CNRS Nantes University UFIP UFIP
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***  3S0E  ***

elNémo ID: 22060700265870943

Job options:

ID        	=	 22060700265870943
JOBID     	=	 3S0E
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 25
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 3S0E

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.