42           O  
ANISOU  800  O   PRO A  96      835   1028    953    -74    -31     35       O  
ATOM    801  CB  PRO A  96       0.134  24.962  23.731  1.00 10.46           C  
ANISOU  801  CB  PRO A  96     1155   1433   1385    -13    -43    -71       C  
ATOM    802  CG  PRO A  96       0.103  26.291  23.113  1.00 12.40           C  
ANISOU  802  CG  PRO A  96     1492   1700   1520     91     50     -9       C  
ATOM    803  CD  PRO A  96      -0.854  27.071  24.000  1.00  9.77           C  
ANISOU  803  CD  PRO A  96     1120   1313   1279    185    -37    120       C  
ATOM    804  N   HIS A  97       2.273  26.232  25.767  1.00  7.20           N  
ANISOU  804  N   HIS A  97      795    908   1030     30    -32    101       N  
ATOM    805  CA  HIS A  97       3.643  26.215  26.277  1.00  7.34           C  
ANISOU  805  CA  HIS A  97      854    924   1008     15     53     91       C  
ATOM    806  C   HIS A  97       3.685  26.172  27.787  1.00  7.16           C  
ANISOU  806  C   HIS A  97      829    832   1057     34     -7    -57       C  
ATOM    807  O   HIS A  97       4.467  25.419  28.357  1.00  6.89           O  
ANISOU  807  O   HIS A  97      781    927    907     22     32     46       O  
ATOM    808  CB  HIS A  97       4.373  27.407  25.714  1.00  8.27           C  
ANISOU  808  CB  HIS A  97      853   1081   1207    -14      3     92       C  
ATOM    809  CG  HIS A  97       4.561  27.302  24.243  1.00 10.22           C  
ANISOU  809  CG  HIS A  97     1233   1330   1318    -75    241    243       C  
ATOM    810  ND1 HIS A  97       5.483  26.454  23.678  1.00 16.27           N  
ANISOU  810  ND1 HIS A  97     2303   2262   1617    199    309     38       N  
ATOM    811  CD2 HIS A  97       3.858  27.837  23.218  1.00 14.15           C  
ANISOU  811  CD2 HIS A  97     2042   1952   1381    401    206    -36       C  
ATOM    812  CE1 HIS A  97       5.409  26.554  22.362  1.00 15.78           C  
ANISOU  812  CE1 HIS A  97     2147   2534   1315     36    263   -249       C  
ATOM    813  NE2 HIS A  97       4.429  27.379  22.057  1.00 18.02           N  
ANISOU  813  NE2 HIS A  97     2890   2676   1278    166    284   -166       N  
ATOM    814  N   LEU A  98       2.830  26.953  28.436  1.00  7.64           N  
ANISOU  814  N   LEU A  98      952    925   1025    167     19    -55       N  
ATOM    815  CA  LEU A  98       2.705  26.887  29.884  1.00  8.62           C  
ANISOU  815  CA  LEU A  98     1072   1050   1153    257     57    -36       C  
ATOM    816  C   LEU A  98       2.093  25.560  30.337  1.00  8.34           C  
ANISOU  816  C   LEU A  98     1120   1082    966    278    142    -14       C  
ATOM    817  O   LEU A  98       2.459  25.036  31.417  1.00  9.14           O  
ANISOU  817  O   LEU A  98     1253   1293    925    326    120     -6       O  
ATOM    818  CB  LEU A  98       1.908  28.091  30.394  1.00 10.30           C  
ANISOU  818  CB  LEU A  98     1241   1283   1388    331    107    -54       C  
ATOM    819  CG  LEU A  98       1.849  28.366  31.893  1.00 13.20           C  
ANISOU  819  CG  LEU A  98     1747   1503   1763    317    248   -197       C  
ATOM    820  CD1 LEU A  98       3.187  28.307  32.565  1.00 15.27           C  
ANISOU  820  CD1 LEU A  98     1859   1989   1952    210    241   -334       C  
ATOM    821  CD2 LEU A  98       1.208  29.739  32.105  1.00 16.29           C  
ANISOU  821  CD2 LEU A  98     2046   1794   2347    519    353   -553       C  
ATOM    822  N   LYS A  99       1.194  24.993  29.533  1.00  8.10           N  
ANISOU  822  N   LYS A  99     1031    992   1055    234    148     75       N  
ATOM    823  CA  LYS A  99       0.676  23.691  29.869  1.00  8.66           C  
ANISOU  823  CA  LYS A  99     1067   1117   1105    147    140    118       C  
ATOM    824  C   LYS A  99       1.803  22.643  29.849  1.00  6.97           C  
ANISOU  824  C   LYS A  99      772    942    933     87    113     91       C  
ATOM    825  O   LYS A  99       1.829  21.732  30.674  1.00  7.12           O  
ANISOU  825  O   LYS A  99      795   1038    869     24    227    107       O  
ATOM    826  CB  LYS A  99      -0.420  23.270  28.917  1.00  9.25           C  
ANISOU  826  CB  LYS A  99      986   1208   1321    187     61    219       C  
ATOM    827  CG  LYS A  99      -1.054  21.987  29.375  1.00 13.73           C  
ANISOU  827  CG  LYS A  99     1628   1588   1999     26   -116    142       C  
ATOM    828  CD  LYS A  99      -2.544  21.931  29.096  1.00 18.70           C  
ANISOU  828  CD  LYS A  99     2047   2514   2541     17   -234     53       C  
ATOM    829  CE  LYS A  99      -3.245  20.945  30.033  1.00 22.41           C  
ANISOU  829  CE  LYS A  99     3021   2720   2773     30   -213    238       C  
ATOM    830  NZ  LYS A  99      -4.714  20.769  29.801  1.00 25.16           N  
ANISOU  830  NZ  LYS A  99     3342   3055   3161   -136   -113     30       N  
ATOM    831  N   ALA A 100       2.739  22.765  28.913  1.00  6.18           N  
ANISOU  831  N   ALA A 100      779    822    745     77     96     42       N  
ATOM    832  CA  ALA A 100       3.818  21.792  28.813  1.00  5.80           C  
ANISOU  832  CA  ALA A 100      736    743    723    -31     67      1       C  
ATOM    833  C   ALA A 100       4.724  21.846  30.044  1.00  5.20           C  
ANISOU  833  C   ALA A 100      609    711    656   -101     66     48       C  
ATOM    834  O   ALA A 100       5.075  20.808  30.612  1.00  5.23           O  
ANISOU  834  O   ALA A 100      567    698    720    -29     52    -72       O  
ATOM    835  CB  ALA A 100       4.629  22.021  27.532  1.00  6.01           C  
ANISOU  835  CB  ALA A 100      832    876    575    -13    227    -14       C  
ATOM    836  N   SER A 101       5.135  23.033  30.464  1.00  5.73           N  
ANISOU  836  N   SER A 101      698    706    770     23    -39     96       N  
ATOM    837  CA  SER A 101       5.944  23.131  31.659  1.00  5.86           C  
ANISOU  837  CA  SER A 101      754    662    809     37     42    -29       C  
ATOM    838  C   SER A 101       5.174  22.686  32.905  1.00  6.05           C  
ANISOU  838  C   SER A 101      649    788    861    -30    -57      1       C  
ATOM    839  O   SER A 101       5.730  22.005  33.763  1.00  6.24           O  
ANISOU  839  O   SER A 101      805    750    813     -4      3     57       O  
ATOM    840  CB  SER A 101       6.551  24.505  31.829  1.00  5.90           C  
ANISOU  840  CB  SER A 101      679    767    795     18     -1    -58       C  
ATOM    841  OG  SER A 101       5.557  25.497  31.902  1.00  6.70           O  
ANISOU  841  OG  SER A 101      759    796    991    136    -20     32       O  
ATOM    842  N   LYS A 102       3.890  23.028  32.997  1.00  6.49           N  
ANISOU  842  N   LYS A 102      745    888    830    104    -10    -11       N  
ATOM    843  CA  LYS A 102       3.109  22.597  34.144  1.00  6.70           C  
ANISOU  843  CA  LYS A 102      825    817    901     66     54     -6       C  
ATOM    844  C   LYS A 102       2.947  21.072  34.160  1.00  6.25           C  
ANISOU  844  C   LYS A 102      772    832    769     41     10     58       C  
ATOM    845  O   LYS A 102       2.901  20.485  35.259  1.00  6.87           O  
ANISOU  845  O   LYS A 102      893    964    752     74    117    109       O  
ATOM    846  CB  LYS A 102       1.759  23.317  34.177  1.00  7.14           C  
ANISOU  846  CB  LYS A 102      876    881    955    -16     78     22       C  
ATOM    847  CG  LYS A 102       1.892  24.776  34.577  1.00  8.55           C  
ANISOU  847  CG  LYS A 102     1202    958   1088     76     28    -24       C  
ATOM    848  CD  LYS A 102       0.538  25.493  34.518  1.00 10.03           C  
ANISOU  848  CD  LYS A 102     1176   1244   1388     51     37    -46       C  
ATOM    849  CE  LYS A 102       0.607  26.898  35.093  1.00 11.16           C  
ANISOU  849  CE  LYS A 102     1412   1338   1489    182     74   -181       C  
ATOM    850  NZ  LYS A 102      -0.726  27.598  35.129  1.00 13.43           N  
ANISOU  850  NZ  LYS A 102     1582   1661   1857    430   -301   -336       N  
ATOM    851  N   LEU A 103       2.804  20.452  32.996  1.00  6.52           N  
ANISOU  851  N   LEU A 103      846    813    815     34    -15     78       N  
ATOM    852  CA ALEU A 103       2.707  18.993  32.896  0.50  6.42           C  
ANISOU  852  CA ALEU A 103      774    799    866     40    -27     33       C  
ATOM    853  CA BLEU A 103       2.690  19.011  32.935  0.50  6.20           C  
ANISOU  853  CA BLEU A 103      744    778    834     39     -8     31       C  
ATOM    854  C   LEU A 103       3.982  18.330  33.418  1.00  6.06           C  
ANISOU  854  C   LEU A 103      750    824    728     10    -89    109       C  
ATOM    855  O   LEU A 103       3.914  17.413  34.248  1.00  6.18           O  
ANISOU  855  O   LEU A 103      782    754    811    -32    -37     81       O  
ATOM    856  CB ALEU A 103       2.422  18.531  31.462  0.50  7.04           C  
ANISOU  856  CB ALEU A 103      814    908    952     96   -111     72       C  
ATOM    857  CB BLEU A 103       2.311  18.573  31.535  0.50  6.59           C  
ANISOU  857  CB BLEU A 103      747    877    879     77    -56     84       C  
ATOM    858  CG ALEU A 103       0.965  18.599  31.012  0.50  8.03           C  
ANISOU  858  CG ALEU A 103      799   1049   1201     29    -66     50       C  
ATOM    859  CG BLEU A 103       2.085  17.088  31.349  0.50  6.49           C  
ANISOU  859  CG BLEU A 103      628    902    934     60     52     13       C  
ATOM    860  CD1ALEU A 103       0.855  18.456  29.500  0.50  8.41           C  
ANISOU  860  CD1ALEU A 103      872   1084   1237    189   -225     84       C  
ATOM    861  CD1BLEU A 103       1.079  16.544  32.354  0.50  8.30           C  
ANISOU  861  CD1BLEU A 103     1189    762   1201   -128     59    148       C  
ATOM    862  CD2ALEU A 103       0.153  17.522  31.728  0.50  9.35           C  
ANISOU  862  CD2ALEU A 103      771   1309   1470    -71    -66    181       C  
ATOM    863  CD2BLEU A 103       1.624  16.855  29.947  0.50  7.36           C  
ANISOU  863  CD2BLEU A 103      853   1054    888    -22    177   -107       C  
ATOM    864  N   VAL A 104       5.138  18.796  32.953  1.00  5.60           N  
ANISOU  864  N   VAL A 104      673    727    727     48   -141    101       N  
ATOM    865  CA  VAL A 104       6.379  18.223  33.443  1.00  5.78           C  
ANISOU  865  CA  VAL A 104      779    687    728     32    -58     51       C  
ATOM    866  C   VAL A 104       6.525  18.459  34.950  1.00  5.54           C  
ANISOU  866  C   VAL A 104      707    676    720     -6   -114     54       C  
ATOM    867  O   VAL A 104       6.990  17.572  35.680  1.00  6.21           O  
ANISOU  867  O   VAL A 104      756    721    879     19    -73     55       O  
ATOM    868  CB  VAL A 104       7.595  18.744  32.636  1.00  5.95           C  
ANISOU  868  CB  VAL A 104      743    699    815      1    -79    100       C  
ATOM    869  CG1 VAL A 104       8.905  18.362  33.319  1.00  6.82           C  
ANISOU  869  CG1 VAL A 104      877    823    889    -10   -135     -5       C  
ATOM    870  CG2 VAL A 104       7.530  18.196  31.207  1.00  6.99           C  
ANISOU  870  CG2 VAL A 104      861   1055    738     -5     -9      1       C  
ATOM    871  N   GLN A 105       6.125  19.628  35.444  1.00  5.96           N  
ANISOU  871  N   GLN A 105      838    711    714     68    -49     93       N  
ATOM    872  CA  GLN A 105       6.186  19.890  36.868  1.00  6.28           C  
ANISOU  872  CA  GLN A 105      706    852    827     19    -80    -32       C  
ATOM    873  C   GLN A 105       5.321  18.885  37.660  1.00  6.57           C  
ANISOU  873  C   GLN A 105      921    724    851     20   -125     38       C  
ATOM    874  O   GLN A 105       5.735  18.355  38.698  1.00  7.02           O  
ANISOU  874  O   GLN A 105      873    975    819     14    -70    -21       O  
ATOM    875  CB  GLN A 105       5.708  21.298  37.159  1.00  6.95           C  
ANISOU  875  CB  GLN A 105      948    833    857    -58     -8    -13       C  
ATOM    876  CG  GLN A 105       5.620  21.627  38.621  1.00  9.27           C  
ANISOU  876  CG  GLN A 105     1387   1119   1014     72    -31    -22       C  
ATOM    877  CD  GLN A 105       5.274  23.081  38.845  1.00 11.47           C  
ANISOU  877  CD  GLN A 105     1530   1296   1528    136     50   -221       C  
ATOM    878  OE1 GLN A 105       4.169  23.529  38.530  1.00 13.09           O  
ANISOU  878  OE1 GLN A 105     1561   1656   1756    323    332     63       O  
ATOM    879  NE2 GLN A 105       6.244  23.841  39.323  1.00 12.34           N  
ANISOU  879  NE2 GLN A 105     1627   1510   1551    -63    200   -369       N  
ATOM    880  N   CYS A 106       4.108  18.639  37.171  1.00  6.66           N  
ANISOU  880  N   CYS A 106      871    809    851    -14    -28     76       N  
ATOM    881  CA  CYS A 106       3.210  17.736  37.844  1.00  7.28           C  
ANISOU  881  CA  CYS A 106      896    915    955    -85     50     23       C  
ATOM    882  C   CYS A 106       3.760  16.303  37.874  1.00  6.19           C  
ANISOU  882  C   CYS A 106      766    853    732   -112    -85     52       C  
ATOM    883  O   CYS A 106       3.761  15.667  38.919  1.00  7.63           O  
ANISOU  883  O   CYS A 106     1115    916    866      7     86     87       O  
ATOM    884  CB  CYS A 106       1.851  17.793  37.153  1.00  7.19           C  
ANISOU  884  CB  CYS A 106      839    802   1089   -112     68     82       C  
ATOM    885  SG  CYS A 106       0.521  16.970  38.067  1.00 10.40           S  
ANISOU  885  SG  CYS A 106     1207   1489   1254   -126     91    166       S  
ATOM    886  N   VAL A 107       4.209  15.804  36.727  1.00  5.86           N  
ANISOU  886  N   VAL A 107      685    822    718    -31    -50     72       N  
ATOM    887  CA  VAL A 107       4.730  14.456  36.642  1.00  6.12           C  
ANISOU  887  CA  VAL A 107      881    811    633    -87    -98     26       C  
ATOM    888  C   VAL A 107       5.961  14.313  37.543  1.00  5.51           C  
ANISOU  888  C   VAL A 107      774    719    600      2    -84     39       C  
ATOM    889  O   VAL A 107       6.159  13.274  38.195  1.00  5.81           O  
ANISOU  889  O   VAL A 107      847    670    687    -26    -37    -14       O  
ATOM    890  CB  VAL A 107       5.070  14.071  35.197  1.00  7.25           C  
ANISOU  890  CB  VAL A 107     1115    858    782     50   -171     16       C  
ATOM    891  CG1 VAL A 107       5.759  12.741  35.124  1.00  9.05           C  
ANISOU  891  CG1 VAL A 107     1300   1017   1121    171    -98   -107       C  
ATOM    892  CG2 VAL A 107       3.819  14.094  34.326  1.00  8.73           C  
ANISOU  892  CG2 VAL A 107     1311   1194    811   -142   -414   -126       C  
ATOM    893  N   SER A 108       6.768  15.364  37.612  1.00  5.45           N  
ANISOU  893  N   SER A 108      725    664    680      8    -97     47       N  
ATOM    894  CA  SER A 108       8.003  15.348  38.389  1.00  5.47           C  
ANISOU  894  CA  SER A 108      684    654    738     54    -28     23       C  
ATOM    895  C   SER A 108       7.780  15.272  39.879  1.00  5.75           C  
ANISOU  895  C   SER A 108      748    681    754    -28    -35     70       C  
ATOM    896  O   SER A 108       8.700  14.874  40.573  1.00  6.55           O  
ANISOU  896  O   SER A 108      794    937    756     61    -77     85       O  
ATOM    897  CB  SER A 108       8.871  16.553  38.057  1.00  6.19           C  
ANISOU  897  CB  SER A 108      720    765    866      1    -77     25       C  
ATOM    898  OG  SER A 108       9.340  16.521  36.721  1.00  7.24           O  
ANISOU  898  OG  SER A 108      820    970    959     86     93    211       O  
ATOM    899  N   LYS A 109       6.567  15.525  40.371  1.00  6.17           N  
ANISOU  899  N   LYS A 109      834    784    724    -20    -27      6       N  
ATOM    900  CA  LYS A 109       6.247  15.273  41.770  1.00  7.07           C  
ANISOU  900  CA  LYS A 109      935   1009    741    -37     11    -60       C  
ATOM    901  C   LYS A 109       6.347  13.778  42.074  1.00  7.19           C  
ANISOU  901  C   LYS A 109      989   1071    670    -70     -5     41       C  
ATOM    902  O   LYS A 109       6.614  13.371  43.198  1.00  8.66           O  
ANISOU  902  O   LYS A 109     1370   1294    627   -184    -54     79       O  
ATOM    903  CB  LYS A 109       4.810  15.708  42.090  1.00  7.21           C  
ANISOU  903  CB  LYS A 109     1044   1026    667     16     25    -41       C  
ATOM    904  CG  LYS A 109       4.526  17.168  41.916  1.00  9.39           C  
ANISOU  904  CG  LYS A 109     1410   1168    990     55     58   -109       C  
ATOM    905  CD  LYS A 109       3.157  17.549  42.458  1.00 10.52           C  
ANISOU  905  CD  LYS A 109     1456   1332   1209    159     42   -145       C  
ATOM    906  CE  LYS A 109       2.040  16.716  41.843  1.00 11.28           C  
ANISOU  906  CE  LYS A 109     1350   1381   1553     50    158   -316       C  
ATOM    907  NZ  LYS A 109       0.669  17.226  42.198  1.00 11.25           N  
ANISOU  907  NZ  LYS A 109     1425   1348   1501    170    -17   -130       N  
ATOM    908  N   TYR A 110       6.083  12.951  41.074  1.00  6.38           N  
ANISOU  908  N   TYR A 110      885    839    700    -83     32      2       N  
ATOM    909  CA  TYR A 110       6.020  11.509  41.240  1.00  6.09           C  
ANISOU  909  CA  TYR A 110      894    779    640    -95     54     29       C  
ATOM    910  C   TYR A 110       7.407  10.898  41.033  1.00  6.42           C  
ANISOU  910  C   TYR A 110      827    840    772   -103    -28     -3       C  
ATOM    911  O   TYR A 110       7.910  10.172  41.894  1.00  8.04           O  
ANISOU  911  O   TYR A 110     1037   1006   1011     38     11    230       O  
ATOM    912  CB  TYR A 110       4.974  10.925  40.266  1.00  6.73           C  
ANISOU  912  CB  TYR A 110      918    912    724    -41     55     96       C  
ATOM    913  CG  TYR A 110       3.574  11.376  40.633  1.00  6.48           C  
ANISOU  913  CG  TYR A 110      799    813    848   -171     38     52       C  
ATOM    914  CD1 TYR A 110       2.734  10.561  41.372  1.00  7.06           C  
ANISOU  914  CD1 TYR A 110      748    915   1017    -99     20    189       C  
ATOM    915  CD2 TYR A 110       3.090  12.624  40.264  1.00  6.65           C  
ANISOU  915  CD2 TYR A 110      757    944    823    -61    148    -13       C  
ATOM    916  CE1 TYR A 110       1.473  11.000  41.752  1.00  7.93           C  
ANISOU  916  CE1 TYR A 110      814    949   1247   -170    233    275       C  
ATOM    917  CE2 TYR A 110       1.819  13.065  40.637  1.00  6.02           C  
ANISOU  917  CE2 TYR A 110      818    830    637    -60    -83     73       C  
ATOM    918  CZ  TYR A 110       1.024  12.247  41.407  1.00  7.30           C  
ANISOU  918  CZ  TYR A 110      723   1080    970    -91     68    130       C  
ATOM    919  OH  TYR A 110      -0.249  12.622  41.807  1.00  8.25           O  
ANISOU  919  OH  TYR A 110      922   1285    926    159    279     72       O  
ATOM    920  N   LYS A 111       8.044  11.192  39.900  1.00  5.96           N  
ANISOU  920  N   LYS A 111      703    843    719    -97    -11    -95       N  
ATOM    921  CA  LYS A 111       9.453  10.851  39.682  1.00  6.60           C  
ANISOU  921  CA  LYS A 111      779    825    902   -184    -35    -60       C  
ATOM    922  C   LYS A 111      10.058  11.966  38.867  1.00  5.71           C  
ANISOU  922  C   LYS A 111      683    739    745    -51     16   -119       C  
ATOM    923  O   LYS A 111       9.492  12.372  37.860  1.00  6.86           O  
ANISOU  923  O   LYS A 111      760   1021    822    -80    -63     61       O  
ATOM    924  CB  LYS A 111       9.633   9.545  38.872  1.00  8.46           C  
ANISOU  924  CB  LYS A 111     1051   1013   1148   -132     57   -123       C  
ATOM    925  CG  LYS A 111       9.191   8.245  39.504  1.00 11.66           C  
ANISOU  925  CG  LYS A 111     1327   1394   1709   -186     72    -57       C  
ATOM    926  CD  LYS A 111       9.992   7.873  40.731  1.00 13.63           C  
ANISOU  926  CD  LYS A 111     1799   1578   1802   -113    -40      7       C  
ATOM    927  CE  LYS A 111      11.477   7.649  40.490  1.00 13.39           C  
ANISOU  927  CE  LYS A 111     1826   1673   1589   -406    -75    -66       C  
ATOM    928  NZ  LYS A 111      12.096   7.059  41.740  1.00 14.56           N  
ANISOU  928  NZ  LYS A 111     2027   1780   1725    -69   -168     -3       N  
ATOM    929  N   THR A 112      11.235  12.428  39.263  1.00  5.77           N  
ANISOU  929  N   THR A 112      573    837    782    -38    -40     10       N  
ATOM    930  CA  THR A 112      11.963  13.381  38.441  1.00  5.59           C  
ANISOU  930  CA  THR A 112      584    736    801     19      2    -33       C  
ATOM    931  C   THR A 112      12.796  12.641  37.419  1.00  5.17           C  
ANISOU  931  C   THR A 112      519    715    729    -33      3    -22       C  
ATOM    932  O   THR A 112      13.142  11.475  37.608  1.00  5.76           O  
ANISOU  932  O   THR A 112      761    681    745     33    -34      9       O  
ATOM    933  CB  THR A 112      12.871  14.259  39.292  1.00  5.82           C  
ANISOU  933  CB  THR A 112      574    827    808    -30    -58     -9       C  
ATOM    934  OG1 THR A 112      13.949  13.467  39.786  1.00  6.24           O  
ANISOU  934  OG1 THR A 112      668    794    909     30     42      7       O  
ATOM    935  CG2 THR A 112      12.104  14.949  40.419  1.00  6.54           C  
ANISOU  935  CG2 THR A 112      818    818    848     27    -17   -222       C  
ATOM    936  N   MET A 113      13.174  13.307  36.331  1.00  5.18           N  
ANISOU  936  N   MET A 113      569    713    685     85     38     55       N  
ATOM    937  CA  MET A 113      14.039  12.656  35.358  1.00  5.17           C  
ANISOU  937  CA  MET A 113      655    673    634     -4    -20    -79       C  
ATOM    938  C   MET A 113      15.381  12.294  35.997  1.00  5.09           C  
ANISOU  938  C   MET A 113      620    658    656     28    -41      7       C  
ATOM    939  O   MET A 113      15.920  11.220  35.742  1.00  5.44           O  
ANISOU  939  O   MET A 113      701    601    764    110    171      7       O  
ATOM    940  CB  MET A 113      14.249  13.525  34.127  1.00  5.42           C  
ANISOU  940  CB  MET A 113      767    617    674    -76     -6    -23       C  
ATOM    941  CG  MET A 113      12.992  13.631  33.276  1.00  5.66           C  
ANISOU  941  CG  MET A 113      674    828    647    -74     17   -166       C  
ATOM    942  SD  MET A 113      13.223  14.446  31.690  1.00  6.73           S  
ANISOU  942  SD  MET A 113      963    828    764    -60   -150    -32       S  
ATOM    943  CE  MET A 113      13.161  16.084  32.237  1.00  8.55           C  
ANISOU  943  CE  MET A 113     1363   1127    756   -327   -252   -103       C  
ATOM    944  N   LYS A 114      15.912  13.147  36.877  1.00  5.37           N  
ANISOU  944  N   LYS A 114      652    675    710     63    -29    -41       N  
ATOM    945  CA ALYS A 114      17.199  12.847  37.477  0.50  6.36           C  
ANISOU  945  CA ALYS A 114      713    810    894     24    -21     46       C  
ATOM    946  CA BLYS A 114      17.189  12.890  37.533  0.50  6.14           C  
ANISOU  946  CA BLYS A 114      665    774    891     42    -19     29       C  
ATOM    947  C   LYS A 114      17.112  11.601  38.325  1.00  6.24           C  
ANISOU  947  C   LYS A 114      718    781    872     10    -26     67       C  
ATOM    948  O   LYS A 114      18.050  10.799  38.373  1.00  6.82           O  
ANISOU  948  O   LYS A 114      751    880    961    121     -9     52       O  
ATOM    949  CB ALYS A 114      17.669  14.003  38.350  0.50  6.52           C  
ANISOU  949  CB ALYS A 114      804    865    807    -72     -6     63       C  
ATOM    950  CB BLYS A 114      17.513  14.057  38.485  0.50  6.06           C  
ANISOU  950  CB BLYS A 114      693    774    834    -45    -43     55       C  
ATOM    951  CG ALYS A 114      18.990  13.745  39.073  0.50  8.55           C  
ANISOU  951  CG ALYS A 114     1030   1125   1093     42   -112    180       C  
ATOM    952  CG BLYS A 114      18.841  13.952  39.268  0.50  7.39           C  
ANISOU  952  CG BLYS A 114      784    927   1097    167    -93    -50       C  
ATOM    953  CD ALYS A 114      19.480  15.015  39.699  0.50 10.46           C  
ANISOU  953  CD ALYS A 114     1235   1455   1282    -54    -36     70       C  
ATOM    954  CD BLYS A 114      20.047  13.958  38.318  0.50 10.90           C  
ANISOU  954  CD BLYS A 114     1138   1567   1434     65    -86   -170       C  
ATOM    955  CE ALYS A 114      20.749  14.866  40.485  0.50 11.71           C  
ANISOU  955  CE ALYS A 114     1342   1594   1511    -69   -111     44       C  
ATOM    956  CE BLYS A 114      21.371  14.271  39.023  0.50 13.54           C  
ANISOU  956  CE BLYS A 114     1430   1885   1827    -60   -178   -141       C  
ATOM    957  NZ ALYS A 114      21.160  16.195  41.010  0.50  9.70           N  
ANISOU  957  NZ ALYS A 114     1110   1468   1104   -113     -2     68       N  
ATOM    958  NZ BLYS A 114      22.473  14.419  38.031  0.50 15.72           N  
ANISOU  958  NZ BLYS A 114     1861   2138   1972   -247    -62   -257       N  
ATOM    959  N   SER A 115      15.990  11.420  38.995  1.00  6.20           N  
ANISOU  959  N   SER A 115      749    787    819     31     -4    128       N  
ATOM    960  CA ASER A 115      15.881  10.299  39.930  0.50  6.14           C  
ANISOU  960  CA ASER A 115      783    814    734    -47     26    149       C  
ATOM    961  CA BSER A 115      15.849  10.290  39.918  0.50  6.91           C  
ANISOU  961  CA BSER A 115      878    906    841    -24     16    139       C  
ATOM    962  C   SER A 115      15.924   8.950  39.218  1.00  6.89           C  
ANISOU  962  C   SER A 115      949    853    815    -38     70    152       C  
ATOM    963  O   SER A 115      16.323   7.946  39.816  1.00  7.62           O  
ANISOU  963  O   SER A 115     1118    927    848    144     30    246       O  
ATOM    964  CB ASER A 115      14.629  10.417  40.799  0.50  6.71           C  
ANISOU  964  CB ASER A 115      784    915    850    -31     72    113       C  
ATOM    965  CB BSER A 115      14.544  10.386  40.699  0.50  7.86           C  
ANISOU  965  CB BSER A 115      914   1078    993     -2     76    151       C  
ATOM    966  OG ASER A 115      13.454  10.248  40.030  0.50  6.42           O  
ANISOU  966  OG ASER A 115      801    839    798   -208     77    245       O  
ATOM    967  OG BSER A 115      14.644  11.407  41.665  0.50 11.40           O  
ANISOU  967  OG BSER A 115     1354   1480   1495    -10    -22     35       O  
ATOM    968  N   VAL A 116      15.572   8.923  37.934  1.00  7.37           N  
ANISOU  968  N   VAL A 116     1036    889    874   -111   -145    111       N  
ATOM    969  CA  VAL A 116      15.611   7.695  37.163  1.00  8.13           C  
ANISOU  969  CA  VAL A 116     1183    965    937   -107    -89    107       C  
ATOM    970  C   VAL A 116      17.035   7.170  37.088  1.00  8.44           C  
ANISOU  970  C   VAL A 116     1308   1047    852     16    -90     98       C  
ATOM    971  O   VAL A 116      17.255   5.963  37.053  1.00  9.69           O  
ANISOU  971  O   VAL A 116     1572   1011   1097     -1    -79    -88       O  
ATOM    972  CB  VAL A 116      15.019   7.879  35.752  1.00  7.84           C  
ANISOU  972  CB  VAL A 116     1130    871    977   -157    -98    120       C  
ATOM    973  CG1 VAL A 116      15.091   6.573  34.963  1.00  9.13           C  
ANISOU  973  CG1 VAL A 116     1131   1216   1121   -265   -173    -11       C  
ATOM    974  CG2 VAL A 116      13.590   8.291  35.875  1.00  8.84           C  
ANISOU  974  CG2 VAL A 116     1058   1103   1198   -351    -80     35       C  
ATOM    975  N   ASP A 117      18.015   8.064  37.059  1.00  9.18           N  
ANISOU  975  N   ASP A 117     1281   1173   1033     65      6    -18       N  
ATOM    976  CA  ASP A 117      19.416   7.639  36.959  1.00 11.11           C  
ANISOU  976  CA  ASP A 117     1385   1437   1397     76     44    -97       C  
ATOM    977  C   ASP A 117      19.945   6.846  38.126  1.00 12.68           C  
ANISOU  977  C   ASP A 117     1483   1696   1636    146    -54    -79       C  
ATOM    978  O   ASP A 117      20.959   6.160  38.004  1.00 14.24           O  
ANISOU  978  O   ASP A 117     1481   1875   2055    396     -3    -94       O  
ATOM    979  CB  ASP A 117      20.311   8.844  36.776  1.00 11.62           C  
ANISOU  979  CB  ASP A 117     1331   1516   1566     69    113   -167       C  
ATOM    980  CG  ASP A 117      20.393   9.270  35.357  1.00 12.49           C  
ANISOU  980  CG  ASP A 117     1443   1523   1776      0   -164    135       C  
ATOM    981  OD1 ASP A 117      20.049   8.462  34.466  1.00 15.75           O  
ANISOU  981  OD1 ASP A 117     2158   2166   1657   -241   -244     18       O  
ATOM    982  OD2 ASP A 117      20.836  10.393  35.121  1.00 15.94           O  
ANISOU  982  OD2 ASP A 117     1668   1787   2600    251    -80    354       O  
ATOM    983  N   PHE A 118      19.283   6.927  39.268  1.00 12.26           N  
ANISOU  983  N   PHE A 118     1589   1626   1443    142   -148    -34       N  
ATOM    984  CA  PHE A 118      19.764   6.224  40.455  1.00 13.25           C  
ANISOU  984  CA  PHE A 118     1810   1755   1468     77   -294    -20       C  
ATOM    985  C   PHE A 118      19.222   4.794  40.520  1.00 14.35           C  
ANISOU  985  C   PHE A 118     2003   1818   1628     35   -236      8       C  
ATOM    986  O   PHE A 118      19.624   4.000  41.365  1.00 16.47           O  
ANISOU  986  O   PHE A 118     2370   1890   1995    109   -375     76       O  
ATOM    987  CB  PHE A 118      19.350   6.980  41.712  1.00 12.47           C  
ANISOU  987  CB  PHE A 118     1798   1663   1277    113   -240      3       C  
ATOM    988  CG  PHE A 118      19.833   8.429  41.795  1.00 13.24           C  
ANISOU  988  CG  PHE A 118     1769   1781   1479    188   -298     56       C  
ATOM    989  CD1 PHE A 118      21.173   8.741  41.902  1.00 13.58           C  
ANISOU  989  CD1 PHE A 118     1759   1861   1537    197   -151    292       C  
ATOM    990  CD2 PHE A 118      18.918   9.466  41.865  1.00 12.75           C  
ANISOU  990  CD2 PHE A 118     1795   1702   1346    245   -535     15       C  
ATOM    991  CE1 PHE A 118      21.591  10.028  42.054  1.00 14.92           C  
ANISOU  991  CE1 PHE A 118     1832   2062   1772     92   -184    346       C  
ATOM    992  CE2 PHE A 118      19.321  10.780  41.980  1.00 12.57           C  
ANISOU  992  CE2 PHE A 118     1834   1706   1235    271    -74    221       C  
ATOM    993  CZ  PHE A 118      20.655  11.070  42.080  1.00 14.25           C  
ANISOU  993  CZ  PHE A 118     2029   1571   1815    -26   -131    304       C  
ATOM    994  N   LEU A 119      18.313   4.443  39.623  1.00 15.24           N  
ANISOU  994  N   LEU A 119     2109   1907   1773     25   -250     16       N  
ATOM    995  CA  LEU A 119      17.624   3.163  39.715  1.00 16.59           C  
ANISOU  995  CA  LEU A 119     2211   2001   2090      7    -50      4       C  
ATOM    996  C   LEU A 119      18.398   1.986  39.116  1.00 18.30           C  
ANISOU  996  C   LEU A 119     2483   2101   2367     22     42     40       C  
ATOM    997  O   LEU A 119      19.328   2.146  38.321  1.00 19.97           O  
ANISOU  997  O   LEU A 119     2494   2316   2776    107    126      9       O  
ATOM    998  CB  LEU A 119      16.237   3.289  39.078  1.00 15.82           C  
ANISOU  998  CB  LEU A 119     2192   1870   1949    -39   -101    -13       C  
ATOM    999  CG  LEU A 119      15.319   4.257  39.837  1.00 15.62           C  
ANISOU  999  CG  LEU A 119     2266   1746   1922    -12     16    109       C  
ATOM   1000  CD1 LEU A 119      13.971   4.354  39.183  1.00 16.47           C  
ANISOU 1000  CD1 LEU A 119     2130   1889   2237   -313    124    143       C  
ATOM   1001  CD2 LEU A 119      15.184   3.842  41.311  1.00 17.01           C  
ANISOU 1001  CD2 LEU A 119     2681   1710   2070     47    197    262       C  
ATOM   1002  OXT LEU A 119      18.102   0.833  39.456  1.00 20.50           O  
ANISOU 1002  OXT LEU A 119     2730   2320   2737    -17    118     51       O  
TER    1003      LEU A 119                                                      
HETATM 1004  O   HOH A 120      -5.185   5.836  34.241  1.00 23.55           O  
ANISOU 1004  O   HOH A 120     3252   1843   3853   1859   -906    513       O  
HETATM 1005  O   HOH A 121      10.688  23.387  43.047  1.00 65.22           O  
ANISOU 1005  O   HOH A 121     9080   6707   8993  -2033   2424  -2296       O  
HETATM 1006  O   HOH A 122       2.449  24.222  41.772  1.00 54.52           O  
ANISOU 1006  O   HOH A 122    10253   4190   6273   2797   3086   1188       O  
HETATM 1007  O   HOH A 123      19.834  -0.016  36.852  1.00 51.40           O  
ANISOU 1007  O   HOH A 123     9318   4857   5352   -212     90  -2078       O  
HETATM 1008  O   HOH A 124      -6.800   8.494  31.134  1.00 31.39           O  
ANISOU 1008  O   HOH A 124     2529   4946   4451   -556  -1132   -558       O  
HETATM 1009  O   HOH A 125       0.399  24.060  19.214  1.00 83.81           O  
ANISOU 1009  O   HOH A 125     8687  15737   7420  -5144  -1084   1135       O  
HETATM 1010  O   HOH A 126      -1.191  27.702  19.487  1.00 15.21           O  
ANISOU 1010  O   HOH A 126     2174   1980   1623    229    514  -1278       O  
HETATM 1011  O   HOH A 127      21.533   3.020  31.002  1.00 23.59           O  
ANISOU 1011  O   HOH A 127     1930   3793   3239    275   -196    329       O  
HETATM 1012  O   HOH A 128      16.557  -5.072  25.862  1.00 13.33           O  
ANISOU 1012  O   HOH A 128     1453   1481   2128   -191   -214   -267       O  
HETATM 1013  O   HOH A 129      22.011  14.203  27.708  1.00 18.40           O  
ANISOU 1013  O   HOH A 129     1756   2447   2785   -570    -15   -743       O  
HETATM 1014  O   HOH A 130       6.790  14.947  45.372  1.00 28.46           O  
ANISOU 1014  O   HOH A 130     4681   3690   2440   -731   -689  -1030       O  
HETATM 1015  O   HOH A 131      -5.069  17.892  36.071  1.00 21.44           O  
ANISOU 1015  O   HOH A 131     2748   2681   2716    861    -24    730       O  
HETATM 1016  O   HOH A 132      -4.630  18.250  29.370  1.00 62.99           O  
ANISOU 1016  O   HOH A 132     5018   9082   9833   -489    281  -3004       O  
HETATM 1017  O   HOH A 133      -7.164  15.011  35.204  1.00 28.66           O  
ANISOU 1017  O   HOH A 133     4859   2474   3556    289  -1811     93       O  
HETATM 1018  O   HOH A 134      18.713  -2.817  29.053  1.00 37.21           O  
ANISOU 1018  O   HOH A 134     4619   3519   5997    568  -1483  -1147       O  
HETATM 1019  O   HOH A 135      22.098  34.729  31.835  1.00 40.09           O  
ANISOU 1019  O   HOH A 135     3288   6509   5433    605    832   -532       O  
HETATM 1020  O   HOH A 136      -0.043  23.409  37.728  1.00 32.78           O  
ANISOU 1020  O   HOH A 136     3787   5102   3565   1822   -255   -480       O  
HETATM 1021  O   HOH A 137      22.800   1.866  26.184  1.00 49.24           O  
ANISOU 1021  O   HOH A 137     8582   4441   5683   -639  -1025   -211       O  
HETATM 1022  O   HOH A 138      23.430  20.314  39.004  1.00 42.63           O  
ANISOU 1022  O   HOH A 138     6783   5373   4039   2417   -263   -700       O  
HETATM 1023  O   HOH A 139      27.141   4.343  26.186  1.00 32.45           O  
ANISOU 1023  O   HOH A 139     3448   4097   4783   -857  -1747  -1712       O  
HETATM 1024  O   HOH A 140       8.450  12.172  29.676  1.00 34.64           O  
ANISOU 1024  O   HOH A 140     3710   4941   4510   -180    911    818       O  
HETATM 1025  O   HOH A 141       8.345  -1.819  38.459  1.00 41.72           O  
ANISOU 1025  O   HOH A 141     3840   7728   4281  -1158    486  -2629       O  
HETATM 1026  O   HOH A 142      21.726   2.168  40.797  1.00 29.64           O  
ANISOU 1026  O   HOH A 142     4627   3128   3507   1465    -40    -58       O  
HETATM 1027  O   HOH A 143      21.160  11.078  39.027  1.00 31.98           O  
ANISOU 1027  O   HOH A 143     4806   4698   2644    310   -435    467       O  
HETATM 1028  O   HOH A 144      20.094  17.787  36.788  1.00 19.88           O  
ANISOU 1028  O   HOH A 144     2616   2837   2097   -391   -404    719       O  
HETATM 1029  O   HOH A 145      22.810  22.538  37.762  1.00 25.99           O  
ANISOU 1029  O   HOH A 145     3681   3460   2731   -500  -1681   -467       O  
HETATM 1030  O   HOH A 146      21.111  17.102  34.968  1.00 22.19           O  
ANISOU 1030  O   HOH A 146     4184   1520   2725   -377   -781    174       O  
HETATM 1031  O   HOH A 147      13.889  26.431  38.794  1.00 23.19           O  
ANISOU 1031  O   HOH A 147     3105   3021   2683    265    -63   -269       O  
HETATM 1032  O   HOH A 148       9.413   8.851  19.430  1.00 33.99           O  
ANISOU 1032  O   HOH A 148     3463   6860   2590    694    110    394       O  
HETATM 1033  O   HOH A 149      -6.717  21.605  37.125  1.00 32.94           O  
ANISOU 1033  O   HOH A 149     4728   4353   3432  -1614   -416    471       O  
HETATM 1034  O   HOH A 150      -5.292  17.910  24.466  1.00 28.88           O  
ANISOU 1034  O   HOH A 150     3361   3653   3955    689   1657    259       O  
HETATM 1035  O   HOH A 151      21.144  21.061  42.159  1.00 34.27           O  
ANISOU 1035  O   HOH A 151     4352   4954   3712   -613     93    578       O  
HETATM 1036  O   HOH A 152       1.784  21.016  44.038  1.00 28.56           O  
ANISOU 1036  O   HOH A 152     4872   3560   2418   -149   1041     80       O  
HETATM 1037  O   HOH A 153      -8.958  13.058  34.340  1.00 30.20           O  
ANISOU 1037  O   HOH A 153     2207   2720   6548    316   -298     25       O  
HETATM 1038  O   HOH A 154      -6.252  19.468  14.299  1.00 26.02           O  
ANISOU 1038  O   HOH A 154     2989   2103   4794    358   -382    177       O  
HETATM 1039  O   HOH A 155      -3.096  24.050  26.656  1.00 43.58           O  
ANISOU 1039  O   HOH A 155     3984   7187   5388  -1113   -935   -534       O  
HETATM 1040  O   HOH A 156      23.023  31.821  30.900  1.00 31.02           O  
ANISOU 1040  O   HOH A 156     2821   3505   5460   -319  -1039    336       O  
HETATM 1041  O   HOH A 157      21.607  24.012  40.956  1.00 37.15           O  
ANISOU 1041  O   HOH A 157     4585   5311   4219    546  -1677   -328       O  
HETATM 1042  O   HOH A 158       3.133  -2.819  30.078  1.00 28.83           O  
ANISOU 1042  O   HOH A 158     4165   3111   3677   1320  -1961   -414       O  
HETATM 1043  O   HOH A 159       2.739  25.831  38.585  1.00 51.44           O  
ANISOU 1043  O   HOH A 159     6629   6971   5942    692  -1156   1790       O  
HETATM 1044  O   HOH A 160       7.541   4.879  24.929  1.00 55.86           O  
ANISOU 1044  O   HOH A 160     6056   6434   8733   1046   2923   -542       O  
HETATM 1045  O   HOH A 161       0.529  20.368  12.355  1.00 42.49           O  
ANISOU 1045  O   HOH A 161     7219   4097   4826  -1294   1441     -8       O  
HETATM 1046  O   HOH A 162      24.470  16.004  24.534  1.00 45.42           O  
ANISOU 1046  O   HOH A 162     1372   7174   8711   -942      7   -655       O  
HETATM 1047  O   HOH A 163      10.933   4.324  41.639  1.00 24.66           O  
ANISOU 1047  O   HOH A 163     3675   1245   4448   -324  -1629    863       O  
HETATM 1048  O   HOH A 164      24.851  18.060  22.332  1.00 35.29           O  
ANISOU 1048  O   HOH A 164     1935   6188   5284    755    604   -612       O  
HETATM 1049  O   HOH A 165       4.696  -2.763  41.513  1.00 33.52           O  
ANISOU 1049  O   HOH A 165     3977   6924   1832   2299   -314    -74       O  
HETATM 1050  O   HOH A 166       5.734  -2.495  32.332  1.00 30.89           O  
ANISOU 1050  O   HOH A 166     4014   4327   3395    645  -1744   -645       O  
HETATM 1051  O   HOH A 167      -4.625  25.175  24.255  1.00 29.72           O  
ANISOU 1051  O   HOH A 167     4304   2693   4294  -1007   -486  -1093       O  
HETATM 1052  O   HOH A 168      13.066  -2.719  36.539  1.00 25.79           O  
ANISOU 1052  O   HOH A 168     3731   2874   3195    -49   1058   -393       O  
HETATM 1053  O   HOH A 169       0.486  30.468  35.605  1.00 47.34           O  
ANISOU 1053  O   HOH A 169     7567   3343   7076    441  -1444  -1296       O  
HETATM 1054  O   HOH A 170      19.436   6.663  23.039  1.00  6.95           O  
ANISOU 1054  O   HOH A 170      737    804   1099     81   -232   -117       O  
HETATM 1055  O   HOH A 171       8.748  14.389  33.900  1.00 31.33           O  
ANISOU 1055  O   HOH A 171     3536   4629   3736  -2913    488  -1401       O  
HETATM 1056  O   HOH A 172       9.595  12.411  34.507  1.00 21.83           O  
ANISOU 1056  O   HOH A 172     1602   4192   2499  -1171   -861   1350       O  
HETATM 1057  O   HOH A 173      10.360  10.678  34.777  1.00 23.35           O  
ANISOU 1057  O   HOH A 173     2104   3061   3706   -522    592  -1945       O  
HETATM 1058  O   HOH A 174      10.137  11.613  32.325  1.00 26.18           O  
ANISOU 1058  O   HOH A 174     1946   3706   4292   -980   1125  -1315       O  
HETATM 1059  O   HOH A 175       9.287  13.584  31.679  1.00 39.16           O  
ANISOU 1059  O   HOH A 175     5422   5189   4269  -1921    -68    303       O  
HETATM 1060  O   HOH A 176      19.256  18.741  28.529  1.00  7.62           O  
ANISOU 1060  O   HOH A 176     1038    860    997    -22    -45   -192       O  
HETATM 1061  O   HOH A 177      12.034  15.932  35.974  1.00  6.28           O  
ANISOU 1061  O   HOH A 177      771    805    811     38     31     48       O  
HETATM 1062  O   HOH A 178       9.372  22.696  22.075  1.00  7.69           O  
ANISOU 1062  O   HOH A 178      915   1293    714    -52    105    173       O  
HETATM 1063  O   HOH A 179      15.567  14.960  41.294  1.00  7.84           O  
ANISOU 1063  O   HOH A 179     1020   1179    776     -1   -119    -58       O  
HETATM 1064  O   HOH A 180      11.036  23.687  20.219  1.00  7.26           O  
ANISOU 1064  O   HOH A 180      794    936   1028   -208    160     67       O  
HETATM 1065  O   HOH A 181      17.862  29.257  28.702  1.00  9.65           O  
ANISOU 1065  O   HOH A 181     1150   1220   1295    211     59   -239       O  
HETATM 1066  O   HOH A 182      13.225  25.114  35.416  1.00  9.44           O  
ANISOU 1066  O   HOH A 182     1296   1052   1236    266   -206    -20       O  
HETATM 1067  O   HOH A 183      17.398  11.599  33.424  1.00  7.61           O  
ANISOU 1067  O   HOH A 183      912   1183    794    172     22     78       O  
HETATM 1068  O   HOH A 184      14.866   7.268  42.112  1.00 10.48           O  
ANISOU 1068  O   HOH A 184     1004   1521   1454   -272   -126    304       O  
HETATM 1069  O   HOH A 185       1.178  21.557  25.391  1.00 13.37           O  
ANISOU 1069  O   HOH A 185     1763   1399   1916   -358    299    -13       O  
HETATM 1070  O   HOH A 186       7.340  19.496  40.515  1.00 13.29           O  
ANISOU 1070  O   HOH A 186     1597   1660   1791    -76   -395   -182       O  
HETATM 1071  O   HOH A 187      18.300   9.153  32.646  1.00 11.45           O  
ANISOU 1071  O   HOH A 187     1750   1316   1285    215   -130   -277       O  
HETATM 1072  O   HOH A 188       2.129  21.865  37.553  1.00 12.36           O  
ANISOU 1072  O   HOH A 188     1589   1785   1320    169    159   -376       O  
HETATM 1073  O   HOH A 189      12.104  10.879  19.715  1.00 12.62           O  
ANISOU 1073  O   HOH A 189     1816   1534   1441    218   -385     15       O  
HETATM 1074  O   HOH A 190      15.511  30.507  29.479  1.00 11.00           O  
ANISOU 1074  O   HOH A 190      829   1329   2019     55     29   -454       O  
HETATM 1075  O   HOH A 191      24.059  26.875  32.011  1.00 13.31           O  
ANISOU 1075  O   HOH A 191     1133   2126   1797   -470    -45    282       O  
HETATM 1076  O   HOH A 192      15.767  19.332  43.753  1.00 11.97           O  
ANISOU 1076  O   HOH A 192     1538   1484   1526    404   -144    443       O  
HETATM 1077  O   HOH A 193       9.242  20.334  20.305  1.00 16.97           O  
ANISOU 1077  O   HOH A 193     2806   1624   2018   -239   -978    331       O  
HETATM 1078  O   HOH A 194       6.771  25.280  20.193  1.00 13.66           O  
ANISOU 1078  O   HOH A 194     1454   2130   1604    330     52    546       O  
HETATM 1079  O   HOH A 195      22.654  18.870  23.887  1.00 15.50           O  
ANISOU 1079  O   HOH A 195     1364   2073   2451   -248   -124    103       O  
HETATM 1080  O   HOH A 196      23.213   6.307  24.295  1.00 12.34           O  
ANISOU 1080  O   HOH A 196     1229   1804   1656   -163    -49   -364       O  
HETATM 1081  O   HOH A 197       4.749  14.360  19.128  1.00 15.87           O  
ANISOU 1081  O   HOH A 197     1430   2614   1983    134   -291   -701       O  
HETATM 1082  O   HOH A 198      -5.056  11.713  41.877  1.00 13.68           O  
ANISOU 1082  O   HOH A 198     1548   2172   1479    140     39    -55       O  
HETATM 1083  O   HOH A 199       8.785  22.320  40.013  1.00 12.67           O  
ANISOU 1083  O   HOH A 199     1497   1819   1497    153    231    147       O  
HETATM 1084  O   HOH A 200      22.024   8.364  25.863  1.00 16.54           O  
ANISOU 1084  O   HOH A 200     1639   2239   2407    691   -481   -546       O  
HETATM 1085  O   HOH A 201      21.676  28.714  26.281  1.00 18.46           O  
ANISOU 1085  O   HOH A 201     1581   3091   2339   -750      2    -79       O  
HETATM 1086  O   HOH A 202      -7.431  10.287  42.175  1.00 16.38           O  
ANISOU 1086  O   HOH A 202     2152   2588   1484   -407   -365    473       O  
HETATM 1087  O   HOH A 203       9.836  16.120  42.850  1.00 12.02           O  
ANISOU 1087  O   HOH A 203     1421   2066   1080    519    -45   -220       O  
HETATM 1088  O   HOH A 204       3.651  -0.025  37.380  1.00 17.41           O  
ANISOU 1088  O   HOH A 204     2689   1578   2347   -480     76    105       O  
HETATM 1089  O   HOH A 205      -5.287   4.766  41.904  1.00 15.68           O  
ANISOU 1089  O   HOH A 205     1789   1891   2277    359    262    835       O  
HETATM 1090  O   HOH A 206      14.004  17.068  19.304  1.00 20.16           O  
ANISOU 1090  O   HOH A 206     2758   1923   2978    653   1256    542       O  
HETATM 1091  O   HOH A 207       7.826  30.345  37.064  1.00 25.62           O  
ANISOU 1091  O   HOH A 207     3377   1884   4470   -328   -642  -1236       O  
HETATM 1092  O   HOH A 208      21.871  17.059  20.724  1.00 16.95           O  
ANISOU 1092  O   HOH A 208     1956   2221   2263    135    311   -347       O  
HETATM 1093  O   HOH A 209      14.096   0.023  24.844  1.00 14.33           O  
ANISOU 1093  O   HOH A 209     1543   2644   1257    563    349   -253       O  
HETATM 1094  O   HOH A 210       7.856   6.162  22.559  1.00 17.33           O  
ANISOU 1094  O   HOH A 210     1858   1007   3718   -172    483   -551       O  
HETATM 1095  O   HOH A 211      14.326  -2.912  34.039  1.00 12.34           O  
ANISOU 1095  O   HOH A 211     1548   1583   1557    -90    225    178       O  
HETATM 1096  O   HOH A 212      17.810  -1.811  32.709  1.00 54.96           O  
ANISOU 1096  O   HOH A 212     7619   6030   7231   -549   1803    413       O  
HETATM 1097  O   HOH A 213      -0.918  30.499  23.161  1.00 14.28           O  
ANISOU 1097  O   HOH A 213     2071   1457   1894   -196   -613   -154       O  
HETATM 1098  O   HOH A 214       3.340  31.877  25.394  1.00 16.32           O  
ANISOU 1098  O   HOH A 214     2013   1838   2349    635   -149   -150       O  
HETATM 1099  O   HOH A 215      -1.870  31.568  30.713  1.00 19.20           O  
ANISOU 1099  O   HOH A 215     2252   1832   3209   -205    334   -340       O  
HETATM 1100  O   HOH A 216       5.762  20.881  42.279  1.00 18.82           O  
ANISOU 1100  O   HOH A 216     2716   2723   1711    329   -129   -331       O  
HETATM 1101  O   HOH A 217      11.693  33.364  29.661  1.00 16.55           O  
ANISOU 1101  O   HOH A 217     2271   1384   2633   -223    817   -258       O  
HETATM 1102  O   HOH A 218       9.408  18.633  41.906  1.00 17.24           O  
ANISOU 1102  O   HOH A 218     1799   2647   2103    328   -396    938       O  
HETATM 1103  O   HOH A 219       0.342  13.654  14.351  1.00 19.40           O  
ANISOU 1103  O   HOH A 219     2926   2464   1979   -405    780    697       O  
HETATM 1104  O   HOH A 220      21.189  14.685  33.784  1.00 14.95           O  
ANISOU 1104  O   HOH A 220     1553   1638   2489   -251    515    174       O  
HETATM 1105  O   HOH A 221      23.026   7.638  28.293  1.00 22.44           O  
ANISOU 1105  O   HOH A 221     2327   2424   3775    549      0   -298       O  
HETATM 1106  O   HOH A 222      15.150  26.989  36.004  1.00 19.62           O  
ANISOU 1106  O   HOH A 222     1940   1763   3750   -356   -306    -56       O  
HETATM 1107  O   HOH A 223      20.143  22.162  38.788  1.00 20.82           O  
ANISOU 1107  O   HOH A 223     2528   2608   2775    382    -35    426       O  
HETATM 1108  O   HOH A 224      18.804  32.055  30.209  1.00 16.24           O  
ANISOU 1108  O   HOH A 224     1943   1764   2462    309      0   -419       O  
HETATM 1109  O   HOH A 225       8.703  14.913  18.339  1.00 22.20           O  
ANISOU 1109  O   HOH A 225     2813   4052   1567   -781   -148    466       O  
HETATM 1110  O   HOH A 226      10.538  12.355  18.182  1.00 26.27           O  
ANISOU 1110  O   HOH A 226     3128   4624   2228   1778   -679   -514       O  
HETATM 1111  O   HOH A 227       2.141  20.282  39.815  1.00 20.97           O  
ANISOU 1111  O   HOH A 227     3993   1843   2130    717    797    135       O  
HETATM 1112  O   HOH A 228       0.471  18.635  44.693  1.00 18.09           O  
ANISOU 1112  O   HOH A 228     2786   1602   2482      4    499   -460       O  
HETATM 1113  O   HOH A 229      -0.092  19.529  40.833  1.00 20.26           O  
ANISOU 1113  O   HOH A 229     3326   1861   2508    141   -357    574       O  
HETATM 1114  O   HOH A 230      13.369  -3.848  26.564  1.00 34.16           O  
ANISOU 1114  O   HOH A 230     5210   3779   3988   -217  -1673    428       O  
HETATM 1115  O   HOH A 231      16.746  33.597  33.833  1.00 15.28           O  
ANISOU 1115  O   HOH A 231     2285   1700   1819   -312    -15   -281       O  
HETATM 1116  O   HOH A 232      -2.813  18.518  31.856  1.00 18.44           O  
ANISOU 1116  O   HOH A 232     2265   2399   2339    -23    421    346       O  
HETATM 1117  O   HOH A 233      19.165  29.930  35.856  1.00 23.58           O  
ANISOU 1117  O   HOH A 233     3811   2377   2770   -170   -661    -65       O  
HETATM 1118  O   HOH A 234       2.359  -2.098  40.115  1.00 20.54           O  
ANISOU 1118  O   HOH A 234     3305   1192   3305    319   -515    410       O  
HETATM 1119  O   HOH A 235      22.433   6.881  34.039  1.00 21.53           O  
ANISOU 1119  O   HOH A 235     1862   3081   3236    281    -39    552       O  
HETATM 1120  O   HOH A 236       1.961   4.425  24.939  1.00 25.07           O  
ANISOU 1120  O   HOH A 236     3443   3577   2503    -26    161   -634       O  
HETATM 1121  O   HOH A 237      12.517  33.416  32.503  1.00 17.24           O  
ANISOU 1121  O   HOH A 237     2672   1584   2291   -586     63   -227       O  
HETATM 1122  O   HOH A 238      21.378  17.696  29.834  1.00 15.74           O  
ANISOU 1122  O   HOH A 238     1067   2702   2210    454   -103     85       O  
HETATM 1123  O   HOH A 239      -6.214   7.542  35.881  1.00 19.17           O  
ANISOU 1123  O   HOH A 239     2027   2577   2678   -435   -638   -437       O  
HETATM 1124  O   HOH A 240       3.302  21.474  41.739  1.00 22.50           O  
ANISOU 1124  O   HOH A 240     3444   2752   2351    622    785   -259       O  
HETATM 1125  O   HOH A 241      13.507  31.897  28.219  1.00 14.37           O  
ANISOU 1125  O   HOH A 241     1769   1409   2282    -49   -484    -44       O  
HETATM 1126  O   HOH A 242      20.832  29.841  33.678  1.00 19.61           O  
ANISOU 1126  O   HOH A 242     2739   2494   2217     20   -406    -83       O  
HETATM 1127  O   HOH A 243      -6.631  10.961  31.893  1.00 58.41           O  
ANISOU 1127  O   HOH A 243     9562   5346   7281   -469  -3886    839       O  
HETATM 1128  O   HOH A 244      10.407  32.843  34.567  1.00 22.22           O  
ANISOU 1128  O   HOH A 244     3088   1580   3772    -70    539   -220       O  
HETATM 1129  O   HOH A 245       3.566  30.416  37.678  1.00 33.49           O  
ANISOU 1129  O   HOH A 245     4594   3582   4546   1181   1913    502       O  
HETATM 1130  O   HOH A 246       8.227   7.579  21.764  1.00 27.66           O  
ANISOU 1130  O   HOH A 246     2014   3053   5441   -424   -773     32       O  
HETATM 1131  O   HOH A 247       9.807  17.792  19.709  1.00 39.10           O  
ANISOU 1131  O   HOH A 247     5537   4156   5163    995  -2430  -4211       O  
HETATM 1132  O   HOH A 248      22.680  11.497  36.554  1.00 30.32           O  
ANISOU 1132  O   HOH A 248     2865   3931   4721  -1511  -1436     57       O  
HETATM 1133  O   HOH A 249      19.609  12.691  34.600  1.00 10.88           O  
ANISOU 1133  O   HOH A 249     1299   1463   1371   -250   -221    202       O  
HETATM 1134  O   HOH A 250      17.502  22.071  40.796  1.00 42.46           O  
ANISOU 1134  O   HOH A 250     4326   8060   3746    184   2432  -1477       O  
HETATM 1135  O   HOH A 251       7.482  12.339  18.242  1.00 26.59           O  
ANISOU 1135  O   HOH A 251     2606   4499   2996  -1059     60   -149       O  
HETATM 1136  O   HOH A 252      10.622  -1.359  35.624  1.00 23.32           O  
ANISOU 1136  O   HOH A 252     3663   1748   3448   1400    545    306       O  
HETATM 1137  O   HOH A 253      23.091   5.100  29.115  1.00 25.57           O  
ANISOU 1137  O   HOH A 253     2540   2626   4550    637  -1891   -368       O  
HETATM 1138  O   HOH A 254       7.473  27.921  38.530  1.00 25.01           O  
ANISOU 1138  O   HOH A 254     2397   4867   2237    904    308    234       O  
HETATM 1139  O   HOH A 255      -2.917  26.176  36.080  1.00 26.01           O  
ANISOU 1139  O   HOH A 255     2541   4058   3284   -139    419     -7       O  
HETATM 1140  O   HOH A 256      22.067  16.848  27.472  1.00 26.64           O  
ANISOU 1140  O   HOH A 256     4702   3231   2188   -933   -154   -737       O  
HETATM 1141  O   HOH A 257      -7.451   8.372  40.189  1.00 19.32           O  
ANISOU 1141  O   HOH A 257     2941   3011   1386    233    403    149       O  
HETATM 1142  O   HOH A 258      18.541  31.739  27.526  1.00 16.71           O  
ANISOU 1142  O   HOH A 258     2596   1841   1911    476    403    481       O  
HETATM 1143  O   HOH A 259      -2.281  18.120  43.202  1.00 29.83           O  
ANISOU 1143  O   HOH A 259     4328   3553   3452  -1109    516  -1524       O  
HETATM 1144  O   HOH A 260      10.911   6.011  18.544  1.00 22.40           O  
ANISOU 1144  O   HOH A 260     3008   3213   2289  -1024    478     49       O  
HETATM 1145  O   HOH A 261      24.464   4.507  26.047  1.00 33.37           O  
ANISOU 1145  O   HOH A 261     3011   5807   3861   -519  -1505    774       O  
HETATM 1146  O   HOH A 262       5.381   7.469  26.138  1.00 21.81           O  
ANISOU 1146  O   HOH A 262     3308   2395   2583    539   1889   -351       O  
HETATM 1147  O   HOH A 263       7.676  28.958  25.447  1.00 18.86           O  
ANISOU 1147  O   HOH A 263     2149   2461   2557   -202    -21    669       O  
HETATM 1148  O   HOH A 264      11.636  -2.075  24.818  1.00 25.68           O  
ANISOU 1148  O   HOH A 264     3176   2656   3925  -1000    434  -1398       O  
HETATM 1149  O   HOH A 265       2.385   6.390  23.282  1.00 36.05           O  
ANISOU 1149  O   HOH A 265     4932   4951   3814   -314     89    492       O  
HETATM 1150  O   HOH A 266       5.944  19.208  44.730  1.00 33.41           O  
ANISOU 1150  O   HOH A 266     4908   5283   2503    319   -593   -710       O  
HETATM 1151  O   HOH A 267      -4.690  23.379  37.170  1.00 25.94           O  
ANISOU 1151  O   HOH A 267     4065   3874   1917    759   -233  -1007       O  
HETATM 1152  O   HOH A 268       7.110  21.849  19.201  1.00 22.39           O  
ANISOU 1152  O   HOH A 268     2705   2282   3519   -423   -513    278       O  
HETATM 1153  O   HOH A 269      -5.423  29.716  31.314  1.00 90.59           O  
ANISOU 1153  O   HOH A 269     7051   6713  20656   -915   2627  -1716       O  
HETATM 1154  O   HOH A 270      -1.289   7.759  23.134  1.00 64.91           O  
ANISOU 1154  O   HOH A 270     7050   3384  14228  -2738   2990  -4577       O  
HETATM 1155  O   HOH A 271       7.345  28.407  20.266  1.00 46.12           O  
ANISOU 1155  O   HOH A 271     4157   8434   4932   1033   -824    799       O  
HETATM 1156  O   HOH A 272       5.403  20.166  16.725  1.00 30.09           O  
ANISOU 1156  O   HOH A 272     4147   4708   2577  -1523    267    110       O  
HETATM 1157  O   HOH A 273       8.795  34.690  35.543  1.00 21.53           O  
ANISOU 1157  O   HOH A 273     2068   2039   4071   -562    919   -609       O  
HETATM 1158  O   HOH A 274      -8.430  12.658  41.237  1.00 47.14           O  
ANISOU 1158  O   HOH A 274     9141   3726   5042    256  -1170   2748       O  
HETATM 1159  O   HOH A 275      -6.925  15.665  29.223  1.00 24.05           O  
ANISOU 1159  O   HOH A 275     2599   4243   2295   -658  -1227   -867       O  
HETATM 1160  O   HOH A 276       8.113  17.057  44.809  1.00 26.97           O  
ANISOU 1160  O   HOH A 276     3357   3668   3222   -447   -349   -845       O  
HETATM 1161  O   HOH A 277      12.112  15.462  17.426  1.00 33.69           O  
ANISOU 1161  O   HOH A 277     3937   4278   4583   -206   -949  -2023       O  
HETATM 1162  O   HOH A 278      18.519  28.236  37.711  1.00 24.09           O  
ANISOU 1162  O   HOH A 278     3796   1929   3427   -449   -157   -750       O  
HETATM 1163  O   HOH A 279       5.250  26.724  39.824  1.00 26.73           O  
ANISOU 1163  O   HOH A 279     4633   2199   3323    548    663   -523       O  
HETATM 1164  O   HOH A 280       3.892  24.576  19.842  1.00 53.13           O  
ANISOU 1164  O   HOH A 280     8798   4333   7053  -1862   -548  -1256       O  
HETATM 1165  O   HOH A 281       8.185  34.670  31.501  1.00 24.64           O  
ANISOU 1165  O   HOH A 281     4608   1614   3140     54    322    489       O  
HETATM 1166  O   HOH A 282       2.173  13.993  16.163  1.00 18.81           O  
ANISOU 1166  O   HOH A 282     3793   1874   1478   -258    341    -66       O  
HETATM 1167  O   HOH A 283      21.068  15.044  30.789  1.00 18.71           O  
ANISOU 1167  O   HOH A 283     1066   2340   3703    340    121   -189       O  
HETATM 1168  O   HOH A 284      -3.001  30.987  25.020  1.00 17.90           O  
ANISOU 1168  O   HOH A 284     3782   1398   1621    102   -328   -163       O  
HETATM 1169  O   HOH A 285      -1.758   2.589  35.934  1.00 22.83           O  
ANISOU 1169  O   HOH A 285     3311   3242   2118     55   -505   -334       O  
HETATM 1170  O   HOH A 286       5.907  16.248  17.371  1.00 25.83           O  
ANISOU 1170  O   HOH A 286     2988   4690   2137    455     93   -248       O  
HETATM 1171  O   HOH A 287      -3.930  16.912  16.375  1.00 21.83           O  
ANISOU 1171  O   HOH A 287     3056   2460   2776   -376   -857    -35       O  
HETATM 1172  O   HOH A 288      -1.476  20.554  25.622  1.00 26.14           O  
ANISOU 1172  O   HOH A 288     1674   5561   2697  -1358    541   -233       O  
HETATM 1173  O   HOH A 289       8.383  13.275  45.458  1.00 26.16           O  
ANISOU 1173  O   HOH A 289     2551   3574   3813    355   1059    368       O  
HETATM 1174  O   HOH A 290       6.350  35.661  35.008  1.00 22.15           O  
ANISOU 1174  O   HOH A 290     2938   2429   3047    118    806    369       O  
HETATM 1175  O   HOH A 291      14.513  29.847  35.052  1.00 27.08           O  
ANISOU 1175  O   HOH A 291     2708   3665   3916  -1470    855   -835       O  
HETATM 1176  O   HOH A 292      -5.394  19.265  16.846  1.00 26.30           O  
ANISOU 1176  O   HOH A 292     3467   2884   3639   -505    645    490       O  
HETATM 1177  O   HOH A 293      26.529  23.068  29.754  1.00 93.21           O  
ANISOU 1177  O   HOH A 293     9163  10602  15648  -5833  10826 -10912       O  
CONECT  151  417                                                                
CONECT  417  151                                                                
CONECT  737  885                                                                
CONECT  885  737                                                                
MASTER      488    0    0    7    0    0    0    6 1117    1    4   10          
END                                                                             


A second structure was input as follows:


HEADER    TRANSPORT PROTEIN                       13-MAY-11   3S0E              
TITLE     APIS MELLIFERA OBP14 IN COMPLEX WITH THE ODORANT EUGENOL (2-METHOXY-  
TITLE    2 4(2-PROPENYL)-PHENOL)                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: OBP14;                                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 18-135;                                       
COMPND   5 SYNONYM: ODORANT BINDING PROTEIN 14;                                 
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: APIS MELLIFERA;                                 
SOURCE   3 ORGANISM_COMMON: HONEYBEE;                                           
SOURCE   4 ORGANISM_TAXID: 7460;                                                
SOURCE   5 GENE: NP_001035313;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET-5 B(+)                            
KEYWDS    ALL HELICAL PROTEIN, UNKNOWN ODORANT MOLECULES, ANTENNAE, TRANSPORT   
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.SPINELLI,A.LAGARDE,I.IOVINELLA,M.TEGONI,P.PELOSI,C.CAMBILLAU        
REVDAT   2   11-JAN-12 3S0E    1       JRNL                                     
REVDAT   1   30-NOV-11 3S0E    0                                                
JRNL        AUTH   S.SPINELLI,A.LAGARDE,I.IOVINELLA,P.LEGRAND,M.TEGONI,         
JRNL        AUTH 2 P.PELOSI,C.CAMBILLAU                                         
JRNL        TITL   CRYSTAL STRUCTURE OF APIS MELLIFERA OBP14, A C-MINUS         
JRNL        TITL 2 ODORANT-BINDING PROTEIN, AND ITS COMPLEXES WITH ODORANT      
JRNL        TITL 3 MOLECULES.                                                   
JRNL        REF    INSECT BIOCHEM.MOL.BIOL.      V.  42    41 2012              
JRNL        REFN                   ISSN 0965-1748                               
JRNL        PMID   22075131                                                     
JRNL        DOI    10.1016/J.IBMB.2011.10.005                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.9.2                                         
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.39                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 17183                          
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)  : 0.190                          
REMARK   3   R VALUE            (WORKING SET)  : 0.190                          
REMARK   3   FREE R VALUE                      : 0.201                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.180                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 890                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 9                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.60                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.70                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2635                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2093                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2497                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2074                   
REMARK   3   BIN FREE R VALUE                        : 0.2470                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.24                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 138                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 943                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 12                                      
REMARK   3   SOLVENT ATOMS            : 139                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 21.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.37                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.00290                                              
REMARK   3    B22 (A**2) : -6.13650                                             
REMARK   3    B33 (A**2) : 1.13350                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.20                
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.940                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.941                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 975    ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 1312   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 368    ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 36     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 129    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 963    ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 133    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 1293   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.07                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.61                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 17.79                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION:   A    1    A   10                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   -2.5236   -1.2336  -12.3114           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0158 T22:   -0.0130                                    
REMARK   3     T33:   -0.0034 T12:    0.0175                                    
REMARK   3     T13:   -0.0062 T23:   -0.0094                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0000 L22:    0.0438                                    
REMARK   3     L33:    0.0415 L12:   -0.0850                                    
REMARK   3     L13:    0.0293 L23:   -0.0460                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0003 S12:   -0.0005 S13:    0.0030                     
REMARK   3     S21:   -0.0012 S22:   -0.0012 S23:    0.0016                     
REMARK   3     S31:   -0.0016 S32:    0.0012 S33:    0.0009                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION:   A   11    A   20                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   -6.7950  -13.1349  -19.7384           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0038 T22:   -0.0085                                    
REMARK   3     T33:   -0.0036 T12:    0.0089                                    
REMARK   3     T13:   -0.0292 T23:    0.0058                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0172 L22:    0.0851                                    
REMARK   3     L33:    0.0647 L12:   -0.0942                                    
REMARK   3     L13:    0.1106 L23:   -0.0954                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0008 S12:   -0.0005 S13:    0.0007                     
REMARK   3     S21:   -0.0010 S22:    0.0006 S23:    0.0032                     
REMARK   3     S31:   -0.0025 S32:   -0.0018 S33:   -0.0014                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION:   A   21    A   30                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   -8.7118  -21.2512  -13.0302           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0010 T22:   -0.0024                                    
REMARK   3     T33:    0.0020 T12:   -0.0027                                    
REMARK   3     T13:   -0.0047 T23:   -0.0137                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0384 L22:    0.0368                                    
REMARK   3     L33:    0.0000 L12:    0.0482                                    
REMARK   3     L13:    0.0330 L23:    0.0360                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0000 S12:   -0.0015 S13:    0.0000                     
REMARK   3     S21:   -0.0014 S22:   -0.0018 S23:    0.0063                     
REMARK   3     S31:    0.0030 S32:   -0.0011 S33:    0.0019                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION:   A   31    A   40                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   -0.8091  -22.7215   -9.2514           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0048 T22:   -0.0042                                    
REMARK   3     T33:   -0.0056 T12:    0.0178                                    
REMARK   3     T13:   -0.0165 T23:   -0.0153                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0000 L22:    0.0030                                    
REMARK   3     L33:    0.0405 L12:   -0.0950                                    
REMARK   3     L13:    0.2262 L23:    0.0592                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0001 S12:   -0.0095 S13:   -0.0046                     
REMARK   3     S21:   -0.0009 S22:   -0.0010 S23:    0.0006                     
REMARK   3     S31:    0.0041 S32:   -0.0035 S33:    0.0009                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION:   A   41    A   50                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   -0.3215  -21.0566  -18.3989           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0148 T22:   -0.0144                                    
REMARK   3     T33:    0.0073 T12:    0.0262                                    
REMARK   3     T13:   -0.0206 T23:   -0.0393                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0978 L22:    0.0478                                    
REMARK   3     L33:    0.0533 L12:    0.0321                                    
REMARK   3     L13:    0.0398 L23:    0.0805                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0006 S12:    0.0073 S13:    0.0003                     
REMARK   3     S21:    0.0012 S22:    0.0012 S23:    0.0030                     
REMARK   3     S31:    0.0017 S32:    0.0027 S33:   -0.0018                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION:   A   51    A   60                                     
REMARK   3    ORIGIN FOR THE GROUP (A):    7.3821  -12.4562  -21.7971           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0040 T22:    0.0012                                    
REMARK   3     T33:   -0.0031 T12:   -0.0028                                    
REMARK   3     T13:   -0.0116 T23:    0.0222                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0330 L22:    0.0346                                    
REMARK   3     L33:    0.0046 L12:    0.0043                                    
REMARK   3     L13:    0.0511 L23:   -0.0326                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0006 S12:    0.0031 S13:    0.0018                     
REMARK   3     S21:   -0.0019 S22:    0.0003 S23:    0.0001                     
REMARK   3     S31:    0.0007 S32:    0.0022 S33:    0.0003                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION:   A   61    A   70                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   12.5709   -9.6730  -16.5647           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0046 T22:    0.0019                                    
REMARK   3     T33:   -0.0015 T12:   -0.0034                                    
REMARK   3     T13:   -0.0014 T23:    0.0037                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0278 L22:    0.0025                                    
REMARK   3     L33:    0.0015 L12:   -0.0038                                    
REMARK   3     L13:    0.0165 L23:   -0.0022                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0006 S12:    0.0015 S13:   -0.0002                     
REMARK   3     S21:    0.0012 S22:    0.0004 S23:   -0.0006                     
REMARK   3     S31:   -0.0030 S32:    0.0021 S33:   -0.0011                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION:   A   71    A   80                                     
REMARK   3    ORIGIN FOR THE GROUP (A):    9.7593   -3.7074   -5.4056           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0091 T22:   -0.0064                                    
REMARK   3     T33:    0.0081 T12:   -0.0078                                    
REMARK   3     T13:   -0.0119 T23:   -0.0295                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0000 L22:    0.0631                                    
REMARK   3     L33:    0.0000 L12:   -0.0133                                    
REMARK   3     L13:    0.0430 L23:    0.1033                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0000 S12:   -0.0004 S13:    0.0014                     
REMARK   3     S21:   -0.0011 S22:   -0.0003 S23:    0.0011                     
REMARK   3     S31:   -0.0040 S32:    0.0016 S33:    0.0003                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION:   A   81    A   90                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   15.8085  -12.6113   -7.5771           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0160 T22:    0.0203                                    
REMARK   3     T33:    0.0007 T12:    0.0009                                    
REMARK   3     T13:   -0.0081 T23:   -0.0294                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0870 L22:    0.0050                                    
REMARK   3     L33:    0.0025 L12:   -0.0414                                    
REMARK   3     L13:    0.0198 L23:    0.0717                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0000 S12:    0.0002 S13:    0.0007                     
REMARK   3     S21:    0.0012 S22:   -0.0020 S23:   -0.0002                     
REMARK   3     S31:   -0.0012 S32:    0.0009 S33:    0.0020                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION:   A   91    A  100                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   10.6463  -24.4883  -18.0195           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0079 T22:    0.0041                                    
REMARK   3     T33:    0.0004 T12:    0.0184                                    
REMARK   3     T13:   -0.0168 T23:   -0.0402                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0743 L22:    0.0002                                    
REMARK   3     L33:    0.0143 L12:   -0.0181                                    
REMARK   3     L13:    0.0080 L23:    0.0922                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0006 S12:   -0.0001 S13:    0.0005                     
REMARK   3     S21:   -0.0042 S22:    0.0006 S23:   -0.0013                     
REMARK   3     S31:   -0.0014 S32:    0.0030 S33:    0.0000                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION:   A  101    A  110                                     
REMARK   3    ORIGIN FOR THE GROUP (A):    7.3803  -17.7479   -8.0322           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0181 T22:    0.0113                                    
REMARK   3     T33:   -0.0018 T12:    0.0035                                    
REMARK   3     T13:   -0.0285 T23:   -0.0333                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0919 L22:    0.0142                                    
REMARK   3     L33:    0.0289 L12:   -0.0601                                    
REMARK   3     L13:    0.1250 L23:    0.0431                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0005 S12:   -0.0075 S13:    0.0019                     
REMARK   3     S21:    0.0000 S22:   -0.0003 S23:   -0.0007                     
REMARK   3     S31:    0.0025 S32:    0.0016 S33:   -0.0003                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION:   A  111    A  119                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   -2.8395   -8.1337   -4.2900           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0087 T22:    0.0175                                    
REMARK   3     T33:   -0.0175 T12:    0.0057                                    
REMARK   3     T13:    0.0025 T23:   -0.0576                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0612 L22:    0.0059                                    
REMARK   3     L33:    0.0378 L12:    0.0533                                    
REMARK   3     L13:    0.0312 L23:    0.1281                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0000 S12:    0.0041 S13:   -0.0007                     
REMARK   3     S21:    0.0026 S22:    0.0021 S23:   -0.0008                     
REMARK   3     S31:   -0.0045 S32:    0.0004 S33:   -0.0021                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3S0E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAY-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB065602.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-FEB-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 1                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8265                             
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17204                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 9.600                              
REMARK 200  R MERGE                    (I) : 0.01000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 15.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 4.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3S0A                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8-1.9 M  TRI-SODIUM CITRATE, 25 MM     
REMARK 280  CHES, PH 9.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K       
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       17.30500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.99500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       20.13000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       45.99500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       17.30500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       20.13000            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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 203        DISTANCE =  6.25 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EOL A 120                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3RZS   RELATED DB: PDB                                   
REMARK 900 APIS MELLIFERA OBP14 IN COMPLEX WITH TA6BR14                         
REMARK 900 RELATED ID: 3S0A   RELATED DB: PDB                                   
REMARK 900 APIS MELLIFERA OBP14, NATIVE APO-PROTEIN                             
REMARK 900 RELATED ID: 3S0B   RELATED DB: PDB                                   
REMARK 900 APIS MELLIFERA OBP14 IN COMPLEX WITH THE FLUORESCENT PROBE           
REMARK 900 1-N-PHENYLNAPHTHYLAMINE                                              
REMARK 900 RELATED ID: 3S0D   RELATED DB: PDB                                   
REMARK 900 APIS MELLIFERA OBP 14 IN COMPLEX WITH THE CITRUS ODORANT             
REMARK 900 CITRALVA                                                             
REMARK 900 RELATED ID: 3S0F   RELATED DB: PDB                                   
REMARK 900 APIS MELLIFERA OBP14, NATIVE APO, CRYSTAL FORM 2                     
REMARK 900 RELATED ID: 3S0G   RELATED DB: PDB                                   
REMARK 900 APIS MELLIFERA OBP 14 DOUBLE MUTANT GLN44CYS, HIS97CYS               
DBREF  3S0E A    2   119  UNP    Q1W640   Q1W640_APIME    18    135             
SEQADV 3S0E MET A    1  UNP  Q1W640              INITIATING METHIONINE          
SEQRES   1 A  119  MET THR ILE GLU GLU LEU LYS THR ARG LEU HIS THR GLU          
SEQRES   2 A  119  GLN SER VAL CYS LYS THR GLU THR GLY ILE ASP GLN GLN          
SEQRES   3 A  119  LYS ALA ASN ASP VAL ILE GLU GLY ASN ILE ASP VAL GLU          
SEQRES   4 A  119  ASP LYS LYS VAL GLN LEU TYR CYS GLU CYS ILE LEU LYS          
SEQRES   5 A  119  ASN PHE ASN ILE LEU ASP LYS ASN ASN VAL PHE LYS PRO          
SEQRES   6 A  119  GLN GLY ILE LYS ALA VAL MET GLU LEU LEU ILE ASP GLU          
SEQRES   7 A  119  ASN SER VAL LYS GLN LEU VAL SER ASP CYS SER THR ILE          
SEQRES   8 A  119  SER GLU GLU ASN PRO HIS LEU LYS ALA SER LYS LEU VAL          
SEQRES   9 A  119  GLN CYS VAL SER LYS TYR LYS THR MET LYS SER VAL ASP          
SEQRES  10 A  119  PHE LEU                                                      
HET    EOL  A 120      12                                                       
HETNAM     EOL 2-METHOXY-4-(PROP-2-EN-1-YL)PHENOL                               
HETSYN     EOL EUGENOL                                                          
FORMUL   2  EOL    C10 H12 O2                                                   
FORMUL   3  HOH   *139(H2 O)                                                    
HELIX    1   1 THR A    2  GLY A   22  1                                  21    
HELIX    2   2 ASP A   24  GLU A   33  1                                  10    
HELIX    3   3 ASP A   40  PHE A   54  1                                  15    
HELIX    4   4 LYS A   64  GLU A   73  1                                  10    
HELIX    5   5 ASP A   77  SER A   89  1                                  13    
HELIX    6   6 ASN A   95  LYS A  109  1                                  15    
HELIX    7   7 MET A  113  LEU A  119  5                                   7    
SSBOND   1 CYS A   17    CYS A   49                          1555   1555  2.05  
SSBOND   2 CYS A   88    CYS A  106                          1555   1555  2.05  
SITE     1 AC1  9 ILE A  56  ILE A  68  VAL A  71  LEU A  75                    
SITE     2 AC1  9 VAL A 107  SER A 108  LYS A 111  THR A 112                    
SITE     3 AC1  9 MET A 113                                                     
CRYST1   34.610   40.260   91.990  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      0.028893  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.024839  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010871        0.00000                         
ATOM      1  N   MET A   1       3.756   3.534 -14.028  1.00 42.17           N  
ANISOU    1  N   MET A   1     5493   5210   5318    171    -64    -80       N  
ATOM      2  CA  MET A   1       2.506   2.818 -13.794  1.00 41.29           C  
ANISOU    2  CA  MET A   1     5385   5100   5204    172    -63    -85       C  
ATOM      3  C   MET A   1       2.074   2.981 -12.341  1.00 44.04           C  
ANISOU    3  C   MET A   1     5735   5447   5552    171    -65    -88       C  
ATOM      4  O   MET A   1       2.878   2.771 -11.435  1.00 44.16           O  
ANISOU    4  O   MET A   1     5749   5461   5567    170    -67    -88       O  
ATOM      5  CB  MET A   1       2.662   1.328 -14.175  1.00 43.43           C  
ANISOU    5  CB  MET A   1     5656   5373   5472    174    -61    -84       C  
ATOM      6  CG  MET A   1       1.447   0.456 -13.842  1.00 46.57           C  
ANISOU    6  CG  MET A   1     6057   5772   5868    174    -61    -88       C  
ATOM      7  SD  MET A   1       1.394  -1.185 -14.614  1.00 50.27           S  
ANISOU    7  SD  MET A   1     6526   6241   6332    177    -60    -87       S  
ATOM      8  CE  MET A   1       3.042  -1.801 -14.257  1.00 47.08           C  
ANISOU    8  CE  MET A   1     6122   5841   5927    177    -59    -84       C  
ATOM      9  N   THR A   2       0.814   3.366 -12.117  1.00 39.85           N  
ANISOU    9  N   THR A   2     5206   4915   5020    171    -66    -91       N  
ATOM     10  CA  THR A   2       0.301   3.506 -10.757  1.00 39.25           C  
ANISOU   10  CA  THR A   2     5132   4838   4943    172    -67    -93       C  
ATOM     11  C   THR A   2      -0.180   2.136 -10.282  1.00 41.14           C  
ANISOU   11  C   THR A   2     5371   5079   5180    173    -65    -94       C  
ATOM     12  O   THR A   2      -0.237   1.190 -11.077  1.00 39.63           O  
ANISOU   12  O   THR A   2     5179   4889   4988    173    -63    -94       O  
ATOM     13  CB  THR A   2      -0.816   4.563 -10.666  1.00 48.12           C  
ANISOU   13  CB  THR A   2     6258   5961   6066    173    -69    -94       C  
ATOM     14  OG1 THR A   2      -1.968   4.114 -11.375  1.00 47.76           O  
ANISOU   14  OG1 THR A   2     6212   5916   6018    174    -66    -95       O  
ATOM     15  CG2 THR A   2      -0.379   5.946 -11.142  1.00 47.89           C  
ANISOU   15  CG2 THR A   2     6229   5930   6038    172    -71    -93       C  
ATOM     16  N   ILE A   3      -0.533   2.036  -8.991  1.00 36.62           N  
ANISOU   16  N   ILE A   3     4800   4507   4608    175    -66    -96       N  
ATOM     17  CA  ILE A   3      -1.079   0.822  -8.386  1.00 35.33           C  
ANISOU   17  CA  ILE A   3     4637   4345   4443    177    -64    -97       C  
ATOM     18  C   ILE A   3      -2.429   0.529  -9.018  1.00 36.97           C  
ANISOU   18  C   ILE A   3     4843   4553   4649    177    -63    -96       C  
ATOM     19  O   ILE A   3      -2.683  -0.609  -9.417  1.00 35.80           O  
ANISOU   19  O   ILE A   3     4694   4406   4501    177    -61    -96       O  
ATOM     20  CB  ILE A   3      -1.182   0.980  -6.839  1.00 38.37           C  
ANISOU   20  CB  ILE A   3     5023   4729   4827    180    -65    -98       C  
ATOM     21  CG1 ILE A   3       0.216   1.019  -6.180  1.00 38.72           C  
ANISOU   21  CG1 ILE A   3     5068   4772   4872    180    -67    -99       C  
ATOM     22  CG2 ILE A   3      -2.094  -0.086  -6.197  1.00 38.55           C  
ANISOU   22  CG2 ILE A   3     5046   4754   4849    183    -62    -98       C  
ATOM     23  CD1 ILE A   3       1.169  -0.136  -6.536  1.00 45.23           C  
ANISOU   23  CD1 ILE A   3     5890   5598   5696    178    -64    -99       C  
ATOM     24  N   GLU A   4      -3.278   1.577  -9.136  1.00 32.66           N  
ANISOU   24  N   GLU A   4     4298   4006   4103    178    -63    -96       N  
ATOM     25  CA  GLU A   4      -4.607   1.467  -9.727  1.00 31.76           C  
ANISOU   25  CA  GLU A   4     4184   3893   3989    178    -62    -95       C  
ATOM     26  C   GLU A   4      -4.518   1.018 -11.186  1.00 31.94           C  
ANISOU   26  C   GLU A   4     4207   3917   4014    176    -62    -95       C  
ATOM     27  O   GLU A   4      -5.334   0.209 -11.620  1.00 31.80           O  
ANISOU   27  O   GLU A   4     4188   3900   3996    176    -62    -94       O  
ATOM     28  CB  GLU A   4      -5.389   2.781  -9.581  1.00 33.40           C  
ANISOU   28  CB  GLU A   4     4394   4101   4195    180    -63    -95       C  
ATOM     29  CG  GLU A   4      -5.867   3.052  -8.157  1.00 44.56           C  
ANISOU   29  CG  GLU A   4     5809   5514   5607    184    -64    -94       C  
ATOM     30  CD  GLU A   4      -6.822   2.049  -7.531  1.00 65.10           C  
ANISOU   30  CD  GLU A   4     8409   8117   8208    186    -62    -92       C  
ATOM     31  OE1 GLU A   4      -7.703   1.523  -8.250  1.00 54.43           O  
ANISOU   31  OE1 GLU A   4     7055   6767   6858    185    -60    -90       O  
ATOM     32  OE2 GLU A   4      -6.706   1.812  -6.307  1.00 62.72           O  
ANISOU   32  OE2 GLU A   4     8108   7816   7907    190    -61    -91       O  
ATOM     33  N   GLU A   5      -3.488   1.489 -11.915  1.00 26.86           N  
ANISOU   33  N   GLU A   5     3563   3272   3370    175    -62    -95       N  
ATOM     34  CA  GLU A   5      -3.244   1.103 -13.308  1.00 25.78           C  
ANISOU   34  CA  GLU A   5     3426   3136   3234    175    -62    -94       C  
ATOM     35  C   GLU A   5      -2.764  -0.335 -13.379  1.00 26.54           C  
ANISOU   35  C   GLU A   5     3521   3232   3329    175    -62    -94       C  
ATOM     36  O   GLU A   5      -3.189  -1.065 -14.274  1.00 24.75           O  
ANISOU   36  O   GLU A   5     3295   3006   3102    177    -62    -94       O  
ATOM     37  CB  GLU A   5      -2.262   2.055 -13.988  1.00 27.64           C  
ANISOU   37  CB  GLU A   5     3661   3370   3469    175    -62    -93       C  
ATOM     38  CG  GLU A   5      -2.972   3.296 -14.504  1.00 37.93           C  
ANISOU   38  CG  GLU A   5     4965   4673   4773    175    -62    -94       C  
ATOM     39  CD  GLU A   5      -2.134   4.529 -14.770  1.00 57.32           C  
ANISOU   39  CD  GLU A   5     7421   7128   7230    175    -62    -93       C  
ATOM     40  OE1 GLU A   5      -0.886   4.420 -14.796  1.00 44.20           O  
ANISOU   40  OE1 GLU A   5     5757   5466   5570    174    -62    -90       O  
ATOM     41  OE2 GLU A   5      -2.735   5.609 -14.970  1.00 52.79           O  
ANISOU   41  OE2 GLU A   5     6849   6554   6656    175    -62    -94       O  
ATOM     42  N   LEU A   6      -1.918  -0.755 -12.419  1.00 21.73           N  
ANISOU   42  N   LEU A   6     2912   2624   2719    175    -62    -94       N  
ATOM     43  CA  LEU A   6      -1.437  -2.142 -12.362  1.00 20.21           C  
ANISOU   43  CA  LEU A   6     2720   2433   2526    175    -61    -93       C  
ATOM     44  C   LEU A   6      -2.600  -3.089 -12.047  1.00 21.69           C  
ANISOU   44  C   LEU A   6     2908   2621   2714    175    -61    -94       C  
ATOM     45  O   LEU A   6      -2.688  -4.155 -12.662  1.00 18.98           O  
ANISOU   45  O   LEU A   6     2566   2278   2370    176    -62    -94       O  
ATOM     46  CB  LEU A   6      -0.290  -2.312 -11.346  1.00 20.00           C  
ANISOU   46  CB  LEU A   6     2693   2407   2498    175    -60    -94       C  
ATOM     47  CG  LEU A   6       0.246  -3.750 -11.135  1.00 23.07           C  
ANISOU   47  CG  LEU A   6     3082   2798   2885    175    -60    -94       C  
ATOM     48  CD1 LEU A   6       0.780  -4.368 -12.428  1.00 22.49           C  
ANISOU   48  CD1 LEU A   6     3010   2725   2809    176    -60    -92       C  
ATOM     49  CD2 LEU A   6       1.290  -3.790 -10.042  1.00 24.04           C  
ANISOU   49  CD2 LEU A   6     3205   2922   3007    175    -59    -95       C  
ATOM     50  N   LYS A   7      -3.488  -2.696 -11.099  1.00 18.99           N  
ANISOU   50  N   LYS A   7     2564   2278   2373    176    -61    -94       N  
ATOM     51  CA  LYS A   7      -4.688  -3.460 -10.736  1.00 19.47           C  
ANISOU   51  CA  LYS A   7     2624   2338   2435    176    -61    -93       C  
ATOM     52  C   LYS A   7      -5.519  -3.762 -11.993  1.00 22.18           C  
ANISOU   52  C   LYS A   7     2968   2681   2780    176    -63    -93       C  
ATOM     53  O   LYS A   7      -5.863  -4.918 -12.239  1.00 20.68           O  
ANISOU   53  O   LYS A   7     2777   2490   2591    175    -65    -92       O  
ATOM     54  CB  LYS A   7      -5.571  -2.678  -9.739  1.00 21.96           C  
ANISOU   54  CB  LYS A   7     2938   2654   2751    178    -60    -93       C  
ATOM     55  CG  LYS A   7      -5.186  -2.808  -8.285  1.00 38.58           C  
ANISOU   55  CG  LYS A   7     5043   4759   4855    180    -58    -93       C  
ATOM     56  CD  LYS A   7      -6.292  -2.260  -7.393  1.00 49.92           C  
ANISOU   56  CD  LYS A   7     6479   6196   6292    183    -58    -91       C  
ATOM     57  CE  LYS A   7      -5.752  -1.494  -6.213  1.00 61.16           C  
ANISOU   57  CE  LYS A   7     7905   7619   7714    187    -57    -92       C  
ATOM     58  NZ  LYS A   7      -6.808  -1.239  -5.198  1.00 70.78           N  
ANISOU   58  NZ  LYS A   7     9123   8838   8931    192    -56    -89       N  
ATOM     59  N   THR A   8      -5.822  -2.718 -12.788  1.00 19.29           N  
ANISOU   59  N   THR A   8     2602   2313   2413    176    -63    -93       N  
ATOM     60  CA  THR A   8      -6.587  -2.815 -14.030  1.00 18.64           C  
ANISOU   60  CA  THR A   8     2520   2230   2332    176    -65    -93       C  
ATOM     61  C   THR A   8      -5.864  -3.699 -15.055  1.00 21.27           C  
ANISOU   61  C   THR A   8     2855   2562   2664    178    -67    -94       C  
ATOM     62  O   THR A   8      -6.493  -4.548 -15.697  1.00 20.25           O  
ANISOU   62  O   THR A   8     2726   2430   2536    178    -70    -94       O  
ATOM     63  CB  THR A   8      -6.844  -1.399 -14.579  1.00 26.32           C  
ANISOU   63  CB  THR A   8     3494   3203   3305    177    -65    -94       C  
ATOM     64  OG1 THR A   8      -7.547  -0.647 -13.588  1.00 28.51           O  
ANISOU   64  OG1 THR A   8     3770   3481   3582    177    -63    -94       O  
ATOM     65  CG2 THR A   8      -7.624  -1.397 -15.898  1.00 25.20           C  
ANISOU   65  CG2 THR A   8     3353   3059   3164    178    -66    -95       C  
ATOM     66  N   ARG A   9      -4.543  -3.486 -15.211  1.00 17.37           N  
ANISOU   66  N   ARG A   9     2363   2070   2168    178    -66    -94       N  
ATOM     67  CA  ARG A   9      -3.725  -4.238 -16.154  1.00 15.81           C  
ANISOU   67  CA  ARG A   9     2167   1871   1968    181    -67    -93       C  
ATOM     68  C   ARG A   9      -3.722  -5.716 -15.786  1.00 18.13           C  
ANISOU   68  C   ARG A   9     2462   2165   2261    181    -69    -93       C  
ATOM     69  O   ARG A   9      -3.883  -6.558 -16.672  1.00 16.91           O  
ANISOU   69  O   ARG A   9     2310   2009   2105    183    -73    -92       O  
ATOM     70  CB  ARG A   9      -2.298  -3.662 -16.205  1.00 17.12           C  
ANISOU   70  CB  ARG A   9     2333   2040   2132    182    -65    -92       C  
ATOM     71  CG  ARG A   9      -1.357  -4.410 -17.124  1.00 18.49           C  
ANISOU   71  CG  ARG A   9     2510   2214   2303    185    -66    -90       C  
ATOM     72  CD  ARG A   9      -1.693  -4.296 -18.605  1.00 18.80           C  
ANISOU   72  CD  ARG A   9     2551   2251   2341    190    -68    -89       C  
ATOM     73  NE  ARG A   9      -0.785  -5.146 -19.363  1.00 19.68           N  
ANISOU   73  NE  ARG A   9     2665   2363   2448    195    -69    -86       N  
ATOM     74  CZ  ARG A   9       0.476  -4.833 -19.639  1.00 23.81           C  
ANISOU   74  CZ  ARG A   9     3188   2888   2969    198    -66    -83       C  
ATOM     75  NH1 ARG A   9       0.956  -3.639 -19.305  1.00 19.55           N  
ANISOU   75  NH1 ARG A   9     2645   2350   2432    195    -63    -82       N  
ATOM     76  NH2 ARG A   9       1.254  -5.688 -20.278  1.00 20.61           N  
ANISOU   76  NH2 ARG A   9     2787   2485   2559    203    -67    -80       N  
ATOM     77  N   LEU A  10      -3.552  -6.034 -14.496  1.00 14.78           N  
ANISOU   77  N   LEU A  10     2036   1743   1837    178    -68    -93       N  
ATOM     78  CA  LEU A  10      -3.577  -7.439 -14.059  1.00 13.15           C  
ANISOU   78  CA  LEU A  10     1830   1536   1630    178    -69    -93       C  
ATOM     79  C   LEU A  10      -4.934  -8.062 -14.354  1.00 17.19           C  
ANISOU   79  C   LEU A  10     2342   2045   2145    177    -73    -92       C  
ATOM     80  O   LEU A  10      -4.974  -9.161 -14.887  1.00 16.65           O  
ANISOU   80  O   LEU A  10     2276   1975   2076    178    -76    -92       O  
ATOM     81  CB  LEU A  10      -3.254  -7.564 -12.566  1.00 13.55           C  
ANISOU   81  CB  LEU A  10     1879   1589   1680    176    -66    -93       C  
ATOM     82  CG  LEU A  10      -1.780  -7.438 -12.200  1.00 16.77           C  
ANISOU   82  CG  LEU A  10     2287   1999   2084    177    -63    -94       C  
ATOM     83  CD1 LEU A  10      -1.633  -7.129 -10.722  1.00 18.75           C  
ANISOU   83  CD1 LEU A  10     2537   2251   2337    176    -60    -95       C  
ATOM     84  CD2 LEU A  10      -1.006  -8.715 -12.540  1.00 16.02           C  
ANISOU   84  CD2 LEU A  10     2196   1906   1986    178    -64    -93       C  
ATOM     85  N   HIS A  11      -6.046  -7.358 -14.059  1.00 15.01           N  
ANISOU   85  N   HIS A  11     1990   1830   1884    108   -309     55       N  
ATOM     86  CA  HIS A  11      -7.370  -7.903 -14.373  1.00 15.51           C  
ANISOU   86  CA  HIS A  11     2048   1899   1944    110   -302     55       C  
ATOM     87  C   HIS A  11      -7.524  -8.169 -15.875  1.00 17.81           C  
ANISOU   87  C   HIS A  11     2335   2193   2239    103   -300     56       C  
ATOM     88  O   HIS A  11      -8.053  -9.209 -16.254  1.00 18.67           O  
ANISOU   88  O   HIS A  11     2439   2306   2350    101   -295     57       O  
ATOM     89  CB  HIS A  11      -8.497  -6.981 -13.874  1.00 17.70           C  
ANISOU   89  CB  HIS A  11     2330   2178   2216    118   -304     55       C  
ATOM     90  CG  HIS A  11      -8.577  -6.841 -12.384  1.00 22.74           C  
ANISOU   90  CG  HIS A  11     2975   2816   2850    129   -305     55       C  
ATOM     91  ND1 HIS A  11      -8.224  -7.875 -11.534  1.00 25.43           N  
ANISOU   91  ND1 HIS A  11     3314   3157   3192    130   -302     56       N  
ATOM     92  CD2 HIS A  11      -9.003  -5.793 -11.641  1.00 25.63           C  
ANISOU   92  CD2 HIS A  11     3350   3181   3209    139   -310     55       C  
ATOM     93  CE1 HIS A  11      -8.437  -7.423 -10.308  1.00 25.52           C  
ANISOU   93  CE1 HIS A  11     3333   3166   3197    141   -304     56       C  
ATOM     94  NE2 HIS A  11      -8.895  -6.172 -10.323  1.00 26.07           N  
ANISOU   94  NE2 HIS A  11     3409   3235   3262    148   -310     55       N  
ATOM     95  N   THR A  12      -7.044  -7.234 -16.726  1.00 15.26           N  
ANISOU   95  N   THR A  12     2012   1868   1918    100   -304     56       N  
ATOM     96  CA  THR A  12      -7.131  -7.373 -18.182  1.00 14.70           C  
ANISOU   96  CA  THR A  12     1937   1799   1849     95   -302     56       C  
ATOM     97  C   THR A  12      -6.357  -8.611 -18.629  1.00 16.05           C  
ANISOU   97  C   THR A  12     2105   1971   2023     92   -298     57       C  
ATOM     98  O   THR A  12      -6.924  -9.462 -19.329  1.00 15.14           O  
ANISOU   98  O   THR A  12     1987   1859   1908     91   -295     57       O  
ATOM     99  CB  THR A  12      -6.666  -6.084 -18.874  1.00 21.57           C  
ANISOU   99  CB  THR A  12     2808   2666   2720     93   -307     57       C  
ATOM    100  OG1 THR A  12      -7.532  -5.026 -18.486  1.00 19.83           O  
ANISOU  100  OG1 THR A  12     2593   2446   2496     97   -311     55       O  
ATOM    101  CG2 THR A  12      -6.661  -6.201 -20.394  1.00 21.08           C  
ANISOU  101  CG2 THR A  12     2742   2606   2660     90   -304     58       C  
ATOM    102  N   GLU A  13      -5.087  -8.743 -18.192  1.00 13.55           N  
ANISOU  102  N   GLU A  13     1788   1652   1708     90   -300     59       N  
ATOM    103  CA  GLU A  13      -4.281  -9.898 -18.601  1.00 11.56           C  
ANISOU  103  CA  GLU A  13     1533   1402   1457     88   -297     60       C  
ATOM    104  C   GLU A  13      -4.837 -11.199 -18.089  1.00 14.17           C  
ANISOU  104  C   GLU A  13     1863   1734   1787     89   -294     58       C  
ATOM    105  O   GLU A  13      -4.787 -12.211 -18.794  1.00 15.10           O  
ANISOU  105  O   GLU A  13     1979   1854   1904     88   -292     58       O  
ATOM    106  CB  GLU A  13      -2.794  -9.749 -18.231  1.00 12.99           C  
ANISOU  106  CB  GLU A  13     1714   1580   1641     86   -300     63       C  
ATOM    107  CG  GLU A  13      -2.132  -8.500 -18.801  1.00 17.26           C  
ANISOU  107  CG  GLU A  13     2254   2120   2185     85   -304     68       C  
ATOM    108  CD  GLU A  13      -2.008  -8.378 -20.314  1.00 28.04           C  
ANISOU  108  CD  GLU A  13     3615   3489   3550     84   -302     71       C  
ATOM    109  OE1 GLU A  13      -2.367  -9.330 -21.044  1.00 19.65           O  
ANISOU  109  OE1 GLU A  13     2552   2430   2485     86   -297     69       O  
ATOM    110  OE2 GLU A  13      -1.510  -7.325 -20.769  1.00 20.97           O  
ANISOU  110  OE2 GLU A  13     2717   2592   2657     82   -306     76       O  
ATOM    111  N   GLN A  14      -5.357 -11.192 -16.864  1.00 11.87           N  
ANISOU  111  N   GLN A  14     1573   1442   1494     91   -294     57       N  
ATOM    112  CA  GLN A  14      -5.943 -12.397 -16.279  1.00 11.25           C  
ANISOU  112  CA  GLN A  14     1493   1365   1415     92   -291     56       C  
ATOM    113  C   GLN A  14      -7.141 -12.855 -17.116  1.00 14.66           C  
ANISOU  113  C   GLN A  14     1922   1800   1847     92   -290     58       C  
ATOM    114  O   GLN A  14      -7.282 -14.046 -17.380  1.00 14.70           O  
ANISOU  114  O   GLN A  14     1926   1807   1854     90   -290     58       O  
ATOM    115  CB  GLN A  14      -6.364 -12.125 -14.837  1.00 12.53           C  
ANISOU  115  CB  GLN A  14     1658   1527   1576     97   -291     56       C  
ATOM    116  CG  GLN A  14      -5.174 -12.039 -13.900  1.00 12.84           C  
ANISOU  116  CG  GLN A  14     1701   1563   1616     97   -293     55       C  
ATOM    117  CD  GLN A  14      -5.501 -11.308 -12.621  1.00 16.18           C  
ANISOU  117  CD  GLN A  14     2129   1983   2035    105   -295     54       C  
ATOM    118  OE1 GLN A  14      -6.642 -10.877 -12.386  1.00 16.27           O  
ANISOU  118  OE1 GLN A  14     2141   1998   2044    110   -293     55       O  
ATOM    119  NE2 GLN A  14      -4.496 -11.134 -11.776  1.00 15.49           N  
ANISOU  119  NE2 GLN A  14     2046   1890   1948    106   -298     53       N  
ATOM    120  N   SER A  15      -7.976 -11.911 -17.569  1.00 12.58           N  
ANISOU  120  N   SER A  15     1659   1537   1583     93   -290     58       N  
ATOM    121  CA  SER A  15      -9.131 -12.237 -18.397  1.00 12.09           C  
ANISOU  121  CA  SER A  15     1595   1476   1523     93   -290     60       C  
ATOM    122  C   SER A  15      -8.716 -12.729 -19.796  1.00 16.78           C  
ANISOU  122  C   SER A  15     2189   2068   2118     90   -292     59       C  
ATOM    123  O   SER A  15      -9.189 -13.781 -20.229  1.00 16.96           O  
ANISOU  123  O   SER A  15     2211   2090   2142     89   -294     60       O  
ATOM    124  CB  SER A  15     -10.058 -11.030 -18.488  1.00 16.22           C  
ANISOU  124  CB  SER A  15     2119   1999   2044     95   -290     60       C  
ATOM    125  OG  SER A  15     -11.197 -11.359 -19.263  1.00 23.07           O  
ANISOU  125  OG  SER A  15     2984   2867   2914     94   -290     63       O  
ATOM    126  N   VAL A  16      -7.818 -11.988 -20.488  1.00 14.37           N  
ANISOU  126  N   VAL A  16     1885   1762   1811     90   -292     58       N  
ATOM    127  CA  VAL A  16      -7.321 -12.354 -21.828  1.00 13.98           C  
ANISOU  127  CA  VAL A  16     1837   1713   1762     90   -292     58       C  
ATOM    128  C   VAL A  16      -6.657 -13.734 -21.772  1.00 15.80           C  
ANISOU  128  C   VAL A  16     2069   1944   1992     91   -293     58       C  
ATOM    129  O   VAL A  16      -6.969 -14.598 -22.593  1.00 16.42           O  
ANISOU  129  O   VAL A  16     2149   2021   2070     92   -296     58       O  
ATOM    130  CB  VAL A  16      -6.361 -11.270 -22.378  1.00 18.74           C  
ANISOU  130  CB  VAL A  16     2439   2315   2364     90   -292     59       C  
ATOM    131  CG1 VAL A  16      -5.667 -11.730 -23.663  1.00 19.32           C  
ANISOU  131  CG1 VAL A  16     2514   2390   2437     93   -291     60       C  
ATOM    132  CG2 VAL A  16      -7.110  -9.958 -22.607  1.00 18.66           C  
ANISOU  132  CG2 VAL A  16     2430   2305   2355     90   -293     58       C  
ATOM    133  N   CYS A  17      -5.780 -13.950 -20.777  1.00 12.75           N  
ANISOU  133  N   CYS A  17     1681   1558   1605     89   -292     58       N  
ATOM    134  CA  CYS A  17      -5.067 -15.217 -20.655  1.00 13.28           C  
ANISOU  134  CA  CYS A  17     1749   1627   1671     90   -293     57       C  
ATOM    135  C   CYS A  17      -5.925 -16.394 -20.258  1.00 15.71           C  
ANISOU  135  C   CYS A  17     2056   1933   1979     89   -296     57       C  
ATOM    136  O   CYS A  17      -5.620 -17.528 -20.649  1.00 15.09           O  
ANISOU  136  O   CYS A  17     1979   1854   1899     90   -300     56       O  
ATOM    137  CB  CYS A  17      -3.836 -15.066 -19.774  1.00 14.70           C  
ANISOU  137  CB  CYS A  17     1929   1807   1851     88   -291     57       C  
ATOM    138  SG  CYS A  17      -2.561 -14.009 -20.512  1.00 18.98           S  
ANISOU  138  SG  CYS A  17     2469   2350   2393     89   -290     61       S  
ATOM    139  N   LYS A  18      -7.015 -16.147 -19.513  1.00 13.97           N  
ANISOU  139  N   LYS A  18     1833   1712   1761     88   -296     58       N  
ATOM    140  CA  LYS A  18      -7.945 -17.223 -19.159  1.00 13.86           C  
ANISOU  140  CA  LYS A  18     1818   1699   1750     87   -299     61       C  
ATOM    141  C   LYS A  18      -8.668 -17.674 -20.437  1.00 17.96           C  
ANISOU  141  C   LYS A  18     2338   2215   2270     88   -305     62       C  
ATOM    142  O   LYS A  18      -8.760 -18.876 -20.698  1.00 17.98           O  
ANISOU  142  O   LYS A  18     2342   2215   2273     88   -311     63       O  
ATOM    143  CB  LYS A  18      -8.960 -16.792 -18.084  1.00 15.56           C  
ANISOU  143  CB  LYS A  18     2029   1916   1967     87   -297     64       C  
ATOM    144  CG  LYS A  18      -9.868 -17.938 -17.661  1.00 22.03           C  
ANISOU  144  CG  LYS A  18     2845   2736   2791     86   -300     69       C  
ATOM    145  CD  LYS A  18     -11.186 -17.474 -17.113  1.00 31.85           C  
ANISOU  145  CD  LYS A  18     4084   3983   4037     87   -298     75       C  
ATOM    146  CE  LYS A  18     -12.167 -18.604 -16.862  1.00 32.79           C  
ANISOU  146  CE  LYS A  18     4197   4102   4161     85   -303     83       C  
ATOM    147  NZ  LYS A  18     -12.663 -19.224 -18.118  1.00 36.67           N  
ANISOU  147  NZ  LYS A  18     4690   4588   4656     83   -312     85       N  
ATOM    148  N   THR A  19      -9.136 -16.718 -21.250  1.00 15.82           N  
ANISOU  148  N   THR A  19     2068   1942   1999     89   -304     62       N  
ATOM    149  CA  THR A  19      -9.815 -17.040 -22.511  1.00 16.53           C  
ANISOU  149  CA  THR A  19     2161   2028   2091     90   -309     63       C  
ATOM    150  C   THR A  19      -8.891 -17.793 -23.492  1.00 21.18           C  
ANISOU  150  C   THR A  19     2756   2615   2676     94   -313     61       C  
ATOM    151  O   THR A  19      -9.319 -18.778 -24.110  1.00 21.64           O  
ANISOU  151  O   THR A  19     2818   2669   2735     96   -321     62       O  
ATOM    152  CB  THR A  19     -10.430 -15.771 -23.120  1.00 24.76           C  
ANISOU  152  CB  THR A  19     3204   3069   3134     91   -306     63       C  
ATOM    153  OG1 THR A  19     -11.270 -15.167 -22.143  1.00 24.01           O  
ANISOU  153  OG1 THR A  19     3105   2978   3042     89   -303     65       O  
ATOM    154  CG2 THR A  19     -11.229 -16.052 -24.387  1.00 24.75           C  
ANISOU  154  CG2 THR A  19     3207   3063   3136     93   -312     63       C  
ATOM    155  N  AGLU A  20      -7.632 -17.331 -23.620  0.50 17.45           N  
ANISOU  155  N  AGLU A  20     2285   2146   2199     96   -308     58       N  
ATOM    156  N  BGLU A  20      -7.635 -17.350 -23.614  0.50 17.72           N  
ANISOU  156  N  BGLU A  20     2319   2181   2234     96   -308     58       N  
ATOM    157  CA AGLU A  20      -6.629 -17.899 -24.528  0.50 16.99           C  
ANISOU  157  CA AGLU A  20     2231   2088   2135    102   -310     57       C  
ATOM    158  CA BGLU A  20      -6.685 -17.963 -24.543  0.50 17.39           C  
ANISOU  158  CA BGLU A  20     2282   2139   2186    102   -310     57       C  
ATOM    159  C  AGLU A  20      -6.226 -19.336 -24.187  0.50 19.50           C  
ANISOU  159  C  AGLU A  20     2552   2406   2451    103   -316     57       C  
ATOM    160  C  BGLU A  20      -6.237 -19.366 -24.187  0.50 19.73           C  
ANISOU  160  C  BGLU A  20     2582   2436   2481    104   -316     57       C  
ATOM    161  O  AGLU A  20      -5.951 -20.115 -25.096  0.50 19.55           O  
ANISOU  161  O  AGLU A  20     2565   2411   2453    110   -321     56       O  
ATOM    162  O  BGLU A  20      -5.933 -20.146 -25.083  0.50 19.83           O  
ANISOU  162  O  BGLU A  20     2600   2447   2488    110   -322     56       O  
ATOM    163  CB AGLU A  20      -5.388 -16.987 -24.580  0.50 18.66           C  
ANISOU  163  CB AGLU A  20     2441   2305   2344    104   -303     58       C  
ATOM    164  CB BGLU A  20      -5.470 -17.068 -24.750  0.50 19.13           C  
ANISOU  164  CB BGLU A  20     2500   2363   2403    104   -303     58       C  
ATOM    165  CG AGLU A  20      -4.342 -17.379 -25.617  0.50 26.20           C  
ANISOU  165  CG AGLU A  20     3400   3262   3293    112   -303     59       C  
ATOM    166  CG BGLU A  20      -5.792 -15.813 -25.530  0.50 27.38           C  
ANISOU  166  CG BGLU A  20     3545   3408   3450    105   -300     58       C  
ATOM    167  CD AGLU A  20      -3.001 -16.683 -25.479  0.50 45.95           C  
ANISOU  167  CD AGLU A  20     5897   5769   5793    112   -296     62       C  
ATOM    168  CD BGLU A  20      -4.624 -14.915 -25.870  0.50 43.78           C  
ANISOU  168  CD BGLU A  20     5620   5490   5525    107   -295     61       C  
ATOM    169  OE1AGLU A  20      -2.985 -15.435 -25.381  0.50 44.00           O  
ANISOU  169  OE1AGLU A  20     5646   5522   5549    108   -292     64       O  
ATOM    170  OE1BGLU A  20      -3.476 -15.253 -25.500  0.50 43.95           O  
ANISOU  170  OE1BGLU A  20     5639   5514   5544    108   -293     63       O  
ATOM    171  OE2AGLU A  20      -1.962 -17.382 -25.493  0.50 32.69           O  
ANISOU  171  OE2AGLU A  20     4218   4092   4109    116   -296     64       O  
ATOM    172  OE2BGLU A  20      -4.858 -13.882 -26.539  0.50 26.18           O  
ANISOU  172  OE2BGLU A  20     3390   3260   3297    107   -293     62       O  
ATOM    173  N   THR A  21      -6.170 -19.680 -22.889  1.00 15.84           N  
ANISOU  173  N   THR A  21     2011   1990   2018    -41    -57   -138       N  
ATOM    174  CA  THR A  21      -5.700 -20.990 -22.421  1.00 15.06           C  
ANISOU  174  CA  THR A  21     1910   1892   1920    -39    -54   -140       C  
ATOM    175  C   THR A  21      -6.763 -22.009 -22.089  1.00 18.84           C  
ANISOU  175  C   THR A  21     2388   2369   2402    -37    -53   -139       C  
ATOM    176  O   THR A  21      -6.445 -23.201 -21.983  1.00 19.43           O  
ANISOU  176  O   THR A  21     2462   2444   2478    -36    -51   -141       O  
ATOM    177  CB  THR A  21      -4.768 -20.787 -21.214  1.00 18.59           C  
ANISOU  177  CB  THR A  21     2356   2339   2367    -36    -52   -140       C  
ATOM    178  OG1 THR A  21      -5.544 -20.217 -20.157  1.00 16.92           O  
ANISOU  178  OG1 THR A  21     2144   2126   2158    -34    -53   -138       O  
ATOM    179  CG2 THR A  21      -3.575 -19.889 -21.537  1.00 18.85           C  
ANISOU  179  CG2 THR A  21     2391   2374   2397    -38    -52   -141       C  
ATOM    180  N   GLY A  22      -7.981 -21.550 -21.833  1.00 16.25           N  
ANISOU  180  N   GLY A  22     2060   2039   2076    -36    -55   -137       N  
ATOM    181  CA  GLY A  22      -9.078 -22.437 -21.461  1.00 16.42           C  
ANISOU  181  CA  GLY A  22     2081   2059   2101    -34    -55   -137       C  
ATOM    182  C   GLY A  22      -9.042 -22.887 -20.012  1.00 19.01           C  
ANISOU  182  C   GLY A  22     2407   2387   2430    -31    -53   -137       C  
ATOM    183  O   GLY A  22      -9.804 -23.779 -19.621  1.00 20.02           O  
ANISOU  183  O   GLY A  22     2534   2513   2559    -30    -52   -137       O  
ATOM    184  N   ILE A  23      -8.169 -22.278 -19.196  1.00 14.76           N  
ANISOU  184  N   ILE A  23     1868   1849   1891    -31    -52   -137       N  
ATOM    185  CA  ILE A  23      -8.060 -22.600 -17.771  1.00 13.12           C  
ANISOU  185  CA  ILE A  23     1659   1641   1683    -29    -50   -137       C  
ATOM    186  C   ILE A  23      -9.393 -22.320 -17.060  1.00 17.73           C  
ANISOU  186  C   ILE A  23     2242   2224   2270    -28    -51   -137       C  
ATOM    187  O   ILE A  23     -10.067 -21.333 -17.356  1.00 17.03           O  
ANISOU  187  O   ILE A  23     2154   2135   2183    -29    -53   -137       O  
ATOM    188  CB  ILE A  23      -6.863 -21.870 -17.087  1.00 15.00           C  
ANISOU  188  CB  ILE A  23     1898   1881   1921    -28    -50   -137       C  
ATOM    189  CG1 ILE A  23      -6.580 -22.447 -15.672  1.00 14.97           C  
ANISOU  189  CG1 ILE A  23     1894   1877   1918    -27    -48   -137       C  
ATOM    190  CG2 ILE A  23      -7.059 -20.336 -17.057  1.00 15.29           C  
ANISOU  190  CG2 ILE A  23     1934   1917   1957    -29    -51   -136       C  
ATOM    191  CD1 ILE A  23      -5.246 -21.972 -15.039  1.00 16.33           C  
ANISOU  191  CD1 ILE A  23     2066   2050   2089    -26    -47   -137       C  
ATOM    192  N   ASP A  24      -9.766 -23.199 -16.142  1.00 15.66           N  
ANISOU  192  N   ASP A  24     1980   1962   2009    -28    -50   -137       N  
ATOM    193  CA  ASP A  24     -10.962 -23.067 -15.315  1.00 16.15           C  
ANISOU  193  CA  ASP A  24     2040   2023   2072    -28    -49   -137       C  
ATOM    194  C   ASP A  24     -10.778 -21.837 -14.396  1.00 17.74           C  
ANISOU  194  C   ASP A  24     2241   2225   2274    -28    -49   -138       C  
ATOM    195  O   ASP A  24      -9.659 -21.565 -13.932  1.00 16.13           O  
ANISOU  195  O   ASP A  24     2038   2023   2069    -28    -48   -137       O  
ATOM    196  CB  ASP A  24     -11.122 -24.366 -14.501  1.00 19.07           C  
ANISOU  196  CB  ASP A  24     2411   2394   2443    -28    -48   -137       C  
ATOM    197  CG  ASP A  24     -12.181 -24.362 -13.431  1.00 38.51           C  
ANISOU  197  CG  ASP A  24     4871   4855   4905    -29    -47   -138       C  
ATOM    198  OD1 ASP A  24     -13.378 -24.452 -13.780  1.00 41.39           O  
ANISOU  198  OD1 ASP A  24     5235   5219   5272    -30    -47   -139       O  
ATOM    199  OD2 ASP A  24     -11.815 -24.343 -12.241  1.00 45.86           O  
ANISOU  199  OD2 ASP A  24     5802   5788   5835    -30    -46   -138       O  
ATOM    200  N   GLN A  25     -11.845 -21.057 -14.190  1.00 14.87           N  
ANISOU  200  N   GLN A  25     1875   1861   1913    -28    -49   -139       N  
ATOM    201  CA  GLN A  25     -11.742 -19.865 -13.341  1.00 14.05           C  
ANISOU  201  CA  GLN A  25     1770   1758   1810    -29    -49   -140       C  
ATOM    202  C   GLN A  25     -11.180 -20.168 -11.951  1.00 17.80           C  
ANISOU  202  C   GLN A  25     2245   2236   2284    -29    -47   -140       C  
ATOM    203  O   GLN A  25     -10.392 -19.378 -11.444  1.00 17.49           O  
ANISOU  203  O   GLN A  25     2205   2197   2244    -29    -46   -140       O  
ATOM    204  CB  GLN A  25     -13.092 -19.136 -13.220  1.00 14.83           C  
ANISOU  204  CB  GLN A  25     1866   1856   1913    -29    -50   -143       C  
ATOM    205  CG  GLN A  25     -13.016 -17.791 -12.468  1.00 20.27           C  
ANISOU  205  CG  GLN A  25     2552   2545   2603    -29    -51   -144       C  
ATOM    206  CD  GLN A  25     -12.171 -16.765 -13.183  1.00 30.28           C  
ANISOU  206  CD  GLN A  25     3821   3813   3871    -28    -53   -143       C  
ATOM    207  OE1 GLN A  25     -11.073 -16.396 -12.739  1.00 23.06           O  
ANISOU  207  OE1 GLN A  25     2907   2900   2954    -28    -52   -141       O  
ATOM    208  NE2 GLN A  25     -12.640 -16.302 -14.324  1.00 23.78           N  
ANISOU  208  NE2 GLN A  25     2998   2988   3050    -28    -57   -143       N  
ATOM    209  N   GLN A  26     -11.586 -21.286 -11.325  1.00 16.92           N  
ANISOU  209  N   GLN A  26     2134   2124   2172    -30    -45   -140       N  
ATOM    210  CA  GLN A  26     -11.091 -21.611  -9.985  1.00 17.51           C  
ANISOU  210  CA  GLN A  26     2209   2200   2244    -32    -43   -139       C  
ATOM    211  C   GLN A  26      -9.591 -21.875  -9.993  1.00 18.79           C  
ANISOU  211  C   GLN A  26     2373   2363   2405    -31    -44   -137       C  
ATOM    212  O   GLN A  26      -8.898 -21.446  -9.068  1.00 17.45           O  
ANISOU  212  O   GLN A  26     2203   2194   2234    -31    -43   -137       O  
ATOM    213  CB  GLN A  26     -11.849 -22.787  -9.373  1.00 19.57           C  
ANISOU  213  CB  GLN A  26     2470   2461   2504    -34    -42   -140       C  
ATOM    214  CG  GLN A  26     -13.297 -22.466  -9.047  1.00 42.82           C  
ANISOU  214  CG  GLN A  26     5412   5406   5451    -36    -41   -143       C  
ATOM    215  CD  GLN A  26     -14.057 -23.662  -8.526  1.00 73.17           C  
ANISOU  215  CD  GLN A  26     9257   9250   9294    -39    -41   -143       C  
ATOM    216  OE1 GLN A  26     -13.738 -24.827  -8.803  1.00 71.21           O  
ANISOU  216  OE1 GLN A  26     9012   9002   9045    -39    -41   -141       O  
ATOM    217  NE2 GLN A  26     -15.109 -23.396  -7.773  1.00 68.91           N  
ANISOU  217  NE2 GLN A  26     8715   8712   8755    -42    -39   -147       N  
ATOM    218  N   LYS A  27      -9.095 -22.561 -11.041  1.00 14.61           N  
ANISOU  218  N   LYS A  27     1845   1832   1874    -29    -45   -136       N  
ATOM    219  CA  LYS A  27      -7.665 -22.828 -11.197  1.00 14.38           C  
ANISOU  219  CA  LYS A  27     1817   1802   1844    -28    -45   -135       C  
ATOM    220  C   LYS A  27      -6.919 -21.518 -11.421  1.00 16.05           C  
ANISOU  220  C   LYS A  27     2028   2015   2055    -27    -45   -135       C  
ATOM    221  O   LYS A  27      -5.848 -21.332 -10.844  1.00 15.70           O  
ANISOU  221  O   LYS A  27     1984   1970   2009    -27    -45   -135       O  
ATOM    222  CB  LYS A  27      -7.405 -23.812 -12.345  1.00 16.43           C  
ANISOU  222  CB  LYS A  27     2077   2060   2103    -28    -46   -135       C  
ATOM    223  CG  LYS A  27      -7.215 -25.261 -11.911  1.00 35.14           C  
ANISOU  223  CG  LYS A  27     4447   4429   4473    -28    -47   -135       C  
ATOM    224  CD  LYS A  27      -5.852 -25.490 -11.268  1.00 40.36           C  
ANISOU  224  CD  LYS A  27     5110   5090   5135    -28    -48   -134       C  
ATOM    225  CE  LYS A  27      -5.326 -26.879 -11.499  1.00 44.32           C  
ANISOU  225  CE  LYS A  27     5612   5590   5638    -28    -50   -134       C  
ATOM    226  NZ  LYS A  27      -4.716 -27.430 -10.265  1.00 41.19           N  
ANISOU  226  NZ  LYS A  27     5217   5192   5242    -29    -51   -133       N  
ATOM    227  N   ALA A  28      -7.489 -20.591 -12.227  1.00 13.14           N  
ANISOU  227  N   ALA A  28     1659   1646   1687    -27    -46   -136       N  
ATOM    228  CA  ALA A  28      -6.881 -19.275 -12.445  1.00 12.51           C  
ANISOU  228  CA  ALA A  28     1578   1567   1607    -26    -46   -136       C  
ATOM    229  C   ALA A  28      -6.841 -18.513 -11.119  1.00 14.06           C  
ANISOU  229  C   ALA A  28     1773   1764   1804    -26    -45   -136       C  
ATOM    230  O   ALA A  28      -5.825 -17.890 -10.802  1.00 13.82           O  
ANISOU  230  O   ALA A  28     1744   1735   1773    -25    -45   -135       O  
ATOM    231  CB  ALA A  28      -7.676 -18.487 -13.477  1.00 13.15           C  
ANISOU  231  CB  ALA A  28     1660   1648   1690    -26    -49   -136       C  
ATOM    232  N   ASN A  29      -7.935 -18.590 -10.326  1.00 11.57           N  
ANISOU  232  N   ASN A  29     1457   1450   1490    -27    -44   -137       N  
ATOM    233  CA  ASN A  29      -7.994 -17.945  -9.011  1.00 11.05           C  
ANISOU  233  CA  ASN A  29     1389   1385   1425    -28    -43   -138       C  
ATOM    234  C   ASN A  29      -6.904 -18.480  -8.070  1.00 14.38           C  
ANISOU  234  C   ASN A  29     1813   1808   1844    -29    -41   -136       C  
ATOM    235  O   ASN A  29      -6.320 -17.691  -7.336  1.00 14.33           O  
ANISOU  235  O   ASN A  29     1806   1803   1837    -29    -40   -136       O  
ATOM    236  CB  ASN A  29      -9.388 -18.089  -8.378  1.00 14.05           C  
ANISOU  236  CB  ASN A  29     1767   1766   1807    -31    -42   -140       C  
ATOM    237  CG  ASN A  29     -10.497 -17.302  -9.050  1.00 23.60           C  
ANISOU  237  CG  ASN A  29     2974   2974   3020    -30    -43   -143       C  
ATOM    238  OD1 ASN A  29     -11.690 -17.488  -8.740  1.00 23.88           O  
ANISOU  238  OD1 ASN A  29     3007   3009   3057    -32    -43   -145       O  
ATOM    239  ND2 ASN A  29     -10.156 -16.385  -9.945  1.00 13.67           N  
ANISOU  239  ND2 ASN A  29     1716   1715   1763    -29    -46   -142       N  
ATOM    240  N   ASP A  30      -6.610 -19.801  -8.118  1.00 13.25           N  
ANISOU  240  N   ASP A  30     1672   1664   1700    -29    -41   -135       N  
ATOM    241  CA  ASP A  30      -5.527 -20.387  -7.328  1.00 13.82           C  
ANISOU  241  CA  ASP A  30     1746   1735   1771    -30    -41   -133       C  
ATOM    242  C   ASP A  30      -4.185 -19.723  -7.708  1.00 16.44           C  
ANISOU  242  C   ASP A  30     2078   2067   2101    -27    -41   -133       C  
ATOM    243  O   ASP A  30      -3.438 -19.294  -6.821  1.00 16.26           O  
ANISOU  243  O   ASP A  30     2056   2045   2078    -27    -41   -132       O  
ATOM    244  CB  ASP A  30      -5.436 -21.909  -7.558  1.00 15.60           C  
ANISOU  244  CB  ASP A  30     1973   1959   1995    -30    -43   -133       C  
ATOM    245  CG  ASP A  30      -6.601 -22.739  -7.052  1.00 24.96           C  
ANISOU  245  CG  ASP A  30     3158   3144   3181    -33    -43   -133       C  
ATOM    246  OD1 ASP A  30      -7.369 -22.235  -6.193  1.00 25.91           O  
ANISOU  246  OD1 ASP A  30     3277   3266   3301    -36    -41   -134       O  
ATOM    247  OD2 ASP A  30      -6.701 -23.924  -7.453  1.00 29.64           O  
ANISOU  247  OD2 ASP A  30     3752   3736   3774    -33    -44   -132       O  
ATOM    248  N   VAL A  31      -3.913 -19.569  -9.024  1.00 12.36           N  
ANISOU  248  N   VAL A  31     1629   1550   1519    179   -175   -167       N  
ATOM    249  CA  VAL A  31      -2.685 -18.929  -9.508  1.00 11.97           C  
ANISOU  249  CA  VAL A  31     1581   1496   1471    179   -177   -166       C  
ATOM    250  C   VAL A  31      -2.606 -17.481  -9.015  1.00 14.90           C  
ANISOU  250  C   VAL A  31     1951   1870   1839    182   -187   -169       C  
ATOM    251  O   VAL A  31      -1.572 -17.051  -8.504  1.00 14.03           O  
ANISOU  251  O   VAL A  31     1839   1760   1730    184   -190   -165       O  
ATOM    252  CB  VAL A  31      -2.602 -19.012 -11.056  1.00 14.66           C  
ANISOU  252  CB  VAL A  31     1926   1829   1814    177   -175   -167       C  
ATOM    253  CG1 VAL A  31      -1.465 -18.150 -11.612  1.00 14.30           C  
ANISOU  253  CG1 VAL A  31     1882   1782   1768    176   -178   -165       C  
ATOM    254  CG2 VAL A  31      -2.462 -20.467 -11.519  1.00 14.60           C  
ANISOU  254  CG2 VAL A  31     1919   1819   1810    178   -169   -163       C  
ATOM    255  N   ILE A  32      -3.715 -16.759  -9.110  1.00 11.47           N  
ANISOU  255  N   ILE A  32     1518   1438   1400    182   -194   -177       N  
ATOM    256  CA  ILE A  32      -3.773 -15.359  -8.701  1.00 11.05           C  
ANISOU  256  CA  ILE A  32     1466   1390   1344    186   -209   -182       C  
ATOM    257  C   ILE A  32      -3.498 -15.236  -7.192  1.00 16.07           C  
ANISOU  257  C   ILE A  32     2095   2033   1978    194   -213   -178       C  
ATOM    258  O   ILE A  32      -2.888 -14.259  -6.770  1.00 15.09           O  
ANISOU  258  O   ILE A  32     1969   1909   1854    199   -225   -177       O  
ATOM    259  CB  ILE A  32      -5.133 -14.742  -9.134  1.00 13.72           C  
ANISOU  259  CB  ILE A  32     1807   1729   1675    185   -217   -195       C  
ATOM    260  CG1 ILE A  32      -5.243 -14.694 -10.666  1.00 14.10           C  
ANISOU  260  CG1 ILE A  32     1863   1767   1726    178   -215   -199       C  
ATOM    261  CG2 ILE A  32      -5.368 -13.349  -8.511  1.00 15.03           C  
ANISOU  261  CG2 ILE A  32     1972   1903   1835    190   -237   -202       C  
ATOM    262  CD1 ILE A  32      -6.688 -14.425 -11.205  1.00 14.32           C  
ANISOU  262  CD1 ILE A  32     1897   1793   1750    177   -219   -213       C  
ATOM    263  N   GLU A  33      -3.889 -16.249  -6.405  1.00 14.89           N  
ANISOU  263  N   GLU A  33     1941   1889   1827    195   -204   -176       N  
ATOM    264  CA  GLU A  33      -3.701 -16.233  -4.946  1.00 15.32           C  
ANISOU  264  CA  GLU A  33     1990   1951   1881    204   -206   -172       C  
ATOM    265  C   GLU A  33      -2.316 -16.772  -4.545  1.00 19.91           C  
ANISOU  265  C   GLU A  33     2571   2524   2469    205   -200   -164       C  
ATOM    266  O   GLU A  33      -1.983 -16.831  -3.361  1.00 19.65           O  
ANISOU  266  O   GLU A  33     2536   2495   2437    213   -201   -162       O  
ATOM    267  CB  GLU A  33      -4.828 -17.020  -4.244  1.00 17.03           C  
ANISOU  267  CB  GLU A  33     2200   2178   2091    204   -201   -173       C  
ATOM    268  CG  GLU A  33      -6.157 -16.289  -4.242  1.00 28.20           C  
ANISOU  268  CG  GLU A  33     3614   3604   3498    206   -210   -183       C  
ATOM    269  CD  GLU A  33      -7.422 -17.076  -3.953  1.00 51.28           C  
ANISOU  269  CD  GLU A  33     6531   6537   6415    203   -203   -184       C  
ATOM    270  OE1 GLU A  33      -7.319 -18.226  -3.471  1.00 35.27           O  
ANISOU  270  OE1 GLU A  33     4501   4509   4389    199   -192   -175       O  
ATOM    271  OE2 GLU A  33      -8.525 -16.527  -4.190  1.00 42.92           O  
ANISOU  271  OE2 GLU A  33     5472   5486   5349    203   -210   -194       O  
ATOM    272  N   GLY A  34      -1.521 -17.164  -5.532  1.00 16.84           N  
ANISOU  272  N   GLY A  34     2187   2126   2085    198   -194   -162       N  
ATOM    273  CA  GLY A  34      -0.177 -17.655  -5.269  1.00 17.58           C  
ANISOU  273  CA  GLY A  34     2282   2213   2184    199   -188   -157       C  
ATOM    274  C   GLY A  34      -0.084 -19.128  -4.948  1.00 21.80           C  
ANISOU  274  C   GLY A  34     2818   2747   2720    196   -178   -154       C  
ATOM    275  O   GLY A  34       0.963 -19.567  -4.461  1.00 23.47           O  
ANISOU  275  O   GLY A  34     3030   2952   2934    198   -175   -153       O  
ATOM    276  N   ASN A  35      -1.148 -19.911  -5.244  1.00 17.36           N  
ANISOU  276  N   ASN A  35     2254   2188   2154    191   -174   -155       N  
ATOM    277  CA  ASN A  35      -1.125 -21.362  -5.063  1.00 17.67           C  
ANISOU  277  CA  ASN A  35     2294   2225   2193    187   -168   -152       C  
ATOM    278  C   ASN A  35      -0.978 -21.945  -6.464  1.00 21.29           C  
ANISOU  278  C   ASN A  35     2757   2679   2654    182   -166   -152       C  
ATOM    279  O   ASN A  35      -1.964 -22.073  -7.192  1.00 20.70           O  
ANISOU  279  O   ASN A  35     2681   2605   2579    179   -166   -153       O  
ATOM    280  CB  ASN A  35      -2.383 -21.878  -4.356  1.00 19.52           C  
ANISOU  280  CB  ASN A  35     2525   2467   2423    185   -167   -150       C  
ATOM    281  CG  ASN A  35      -2.338 -23.375  -4.091  1.00 49.44           C  
ANISOU  281  CG  ASN A  35     6316   6255   6214    179   -164   -146       C  
ATOM    282  OD1 ASN A  35      -1.276 -23.973  -3.861  1.00 47.86           O  
ANISOU  282  OD1 ASN A  35     6120   6049   6016    179   -163   -146       O  
ATOM    283  ND2 ASN A  35      -3.494 -24.012  -4.101  1.00 41.91           N  
ANISOU  283  ND2 ASN A  35     5360   5307   5258    174   -163   -142       N  
ATOM    284  N   ILE A  36       0.273 -22.218  -6.860  1.00 18.74           N  
ANISOU  284  N   ILE A  36     2436   2351   2333    182   -165   -152       N  
ATOM    285  CA  ILE A  36       0.572 -22.657  -8.213  1.00 18.63           C  
ANISOU  285  CA  ILE A  36     2424   2334   2320    179   -165   -153       C  
ATOM    286  C   ILE A  36       0.826 -24.147  -8.337  1.00 21.96           C  
ANISOU  286  C   ILE A  36     2847   2754   2742    178   -166   -152       C  
ATOM    287  O   ILE A  36       1.796 -24.669  -7.779  1.00 22.31           O  
ANISOU  287  O   ILE A  36     2894   2797   2786    178   -167   -154       O  
ATOM    288  CB  ILE A  36       1.651 -21.743  -8.872  1.00 22.26           C  
ANISOU  288  CB  ILE A  36     2883   2793   2781    180   -165   -153       C  
ATOM    289  CG1 ILE A  36       1.117 -20.278  -8.980  1.00 24.18           C  
ANISOU  289  CG1 ILE A  36     3126   3037   3024    181   -168   -154       C  
ATOM    290  CG2 ILE A  36       2.051 -22.231 -10.276  1.00 20.92           C  
ANISOU  290  CG2 ILE A  36     2714   2623   2610    180   -165   -153       C  
ATOM    291  CD1 ILE A  36       1.700 -19.368  -8.065  1.00 36.70           C  
ANISOU  291  CD1 ILE A  36     4710   4623   4611    184   -172   -153       C  
ATOM    292  N   ASP A  37      -0.053 -24.820  -9.095  1.00 18.57           N  
ANISOU  292  N   ASP A  37     2418   2324   2314    177   -168   -150       N  
ATOM    293  CA  ASP A  37       0.056 -26.243  -9.407  1.00 18.06           C  
ANISOU  293  CA  ASP A  37     2356   2258   2249    177   -174   -149       C  
ATOM    294  C   ASP A  37       0.971 -26.277 -10.640  1.00 19.96           C  
ANISOU  294  C   ASP A  37     2596   2498   2489    182   -176   -152       C  
ATOM    295  O   ASP A  37       0.503 -26.274 -11.782  1.00 19.52           O  
ANISOU  295  O   ASP A  37     2541   2442   2436    185   -177   -151       O  
ATOM    296  CB  ASP A  37      -1.336 -26.823  -9.705  1.00 19.66           C  
ANISOU  296  CB  ASP A  37     2558   2459   2455    176   -176   -145       C  
ATOM    297  CG  ASP A  37      -1.407 -28.328  -9.890  1.00 28.00           C  
ANISOU  297  CG  ASP A  37     3615   3513   3512    177   -187   -142       C  
ATOM    298  OD1 ASP A  37      -2.523 -28.843 -10.098  1.00 28.66           O  
ANISOU  298  OD1 ASP A  37     3698   3594   3599    176   -190   -138       O  
ATOM    299  OD2 ASP A  37      -0.343 -28.988  -9.850  1.00 31.41           O  
ANISOU  299  OD2 ASP A  37     4049   3944   3941    178   -193   -145       O  
ATOM    300  N   VAL A  38       2.295 -26.225 -10.389  1.00 16.30           N  
ANISOU  300  N   VAL A  38     2134   2037   2024    182   -176   -155       N  
ATOM    301  CA  VAL A  38       3.338 -26.117 -11.416  1.00 15.94           C  
ANISOU  301  CA  VAL A  38     2087   1995   1976    186   -177   -158       C  
ATOM    302  C   VAL A  38       3.280 -27.133 -12.552  1.00 19.02           C  
ANISOU  302  C   VAL A  38     2476   2387   2364    192   -185   -159       C  
ATOM    303  O   VAL A  38       3.635 -26.801 -13.681  1.00 17.60           O  
ANISOU  303  O   VAL A  38     2294   2211   2183    196   -184   -159       O  
ATOM    304  CB  VAL A  38       4.764 -25.969 -10.835  1.00 19.80           C  
ANISOU  304  CB  VAL A  38     2576   2486   2462    185   -176   -163       C  
ATOM    305  CG1 VAL A  38       4.888 -24.713  -9.974  1.00 19.06           C  
ANISOU  305  CG1 VAL A  38     2482   2390   2371    183   -169   -161       C  
ATOM    306  CG2 VAL A  38       5.169 -27.209 -10.048  1.00 20.02           C  
ANISOU  306  CG2 VAL A  38     2608   2511   2487    185   -183   -168       C  
ATOM    307  N   GLU A  39       2.860 -28.369 -12.247  1.00 17.42           N  
ANISOU  307  N   GLU A  39     2276   2181   2162    193   -195   -158       N  
ATOM    308  CA  GLU A  39       2.799 -29.459 -13.214  1.00 17.08           C  
ANISOU  308  CA  GLU A  39     2232   2139   2117    201   -207   -159       C  
ATOM    309  C   GLU A  39       1.543 -29.460 -14.096  1.00 20.36           C  
ANISOU  309  C   GLU A  39     2647   2549   2539    206   -208   -154       C  
ATOM    310  O   GLU A  39       1.529 -30.153 -15.118  1.00 20.49           O  
ANISOU  310  O   GLU A  39     2662   2566   2557    216   -218   -154       O  
ATOM    311  CB  GLU A  39       2.953 -30.817 -12.502  1.00 18.60           C  
ANISOU  311  CB  GLU A  39     2428   2330   2308    199   -222   -161       C  
ATOM    312  CG  GLU A  39       4.279 -31.002 -11.769  1.00 30.63           C  
ANISOU  312  CG  GLU A  39     3954   3857   3826    196   -224   -170       C  
ATOM    313  CD  GLU A  39       5.547 -30.989 -12.605  1.00 56.49           C  
ANISOU  313  CD  GLU A  39     7228   7142   7095    203   -228   -177       C  
ATOM    314  OE1 GLU A  39       5.556 -31.602 -13.697  1.00 52.02           O  
ANISOU  314  OE1 GLU A  39     6658   6580   6525    213   -239   -178       O  
ATOM    315  OE2 GLU A  39       6.547 -30.388 -12.148  1.00 53.46           O  
ANISOU  315  OE2 GLU A  39     6843   6760   6707    200   -220   -183       O  
ATOM    316  N   ASP A  40       0.505 -28.679 -13.730  1.00 16.19           N  
ANISOU  316  N   ASP A  40     2119   2016   2015    200   -198   -150       N  
ATOM    317  CA  ASP A  40      -0.726 -28.608 -14.502  1.00 15.35           C  
ANISOU  317  CA  ASP A  40     2014   1904   1916    205   -198   -148       C  
ATOM    318  C   ASP A  40      -0.528 -27.831 -15.803  1.00 17.69           C  
ANISOU  318  C   ASP A  40     2309   2199   2212    212   -193   -150       C  
ATOM    319  O   ASP A  40      -0.066 -26.686 -15.775  1.00 15.87           O  
ANISOU  319  O   ASP A  40     2078   1972   1979    207   -184   -152       O  
ATOM    320  CB  ASP A  40      -1.847 -27.992 -13.663  1.00 16.71           C  
ANISOU  320  CB  ASP A  40     2186   2073   2091    197   -190   -146       C  
ATOM    321  CG  ASP A  40      -3.182 -28.019 -14.371  1.00 25.77           C  
ANISOU  321  CG  ASP A  40     3335   3212   3245    201   -190   -145       C  
ATOM    322  OD1 ASP A  40      -3.825 -29.093 -14.384  1.00 28.47           O  
ANISOU  322  OD1 ASP A  40     3677   3550   3592    204   -199   -140       O  
ATOM    323  OD2 ASP A  40      -3.546 -26.999 -14.980  1.00 24.91           O  
ANISOU  323  OD2 ASP A  40     3227   3099   3136    202   -183   -149       O  
ATOM    324  N   LYS A  41      -0.895 -28.455 -16.943  1.00 15.68           N  
ANISOU  324  N   LYS A  41     2116   1802   2038    263   -215   -399       N  
ATOM    325  CA  LYS A  41      -0.745 -27.856 -18.272  1.00 13.98           C  
ANISOU  325  CA  LYS A  41     1896   1592   1823    265   -214   -401       C  
ATOM    326  C   LYS A  41      -1.424 -26.514 -18.411  1.00 15.44           C  
ANISOU  326  C   LYS A  41     2081   1780   2007    263   -210   -399       C  
ATOM    327  O   LYS A  41      -0.800 -25.574 -18.900  1.00 14.67           O  
ANISOU  327  O   LYS A  41     1982   1686   1908    264   -210   -399       O  
ATOM    328  CB  LYS A  41      -1.247 -28.797 -19.366  1.00 17.27           C  
ANISOU  328  CB  LYS A  41     2310   2010   2242    265   -215   -404       C  
ATOM    329  CG  LYS A  41      -0.791 -28.376 -20.755  1.00 21.05           C  
ANISOU  329  CG  LYS A  41     2783   2494   2719    266   -214   -407       C  
ATOM    330  CD  LYS A  41       0.691 -28.642 -20.909  1.00 22.02           C  
ANISOU  330  CD  LYS A  41     2905   2619   2843    268   -217   -410       C  
ATOM    331  CE  LYS A  41       1.293 -27.821 -21.991  1.00 24.71           C  
ANISOU  331  CE  LYS A  41     3242   2966   3181    267   -216   -412       C  
ATOM    332  NZ  LYS A  41       2.653 -28.340 -22.291  1.00 23.11           N  
ANISOU  332  NZ  LYS A  41     3036   2766   2979    269   -219   -418       N  
ATOM    333  N   LYS A  42      -2.703 -26.413 -17.998  1.00 12.84           N  
ANISOU  333  N   LYS A  42     1752   1450   1678    261   -208   -398       N  
ATOM    334  CA  LYS A  42      -3.378 -25.126 -18.138  1.00 12.65           C  
ANISOU  334  CA  LYS A  42     1726   1427   1653    261   -206   -397       C  
ATOM    335  C   LYS A  42      -2.800 -24.049 -17.272  1.00 14.62           C  
ANISOU  335  C   LYS A  42     1977   1677   1902    260   -205   -396       C  
ATOM    336  O   LYS A  42      -2.735 -22.893 -17.699  1.00 14.43           O  
ANISOU  336  O   LYS A  42     1951   1654   1877    261   -205   -395       O  
ATOM    337  CB  LYS A  42      -4.892 -25.248 -18.034  1.00 15.42           C  
ANISOU  337  CB  LYS A  42     2077   1777   2005    259   -204   -399       C  
ATOM    338  CG  LYS A  42      -5.442 -25.896 -19.303  1.00 22.06           C  
ANISOU  338  CG  LYS A  42     2915   2619   2847    260   -205   -401       C  
ATOM    339  CD  LYS A  42      -6.936 -25.976 -19.303  1.00 28.30           C  
ANISOU  339  CD  LYS A  42     3704   3410   3639    259   -203   -404       C  
ATOM    340  CE  LYS A  42      -7.408 -26.682 -20.541  1.00 25.31           C  
ANISOU  340  CE  LYS A  42     3323   3033   3262    261   -203   -406       C  
ATOM    341  NZ  LYS A  42      -7.160 -28.160 -20.480  1.00 33.96           N  
ANISOU  341  NZ  LYS A  42     4418   4126   4358    260   -204   -407       N  
ATOM    342  N   VAL A  43      -2.332 -24.417 -16.066  1.00 12.65           N  
ANISOU  342  N   VAL A  43     1731   1425   1651    260   -206   -395       N  
ATOM    343  CA  VAL A  43      -1.656 -23.474 -15.183  1.00 11.99           C  
ANISOU  343  CA  VAL A  43     1647   1341   1566    260   -205   -394       C  
ATOM    344  C   VAL A  43      -0.355 -23.005 -15.889  1.00 13.93           C  
ANISOU  344  C   VAL A  43     1891   1589   1812    262   -207   -394       C  
ATOM    345  O   VAL A  43      -0.055 -21.808 -15.911  1.00 12.45           O  
ANISOU  345  O   VAL A  43     1702   1403   1624    262   -206   -394       O  
ATOM    346  CB  VAL A  43      -1.368 -24.118 -13.801  1.00 14.96           C  
ANISOU  346  CB  VAL A  43     2028   1716   1941    258   -206   -393       C  
ATOM    347  CG1 VAL A  43      -0.375 -23.279 -12.991  1.00 14.91           C  
ANISOU  347  CG1 VAL A  43     2022   1711   1934    259   -206   -393       C  
ATOM    348  CG2 VAL A  43      -2.659 -24.313 -13.014  1.00 14.75           C  
ANISOU  348  CG2 VAL A  43     2003   1689   1914    254   -203   -393       C  
ATOM    349  N   GLN A  44       0.387 -23.940 -16.498  1.00 11.78           N  
ANISOU  349  N   GLN A  44     1620   1317   1540    264   -209   -396       N  
ATOM    350  CA  GLN A  44       1.615 -23.583 -17.228  1.00 11.06           C  
ANISOU  350  CA  GLN A  44     1526   1229   1448    265   -210   -398       C  
ATOM    351  C   GLN A  44       1.332 -22.593 -18.361  1.00 15.07           C  
ANISOU  351  C   GLN A  44     2032   1740   1955    264   -208   -397       C  
ATOM    352  O   GLN A  44       1.996 -21.543 -18.444  1.00 14.22           O  
ANISOU  352  O   GLN A  44     1923   1634   1847    263   -207   -397       O  
ATOM    353  CB  GLN A  44       2.277 -24.838 -17.789  1.00 11.83           C  
ANISOU  353  CB  GLN A  44     1623   1327   1546    266   -213   -402       C  
ATOM    354  CG  GLN A  44       2.939 -25.674 -16.701  1.00 16.13           C  
ANISOU  354  CG  GLN A  44     2171   1868   2092    268   -216   -403       C  
ATOM    355  CD  GLN A  44       3.355 -27.018 -17.233  1.00 21.28           C  
ANISOU  355  CD  GLN A  44     2821   2518   2746    270   -220   -406       C  
ATOM    356  OE1 GLN A  44       3.190 -27.326 -18.420  1.00 18.65           O  
ANISOU  356  OE1 GLN A  44     2484   2188   2413    270   -220   -409       O  
ATOM    357  NE2 GLN A  44       3.935 -27.837 -16.365  1.00 19.39           N  
ANISOU  357  NE2 GLN A  44     2585   2274   2507    272   -224   -407       N  
ATOM    358  N   LEU A  45       0.300 -22.895 -19.194  1.00 11.97           N  
ANISOU  358  N   LEU A  45     1638   1348   1563    263   -208   -397       N  
ATOM    359  CA  LEU A  45      -0.080 -22.016 -20.306  1.00 11.29           C  
ANISOU  359  CA  LEU A  45     1549   1264   1475    262   -208   -395       C  
ATOM    360  C   LEU A  45      -0.542 -20.659 -19.807  1.00 13.82           C  
ANISOU  360  C   LEU A  45     1870   1583   1796    262   -207   -392       C  
ATOM    361  O   LEU A  45      -0.177 -19.651 -20.393  1.00 13.95           O  
ANISOU  361  O   LEU A  45     1887   1602   1813    260   -207   -391       O  
ATOM    362  CB  LEU A  45      -1.160 -22.667 -21.169  1.00 11.91           C  
ANISOU  362  CB  LEU A  45     1627   1344   1555    262   -208   -396       C  
ATOM    363  CG  LEU A  45      -0.745 -23.935 -21.897  1.00 16.81           C  
ANISOU  363  CG  LEU A  45     2246   1968   2175    263   -209   -399       C  
ATOM    364  CD1 LEU A  45      -1.957 -24.581 -22.529  1.00 16.76           C  
ANISOU  364  CD1 LEU A  45     2238   1961   2170    264   -209   -400       C  
ATOM    365  CD2 LEU A  45       0.340 -23.653 -22.936  1.00 18.95           C  
ANISOU  365  CD2 LEU A  45     2513   2243   2442    262   -209   -401       C  
ATOM    366  N   TYR A  46      -1.349 -20.618 -18.731  1.00 11.00           N  
ANISOU  366  N   TYR A  46     1515   1223   1442    262   -206   -392       N  
ATOM    367  CA  TYR A  46      -1.837 -19.353 -18.167  1.00 10.76           C  
ANISOU  367  CA  TYR A  46     1483   1191   1413    261   -206   -391       C  
ATOM    368  C   TYR A  46      -0.659 -18.506 -17.643  1.00 13.94           C  
ANISOU  368  C   TYR A  46     1886   1594   1816    261   -205   -391       C  
ATOM    369  O   TYR A  46      -0.572 -17.302 -17.935  1.00 13.47           O  
ANISOU  369  O   TYR A  46     1827   1535   1758    261   -206   -389       O  
ATOM    370  CB  TYR A  46      -2.816 -19.691 -17.029  1.00 12.26           C  
ANISOU  370  CB  TYR A  46     1674   1379   1605    261   -205   -393       C  
ATOM    371  CG  TYR A  46      -3.473 -18.504 -16.362  1.00 12.98           C  
ANISOU  371  CG  TYR A  46     1763   1469   1699    260   -205   -394       C  
ATOM    372  CD1 TYR A  46      -4.439 -17.751 -17.024  1.00 13.60           C  
ANISOU  372  CD1 TYR A  46     1840   1547   1780    261   -207   -395       C  
ATOM    373  CD2 TYR A  46      -3.245 -18.235 -15.015  1.00 15.10           C  
ANISOU  373  CD2 TYR A  46     2032   1738   1968    259   -203   -395       C  
ATOM    374  CE1 TYR A  46      -5.096 -16.694 -16.389  1.00 12.59           C  
ANISOU  374  CE1 TYR A  46     1709   1417   1656    260   -207   -397       C  
ATOM    375  CE2 TYR A  46      -3.911 -17.198 -14.364  1.00 16.11           C  
ANISOU  375  CE2 TYR A  46     2157   1865   2099    259   -203   -398       C  
ATOM    376  CZ  TYR A  46      -4.840 -16.437 -15.050  1.00 20.12           C  
ANISOU  376  CZ  TYR A  46     2663   2372   2611    259   -205   -399       C  
ATOM    377  OH  TYR A  46      -5.464 -15.410 -14.384  1.00 22.30           O  
ANISOU  377  OH  TYR A  46     2935   2648   2891    259   -206   -402       O  
ATOM    378  N   CYS A  47       0.264 -19.138 -16.884  1.00 11.93           N  
ANISOU  378  N   CYS A  47     1632   1339   1560    262   -205   -392       N  
ATOM    379  CA  CYS A  47       1.453 -18.466 -16.354  1.00 11.51           C  
ANISOU  379  CA  CYS A  47     1579   1287   1506    262   -204   -392       C  
ATOM    380  C   CYS A  47       2.321 -17.905 -17.492  1.00 13.71           C  
ANISOU  380  C   CYS A  47     1857   1567   1784    261   -204   -392       C  
ATOM    381  O   CYS A  47       2.792 -16.763 -17.405  1.00 14.32           O  
ANISOU  381  O   CYS A  47     1934   1645   1863    260   -203   -391       O  
ATOM    382  CB  CYS A  47       2.252 -19.431 -15.490  1.00 11.39           C  
ANISOU  382  CB  CYS A  47     1566   1272   1490    263   -204   -394       C  
ATOM    383  SG  CYS A  47       1.484 -19.777 -13.889  1.00 14.92           S  
ANISOU  383  SG  CYS A  47     2015   1716   1937    263   -204   -394       S  
ATOM    384  N   GLU A  48       2.529 -18.703 -18.546  1.00 12.25           N  
ANISOU  384  N   GLU A  48     1673   1386   1597    261   -205   -393       N  
ATOM    385  CA  GLU A  48       3.311 -18.256 -19.700  1.00 12.15           C  
ANISOU  385  CA  GLU A  48     1658   1376   1581    258   -205   -393       C  
ATOM    386  C   GLU A  48       2.683 -17.040 -20.348  1.00 15.46           C  
ANISOU  386  C   GLU A  48     2078   1794   2001    256   -205   -389       C  
ATOM    387  O   GLU A  48       3.383 -16.067 -20.641  1.00 15.70           O  
ANISOU  387  O   GLU A  48     2109   1826   2030    254   -204   -387       O  
ATOM    388  CB  GLU A  48       3.424 -19.366 -20.725  1.00 13.63           C  
ANISOU  388  CB  GLU A  48     1845   1567   1767    258   -205   -395       C  
ATOM    389  CG  GLU A  48       4.346 -18.964 -21.858  1.00 19.26           C  
ANISOU  389  CG  GLU A  48     2556   2286   2477    255   -205   -396       C  
ATOM    390  CD  GLU A  48       4.321 -19.946 -22.996  1.00 32.06           C  
ANISOU  390  CD  GLU A  48     4175   3912   4096    254   -205   -399       C  
ATOM    391  OE1 GLU A  48       3.228 -20.186 -23.558  1.00 29.88           O  
ANISOU  391  OE1 GLU A  48     3899   3634   3818    254   -206   -397       O  
ATOM    392  OE2 GLU A  48       5.395 -20.511 -23.292  1.00 30.68           O  
ANISOU  392  OE2 GLU A  48     3997   3740   3919    253   -205   -405       O  
ATOM    393  N   CYS A  49       1.361 -17.098 -20.562  1.00 12.55           N  
ANISOU  393  N   CYS A  49     1710   1424   1634    257   -207   -387       N  
ATOM    394  CA  CYS A  49       0.616 -16.015 -21.187  1.00 13.70           C  
ANISOU  394  CA  CYS A  49     1856   1568   1780    256   -209   -383       C  
ATOM    395  C   CYS A  49       0.762 -14.732 -20.373  1.00 15.19           C  
ANISOU  395  C   CYS A  49     2046   1753   1973    256   -209   -382       C  
ATOM    396  O   CYS A  49       1.031 -13.661 -20.931  1.00 14.98           O  
ANISOU  396  O   CYS A  49     2020   1726   1946    253   -210   -378       O  
ATOM    397  CB  CYS A  49      -0.846 -16.433 -21.351  1.00 15.45           C  
ANISOU  397  CB  CYS A  49     2078   1788   2004    258   -210   -383       C  
ATOM    398  SG  CYS A  49      -1.923 -15.172 -22.080  1.00 21.27           S  
ANISOU  398  SG  CYS A  49     2816   2522   2743    257   -215   -379       S  
ATOM    399  N   ILE A  50       0.576 -14.810 -19.046  1.00 11.54           N  
ANISOU  399  N   ILE A  50     1582   1288   1513    258   -208   -384       N  
ATOM    400  CA  ILE A  50       0.675 -13.615 -18.199  1.00 11.79           C  
ANISOU  400  CA  ILE A  50     1613   1318   1549    258   -208   -384       C  
ATOM    401  C   ILE A  50       2.105 -13.064 -18.231  1.00 14.02           C  
ANISOU  401  C   ILE A  50     1896   1602   1831    256   -206   -384       C  
ATOM    402  O   ILE A  50       2.295 -11.854 -18.410  1.00 14.50           O  
ANISOU  402  O   ILE A  50     1956   1660   1893    255   -207   -382       O  
ATOM    403  CB  ILE A  50       0.207 -13.932 -16.757  1.00 15.31           C  
ANISOU  403  CB  ILE A  50     2057   1762   1997    260   -207   -388       C  
ATOM    404  CG1 ILE A  50      -1.332 -14.162 -16.749  1.00 16.58           C  
ANISOU  404  CG1 ILE A  50     2217   1923   2161    261   -208   -389       C  
ATOM    405  CG2 ILE A  50       0.605 -12.799 -15.775  1.00 17.23           C  
ANISOU  405  CG2 ILE A  50     2297   2004   2244    260   -206   -389       C  
ATOM    406  CD1 ILE A  50      -1.873 -14.639 -15.467  1.00 23.90           C  
ANISOU  406  CD1 ILE A  50     3142   2849   3088    261   -207   -392       C  
ATOM    407  N   LEU A  51       3.107 -13.931 -18.053  1.00 11.68           N  
ANISOU  407  N   LEU A  51     1511   1484   1443    -26   -117    223       N  
ATOM    408  CA  LEU A  51       4.490 -13.430 -18.056  1.00 11.55           C  
ANISOU  408  CA  LEU A  51     1495   1467   1426    -27   -116    222       C  
ATOM    409  C   LEU A  51       4.918 -12.823 -19.381  1.00 15.34           C  
ANISOU  409  C   LEU A  51     1976   1946   1906    -27   -116    222       C  
ATOM    410  O   LEU A  51       5.576 -11.780 -19.392  1.00 15.69           O  
ANISOU  410  O   LEU A  51     2021   1991   1951    -27   -116    222       O  
ATOM    411  CB  LEU A  51       5.499 -14.486 -17.599  1.00 11.00           C  
ANISOU  411  CB  LEU A  51     1425   1397   1356    -27   -117    221       C  
ATOM    412  CG  LEU A  51       5.323 -15.036 -16.184  1.00 14.79           C  
ANISOU  412  CG  LEU A  51     1905   1878   1836    -28   -117    222       C  
ATOM    413  CD1 LEU A  51       6.317 -16.167 -15.940  1.00 15.36           C  
ANISOU  413  CD1 LEU A  51     1978   1951   1909    -29   -118    221       C  
ATOM    414  CD2 LEU A  51       5.504 -13.943 -15.125  1.00 19.27           C  
ANISOU  414  CD2 LEU A  51     2473   2446   2403    -27   -116    221       C  
ATOM    415  N   LYS A  52       4.518 -13.442 -20.501  1.00 12.92           N  
ANISOU  415  N   LYS A  52     1670   1640   1600    -27   -117    223       N  
ATOM    416  CA  LYS A  52       4.849 -12.888 -21.814  1.00 12.67           C  
ANISOU  416  CA  LYS A  52     1639   1609   1568    -28   -117    223       C  
ATOM    417  C   LYS A  52       4.184 -11.552 -22.042  1.00 17.54           C  
ANISOU  417  C   LYS A  52     2254   2224   2185    -28   -117    223       C  
ATOM    418  O   LYS A  52       4.832 -10.620 -22.534  1.00 16.99           O  
ANISOU  418  O   LYS A  52     2185   2155   2116    -29   -118    223       O  
ATOM    419  CB  LYS A  52       4.519 -13.878 -22.924  1.00 14.93           C  
ANISOU  419  CB  LYS A  52     1926   1894   1853    -28   -118    223       C  
ATOM    420  CG  LYS A  52       5.515 -15.031 -22.976  1.00 22.62           C  
ANISOU  420  CG  LYS A  52     2900   2869   2826    -27   -118    222       C  
ATOM    421  CD  LYS A  52       5.280 -15.958 -24.148  1.00 28.06           C  
ANISOU  421  CD  LYS A  52     3591   3558   3515    -26   -119    222       C  
ATOM    422  CE  LYS A  52       6.459 -16.886 -24.315  1.00 38.75           C  
ANISOU  422  CE  LYS A  52     4944   4912   4866    -25   -119    220       C  
ATOM    423  NZ  LYS A  52       6.249 -17.855 -25.419  1.00 51.63           N  
ANISOU  423  NZ  LYS A  52     6578   6543   6497    -24   -121    220       N  
ATOM    424  N   ASN A  53       2.909 -11.430 -21.639  1.00 14.77           N  
ANISOU  424  N   ASN A  53     1904   1873   1836    -28   -117    224       N  
ATOM    425  CA  ASN A  53       2.172 -10.183 -21.820  1.00 14.35           C  
ANISOU  425  CA  ASN A  53     1850   1818   1785    -29   -118    224       C  
ATOM    426  C   ASN A  53       2.722  -9.025 -21.014  1.00 17.08           C  
ANISOU  426  C   ASN A  53     2195   2165   2131    -28   -118    223       C  
ATOM    427  O   ASN A  53       2.575  -7.875 -21.435  1.00 16.56           O  
ANISOU  427  O   ASN A  53     2128   2097   2066    -29   -119    223       O  
ATOM    428  CB  ASN A  53       0.687 -10.406 -21.587  1.00 16.84           C  
ANISOU  428  CB  ASN A  53     2165   2133   2102    -29   -118    225       C  
ATOM    429  CG  ASN A  53       0.016 -11.215 -22.680  1.00 22.46           C  
ANISOU  429  CG  ASN A  53     2878   2843   2814    -30   -119    227       C  
ATOM    430  OD1 ASN A  53       0.637 -11.633 -23.672  1.00 19.92           O  
ANISOU  430  OD1 ASN A  53     2557   2521   2491    -31   -119    227       O  
ATOM    431  ND2 ASN A  53      -1.270 -11.457 -22.520  1.00 19.81           N  
ANISOU  431  ND2 ASN A  53     2541   2505   2479    -30   -119    229       N  
ATOM    432  N   PHE A  54       3.430  -9.331 -19.903  1.00 14.23           N  
ANISOU  432  N   PHE A  54     1834   1804   1769    -27   -117    222       N  
ATOM    433  CA  PHE A  54       4.081  -8.325 -19.062  1.00 13.83           C  
ANISOU  433  CA  PHE A  54     1784   1753   1718    -26   -118    221       C  
ATOM    434  C   PHE A  54       5.554  -8.141 -19.429  1.00 17.72           C  
ANISOU  434  C   PHE A  54     2277   2246   2211    -27   -119    222       C  
ATOM    435  O   PHE A  54       6.267  -7.415 -18.736  1.00 18.89           O  
ANISOU  435  O   PHE A  54     2425   2393   2359    -26   -120    222       O  
ATOM    436  CB  PHE A  54       3.935  -8.682 -17.582  1.00 15.24           C  
ANISOU  436  CB  PHE A  54     1963   1932   1896    -25   -117    220       C  
ATOM    437  CG  PHE A  54       2.659  -8.186 -16.959  1.00 15.97           C  
ANISOU  437  CG  PHE A  54     2055   2025   1989    -24   -116    220       C  
ATOM    438  CD1 PHE A  54       2.548  -6.875 -16.513  1.00 18.10           C  
ANISOU  438  CD1 PHE A  54     2325   2294   2259    -22   -117    218       C  
ATOM    439  CD2 PHE A  54       1.574  -9.040 -16.787  1.00 17.88           C  
ANISOU  439  CD2 PHE A  54     2296   2268   2231    -23   -115    221       C  
ATOM    440  CE1 PHE A  54       1.375  -6.425 -15.904  1.00 19.63           C  
ANISOU  440  CE1 PHE A  54     2518   2488   2454    -21   -117    217       C  
ATOM    441  CE2 PHE A  54       0.407  -8.593 -16.166  1.00 21.11           C  
ANISOU  441  CE2 PHE A  54     2704   2678   2640    -22   -114    220       C  
ATOM    442  CZ  PHE A  54       0.318  -7.287 -15.731  1.00 19.50           C  
ANISOU  442  CZ  PHE A  54     2501   2473   2437    -20   -115    219       C  
ATOM    443  N   ASN A  55       6.008  -8.781 -20.527  1.00 13.96           N  
ANISOU  443  N   ASN A  55     1799   1770   1733    -28   -118    223       N  
ATOM    444  CA  ASN A  55       7.396  -8.681 -20.998  1.00 14.13           C  
ANISOU  444  CA  ASN A  55     1822   1793   1755    -28   -119    224       C  
ATOM    445  C   ASN A  55       8.397  -9.227 -19.967  1.00 18.68           C  
ANISOU  445  C   ASN A  55     2398   2369   2330    -28   -118    223       C  
ATOM    446  O   ASN A  55       9.521  -8.723 -19.852  1.00 19.06           O  
ANISOU  446  O   ASN A  55     2446   2416   2379    -28   -119    225       O  
ATOM    447  CB  ASN A  55       7.724  -7.227 -21.400  1.00 15.60           C  
ANISOU  447  CB  ASN A  55     2007   1979   1942    -29   -121    225       C  
ATOM    448  CG  ASN A  55       8.841  -7.116 -22.398  1.00 26.63           C  
ANISOU  448  CG  ASN A  55     3403   3378   3339    -30   -122    227       C  
ATOM    449  OD1 ASN A  55       9.079  -8.026 -23.194  1.00 18.91           O  
ANISOU  449  OD1 ASN A  55     2425   2401   2360    -30   -120    227       O  
ATOM    450  ND2 ASN A  55       9.508  -5.971 -22.420  1.00 21.80           N  
ANISOU  450  ND2 ASN A  55     2790   2766   2728    -31   -124    229       N  
ATOM    451  N   ILE A  56       7.993 -10.284 -19.235  1.00 14.63           N  
ANISOU  451  N   ILE A  56     1886   1856   1817    -27   -117    222       N  
ATOM    452  CA  ILE A  56       8.832 -10.936 -18.222  1.00 14.57           C  
ANISOU  452  CA  ILE A  56     1878   1847   1809    -27   -117    222       C  
ATOM    453  C   ILE A  56       9.519 -12.153 -18.819  1.00 19.09           C  
ANISOU  453  C   ILE A  56     2451   2421   2382    -28   -116    222       C  
ATOM    454  O   ILE A  56      10.571 -12.578 -18.333  1.00 18.78           O  
ANISOU  454  O   ILE A  56     2412   2381   2343    -28   -116    222       O  
ATOM    455  CB  ILE A  56       8.027 -11.212 -16.931  1.00 17.44           C  
ANISOU  455  CB  ILE A  56     2243   2211   2173    -27   -117    221       C  
ATOM    456  CG1 ILE A  56       7.614  -9.865 -16.306  1.00 18.50           C  
ANISOU  456  CG1 ILE A  56     2377   2344   2307    -26   -117    220       C  
ATOM    457  CG2 ILE A  56       8.819 -12.070 -15.911  1.00 17.85           C  
ANISOU  457  CG2 ILE A  56     2295   2262   2224    -28   -116    221       C  
ATOM    458  CD1 ILE A  56       6.517  -9.942 -15.443  1.00 27.38           C  
ANISOU  458  CD1 ILE A  56     3503   3470   3431    -25   -117    220       C  
ATOM    459  N   LEU A  57       8.944 -12.688 -19.900  1.00 18.23           N  
ANISOU  459  N   LEU A  57     2342   2313   2271    -27   -116    222       N  
ATOM    460  CA  LEU A  57       9.532 -13.790 -20.648  1.00 18.45           C  
ANISOU  460  CA  LEU A  57     2370   2342   2299    -27   -115    221       C  
ATOM    461  C   LEU A  57       9.628 -13.331 -22.070  1.00 25.38           C  
ANISOU  461  C   LEU A  57     3247   3221   3176    -27   -115    222       C  
ATOM    462  O   LEU A  57       8.657 -12.790 -22.611  1.00 24.65           O  
ANISOU  462  O   LEU A  57     3155   3128   3083    -27   -115    222       O  
ATOM    463  CB  LEU A  57       8.690 -15.074 -20.597  1.00 18.43           C  
ANISOU  463  CB  LEU A  57     2367   2339   2296    -27   -116    220       C  
ATOM    464  CG  LEU A  57       8.724 -15.899 -19.330  1.00 22.90           C  
ANISOU  464  CG  LEU A  57     2933   2904   2863    -27   -117    220       C  
ATOM    465  CD1 LEU A  57       7.825 -17.122 -19.468  1.00 23.66           C  
ANISOU  465  CD1 LEU A  57     3030   3001   2960    -27   -119    220       C  
ATOM    466  CD2 LEU A  57      10.137 -16.365 -19.013  1.00 24.67           C  
ANISOU  466  CD2 LEU A  57     3158   3129   3089    -28   -117    219       C  
ATOM    467  N   ASP A  58      10.790 -13.542 -22.687  1.00 25.01           N  
ANISOU  467  N   ASP A  58     3200   3175   3128    -26   -114    222       N  
ATOM    468  CA  ASP A  58      10.919 -13.162 -24.079  1.00 26.84           C  
ANISOU  468  CA  ASP A  58     3430   3408   3358    -26   -114    223       C  
ATOM    469  C   ASP A  58      10.440 -14.311 -24.961  1.00 33.85           C  
ANISOU  469  C   ASP A  58     4320   4297   4245    -25   -114    221       C  
ATOM    470  O   ASP A  58      10.083 -15.376 -24.445  1.00 32.35           O  
ANISOU  470  O   ASP A  58     4132   4106   4056    -25   -115    220       O  
ATOM    471  CB  ASP A  58      12.349 -12.685 -24.412  1.00 29.20           C  
ANISOU  471  CB  ASP A  58     3728   3709   3657    -26   -113    225       C  
ATOM    472  CG  ASP A  58      13.466 -13.713 -24.410  1.00 38.74           C  
ANISOU  472  CG  ASP A  58     4936   4918   4865    -25   -112    224       C  
ATOM    473  OD1 ASP A  58      13.170 -14.924 -24.285  1.00 37.78           O  
ANISOU  473  OD1 ASP A  58     4816   4796   4743    -24   -112    222       O  
ATOM    474  OD2 ASP A  58      14.641 -13.309 -24.554  1.00 46.54           O  
ANISOU  474  OD2 ASP A  58     5922   5907   5853    -24   -111    226       O  
ATOM    475  N   LYS A  59      10.457 -14.102 -26.289  1.00 33.49           N  
ANISOU  475  N   LYS A  59     4274   4253   4197    -25   -113    222       N  
ATOM    476  CA  LYS A  59      10.033 -15.077 -27.302  1.00 34.66           C  
ANISOU  476  CA  LYS A  59     4424   4401   4343    -24   -114    220       C  
ATOM    477  C   LYS A  59      10.753 -16.419 -27.131  1.00 39.86           C  
ANISOU  477  C   LYS A  59     5083   5060   5001    -22   -113    218       C  
ATOM    478  O   LYS A  59      10.214 -17.467 -27.496  1.00 40.04           O  
ANISOU  478  O   LYS A  59     5108   5082   5023    -20   -115    217       O  
ATOM    479  CB  LYS A  59      10.254 -14.501 -28.718  1.00 38.04           C  
ANISOU  479  CB  LYS A  59     4853   4833   4769    -24   -113    221       C  
ATOM    480  CG  LYS A  59       9.974 -13.002 -28.780  1.00 56.57           C  
ANISOU  480  CG  LYS A  59     7198   7179   7117    -26   -113    224       C  
ATOM    481  CD  LYS A  59       9.454 -12.492 -30.098  1.00 68.70           C  
ANISOU  481  CD  LYS A  59     8735   8717   8652    -28   -114    225       C  
ATOM    482  CE  LYS A  59       8.703 -11.201 -29.876  1.00 81.67           C  
ANISOU  482  CE  LYS A  59    10377  10358  10297    -31   -115    227       C  
ATOM    483  NZ  LYS A  59       7.367 -11.223 -30.527  1.00 91.12           N  
ANISOU  483  NZ  LYS A  59    11575  11552  11493    -32   -117    227       N  
ATOM    484  N   ASN A  60      11.945 -16.383 -26.509  1.00 37.08           N  
ANISOU  484  N   ASN A  60     4729   4708   4649    -21   -112    219       N  
ATOM    485  CA  ASN A  60      12.764 -17.556 -26.235  1.00 37.27           C  
ANISOU  485  CA  ASN A  60     4753   4733   4674    -20   -112    217       C  
ATOM    486  C   ASN A  60      12.688 -18.060 -24.798  1.00 40.64           C  
ANISOU  486  C   ASN A  60     5181   5158   5105    -21   -114    216       C  
ATOM    487  O   ASN A  60      13.531 -18.861 -24.377  1.00 41.13           O  
ANISOU  487  O   ASN A  60     5242   5219   5168    -20   -114    215       O  
ATOM    488  CB  ASN A  60      14.194 -17.302 -26.667  1.00 40.81           C  
ANISOU  488  CB  ASN A  60     5200   5183   5122    -18   -110    218       C  
ATOM    489  CG  ASN A  60      14.397 -17.747 -28.084  1.00 68.68           C  
ANISOU  489  CG  ASN A  60     8731   8717   8649    -16   -109    216       C  
ATOM    490  OD1 ASN A  60      14.129 -18.904 -28.442  1.00 65.12           O  
ANISOU  490  OD1 ASN A  60     8282   8265   8197    -14   -110    214       O  
ATOM    491  ND2 ASN A  60      14.799 -16.823 -28.936  1.00 61.84           N  
ANISOU  491  ND2 ASN A  60     7864   7853   7780    -16   -107    219       N  
ATOM    492  N   ASN A  61      11.653 -17.609 -24.057  1.00 35.15           N  
ANISOU  492  N   ASN A  61     4409   4491   4455    -26    -20     30       N  
ATOM    493  CA  ASN A  61      11.380 -17.974 -22.666  1.00 34.14           C  
ANISOU  493  CA  ASN A  61     4282   4362   4329    -27    -20     31       C  
ATOM    494  C   ASN A  61      12.502 -17.716 -21.678  1.00 34.77           C  
ANISOU  494  C   ASN A  61     4362   4441   4408    -28    -20     31       C  
ATOM    495  O   ASN A  61      12.642 -18.428 -20.684  1.00 34.46           O  
ANISOU  495  O   ASN A  61     4323   4401   4370    -28    -21     31       O  
ATOM    496  CB  ASN A  61      10.766 -19.365 -22.542  1.00 38.36           C  
ANISOU  496  CB  ASN A  61     4815   4895   4866    -26    -22     31       C  
ATOM    497  CG  ASN A  61       9.324 -19.361 -22.959  1.00 66.61           C  
ANISOU  497  CG  ASN A  61     8393   8472   8444    -25    -22     31       C  
ATOM    498  OD1 ASN A  61       8.990 -19.136 -24.129  1.00 62.20           O  
ANISOU  498  OD1 ASN A  61     7835   7914   7885    -24    -21     31       O  
ATOM    499  ND2 ASN A  61       8.434 -19.545 -21.998  1.00 58.91           N  
ANISOU  499  ND2 ASN A  61     7419   7495   7470    -25    -22     33       N  
ATOM    500  N   VAL A  62      13.272 -16.662 -21.944  1.00 28.80           N  
ANISOU  500  N   VAL A  62     3606   3686   3650    -29    -19     31       N  
ATOM    501  CA  VAL A  62      14.328 -16.222 -21.056  1.00 27.58           C  
ANISOU  501  CA  VAL A  62     3453   3531   3496    -30    -18     32       C  
ATOM    502  C   VAL A  62      13.670 -15.209 -20.143  1.00 26.68           C  
ANISOU  502  C   VAL A  62     3341   3416   3381    -31    -17     33       C  
ATOM    503  O   VAL A  62      12.939 -14.334 -20.613  1.00 25.01           O  
ANISOU  503  O   VAL A  62     3130   3204   3169    -31    -17     34       O  
ATOM    504  CB  VAL A  62      15.546 -15.623 -21.809  1.00 32.33           C  
ANISOU  504  CB  VAL A  62     4053   4135   4096    -31    -18     31       C  
ATOM    505  CG1 VAL A  62      16.619 -15.130 -20.833  1.00 31.93           C  
ANISOU  505  CG1 VAL A  62     4003   4083   4044    -32    -18     31       C  
ATOM    506  CG2 VAL A  62      16.134 -16.636 -22.790  1.00 32.31           C  
ANISOU  506  CG2 VAL A  62     4050   4135   4094    -30    -19     29       C  
ATOM    507  N   PHE A  63      13.938 -15.329 -18.844  1.00 21.84           N  
ANISOU  507  N   PHE A  63     2728   2802   2769    -31    -18     34       N  
ATOM    508  CA  PHE A  63      13.444 -14.420 -17.829  1.00 21.14           C  
ANISOU  508  CA  PHE A  63     2641   2712   2679    -32    -17     35       C  
ATOM    509  C   PHE A  63      14.082 -13.044 -18.041  1.00 25.42           C  
ANISOU  509  C   PHE A  63     3184   3255   3221    -33    -16     35       C  
ATOM    510  O   PHE A  63      15.303 -12.946 -18.204  1.00 26.11           O  
ANISOU  510  O   PHE A  63     3270   3343   3307    -33    -16     34       O  
ATOM    511  CB  PHE A  63      13.786 -14.995 -16.449  1.00 22.67           C  
ANISOU  511  CB  PHE A  63     2834   2905   2873    -32    -18     35       C  
ATOM    512  CG  PHE A  63      13.498 -14.111 -15.269  1.00 24.82           C  
ANISOU  512  CG  PHE A  63     3109   3178   3146    -33    -17     36       C  
ATOM    513  CD1 PHE A  63      12.194 -13.743 -14.957  1.00 28.18           C  
ANISOU  513  CD1 PHE A  63     3535   3603   3571    -32    -16     37       C  
ATOM    514  CD2 PHE A  63      14.524 -13.690 -14.433  1.00 27.30           C  
ANISOU  514  CD2 PHE A  63     3422   3491   3458    -34    -17     36       C  
ATOM    515  CE1 PHE A  63      11.926 -12.941 -13.846  1.00 29.58           C  
ANISOU  515  CE1 PHE A  63     3713   3779   3747    -33    -16     37       C  
ATOM    516  CE2 PHE A  63      14.258 -12.875 -13.334  1.00 30.69           C  
ANISOU  516  CE2 PHE A  63     3853   3920   3888    -34    -16     36       C  
ATOM    517  CZ  PHE A  63      12.961 -12.520 -13.036  1.00 29.00           C  
ANISOU  517  CZ  PHE A  63     3639   3705   3673    -33    -16     37       C  
ATOM    518  N   LYS A  64      13.245 -11.998 -18.092  1.00 21.30           N  
ANISOU  518  N   LYS A  64     2663   2732   2697    -33    -15     36       N  
ATOM    519  CA  LYS A  64      13.664 -10.614 -18.300  1.00 21.09           C  
ANISOU  519  CA  LYS A  64     2637   2705   2670    -34    -15     36       C  
ATOM    520  C   LYS A  64      13.600  -9.851 -16.977  1.00 24.96           C  
ANISOU  520  C   LYS A  64     3129   3195   3161    -34    -15     37       C  
ATOM    521  O   LYS A  64      12.509  -9.451 -16.543  1.00 23.69           O  
ANISOU  521  O   LYS A  64     2969   3034   3000    -34    -14     37       O  
ATOM    522  CB  LYS A  64      12.828  -9.920 -19.397  1.00 23.75           C  
ANISOU  522  CB  LYS A  64     2974   3043   3006    -33    -14     37       C  
ATOM    523  CG  LYS A  64      12.738 -10.707 -20.701  1.00 36.41           C  
ANISOU  523  CG  LYS A  64     4576   4647   4610    -33    -14     36       C  
ATOM    524  CD  LYS A  64      13.472 -10.016 -21.838  1.00 53.22           C  
ANISOU  524  CD  LYS A  64     6705   6779   6739    -33    -14     36       C  
ATOM    525  CE  LYS A  64      12.524  -9.365 -22.820  1.00 68.94           C  
ANISOU  525  CE  LYS A  64     8696   8769   8729    -33    -14     37       C  
ATOM    526  NZ  LYS A  64      13.148  -9.217 -24.162  1.00 80.16           N  
ANISOU  526  NZ  LYS A  64    10116  10193  10149    -33    -13     37       N  
ATOM    527  N   PRO A  65      14.762  -9.658 -16.308  1.00 23.30           N  
ANISOU  527  N   PRO A  65     2918   2984   2949    -35    -15     36       N  
ATOM    528  CA  PRO A  65      14.770  -8.940 -15.022  1.00 24.13           C  
ANISOU  528  CA  PRO A  65     3025   3089   3055    -35    -15     37       C  
ATOM    529  C   PRO A  65      14.147  -7.550 -15.086  1.00 28.77           C  
ANISOU  529  C   PRO A  65     3614   3676   3643    -35    -14     37       C  
ATOM    530  O   PRO A  65      13.568  -7.116 -14.099  1.00 29.34           O  
ANISOU  530  O   PRO A  65     3686   3747   3714    -35    -14     37       O  
ATOM    531  CB  PRO A  65      16.264  -8.836 -14.691  1.00 25.99           C  
ANISOU  531  CB  PRO A  65     3260   3325   3291    -36    -15     36       C  
ATOM    532  CG  PRO A  65      16.881  -9.980 -15.389  1.00 29.97           C  
ANISOU  532  CG  PRO A  65     3763   3830   3795    -36    -15     36       C  
ATOM    533  CD  PRO A  65      16.125 -10.097 -16.677  1.00 25.00           C  
ANISOU  533  CD  PRO A  65     3133   3201   3166    -35    -15     36       C  
ATOM    534  N   GLN A  66      14.254  -6.850 -16.231  1.00 25.97           N  
ANISOU  534  N   GLN A  66     3258   3321   3287    -35    -14     37       N  
ATOM    535  CA  GLN A  66      13.686  -5.506 -16.322  1.00 26.50           C  
ANISOU  535  CA  GLN A  66     3326   3388   3355    -36    -14     38       C  
ATOM    536  C   GLN A  66      12.155  -5.490 -16.316  1.00 29.23           C  
ANISOU  536  C   GLN A  66     3672   3732   3700    -35    -14     38       C  
ATOM    537  O   GLN A  66      11.564  -4.567 -15.750  1.00 28.96           O  
ANISOU  537  O   GLN A  66     3639   3697   3666    -35    -14     38       O  
ATOM    538  CB  GLN A  66      14.298  -4.694 -17.475  1.00 28.52           C  
ANISOU  538  CB  GLN A  66     3582   3644   3611    -37    -14     39       C  
ATOM    539  CG  GLN A  66      15.805  -4.408 -17.294  1.00 47.83           C  
ANISOU  539  CG  GLN A  66     6027   6089   6056    -37    -15     39       C  
ATOM    540  CD  GLN A  66      16.147  -3.663 -16.017  1.00 74.29           C  
ANISOU  540  CD  GLN A  66     9379   9440   9408    -38    -15     38       C  
ATOM    541  OE1 GLN A  66      15.467  -2.711 -15.611  1.00 72.45           O  
ANISOU  541  OE1 GLN A  66     9147   9206   9175    -37    -16     38       O  
ATOM    542  NE2 GLN A  66      17.223  -4.074 -15.363  1.00 67.00           N  
ANISOU  542  NE2 GLN A  66     8455   8516   8484    -38    -16     38       N  
ATOM    543  N   GLY A  67      11.539  -6.522 -16.893  1.00 24.55           N  
ANISOU  543  N   GLY A  67     3079   3140   3107    -34    -14     38       N  
ATOM    544  CA  GLY A  67      10.092  -6.683 -16.927  1.00 24.03           C  
ANISOU  544  CA  GLY A  67     3014   3074   3042    -33    -13     38       C  
ATOM    545  C   GLY A  67       9.524  -6.891 -15.539  1.00 26.36           C  
ANISOU  545  C   GLY A  67     3310   3369   3337    -33    -13     38       C  
ATOM    546  O   GLY A  67       8.523  -6.264 -15.183  1.00 26.86           O  
ANISOU  546  O   GLY A  67     3373   3431   3400    -32    -13     38       O  
ATOM    547  N   ILE A  68      10.161  -7.778 -14.738  1.00 21.93           N  
ANISOU  547  N   ILE A  68     2749   2809   2776    -33    -14     38       N  
ATOM    548  CA  ILE A  68       9.715  -8.060 -13.369  1.00 21.33           C  
ANISOU  548  CA  ILE A  68     2672   2732   2700    -32    -14     38       C  
ATOM    549  C   ILE A  68       9.970  -6.865 -12.437  1.00 24.75           C  
ANISOU  549  C   ILE A  68     3106   3165   3132    -33    -14     37       C  
ATOM    550  O   ILE A  68       9.151  -6.595 -11.566  1.00 23.90           O  
ANISOU  550  O   ILE A  68     2999   3057   3024    -32    -14     37       O  
ATOM    551  CB  ILE A  68      10.250  -9.416 -12.815  1.00 24.27           C  
ANISOU  551  CB  ILE A  68     3044   3105   3072    -32    -14     38       C  
ATOM    552  CG1 ILE A  68       9.452  -9.902 -11.588  1.00 24.40           C  
ANISOU  552  CG1 ILE A  68     3060   3122   3088    -32    -14     38       C  
ATOM    553  CG2 ILE A  68      11.753  -9.360 -12.504  1.00 26.33           C  
ANISOU  553  CG2 ILE A  68     3304   3366   3333    -33    -15     37       C  
ATOM    554  CD1 ILE A  68       8.026 -10.292 -11.816  1.00 29.20           C  
ANISOU  554  CD1 ILE A  68     3668   3730   3697    -31    -14     39       C  
ATOM    555  N   LYS A  69      11.092  -6.148 -12.637  1.00 21.92           N  
ANISOU  555  N   LYS A  69     2748   2807   2774    -33    -14     37       N  
ATOM    556  CA  LYS A  69      11.433  -4.953 -11.862  1.00 22.46           C  
ANISOU  556  CA  LYS A  69     2818   2875   2843    -33    -15     37       C  
ATOM    557  C   LYS A  69      10.345  -3.894 -12.057  1.00 26.50           C  
ANISOU  557  C   LYS A  69     3329   3385   3354    -33    -14     36       C  
ATOM    558  O   LYS A  69       9.849  -3.364 -11.064  1.00 26.46           O  
ANISOU  558  O   LYS A  69     3325   3379   3348    -32    -15     36       O  
ATOM    559  CB  LYS A  69      12.818  -4.413 -12.271  1.00 25.40           C  
ANISOU  559  CB  LYS A  69     3190   3247   3216    -34    -15     36       C  
ATOM    560  CG  LYS A  69      13.265  -3.183 -11.488  1.00 45.37           C  
ANISOU  560  CG  LYS A  69     5719   5774   5744    -35    -16     36       C  
ATOM    561  CD  LYS A  69      14.650  -2.728 -11.905  1.00 57.73           C  
ANISOU  561  CD  LYS A  69     7285   7340   7311    -36    -16     36       C  
ATOM    562  CE  LYS A  69      15.069  -1.489 -11.157  1.00 72.54           C  
ANISOU  562  CE  LYS A  69     9161   9215   9187    -36    -17     36       C  
ATOM    563  NZ  LYS A  69      16.425  -1.040 -11.562  1.00 83.31           N  
ANISOU  563  NZ  LYS A  69    10525  10578  10552    -37    -18     36       N  
ATOM    564  N   ALA A  70       9.927  -3.640 -13.319  1.00 22.83           N  
ANISOU  564  N   ALA A  70     2865   2920   2890    -33    -14     37       N  
ATOM    565  CA  ALA A  70       8.888  -2.658 -13.656  1.00 22.78           C  
ANISOU  565  CA  ALA A  70     2859   2913   2884    -33    -14     37       C  
ATOM    566  C   ALA A  70       7.571  -2.882 -12.900  1.00 26.19           C  
ANISOU  566  C   ALA A  70     3292   3345   3315    -32    -14     37       C  
ATOM    567  O   ALA A  70       6.936  -1.915 -12.488  1.00 26.57           O  
ANISOU  567  O   ALA A  70     3339   3392   3363    -32    -14     36       O  
ATOM    568  CB  ALA A  70       8.646  -2.634 -15.156  1.00 23.17           C  
ANISOU  568  CB  ALA A  70     2909   2963   2934    -34    -14     38       C  
ATOM    569  N   VAL A  71       7.192  -4.155 -12.675  1.00 22.10           N  
ANISOU  569  N   VAL A  71     2742   2751   2906    -67   -124   -296       N  
ATOM    570  CA  VAL A  71       5.991  -4.515 -11.931  1.00 21.79           C  
ANISOU  570  CA  VAL A  71     2700   2711   2870    -64   -125   -299       C  
ATOM    571  C   VAL A  71       6.256  -4.495 -10.416  1.00 24.54           C  
ANISOU  571  C   VAL A  71     3045   3062   3218    -67   -124   -298       C  
ATOM    572  O   VAL A  71       5.539  -3.816  -9.680  1.00 23.14           O  
ANISOU  572  O   VAL A  71     2868   2882   3040    -68   -124   -301       O  
ATOM    573  CB  VAL A  71       5.423  -5.891 -12.394  1.00 26.17           C  
ANISOU  573  CB  VAL A  71     3250   3266   3428    -60   -125   -299       C  
ATOM    574  CG1 VAL A  71       4.267  -6.353 -11.508  1.00 26.07           C  
ANISOU  574  CG1 VAL A  71     3234   3252   3418    -58   -125   -303       C  
ATOM    575  CG2 VAL A  71       4.989  -5.845 -13.857  1.00 26.25           C  
ANISOU  575  CG2 VAL A  71     3263   3273   3439    -55   -127   -301       C  
ATOM    576  N   MET A  72       7.266  -5.258  -9.957  1.00 20.51           N  
ANISOU  576  N   MET A  72     2531   2554   2706    -70   -122   -296       N  
ATOM    577  CA  MET A  72       7.545  -5.432  -8.532  1.00 19.29           C  
ANISOU  577  CA  MET A  72     2376   2402   2552    -72   -121   -296       C  
ATOM    578  C   MET A  72       7.995  -4.211  -7.762  1.00 23.59           C  
ANISOU  578  C   MET A  72     2922   2946   3095    -74   -121   -296       C  
ATOM    579  O   MET A  72       7.715  -4.132  -6.564  1.00 23.25           O  
ANISOU  579  O   MET A  72     2878   2903   3052    -75   -120   -296       O  
ATOM    580  CB  MET A  72       8.422  -6.656  -8.249  1.00 20.72           C  
ANISOU  580  CB  MET A  72     2554   2586   2733    -73   -121   -294       C  
ATOM    581  CG  MET A  72       7.877  -7.950  -8.828  1.00 23.64           C  
ANISOU  581  CG  MET A  72     2921   2956   3105    -70   -122   -294       C  
ATOM    582  SD  MET A  72       6.197  -8.410  -8.316  1.00 27.45           S  
ANISOU  582  SD  MET A  72     3403   3437   3590    -68   -120   -296       S  
ATOM    583  CE  MET A  72       6.493  -8.889  -6.667  1.00 23.99           C  
ANISOU  583  CE  MET A  72     2965   2999   3150    -71   -119   -296       C  
ATOM    584  N   GLU A  73       8.631  -3.236  -8.437  1.00 22.69           N  
ANISOU  584  N   GLU A  73     2810   2831   2979    -75   -121   -295       N  
ATOM    585  CA  GLU A  73       9.078  -2.011  -7.761  1.00 23.95           C  
ANISOU  585  CA  GLU A  73     2972   2990   3138    -77   -121   -295       C  
ATOM    586  C   GLU A  73       7.926  -1.132  -7.267  1.00 29.12           C  
ANISOU  586  C   GLU A  73     3627   3644   3793    -76   -123   -297       C  
ATOM    587  O   GLU A  73       8.141  -0.227  -6.463  1.00 28.71           O  
ANISOU  587  O   GLU A  73     3575   3592   3742    -77   -124   -297       O  
ATOM    588  CB  GLU A  73      10.115  -1.232  -8.581  1.00 25.61           C  
ANISOU  588  CB  GLU A  73     3184   3200   3346    -79   -120   -294       C  
ATOM    589  CG  GLU A  73       9.592  -0.434  -9.766  1.00 37.00           C  
ANISOU  589  CG  GLU A  73     4632   4639   4787    -79   -121   -294       C  
ATOM    590  CD  GLU A  73      10.689   0.136 -10.649  1.00 63.80           C  
ANISOU  590  CD  GLU A  73     8030   8032   8179    -82   -119   -293       C  
ATOM    591  OE1 GLU A  73      11.881  -0.165 -10.402  1.00 59.68           O  
ANISOU  591  OE1 GLU A  73     7506   7513   7658    -84   -117   -294       O  
ATOM    592  OE2 GLU A  73      10.354   0.878 -11.599  1.00 61.37           O  
ANISOU  592  OE2 GLU A  73     7728   7722   7869    -82   -121   -293       O  
ATOM    593  N   LEU A  74       6.709  -1.411  -7.739  1.00 26.69           N  
ANISOU  593  N   LEU A  74     3320   3334   3487    -74   -124   -299       N  
ATOM    594  CA  LEU A  74       5.513  -0.687  -7.320  1.00 26.41           C  
ANISOU  594  CA  LEU A  74     3285   3298   3453    -73   -127   -303       C  
ATOM    595  C   LEU A  74       4.925  -1.320  -6.056  1.00 28.28           C  
ANISOU  595  C   LEU A  74     3517   3536   3691    -74   -125   -304       C  
ATOM    596  O   LEU A  74       4.167  -0.668  -5.337  1.00 27.90           O  
ANISOU  596  O   LEU A  74     3468   3488   3645    -75   -127   -308       O  
ATOM    597  CB  LEU A  74       4.461  -0.726  -8.448  1.00 26.81           C  
ANISOU  597  CB  LEU A  74     3338   3344   3505    -70   -130   -307       C  
ATOM    598  CG  LEU A  74       4.872  -0.178  -9.821  1.00 32.07           C  
ANISOU  598  CG  LEU A  74     4010   4007   4168    -69   -132   -305       C  
ATOM    599  CD1 LEU A  74       3.787  -0.432 -10.844  1.00 32.30           C  
ANISOU  599  CD1 LEU A  74     4042   4032   4200    -65   -135   -310       C  
ATOM    600  CD2 LEU A  74       5.199   1.321  -9.752  1.00 35.80           C  
ANISOU  600  CD2 LEU A  74     4486   4479   4639    -71   -135   -305       C  
ATOM    601  N   LEU A  75       5.309  -2.581  -5.774  1.00 22.43           N  
ANISOU  601  N   LEU A  75     2775   2797   2951    -74   -122   -302       N  
ATOM    602  CA  LEU A  75       4.745  -3.417  -4.717  1.00 21.12           C  
ANISOU  602  CA  LEU A  75     2607   2632   2786    -75   -120   -304       C  
ATOM    603  C   LEU A  75       5.621  -3.746  -3.521  1.00 24.11           C  
ANISOU  603  C   LEU A  75     2986   3013   3163    -77   -118   -301       C  
ATOM    604  O   LEU A  75       5.075  -3.975  -2.440  1.00 24.32           O  
ANISOU  604  O   LEU A  75     3012   3040   3190    -78   -116   -302       O  
ATOM    605  CB  LEU A  75       4.260  -4.736  -5.343  1.00 20.57           C  
ANISOU  605  CB  LEU A  75     2537   2562   2718    -74   -118   -304       C  
ATOM    606  CG  LEU A  75       3.397  -4.633  -6.598  1.00 24.28           C  
ANISOU  606  CG  LEU A  75     3007   3029   3191    -70   -120   -308       C  
ATOM    607  CD1 LEU A  75       3.123  -5.999  -7.160  1.00 23.40           C  
ANISOU  607  CD1 LEU A  75     2893   2917   3081    -68   -119   -307       C  
ATOM    608  CD2 LEU A  75       2.091  -3.896  -6.316  1.00 26.51           C  
ANISOU  608  CD2 LEU A  75     3289   3309   3475    -70   -122   -314       C  
ATOM    609  N   ILE A  76       6.944  -3.881  -3.723  1.00 21.51           N  
ANISOU  609  N   ILE A  76     2657   2684   2832    -77   -118   -298       N  
ATOM    610  CA  ILE A  76       7.880  -4.265  -2.665  1.00 22.26           C  
ANISOU  610  CA  ILE A  76     2753   2779   2925    -78   -118   -296       C  
ATOM    611  C   ILE A  76       9.099  -3.382  -2.686  1.00 25.67           C  
ANISOU  611  C   ILE A  76     3184   3211   3357    -77   -119   -296       C  
ATOM    612  O   ILE A  76       9.421  -2.796  -3.724  1.00 24.48           O  
ANISOU  612  O   ILE A  76     3034   3061   3206    -77   -119   -295       O  
ATOM    613  CB  ILE A  76       8.292  -5.770  -2.722  1.00 26.30           C  
ANISOU  613  CB  ILE A  76     3265   3291   3437    -78   -118   -296       C  
ATOM    614  CG1 ILE A  76       8.916  -6.157  -4.084  1.00 26.71           C  
ANISOU  614  CG1 ILE A  76     3316   3344   3489    -77   -119   -295       C  
ATOM    615  CG2 ILE A  76       7.149  -6.688  -2.319  1.00 29.76           C  
ANISOU  615  CG2 ILE A  76     3704   3729   3875    -78   -116   -297       C  
ATOM    616  CD1 ILE A  76       9.615  -7.532  -4.178  1.00 37.86           C  
ANISOU  616  CD1 ILE A  76     4728   4757   4901    -77   -120   -295       C  
ATOM    617  N   ASP A  77       9.807  -3.342  -1.541  1.00 23.22           N  
ANISOU  617  N   ASP A  77     2875   2901   3046    -77   -119   -296       N  
ATOM    618  CA  ASP A  77      11.035  -2.571  -1.376  1.00 23.07           C  
ANISOU  618  CA  ASP A  77     2856   2882   3028    -76   -119   -296       C  
ATOM    619  C   ASP A  77      12.114  -2.996  -2.368  1.00 28.04           C  
ANISOU  619  C   ASP A  77     3485   3511   3657    -77   -119   -297       C  
ATOM    620  O   ASP A  77      12.118  -4.144  -2.840  1.00 27.07           O  
ANISOU  620  O   ASP A  77     3362   3388   3534    -77   -120   -297       O  
ATOM    621  CB  ASP A  77      11.565  -2.680   0.060  1.00 24.25           C  
ANISOU  621  CB  ASP A  77     3006   3031   3178    -74   -120   -297       C  
ATOM    622  CG  ASP A  77      12.050  -4.066   0.406  1.00 30.93           C  
ANISOU  622  CG  ASP A  77     3855   3875   4022    -74   -120   -298       C  
ATOM    623  OD1 ASP A  77      11.206  -4.917   0.738  1.00 30.42           O  
ANISOU  623  OD1 ASP A  77     3793   3811   3956    -75   -120   -297       O  
ATOM    624  OD2 ASP A  77      13.271  -4.310   0.307  1.00 36.23           O  
ANISOU  624  OD2 ASP A  77     4526   4545   4693    -73   -122   -301       O  
ATOM    625  N   GLU A  78      13.029  -2.075  -2.646  1.00 26.94           N  
ANISOU  625  N   GLU A  78     3345   3372   3519    -77   -119   -298       N  
ATOM    626  CA  GLU A  78      14.125  -2.247  -3.586  1.00 27.26           C  
ANISOU  626  CA  GLU A  78     3386   3413   3561    -78   -118   -300       C  
ATOM    627  C   GLU A  78      15.002  -3.471  -3.314  1.00 28.19           C  
ANISOU  627  C   GLU A  78     3503   3530   3678    -78   -120   -304       C  
ATOM    628  O   GLU A  78      15.382  -4.159  -4.278  1.00 27.62           O  
ANISOU  628  O   GLU A  78     3429   3458   3606    -79   -120   -305       O  
ATOM    629  CB  GLU A  78      14.963  -0.980  -3.585  1.00 29.28           C  
ANISOU  629  CB  GLU A  78     3641   3667   3818    -78   -117   -302       C  
ATOM    630  CG  GLU A  78      16.046  -0.978  -4.637  1.00 45.57           C  
ANISOU  630  CG  GLU A  78     5704   5730   5881    -81   -115   -305       C  
ATOM    631  CD  GLU A  78      16.821   0.316  -4.758  1.00 75.99           C  
ANISOU  631  CD  GLU A  78     9556   9582   9736    -82   -112   -307       C  
ATOM    632  OE1 GLU A  78      16.535   1.277  -4.005  1.00 75.34           O  
ANISOU  632  OE1 GLU A  78     9473   9498   9654    -80   -113   -305       O  
ATOM    633  OE2 GLU A  78      17.717   0.368  -5.630  1.00 74.49           O  
ANISOU  633  OE2 GLU A  78     9366   9391   9545    -85   -110   -310       O  
ATOM    634  N   ASN A  79      15.343  -3.732  -2.037  1.00 23.64           N  
ANISOU  634  N   ASN A  79     2927   2952   3102    -75   -121   -306       N  
ATOM    635  CA  ASN A  79      16.201  -4.871  -1.733  1.00 22.48           C  
ANISOU  635  CA  ASN A  79     2781   2804   2955    -74   -124   -310       C  
ATOM    636  C   ASN A  79      15.475  -6.205  -1.947  1.00 23.67           C  
ANISOU  636  C   ASN A  79     2933   2956   3104    -75   -126   -308       C  
ATOM    637  O   ASN A  79      16.091  -7.164  -2.411  1.00 22.94           O  
ANISOU  637  O   ASN A  79     2841   2864   3012    -76   -129   -311       O  
ATOM    638  CB  ASN A  79      16.882  -4.700  -0.387  1.00 25.40           C  
ANISOU  638  CB  ASN A  79     3154   3171   3327    -71   -126   -314       C  
ATOM    639  CG  ASN A  79      17.829  -3.515  -0.413  1.00 52.31           C  
ANISOU  639  CG  ASN A  79     6560   6578   6739    -70   -124   -317       C  
ATOM    640  OD1 ASN A  79      18.644  -3.347  -1.333  1.00 48.16           O  
ANISOU  640  OD1 ASN A  79     6031   6052   6214    -72   -123   -321       O  
ATOM    641  ND2 ASN A  79      17.677  -2.617   0.545  1.00 47.43           N  
ANISOU  641  ND2 ASN A  79     5941   5959   6122    -67   -123   -316       N  
ATOM    642  N   SER A  80      14.145  -6.227  -1.752  1.00 18.35           N  
ANISOU  642  N   SER A  80     2260   2282   2429    -76   -125   -303       N  
ATOM    643  CA  SER A  80      13.337  -7.425  -2.017  1.00 17.49           C  
ANISOU  643  CA  SER A  80     2153   2175   2319    -77   -126   -301       C  
ATOM    644  C   SER A  80      13.234  -7.701  -3.519  1.00 18.73           C  
ANISOU  644  C   SER A  80     2306   2334   2477    -78   -125   -301       C  
ATOM    645  O   SER A  80      13.223  -8.869  -3.910  1.00 17.25           O  
ANISOU  645  O   SER A  80     2118   2148   2290    -78   -128   -301       O  
ATOM    646  CB  SER A  80      11.947  -7.289  -1.407  1.00 20.20           C  
ANISOU  646  CB  SER A  80     2496   2517   2661    -77   -123   -298       C  
ATOM    647  OG  SER A  80      12.021  -7.295   0.009  1.00 24.52           O  
ANISOU  647  OG  SER A  80     3047   3062   3206    -76   -123   -299       O  
ATOM    648  N   VAL A  81      13.168  -6.641  -4.356  1.00 17.19           N  
ANISOU  648  N   VAL A  81     1995   2364   2172      8    -90   -302       N  
ATOM    649  CA  VAL A  81      13.134  -6.773  -5.826  1.00 17.40           C  
ANISOU  649  CA  VAL A  81     2025   2388   2199      8    -89   -300       C  
ATOM    650  C   VAL A  81      14.439  -7.447  -6.300  1.00 21.10           C  
ANISOU  650  C   VAL A  81     2493   2856   2666      8    -86   -297       C  
ATOM    651  O   VAL A  81      14.392  -8.399  -7.084  1.00 20.13           O  
ANISOU  651  O   VAL A  81     2373   2733   2542      8    -85   -296       O  
ATOM    652  CB  VAL A  81      12.899  -5.415  -6.556  1.00 22.44           C  
ANISOU  652  CB  VAL A  81     2663   3024   2839      8    -91   -300       C  
ATOM    653  CG1 VAL A  81      12.952  -5.581  -8.079  1.00 22.84           C  
ANISOU  653  CG1 VAL A  81     2717   3073   2888      9    -90   -298       C  
ATOM    654  CG2 VAL A  81      11.570  -4.789  -6.145  1.00 22.40           C  
ANISOU  654  CG2 VAL A  81     2657   3019   2833      8    -95   -305       C  
ATOM    655  N   LYS A  82      15.597  -6.982  -5.788  1.00 19.52           N  
ANISOU  655  N   LYS A  82     2291   2655   2468      8    -86   -297       N  
ATOM    656  CA  LYS A  82      16.904  -7.547  -6.144  1.00 19.03           C  
ANISOU  656  CA  LYS A  82     2230   2593   2406      8    -84   -295       C  
ATOM    657  C   LYS A  82      16.975  -9.014  -5.728  1.00 21.30           C  
ANISOU  657  C   LYS A  82     2518   2882   2691      9    -83   -295       C  
ATOM    658  O   LYS A  82      17.483  -9.840  -6.486  1.00 20.64           O  
ANISOU  658  O   LYS A  82     2436   2798   2606      8    -82   -294       O  
ATOM    659  CB  LYS A  82      18.045  -6.734  -5.508  1.00 22.28           C  
ANISOU  659  CB  LYS A  82     2639   3004   2822      9    -84   -296       C  
ATOM    660  CG  LYS A  82      18.265  -5.371  -6.169  1.00 39.10           C  
ANISOU  660  CG  LYS A  82     4769   5133   4956      8    -84   -295       C  
ATOM    661  CD  LYS A  82      19.414  -4.603  -5.522  1.00 52.76           C  
ANISOU  661  CD  LYS A  82     6495   6861   6691      9    -84   -297       C  
ATOM    662  CE  LYS A  82      19.491  -3.172  -6.000  1.00 67.78           C  
ANISOU  662  CE  LYS A  82     8396   8760   8599      8    -85   -296       C  
ATOM    663  NZ  LYS A  82      20.524  -2.399  -5.258  1.00 78.31           N  
ANISOU  663  NZ  LYS A  82     9724  10092   9938     10    -84   -300       N  
ATOM    664  N   GLN A  83      16.411  -9.348  -4.546  1.00 17.06           N  
ANISOU  664  N   GLN A  83     1982   2348   2154      9    -84   -296       N  
ATOM    665  CA  GLN A  83      16.393 -10.726  -4.053  1.00 16.15           C  
ANISOU  665  CA  GLN A  83     1868   2233   2037     10    -82   -296       C  
ATOM    666  C   GLN A  83      15.554 -11.614  -4.973  1.00 18.95           C  
ANISOU  666  C   GLN A  83     2223   2587   2390      9    -82   -295       C  
ATOM    667  O   GLN A  83      15.973 -12.725  -5.303  1.00 17.65           O  
ANISOU  667  O   GLN A  83     2060   2422   2225      9    -81   -294       O  
ATOM    668  CB  GLN A  83      15.851 -10.773  -2.624  1.00 16.93           C  
ANISOU  668  CB  GLN A  83     1965   2334   2134     11    -83   -297       C  
ATOM    669  CG  GLN A  83      15.877 -12.171  -2.001  1.00 19.20           C  
ANISOU  669  CG  GLN A  83     2254   2622   2419     11    -81   -295       C  
ATOM    670  CD  GLN A  83      15.254 -12.186  -0.626  1.00 24.73           C  
ANISOU  670  CD  GLN A  83     2953   3325   3117     12    -81   -295       C  
ATOM    671  OE1 GLN A  83      14.776 -11.166  -0.118  1.00 23.16           O  
ANISOU  671  OE1 GLN A  83     2752   3129   2919     12    -83   -297       O  
ATOM    672  NE2 GLN A  83      15.227 -13.349  -0.002  1.00 20.97           N  
ANISOU  672  NE2 GLN A  83     2479   2850   2639     13    -80   -293       N  
ATOM    673  N   LEU A  84      14.359 -11.125  -5.366  1.00 16.55           N  
ANISOU  673  N   LEU A  84     1920   2283   2087      8    -82   -296       N  
ATOM    674  CA  LEU A  84      13.439 -11.828  -6.259  1.00 16.27           C  
ANISOU  674  CA  LEU A  84     1884   2246   2050      8    -81   -297       C  
ATOM    675  C   LEU A  84      14.132 -12.091  -7.597  1.00 18.86           C  
ANISOU  675  C   LEU A  84     2212   2574   2379      9    -81   -296       C  
ATOM    676  O   LEU A  84      14.099 -13.218  -8.085  1.00 17.79           O  
ANISOU  676  O   LEU A  84     2077   2439   2244     10    -80   -296       O  
ATOM    677  CB  LEU A  84      12.170 -10.960  -6.440  1.00 16.50           C  
ANISOU  677  CB  LEU A  84     1914   2275   2080      8    -82   -300       C  
ATOM    678  CG  LEU A  84      11.043 -11.464  -7.357  1.00 21.35           C  
ANISOU  678  CG  LEU A  84     2529   2890   2695      9    -81   -302       C  
ATOM    679  CD1 LEU A  84       9.755 -10.737  -7.049  1.00 21.15           C  
ANISOU  679  CD1 LEU A  84     2504   2865   2669      9    -83   -306       C  
ATOM    680  CD2 LEU A  84      11.370 -11.238  -8.827  1.00 24.85           C  
ANISOU  680  CD2 LEU A  84     2972   3333   3138     11    -82   -302       C  
ATOM    681  N   VAL A  85      14.748 -11.052  -8.187  1.00 16.81           N  
ANISOU  681  N   VAL A  85     1954   2315   2120      9    -81   -294       N  
ATOM    682  CA  VAL A  85      15.447 -11.176  -9.480  1.00 16.89           C  
ANISOU  682  CA  VAL A  85     1963   2325   2130     10    -81   -293       C  
ATOM    683  C   VAL A  85      16.516 -12.281  -9.424  1.00 19.26           C  
ANISOU  683  C   VAL A  85     2262   2626   2429      9    -81   -293       C  
ATOM    684  O   VAL A  85      16.545 -13.134 -10.310  1.00 19.16           O  
ANISOU  684  O   VAL A  85     2248   2615   2416     10    -81   -293       O  
ATOM    685  CB  VAL A  85      16.021  -9.817  -9.963  1.00 21.00           C  
ANISOU  685  CB  VAL A  85     2484   2845   2650      9    -81   -291       C  
ATOM    686  CG1 VAL A  85      16.980 -10.000 -11.142  1.00 21.37           C  
ANISOU  686  CG1 VAL A  85     2530   2893   2696     10    -80   -289       C  
ATOM    687  CG2 VAL A  85      14.900  -8.851 -10.337  1.00 20.99           C  
ANISOU  687  CG2 VAL A  85     2484   2843   2649     10    -82   -292       C  
ATOM    688  N   SER A  86      17.367 -12.279  -8.376  1.00 17.33           N  
ANISOU  688  N   SER A  86     2018   2381   2185      9    -81   -293       N  
ATOM    689  CA  SER A  86      18.420 -13.288  -8.226  1.00 17.40           C  
ANISOU  689  CA  SER A  86     2027   2391   2194      8    -81   -293       C  
ATOM    690  C   SER A  86      17.862 -14.679  -8.001  1.00 22.18           C  
ANISOU  690  C   SER A  86     2632   2996   2799      9    -82   -294       C  
ATOM    691  O   SER A  86      18.385 -15.650  -8.550  1.00 23.26           O  
ANISOU  691  O   SER A  86     2768   3134   2937      9    -83   -294       O  
ATOM    692  CB  SER A  86      19.371 -12.912  -7.092  1.00 22.70           C  
ANISOU  692  CB  SER A  86     2699   3062   2865      8    -82   -294       C  
ATOM    693  OG  SER A  86      19.993 -11.668  -7.370  1.00 35.15           O  
ANISOU  693  OG  SER A  86     4275   4638   4443      8    -81   -294       O  
ATOM    694  N   ASP A  87      16.782 -14.775  -7.219  1.00 18.81           N  
ANISOU  694  N   ASP A  87     2206   2569   2373      9    -81   -293       N  
ATOM    695  CA  ASP A  87      16.147 -16.041  -6.892  1.00 18.27           C  
ANISOU  695  CA  ASP A  87     2137   2499   2306      9    -80   -293       C  
ATOM    696  C   ASP A  87      15.497 -16.638  -8.131  1.00 22.09           C  
ANISOU  696  C   ASP A  87     2618   2983   2791     10    -80   -295       C  
ATOM    697  O   ASP A  87      15.763 -17.785  -8.491  1.00 22.55           O  
ANISOU  697  O   ASP A  87     2674   3041   2851     10    -81   -295       O  
ATOM    698  CB  ASP A  87      15.105 -15.783  -5.785  1.00 19.98           C  
ANISOU  698  CB  ASP A  87     2354   2715   2521      9    -79   -293       C  
ATOM    699  CG  ASP A  87      14.330 -16.960  -5.237  1.00 23.57           C  
ANISOU  699  CG  ASP A  87     2809   3169   2978      8    -77   -292       C  
ATOM    700  OD1 ASP A  87      14.648 -18.120  -5.606  1.00 23.70           O  
ANISOU  700  OD1 ASP A  87     2825   3184   2996      9    -78   -292       O  
ATOM    701  OD2 ASP A  87      13.420 -16.727  -4.426  1.00 23.14           O  
ANISOU  701  OD2 ASP A  87     2756   3115   2923      8    -76   -292       O  
ATOM    702  N   CYS A  88      14.664 -15.856  -8.805  1.00 18.12           N  
ANISOU  702  N   CYS A  88     2116   2481   2289     11    -80   -296       N  
ATOM    703  CA  CYS A  88      13.973 -16.399  -9.947  0.70 18.21           C  
ANISOU  703  CA  CYS A  88     2124   2493   2301     13    -79   -298       C  
ATOM    704  C   CYS A  88      14.853 -16.574 -11.222  1.00 20.32           C  
ANISOU  704  C   CYS A  88     2389   2764   2569     14    -81   -298       C  
ATOM    705  O   CYS A  88      14.553 -17.428 -12.054  1.00 20.25           O  
ANISOU  705  O   CYS A  88     2376   2756   2562     17    -81   -301       O  
ATOM    706  CB  CYS A  88      12.636 -15.695 -10.159  0.70 19.40           C  
ANISOU  706  CB  CYS A  88     2275   2644   2452     14    -78   -300       C  
ATOM    707  SG  CYS A  88      11.684 -15.446  -8.610  0.70 22.64           S  
ANISOU  707  SG  CYS A  88     2688   3052   2862     12    -77   -301       S  
ATOM    708  N   SER A  89      16.065 -15.955 -11.236  1.00 16.56           N  
ANISOU  708  N   SER A  89     1914   2288   2090     13    -82   -296       N  
ATOM    709  CA  SER A  89      17.040 -16.183 -12.316  1.00 16.39           C  
ANISOU  709  CA  SER A  89     1890   2270   2069     13    -83   -297       C  
ATOM    710  C   SER A  89      17.673 -17.593 -12.223  1.00 20.15           C  
ANISOU  710  C   SER A  89     2363   2747   2547     13    -85   -298       C  
ATOM    711  O   SER A  89      18.284 -18.039 -13.192  1.00 19.87           O  
ANISOU  711  O   SER A  89     2323   2714   2511     14    -87   -300       O  
ATOM    712  CB  SER A  89      18.138 -15.129 -12.288  1.00 18.79           C  
ANISOU  712  CB  SER A  89     2196   2574   2370     12    -83   -295       C  
ATOM    713  OG  SER A  89      17.635 -13.863 -12.674  1.00 25.07           O  
ANISOU  713  OG  SER A  89     2993   3369   3164     12    -82   -293       O  
ATOM    714  N   THR A  90      17.533 -18.289 -11.067  1.00 18.64           N  
ANISOU  714  N   THR A  90     2173   2552   2356     12    -85   -298       N  
ATOM    715  CA  THR A  90      18.100 -19.636 -10.880  1.00 18.25           C  
ANISOU  715  CA  THR A  90     2122   2503   2310     12    -88   -299       C  
ATOM    716  C   THR A  90      17.245 -20.745 -11.472  1.00 23.76           C  
ANISOU  716  C   THR A  90     2814   3200   3012     14    -88   -301       C  
ATOM    717  O   THR A  90      17.727 -21.878 -11.605  1.00 24.27           O  
ANISOU  717  O   THR A  90     2876   3266   3080     14    -91   -303       O  
ATOM    718  CB  THR A  90      18.432 -19.922  -9.405  1.00 24.10           C  
ANISOU  718  CB  THR A  90     2866   3240   3050     11    -88   -297       C  
ATOM    719  OG1 THR A  90      17.226 -20.001  -8.648  1.00 24.22           O  
ANISOU  719  OG1 THR A  90     2883   3253   3067     11    -85   -296       O  
ATOM    720  CG2 THR A  90      19.402 -18.917  -8.805  1.00 25.08           C  
ANISOU  720  CG2 THR A  90     2994   3365   3170      9    -87   -297       C  
ATOM    721  N   ILE A  91      15.966 -20.439 -11.797  1.00 20.30           N  
ANISOU  721  N   ILE A  91     2482   2637   2595    193   -162   -418       N  
ATOM    722  CA  ILE A  91      15.042 -21.411 -12.383  1.00 20.19           C  
ANISOU  722  CA  ILE A  91     2473   2620   2577    191   -164   -413       C  
ATOM    723  C   ILE A  91      15.526 -21.744 -13.783  1.00 23.82           C  
ANISOU  723  C   ILE A  91     2937   3077   3036    189   -163   -413       C  
ATOM    724  O   ILE A  91      15.658 -20.860 -14.624  1.00 22.31           O  
ANISOU  724  O   ILE A  91     2746   2884   2846    186   -162   -413       O  
ATOM    725  CB  ILE A  91      13.570 -20.918 -12.344  1.00 22.97           C  
ANISOU  725  CB  ILE A  91     2825   2973   2931    189   -166   -411       C  
ATOM    726  CG1 ILE A  91      13.078 -20.796 -10.878  1.00 23.32           C  
ANISOU  726  CG1 ILE A  91     2864   3021   2975    191   -168   -411       C  
ATOM    727  CG2 ILE A  91      12.647 -21.845 -13.172  1.00 23.20           C  
ANISOU  727  CG2 ILE A  91     2859   2999   2958    187   -168   -407       C  
ATOM    728  CD1 ILE A  91      11.871 -19.943 -10.711  1.00 27.57           C  
ANISOU  728  CD1 ILE A  91     3401   3560   3516    189   -170   -411       C  
ATOM    729  N   SER A  92      15.854 -23.013 -13.990  1.00 23.10           N  
ANISOU  729  N   SER A  92     2848   2986   2943    189   -164   -413       N  
ATOM    730  CA  SER A  92      16.356 -23.536 -15.247  1.00 23.97           C  
ANISOU  730  CA  SER A  92     2960   3094   3051    187   -163   -413       C  
ATOM    731  C   SER A  92      15.491 -24.729 -15.567  1.00 27.33           C  
ANISOU  731  C   SER A  92     3389   3519   3477    187   -165   -410       C  
ATOM    732  O   SER A  92      15.405 -25.674 -14.782  1.00 26.77           O  
ANISOU  732  O   SER A  92     3317   3448   3405    189   -167   -409       O  
ATOM    733  CB  SER A  92      17.825 -23.932 -15.114  1.00 29.12           C  
ANISOU  733  CB  SER A  92     3612   3748   3703    189   -163   -419       C  
ATOM    734  OG  SER A  92      18.319 -24.490 -16.320  1.00 37.63           O  
ANISOU  734  OG  SER A  92     4692   4825   4780    186   -163   -420       O  
ATOM    735  N   GLU A  93      14.775 -24.636 -16.675  1.00 24.92           N  
ANISOU  735  N   GLU A  93     3084   3212   3171    185   -166   -408       N  
ATOM    736  CA  GLU A  93      13.827 -25.658 -17.080  1.00 25.22           C  
ANISOU  736  CA  GLU A  93     3124   3249   3209    185   -167   -405       C  
ATOM    737  C   GLU A  93      13.856 -25.773 -18.584  1.00 28.92           C  
ANISOU  737  C   GLU A  93     3593   3717   3677    183   -167   -405       C  
ATOM    738  O   GLU A  93      13.676 -24.763 -19.268  1.00 28.92           O  
ANISOU  738  O   GLU A  93     3595   3717   3677    182   -166   -405       O  
ATOM    739  CB  GLU A  93      12.431 -25.224 -16.596  1.00 27.05           C  
ANISOU  739  CB  GLU A  93     3356   3481   3441    185   -167   -403       C  
ATOM    740  CG  GLU A  93      11.569 -26.301 -15.980  1.00 37.77           C  
ANISOU  740  CG  GLU A  93     4715   4838   4799    186   -168   -402       C  
ATOM    741  CD  GLU A  93      12.230 -27.187 -14.945  1.00 52.20           C  
ANISOU  741  CD  GLU A  93     6541   6666   6626    187   -168   -402       C  
ATOM    742  OE1 GLU A  93      12.578 -26.688 -13.852  1.00 43.46           O  
ANISOU  742  OE1 GLU A  93     5434   5561   5519    189   -168   -402       O  
ATOM    743  OE2 GLU A  93      12.395 -28.391 -15.234  1.00 40.81           O  
ANISOU  743  OE2 GLU A  93     5100   5223   5184    188   -169   -401       O  
ATOM    744  N   GLU A  94      14.102 -26.993 -19.104  1.00 25.40           N  
ANISOU  744  N   GLU A  94     3147   3272   3231    183   -168   -406       N  
ATOM    745  CA  GLU A  94      14.136 -27.236 -20.550  1.00 25.97           C  
ANISOU  745  CA  GLU A  94     3219   3346   3304    182   -168   -407       C  
ATOM    746  C   GLU A  94      12.717 -27.107 -21.112  1.00 26.83           C  
ANISOU  746  C   GLU A  94     3328   3454   3413    183   -168   -405       C  
ATOM    747  O   GLU A  94      12.550 -26.657 -22.244  1.00 26.88           O  
ANISOU  747  O   GLU A  94     3335   3461   3418    183   -167   -405       O  
ATOM    748  CB  GLU A  94      14.738 -28.615 -20.879  1.00 27.99           C  
ANISOU  748  CB  GLU A  94     3471   3602   3561    183   -170   -409       C  
ATOM    749  CG  GLU A  94      15.142 -28.793 -22.338  1.00 43.85           C  
ANISOU  749  CG  GLU A  94     5478   5614   5569    181   -170   -411       C  
ATOM    750  CD  GLU A  94      16.440 -28.159 -22.811  1.00 73.40           C  
ANISOU  750  CD  GLU A  94     9220   9358   9309    178   -170   -415       C  
ATOM    751  OE1 GLU A  94      17.356 -27.953 -21.981  1.00 74.13           O  
ANISOU  751  OE1 GLU A  94     9314   9451   9402    178   -169   -417       O  
ATOM    752  OE2 GLU A  94      16.561 -27.925 -24.035  1.00 69.59           O  
ANISOU  752  OE2 GLU A  94     8737   8878   8826    176   -169   -415       O  
ATOM    753  N   ASN A  95      11.698 -27.471 -20.311  1.00 20.46           N  
ANISOU  753  N   ASN A  95     2522   2646   2607    185   -168   -404       N  
ATOM    754  CA  ASN A  95      10.299 -27.337 -20.718  1.00 18.14           C  
ANISOU  754  CA  ASN A  95     2228   2350   2313    186   -168   -403       C  
ATOM    755  C   ASN A  95       9.896 -25.865 -20.463  1.00 19.08           C  
ANISOU  755  C   ASN A  95     2349   2469   2431    185   -168   -403       C  
ATOM    756  O   ASN A  95       9.827 -25.462 -19.300  1.00 17.50           O  
ANISOU  756  O   ASN A  95     2150   2268   2231    185   -168   -402       O  
ATOM    757  CB  ASN A  95       9.422 -28.308 -19.944  1.00 16.57           C  
ANISOU  757  CB  ASN A  95     2028   2150   2116    187   -168   -404       C  
ATOM    758  CG  ASN A  95       7.942 -28.199 -20.269  1.00 22.21           C  
ANISOU  758  CG  ASN A  95     2743   2864   2830    188   -167   -405       C  
ATOM    759  OD1 ASN A  95       7.454 -27.212 -20.841  1.00 21.25           O  
ANISOU  759  OD1 ASN A  95     2624   2743   2708    188   -168   -406       O  
ATOM    760  ND2 ASN A  95       7.196 -29.204 -19.892  1.00 19.76           N  
ANISOU  760  ND2 ASN A  95     2432   2553   2522    188   -166   -407       N  
ATOM    761  N   PRO A  96       9.646 -25.046 -21.513  1.00 16.83           N  
ANISOU  761  N   PRO A  96     2067   2184   2145    185   -168   -402       N  
ATOM    762  CA  PRO A  96       9.337 -23.622 -21.277  1.00 17.06           C  
ANISOU  762  CA  PRO A  96     2097   2211   2172    185   -169   -402       C  
ATOM    763  C   PRO A  96       8.016 -23.365 -20.553  1.00 19.45           C  
ANISOU  763  C   PRO A  96     2400   2513   2476    186   -170   -403       C  
ATOM    764  O   PRO A  96       7.865 -22.330 -19.906  1.00 18.65           O  
ANISOU  764  O   PRO A  96     2300   2412   2376    185   -172   -403       O  
ATOM    765  CB  PRO A  96       9.362 -23.017 -22.684  1.00 19.25           C  
ANISOU  765  CB  PRO A  96     2377   2489   2448    185   -168   -401       C  
ATOM    766  CG  PRO A  96       9.012 -24.149 -23.580  1.00 23.61           C  
ANISOU  766  CG  PRO A  96     2928   3043   3000    187   -168   -402       C  
ATOM    767  CD  PRO A  96       9.658 -25.355 -22.960  1.00 18.77           C  
ANISOU  767  CD  PRO A  96     2312   2432   2389    186   -168   -403       C  
ATOM    768  N   HIS A  97       7.064 -24.309 -20.658  1.00 16.25           N  
ANISOU  768  N   HIS A  97     1994   2108   2071    187   -170   -405       N  
ATOM    769  CA  HIS A  97       5.768 -24.197 -20.000  1.00 14.82           C  
ANISOU  769  CA  HIS A  97     1814   1927   1891    187   -172   -408       C  
ATOM    770  C   HIS A  97       5.957 -24.419 -18.500  1.00 16.38           C  
ANISOU  770  C   HIS A  97     2010   2125   2089    185   -172   -408       C  
ATOM    771  O   HIS A  97       5.417 -23.664 -17.690  1.00 14.68           O  
ANISOU  771  O   HIS A  97     1793   1909   1873    184   -173   -409       O  
ATOM    772  CB  HIS A  97       4.770 -25.205 -20.585  1.00 15.80           C  
ANISOU  772  CB  HIS A  97     1937   2051   2015    190   -171   -412       C  
ATOM    773  CG  HIS A  97       4.388 -24.942 -22.010  1.00 19.25           C  
ANISOU  773  CG  HIS A  97     2375   2488   2450    193   -171   -414       C  
ATOM    774  ND1 HIS A  97       4.370 -23.661 -22.537  1.00 21.67           N  
ANISOU  774  ND1 HIS A  97     2685   2794   2755    193   -173   -413       N  
ATOM    775  CD2 HIS A  97       3.941 -25.802 -22.949  1.00 20.77           C  
ANISOU  775  CD2 HIS A  97     2566   2682   2643    195   -170   -417       C  
ATOM    776  CE1 HIS A  97       3.950 -23.796 -23.785  1.00 20.46           C  
ANISOU  776  CE1 HIS A  97     2532   2641   2600    197   -173   -415       C  
ATOM    777  NE2 HIS A  97       3.671 -25.061 -24.072  1.00 20.91           N  
ANISOU  777  NE2 HIS A  97     2586   2700   2659    198   -171   -417       N  
ATOM    778  N   LEU A  98       6.794 -25.414 -18.126  1.00 15.42           N  
ANISOU  778  N   LEU A  98     1887   2004   1968    185   -170   -406       N  
ATOM    779  CA  LEU A  98       7.086 -25.653 -16.713  1.00 15.34           C  
ANISOU  779  CA  LEU A  98     1876   1995   1959    184   -170   -405       C  
ATOM    780  C   LEU A  98       7.917 -24.505 -16.152  1.00 17.39           C  
ANISOU  780  C   LEU A  98     2134   2255   2218    184   -171   -404       C  
ATOM    781  O   LEU A  98       7.755 -24.134 -14.987  1.00 16.97           O  
ANISOU  781  O   LEU A  98     2079   2204   2165    183   -171   -404       O  
ATOM    782  CB  LEU A  98       7.790 -27.005 -16.518  1.00 15.81           C  
ANISOU  782  CB  LEU A  98     1934   2053   2018    185   -168   -403       C  
ATOM    783  CG  LEU A  98       8.159 -27.404 -15.082  1.00 20.34           C  
ANISOU  783  CG  LEU A  98     2508   2628   2592    185   -168   -401       C  
ATOM    784  CD1 LEU A  98       6.943 -27.461 -14.181  1.00 20.03           C  
ANISOU  784  CD1 LEU A  98     2469   2590   2552    183   -168   -402       C  
ATOM    785  CD2 LEU A  98       8.884 -28.747 -15.074  1.00 22.14           C  
ANISOU  785  CD2 LEU A  98     2737   2856   2821    186   -167   -400       C  
ATOM    786  N   LYS A  99       8.799 -23.925 -16.983  1.00 15.43           N  
ANISOU  786  N   LYS A  99     1886   2007   1970    184   -170   -403       N  
ATOM    787  CA  LYS A  99       9.597 -22.777 -16.577  1.00 14.40           C  
ANISOU  787  CA  LYS A  99     1755   1877   1840    183   -170   -403       C  
ATOM    788  C   LYS A  99       8.671 -21.624 -16.186  1.00 16.31           C  
ANISOU  788  C   LYS A  99     1996   2119   2083    183   -172   -404       C  
ATOM    789  O   LYS A  99       8.893 -20.993 -15.154  1.00 14.79           O  
ANISOU  789  O   LYS A  99     1800   1928   1892    183   -173   -405       O  
ATOM    790  CB  LYS A  99      10.529 -22.323 -17.703  1.00 17.02           C  
ANISOU  790  CB  LYS A  99     2088   2207   2171    183   -169   -402       C  
ATOM    791  CG  LYS A  99      11.689 -21.501 -17.171  1.00 28.08           C  
ANISOU  791  CG  LYS A  99     3487   3609   3573    182   -167   -403       C  
ATOM    792  CD  LYS A  99      12.179 -20.514 -18.186  1.00 35.16           C  
ANISOU  792  CD  LYS A  99     4386   4504   4470    181   -166   -403       C  
ATOM    793  CE  LYS A  99      13.457 -19.850 -17.740  1.00 34.99           C  
ANISOU  793  CE  LYS A  99     4362   4483   4451    180   -164   -405       C  
ATOM    794  NZ  LYS A  99      14.601 -20.307 -18.566  1.00 44.43           N  
ANISOU  794  NZ  LYS A  99     5558   5678   5644    179   -161   -406       N  
ATOM    795  N   ALA A 100       7.610 -21.387 -16.978  1.00 12.90           N  
ANISOU  795  N   ALA A 100     1566   1685   1651    183   -174   -405       N  
ATOM    796  CA  ALA A 100       6.667 -20.310 -16.701  1.00 12.60           C  
ANISOU  796  CA  ALA A 100     1527   1646   1613    182   -177   -408       C  
ATOM    797  C   ALA A 100       5.927 -20.490 -15.380  1.00 14.02           C  
ANISOU  797  C   ALA A 100     1704   1829   1793    181   -179   -410       C  
ATOM    798  O   ALA A 100       5.815 -19.527 -14.629  1.00 13.23           O  
ANISOU  798  O   ALA A 100     1601   1731   1696    181   -181   -412       O  
ATOM    799  CB  ALA A 100       5.681 -20.161 -17.845  1.00 13.65           C  
ANISOU  799  CB  ALA A 100     1664   1777   1744    184   -179   -409       C  
ATOM    800  N   SER A 101       5.430 -21.713 -15.085  1.00 11.73           N  
ANISOU  800  N   SER A 101     1337   1615   1504     58   -295   -333       N  
ATOM    801  CA  SER A 101       4.714 -21.906 -13.823  1.00 12.45           C  
ANISOU  801  CA  SER A 101     1429   1704   1597     53   -295   -332       C  
ATOM    802  C   SER A 101       5.682 -21.832 -12.645  1.00 14.73           C  
ANISOU  802  C   SER A 101     1717   1997   1883     48   -294   -330       C  
ATOM    803  O   SER A 101       5.334 -21.251 -11.620  1.00 13.23           O  
ANISOU  803  O   SER A 101     1527   1807   1692     43   -291   -330       O  
ATOM    804  CB  SER A 101       3.949 -23.223 -13.822  1.00 14.31           C  
ANISOU  804  CB  SER A 101     1663   1935   1837     55   -300   -331       C  
ATOM    805  OG  SER A 101       4.843 -24.298 -14.053  1.00 15.69           O  
ANISOU  805  OG  SER A 101     1837   2112   2012     59   -307   -331       O  
ATOM    806  N   LYS A 102       6.930 -22.337 -12.805  1.00 12.08           N  
ANISOU  806  N   LYS A 102     1380   1664   1545     50   -296   -331       N  
ATOM    807  CA  LYS A 102       7.919 -22.239 -11.735  1.00 11.88           C  
ANISOU  807  CA  LYS A 102     1354   1642   1517     46   -296   -331       C  
ATOM    808  C   LYS A 102       8.269 -20.779 -11.465  1.00 15.77           C  
ANISOU  808  C   LYS A 102     1847   2137   2009     43   -290   -331       C  
ATOM    809  O   LYS A 102       8.440 -20.400 -10.311  1.00 17.33           O  
ANISOU  809  O   LYS A 102     2045   2335   2206     40   -289   -331       O  
ATOM    810  CB  LYS A 102       9.160 -23.065 -12.059  1.00 14.27           C  
ANISOU  810  CB  LYS A 102     1656   1948   1818     49   -300   -333       C  
ATOM    811  CG  LYS A 102       8.876 -24.546 -11.909  1.00 20.43           C  
ANISOU  811  CG  LYS A 102     2436   2725   2600     51   -309   -333       C  
ATOM    812  CD  LYS A 102      10.095 -25.382 -12.088  1.00 26.87           C  
ANISOU  812  CD  LYS A 102     3251   3545   3414     55   -315   -337       C  
ATOM    813  CE  LYS A 102       9.814 -26.797 -11.644  1.00 33.97           C  
ANISOU  813  CE  LYS A 102     4150   4440   4316     55   -325   -336       C  
ATOM    814  NZ  LYS A 102      11.055 -27.603 -11.624  1.00 44.98           N  
ANISOU  814  NZ  LYS A 102     5545   5837   5708     58   -333   -342       N  
ATOM    815  N   LEU A 103       8.316 -19.953 -12.522  1.00 13.13           N  
ANISOU  815  N   LEU A 103     1513   1804   1674     44   -288   -331       N  
ATOM    816  CA  LEU A 103       8.597 -18.522 -12.368  1.00 12.08           C  
ANISOU  816  CA  LEU A 103     1378   1670   1540     41   -285   -331       C  
ATOM    817  C   LEU A 103       7.478 -17.786 -11.636  1.00 15.03           C  
ANISOU  817  C   LEU A 103     1753   2041   1915     38   -284   -332       C  
ATOM    818  O   LEU A 103       7.762 -16.985 -10.742  1.00 14.23           O  
ANISOU  818  O   LEU A 103     1652   1941   1815     36   -284   -332       O  
ATOM    819  CB  LEU A 103       8.899 -17.860 -13.713  1.00 12.49           C  
ANISOU  819  CB  LEU A 103     1430   1725   1592     42   -284   -330       C  
ATOM    820  CG  LEU A 103      10.323 -18.086 -14.227  1.00 15.77           C  
ANISOU  820  CG  LEU A 103     1843   2146   2004     43   -284   -329       C  
ATOM    821  CD1 LEU A 103      10.401 -17.815 -15.698  1.00 17.02           C  
ANISOU  821  CD1 LEU A 103     1999   2307   2161     46   -283   -327       C  
ATOM    822  CD2 LEU A 103      11.340 -17.238 -13.464  1.00 16.40           C  
ANISOU  822  CD2 LEU A 103     1921   2227   2085     39   -282   -328       C  
ATOM    823  N   VAL A 104       6.212 -18.052 -11.994  1.00 12.00           N  
ANISOU  823  N   VAL A 104     1372   1655   1534     39   -285   -332       N  
ATOM    824  CA  VAL A 104       5.081 -17.428 -11.304  1.00 11.87           C  
ANISOU  824  CA  VAL A 104     1356   1637   1518     37   -284   -334       C  
ATOM    825  C   VAL A 104       5.082 -17.875  -9.838  1.00 14.73           C  
ANISOU  825  C   VAL A 104     1716   2002   1878     36   -285   -334       C  
ATOM    826  O   VAL A 104       4.854 -17.055  -8.958  1.00 13.85           O  
ANISOU  826  O   VAL A 104     1603   1892   1766     35   -285   -335       O  
ATOM    827  CB  VAL A 104       3.745 -17.711 -12.027  1.00 14.70           C  
ANISOU  827  CB  VAL A 104     1716   1991   1878     39   -285   -336       C  
ATOM    828  CG1 VAL A 104       2.539 -17.311 -11.172  1.00 14.77           C  
ANISOU  828  CG1 VAL A 104     1724   2000   1886     37   -285   -339       C  
ATOM    829  CG2 VAL A 104       3.700 -16.984 -13.372  1.00 14.49           C  
ANISOU  829  CG2 VAL A 104     1692   1962   1852     41   -285   -337       C  
ATOM    830  N   GLN A 105       5.368 -19.163  -9.575  1.00 12.62           N  
ANISOU  830  N   GLN A 105     1449   1735   1611     37   -286   -331       N  
ATOM    831  CA  GLN A 105       5.450 -19.668  -8.210  1.00 12.80           C  
ANISOU  831  CA  GLN A 105     1471   1761   1632     35   -286   -330       C  
ATOM    832  C   GLN A 105       6.550 -18.916  -7.428  1.00 16.15           C  
ANISOU  832  C   GLN A 105     1893   2187   2054     35   -285   -331       C  
ATOM    833  O   GLN A 105       6.333 -18.537  -6.273  1.00 15.89           O  
ANISOU  833  O   GLN A 105     1860   2159   2021     35   -285   -332       O  
ATOM    834  CB  GLN A 105       5.709 -21.180  -8.236  1.00 13.27           C  
ANISOU  834  CB  GLN A 105     1531   1819   1693     35   -289   -327       C  
ATOM    835  CG  GLN A 105       5.819 -21.806  -6.844  1.00 17.52           C  
ANISOU  835  CG  GLN A 105     2068   2360   2229     33   -290   -324       C  
ATOM    836  CD  GLN A 105       6.133 -23.275  -6.926  1.00 29.65           C  
ANISOU  836  CD  GLN A 105     3605   3894   3766     33   -295   -322       C  
ATOM    837  OE1 GLN A 105       7.161 -23.688  -7.473  1.00 24.12           O  
ANISOU  837  OE1 GLN A 105     2906   3192   3066     36   -298   -324       O  
ATOM    838  NE2 GLN A 105       5.234 -24.098  -6.414  1.00 24.11           N  
ANISOU  838  NE2 GLN A 105     2903   3192   3065     31   -297   -317       N  
ATOM    839  N   CYS A 106       7.707 -18.655  -8.071  1.00 13.25           N  
ANISOU  839  N   CYS A 106     1526   1819   1688     36   -285   -332       N  
ATOM    840  CA  CYS A 106       8.815 -17.930  -7.456  1.00 15.01           C  
ANISOU  840  CA  CYS A 106     1749   2044   1912     36   -285   -333       C  
ATOM    841  C   CYS A 106       8.425 -16.492  -7.118  1.00 17.04           C  
ANISOU  841  C   CYS A 106     2004   2301   2170     36   -285   -335       C  
ATOM    842  O   CYS A 106       8.628 -16.050  -5.984  1.00 16.53           O  
ANISOU  842  O   CYS A 106     1937   2238   2105     37   -286   -337       O  
ATOM    843  CB  CYS A 106      10.033 -17.971  -8.367  1.00 16.80           C  
ANISOU  843  CB  CYS A 106     1975   2271   2139     37   -285   -333       C  
ATOM    844  SG  CYS A 106      11.526 -17.241  -7.640  1.00 21.80           S  
ANISOU  844  SG  CYS A 106     2607   2905   2773     37   -284   -335       S  
ATOM    845  N   VAL A 107       7.836 -15.771  -8.087  1.00 13.53           N  
ANISOU  845  N   VAL A 107     1560   1855   1727     35   -286   -335       N  
ATOM    846  CA  VAL A 107       7.413 -14.379  -7.867  1.00 13.31           C  
ANISOU  846  CA  VAL A 107     1530   1827   1701     35   -289   -338       C  
ATOM    847  C   VAL A 107       6.359 -14.328  -6.730  1.00 15.84           C  
ANISOU  847  C   VAL A 107     1849   2151   2019     36   -290   -340       C  
ATOM    848  O   VAL A 107       6.393 -13.409  -5.912  1.00 14.42           O  
ANISOU  848  O   VAL A 107     1667   1973   1840     38   -294   -343       O  
ATOM    849  CB  VAL A 107       6.859 -13.719  -9.164  1.00 16.31           C  
ANISOU  849  CB  VAL A 107     1912   2204   2082     33   -290   -338       C  
ATOM    850  CG1 VAL A 107       6.371 -12.292  -8.894  1.00 15.49           C  
ANISOU  850  CG1 VAL A 107     1807   2099   1981     33   -295   -341       C  
ATOM    851  CG2 VAL A 107       7.901 -13.720 -10.288  1.00 15.95           C  
ANISOU  851  CG2 VAL A 107     1867   2157   2037     32   -288   -334       C  
ATOM    852  N   SER A 108       5.436 -15.310  -6.698  1.00 14.99           N  
ANISOU  852  N   SER A 108     1742   2044   1909     35   -288   -339       N  
ATOM    853  CA  SER A 108       4.330 -15.405  -5.738  1.00 14.37           C  
ANISOU  853  CA  SER A 108     1662   1971   1828     36   -288   -341       C  
ATOM    854  C   SER A 108       4.754 -15.479  -4.283  1.00 19.12           C  
ANISOU  854  C   SER A 108     2261   2578   2427     38   -289   -341       C  
ATOM    855  O   SER A 108       3.969 -15.096  -3.410  1.00 20.74           O  
ANISOU  855  O   SER A 108     2462   2789   2629     40   -290   -343       O  
ATOM    856  CB  SER A 108       3.385 -16.549  -6.086  1.00 16.21           C  
ANISOU  856  CB  SER A 108     1896   2203   2059     34   -286   -338       C  
ATOM    857  OG  SER A 108       2.739 -16.286  -7.323  1.00 17.50           O  
ANISOU  857  OG  SER A 108     2062   2362   2226     34   -286   -340       O  
ATOM    858  N   LYS A 109       5.991 -15.934  -4.019  1.00 15.38           N  
ANISOU  858  N   LYS A 109     1788   2103   1954     39   -288   -339       N  
ATOM    859  CA  LYS A 109       6.549 -15.969  -2.658  1.00 15.66           C  
ANISOU  859  CA  LYS A 109     1820   2142   1987     42   -288   -340       C  
ATOM    860  C   LYS A 109       6.719 -14.538  -2.110  1.00 20.14           C  
ANISOU  860  C   LYS A 109     2385   2712   2557     47   -292   -345       C  
ATOM    861  O   LYS A 109       6.684 -14.341  -0.890  1.00 21.19           O  
ANISOU  861  O   LYS A 109     2513   2850   2687     51   -294   -347       O  
ATOM    862  CB  LYS A 109       7.945 -16.612  -2.647  1.00 17.66           C  
ANISOU  862  CB  LYS A 109     2076   2391   2241     43   -287   -338       C  
ATOM    863  CG  LYS A 109       7.996 -18.100  -2.961  1.00 30.48           C  
ANISOU  863  CG  LYS A 109     3703   4014   3864     40   -285   -334       C  
ATOM    864  CD  LYS A 109       9.391 -18.668  -2.642  1.00 38.53           C  
ANISOU  864  CD  LYS A 109     4724   5030   4883     41   -285   -335       C  
ATOM    865  CE  LYS A 109      10.499 -18.083  -3.493  1.00 45.00           C  
ANISOU  865  CE  LYS A 109     5544   5846   5706     41   -286   -338       C  
ATOM    866  NZ  LYS A 109      11.838 -18.531  -3.037  1.00 52.98           N  
ANISOU  866  NZ  LYS A 109     6557   6856   6718     43   -286   -340       N  
ATOM    867  N   TYR A 110       6.961 -13.559  -3.000  1.00 15.93           N  
ANISOU  867  N   TYR A 110     1851   2173   2027     46   -295   -346       N  
ATOM    868  CA  TYR A 110       7.211 -12.153  -2.646  1.00 15.73           C  
ANISOU  868  CA  TYR A 110     1822   2148   2006     50   -302   -351       C  
ATOM    869  C   TYR A 110       5.915 -11.355  -2.585  1.00 20.19           C  
ANISOU  869  C   TYR A 110     2385   2717   2570     51   -307   -355       C  
ATOM    870  O   TYR A 110       5.654 -10.685  -1.587  1.00 20.94           O  
ANISOU  870  O   TYR A 110     2475   2817   2664     56   -313   -360       O  
ATOM    871  CB  TYR A 110       8.241 -11.531  -3.613  1.00 16.69           C  
ANISOU  871  CB  TYR A 110     1946   2263   2134     48   -303   -349       C  
ATOM    872  CG  TYR A 110       9.579 -12.240  -3.578  1.00 16.99           C  
ANISOU  872  CG  TYR A 110     1985   2299   2173     47   -299   -346       C  
ATOM    873  CD1 TYR A 110      10.617 -11.769  -2.779  1.00 18.80           C  
ANISOU  873  CD1 TYR A 110     2211   2526   2406     52   -302   -348       C  
ATOM    874  CD2 TYR A 110       9.797 -13.404  -4.313  1.00 16.50           C  
ANISOU  874  CD2 TYR A 110     1927   2235   2108     44   -294   -343       C  
ATOM    875  CE1 TYR A 110      11.849 -12.418  -2.741  1.00 19.63           C  
ANISOU  875  CE1 TYR A 110     2318   2628   2512     52   -298   -347       C  
ATOM    876  CE2 TYR A 110      11.022 -14.068  -4.273  1.00 17.20           C  
ANISOU  876  CE2 TYR A 110     2017   2322   2197     44   -291   -342       C  
ATOM    877  CZ  TYR A 110      12.031 -13.593  -3.450  1.00 22.69           C  
ANISOU  877  CZ  TYR A 110     2709   3015   2895     48   -293   -345       C  
ATOM    878  OH  TYR A 110      13.244 -14.236  -3.400  1.00 23.04           O  
ANISOU  878  OH  TYR A 110     2756   3059   2941     48   -291   -345       O  
ATOM    879  N   LYS A 111       5.095 -11.439  -3.643  1.00 15.87           N  
ANISOU  879  N   LYS A 111     1943   2214   1872     56      8   -610       N  
ATOM    880  CA  LYS A 111       3.770 -10.812  -3.724  1.00 15.51           C  
ANISOU  880  CA  LYS A 111     1901   2169   1825     55     13   -601       C  
ATOM    881  C   LYS A 111       2.950 -11.621  -4.699  1.00 17.15           C  
ANISOU  881  C   LYS A 111     2104   2378   2034     54     12   -599       C  
ATOM    882  O   LYS A 111       3.453 -11.982  -5.765  1.00 17.36           O  
ANISOU  882  O   LYS A 111     2126   2408   2062     51     11   -604       O  
ATOM    883  CB  LYS A 111       3.807  -9.359  -4.249  1.00 18.43           C  
ANISOU  883  CB  LYS A 111     2271   2542   2191     53     18   -600       C  
ATOM    884  CG  LYS A 111       4.210  -8.276  -3.261  1.00 34.89           C  
ANISOU  884  CG  LYS A 111     4359   4625   4273     54     21   -600       C  
ATOM    885  CD  LYS A 111       3.409  -8.285  -1.961  1.00 46.85           C  
ANISOU  885  CD  LYS A 111     5875   6136   5788     58     21   -594       C  
ATOM    886  CE  LYS A 111       2.432  -7.157  -1.887  1.00 59.72           C  
ANISOU  886  CE  LYS A 111     7507   7767   7417     57     25   -588       C  
ATOM    887  NZ  LYS A 111       2.768  -6.193  -0.813  1.00 68.27           N  
ANISOU  887  NZ  LYS A 111     8591   8850   8500     59     27   -588       N  
ATOM    888  N   THR A 112       1.672 -11.829  -4.374  1.00 14.69           N  
ANISOU  888  N   THR A 112     1795   2066   1722     55     14   -592       N  
ATOM    889  CA  THR A 112       0.764 -12.538  -5.266  1.00 14.64           C  
ANISOU  889  CA  THR A 112     1785   2061   1717     55     15   -590       C  
ATOM    890  C   THR A 112       0.053 -11.522  -6.141  1.00 16.72           C  
ANISOU  890  C   THR A 112     2048   2327   1978     53     19   -587       C  
ATOM    891  O   THR A 112       0.007 -10.337  -5.798  1.00 16.88           O  
ANISOU  891  O   THR A 112     2071   2346   1995     53     21   -585       O  
ATOM    892  CB  THR A 112      -0.251 -13.360  -4.461  1.00 16.07           C  
ANISOU  892  CB  THR A 112     1969   2239   1898     57     14   -586       C  
ATOM    893  OG1 THR A 112      -1.106 -12.467  -3.747  1.00 16.20           O  
ANISOU  893  OG1 THR A 112     1990   2254   1912     57     17   -582       O  
ATOM    894  CG2 THR A 112       0.412 -14.360  -3.500  1.00 16.52           C  
ANISOU  894  CG2 THR A 112     2028   2292   1957     58      9   -588       C  
ATOM    895  N   MET A 113      -0.543 -11.978  -7.256  1.00 14.17           N  
ANISOU  895  N   MET A 113     1721   2007   1656     52     20   -587       N  
ATOM    896  CA  MET A 113      -1.335 -11.070  -8.096  1.00 12.62           C  
ANISOU  896  CA  MET A 113     1525   1813   1457     52     23   -584       C  
ATOM    897  C   MET A 113      -2.551 -10.583  -7.314  1.00 17.00           C  
ANISOU  897  C   MET A 113     2085   2365   2010     55     25   -580       C  
ATOM    898  O   MET A 113      -2.902  -9.409  -7.411  1.00 17.15           O  
ANISOU  898  O   MET A 113     2106   2382   2026     55     26   -578       O  
ATOM    899  CB  MET A 113      -1.777 -11.770  -9.372  1.00 13.99           C  
ANISOU  899  CB  MET A 113     1693   1992   1633     50     24   -586       C  
ATOM    900  CG  MET A 113      -0.637 -11.983 -10.312  1.00 15.89           C  
ANISOU  900  CG  MET A 113     1928   2236   1874     45     23   -591       C  
ATOM    901  SD  MET A 113      -1.186 -12.528 -11.942  1.00 18.12           S  
ANISOU  901  SD  MET A 113     2201   2525   2157     43     25   -592       S  
ATOM    902  CE  MET A 113      -1.195 -14.290 -11.703  1.00 15.28           C  
ANISOU  902  CE  MET A 113     1833   2166   1805     45     23   -595       C  
ATOM    903  N   LYS A 114      -3.141 -11.459  -6.476  1.00 14.72           N  
ANISOU  903  N   LYS A 114     1796   2074   1722     57     25   -580       N  
ATOM    904  CA  LYS A 114      -4.307 -11.090  -5.662  1.00 14.48           C  
ANISOU  904  CA  LYS A 114     1769   2042   1690     58     26   -578       C  
ATOM    905  C   LYS A 114      -3.988  -9.937  -4.706  1.00 17.72           C  
ANISOU  905  C   LYS A 114     2184   2450   2099     58     26   -577       C  
ATOM    906  O   LYS A 114      -4.841  -9.061  -4.500  1.00 18.59           O  
ANISOU  906  O   LYS A 114     2295   2560   2208     58     26   -577       O  
ATOM    907  CB  LYS A 114      -4.792 -12.291  -4.846  1.00 16.49           C  
ANISOU  907  CB  LYS A 114     2025   2295   1945     58     26   -579       C  
ATOM    908  CG  LYS A 114      -6.111 -12.002  -4.116  1.00 25.91           C  
ANISOU  908  CG  LYS A 114     3221   3488   3136     58     28   -580       C  
ATOM    909  CD  LYS A 114      -6.490 -13.111  -3.189  1.00 36.50           C  
ANISOU  909  CD  LYS A 114     4564   4827   4475     56     29   -580       C  
ATOM    910  CE  LYS A 114      -7.953 -13.068  -2.824  1.00 45.74           C  
ANISOU  910  CE  LYS A 114     5736   5999   5643     55     32   -584       C  
ATOM    911  NZ  LYS A 114      -8.359 -14.258  -2.029  1.00 51.75           N  
ANISOU  911  NZ  LYS A 114     6501   6759   6402     52     33   -585       N  
ATOM    912  N   SER A 115      -2.756  -9.927  -4.148  1.00 14.95           N  
ANISOU  912  N   SER A 115     1834   2098   1749     57     24   -578       N  
ATOM    913  CA  SER A 115      -2.346  -8.921  -3.166  1.00 14.86           C  
ANISOU  913  CA  SER A 115     1825   2086   1737     57     24   -577       C  
ATOM    914  C   SER A 115      -2.523  -7.484  -3.655  1.00 18.17           C  
ANISOU  914  C   SER A 115     2245   2505   2155     57     25   -576       C  
ATOM    915  O   SER A 115      -2.804  -6.591  -2.851  1.00 17.74           O  
ANISOU  915  O   SER A 115     2190   2449   2100     57     26   -576       O  
ATOM    916  CB  SER A 115      -0.906  -9.165  -2.725  1.00 18.33           C  
ANISOU  916  CB  SER A 115     2264   2524   2177     57     22   -579       C  
ATOM    917  OG  SER A 115       0.016  -8.719  -3.703  1.00 21.48           O  
ANISOU  917  OG  SER A 115     2661   2924   2575     56     23   -582       O  
ATOM    918  N   VAL A 116      -2.399  -7.266  -4.981  1.00 15.84           N  
ANISOU  918  N   VAL A 116     1948   2211   1859     56     25   -576       N  
ATOM    919  CA  VAL A 116      -2.518  -5.938  -5.590  1.00 16.83           C  
ANISOU  919  CA  VAL A 116     2076   2336   1983     55     25   -575       C  
ATOM    920  C   VAL A 116      -3.934  -5.336  -5.408  1.00 22.45           C  
ANISOU  920  C   VAL A 116     2789   3047   2696     57     24   -574       C  
ATOM    921  O   VAL A 116      -4.071  -4.116  -5.295  1.00 23.67           O  
ANISOU  921  O   VAL A 116     2945   3199   2850     58     23   -573       O  
ATOM    922  CB  VAL A 116      -2.035  -5.964  -7.068  1.00 19.75           C  
ANISOU  922  CB  VAL A 116     2445   2707   2351     52     25   -575       C  
ATOM    923  CG1 VAL A 116      -2.011  -4.565  -7.677  1.00 20.22           C  
ANISOU  923  CG1 VAL A 116     2509   2766   2409     50     24   -573       C  
ATOM    924  CG2 VAL A 116      -0.649  -6.603  -7.171  1.00 18.97           C  
ANISOU  924  CG2 VAL A 116     2345   2611   2253     49     25   -579       C  
ATOM    925  N   ASP A 117      -4.963  -6.190  -5.311  1.00 19.92           N  
ANISOU  925  N   ASP A 117     2466   2726   2375     59     24   -575       N  
ATOM    926  CA  ASP A 117      -6.347  -5.724  -5.143  1.00 21.11           C  
ANISOU  926  CA  ASP A 117     2617   2876   2526     61     23   -577       C  
ATOM    927  C   ASP A 117      -6.628  -5.074  -3.792  1.00 28.24           C  
ANISOU  927  C   ASP A 117     3520   3778   3431     61     23   -579       C  
ATOM    928  O   ASP A 117      -7.586  -4.306  -3.683  1.00 29.64           O  
ANISOU  928  O   ASP A 117     3697   3955   3609     62     20   -581       O  
ATOM    929  CB  ASP A 117      -7.337  -6.854  -5.421  1.00 22.98           C  
ANISOU  929  CB  ASP A 117     2853   3116   2764     62     25   -580       C  
ATOM    930  CG  ASP A 117      -7.484  -7.168  -6.897  1.00 37.12           C  
ANISOU  930  CG  ASP A 117     4643   4908   4554     63     25   -579       C  
ATOM    931  OD1 ASP A 117      -7.039  -6.339  -7.733  1.00 37.22           O  
ANISOU  931  OD1 ASP A 117     4656   4919   4565     63     24   -577       O  
ATOM    932  OD2 ASP A 117      -8.077  -8.219  -7.221  1.00 45.36           O  
ANISOU  932  OD2 ASP A 117     5683   5954   5597     65     28   -581       O  
ATOM    933  N   PHE A 118      -5.802  -5.376  -2.774  1.00 24.27           N  
ANISOU  933  N   PHE A 118     3017   3276   2928     59     24   -578       N  
ATOM    934  CA  PHE A 118      -5.960  -4.825  -1.417  1.00 23.80           C  
ANISOU  934  CA  PHE A 118     2956   3217   2870     57     24   -579       C  
ATOM    935  C   PHE A 118      -5.131  -3.578  -1.168  1.00 31.07           C  
ANISOU  935  C   PHE A 118     3876   4137   3793     58     24   -578       C  
ATOM    936  O   PHE A 118      -5.115  -3.072  -0.042  1.00 31.77           O  
ANISOU  936  O   PHE A 118     3962   4226   3882     57     24   -579       O  
ATOM    937  CB  PHE A 118      -5.636  -5.907  -0.379  1.00 24.38           C  
ANISOU  937  CB  PHE A 118     3030   3291   2942     55     25   -579       C  
ATOM    938  CG  PHE A 118      -6.447  -7.168  -0.562  1.00 24.34           C  
ANISOU  938  CG  PHE A 118     3026   3287   2936     54     26   -581       C  
ATOM    939  CD1 PHE A 118      -7.838  -7.125  -0.595  1.00 25.64           C  
ANISOU  939  CD1 PHE A 118     3189   3452   3099     54     26   -585       C  
ATOM    940  CD2 PHE A 118      -5.825  -8.402  -0.689  1.00 25.53           C  
ANISOU  940  CD2 PHE A 118     3178   3437   3085     54     26   -579       C  
ATOM    941  CE1 PHE A 118      -8.589  -8.292  -0.774  1.00 25.75           C  
ANISOU  941  CE1 PHE A 118     3205   3468   3112     53     28   -588       C  
ATOM    942  CE2 PHE A 118      -6.580  -9.570  -0.856  1.00 27.27           C  
ANISOU  942  CE2 PHE A 118     3400   3658   3305     53     27   -580       C  
ATOM    943  CZ  PHE A 118      -7.958  -9.508  -0.890  1.00 25.14           C  
ANISOU  943  CZ  PHE A 118     3129   3390   3034     52     28   -585       C  
ATOM    944  N   LEU A 119      -4.468  -3.069  -2.220  1.00 28.97           N  
ANISOU  944  N   LEU A 119     3613   3869   3526     58     23   -576       N  
ATOM    945  CA  LEU A 119      -3.599  -1.893  -2.186  1.00 32.47           C  
ANISOU  945  CA  LEU A 119     4056   4311   3969     58     24   -574       C  
ATOM    946  C   LEU A 119      -4.297  -0.620  -2.673  1.00 47.29           C  
ANISOU  946  C   LEU A 119     5934   6185   5847     59     21   -574       C  
ATOM    947  O   LEU A 119      -5.534  -0.553  -2.685  1.00 49.93           O  
ANISOU  947  O   LEU A 119     6268   6519   6184     60     17   -576       O  
ATOM    948  CB  LEU A 119      -2.382  -2.132  -3.074  1.00 32.65           C  
ANISOU  948  CB  LEU A 119     4082   4334   3990     57     26   -573       C  
ATOM    949  CG  LEU A 119      -1.358  -3.181  -2.695  1.00 37.28           C  
ANISOU  949  CG  LEU A 119     4667   4922   4575     56     28   -575       C  
ATOM    950  CD1 LEU A 119      -0.204  -3.097  -3.656  1.00 37.29           C  
ANISOU  950  CD1 LEU A 119     4670   4924   4574     54     29   -576       C  
ATOM    951  CD2 LEU A 119      -0.829  -2.981  -1.279  1.00 39.60           C  
ANISOU  951  CD2 LEU A 119     4960   5217   4871     57     29   -576       C  
ATOM    952  OXT LEU A 119      -3.586   0.323  -3.099  1.00 71.61           O  
ANISOU  952  OXT LEU A 119     9017   9264   8927     58     21   -572       O  
TER     953      LEU A 119                                                      
HETATM  954  C1  EOL A 120       2.647 -10.674 -10.663  1.00 22.39           C  
HETATM  955  O1  EOL A 120       2.898 -13.159  -8.006  1.00 17.52           O  
HETATM  956  C2  EOL A 120       2.807 -11.494 -11.785  1.00 31.24           C  
HETATM  957  O2  EOL A 120       2.513 -10.499  -8.241  1.00 17.05           O  
HETATM  958  C3  EOL A 120       2.691 -11.242  -9.392  1.00 18.06           C  
HETATM  959  C4  EOL A 120       3.033 -12.859 -11.630  1.00 20.41           C  
HETATM  960  C5  EOL A 120       2.868 -12.610  -9.251  1.00 15.66           C  
HETATM  961  C6  EOL A 120       3.059 -13.427 -10.361  1.00 19.96           C  
HETATM  962  C7  EOL A 120       2.742 -10.915 -13.163  1.00 27.12           C  
HETATM  963  C8  EOL A 120       3.628  -9.766 -13.473  1.00 37.65           C  
HETATM  964  C9  EOL A 120       4.805  -9.630 -12.803  1.00 74.99           C  
HETATM  965  C10 EOL A 120       2.360  -9.130  -8.313  1.00 16.80           C  
HETATM  966  O   HOH A 121     -12.949 -13.058 -10.494  1.00 43.68           O  
HETATM  967  O   HOH A 122       2.775 -22.031  -5.090  1.00 35.38           O  
HETATM  968  O   HOH A 123      -8.050 -13.740 -25.446  1.00 45.51           O  
HETATM  969  O   HOH A 124      19.237 -16.168  -5.193  1.00 49.49           O  
HETATM  970  O   HOH A 125      -1.403 -26.732  -6.072  1.00 51.25           O  
HETATM  971  O   HOH A 126       7.687   0.582 -12.827  1.00 38.12           O  
HETATM  972  O   HOH A 127       7.447 -22.724 -26.939  1.00 39.35           O  
HETATM  973  O   HOH A 128      -5.770 -19.876  -2.850  1.00 32.59           O  
HETATM  974  O   HOH A 129      15.751 -17.420 -17.748  1.00 32.58           O  
HETATM  975  O   HOH A 130      14.258  -6.454   2.127  1.00 34.13           O  
HETATM  976  O   HOH A 131      11.955 -28.821 -17.832  1.00 33.80           O  
HETATM  977  O   HOH A 132      12.174 -30.771 -14.424  1.00 48.79           O  
HETATM  978  O   HOH A 133      16.447 -27.928 -14.129  1.00 52.36           O  
HETATM  979  O   HOH A 134       0.218  -6.083  -3.260  1.00 35.00           O  
HETATM  980  O   HOH A 135       8.295 -24.330  -4.549  1.00 58.23           O  
HETATM  981  O   HOH A 136      -7.877 -22.565 -25.436  1.00 48.70           O  
HETATM  982  O   HOH A 137      20.046  -9.661  -2.484  1.00 51.02           O  
HETATM  983  O   HOH A 138       2.873  -8.006   3.519  1.00 43.64           O  
HETATM  984  O   HOH A 139      -9.760 -14.102 -13.789  1.00 28.38           O  
HETATM  985  O   HOH A 140      -2.158 -12.993 -24.962  1.00 29.38           O  
HETATM  986  O   HOH A 141       9.399  -3.970 -19.775  1.00 33.72           O  
HETATM  987  O   HOH A 142       0.175 -14.721  -7.978  1.00 15.80           O  
HETATM  988  O   HOH A 143       3.263 -13.447  -0.962  1.00 34.79           O  
HETATM  989  O   HOH A 144       6.715  -0.353  -2.313  1.00 51.54           O  
HETATM  990  O   HOH A 145       6.874 -16.353   0.878  1.00 43.48           O  
HETATM  991  O   HOH A 146      -0.546  -1.053 -19.222  1.00 24.98           O  
HETATM  992  O   HOH A 147     -11.495 -20.230 -23.571  1.00 28.60           O  
HETATM  993  O   HOH A 148      11.627 -30.196 -11.905  1.00 58.80           O  
HETATM  994  O   HOH A 149       3.029 -21.708 -25.703  1.00 25.27           O  
HETATM  995  O   HOH A 150      -5.311 -25.163 -23.432  1.00 19.87           O  
HETATM  996  O   HOH A 151       2.395 -29.408  -9.383  1.00 26.59           O  
HETATM  997  O   HOH A 152      -2.623 -23.576  -9.567  1.00 20.36           O  
HETATM  998  O   HOH A 153      -0.037  -4.815   1.573  1.00 32.81           O  
HETATM  999  O   HOH A 154      15.653  -7.515 -18.680  1.00 35.17           O  
HETATM 1000  O   HOH A 155      -7.215 -10.324  -8.449  1.00 30.24           O  
HETATM 1001  O   HOH A 156      19.405  -9.097  -8.424  1.00 36.67           O  
HETATM 1002  O   HOH A 157      17.503 -14.049 -17.050  1.00 34.31           O  
HETATM 1003  O   HOH A 158      -9.161 -11.861 -12.621  1.00 25.96           O  
HETATM 1004  O   HOH A 159      -4.794  -9.330  -9.437  1.00 20.59           O  
HETATM 1005  O   HOH A 160      14.169  -8.738   0.944  1.00 42.55           O  
HETATM 1006  O   HOH A 161      14.547  -5.980 -20.715  1.00 50.31           O  
HETATM 1007  O   HOH A 162       4.188 -29.185 -20.123  1.00 19.22           O  
HETATM 1008  O   HOH A 163      -8.034 -15.327 -14.956  1.00 23.77           O  
HETATM 1009  O   HOH A 164      -8.425 -25.787 -15.824  1.00 24.69           O  
HETATM 1010  O   HOH A 165       0.583 -19.591 -23.071  1.00 22.66           O  
HETATM 1011  O   HOH A 166      20.851 -15.747  -9.738  1.00 22.44           O  
HETATM 1012  O   HOH A 167      12.529  -1.785 -15.289  1.00 43.58           O  
HETATM 1013  O   HOH A 168      14.860 -29.205 -15.956  1.00 42.41           O  
HETATM 1014  O   HOH A 169       5.205  -4.770 -18.027  1.00 40.96           O  
HETATM 1015  O   HOH A 170     -14.318 -22.447 -12.260  1.00 27.43           O  
HETATM 1016  O   HOH A 171      10.458 -20.784  -6.146  1.00 44.70           O  
HETATM 1017  O   HOH A 172       9.348 -22.001  -8.296  1.00 22.80           O  
HETATM 1018  O   HOH A 173       3.785 -31.656 -19.188  1.00 28.04           O  
HETATM 1019  O   HOH A 174       5.680 -27.458  -3.447  1.00 55.92           O  
HETATM 1020  O   HOH A 175     -11.353 -25.281 -21.429  1.00 33.93           O  
HETATM 1021  O   HOH A 176     -14.087 -21.315 -15.954  1.00 24.13           O  
HETATM 1022  O   HOH A 177      -9.157 -19.916  -5.220  1.00 47.44           O  
HETATM 1023  O   HOH A 178      10.350  -0.475  -4.755  1.00 39.38           O  
HETATM 1024  O   HOH A 179      -2.207  -0.619   1.528  1.00 38.68           O  
HETATM 1025  O   HOH A 180      17.615 -18.980  -4.794  1.00 54.33           O  
HETATM 1026  O   HOH A 181     -16.274 -19.730 -15.646  1.00 31.09           O  
HETATM 1027  O   HOH A 182       6.794 -21.115 -25.176  1.00 38.61           O  
HETATM 1028  O   HOH A 183       1.277 -11.357  -1.327  1.00 27.83           O  
HETATM 1029  O   HOH A 184      -6.228 -27.328 -15.202  1.00 28.29           O  
HETATM 1030  O   HOH A 185      -1.064 -12.433 -27.882  1.00 62.97           O  
HETATM 1031  O   HOH A 186       6.527 -14.173   3.793  1.00 56.71           O  
HETATM 1032  O   HOH A 187     -14.979 -17.090 -15.562  1.00 30.98           O  
HETATM 1033  O   HOH A 188     -11.628 -22.859 -23.977  1.00 37.08           O  
HETATM 1034  O   HOH A 189      15.918 -22.823 -18.826  1.00 48.23           O  
HETATM 1035  O   HOH A 190     -10.821 -28.891 -20.088  1.00 49.56           O  
HETATM 1036  O   HOH A 191       4.927 -30.610 -16.421  1.00 34.25           O  
HETATM 1037  O   HOH A 192       7.382 -30.369  -9.511  1.00 60.77           O  
HETATM 1038  O   HOH A 193       3.820  -4.117 -20.316  1.00 19.71           O  
HETATM 1039  O   HOH A 194      12.907 -23.095 -21.321  1.00 31.12           O  
HETATM 1040  O   HOH A 195      -9.564 -16.679  -1.167  1.00 44.26           O  
HETATM 1041  O   HOH A 196      -1.830 -31.105 -16.942  1.00 31.59           O  
HETATM 1042  O   HOH A 197       2.976 -18.150  -2.828  1.00 53.39           O  
HETATM 1043  O   HOH A 198      15.023 -18.213 -14.760  1.00 18.72           O  
HETATM 1044  O   HOH A 199      10.594 -25.038  -5.001  1.00 60.41           O  
HETATM 1045  O   HOH A 200      17.811 -14.217  -3.940  1.00 32.63           O  
HETATM 1046  O   HOH A 201       5.182  -2.495 -16.746  1.00 56.96           O  
HETATM 1047  O   HOH A 202     -10.523 -19.636 -27.623  1.00 55.29           O  
HETATM 1048  O   HOH A 203      -6.531 -30.470  -5.113  1.00 57.40           O  
HETATM 1049  O   HOH A 204      18.730  -7.794  -2.211  1.00 43.34           O  
HETATM 1050  O   HOH A 205      -5.320  -6.683  -9.836  1.00 25.83           O  
HETATM 1051  O   HOH A 206      -1.302 -20.003 -25.058  1.00 24.80           O  
HETATM 1052  O   HOH A 207       4.069  -7.201 -23.758  1.00 23.81           O  
HETATM 1053  O   HOH A 208      -7.143 -29.099 -13.339  1.00 52.66           O  
HETATM 1054  O   HOH A 209       0.948 -16.833 -24.617  1.00 50.68           O  
HETATM 1055  O   HOH A 210      -8.847 -25.471  -8.302  1.00 41.14           O  
HETATM 1056  O   HOH A 211      -1.435   4.514  -7.248  1.00 60.93           O  
HETATM 1057  O   HOH A 212     -10.198 -10.185 -14.814  1.00 26.83           O  
HETATM 1058  O   HOH A 213       8.359 -26.104  -8.078  1.00 43.54           O  
HETATM 1059  O   HOH A 214       1.434  -9.261   0.566  1.00 41.78           O  
HETATM 1060  O   HOH A 215      -3.478 -21.649 -25.258  1.00 24.94           O  
HETATM 1061  O   HOH A 216       5.566 -26.972  -6.365  1.00 28.95           O  
HETATM 1062  O   HOH A 217       4.898 -19.677  -4.265  1.00 29.41           O  
HETATM 1063  O   HOH A 218       4.800 -22.061 -27.648  1.00 31.76           O  
HETATM 1064  O   HOH A 219     -10.230 -13.719 -10.432  1.00 29.73           O  
HETATM 1065  O   HOH A 220     -11.926 -14.461 -19.044  1.00 33.60           O  
HETATM 1066  O   HOH A 221       3.035 -27.372  -7.361  1.00 36.63           O  
HETATM 1067  O   HOH A 222       5.461  -9.700   0.858  1.00 35.25           O  
HETATM 1068  O   HOH A 223       9.026 -21.814  -4.109  1.00 53.79           O  
HETATM 1069  O   HOH A 224      14.490 -20.766 -21.402  1.00 47.66           O  
HETATM 1070  O   HOH A 225       6.174 -21.717  -2.867  1.00 43.03           O  
HETATM 1071  O   HOH A 226      17.071 -16.451 -15.907  1.00 42.73           O  
HETATM 1072  O   HOH A 227      11.351  -6.784 -19.883  1.00 31.97           O  
HETATM 1073  O   HOH A 228     -11.012 -12.431 -22.575  1.00 45.50           O  
HETATM 1074  O   HOH A 229     -12.065 -19.444  -6.503  1.00 37.62           O  
HETATM 1075  O   HOH A 230      -1.899   8.264 -13.274  1.00 59.05           O  
HETATM 1076  O   HOH A 231      20.570 -10.039  -4.890  1.00 54.87           O  
HETATM 1077  O   HOH A 232      -7.856 -15.308  -6.726  1.00 33.03           O  
HETATM 1078  O   HOH A 233       4.088   1.992  -5.328  1.00 44.69           O  
HETATM 1079  O   HOH A 234     -11.323 -14.546 -16.198  1.00 33.38           O  
HETATM 1080  O   HOH A 235      15.549  -3.150  -7.246  1.00 44.56           O  
HETATM 1081  O   HOH A 236      10.536 -11.080 -26.671  1.00 44.32           O  
HETATM 1082  O   HOH A 237     -10.894 -12.403 -15.428  1.00 44.22           O  
HETATM 1083  O   HOH A 238       4.711  -9.295 -25.272  1.00 31.46           O  
HETATM 1084  O   HOH A 239     -10.855 -13.236  -1.354  1.00 35.02           O  
HETATM 1085  O   HOH A 240       7.172 -10.831 -24.146  1.00 37.04           O  
HETATM 1086  O   HOH A 241      12.741   0.438  -1.409  1.00 37.29           O  
HETATM 1087  O   HOH A 242      -6.057 -22.186  -3.729  1.00 35.11           O  
HETATM 1088  O   HOH A 243      13.423 -20.709  -5.595  1.00 58.09           O  
HETATM 1089  O   HOH A 244      -4.052   0.010 -16.586  1.00 31.78           O  
HETATM 1090  O   HOH A 245      -1.782   0.978 -17.864  1.00 37.42           O  
HETATM 1091  O   HOH A 246     -10.113 -26.455 -17.880  1.00 48.08           O  
HETATM 1092  O   HOH A 247      13.539 -24.002 -23.794  1.00 53.23           O  
HETATM 1093  O   HOH A 248      23.023 -14.916  -5.559  1.00 56.03           O  
HETATM 1094  O   HOH A 249      18.786   0.004   1.572  1.00 52.37           O  
HETATM 1095  O   HOH A 250      -9.168 -11.444  -9.776  1.00 48.72           O  
HETATM 1096  O   HOH A 251      -4.348 -29.032 -17.585  1.00 28.66           O  
HETATM 1097  O   HOH A 252       1.813 -30.194 -17.807  1.00 36.13           O  
HETATM 1098  O   HOH A 253      14.506 -24.828 -12.235  1.00 46.00           O  
HETATM 1099  O   HOH A 254       0.912 -14.185 -24.304  1.00 40.78           O  
HETATM 1100  O   HOH A 255      18.676 -12.933 -14.943  1.00 40.11           O  
HETATM 1101  O   HOH A 256       0.838 -28.811  -5.883  1.00 52.62           O  
HETATM 1102  O   HOH A 257      -4.484 -25.372  -8.202  1.00 34.07           O  
HETATM 1103  O   HOH A 258      10.766 -27.759 -25.409  1.00 52.51           O  
HETATM 1104  O   HOH A 259      10.745 -31.122 -17.345  1.00 39.91           O  
CONECT  138  398                                                                
CONECT  398  138                                                                
CONECT  707  844                                                                
CONECT  844  707                                                                
CONECT  954  956  958                                                           
CONECT  955  960                                                                
CONECT  956  954  959  962                                                      
CONECT  957  958  965                                                           
CONECT  958  954  957  960                                                      
CONECT  959  956  961                                                           
CONECT  960  955  958  961                                                      
CONECT  961  959  960                                                           
CONECT  962  956  963                                                           
CONECT  963  962  964                                                           
CONECT  964  963                                                                
CONECT  965  957                                                                
MASTER      439    0    1    7    0    0    3    6 1094    1   16   10          
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.