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***  OXIDOREDUCTASE 25-JUN-82 3DFR  ***

elNémo ID: 221003211019124729

Job options:

ID        	=	 221003211019124729
JOBID     	=	 OXIDOREDUCTASE 25-JUN-82 3DFR
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    OXIDOREDUCTASE                          25-JUN-82   3DFR              
TITLE     CRYSTAL STRUCTURES OF ESCHERICHIA COLI AND LACTOBACILLUS CASEI        
TITLE    2 DIHYDROFOLATE REDUCTASE REFINED AT 1.7 ANGSTROMS RESOLUTION. I.      
TITLE    3 GENERAL FEATURES AND BINDING OF METHOTREXATE                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIHYDROFOLATE REDUCTASE;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 1.5.1.3;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: LACTOBACILLUS CASEI;                            
SOURCE   3 ORGANISM_TAXID: 1582                                                 
KEYWDS    OXIDO-REDUCTASE, OXIDOREDUCTASE                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.J.FILMAN,D.A.MATTHEWS,J.T.BOLIN,J.KRAUT                             
REVDAT   7   29-NOV-17 3DFR    1       KEYWDS HELIX                             
REVDAT   6   24-FEB-09 3DFR    1       VERSN                                    
REVDAT   5   01-APR-03 3DFR    1       JRNL                                     
REVDAT   4   31-JAN-84 3DFR    1       REMARK                                   
REVDAT   3   30-SEP-83 3DFR    1       REVDAT                                   
REVDAT   2   07-MAR-83 3DFR    2       JRNL   REMARK CONECT                     
REVDAT   1   21-OCT-82 3DFR    0                                                
SPRSDE     21-OCT-82 3DFR      1DFR                                             
JRNL        AUTH   J.T.BOLIN,D.J.FILMAN,D.A.MATTHEWS,R.C.HAMLIN,J.KRAUT         
JRNL        TITL   CRYSTAL STRUCTURES OF ESCHERICHIA COLI AND LACTOBACILLUS     
JRNL        TITL 2 CASEI DIHYDROFOLATE REDUCTASE REFINED AT 1.7 A RESOLUTION.   
JRNL        TITL 3 I. GENERAL FEATURES AND BINDING OF METHOTREXATE.             
JRNL        REF    J.BIOL.CHEM.                  V. 257 13650 1982              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   6815178                                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   D.J.FILMAN,J.T.BOLIN,D.A.MATTHEWS,J.KRAUT                    
REMARK   1  TITL   CRYSTAL STRUCTURES OF ESCHERICHIA COLI AND LACTOBACILLUS     
REMARK   1  TITL 2 CASEI DIHYDROFOLATE REDUCTASE REFINED AT 1.7 ANGSTROMS       
REMARK   1  TITL 3 RESOLUTION. II. ENVIRONMENT OF BOUND NADPH AND IMPLICATIONS  
REMARK   1  TITL 4 FOR CATALYSIS                                                
REMARK   1  REF    J.BIOL.CHEM.                  V. 257 13663 1982              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   K.W.VOLZ,D.A.MATTHEWS,R.A.ALDEN,S.T.FREER,C.HANSCH,          
REMARK   1  AUTH 2 B.T.KAUFMAN,J.KRAUT                                          
REMARK   1  TITL   CRYSTAL STRUCTURE OF AVIAN DIHYDROFOLATE REDUCTASE           
REMARK   1  TITL 2 CONTAINING PHENYLTRIAZINE AND NADPH                          
REMARK   1  REF    J.BIOL.CHEM.                  V. 257  2528 1982              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   D.A.MATTHEWS                                                 
REMARK   1  TITL   INTERPRETATION OF NUCLEAR MAGNETIC RESONANCE SPECTRA FOR     
REMARK   1  TITL 2 LACTOBACILLUS CASEI DIHYDROFOLATE REDUCTASE BASED ON THE     
REMARK   1  TITL 3 X-RAY STRUCTURE OF THE ENZYME-METHOTREXATE-NADPH COMPLEX     
REMARK   1  REF    BIOCHEMISTRY                  V.  18  1602 1979              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   D.A.MATTHEWS,R.A.ALDEN,S.T.FREER,N.-H.XUONG,J.KRAUT          
REMARK   1  TITL   DIHYDROFOLATE REDUCTASE FROM LACTOBACILLUS CASEI.            
REMARK   1  TITL 2 STEREOCHEMISTRY OF NADPH BINDING                             
REMARK   1  REF    J.BIOL.CHEM.                  V. 254  4144 1979              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   D.A.MATTHEWS,R.A.ALDEN,J.T.BOLIN,D.J.FILMAN,S.T.FREER,       
REMARK   1  AUTH 2 R.HAMLIN,W.G.J.HOL,R.L.KISLIUK,E.J.PASTORE,L.T.PLANTE,       
REMARK   1  AUTH 3 N.-H.XUONG,J.KRAUT                                           
REMARK   1  TITL   DIHYDROFOLATE REDUCTASE FROM LACTOBACILLUS CASEI. X-RAY      
REMARK   1  TITL 2 STRUCTURE OF THE ENZYME-METHOTREXATE-NADPH COMPLEX           
REMARK   1  REF    J.BIOL.CHEM.                  V. 253  6946 1978              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 6                                                          
REMARK   1  AUTH   D.A.MATTHEWS,R.A.ALDEN,J.T.BOLIN,S.T.FREER,R.HAMLIN,N.XUONG, 
REMARK   1  AUTH 2 J.KRAUT,M.POE,M.WILLIAMS,K.HOOGSTEEN                         
REMARK   1  TITL   DIHYDROFOLATE REDUCTASE. X-RAY STRUCTURE OF THE BINARY       
REMARK   1  TITL 2 COMPLEX WITH METHOTREXATE                                    
REMARK   1  REF    SCIENCE                       V. 197   452 1977              
REMARK   1  REFN                   ISSN 0036-8075                               
REMARK   1 REFERENCE 7                                                          
REMARK   1  AUTH   T.C.CRUSBERG,R.LEARY,R.L.KISLIUK                             
REMARK   1  TITL   PROPERTIES OF THYMIDYLATE SYNTHETASE FROM                    
REMARK   1  TITL 2 DICHLOROMETHOTREXATE-RESISTANT LACTOBACILLUS CASEI           
REMARK   1  REF    J.BIOL.CHEM.                  V. 245  5292 1970              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : NULL                                                 
REMARK   3   AUTHORS     : NULL                                                 
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.152                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
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           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
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            : 1294                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 81                                      
REMARK   3   SOLVENT ATOMS            : 264                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3DFR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000178937.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.57                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.79                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       31.12667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       62.25333            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       46.69000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       77.81667            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       15.56333            
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 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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  51    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PHE A   3   CG    PHE A   3   CD1     0.114                       
REMARK 500    ARG A   9   CG    ARG A   9   CD      0.167                       
REMARK 500    ARG A   9   CZ    ARG A   9   NH1     0.088                       
REMARK 500    ARG A   9   CZ    ARG A   9   NH2     0.093                       
REMARK 500    ASN A  10   CB    ASN A  10   CG      0.227                       
REMARK 500    ASN A  10   CG    ASN A  10   OD1     0.229                       
REMARK 500    GLY A  14   CA    GLY A  14   C       0.117                       
REMARK 500    ASP A  16   CA    ASP A  16   CB      0.150                       
REMARK 500    GLY A  17   N     GLY A  17   CA      0.113                       
REMARK 500    HIS A  18   CG    HIS A  18   ND1     0.139                       
REMARK 500    HIS A  18   NE2   HIS A  18   CD2     0.199                       
REMARK 500    LEU A  19   C     LEU A  19   O      -0.130                       
REMARK 500    LEU A  19   C     PRO A  20   N       0.217                       
REMARK 500    PRO A  20   N     PRO A  20   CA      0.120                       
REMARK 500    PRO A  20   CD    PRO A  20   N       0.182                       
REMARK 500    HIS A  22   CG    HIS A  22   CD2     0.116                       
REMARK 500    LEU A  23   C     LEU A  23   O      -0.141                       
REMARK 500    LEU A  23   C     PRO A  24   N       0.167                       
REMARK 500    PRO A  24   CD    PRO A  24   N       0.305                       
REMARK 500    HIS A  28   CG    HIS A  28   CD2     0.161                       
REMARK 500    TYR A  29   CZ    TYR A  29   CE2     0.078                       
REMARK 500    ARG A  31   NE    ARG A  31   CZ      0.142                       
REMARK 500    ARG A  31   CZ    ARG A  31   NH2     0.089                       
REMARK 500    ARG A  44   CD    ARG A  44   NE     -0.143                       
REMARK 500    ARG A  44   CZ    ARG A  44   NH1     0.123                       
REMARK 500    ARG A  44   CZ    ARG A  44   NH2     0.079                       
REMARK 500    TYR A  46   CG    TYR A  46   CD1     0.080                       
REMARK 500    PHE A  49   CG    PHE A  49   CD2     0.165                       
REMARK 500    PHE A  49   C     PRO A  50   N       0.158                       
REMARK 500    PRO A  50   N     PRO A  50   CA      0.125                       
REMARK 500    PRO A  50   CA    PRO A  50   CB      0.156                       
REMARK 500    PRO A  50   CD    PRO A  50   N       0.309                       
REMARK 500    LYS A  51   CA    LYS A  51   CB      0.152                       
REMARK 500    ARG A  52   N     ARG A  52   CA      0.137                       
REMARK 500    ARG A  52   C     PRO A  53   N       0.305                       
REMARK 500    PRO A  53   CD    PRO A  53   N       0.210                       
REMARK 500    LEU A  54   C     PRO A  55   N       0.234                       
REMARK 500    PRO A  55   CD    PRO A  55   N       0.213                       
REMARK 500    GLU A  56   CB    GLU A  56   CG      0.155                       
REMARK 500    GLU A  56   CD    GLU A  56   OE1     0.079                       
REMARK 500    HIS A  64   CG    HIS A  64   CD2     0.060                       
REMARK 500    HIS A  64   CG    HIS A  64   ND1    -0.107                       
REMARK 500    GLN A  65   CD    GLN A  65   NE2     0.173                       
REMARK 500    GLU A  66   CB    GLU A  66   CG      0.126                       
REMARK 500    GLU A  66   CD    GLU A  66   OE2     0.074                       
REMARK 500    ASP A  67   CA    ASP A  67   CB      0.335                       
REMARK 500    ASP A  67   CG    ASP A  67   OD1     0.249                       
REMARK 500    ASP A  67   CG    ASP A  67   OD2     0.224                       
REMARK 500    ASP A  67   C     TYR A  68   N       0.142                       
REMARK 500    TYR A  68   CE1   TYR A  68   CZ      0.092                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     103 BOND DEVIATIONS.                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    THR A   1   CA  -  CB  -  CG2 ANGL. DEV. =   9.0 DEGREES          
REMARK 500    PHE A   3   CB  -  CG  -  CD2 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    PHE A   3   CD1 -  CG  -  CD2 ANGL. DEV. = -14.1 DEGREES          
REMARK 500    PHE A   3   CB  -  CG  -  CD1 ANGL. DEV. =   9.8 DEGREES          
REMARK 500    PHE A   3   CG  -  CD2 -  CE2 ANGL. DEV. =  21.4 DEGREES          
REMARK 500    PHE A   3   CD1 -  CE1 -  CZ  ANGL. DEV. =   8.8 DEGREES          
REMARK 500    TRP A   5   CE3 -  CZ3 -  CH2 ANGL. DEV. =   9.9 DEGREES          
REMARK 500    TRP A   5   CZ3 -  CH2 -  CZ2 ANGL. DEV. =  -9.3 DEGREES          
REMARK 500    ASN A   8   CB  -  CA  -  C   ANGL. DEV. =  14.1 DEGREES          
REMARK 500    ASN A   8   CA  -  C   -  O   ANGL. DEV. =  14.2 DEGREES          
REMARK 500    ARG A   9   CG  -  CD  -  NE  ANGL. DEV. = -20.3 DEGREES          
REMARK 500    ARG A   9   CD  -  NE  -  CZ  ANGL. DEV. =  42.1 DEGREES          
REMARK 500    ARG A   9   NE  -  CZ  -  NH2 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ASN A  10   OD1 -  CG  -  ND2 ANGL. DEV. =  33.6 DEGREES          
REMARK 500    ASN A  10   CB  -  CG  -  OD1 ANGL. DEV. = -27.9 DEGREES          
REMARK 500    LEU A  12   CB  -  CG  -  CD1 ANGL. DEV. = -11.4 DEGREES          
REMARK 500    ASP A  16   CB  -  CG  -  OD1 ANGL. DEV. =   9.2 DEGREES          
REMARK 500    LEU A  19   CB  -  CG  -  CD1 ANGL. DEV. = -12.2 DEGREES          
REMARK 500    LEU A  19   CA  -  C   -  O   ANGL. DEV. =  19.7 DEGREES          
REMARK 500    LEU A  19   CA  -  C   -  N   ANGL. DEV. = -17.1 DEGREES          
REMARK 500    PRO A  20   C   -  N   -  CA  ANGL. DEV. = -15.3 DEGREES          
REMARK 500    PRO A  20   C   -  N   -  CD  ANGL. DEV. =  24.1 DEGREES          
REMARK 500    PRO A  20   CA  -  N   -  CD  ANGL. DEV. =  -9.8 DEGREES          
REMARK 500    PRO A  20   CB  -  CA  -  C   ANGL. DEV. = -13.7 DEGREES          
REMARK 500    PRO A  20   O   -  C   -  N   ANGL. DEV. = -10.2 DEGREES          
REMARK 500    TRP A  21   CB  -  CG  -  CD2 ANGL. DEV. = -12.7 DEGREES          
REMARK 500    TRP A  21   CB  -  CG  -  CD1 ANGL. DEV. =  14.0 DEGREES          
REMARK 500    HIS A  22   CA  -  C   -  O   ANGL. DEV. =  17.4 DEGREES          
REMARK 500    HIS A  22   CA  -  C   -  N   ANGL. DEV. = -14.0 DEGREES          
REMARK 500    LEU A  23   CA  -  C   -  O   ANGL. DEV. =  14.3 DEGREES          
REMARK 500    LEU A  23   CA  -  C   -  N   ANGL. DEV. = -19.2 DEGREES          
REMARK 500    PRO A  24   C   -  N   -  CA  ANGL. DEV. = -12.1 DEGREES          
REMARK 500    PRO A  24   C   -  N   -  CD  ANGL. DEV. =  25.5 DEGREES          
REMARK 500    PRO A  24   CA  -  N   -  CD  ANGL. DEV. = -13.1 DEGREES          
REMARK 500    PRO A  24   CA  -  C   -  N   ANGL. DEV. =  15.6 DEGREES          
REMARK 500    ASP A  25   OD1 -  CG  -  OD2 ANGL. DEV. = -15.7 DEGREES          
REMARK 500    ASP A  25   CB  -  CG  -  OD1 ANGL. DEV. =  14.4 DEGREES          
REMARK 500    ASP A  26   CB  -  CG  -  OD1 ANGL. DEV. =   8.5 DEGREES          
REMARK 500    ASP A  26   CA  -  C   -  O   ANGL. DEV. =  13.2 DEGREES          
REMARK 500    ASP A  26   O   -  C   -  N   ANGL. DEV. = -14.8 DEGREES          
REMARK 500    LEU A  27   CA  -  C   -  O   ANGL. DEV. = -13.5 DEGREES          
REMARK 500    HIS A  28   CB  -  CG  -  CD2 ANGL. DEV. = -12.1 DEGREES          
REMARK 500    HIS A  28   CA  -  C   -  N   ANGL. DEV. =  16.0 DEGREES          
REMARK 500    TYR A  29   CB  -  CG  -  CD2 ANGL. DEV. =   8.7 DEGREES          
REMARK 500    TYR A  29   CD1 -  CG  -  CD2 ANGL. DEV. =  -9.0 DEGREES          
REMARK 500    TYR A  29   CG  -  CD1 -  CE1 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    TYR A  29   CG  -  CD2 -  CE2 ANGL. DEV. =  10.2 DEGREES          
REMARK 500    TYR A  29   CZ  -  CE2 -  CD2 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    PHE A  30   CB  -  CG  -  CD1 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    ARG A  31   CG  -  CD  -  NE  ANGL. DEV. =  13.0 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     270 ANGLE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A  89     -113.71   -100.97                                   
REMARK 500    LEU A  90      -67.47    132.53                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A   9         0.07    SIDE CHAIN                              
REMARK 500    ARG A  31         0.19    SIDE CHAIN                              
REMARK 500    ARG A  44         0.09    SIDE CHAIN                              
REMARK 500    ARG A  52         0.12    SIDE CHAIN                              
REMARK 500    ARG A  57         0.15    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    TRP A  21        -11.24                                           
REMARK 500    ASP A  78        -12.18                                           
REMARK 500    GLU A 145         10.90                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: NDN                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE ADENINE BASE OF      
REMARK 800  THE NADPH COFACTOR                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NAR                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE ADENINE              
REMARK 800  MONONUCLEOTIDE RIBOSE OF THE NADPH COFACTOR                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NPP                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE PYROPHOSPHATE OF     
REMARK 800  THE NADPH COFACTOR                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NMR                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE NICOTINAMIDE         
REMARK 800  MONONUCLEOTIDE RIBOSE OF THE NADPH COFACTOR                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NND                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE NICOTINAMIDE BASE    
REMARK 800  OF THE NADPH COFACTOR                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MPT                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE PTERIDINE of THE     
REMARK 800  METHOTREXATE INHIBITOR                                              
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MNM                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE N(10) METHYL OF      
REMARK 800  THE METHOTREXATE INHIBITOR                                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MAB                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE P-AMINOBENZOYL OF    
REMARK 800  THE METHOTREXATE INHIBITOR                                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MGL                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE GLUTAMATE OF THE     
REMARK 800  METHOTREXATE INHIBITOR                                              
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP A 163                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTX A 164                 
DBREF  3DFR A    1   162  UNP    P00381   DYR_LACCA        1    162             
SEQADV 3DFR ASN A    8  UNP  P00381    ASP     8 CONFLICT                       
SEQADV 3DFR ASN A   10  UNP  P00381    ASP    10 CONFLICT                       
SEQADV 3DFR LEU A   90  UNP  P00381    PRO    90 CONFLICT                       
SEQRES   1 A  162  THR ALA PHE LEU TRP ALA GLN ASN ARG ASN GLY LEU ILE          
SEQRES   2 A  162  GLY LYS ASP GLY HIS LEU PRO TRP HIS LEU PRO ASP ASP          
SEQRES   3 A  162  LEU HIS TYR PHE ARG ALA GLN THR VAL GLY LYS ILE MET          
SEQRES   4 A  162  VAL VAL GLY ARG ARG THR TYR GLU SER PHE PRO LYS ARG          
SEQRES   5 A  162  PRO LEU PRO GLU ARG THR ASN VAL VAL LEU THR HIS GLN          
SEQRES   6 A  162  GLU ASP TYR GLN ALA GLN GLY ALA VAL VAL VAL HIS ASP          
SEQRES   7 A  162  VAL ALA ALA VAL PHE ALA TYR ALA LYS GLN HIS LEU ASP          
SEQRES   8 A  162  GLN GLU LEU VAL ILE ALA GLY GLY ALA GLN ILE PHE THR          
SEQRES   9 A  162  ALA PHE LYS ASP ASP VAL ASP THR LEU LEU VAL THR ARG          
SEQRES  10 A  162  LEU ALA GLY SER PHE GLU GLY ASP THR LYS MET ILE PRO          
SEQRES  11 A  162  LEU ASN TRP ASP ASP PHE THR LYS VAL SER SER ARG THR          
SEQRES  12 A  162  VAL GLU ASP THR ASN PRO ALA LEU THR HIS THR TYR GLU          
SEQRES  13 A  162  VAL TRP GLN LYS LYS ALA                                      
HET    NDP  A 163      48                                                       
HET    MTX  A 164      33                                                       
HETNAM     NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE                  
HETNAM   2 NDP  PHOSPHATE                                                       
HETNAM     MTX METHOTREXATE                                                     
FORMUL   2  NDP    C21 H30 N7 O17 P3                                            
FORMUL   3  MTX    C20 H22 N8 O5                                                
FORMUL   4  HOH   *264(H2 O)                                                    
HELIX    1  HB LEU A   23  THR A   34  1                                  12    
HELIX    2  HC GLY A   42  PHE A   49  1                                   8    
HELIX    3  HE ASP A   78  HIS A   89  1                                  12    
HELIX    4  HF GLY A   99  LYS A  107  1                                   9    
SHEET    1  S1 8 VAL A  74  VAL A  76  0                                        
SHEET    2  S1 8 GLU A  56  THR A  63  1  O  ASN A  59   N  VAL A  74           
SHEET    3  S1 8 GLY A  36  GLY A  42  1  O  LYS A  37   N  THR A  58           
SHEET    4  S1 8 GLU A  93  GLY A  98  1  O  GLU A  93   N  ILE A  38           
SHEET    5  S1 8 THR A   1  GLN A   7  1  N  ALA A   2   O  LEU A  94           
SHEET    6  S1 8 ASP A 111  ALA A 119  1  O  THR A 112   N  PHE A   3           
SHEET    7  S1 8 THR A 152  LYS A 161 -1  N  LYS A 160   O  ASP A 111           
SHEET    8  S1 8 ASP A 135  VAL A 144 -1  N  THR A 137   O  GLN A 159           
CISPEP   1 ARG A   52    PRO A   53          0        -8.17                     
CISPEP   2 GLY A   98    GLY A   99          0         2.29                     
SITE     1 NDN  8 LEU A  62  THR A  63  HIS A  64  HIS A  77                    
SITE     2 NDN  8 GLN A 101  ILE A 102  HOH A 279  HOH A 318                    
SITE     1 NAR  9 GLY A  42  ARG A  43  ARG A  44  THR A  63                    
SITE     2 NAR  9 HIS A  64  GLN A  65  GLN A 101  ILE A 102                    
SITE     3 NAR  9 HOH A 401                                                     
SITE     1 NPP  7 ARG A  44  THR A  45  GLY A  99  GLN A 101                    
SITE     2 NPP  7 ILE A 102  THR A 126  HOH A 301                               
SITE     1 NMR  7 ILE A  13  GLY A  14  HIS A  18  SER A  48                    
SITE     2 NMR  7 GLY A  99  HOH A 208  HOH A 439                               
SITE     1 NND 12 TRP A   5  ALA A   6  ILE A  13  LEU A  19                    
SITE     2 NND 12 TRP A  21  THR A  45  ALA A  97  GLY A  98                    
SITE     3 NND 12 GLY A  99  PHE A 103  MTX A 164  HOH A 439                    
SITE     1 MPT 14 LEU A   4  TRP A   5  ALA A   6  LEU A  19                    
SITE     2 MPT 14 TRP A  21  ASP A  26  LEU A  27  PHE A  30                    
SITE     3 MPT 14 ALA A  97  THR A 116  NDP A 163  HOH A 201                    
SITE     4 MPT 14 HOH A 217  HOH A 253                                          
SITE     1 MNM  2 LEU A  19  SER A  48                                          
SITE     1 MAB  5 LEU A  27  PHE A  30  PHE A  49  PRO A  50                    
SITE     2 MAB  5 LEU A  54                                                     
SITE     1 MGL  6 LEU A  27  HIS A  28  PHE A  30  ARG A  31                    
SITE     2 MGL  6 LEU A  54  ARG A  57                                          
SITE     1 AC1 34 TRP A   5  ALA A   6  ILE A  13  GLY A  14                    
SITE     2 AC1 34 LYS A  15  GLY A  17  HIS A  18  LEU A  19                    
SITE     3 AC1 34 GLY A  42  ARG A  43  ARG A  44  THR A  45                    
SITE     4 AC1 34 LEU A  62  THR A  63  HIS A  64  GLN A  65                    
SITE     5 AC1 34 HIS A  77  ALA A  97  GLY A  99  ALA A 100                    
SITE     6 AC1 34 GLN A 101  ILE A 102  MTX A 164  HOH A 208                    
SITE     7 AC1 34 HOH A 276  HOH A 279  HOH A 301  HOH A 302                    
SITE     8 AC1 34 HOH A 318  HOH A 326  HOH A 373  HOH A 401                    
SITE     9 AC1 34 HOH A 439  HOH A 579                                          
SITE     1 AC2 21 LEU A   4  TRP A   5  LEU A  19  ASP A  26                    
SITE     2 AC2 21 LEU A  27  HIS A  28  PHE A  30  ARG A  31                    
SITE     3 AC2 21 SER A  48  PHE A  49  PRO A  50  ARG A  57                    
SITE     4 AC2 21 ALA A  97  THR A 116  NDP A 163  HOH A 322                    
SITE     5 AC2 21 HOH A 329  HOH A 331  HOH A 559  HOH A 606                    
SITE     6 AC2 21 HOH A 621                                                     
CRYST1   71.860   71.860   93.380  90.00  90.00 120.00 P 61          6          
ORIGX1      0.013916  0.008034  0.000000        0.00000                         
ORIGX2      0.000000  0.016069  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  0.010709        0.00000                         
SCALE1      0.013916  0.008034  0.000000        0.00000                         
SCALE2      0.000000  0.016069  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010709        0.00000                         
ATOM      1  N   THR A   1      -0.313  18.726  33.523  1.00 21.00           N  
ATOM      2  CA  THR A   1       0.244  19.616  32.506  1.00 21.40           C  
ATOM      3  C   THR A   1      -0.578  19.597  31.226  1.00 18.90           C  
ATOM      4  O   THR A   1      -0.895  18.552  30.694  1.00 17.80           O  
ATOM      5  CB  THR A   1       1.466  18.956  32.113  1.00 21.50           C  
ATOM      6  OG1 THR A   1       2.321  18.956  33.299  1.00 26.50           O  
ATOM      7  CG2 THR A   1       2.512  19.659  31.133  1.00 14.90           C  
ATOM      8  N   ALA A   2      -1.002  20.842  30.834  1.00 13.20           N  
ATOM      9  CA  ALA A   2      -1.868  21.010  29.648  1.00 13.50           C  
ATOM     10  C   ALA A   2      -0.999  21.570  28.416  1.00 11.60           C  
ATOM     11  O   ALA A   2      -0.040  22.323  28.649  1.00 12.60           O  
ATOM     12  CB  ALA A   2      -3.015  21.925  29.975  1.00  9.90           C  
ATOM     13  N   PHE A   3      -1.387  21.234  27.174  1.00 13.20           N  
ATOM     14  CA  PHE A   3      -0.891  21.968  26.025  1.00 12.00           C  
ATOM     15  C   PHE A   3      -2.084  22.827  25.567  1.00 13.00           C  
ATOM     16  O   PHE A   3      -3.230  22.348  25.549  1.00 13.20           O  
ATOM     17  CB  PHE A   3      -0.733  20.923  24.895  1.00 10.50           C  
ATOM     18  CG  PHE A   3       0.600  20.257  24.923  1.00 11.30           C  
ATOM     19  CD1 PHE A   3       1.689  20.300  25.950  1.00  9.50           C  
ATOM     20  CD2 PHE A   3       1.099  19.516  23.952  1.00 11.90           C  
ATOM     21  CE1 PHE A   3       2.874  19.603  25.698  1.00 10.10           C  
ATOM     22  CE2 PHE A   3       2.181  18.800  23.616  1.00 15.90           C  
ATOM     23  CZ  PHE A   3       3.234  18.832  24.550  1.00 11.50           C  
ATOM     24  N   LEU A   4      -1.761  24.009  25.222  1.00 10.90           N  
ATOM     25  CA  LEU A   4      -2.806  24.912  24.764  1.00 11.50           C  
ATOM     26  C   LEU A   4      -2.386  25.478  23.401  1.00  8.00           C  
ATOM     27  O   LEU A   4      -1.311  26.082  23.270  1.00 11.00           O  
ATOM     28  CB  LEU A   4      -2.813  26.094  25.810  1.00  9.20           C  
ATOM     29  CG  LEU A   4      -3.747  27.351  25.474  1.00  8.00           C  
ATOM     30  CD1 LEU A   4      -5.213  26.978  25.381  1.00 11.00           C  
ATOM     31  CD2 LEU A   4      -3.582  28.372  26.688  1.00 10.70           C  
ATOM     32  N   TRP A   5      -3.176  25.242  22.430  1.00 10.60           N  
ATOM     33  CA  TRP A   5      -2.856  25.746  21.057  1.00  7.80           C  
ATOM     34  C   TRP A   5      -4.189  25.939  20.245  1.00 10.30           C  
ATOM     35  O   TRP A   5      -5.192  25.347  20.441  1.00 11.40           O  
ATOM     36  CB  TRP A   5      -1.761  24.843  20.348  1.00  8.00           C  
ATOM     37  CG  TRP A   5      -2.289  23.605  19.741  1.00 12.00           C  
ATOM     38  CD1 TRP A   5      -2.587  23.437  18.415  1.00  8.90           C  
ATOM     39  CD2 TRP A   5      -2.695  22.366  20.348  1.00  7.80           C  
ATOM     40  NE1 TRP A   5      -2.986  22.124  18.088  1.00  8.60           N  
ATOM     41  CE2 TRP A   5      -3.054  21.483  19.255  1.00  8.20           C  
ATOM     42  CE3 TRP A   5      -2.634  21.937  21.655  1.00 12.50           C  
ATOM     43  CZ2 TRP A   5      -3.453  20.157  19.516  1.00 11.00           C  
ATOM     44  CZ3 TRP A   5      -3.065  20.655  21.814  1.00 10.30           C  
ATOM     45  CH2 TRP A   5      -3.500  19.665  20.842  1.00  8.80           C  
ATOM     46  N   ALA A   6      -3.880  26.710  19.134  1.00  9.00           N  
ATOM     47  CA  ALA A   6      -5.005  26.891  18.069  1.00  8.30           C  
ATOM     48  C   ALA A   6      -4.383  26.399  16.771  1.00 11.30           C  
ATOM     49  O   ALA A   6      -3.212  26.772  16.510  1.00 13.50           O  
ATOM     50  CB  ALA A   6      -5.328  28.397  17.994  1.00  6.10           C  
ATOM     51  N   GLN A   7      -5.163  25.683  15.949  1.00 12.60           N  
ATOM     52  CA  GLN A   7      -4.613  25.142  14.679  1.00  6.90           C  
ATOM     53  C   GLN A   7      -5.846  25.260  13.718  1.00 12.10           C  
ATOM     54  O   GLN A   7      -6.974  25.335  13.988  1.00 14.90           O  
ATOM     55  CB  GLN A   7      -4.168  23.673  14.847  1.00  6.50           C  
ATOM     56  CG  GLN A   7      -5.357  22.734  15.193  1.00  7.20           C  
ATOM     57  CD  GLN A   7      -4.901  21.308  15.174  1.00 15.90           C  
ATOM     58  OE1 GLN A   7      -3.880  20.985  15.650  1.00 13.40           O  
ATOM     59  NE2 GLN A   7      -5.519  20.562  14.324  1.00 16.10           N  
ATOM     60  N   ASN A   8      -5.404  25.354  12.457  1.00 12.90           N  
ATOM     61  CA  ASN A   8      -6.392  25.310  11.234  1.00 12.10           C  
ATOM     62  C   ASN A   8      -6.643  23.792  11.224  1.00 12.90           C  
ATOM     63  O   ASN A   8      -6.148  22.846  11.803  1.00 15.50           O  
ATOM     64  CB  ASN A   8      -5.770  26.100  10.066  1.00 14.10           C  
ATOM     65  CG  ASN A   8      -4.800  25.304   9.217  1.00 13.40           C  
ATOM     66  OD1 ASN A   8      -4.466  25.833   8.152  1.00 17.40           O  
ATOM     67  ND2 ASN A   8      -4.268  24.096   9.403  1.00  9.40           N  
ATOM     68  N   ARG A   9      -7.491  23.580  10.104  1.00 12.40           N  
ATOM     69  CA  ARG A   9      -7.948  22.217   9.777  1.00 16.00           C  
ATOM     70  C   ARG A   9      -6.981  21.203   9.459  1.00 17.60           C  
ATOM     71  O   ARG A   9      -7.154  20.045   9.590  1.00 18.20           O  
ATOM     72  CB  ARG A   9      -9.177  22.304   8.712  1.00 18.60           C  
ATOM     73  CG  ARG A   9      -8.648  22.373   7.358  1.00 23.00           C  
ATOM     74  CD  ARG A   9      -9.834  21.526   6.518  1.00 48.50           C  
ATOM     75  NE  ARG A   9      -9.830  22.491   5.463  1.00 35.60           N  
ATOM     76  CZ  ARG A   9     -10.150  23.319   4.398  1.00 56.50           C  
ATOM     77  NH1 ARG A   9     -10.969  24.439   4.669  1.00 49.30           N  
ATOM     78  NH2 ARG A   9      -9.676  23.144   3.072  1.00 59.00           N  
ATOM     79  N   ASN A  10      -5.770  21.582   8.974  1.00 13.60           N  
ATOM     80  CA  ASN A  10      -4.624  20.680   8.600  1.00 16.50           C  
ATOM     81  C   ASN A  10      -3.625  20.705   9.758  1.00 17.50           C  
ATOM     82  O   ASN A  10      -2.576  20.194   9.487  1.00 19.80           O  
ATOM     83  CB  ASN A  10      -4.042  21.153   7.209  1.00 16.10           C  
ATOM     84  CG  ASN A  10      -5.278  20.891   6.023  1.00 18.60           C  
ATOM     85  OD1 ASN A  10      -5.116  22.217   5.425  1.00 42.30           O  
ATOM     86  ND2 ASN A  10      -5.738  19.560   6.088  1.00 48.80           N  
ATOM     87  N   GLY A  11      -3.805  21.427  10.879  1.00 14.30           N  
ATOM     88  CA  GLY A  11      -2.774  21.408  11.925  1.00 12.30           C  
ATOM     89  C   GLY A  11      -1.775  22.566  12.027  1.00 14.20           C  
ATOM     90  O   GLY A  11      -0.819  22.603  12.793  1.00 15.90           O  
ATOM     91  N   LEU A  12      -2.041  23.499  10.944  1.00 14.30           N  
ATOM     92  CA  LEU A  12      -1.096  24.576  10.916  1.00 13.00           C  
ATOM     93  C   LEU A  12      -1.121  25.466  12.130  1.00 12.10           C  
ATOM     94  O   LEU A  12      -2.228  25.827  12.569  1.00 10.90           O  
ATOM     95  CB  LEU A  12      -1.337  25.466   9.693  1.00 15.10           C  
ATOM     96  CG  LEU A  12      -0.384  26.704   9.403  1.00 17.80           C  
ATOM     97  CD1 LEU A  12       0.794  25.970   8.740  1.00 15.20           C  
ATOM     98  CD2 LEU A  12      -1.107  27.669   8.544  1.00 17.80           C  
ATOM     99  N   ILE A  13      -0.057  25.926  12.812  1.00 12.30           N  
ATOM    100  CA  ILE A  13      -0.075  26.828  13.932  1.00  7.60           C  
ATOM    101  C   ILE A  13       0.636  28.210  13.830  1.00  9.80           C  
ATOM    102  O   ILE A  13       0.492  29.193  14.530  1.00 13.90           O  
ATOM    103  CB  ILE A  13       0.456  26.119  15.286  1.00 10.30           C  
ATOM    104  CG1 ILE A  13       1.965  25.845  15.156  1.00 11.80           C  
ATOM    105  CG2 ILE A  13      -0.453  24.831  15.529  1.00  9.50           C  
ATOM    106  CD1 ILE A  13       2.537  25.428  16.547  1.00 14.30           C  
ATOM    107  N   GLY A  14       1.541  28.210  12.700  1.00 12.80           N  
ATOM    108  CA  GLY A  14       2.317  29.492  12.662  1.00  9.90           C  
ATOM    109  C   GLY A  14       2.774  29.859  11.140  1.00  8.50           C  
ATOM    110  O   GLY A  14       2.777  28.969  10.309  1.00 12.90           O  
ATOM    111  N   LYS A  15       3.223  31.098  10.981  1.00 11.90           N  
ATOM    112  CA  LYS A  15       3.650  31.539   9.712  1.00 17.60           C  
ATOM    113  C   LYS A  15       4.628  32.660  10.001  1.00 14.40           C  
ATOM    114  O   LYS A  15       4.330  33.711  10.701  1.00 14.80           O  
ATOM    115  CB  LYS A  15       2.619  32.255   8.862  1.00 18.60           C  
ATOM    116  CG  LYS A  15       3.004  32.622   7.349  1.00 30.80           C  
ATOM    117  CD  LYS A  15       1.901  33.388   6.621  1.00 36.10           C  
ATOM    118  CE  LYS A  15       2.023  33.786   5.173  1.00 65.10           C  
ATOM    119  NZ  LYS A  15       2.001  32.678   4.090  1.00110.40           N  
ATOM    120  N   ASP A  16       5.907  32.573   9.618  1.00 18.30           N  
ATOM    121  CA  ASP A  16       6.960  33.649   9.599  1.00 28.80           C  
ATOM    122  C   ASP A  16       7.136  34.128  10.972  1.00 26.10           C  
ATOM    123  O   ASP A  16       7.330  35.336  11.122  1.00 24.80           O  
ATOM    124  CB  ASP A  16       6.701  34.819   8.414  1.00 32.90           C  
ATOM    125  CG  ASP A  16       6.690  34.365   6.947  1.00 45.50           C  
ATOM    126  OD1 ASP A  16       7.621  33.662   6.312  1.00107.60           O  
ATOM    127  OD2 ASP A  16       5.731  34.856   6.154  1.00 60.20           O  
ATOM    128  N   GLY A  17       7.042  33.319  12.037  1.00 18.90           N  
ATOM    129  CA  GLY A  17       7.168  33.811  13.521  1.00 14.30           C  
ATOM    130  C   GLY A  17       5.964  34.427  14.091  1.00 15.00           C  
ATOM    131  O   GLY A  17       6.105  34.794  15.268  1.00 20.80           O  
ATOM    132  N   HIS A  18       4.793  34.352  13.409  1.00 18.10           N  
ATOM    133  CA  HIS A  18       3.618  35.031  13.932  1.00 14.10           C  
ATOM    134  C   HIS A  18       2.440  34.010  13.652  1.00 11.30           C  
ATOM    135  O   HIS A  18       2.680  32.834  13.251  1.00 12.60           O  
ATOM    136  CB  HIS A  18       3.324  36.462  13.223  1.00 20.00           C  
ATOM    137  CG  HIS A  18       3.352  36.599  11.710  1.00 55.30           C  
ATOM    138  ND1 HIS A  18       2.188  36.275  10.785  1.00 44.50           N  
ATOM    139  CD2 HIS A  18       4.344  37.022  10.851  1.00 39.90           C  
ATOM    140  CE1 HIS A  18       2.637  36.406   9.413  1.00 58.50           C  
ATOM    141  NE2 HIS A  18       3.880  36.904   9.310  1.00 61.90           N  
ATOM    142  N   LEU A  19       1.211  34.284  13.988  1.00 14.40           N  
ATOM    143  CA  LEU A  19       0.036  33.531  13.820  1.00 16.50           C  
ATOM    144  C   LEU A  19      -0.291  33.836  12.326  1.00 19.20           C  
ATOM    145  O   LEU A  19      -0.115  34.614  11.570  1.00 21.90           O  
ATOM    146  CB  LEU A  19      -1.161  33.724  14.679  1.00 15.20           C  
ATOM    147  CG  LEU A  19      -0.697  33.543  16.164  1.00 20.10           C  
ATOM    148  CD1 LEU A  19      -1.904  34.128  16.855  1.00 28.40           C  
ATOM    149  CD2 LEU A  19      -0.625  32.174  16.547  1.00 14.50           C  
ATOM    150  N   PRO A  20      -0.923  32.479  11.906  1.00 14.70           N  
ATOM    151  CA  PRO A  20      -1.293  32.685  10.375  1.00 11.40           C  
ATOM    152  C   PRO A  20      -2.652  33.369  10.225  1.00 17.90           C  
ATOM    153  O   PRO A  20      -3.212  33.506   9.067  1.00 21.40           O  
ATOM    154  CB  PRO A  20      -1.699  31.259   9.814  1.00  8.80           C  
ATOM    155  CG  PRO A  20      -0.870  30.394  10.673  1.00 12.90           C  
ATOM    156  CD  PRO A  20      -1.179  30.855  12.102  1.00 15.40           C  
ATOM    157  N   TRP A  21      -3.431  33.799  11.224  1.00 13.30           N  
ATOM    158  CA  TRP A  21      -4.782  34.334  11.271  1.00 14.00           C  
ATOM    159  C   TRP A  21      -4.674  35.417  12.382  1.00 15.30           C  
ATOM    160  O   TRP A  21      -3.848  35.479  13.297  1.00 13.40           O  
ATOM    161  CB  TRP A  21      -5.900  33.319  11.458  1.00 10.50           C  
ATOM    162  CG  TRP A  21      -5.627  32.635  12.830  1.00 14.60           C  
ATOM    163  CD1 TRP A  21      -5.688  32.890  14.194  1.00 14.20           C  
ATOM    164  CD2 TRP A  21      -4.976  31.272  12.718  1.00 14.50           C  
ATOM    165  NE1 TRP A  21      -5.124  31.900  14.903  1.00 14.10           N  
ATOM    166  CE2 TRP A  21      -4.728  30.855  14.100  1.00 15.10           C  
ATOM    167  CE3 TRP A  21      -4.703  30.313  11.635  1.00 13.40           C  
ATOM    168  CZ2 TRP A  21      -4.067  29.685  14.483  1.00 12.20           C  
ATOM    169  CZ3 TRP A  21      -4.161  29.075  12.055  1.00 16.30           C  
ATOM    170  CH2 TRP A  21      -3.888  28.789  13.409  1.00 11.60           C  
ATOM    171  N   HIS A  22      -5.849  36.058  12.606  1.00 16.10           N  
ATOM    172  CA  HIS A  22      -6.112  37.022  13.680  1.00 14.00           C  
ATOM    173  C   HIS A  22      -7.621  36.748  13.970  1.00 14.60           C  
ATOM    174  O   HIS A  22      -8.612  36.798  13.400  1.00 18.00           O  
ATOM    175  CB  HIS A  22      -5.946  38.541  13.195  1.00 19.10           C  
ATOM    176  CG  HIS A  22      -6.202  39.356  14.418  1.00 19.40           C  
ATOM    177  ND1 HIS A  22      -5.612  39.356  15.604  1.00 23.80           N  
ATOM    178  CD2 HIS A  22      -7.247  40.383  14.539  1.00 24.40           C  
ATOM    179  CE1 HIS A  22      -6.130  40.289  16.482  1.00 31.90           C  
ATOM    180  NE2 HIS A  22      -7.071  40.961  15.707  1.00 27.90           N  
ATOM    181  N   LEU A  23      -7.606  36.213  15.249  1.00 13.10           N  
ATOM    182  CA  LEU A  23      -8.828  35.591  15.912  1.00 15.60           C  
ATOM    183  C   LEU A  23      -8.878  35.927  17.518  1.00 15.90           C  
ATOM    184  O   LEU A  23      -8.760  35.336  18.424  1.00 20.00           O  
ATOM    185  CB  LEU A  23      -9.076  34.054  15.763  1.00 17.60           C  
ATOM    186  CG  LEU A  23     -10.290  33.481  16.201  1.00 15.30           C  
ATOM    187  CD1 LEU A  23     -11.454  34.128  15.482  1.00 15.30           C  
ATOM    188  CD2 LEU A  23     -10.021  31.932  16.071  1.00 13.00           C  
ATOM    189  N   PRO A  24      -9.536  37.277  17.425  1.00 15.00           N  
ATOM    190  CA  PRO A  24      -9.662  37.806  18.825  1.00 11.70           C  
ATOM    191  C   PRO A  24     -10.416  36.873  19.713  1.00 16.60           C  
ATOM    192  O   PRO A  24      -9.938  36.941  20.889  1.00 13.10           O  
ATOM    193  CB  PRO A  24     -10.571  39.182  18.751  1.00 14.80           C  
ATOM    194  CG  PRO A  24      -9.795  39.767  17.621  1.00 28.50           C  
ATOM    195  CD  PRO A  24     -10.154  38.696  16.547  1.00 22.50           C  
ATOM    196  N   ASP A  25     -11.469  36.207  19.554  1.00 12.90           N  
ATOM    197  CA  ASP A  25     -12.112  35.429  20.478  1.00 18.00           C  
ATOM    198  C   ASP A  25     -11.167  34.452  21.281  1.00 16.60           C  
ATOM    199  O   ASP A  25     -11.282  33.991  22.308  1.00 16.80           O  
ATOM    200  CB  ASP A  25     -13.140  34.670  19.638  1.00 15.40           C  
ATOM    201  CG  ASP A  25     -14.113  34.066  20.441  1.00 20.00           C  
ATOM    202  OD1 ASP A  25     -14.800  34.483  21.403  1.00 23.10           O  
ATOM    203  OD2 ASP A  25     -14.246  32.765  20.394  1.00 16.80           O  
ATOM    204  N   ASP A  26     -10.355  33.879  20.301  1.00 14.80           N  
ATOM    205  CA  ASP A  26      -9.367  32.815  20.758  1.00 10.40           C  
ATOM    206  C   ASP A  26      -8.357  33.369  21.673  1.00 11.10           C  
ATOM    207  O   ASP A  26      -7.671  32.865  22.645  1.00 12.00           O  
ATOM    208  CB  ASP A  26      -8.821  32.068  19.488  1.00 10.90           C  
ATOM    209  CG  ASP A  26      -7.599  31.185  19.862  1.00 13.00           C  
ATOM    210  OD1 ASP A  26      -6.410  31.465  19.703  1.00 10.10           O  
ATOM    211  OD2 ASP A  26      -7.876  30.071  20.553  1.00 13.30           O  
ATOM    212  N   LEU A  27      -7.869  34.626  21.421  1.00 13.60           N  
ATOM    213  CA  LEU A  27      -6.927  35.336  22.299  1.00 12.70           C  
ATOM    214  C   LEU A  27      -7.696  35.609  23.634  1.00 11.80           C  
ATOM    215  O   LEU A  27      -6.870  35.485  24.550  1.00 16.60           O  
ATOM    216  CB  LEU A  27      -6.414  36.674  21.655  1.00 15.90           C  
ATOM    217  CG  LEU A  27      -5.576  36.605  20.450  1.00 21.10           C  
ATOM    218  CD1 LEU A  27      -5.178  38.005  19.806  1.00 19.70           C  
ATOM    219  CD2 LEU A  27      -4.355  35.746  20.413  1.00 14.30           C  
ATOM    220  N   HIS A  28      -8.997  35.896  23.691  1.00 12.20           N  
ATOM    221  CA  HIS A  28      -9.514  36.194  25.063  1.00 15.20           C  
ATOM    222  C   HIS A  28      -9.597  34.744  25.549  1.00 17.80           C  
ATOM    223  O   HIS A  28      -9.424  34.657  26.791  1.00 13.60           O  
ATOM    224  CB  HIS A  28     -11.002  36.680  24.886  1.00 17.00           C  
ATOM    225  CG  HIS A  28     -11.031  37.974  24.036  1.00 25.80           C  
ATOM    226  ND1 HIS A  28     -10.179  38.964  23.728  1.00 33.00           N  
ATOM    227  CD2 HIS A  28     -12.249  38.217  23.168  1.00 18.70           C  
ATOM    228  CE1 HIS A  28     -10.689  39.798  22.813  1.00 23.80           C  
ATOM    229  NE2 HIS A  28     -11.929  39.381  22.449  1.00 34.30           N  
ATOM    230  N   TYR A  29      -9.812  33.612  24.942  1.00 15.90           N  
ATOM    231  CA  TYR A  29      -9.863  32.292  25.577  1.00 17.50           C  
ATOM    232  C   TYR A  29      -8.444  31.963  26.137  1.00 16.20           C  
ATOM    233  O   TYR A  29      -8.311  31.347  27.164  1.00 14.70           O  
ATOM    234  CB  TYR A  29     -10.240  31.328  24.466  1.00 14.50           C  
ATOM    235  CG  TYR A  29     -10.190  29.921  24.942  1.00 14.50           C  
ATOM    236  CD1 TYR A  29     -11.275  29.361  25.661  1.00 14.90           C  
ATOM    237  CD2 TYR A  29      -9.302  28.932  24.643  1.00 11.20           C  
ATOM    238  CE1 TYR A  29     -11.465  27.998  26.044  1.00 18.90           C  
ATOM    239  CE2 TYR A  29      -9.306  27.569  24.932  1.00 13.00           C  
ATOM    240  CZ  TYR A  29     -10.430  27.152  25.764  1.00 15.90           C  
ATOM    241  OH  TYR A  29     -10.657  25.814  26.118  1.00 18.30           O  
ATOM    242  N   PHE A  30      -7.369  32.243  25.297  1.00 16.60           N  
ATOM    243  CA  PHE A  30      -5.961  32.056  25.773  1.00 16.70           C  
ATOM    244  C   PHE A  30      -5.698  32.660  27.192  1.00 11.60           C  
ATOM    245  O   PHE A  30      -5.012  32.143  27.939  1.00 15.50           O  
ATOM    246  CB  PHE A  30      -4.994  32.647  24.587  1.00 15.40           C  
ATOM    247  CG  PHE A  30      -3.589  32.517  24.923  1.00 14.00           C  
ATOM    248  CD1 PHE A  30      -3.029  33.649  25.558  1.00 12.00           C  
ATOM    249  CD2 PHE A  30      -2.874  31.403  24.783  1.00 11.80           C  
ATOM    250  CE1 PHE A  30      -1.667  33.668  26.016  1.00 13.20           C  
ATOM    251  CE2 PHE A  30      -1.448  31.371  25.119  1.00 14.80           C  
ATOM    252  CZ  PHE A  30      -0.963  32.548  25.708  1.00 16.10           C  
ATOM    253  N   ARG A  31      -6.130  33.942  27.136  1.00 12.00           N  
ATOM    254  CA  ARG A  31      -5.950  34.664  28.462  1.00 15.70           C  
ATOM    255  C   ARG A  31      -6.726  33.904  29.555  1.00 13.70           C  
ATOM    256  O   ARG A  31      -6.202  33.668  30.685  1.00 19.70           O  
ATOM    257  CB  ARG A  31      -6.493  36.076  28.247  1.00 16.80           C  
ATOM    258  CG  ARG A  31      -6.360  36.879  29.629  1.00 20.80           C  
ATOM    259  CD  ARG A  31      -6.791  38.435  29.639  1.00 26.30           C  
ATOM    260  NE  ARG A  31      -7.366  39.169  30.843  1.00 73.50           N  
ATOM    261  CZ  ARG A  31      -6.313  39.661  31.740  1.00 65.60           C  
ATOM    262  NH1 ARG A  31      -5.048  40.084  31.394  1.00 51.30           N  
ATOM    263  NH2 ARG A  31      -6.827  39.592  33.057  1.00 79.10           N  
ATOM    264  N   ALA A  32      -8.012  33.543  29.405  1.00 14.20           N  
ATOM    265  CA  ALA A  32      -8.835  32.803  30.414  1.00 16.30           C  
ATOM    266  C   ALA A  32      -8.145  31.608  30.955  1.00 15.80           C  
ATOM    267  O   ALA A  32      -8.318  31.098  31.973  1.00 19.90           O  
ATOM    268  CB  ALA A  32     -10.197  32.411  29.863  1.00 17.00           C  
ATOM    269  N   GLN A  33      -7.423  30.867  29.956  1.00 16.50           N  
ATOM    270  CA  GLN A  33      -6.755  29.635  30.190  1.00 15.50           C  
ATOM    271  C   GLN A  33      -5.415  29.853  30.778  1.00 13.50           C  
ATOM    272  O   GLN A  33      -4.822  28.727  31.011  1.00 19.70           O  
ATOM    273  CB  GLN A  33      -6.758  28.633  28.901  1.00 13.30           C  
ATOM    274  CG  GLN A  33      -8.188  28.322  28.322  1.00 14.60           C  
ATOM    275  CD  GLN A  33      -8.961  27.469  29.340  1.00 23.90           C  
ATOM    276  OE1 GLN A  33      -8.451  26.735  30.162  1.00 26.20           O  
ATOM    277  NE2 GLN A  33     -10.024  28.017  29.443  1.00 28.80           N  
ATOM    278  N   THR A  34      -4.865  31.067  30.871  1.00 16.20           N  
ATOM    279  CA  THR A  34      -3.474  31.010  31.301  1.00 10.60           C  
ATOM    280  C   THR A  34      -3.334  32.000  32.534  1.00 13.10           C  
ATOM    281  O   THR A  34      -2.300  31.776  33.150  1.00 18.90           O  
ATOM    282  CB  THR A  34      -2.429  31.539  30.208  1.00 12.80           C  
ATOM    283  OG1 THR A  34      -2.928  32.691  29.583  1.00 12.50           O  
ATOM    284  CG2 THR A  34      -2.267  30.475  29.060  1.00 15.30           C  
ATOM    285  N   VAL A  35      -4.391  32.859  32.608  1.00 16.20           N  
ATOM    286  CA  VAL A  35      -4.240  33.755  33.822  1.00 16.20           C  
ATOM    287  C   VAL A  35      -4.118  32.909  35.139  1.00 10.70           C  
ATOM    288  O   VAL A  35      -4.851  31.925  35.279  1.00 19.30           O  
ATOM    289  CB  VAL A  35      -5.386  34.782  34.130  1.00 17.70           C  
ATOM    290  CG1 VAL A  35      -5.081  35.784  33.141  1.00 21.50           C  
ATOM    291  CG2 VAL A  35      -6.651  34.060  33.804  1.00 25.60           C  
ATOM    292  N   GLY A  36      -3.194  33.400  36.017  1.00 18.10           N  
ATOM    293  CA  GLY A  36      -2.961  32.597  37.184  1.00 14.10           C  
ATOM    294  C   GLY A  36      -2.177  31.403  37.128  1.00 24.20           C  
ATOM    295  O   GLY A  36      -1.797  30.867  38.090  1.00 24.60           O  
ATOM    296  N   LYS A  37      -1.721  30.911  35.942  1.00 20.60           N  
ATOM    297  CA  LYS A  37      -1.060  29.592  35.914  1.00 18.60           C  
ATOM    298  C   LYS A  37       0.359  29.834  35.615  1.00 18.30           C  
ATOM    299  O   LYS A  37       0.812  31.004  35.438  1.00 14.70           O  
ATOM    300  CB  LYS A  37      -1.750  28.919  34.635  1.00 15.70           C  
ATOM    301  CG  LYS A  37      -3.176  28.652  35.111  1.00 23.20           C  
ATOM    302  CD  LYS A  37      -3.898  27.812  34.186  1.00 29.00           C  
ATOM    303  CE  LYS A  37      -5.296  27.258  34.709  1.00 27.20           C  
ATOM    304  NZ  LYS A  37      -6.414  27.949  35.083  1.00 61.60           N  
ATOM    305  N   ILE A  38       1.204  28.832  35.484  1.00 17.30           N  
ATOM    306  CA  ILE A  38       2.576  28.895  34.952  1.00 15.30           C  
ATOM    307  C   ILE A  38       2.565  28.590  33.505  1.00 18.90           C  
ATOM    308  O   ILE A  38       2.177  27.532  32.991  1.00 13.80           O  
ATOM    309  CB  ILE A  38       3.460  27.837  35.774  1.00 14.90           C  
ATOM    310  CG1 ILE A  38       3.341  28.254  37.287  1.00 13.30           C  
ATOM    311  CG2 ILE A  38       4.879  27.818  35.130  1.00 14.40           C  
ATOM    312  CD1 ILE A  38       3.913  27.065  37.978  1.00 19.80           C  
ATOM    313  N   MET A  39       2.749  29.567  32.683  1.00 15.50           N  
ATOM    314  CA  MET A  39       2.623  29.585  31.329  1.00 14.30           C  
ATOM    315  C   MET A  39       3.999  29.318  30.610  1.00 14.20           C  
ATOM    316  O   MET A  39       4.847  30.251  30.741  1.00 16.60           O  
ATOM    317  CB  MET A  39       1.908  30.836  30.787  1.00 12.40           C  
ATOM    318  CG  MET A  39       1.664  30.712  29.144  1.00 15.10           C  
ATOM    319  SD  MET A  39       1.358  32.398  28.528  1.00 17.60           S  
ATOM    320  CE  MET A  39       2.770  33.338  28.789  1.00 19.20           C  
ATOM    321  N   VAL A  40       4.380  28.247  29.938  1.00 11.90           N  
ATOM    322  CA  VAL A  40       5.677  28.017  29.256  1.00 10.00           C  
ATOM    323  C   VAL A  40       5.609  28.222  27.790  1.00 14.00           C  
ATOM    324  O   VAL A  40       4.768  27.625  27.183  1.00  9.60           O  
ATOM    325  CB  VAL A  40       6.072  26.586  29.620  1.00 10.60           C  
ATOM    326  CG1 VAL A  40       7.416  26.225  29.163  1.00 12.60           C  
ATOM    327  CG2 VAL A  40       6.007  26.324  31.217  1.00 11.40           C  
ATOM    328  N   VAL A  41       6.482  29.075  27.360  1.00 12.60           N  
ATOM    329  CA  VAL A  41       6.572  29.380  25.922  1.00 13.10           C  
ATOM    330  C   VAL A  41       8.059  29.392  25.521  1.00 20.00           C  
ATOM    331  O   VAL A  41       8.939  29.560  26.342  1.00 16.10           O  
ATOM    332  CB  VAL A  41       6.069  30.824  25.530  1.00 12.00           C  
ATOM    333  CG1 VAL A  41       4.520  30.755  25.680  1.00 21.60           C  
ATOM    334  CG2 VAL A  41       6.550  31.882  26.576  1.00 13.20           C  
ATOM    335  N   GLY A  42       8.332  28.994  24.325  1.00 14.20           N  
ATOM    336  CA  GLY A  42       9.651  29.025  23.662  1.00 12.90           C  
ATOM    337  C   GLY A  42       9.949  30.475  23.420  1.00 12.80           C  
ATOM    338  O   GLY A  42       9.159  31.483  23.336  1.00 12.90           O  
ATOM    339  N   ARG A  43      11.286  30.799  23.364  1.00 14.30           N  
ATOM    340  CA  ARG A  43      11.817  32.131  23.252  1.00 15.10           C  
ATOM    341  C   ARG A  43      11.117  32.871  22.010  1.00 14.40           C  
ATOM    342  O   ARG A  43      10.858  34.103  22.094  1.00 17.20           O  
ATOM    343  CB  ARG A  43      13.319  32.106  23.233  1.00 12.90           C  
ATOM    344  CG  ARG A  43      13.891  33.543  23.140  1.00 15.60           C  
ATOM    345  CD  ARG A  43      14.153  34.197  21.823  1.00 17.50           C  
ATOM    346  NE  ARG A  43      14.871  33.288  20.842  1.00 19.30           N  
ATOM    347  CZ  ARG A  43      14.825  33.494  19.460  1.00 18.70           C  
ATOM    348  NH1 ARG A  43      14.038  34.496  19.022  1.00 21.80           N  
ATOM    349  NH2 ARG A  43      15.342  32.510  18.704  1.00 22.80           N  
ATOM    350  N   ARG A  44      11.142  32.068  20.833  1.00 15.50           N  
ATOM    351  CA  ARG A  44      10.517  32.853  19.703  1.00 15.10           C  
ATOM    352  C   ARG A  44       9.133  33.195  19.797  1.00 16.80           C  
ATOM    353  O   ARG A  44       8.641  34.284  19.479  1.00 15.20           O  
ATOM    354  CB  ARG A  44      10.872  31.726  18.639  1.00 18.20           C  
ATOM    355  CG  ARG A  44      10.772  32.025  17.154  1.00 34.60           C  
ATOM    356  CD  ARG A  44      11.573  30.774  16.659  1.00 31.30           C  
ATOM    357  NE  ARG A  44      12.708  30.600  16.015  1.00 37.60           N  
ATOM    358  CZ  ARG A  44      13.186  29.424  15.529  1.00 44.50           C  
ATOM    359  NH1 ARG A  44      12.399  28.260  15.174  1.00 36.90           N  
ATOM    360  NH2 ARG A  44      14.577  29.517  15.352  1.00 60.40           N  
ATOM    361  N   THR A  45       8.242  32.373  20.366  1.00 15.10           N  
ATOM    362  CA  THR A  45       6.773  32.666  20.665  1.00 17.40           C  
ATOM    363  C   THR A  45       6.967  33.799  21.795  1.00 18.70           C  
ATOM    364  O   THR A  45       6.180  34.738  21.589  1.00 17.00           O  
ATOM    365  CB  THR A  45       5.972  31.490  21.347  1.00 12.50           C  
ATOM    366  OG1 THR A  45       6.101  30.594  20.207  1.00 18.30           O  
ATOM    367  CG2 THR A  45       4.567  31.820  21.860  1.00 12.00           C  
ATOM    368  N   TYR A  46       7.703  33.755  22.841  1.00 16.20           N  
ATOM    369  CA  TYR A  46       7.617  34.900  23.700  1.00 13.30           C  
ATOM    370  C   TYR A  46       7.872  36.213  23.018  1.00 14.70           C  
ATOM    371  O   TYR A  46       7.236  37.327  23.317  1.00 14.90           O  
ATOM    372  CB  TYR A  46       8.745  34.688  24.811  1.00 16.50           C  
ATOM    373  CG  TYR A  46       8.799  35.641  25.904  1.00 19.00           C  
ATOM    374  CD1 TYR A  46       7.675  35.622  26.847  1.00 16.30           C  
ATOM    375  CD2 TYR A  46       9.816  36.680  26.006  1.00 16.50           C  
ATOM    376  CE1 TYR A  46       7.628  36.512  27.949  1.00 16.60           C  
ATOM    377  CE2 TYR A  46       9.629  37.626  27.108  1.00 15.40           C  
ATOM    378  CZ  TYR A  46       8.659  37.501  27.986  1.00 23.60           C  
ATOM    379  OH  TYR A  46       8.569  38.441  29.060  1.00 25.20           O  
ATOM    380  N   GLU A  47       8.918  36.406  22.131  1.00 23.40           N  
ATOM    381  CA  GLU A  47       9.299  37.651  21.440  1.00 21.60           C  
ATOM    382  C   GLU A  47       8.250  38.136  20.544  1.00 26.30           C  
ATOM    383  O   GLU A  47       8.091  39.343  20.170  1.00 26.30           O  
ATOM    384  CB  GLU A  47      10.542  37.414  20.600  1.00 19.70           C  
ATOM    385  CG  GLU A  47      11.605  37.476  21.748  1.00 21.00           C  
ATOM    386  CD  GLU A  47      12.982  37.420  20.982  1.00 26.00           C  
ATOM    387  OE1 GLU A  47      13.183  36.935  19.918  1.00 31.90           O  
ATOM    388  OE2 GLU A  47      13.905  37.651  21.758  1.00 26.90           O  
ATOM    389  N   SER A  48       7.272  37.427  20.067  1.00 25.40           N  
ATOM    390  CA  SER A  48       6.033  37.682  19.246  1.00 25.70           C  
ATOM    391  C   SER A  48       4.815  38.186  19.993  1.00 22.50           C  
ATOM    392  O   SER A  48       3.834  38.628  19.535  1.00 32.20           O  
ATOM    393  CB  SER A  48       5.526  36.431  18.564  1.00 16.60           C  
ATOM    394  OG  SER A  48       4.750  35.522  19.339  1.00 24.90           O  
ATOM    395  N   PHE A  49       4.840  38.030  21.421  1.00 25.40           N  
ATOM    396  CA  PHE A  49       3.791  38.678  22.290  1.00 21.50           C  
ATOM    397  C   PHE A  49       3.942  40.296  22.094  1.00 20.40           C  
ATOM    398  O   PHE A  49       5.023  40.800  22.206  1.00 27.10           O  
ATOM    399  CB  PHE A  49       3.801  38.261  23.709  1.00 18.90           C  
ATOM    400  CG  PHE A  49       3.676  36.748  23.933  1.00 19.10           C  
ATOM    401  CD1 PHE A  49       3.032  35.734  23.336  1.00 14.90           C  
ATOM    402  CD2 PHE A  49       4.254  36.431  25.334  1.00 17.10           C  
ATOM    403  CE1 PHE A  49       2.813  34.520  23.803  1.00 18.10           C  
ATOM    404  CE2 PHE A  49       4.017  35.037  25.801  1.00 13.60           C  
ATOM    405  CZ  PHE A  49       3.345  34.122  24.970  1.00 22.00           C  
ATOM    406  N   PRO A  50       2.508  40.713  22.000  1.00 26.00           N  
ATOM    407  CA  PRO A  50       2.706  42.287  21.860  1.00 26.70           C  
ATOM    408  C   PRO A  50       3.130  43.034  23.112  1.00 30.60           C  
ATOM    409  O   PRO A  50       3.665  44.098  22.943  1.00 33.30           O  
ATOM    410  CB  PRO A  50       1.157  42.953  21.823  1.00 23.20           C  
ATOM    411  CG  PRO A  50       0.449  41.715  21.412  1.00 30.10           C  
ATOM    412  CD  PRO A  50       0.762  40.601  22.346  1.00 28.20           C  
ATOM    413  N   LYS A  51       2.921  42.561  24.335  1.00 25.90           N  
ATOM    414  CA  LYS A  51       3.219  43.077  25.773  1.00 26.50           C  
ATOM    415  C   LYS A  51       4.042  41.901  26.277  1.00 26.00           C  
ATOM    416  O   LYS A  51       3.589  40.669  26.305  1.00 28.80           O  
ATOM    417  CB  LYS A  51       1.775  43.339  26.604  1.00 31.40           C  
ATOM    418  N   ARG A  52       5.278  41.963  26.875  1.00 23.90           N  
ATOM    419  CA  ARG A  52       6.169  40.731  27.360  1.00 30.70           C  
ATOM    420  C   ARG A  52       6.611  41.584  28.602  1.00 32.80           C  
ATOM    421  O   ARG A  52       7.222  42.629  28.976  1.00 29.80           O  
ATOM    422  CB  ARG A  52       7.549  40.856  26.567  1.00 17.10           C  
ATOM    423  CG  ARG A  52       7.513  40.184  25.194  1.00 19.70           C  
ATOM    424  CD  ARG A  52       8.918  40.563  24.503  1.00 23.60           C  
ATOM    425  NE  ARG A  52       8.199  41.260  23.448  1.00 42.80           N  
ATOM    426  CZ  ARG A  52       8.433  42.486  23.214  1.00 38.80           C  
ATOM    427  NH1 ARG A  52       9.539  43.071  23.606  1.00 66.20           N  
ATOM    428  NH2 ARG A  52       7.427  43.133  22.607  1.00 44.70           N  
ATOM    429  N   PRO A  53       6.460  40.961  30.115  1.00 19.70           N  
ATOM    430  CA  PRO A  53       5.691  39.667  29.984  1.00 18.50           C  
ATOM    431  C   PRO A  53       4.164  39.810  29.826  1.00 20.10           C  
ATOM    432  O   PRO A  53       3.618  40.918  30.068  1.00 17.30           O  
ATOM    433  CB  PRO A  53       5.936  38.995  31.413  1.00 19.90           C  
ATOM    434  CG  PRO A  53       5.928  40.264  32.337  1.00 25.40           C  
ATOM    435  CD  PRO A  53       7.067  40.769  31.674  1.00 22.80           C  
ATOM    436  N   LEU A  54       3.388  38.727  29.592  1.00 16.70           N  
ATOM    437  CA  LEU A  54       1.911  38.808  29.508  1.00 16.70           C  
ATOM    438  C   LEU A  54       1.678  38.839  31.058  1.00 15.50           C  
ATOM    439  O   LEU A  54       1.980  38.205  31.936  1.00 18.60           O  
ATOM    440  CB  LEU A  54       1.168  37.620  28.789  1.00 14.30           C  
ATOM    441  CG  LEU A  54       1.347  37.732  27.211  1.00 20.00           C  
ATOM    442  CD1 LEU A  54       0.575  36.369  26.819  1.00 12.50           C  
ATOM    443  CD2 LEU A  54       0.607  38.864  26.735  1.00 18.30           C  
ATOM    444  N   PRO A  55       0.557  39.935  31.170  1.00 18.40           N  
ATOM    445  CA  PRO A  55       0.406  40.059  32.711  1.00 16.60           C  
ATOM    446  C   PRO A  55      -0.485  39.138  33.421  1.00 21.60           C  
ATOM    447  O   PRO A  55      -1.276  38.379  32.748  1.00 20.20           O  
ATOM    448  CB  PRO A  55      -0.381  41.422  32.888  1.00 16.70           C  
ATOM    449  CG  PRO A  55      -1.329  41.397  31.693  1.00 31.70           C  
ATOM    450  CD  PRO A  55      -0.223  41.347  30.675  1.00 20.30           C  
ATOM    451  N   GLU A  56      -0.446  39.020  34.765  1.00 20.70           N  
ATOM    452  CA  GLU A  56      -1.329  38.161  35.615  1.00 19.80           C  
ATOM    453  C   GLU A  56      -1.067  36.636  35.466  1.00 22.60           C  
ATOM    454  O   GLU A  56      -2.041  35.896  35.821  1.00 20.60           O  
ATOM    455  CB  GLU A  56      -2.846  38.510  35.512  1.00 18.40           C  
ATOM    456  CG  GLU A  56      -3.302  39.935  36.259  1.00 52.40           C  
ATOM    457  CD  GLU A  56      -4.782  40.146  35.877  1.00 70.30           C  
ATOM    458  OE1 GLU A  56      -5.447  39.319  36.680  1.00 72.90           O  
ATOM    459  OE2 GLU A  56      -4.538  40.943  34.896  1.00 70.70           O  
ATOM    460  N   ARG A  57       0.137  36.157  35.008  1.00 20.30           N  
ATOM    461  CA  ARG A  57       0.341  34.707  34.915  1.00 16.50           C  
ATOM    462  C   ARG A  57       1.904  34.751  34.989  1.00 16.00           C  
ATOM    463  O   ARG A  57       2.623  35.734  34.663  1.00 17.40           O  
ATOM    464  CB  ARG A  57      -0.154  34.122  33.449  1.00 15.30           C  
ATOM    465  CG  ARG A  57       0.665  34.732  32.216  1.00 12.40           C  
ATOM    466  CD  ARG A  57      -0.435  34.570  31.170  1.00 14.70           C  
ATOM    467  NE  ARG A  57      -1.304  35.703  31.329  1.00 16.00           N  
ATOM    468  CZ  ARG A  57      -1.987  36.300  30.433  1.00 20.60           C  
ATOM    469  NH1 ARG A  57      -2.303  35.591  29.265  1.00 14.30           N  
ATOM    470  NH2 ARG A  57      -2.274  37.595  30.320  1.00 14.90           N  
ATOM    471  N   THR A  58       2.504  33.599  35.316  1.00 17.50           N  
ATOM    472  CA  THR A  58       3.934  33.425  35.372  1.00 13.70           C  
ATOM    473  C   THR A  58       4.337  33.077  33.888  1.00 18.80           C  
ATOM    474  O   THR A  58       3.809  32.124  33.449  1.00 17.50           O  
ATOM    475  CB  THR A  58       4.488  32.255  36.418  1.00 11.80           C  
ATOM    476  OG1 THR A  58       3.679  32.747  37.501  1.00 16.30           O  
ATOM    477  CG2 THR A  58       5.885  32.311  36.568  1.00 16.80           C  
ATOM    478  N   ASN A  59       5.170  33.911  33.327  1.00 11.40           N  
ATOM    479  CA  ASN A  59       5.623  33.562  31.936  1.00 10.60           C  
ATOM    480  C   ASN A  59       6.891  32.921  32.188  1.00 14.90           C  
ATOM    481  O   ASN A  59       7.955  33.481  32.590  1.00 14.70           O  
ATOM    482  CB  ASN A  59       5.925  34.906  31.264  1.00 11.70           C  
ATOM    483  CG  ASN A  59       4.728  35.697  31.002  1.00 16.30           C  
ATOM    484  OD1 ASN A  59       4.653  36.151  29.770  1.00 13.70           O  
ATOM    485  ND2 ASN A  59       3.730  35.983  31.787  1.00 13.30           N  
ATOM    486  N   VAL A  60       7.139  31.670  31.805  1.00 10.70           N  
ATOM    487  CA  VAL A  60       8.465  31.029  31.815  1.00  9.80           C  
ATOM    488  C   VAL A  60       8.947  30.905  30.349  1.00 20.60           C  
ATOM    489  O   VAL A  60       8.170  30.407  29.499  1.00 16.10           O  
ATOM    490  CB  VAL A  60       8.203  29.604  32.337  1.00 14.20           C  
ATOM    491  CG1 VAL A  60       9.475  28.671  32.160  1.00  9.60           C  
ATOM    492  CG2 VAL A  60       7.606  29.604  33.850  1.00 16.20           C  
ATOM    493  N   VAL A  61      10.028  31.371  30.003  1.00 16.50           N  
ATOM    494  CA  VAL A  61      10.592  31.427  28.658  1.00 14.00           C  
ATOM    495  C   VAL A  61      11.666  30.438  28.677  1.00 18.00           C  
ATOM    496  O   VAL A  61      12.701  30.450  29.443  1.00 15.60           O  
ATOM    497  CB  VAL A  61      11.174  32.846  28.388  1.00 17.60           C  
ATOM    498  CG1 VAL A  61      11.659  32.765  26.959  1.00 17.60           C  
ATOM    499  CG2 VAL A  61      10.086  33.799  28.742  1.00 15.10           C  
ATOM    500  N   LEU A  62      11.706  29.511  27.762  1.00 11.10           N  
ATOM    501  CA  LEU A  62      12.712  28.403  27.575  1.00 12.60           C  
ATOM    502  C   LEU A  62      13.714  28.870  26.473  1.00 18.70           C  
ATOM    503  O   LEU A  62      13.362  29.318  25.362  1.00 16.80           O  
ATOM    504  CB  LEU A  62      12.338  26.947  27.099  1.00 12.60           C  
ATOM    505  CG  LEU A  62      11.695  26.094  28.126  1.00 24.50           C  
ATOM    506  CD1 LEU A  62      11.498  24.644  27.556  1.00 22.50           C  
ATOM    507  CD2 LEU A  62      13.222  25.690  28.705  1.00 24.60           C  
ATOM    508  N   THR A  63      15.076  29.125  26.613  1.00 15.30           N  
ATOM    509  CA  THR A  63      15.971  29.753  25.651  1.00 17.60           C  
ATOM    510  C   THR A  63      17.361  29.025  25.670  1.00 27.80           C  
ATOM    511  O   THR A  63      17.545  28.534  26.893  1.00 17.20           O  
ATOM    512  CB  THR A  63      16.204  31.303  25.801  1.00 21.30           C  
ATOM    513  OG1 THR A  63      17.157  31.558  24.755  1.00 19.60           O  
ATOM    514  CG2 THR A  63      16.510  31.645  27.342  1.00 14.20           C  
ATOM    515  N   HIS A  64      18.213  28.720  24.802  1.00 23.80           N  
ATOM    516  CA  HIS A  64      19.528  28.135  25.091  1.00 21.60           C  
ATOM    517  C   HIS A  64      20.591  29.243  25.334  1.00 25.00           C  
ATOM    518  O   HIS A  64      21.748  28.832  25.726  1.00 36.10           O  
ATOM    519  CB  HIS A  64      19.995  27.401  23.765  1.00 22.70           C  
ATOM    520  CG  HIS A  64      19.237  26.187  23.681  1.00 23.60           C  
ATOM    521  ND1 HIS A  64      19.093  25.167  24.410  1.00 23.00           N  
ATOM    522  CD2 HIS A  64      18.504  26.075  22.477  1.00 31.00           C  
ATOM    523  CE1 HIS A  64      18.342  24.140  23.821  1.00 29.40           C  
ATOM    524  NE2 HIS A  64      17.918  24.775  22.710  1.00 26.90           N  
ATOM    525  N   GLN A  65      20.078  30.531  25.110  1.00 23.50           N  
ATOM    526  CA  GLN A  65      20.987  31.708  25.203  1.00 22.20           C  
ATOM    527  C   GLN A  65      21.281  31.844  26.651  1.00 26.30           C  
ATOM    528  O   GLN A  65      20.336  32.274  27.454  1.00 27.10           O  
ATOM    529  CB  GLN A  65      20.530  32.946  24.624  1.00 21.90           C  
ATOM    530  CG  GLN A  65      19.923  32.778  23.205  1.00 29.50           C  
ATOM    531  CD  GLN A  65      19.589  34.191  22.673  1.00 32.60           C  
ATOM    532  OE1 GLN A  65      20.074  35.255  23.093  1.00 46.50           O  
ATOM    533  NE2 GLN A  65      18.317  33.867  21.954  1.00 23.20           N  
ATOM    534  N   GLU A  66      22.381  31.508  27.407  1.00 35.70           N  
ATOM    535  CA  GLU A  66      22.729  31.726  28.845  1.00 43.20           C  
ATOM    536  C   GLU A  66      22.395  33.151  29.424  1.00 41.50           C  
ATOM    537  O   GLU A  66      21.871  33.438  30.498  1.00 45.50           O  
ATOM    538  CB  GLU A  66      24.163  31.172  29.004  1.00 62.30           C  
ATOM    539  CG  GLU A  66      23.764  29.635  29.424  1.00 76.50           C  
ATOM    540  CD  GLU A  66      24.943  29.075  30.199  1.00132.10           C  
ATOM    541  OE1 GLU A  66      25.787  29.865  30.759  1.00108.10           O  
ATOM    542  OE2 GLU A  66      24.544  27.849  29.891  1.00136.30           O  
ATOM    543  N   ASP A  67      22.686  34.228  28.593  1.00 25.20           N  
ATOM    544  CA  ASP A  67      22.485  35.647  28.826  1.00 31.40           C  
ATOM    545  C   ASP A  67      21.206  36.369  28.649  1.00 34.80           C  
ATOM    546  O   ASP A  67      21.037  37.545  28.602  1.00 30.80           O  
ATOM    547  CB  ASP A  67      22.966  36.207  27.108  1.00 70.60           C  
ATOM    548  CG  ASP A  67      24.307  35.665  26.847  1.00111.50           C  
ATOM    549  OD1 ASP A  67      24.935  36.219  28.089  1.00 90.60           O  
ATOM    550  OD2 ASP A  67      23.944  35.012  25.577  1.00111.80           O  
ATOM    551  N   TYR A  68      20.132  35.504  28.117  1.00 23.90           N  
ATOM    552  CA  TYR A  68      18.967  36.188  27.594  1.00 21.80           C  
ATOM    553  C   TYR A  68      18.375  36.954  28.770  1.00 19.50           C  
ATOM    554  O   TYR A  68      18.256  36.412  29.891  1.00 32.00           O  
ATOM    555  CB  TYR A  68      17.954  34.993  27.136  1.00 19.00           C  
ATOM    556  CG  TYR A  68      16.657  35.547  26.529  1.00 18.80           C  
ATOM    557  CD1 TYR A  68      16.887  35.933  25.157  1.00 18.60           C  
ATOM    558  CD2 TYR A  68      15.414  35.485  27.043  1.00 18.10           C  
ATOM    559  CE1 TYR A  68      15.845  36.580  24.428  1.00 17.30           C  
ATOM    560  CE2 TYR A  68      14.340  36.039  26.361  1.00 21.40           C  
ATOM    561  CZ  TYR A  68      14.491  36.537  25.007  1.00 21.00           C  
ATOM    562  OH  TYR A  68      13.456  37.134  24.325  1.00 22.60           O  
ATOM    563  N   GLN A  69      17.811  38.105  28.444  1.00 30.10           N  
ATOM    564  CA  GLN A  69      17.063  38.914  29.359  1.00 23.60           C  
ATOM    565  C   GLN A  69      15.608  39.082  28.938  1.00 22.00           C  
ATOM    566  O   GLN A  69      15.191  39.518  27.958  1.00 29.40           O  
ATOM    567  CB  GLN A  69      17.735  40.377  29.387  1.00 31.50           C  
ATOM    568  CG  GLN A  69      19.338  40.464  29.667  1.00 53.20           C  
ATOM    569  CD  GLN A  69      19.715  40.607  31.180  1.00 93.10           C  
ATOM    570  OE1 GLN A  69      19.341  41.316  32.197  1.00109.70           O  
ATOM    571  NE2 GLN A  69      20.678  39.636  31.665  1.00107.20           N  
ATOM    572  N   ALA A  70      14.818  38.870  30.012  1.00 21.70           N  
ATOM    573  CA  ALA A  70      13.380  39.045  29.919  1.00 20.00           C  
ATOM    574  C   ALA A  70      12.996  39.511  31.338  1.00 22.10           C  
ATOM    575  O   ALA A  70      12.518  38.597  32.179  1.00 18.60           O  
ATOM    576  CB  ALA A  70      12.669  37.713  29.331  1.00 16.80           C  
ATOM    577  N   GLN A  71      12.895  40.756  31.665  1.00 21.70           N  
ATOM    578  CA  GLN A  71      12.475  41.298  32.916  1.00 18.10           C  
ATOM    579  C   GLN A  71      11.124  40.812  33.225  1.00 21.00           C  
ATOM    580  O   GLN A  71      10.251  41.092  32.478  1.00 19.90           O  
ATOM    581  CB  GLN A  71      12.543  42.884  32.916  1.00 14.00           C  
ATOM    582  CG  GLN A  71      14.016  43.121  32.944  1.00 18.90           C  
ATOM    583  CD  GLN A  71      14.120  44.633  32.851  1.00 35.50           C  
ATOM    584  OE1 GLN A  71      13.312  45.461  32.552  1.00 37.10           O  
ATOM    585  NE2 GLN A  71      15.141  45.256  33.309  1.00 35.80           N  
ATOM    586  N   GLY A  72      10.876  40.358  34.467  1.00 16.70           N  
ATOM    587  CA  GLY A  72       9.493  39.991  34.859  1.00 16.30           C  
ATOM    588  C   GLY A  72       9.090  38.572  34.383  1.00 12.00           C  
ATOM    589  O   GLY A  72       8.045  38.167  34.896  1.00 20.30           O  
ATOM    590  N   ALA A  73       9.917  37.825  33.579  1.00 18.30           N  
ATOM    591  CA  ALA A  73       9.583  36.437  33.103  1.00 17.80           C  
ATOM    592  C   ALA A  73      10.484  35.522  33.832  1.00 20.40           C  
ATOM    593  O   ALA A  73      11.516  35.939  34.485  1.00 18.60           O  
ATOM    594  CB  ALA A  73       9.942  36.338  31.590  1.00 14.60           C  
ATOM    595  N   VAL A  74      10.470  34.215  33.934  1.00 13.80           N  
ATOM    596  CA  VAL A  74      11.278  33.238  34.541  1.00 12.50           C  
ATOM    597  C   VAL A  74      11.943  32.709  33.327  1.00 22.60           C  
ATOM    598  O   VAL A  74      11.505  32.000  32.459  1.00 17.60           O  
ATOM    599  CB  VAL A  74      10.441  32.137  35.251  1.00 14.20           C  
ATOM    600  CG1 VAL A  74      11.404  31.067  35.821  1.00 12.90           C  
ATOM    601  CG2 VAL A  74       9.381  32.604  36.185  1.00 16.90           C  
ATOM    602  N   VAL A  75      13.215  32.971  33.187  1.00 13.90           N  
ATOM    603  CA  VAL A  75      14.099  32.622  32.039  1.00 17.30           C  
ATOM    604  C   VAL A  75      14.832  31.340  32.468  1.00 21.60           C  
ATOM    605  O   VAL A  75      15.734  31.409  33.309  1.00 21.70           O  
ATOM    606  CB  VAL A  75      15.119  33.668  31.525  1.00 14.50           C  
ATOM    607  CG1 VAL A  75      16.068  33.195  30.470  1.00 20.70           C  
ATOM    608  CG2 VAL A  75      14.257  34.937  31.254  1.00 10.60           C  
ATOM    609  N   VAL A  76      14.652  30.033  31.889  1.00 18.20           N  
ATOM    610  CA  VAL A  76      15.339  28.820  32.113  1.00 15.60           C  
ATOM    611  C   VAL A  76      15.683  28.322  30.722  1.00 14.70           C  
ATOM    612  O   VAL A  76      15.489  28.745  29.527  1.00 19.30           O  
ATOM    613  CB  VAL A  76      14.480  27.830  32.916  1.00 16.30           C  
ATOM    614  CG1 VAL A  76      14.120  28.440  34.224  1.00 17.90           C  
ATOM    615  CG2 VAL A  76      13.125  27.538  32.160  1.00 16.50           C  
ATOM    616  N   HIS A  77      16.596  27.227  30.937  1.00 16.10           N  
ATOM    617  CA  HIS A  77      17.394  26.667  29.826  1.00 17.60           C  
ATOM    618  C   HIS A  77      17.225  25.229  29.545  1.00 20.00           C  
ATOM    619  O   HIS A  77      17.893  24.756  28.640  1.00 20.90           O  
ATOM    620  CB  HIS A  77      19.014  27.071  29.844  1.00 23.80           C  
ATOM    621  CG  HIS A  77      19.330  28.465  30.190  1.00 24.00           C  
ATOM    622  ND1 HIS A  77      19.075  29.604  29.517  1.00 20.70           N  
ATOM    623  CD2 HIS A  77      19.532  28.975  31.488  1.00 23.80           C  
ATOM    624  CE1 HIS A  77      19.363  30.786  30.134  1.00 19.90           C  
ATOM    625  NE2 HIS A  77      19.679  30.276  31.441  1.00 26.30           N  
ATOM    626  N   ASP A  78      16.345  24.563  30.264  1.00 19.60           N  
ATOM    627  CA  ASP A  78      16.172  23.107  29.872  1.00 24.60           C  
ATOM    628  C   ASP A  78      14.839  22.814  30.358  1.00 19.10           C  
ATOM    629  O   ASP A  78      14.275  23.493  31.422  1.00 18.70           O  
ATOM    630  CB  ASP A  78      17.451  22.497  30.461  1.00 33.40           C  
ATOM    631  CG  ASP A  78      17.976  22.323  31.759  1.00 39.30           C  
ATOM    632  OD1 ASP A  78      16.991  22.385  32.683  1.00 26.80           O  
ATOM    633  OD2 ASP A  78      19.330  21.906  31.572  1.00108.20           O  
ATOM    634  N   VAL A  79      14.192  21.657  30.143  1.00 18.20           N  
ATOM    635  CA  VAL A  79      12.942  21.184  30.713  1.00 20.20           C  
ATOM    636  C   VAL A  79      12.992  20.848  32.216  1.00 21.00           C  
ATOM    637  O   VAL A  79      12.022  21.184  32.898  1.00 18.30           O  
ATOM    638  CB  VAL A  79      12.532  19.865  29.798  1.00 19.10           C  
ATOM    639  CG1 VAL A  79      11.426  19.180  30.339  1.00 19.80           C  
ATOM    640  CG2 VAL A  79      12.055  20.468  28.500  1.00 18.30           C  
ATOM    641  N   ALA A  80      14.074  20.344  32.823  1.00 20.10           N  
ATOM    642  CA  ALA A  80      14.307  19.927  34.224  1.00 17.00           C  
ATOM    643  C   ALA A  80      14.067  21.290  34.952  1.00 11.50           C  
ATOM    644  O   ALA A  80      13.370  21.190  35.979  1.00 20.60           O  
ATOM    645  CB  ALA A  80      15.734  19.361  34.401  1.00 19.50           C  
ATOM    646  N   ALA A  81      14.541  22.447  34.476  1.00 14.90           N  
ATOM    647  CA  ALA A  81      14.250  23.698  35.242  1.00 17.00           C  
ATOM    648  C   ALA A  81      12.899  24.096  35.260  1.00 25.20           C  
ATOM    649  O   ALA A  81      12.464  24.688  36.222  1.00 20.10           O  
ATOM    650  CB  ALA A  81      15.101  24.762  34.569  1.00 16.40           C  
ATOM    651  N   VAL A  82      12.055  23.767  34.270  1.00 21.40           N  
ATOM    652  CA  VAL A  82      10.736  24.121  34.205  1.00 19.50           C  
ATOM    653  C   VAL A  82      10.093  23.368  35.382  1.00 16.50           C  
ATOM    654  O   VAL A  82       9.198  23.736  36.185  1.00 19.20           O  
ATOM    655  CB  VAL A  82      10.014  23.966  32.767  1.00 16.00           C  
ATOM    656  CG1 VAL A  82       8.490  24.252  32.963  1.00 17.10           C  
ATOM    657  CG2 VAL A  82      10.657  24.905  31.768  1.00 14.80           C  
ATOM    658  N   PHE A  83      10.265  22.012  35.344  1.00 15.20           N  
ATOM    659  CA  PHE A  83       9.604  21.178  36.353  1.00 14.30           C  
ATOM    660  C   PHE A  83      10.222  21.576  37.772  1.00 17.90           C  
ATOM    661  O   PHE A  83       9.360  21.464  38.603  1.00 20.10           O  
ATOM    662  CB  PHE A  83       9.884  19.709  35.989  1.00 19.50           C  
ATOM    663  CG  PHE A  83       8.893  19.273  34.887  1.00 14.90           C  
ATOM    664  CD1 PHE A  83       7.545  19.242  35.046  1.00 26.10           C  
ATOM    665  CD2 PHE A  83       9.618  18.825  33.785  1.00 19.70           C  
ATOM    666  CE1 PHE A  83       6.676  18.794  34.009  1.00 27.50           C  
ATOM    667  CE2 PHE A  83       8.835  18.390  32.646  1.00 26.60           C  
ATOM    668  CZ  PHE A  83       7.491  18.402  32.842  1.00 23.60           C  
ATOM    669  N   ALA A  84      11.408  21.788  37.950  1.00 17.30           N  
ATOM    670  CA  ALA A  84      12.004  22.248  39.294  1.00 20.80           C  
ATOM    671  C   ALA A  84      11.250  23.543  39.658  1.00 28.20           C  
ATOM    672  O   ALA A  84      10.732  23.642  40.798  1.00 22.00           O  
ATOM    673  CB  ALA A  84      13.470  22.734  39.126  1.00 20.90           C  
ATOM    674  N   TYR A  85      10.865  24.495  38.781  1.00 19.10           N  
ATOM    675  CA  TYR A  85      10.125  25.677  39.098  1.00 14.20           C  
ATOM    676  C   TYR A  85       8.720  25.260  39.500  1.00 22.50           C  
ATOM    677  O   TYR A  85       8.142  25.677  40.462  1.00 18.50           O  
ATOM    678  CB  TYR A  85      10.143  26.654  37.884  1.00 13.90           C  
ATOM    679  CG  TYR A  85       9.349  27.930  38.211  1.00 16.40           C  
ATOM    680  CD1 TYR A  85       9.974  29.000  38.846  1.00 19.10           C  
ATOM    681  CD2 TYR A  85       7.912  28.154  37.931  1.00 15.20           C  
ATOM    682  CE1 TYR A  85       9.270  30.158  39.294  1.00 21.90           C  
ATOM    683  CE2 TYR A  85       7.254  29.343  38.389  1.00 19.90           C  
ATOM    684  CZ  TYR A  85       7.955  30.432  39.024  1.00 18.20           C  
ATOM    685  OH  TYR A  85       7.305  31.471  39.453  1.00 20.70           O  
ATOM    686  N   ALA A  86       8.005  24.482  38.687  1.00 17.90           N  
ATOM    687  CA  ALA A  86       6.654  23.935  38.911  1.00 20.00           C  
ATOM    688  C   ALA A  86       6.511  23.138  40.340  1.00 17.90           C  
ATOM    689  O   ALA A  86       5.522  23.480  41.087  1.00 26.30           O  
ATOM    690  CB  ALA A  86       6.162  23.045  37.707  1.00 17.10           C  
ATOM    691  N   LYS A  87       7.499  22.385  40.732  1.00 24.10           N  
ATOM    692  CA  LYS A  87       7.646  21.694  42.002  1.00 30.40           C  
ATOM    693  C   LYS A  87       7.596  22.790  43.170  1.00 19.70           C  
ATOM    694  O   LYS A  87       6.988  22.671  44.262  1.00 34.50           O  
ATOM    695  CB  LYS A  87       8.763  20.767  42.320  1.00 28.40           C  
ATOM    696  CG  LYS A  87       8.325  19.273  42.208  1.00 60.90           C  
ATOM    697  CD  LYS A  87       9.521  18.172  42.096  1.00 61.20           C  
ATOM    698  CE  LYS A  87      10.660  18.527  43.291  1.00 71.30           C  
ATOM    699  NZ  LYS A  87      10.664  17.400  44.440  1.00 82.30           N  
ATOM    700  N   GLN A  88       8.253  23.978  43.011  1.00 21.50           N  
ATOM    701  CA  GLN A  88       8.271  25.042  44.001  1.00 26.10           C  
ATOM    702  C   GLN A  88       7.078  25.827  44.346  1.00 20.40           C  
ATOM    703  O   GLN A  88       6.676  26.573  45.261  1.00 36.00           O  
ATOM    704  CB  GLN A  88       9.593  25.864  43.889  1.00 31.00           C  
ATOM    705  CG  GLN A  88      10.524  26.542  44.841  1.00 95.70           C  
ATOM    706  CD  GLN A  88      11.052  28.067  44.729  1.00 71.00           C  
ATOM    707  OE1 GLN A  88      10.650  29.237  45.103  1.00 56.30           O  
ATOM    708  NE2 GLN A  88      12.169  28.073  44.066  1.00 37.30           N  
ATOM    709  N   HIS A  89       6.087  25.752  43.282  1.00 22.60           N  
ATOM    710  CA  HIS A  89       4.836  26.287  42.740  1.00 31.80           C  
ATOM    711  C   HIS A  89       3.758  25.391  43.076  1.00 44.20           C  
ATOM    712  O   HIS A  89       3.949  25.372  44.636  1.00 53.80           O  
ATOM    713  CB  HIS A  89       4.700  27.606  41.965  1.00 21.30           C  
ATOM    714  CG  HIS A  89       5.907  28.440  42.170  1.00 26.00           C  
ATOM    715  ND1 HIS A  89       5.835  29.697  42.796  1.00 25.10           N  
ATOM    716  CD2 HIS A  89       7.279  28.490  41.900  1.00 20.20           C  
ATOM    717  CE1 HIS A  89       7.085  30.282  42.899  1.00 25.10           C  
ATOM    718  NE2 HIS A  89       7.994  29.592  42.320  1.00 24.70           N  
ATOM    719  N   LEU A  90       3.158  24.812  42.591  1.00 39.50           N  
ATOM    720  CA  LEU A  90       2.389  23.767  43.599  1.00 33.20           C  
ATOM    721  C   LEU A  90       0.938  23.754  43.300  1.00 41.70           C  
ATOM    722  O   LEU A  90       0.140  22.970  42.703  1.00 45.20           O  
ATOM    723  CB  LEU A  90       2.946  23.263  45.056  1.00 36.80           C  
ATOM    724  CG  LEU A  90       3.101  22.074  44.580  1.00 64.70           C  
ATOM    725  CD1 LEU A  90       4.531  20.904  44.944  1.00 66.90           C  
ATOM    726  CD2 LEU A  90       1.534  21.078  45.140  1.00 87.60           C  
ATOM    727  N   ASP A  91       0.363  24.862  43.590  1.00 39.90           N  
ATOM    728  CA  ASP A  91      -0.952  25.434  43.646  1.00 46.50           C  
ATOM    729  C   ASP A  91      -1.182  26.144  42.198  1.00 28.70           C  
ATOM    730  O   ASP A  91      -2.386  26.660  41.918  1.00 59.70           O  
ATOM    731  CB  ASP A  91      -0.902  26.380  45.065  1.00 40.20           C  
ATOM    732  CG  ASP A  91       0.162  27.463  44.701  1.00 63.80           C  
ATOM    733  OD1 ASP A  91       0.133  28.671  44.075  1.00 90.20           O  
ATOM    734  OD2 ASP A  91       1.513  27.177  44.785  1.00 67.30           O  
ATOM    735  N   GLN A  92      -0.025  26.281  41.330  1.00 24.10           N  
ATOM    736  CA  GLN A  92      -0.305  26.916  39.957  1.00 23.50           C  
ATOM    737  C   GLN A  92      -0.137  25.627  38.995  1.00 20.70           C  
ATOM    738  O   GLN A  92       0.578  24.601  39.164  1.00 30.80           O  
ATOM    739  CB  GLN A  92       0.740  27.893  39.658  1.00 21.50           C  
ATOM    740  CG  GLN A  92       0.345  29.137  40.602  1.00 27.30           C  
ATOM    741  CD  GLN A  92       1.272  30.183  40.079  1.00 43.00           C  
ATOM    742  OE1 GLN A  92       2.501  29.996  40.434  1.00 32.80           O  
ATOM    743  NE2 GLN A  92       0.895  30.998  39.061  1.00 39.40           N  
ATOM    744  N   GLU A  93      -1.096  25.546  38.108  1.00 20.00           N  
ATOM    745  CA  GLU A  93      -1.132  24.501  37.006  1.00 25.80           C  
ATOM    746  C   GLU A  93      -0.165  24.843  35.961  1.00 27.70           C  
ATOM    747  O   GLU A  93       0.129  26.051  35.709  1.00 18.90           O  
ATOM    748  CB  GLU A  93      -2.526  24.401  36.568  1.00 33.50           C  
ATOM    749  CG  GLU A  93      -3.633  23.480  37.193  1.00 44.90           C  
ATOM    750  CD  GLU A  93      -4.969  24.103  36.680  1.00 93.30           C  
ATOM    751  OE1 GLU A  93      -5.001  25.316  37.277  1.00117.50           O  
ATOM    752  OE2 GLU A  93      -5.792  23.623  35.821  1.00127.60           O  
ATOM    753  N   LEU A  94       0.507  23.941  35.326  1.00 19.00           N  
ATOM    754  CA  LEU A  94       1.444  24.196  34.270  1.00 17.60           C  
ATOM    755  C   LEU A  94       0.722  23.953  32.804  1.00 20.70           C  
ATOM    756  O   LEU A  94       0.097  23.007  32.487  1.00 17.30           O  
ATOM    757  CB  LEU A  94       2.486  23.076  34.383  1.00 19.60           C  
ATOM    758  CG  LEU A  94       3.694  23.001  33.692  1.00 16.70           C  
ATOM    759  CD1 LEU A  94       4.459  24.426  33.878  1.00 15.10           C  
ATOM    760  CD2 LEU A  94       4.685  21.856  33.841  1.00 19.00           C  
ATOM    761  N   VAL A  95       0.780  25.036  32.076  1.00 15.20           N  
ATOM    762  CA  VAL A  95       0.262  25.161  30.741  1.00 14.00           C  
ATOM    763  C   VAL A  95       1.527  25.559  29.714  1.00 17.10           C  
ATOM    764  O   VAL A  95       2.185  26.511  29.882  1.00 15.10           O  
ATOM    765  CB  VAL A  95      -0.755  26.337  30.647  1.00 16.90           C  
ATOM    766  CG1 VAL A  95      -1.401  26.138  29.247  1.00 18.60           C  
ATOM    767  CG2 VAL A  95      -1.811  26.075  31.684  1.00 22.70           C  
ATOM    768  N   ILE A  96       1.613  24.576  28.752  1.00  9.20           N  
ATOM    769  CA  ILE A  96       2.648  24.688  27.659  1.00  9.80           C  
ATOM    770  C   ILE A  96       1.854  25.341  26.483  1.00 11.20           C  
ATOM    771  O   ILE A  96       0.880  24.800  26.100  1.00 11.80           O  
ATOM    772  CB  ILE A  96       3.205  23.263  27.472  1.00  8.40           C  
ATOM    773  CG1 ILE A  96       3.593  22.354  28.714  1.00 12.20           C  
ATOM    774  CG2 ILE A  96       4.369  23.561  26.417  1.00  8.50           C  
ATOM    775  CD1 ILE A  96       4.624  23.169  29.433  1.00 11.40           C  
ATOM    776  N   ALA A  97       2.339  26.555  26.156  1.00 10.00           N  
ATOM    777  CA  ALA A  97       1.635  27.351  25.138  1.00  8.10           C  
ATOM    778  C   ALA A  97       2.436  27.420  23.737  1.00 13.20           C  
ATOM    779  O   ALA A  97       1.865  28.198  22.981  1.00 14.10           O  
ATOM    780  CB  ALA A  97       1.373  28.714  25.838  1.00 10.60           C  
ATOM    781  N   GLY A  98       3.482  26.654  23.569  1.00 12.00           N  
ATOM    782  CA  GLY A  98       4.161  26.660  22.336  1.00 14.70           C  
ATOM    783  C   GLY A  98       5.436  27.364  22.215  1.00 14.70           C  
ATOM    784  O   GLY A  98       5.774  27.924  23.168  1.00 13.30           O  
ATOM    785  N   GLY A  99       6.036  27.382  20.936  1.00  9.10           N  
ATOM    786  CA  GLY A  99       5.487  26.816  19.750  1.00 12.10           C  
ATOM    787  C   GLY A  99       5.925  25.497  19.675  1.00 12.90           C  
ATOM    788  O   GLY A  99       6.036  24.669  20.544  1.00 11.90           O  
ATOM    789  N   ALA A 100       6.097  24.961  18.405  1.00 11.60           N  
ATOM    790  CA  ALA A 100       6.381  23.586  18.032  1.00 14.10           C  
ATOM    791  C   ALA A 100       7.624  22.877  18.732  1.00 12.00           C  
ATOM    792  O   ALA A 100       7.509  21.744  19.274  1.00 14.60           O  
ATOM    793  CB  ALA A 100       6.514  23.368  16.510  1.00 15.10           C  
ATOM    794  N   GLN A 101       8.713  23.692  18.816  1.00 13.40           N  
ATOM    795  CA  GLN A 101       9.924  23.076  19.442  1.00 14.60           C  
ATOM    796  C   GLN A 101       9.579  22.839  20.898  1.00 10.90           C  
ATOM    797  O   GLN A 101       9.999  21.887  21.524  1.00 15.70           O  
ATOM    798  CB  GLN A 101      11.027  24.103  19.554  1.00 13.70           C  
ATOM    799  CG  GLN A 101      11.505  24.034  18.134  1.00 13.70           C  
ATOM    800  CD  GLN A 101      12.823  24.775  18.041  1.00 28.30           C  
ATOM    801  OE1 GLN A 101      13.118  25.459  17.117  1.00 24.30           O  
ATOM    802  NE2 GLN A 101      13.686  24.787  18.965  1.00 19.50           N  
ATOM    803  N   ILE A 102       8.832  23.785  21.552  1.00 13.10           N  
ATOM    804  CA  ILE A 102       8.490  23.443  22.999  1.00 11.10           C  
ATOM    805  C   ILE A 102       7.459  22.429  23.214  1.00 12.80           C  
ATOM    806  O   ILE A 102       7.614  21.663  24.185  1.00 12.50           O  
ATOM    807  CB  ILE A 102       8.070  24.856  23.672  1.00 16.00           C  
ATOM    808  CG1 ILE A 102       9.097  25.665  24.363  1.00 18.60           C  
ATOM    809  CG2 ILE A 102       7.067  24.937  24.811  1.00 12.80           C  
ATOM    810  CD1 ILE A 102      10.481  25.596  23.709  1.00 15.50           C  
ATOM    811  N   PHE A 103       6.489  22.391  22.280  1.00 12.40           N  
ATOM    812  CA  PHE A 103       5.573  21.215  22.402  1.00 13.50           C  
ATOM    813  C   PHE A 103       6.313  19.883  22.327  1.00 14.60           C  
ATOM    814  O   PHE A 103       6.054  18.888  22.990  1.00 11.70           O  
ATOM    815  CB  PHE A 103       4.427  21.296  21.365  1.00 11.70           C  
ATOM    816  CG  PHE A 103       3.381  22.447  21.533  1.00 11.40           C  
ATOM    817  CD1 PHE A 103       2.849  22.522  22.878  1.00 12.70           C  
ATOM    818  CD2 PHE A 103       3.061  23.287  20.469  1.00 13.60           C  
ATOM    819  CE1 PHE A 103       1.811  23.462  22.971  1.00 11.60           C  
ATOM    820  CE2 PHE A 103       2.030  24.227  20.628  1.00 15.40           C  
ATOM    821  CZ  PHE A 103       1.538  24.358  21.982  1.00 11.70           C  
ATOM    822  N   THR A 104       7.362  19.809  21.375  1.00 13.50           N  
ATOM    823  CA  THR A 104       8.181  18.514  21.272  1.00 11.60           C  
ATOM    824  C   THR A 104       8.936  18.253  22.579  1.00 12.80           C  
ATOM    825  O   THR A 104       8.839  17.139  23.046  1.00 18.60           O  
ATOM    826  CB  THR A 104       9.259  18.950  20.273  1.00 11.60           C  
ATOM    827  OG1 THR A 104       8.623  19.056  18.909  1.00 16.80           O  
ATOM    828  CG2 THR A 104      10.204  17.674  19.993  1.00 16.00           C  
ATOM    829  N   ALA A 105       9.471  19.342  23.177  1.00 13.00           N  
ATOM    830  CA  ALA A 105      10.276  19.130  24.456  1.00 14.20           C  
ATOM    831  C   ALA A 105       9.248  18.695  25.362  1.00 16.60           C  
ATOM    832  O   ALA A 105       9.741  17.792  26.333  1.00 16.80           O  
ATOM    833  CB  ALA A 105      10.772  20.587  24.839  1.00 15.30           C  
ATOM    834  N   PHE A 106       7.969  18.856  25.670  1.00 16.40           N  
ATOM    835  CA  PHE A 106       7.100  18.359  26.819  1.00 17.60           C  
ATOM    836  C   PHE A 106       6.223  17.288  26.202  1.00 19.80           C  
ATOM    837  O   PHE A 106       5.321  16.896  26.884  1.00 15.10           O  
ATOM    838  CB  PHE A 106       6.223  19.616  27.342  1.00 16.30           C  
ATOM    839  CG  PHE A 106       7.096  20.543  27.958  1.00 14.10           C  
ATOM    840  CD1 PHE A 106       7.793  21.663  27.435  1.00 13.10           C  
ATOM    841  CD2 PHE A 106       7.315  20.325  29.368  1.00 14.30           C  
ATOM    842  CE1 PHE A 106       8.666  22.566  28.070  1.00 21.10           C  
ATOM    843  CE2 PHE A 106       8.034  21.246  30.152  1.00 16.00           C  
ATOM    844  CZ  PHE A 106       8.756  22.248  29.545  1.00 12.90           C  
ATOM    845  N   LYS A 107       6.414  16.685  24.998  1.00 16.60           N  
ATOM    846  CA  LYS A 107       5.418  15.720  24.316  1.00 14.80           C  
ATOM    847  C   LYS A 107       5.253  14.550  25.362  1.00 23.50           C  
ATOM    848  O   LYS A 107       4.128  14.083  25.362  1.00 24.60           O  
ATOM    849  CB  LYS A 107       6.227  15.166  22.990  1.00 21.30           C  
ATOM    850  CG  LYS A 107       5.461  14.376  22.075  1.00 56.20           C  
ATOM    851  CD  LYS A 107       5.860  13.324  20.926  1.00 81.10           C  
ATOM    852  CE  LYS A 107       4.365  12.714  20.469  1.00 42.00           C  
ATOM    853  NZ  LYS A 107       4.922  11.389  20.011  1.00 87.30           N  
ATOM    854  N   ASP A 108       6.051  14.177  26.305  1.00 22.00           N  
ATOM    855  CA  ASP A 108       5.709  13.013  27.211  1.00 20.70           C  
ATOM    856  C   ASP A 108       5.095  13.330  28.537  1.00 19.40           C  
ATOM    857  O   ASP A 108       4.764  12.310  29.163  1.00 26.60           O  
ATOM    858  CB  ASP A 108       7.010  12.079  27.295  1.00 24.00           C  
ATOM    859  CG  ASP A 108       7.797  11.513  25.857  1.00 27.50           C  
ATOM    860  OD1 ASP A 108       6.920  10.990  24.942  1.00 38.00           O  
ATOM    861  OD2 ASP A 108       9.148  11.737  26.100  1.00 61.70           O  
ATOM    862  N   ASP A 109       4.962  14.581  28.696  1.00 16.00           N  
ATOM    863  CA  ASP A 109       4.463  14.774  30.078  1.00 18.30           C  
ATOM    864  C   ASP A 109       3.176  15.471  29.882  1.00 26.50           C  
ATOM    865  O   ASP A 109       2.594  15.857  30.890  1.00 25.00           O  
ATOM    866  CB  ASP A 109       5.479  15.988  30.442  1.00 19.00           C  
ATOM    867  CG  ASP A 109       6.945  15.253  30.909  1.00 22.20           C  
ATOM    868  OD1 ASP A 109       6.942  14.401  31.908  1.00 50.60           O  
ATOM    869  OD2 ASP A 109       7.829  15.788  30.012  1.00 36.70           O  
ATOM    870  N   VAL A 110       2.479  15.608  28.724  1.00 17.90           N  
ATOM    871  CA  VAL A 110       1.157  16.367  28.714  1.00 19.40           C  
ATOM    872  C   VAL A 110       0.111  15.340  29.023  1.00 16.70           C  
ATOM    873  O   VAL A 110      -0.126  14.145  28.733  1.00 16.50           O  
ATOM    874  CB  VAL A 110       0.895  16.896  27.258  1.00 12.30           C  
ATOM    875  CG1 VAL A 110       1.010  15.764  26.230  1.00 18.30           C  
ATOM    876  CG2 VAL A 110      -0.446  17.587  27.118  1.00  8.20           C  
ATOM    877  N   ASP A 111      -0.884  15.795  29.835  1.00 11.00           N  
ATOM    878  CA  ASP A 111      -2.149  14.998  30.264  1.00 14.50           C  
ATOM    879  C   ASP A 111      -3.428  15.645  29.657  1.00 11.30           C  
ATOM    880  O   ASP A 111      -4.506  14.961  29.657  1.00 12.60           O  
ATOM    881  CB  ASP A 111      -2.138  14.569  31.759  1.00 27.60           C  
ATOM    882  CG  ASP A 111      -1.480  15.633  32.720  1.00 28.30           C  
ATOM    883  OD1 ASP A 111      -2.605  16.398  32.487  1.00 39.90           O  
ATOM    884  OD2 ASP A 111      -0.334  15.315  33.094  1.00 42.50           O  
ATOM    885  N   THR A 112      -3.442  16.902  29.284  1.00  8.70           N  
ATOM    886  CA  THR A 112      -4.689  17.494  28.752  1.00  9.00           C  
ATOM    887  C   THR A 112      -4.387  18.340  27.519  1.00 10.70           C  
ATOM    888  O   THR A 112      -3.320  19.056  27.547  1.00 12.20           O  
ATOM    889  CB  THR A 112      -5.048  18.576  29.900  1.00 12.80           C  
ATOM    890  OG1 THR A 112      -5.278  17.805  31.152  1.00 16.10           O  
ATOM    891  CG2 THR A 112      -6.435  19.311  29.555  1.00 10.00           C  
ATOM    892  N   LEU A 113      -5.264  18.253  26.576  1.00 10.70           N  
ATOM    893  CA  LEU A 113      -5.066  19.105  25.362  1.00 14.50           C  
ATOM    894  C   LEU A 113      -6.137  20.201  25.343  1.00 13.50           C  
ATOM    895  O   LEU A 113      -7.333  19.697  25.250  1.00 12.10           O  
ATOM    896  CB  LEU A 113      -5.088  18.122  24.111  1.00  8.30           C  
ATOM    897  CG  LEU A 113      -4.222  16.821  24.260  1.00  8.70           C  
ATOM    898  CD1 LEU A 113      -4.480  15.925  22.999  1.00 12.10           C  
ATOM    899  CD2 LEU A 113      -2.741  17.257  24.325  1.00  8.40           C  
ATOM    900  N   LEU A 114      -5.785  21.433  25.269  1.00 12.40           N  
ATOM    901  CA  LEU A 114      -6.740  22.566  25.129  1.00 11.10           C  
ATOM    902  C   LEU A 114      -6.467  23.026  23.644  1.00 11.30           C  
ATOM    903  O   LEU A 114      -5.537  23.792  23.448  1.00 11.40           O  
ATOM    904  CB  LEU A 114      -6.521  23.679  26.165  1.00  8.50           C  
ATOM    905  CG  LEU A 114      -6.554  22.902  27.556  1.00 15.30           C  
ATOM    906  CD1 LEU A 114      -6.022  23.984  28.453  1.00 16.40           C  
ATOM    907  CD2 LEU A 114      -7.933  22.553  27.967  1.00 14.90           C  
ATOM    908  N   VAL A 115      -7.333  22.497  22.710  1.00 13.50           N  
ATOM    909  CA  VAL A 115      -7.085  22.790  21.272  1.00 14.30           C  
ATOM    910  C   VAL A 115      -8.181  23.679  20.730  1.00 14.00           C  
ATOM    911  O   VAL A 115      -9.306  23.362  21.011  1.00 14.30           O  
ATOM    912  CB  VAL A 115      -6.812  21.495  20.441  1.00 15.40           C  
ATOM    913  CG1 VAL A 115      -7.858  20.543  20.553  1.00 15.80           C  
ATOM    914  CG2 VAL A 115      -6.608  21.887  18.965  1.00 11.60           C  
ATOM    915  N   THR A 116      -7.923  24.737  19.965  1.00 11.10           N  
ATOM    916  CA  THR A 116      -8.950  25.484  19.264  1.00 11.00           C  
ATOM    917  C   THR A 116      -8.702  25.005  17.770  1.00 12.00           C  
ATOM    918  O   THR A 116      -7.610  25.167  17.266  1.00 14.40           O  
ATOM    919  CB  THR A 116      -8.666  26.947  19.227  1.00 12.60           C  
ATOM    920  OG1 THR A 116      -8.537  27.445  20.628  1.00 12.10           O  
ATOM    921  CG2 THR A 116      -9.827  27.874  18.601  1.00 11.70           C  
ATOM    922  N   ARG A 117      -9.698  24.489  17.210  1.00  8.90           N  
ATOM    923  CA  ARG A 117      -9.705  23.991  15.791  1.00 15.60           C  
ATOM    924  C   ARG A 117     -10.427  25.055  14.857  1.00 15.40           C  
ATOM    925  O   ARG A 117     -11.652  25.123  15.090  1.00 12.90           O  
ATOM    926  CB  ARG A 117     -10.369  22.640  15.679  1.00 19.10           C  
ATOM    927  CG  ARG A 117      -9.669  21.476  15.735  1.00 34.60           C  
ATOM    928  CD  ARG A 117     -10.538  20.157  15.837  1.00 20.50           C  
ATOM    929  NE  ARG A 117      -9.690  19.137  16.556  1.00 22.00           N  
ATOM    930  CZ  ARG A 117      -8.824  18.384  16.668  1.00 21.40           C  
ATOM    931  NH1 ARG A 117      -8.285  18.471  15.296  1.00 18.30           N  
ATOM    932  NH2 ARG A 117      -7.987  17.456  17.191  1.00 34.20           N  
ATOM    933  N   LEU A 118      -9.672  25.602  13.867  1.00 13.40           N  
ATOM    934  CA  LEU A 118     -10.323  26.604  12.914  1.00 12.00           C  
ATOM    935  C   LEU A 118     -10.941  25.696  11.887  1.00 12.20           C  
ATOM    936  O   LEU A 118     -10.254  24.769  11.458  1.00 14.50           O  
ATOM    937  CB  LEU A 118      -9.295  27.700  12.522  1.00 10.20           C  
ATOM    938  CG  LEU A 118      -9.356  28.888  13.699  1.00 15.40           C  
ATOM    939  CD1 LEU A 118      -8.533  28.471  14.810  1.00 17.10           C  
ATOM    940  CD2 LEU A 118      -8.174  29.579  12.821  1.00 16.30           C  
ATOM    941  N   ALA A 119     -12.090  26.181  11.271  1.00 15.20           N  
ATOM    942  CA  ALA A 119     -12.705  25.316  10.160  1.00 15.60           C  
ATOM    943  C   ALA A 119     -11.868  25.596   8.918  1.00 15.20           C  
ATOM    944  O   ALA A 119     -11.817  24.650   8.040  1.00 18.90           O  
ATOM    945  CB  ALA A 119     -14.113  26.001  10.029  1.00 14.70           C  
ATOM    946  N   GLY A 120     -11.142  26.629   8.619  1.00 13.60           N  
ATOM    947  CA  GLY A 120     -10.484  26.872   7.433  1.00 16.30           C  
ATOM    948  C   GLY A 120      -9.083  26.449   7.396  1.00 15.10           C  
ATOM    949  O   GLY A 120      -8.462  25.833   8.245  1.00 20.10           O  
ATOM    950  N   SER A 121      -8.555  26.866   6.172  1.00 15.90           N  
ATOM    951  CA  SER A 121      -7.136  26.474   5.892  1.00 14.90           C  
ATOM    952  C   SER A 121      -6.306  27.662   5.575  1.00 14.30           C  
ATOM    953  O   SER A 121      -6.870  28.677   4.968  1.00 16.10           O  
ATOM    954  CB  SER A 121      -7.362  25.546   4.697  1.00 25.30           C  
ATOM    955  OG  SER A 121      -6.202  25.329   4.211  1.00 25.40           O  
ATOM    956  N   PHE A 122      -5.088  27.880   6.107  1.00 16.00           N  
ATOM    957  CA  PHE A 122      -4.315  29.106   6.107  1.00 14.50           C  
ATOM    958  C   PHE A 122      -2.950  28.720   5.565  1.00 16.20           C  
ATOM    959  O   PHE A 122      -2.619  27.513   5.537  1.00 20.00           O  
ATOM    960  CB  PHE A 122      -4.107  29.729   7.414  1.00 17.40           C  
ATOM    961  CG  PHE A 122      -5.487  30.289   7.853  1.00 12.20           C  
ATOM    962  CD1 PHE A 122      -6.370  29.380   8.591  1.00 16.10           C  
ATOM    963  CD2 PHE A 122      -5.767  31.633   7.564  1.00 18.10           C  
ATOM    964  CE1 PHE A 122      -7.664  29.915   8.908  1.00 21.70           C  
ATOM    965  CE2 PHE A 122      -6.981  32.031   8.021  1.00 18.80           C  
ATOM    966  CZ  PHE A 122      -7.930  31.235   8.600  1.00 16.40           C  
ATOM    967  N   GLU A 123      -2.156  29.585   5.080  1.00 19.00           N  
ATOM    968  CA  GLU A 123      -0.834  29.249   4.613  1.00 19.10           C  
ATOM    969  C   GLU A 123       0.068  29.579   5.668  1.00 16.60           C  
ATOM    970  O   GLU A 123      -0.025  30.500   6.593  1.00 14.00           O  
ATOM    971  CB  GLU A 123      -0.798  30.407   3.408  1.00 23.00           C  
ATOM    972  CG  GLU A 123       0.478  30.351   2.465  1.00 90.00           C  
ATOM    973  CD  GLU A 123       0.420  31.160   1.167  1.00 98.20           C  
ATOM    974  OE1 GLU A 123      -0.848  31.340   0.710  1.00 65.80           O  
ATOM    975  OE2 GLU A 123       1.692  31.409   0.971  1.00101.80           O  
ATOM    976  N   GLY A 124       1.096  28.832   5.958  1.00 14.30           N  
ATOM    977  CA  GLY A 124       2.152  29.081   6.882  1.00 12.50           C  
ATOM    978  C   GLY A 124       3.244  27.974   6.723  1.00 16.00           C  
ATOM    979  O   GLY A 124       3.338  27.077   5.864  1.00 18.50           O  
ATOM    980  N   ASP A 125       4.017  27.918   7.835  1.00 14.10           N  
ATOM    981  CA  ASP A 125       5.249  27.065   7.872  1.00 12.90           C  
ATOM    982  C   ASP A 125       5.451  26.256   9.170  1.00 22.40           C  
ATOM    983  O   ASP A 125       6.460  25.565   9.170  1.00 17.60           O  
ATOM    984  CB  ASP A 125       6.316  28.117   7.638  1.00 14.10           C  
ATOM    985  CG  ASP A 125       6.550  29.256   8.526  1.00 16.80           C  
ATOM    986  OD1 ASP A 125       6.252  29.025   9.861  1.00 17.50           O  
ATOM    987  OD2 ASP A 125       7.075  30.376   8.395  1.00 19.90           O  
ATOM    988  N   THR A 126       4.538  26.306  10.122  1.00 15.30           N  
ATOM    989  CA  THR A 126       4.807  25.565  11.402  1.00 12.60           C  
ATOM    990  C   THR A 126       3.431  24.862  11.654  1.00 13.50           C  
ATOM    991  O   THR A 126       2.422  25.490  11.570  1.00 12.60           O  
ATOM    992  CB  THR A 126       5.163  26.592  12.606  1.00 15.40           C  
ATOM    993  OG1 THR A 126       6.259  27.245  11.981  1.00 17.70           O  
ATOM    994  CG2 THR A 126       5.508  25.833  13.858  1.00 13.50           C  
ATOM    995  N   LYS A 127       3.507  23.536  11.962  1.00 12.90           N  
ATOM    996  CA  LYS A 127       2.332  22.684  12.233  1.00 10.70           C  
ATOM    997  C   LYS A 127       2.598  22.186  13.727  1.00 12.10           C  
ATOM    998  O   LYS A 127       3.686  22.142  14.259  1.00 13.10           O  
ATOM    999  CB  LYS A 127       2.156  21.570  11.243  1.00  9.90           C  
ATOM   1000  CG  LYS A 127       1.937  22.099   9.824  1.00 18.60           C  
ATOM   1001  CD  LYS A 127       1.344  20.736   9.366  1.00 27.40           C  
ATOM   1002  CE  LYS A 127       1.671  20.605   7.872  1.00 65.40           C  
ATOM   1003  NZ  LYS A 127       1.049  19.280   7.330  1.00 54.10           N  
ATOM   1004  N   MET A 128       1.416  21.844  14.203  1.00 14.40           N  
ATOM   1005  CA  MET A 128       1.383  21.153  15.557  1.00  9.30           C  
ATOM   1006  C   MET A 128       2.102  19.734  15.314  1.00  9.20           C  
ATOM   1007  O   MET A 128       2.073  18.987  14.287  1.00 13.40           O  
ATOM   1008  CB  MET A 128      -0.047  21.016  16.127  1.00 12.40           C  
ATOM   1009  CG  MET A 128      -0.068  20.207  17.490  1.00  9.70           C  
ATOM   1010  SD  MET A 128       0.870  21.284  18.611  1.00 11.60           S  
ATOM   1011  CE  MET A 128       0.553  20.400  20.142  1.00 11.40           C  
ATOM   1012  N   ILE A 129       2.817  19.379  16.426  1.00 12.10           N  
ATOM   1013  CA  ILE A 129       3.507  18.135  16.594  1.00 10.70           C  
ATOM   1014  C   ILE A 129       2.325  17.070  16.650  1.00  9.40           C  
ATOM   1015  O   ILE A 129       1.247  17.070  17.004  1.00 14.10           O  
ATOM   1016  CB  ILE A 129       4.495  18.016  17.826  1.00 12.10           C  
ATOM   1017  CG1 ILE A 129       3.582  18.016  19.059  1.00 13.90           C  
ATOM   1018  CG2 ILE A 129       5.533  19.118  17.677  1.00 11.60           C  
ATOM   1019  CD1 ILE A 129       4.301  17.494  20.310  1.00 18.90           C  
ATOM   1020  N   PRO A 130       3.004  15.869  15.959  1.00 14.30           N  
ATOM   1021  CA  PRO A 130       2.055  14.712  15.987  1.00 11.20           C  
ATOM   1022  C   PRO A 130       1.667  14.102  17.331  1.00 14.20           C  
ATOM   1023  O   PRO A 130       2.623  14.102  18.228  1.00 20.90           O  
ATOM   1024  CB  PRO A 130       2.616  13.579  15.118  1.00 15.10           C  
ATOM   1025  CG  PRO A 130       3.995  13.878  14.903  1.00 15.30           C  
ATOM   1026  CD  PRO A 130       4.319  15.297  14.997  1.00 10.30           C  
ATOM   1027  N   LEU A 131       0.413  13.834  17.658  1.00 16.70           N  
ATOM   1028  CA  LEU A 131       0.230  13.280  19.068  1.00 18.60           C  
ATOM   1029  C   LEU A 131      -0.632  12.048  18.797  1.00 17.90           C  
ATOM   1030  O   LEU A 131      -1.240  11.830  17.630  1.00 16.90           O  
ATOM   1031  CB  LEU A 131      -0.672  14.307  19.862  1.00 17.10           C  
ATOM   1032  CG  LEU A 131      -0.201  15.795  20.170  1.00 20.70           C  
ATOM   1033  CD1 LEU A 131      -1.505  16.436  19.965  1.00 23.60           C  
ATOM   1034  CD2 LEU A 131       0.862  15.533  21.151  1.00 20.40           C  
ATOM   1035  N   ASN A 132      -0.589  11.177  19.881  1.00 21.00           N  
ATOM   1036  CA  ASN A 132      -1.491   9.864  19.815  1.00 19.10           C  
ATOM   1037  C   ASN A 132      -2.871  10.312  20.170  1.00 17.20           C  
ATOM   1038  O   ASN A 132      -3.029  10.138  21.487  1.00 18.40           O  
ATOM   1039  CB  ASN A 132      -0.668   8.825  20.553  1.00 22.70           C  
ATOM   1040  CG  ASN A 132      -1.602   7.493  20.291  1.00 22.00           C  
ATOM   1041  OD1 ASN A 132      -2.529   7.281  19.432  1.00 30.50           O  
ATOM   1042  ND2 ASN A 132      -0.913   6.410  20.870  1.00 38.50           N  
ATOM   1043  N   TRP A 133      -3.938  10.766  19.470  1.00 16.80           N  
ATOM   1044  CA  TRP A 133      -5.307  11.208  19.731  1.00 22.00           C  
ATOM   1045  C   TRP A 133      -5.986  10.032  20.432  1.00 25.60           C  
ATOM   1046  O   TRP A 133      -6.927  10.256  21.123  1.00 21.30           O  
ATOM   1047  CB  TRP A 133      -6.000  11.737  18.517  1.00 24.60           C  
ATOM   1048  CG  TRP A 133      -5.343  13.100  18.190  1.00 27.50           C  
ATOM   1049  CD1 TRP A 133      -4.268  13.256  17.369  1.00 19.50           C  
ATOM   1050  CD2 TRP A 133      -5.508  14.295  18.900  1.00 18.40           C  
ATOM   1051  NE1 TRP A 133      -3.870  14.519  17.257  1.00 19.90           N  
ATOM   1052  CE2 TRP A 133      -4.682  15.253  18.088  1.00 23.00           C  
ATOM   1053  CE3 TRP A 133      -6.406  14.842  19.797  1.00 15.80           C  
ATOM   1054  CZ2 TRP A 133      -4.613  16.616  18.359  1.00 23.60           C  
ATOM   1055  CZ3 TRP A 133      -6.392  16.236  20.095  1.00 16.90           C  
ATOM   1056  CH2 TRP A 133      -5.483  17.077  19.292  1.00 16.90           C  
ATOM   1057  N   ASP A 134      -5.641   8.874  20.049  1.00 20.60           N  
ATOM   1058  CA  ASP A 134      -6.306   7.586  20.432  1.00 30.00           C  
ATOM   1059  C   ASP A 134      -6.043   7.455  21.935  1.00 22.10           C  
ATOM   1060  O   ASP A 134      -6.848   6.746  22.617  1.00 30.90           O  
ATOM   1061  CB  ASP A 134      -5.964   6.236  19.479  1.00 28.70           C  
ATOM   1062  CG  ASP A 134      -6.762   6.323  18.153  1.00 34.80           C  
ATOM   1063  OD1 ASP A 134      -8.131   6.690  17.920  1.00 63.10           O  
ATOM   1064  OD2 ASP A 134      -5.756   6.037  17.182  1.00 61.80           O  
ATOM   1065  N   ASP A 135      -5.070   7.960  22.626  1.00 19.30           N  
ATOM   1066  CA  ASP A 135      -4.721   7.941  24.036  1.00 16.20           C  
ATOM   1067  C   ASP A 135      -5.548   9.123  24.951  1.00 10.10           C  
ATOM   1068  O   ASP A 135      -5.332   9.111  26.146  1.00 17.90           O  
ATOM   1069  CB  ASP A 135      -3.309   8.184  24.531  1.00 19.50           C  
ATOM   1070  CG  ASP A 135      -2.432   6.827  24.223  1.00 32.00           C  
ATOM   1071  OD1 ASP A 135      -3.086   5.757  23.831  1.00 45.60           O  
ATOM   1072  OD2 ASP A 135      -1.175   7.238  24.484  1.00 49.30           O  
ATOM   1073  N   PHE A 136      -6.421   9.777  24.223  1.00 15.50           N  
ATOM   1074  CA  PHE A 136      -7.082  10.884  24.914  1.00 13.00           C  
ATOM   1075  C   PHE A 136      -8.548  10.735  24.624  1.00 20.00           C  
ATOM   1076  O   PHE A 136      -9.000  10.163  23.625  1.00 19.20           O  
ATOM   1077  CB  PHE A 136      -6.672  12.341  24.297  1.00 10.10           C  
ATOM   1078  CG  PHE A 136      -5.300  12.602  24.662  1.00 13.70           C  
ATOM   1079  CD1 PHE A 136      -4.136  12.129  24.017  1.00 13.50           C  
ATOM   1080  CD2 PHE A 136      -5.019  13.386  25.745  1.00 12.10           C  
ATOM   1081  CE1 PHE A 136      -2.799  12.366  24.354  1.00 11.10           C  
ATOM   1082  CE2 PHE A 136      -3.701  13.766  26.184  1.00 16.10           C  
ATOM   1083  CZ  PHE A 136      -2.655  13.212  25.474  1.00 16.20           C  
ATOM   1084  N   THR A 137      -9.399  11.326  25.483  1.00 15.70           N  
ATOM   1085  CA  THR A 137     -10.858  11.364  25.194  1.00 13.30           C  
ATOM   1086  C   THR A 137     -11.379  12.801  24.904  1.00 10.10           C  
ATOM   1087  O   THR A 137     -10.808  13.604  25.820  1.00 14.10           O  
ATOM   1088  CB  THR A 137     -11.728  10.841  26.492  1.00 17.80           C  
ATOM   1089  OG1 THR A 137     -11.390   9.522  26.417  1.00 21.50           O  
ATOM   1090  CG2 THR A 137     -13.265  10.940  26.380  1.00 16.60           C  
ATOM   1091  N   LYS A 138     -12.245  13.318  23.989  1.00 15.80           N  
ATOM   1092  CA  LYS A 138     -12.647  14.637  23.971  1.00 15.70           C  
ATOM   1093  C   LYS A 138     -13.704  14.774  24.998  1.00 12.40           C  
ATOM   1094  O   LYS A 138     -14.879  14.295  24.811  1.00 18.50           O  
ATOM   1095  CB  LYS A 138     -13.193  14.861  22.514  1.00 15.40           C  
ATOM   1096  CG  LYS A 138     -13.431  16.392  22.299  1.00 14.50           C  
ATOM   1097  CD  LYS A 138     -13.901  16.647  20.898  1.00 18.80           C  
ATOM   1098  CE  LYS A 138     -15.198  16.019  20.469  1.00 28.30           C  
ATOM   1099  NZ  LYS A 138     -15.040  16.019  18.863  1.00 32.10           N  
ATOM   1100  N   VAL A 139     -13.488  15.471  26.053  1.00 11.90           N  
ATOM   1101  CA  VAL A 139     -14.469  15.676  27.118  1.00 12.30           C  
ATOM   1102  C   VAL A 139     -15.432  16.734  26.809  1.00 14.00           C  
ATOM   1103  O   VAL A 139     -16.607  16.765  27.276  1.00 14.40           O  
ATOM   1104  CB  VAL A 139     -13.596  15.956  28.500  1.00 17.70           C  
ATOM   1105  CG1 VAL A 139     -14.419  16.361  29.611  1.00 18.00           C  
ATOM   1106  CG2 VAL A 139     -13.086  14.525  28.957  1.00 18.30           C  
ATOM   1107  N   SER A 140     -14.986  17.879  26.174  1.00 11.10           N  
ATOM   1108  CA  SER A 140     -15.834  19.074  26.044  1.00 11.90           C  
ATOM   1109  C   SER A 140     -15.533  19.535  24.634  1.00 15.40           C  
ATOM   1110  O   SER A 140     -14.390  19.547  24.167  1.00 13.80           O  
ATOM   1111  CB  SER A 140     -14.968  20.263  26.903  1.00 17.20           C  
ATOM   1112  OG  SER A 140     -16.143  20.817  26.959  1.00 26.10           O  
ATOM   1113  N   SER A 141     -16.614  20.101  24.036  1.00 12.70           N  
ATOM   1114  CA  SER A 141     -16.424  20.755  22.701  1.00 13.40           C  
ATOM   1115  C   SER A 141     -17.340  21.906  22.654  1.00 16.80           C  
ATOM   1116  O   SER A 141     -18.569  21.856  23.140  1.00 15.80           O  
ATOM   1117  CB  SER A 141     -16.919  19.622  21.758  1.00 23.50           C  
ATOM   1118  OG  SER A 141     -16.679  20.400  20.525  1.00 27.50           O  
ATOM   1119  N   ARG A 142     -16.981  23.151  22.262  1.00 14.10           N  
ATOM   1120  CA  ARG A 142     -17.958  24.358  22.262  1.00 11.10           C  
ATOM   1121  C   ARG A 142     -17.519  24.943  20.786  1.00 17.00           C  
ATOM   1122  O   ARG A 142     -16.363  25.291  20.609  1.00 15.80           O  
ATOM   1123  CB  ARG A 142     -17.469  25.316  23.270  1.00 18.90           C  
ATOM   1124  CG  ARG A 142     -18.508  26.343  23.261  1.00 26.50           C  
ATOM   1125  CD  ARG A 142     -18.213  27.140  24.540  1.00 28.40           C  
ATOM   1126  NE  ARG A 142     -16.862  27.513  25.045  1.00 48.70           N  
ATOM   1127  CZ  ARG A 142     -16.650  28.951  24.522  1.00 44.10           C  
ATOM   1128  NH1 ARG A 142     -17.559  29.691  23.681  1.00 43.80           N  
ATOM   1129  NH2 ARG A 142     -15.425  29.330  25.035  1.00 35.50           N  
ATOM   1130  N   THR A 143     -18.468  25.217  19.955  1.00 17.80           N  
ATOM   1131  CA  THR A 143     -18.242  25.883  18.685  1.00 16.60           C  
ATOM   1132  C   THR A 143     -18.712  27.320  18.573  1.00 21.20           C  
ATOM   1133  O   THR A 143     -19.726  27.756  19.068  1.00 21.90           O  
ATOM   1134  CB  THR A 143     -18.982  25.210  17.453  1.00 25.40           C  
ATOM   1135  OG1 THR A 143     -18.479  23.804  17.509  1.00 20.90           O  
ATOM   1136  CG2 THR A 143     -18.597  25.739  16.024  1.00 20.40           C  
ATOM   1137  N   VAL A 144     -17.882  28.210  18.041  1.00 18.60           N  
ATOM   1138  CA  VAL A 144     -18.091  29.691  17.854  1.00 17.00           C  
ATOM   1139  C   VAL A 144     -18.026  29.977  16.248  1.00 21.70           C  
ATOM   1140  O   VAL A 144     -16.981  29.809  15.594  1.00 17.50           O  
ATOM   1141  CB  VAL A 144     -17.182  30.681  18.648  1.00 22.50           C  
ATOM   1142  CG1 VAL A 144     -17.487  32.168  18.489  1.00 15.80           C  
ATOM   1143  CG2 VAL A 144     -17.246  30.096  19.918  1.00 18.10           C  
ATOM   1144  N   GLU A 145     -19.165  30.594  15.865  1.00 16.70           N  
ATOM   1145  CA  GLU A 145     -19.169  30.824  14.399  1.00 18.00           C  
ATOM   1146  C   GLU A 145     -18.737  32.218  14.250  1.00 17.80           C  
ATOM   1147  O   GLU A 145     -18.676  33.070  15.081  1.00 19.30           O  
ATOM   1148  CB  GLU A 145     -20.688  30.855  13.848  1.00 21.30           C  
ATOM   1149  CG  GLU A 145     -21.306  29.249  13.428  1.00 29.90           C  
ATOM   1150  CD  GLU A 145     -22.884  29.654  13.129  1.00 92.30           C  
ATOM   1151  OE1 GLU A 145     -22.884  30.052  11.775  1.00103.80           O  
ATOM   1152  OE2 GLU A 145     -24.019  29.691  14.100  1.00 83.80           O  
ATOM   1153  N   ASP A 146     -17.915  32.398  13.167  1.00 10.30           N  
ATOM   1154  CA  ASP A 146     -17.343  33.761  12.849  1.00  8.60           C  
ATOM   1155  C   ASP A 146     -17.976  34.234  11.392  1.00 14.70           C  
ATOM   1156  O   ASP A 146     -18.296  33.294  10.617  1.00 16.70           O  
ATOM   1157  CB  ASP A 146     -15.852  33.581  12.700  1.00 10.20           C  
ATOM   1158  CG  ASP A 146     -15.162  34.875  12.830  1.00 12.10           C  
ATOM   1159  OD1 ASP A 146     -14.645  35.385  13.792  1.00 25.00           O  
ATOM   1160  OD2 ASP A 146     -15.015  35.566  11.663  1.00 16.00           O  
ATOM   1161  N   THR A 147     -18.105  35.566  11.056  1.00 17.70           N  
ATOM   1162  CA  THR A 147     -18.554  35.970   9.777  1.00 19.10           C  
ATOM   1163  C   THR A 147     -17.516  35.703   8.675  1.00 15.20           C  
ATOM   1164  O   THR A 147     -17.936  35.572   7.536  1.00 21.30           O  
ATOM   1165  CB  THR A 147     -18.852  37.520   9.852  1.00 15.90           C  
ATOM   1166  OG1 THR A 147     -17.800  38.186  10.440  1.00 18.90           O  
ATOM   1167  CG2 THR A 147     -20.168  37.582  10.804  1.00 16.00           C  
ATOM   1168  N   ASN A 148     -16.226  35.510   9.011  1.00 15.50           N  
ATOM   1169  CA  ASN A 148     -15.259  34.869   7.993  1.00 16.00           C  
ATOM   1170  C   ASN A 148     -15.443  33.319   8.544  1.00 17.70           C  
ATOM   1171  O   ASN A 148     -15.004  32.685   9.338  1.00 16.00           O  
ATOM   1172  CB  ASN A 148     -13.826  35.298   8.096  1.00 13.70           C  
ATOM   1173  CG  ASN A 148     -12.989  34.396   7.302  1.00  9.00           C  
ATOM   1174  OD1 ASN A 148     -13.132  33.462   6.611  1.00 15.30           O  
ATOM   1175  ND2 ASN A 148     -11.792  34.863   7.564  1.00 14.40           N  
ATOM   1176  N   PRO A 149     -16.068  32.647   7.349  1.00 14.60           N  
ATOM   1177  CA  PRO A 149     -16.212  31.228   7.788  1.00 12.70           C  
ATOM   1178  C   PRO A 149     -14.950  30.363   7.965  1.00 18.90           C  
ATOM   1179  O   PRO A 149     -15.080  29.218   8.656  1.00 17.50           O  
ATOM   1180  CB  PRO A 149     -17.113  30.351   6.789  1.00 13.40           C  
ATOM   1181  CG  PRO A 149     -16.657  31.116   5.706  1.00 30.00           C  
ATOM   1182  CD  PRO A 149     -16.747  32.691   5.790  1.00 19.60           C  
ATOM   1183  N   ALA A 150     -13.768  30.643   7.592  1.00 16.80           N  
ATOM   1184  CA  ALA A 150     -12.425  30.009   7.760  1.00 12.80           C  
ATOM   1185  C   ALA A 150     -12.123  30.071   9.263  1.00 12.80           C  
ATOM   1186  O   ALA A 150     -11.289  29.436   9.880  1.00 15.40           O  
ATOM   1187  CB  ALA A 150     -11.426  30.718   6.798  1.00 14.00           C  
ATOM   1188  N   LEU A 151     -12.708  31.073  10.057  1.00 11.10           N  
ATOM   1189  CA  LEU A 151     -12.461  31.564  11.383  1.00 18.00           C  
ATOM   1190  C   LEU A 151     -13.366  30.905  12.485  1.00 14.60           C  
ATOM   1191  O   LEU A 151     -13.276  31.098  13.671  1.00 19.70           O  
ATOM   1192  CB  LEU A 151     -12.216  33.021  11.626  1.00 10.70           C  
ATOM   1193  CG  LEU A 151     -10.926  33.612  10.935  1.00 10.90           C  
ATOM   1194  CD1 LEU A 151     -11.095  35.137  11.224  1.00 12.60           C  
ATOM   1195  CD2 LEU A 151      -9.683  32.790  11.448  1.00 13.50           C  
ATOM   1196  N   THR A 152     -14.473  30.295  11.999  1.00 11.20           N  
ATOM   1197  CA  THR A 152     -15.410  29.504  12.774  1.00 13.60           C  
ATOM   1198  C   THR A 152     -14.480  28.366  13.512  1.00 13.60           C  
ATOM   1199  O   THR A 152     -13.596  27.768  12.877  1.00 15.00           O  
ATOM   1200  CB  THR A 152     -16.531  28.783  11.906  1.00 14.60           C  
ATOM   1201  OG1 THR A 152     -17.408  29.816  11.495  1.00 16.10           O  
ATOM   1202  CG2 THR A 152     -17.304  27.731  12.802  1.00 13.50           C  
ATOM   1203  N   HIS A 153     -14.688  28.341  14.754  1.00 13.70           N  
ATOM   1204  CA  HIS A 153     -13.747  27.469  15.594  1.00 11.60           C  
ATOM   1205  C   HIS A 153     -14.437  26.698  16.678  1.00 17.80           C  
ATOM   1206  O   HIS A 153     -15.342  27.183  17.275  1.00 13.60           O  
ATOM   1207  CB  HIS A 153     -12.611  28.478  16.127  1.00 12.60           C  
ATOM   1208  CG  HIS A 153     -13.061  29.679  16.799  1.00 15.50           C  
ATOM   1209  ND1 HIS A 153     -13.650  30.811  16.155  1.00 11.60           N  
ATOM   1210  CD2 HIS A 153     -13.240  30.089  18.097  1.00 12.90           C  
ATOM   1211  CE1 HIS A 153     -13.984  31.676  17.098  1.00 20.30           C  
ATOM   1212  NE2 HIS A 153     -13.682  31.315  18.284  1.00 14.00           N  
ATOM   1213  N   THR A 154     -13.772  25.683  17.079  1.00 14.00           N  
ATOM   1214  CA  THR A 154     -14.340  24.787  18.097  1.00  8.70           C  
ATOM   1215  C   THR A 154     -13.226  24.713  19.227  1.00 11.60           C  
ATOM   1216  O   THR A 154     -12.076  24.302  18.937  1.00 15.20           O  
ATOM   1217  CB  THR A 154     -14.498  23.343  17.499  1.00 11.80           C  
ATOM   1218  OG1 THR A 154     -15.554  23.567  16.482  1.00 20.40           O  
ATOM   1219  CG2 THR A 154     -15.213  22.404  18.545  1.00 13.20           C  
ATOM   1220  N   TYR A 155     -13.635  24.999  20.450  1.00 12.90           N  
ATOM   1221  CA  TYR A 155     -12.723  24.787  21.673  1.00 11.00           C  
ATOM   1222  C   TYR A 155     -12.978  23.337  22.178  1.00 11.60           C  
ATOM   1223  O   TYR A 155     -14.088  22.970  22.477  1.00 12.40           O  
ATOM   1224  CB  TYR A 155     -13.050  25.814  22.663  1.00 11.40           C  
ATOM   1225  CG  TYR A 155     -12.942  27.308  22.280  1.00 10.60           C  
ATOM   1226  CD1 TYR A 155     -11.595  27.662  22.094  1.00 12.10           C  
ATOM   1227  CD2 TYR A 155     -14.027  28.142  22.000  1.00 13.80           C  
ATOM   1228  CE1 TYR A 155     -11.343  29.019  21.739  1.00 11.10           C  
ATOM   1229  CE2 TYR A 155     -13.808  29.442  21.795  1.00 10.90           C  
ATOM   1230  CZ  TYR A 155     -12.486  29.878  21.702  1.00 11.90           C  
ATOM   1231  OH  TYR A 155     -12.169  31.197  21.328  1.00 14.90           O  
ATOM   1232  N   GLU A 156     -11.907  22.516  22.178  1.00 11.40           N  
ATOM   1233  CA  GLU A 156     -11.986  21.147  22.654  1.00 11.30           C  
ATOM   1234  C   GLU A 156     -11.034  21.041  23.887  1.00 15.60           C  
ATOM   1235  O   GLU A 156      -9.974  21.682  23.943  1.00 12.40           O  
ATOM   1236  CB  GLU A 156     -11.584  20.176  21.543  1.00  9.30           C  
ATOM   1237  CG  GLU A 156     -12.435  20.481  20.198  1.00 16.60           C  
ATOM   1238  CD  GLU A 156     -11.843  19.529  19.171  1.00 18.70           C  
ATOM   1239  OE1 GLU A 156     -10.757  18.956  19.208  1.00 19.70           O  
ATOM   1240  OE2 GLU A 156     -12.662  19.280  18.256  1.00 24.70           O  
ATOM   1241  N   VAL A 157     -11.562  20.163  24.783  1.00 11.50           N  
ATOM   1242  CA  VAL A 157     -10.732  19.746  26.006  1.00  7.80           C  
ATOM   1243  C   VAL A 157     -10.484  18.222  25.894  1.00 10.30           C  
ATOM   1244  O   VAL A 157     -11.623  17.668  25.792  1.00 12.80           O  
ATOM   1245  CB  VAL A 157     -11.304  20.163  27.407  1.00  9.90           C  
ATOM   1246  CG1 VAL A 157     -10.405  19.529  28.481  1.00 13.60           C  
ATOM   1247  CG2 VAL A 157     -11.562  21.669  27.388  1.00 10.20           C  
ATOM   1248  N   TRP A 158      -9.270  17.774  25.848  1.00  9.90           N  
ATOM   1249  CA  TRP A 158      -9.112  16.392  25.745  1.00  8.90           C  
ATOM   1250  C   TRP A 158      -8.307  15.944  26.987  1.00 10.00           C  
ATOM   1251  O   TRP A 158      -7.405  16.672  27.332  1.00 13.10           O  
ATOM   1252  CB  TRP A 158      -8.239  15.851  24.550  1.00  8.10           C  
ATOM   1253  CG  TRP A 158      -8.950  16.212  23.242  1.00  9.80           C  
ATOM   1254  CD1 TRP A 158      -9.062  17.525  22.654  1.00 17.90           C  
ATOM   1255  CD2 TRP A 158      -9.349  15.259  22.243  1.00 12.90           C  
ATOM   1256  NE1 TRP A 158      -9.687  17.487  21.440  1.00 16.30           N  
ATOM   1257  CE2 TRP A 158      -9.748  16.149  21.235  1.00 12.10           C  
ATOM   1258  CE3 TRP A 158      -9.313  13.878  22.243  1.00 18.20           C  
ATOM   1259  CZ2 TRP A 158     -10.244  15.564  20.049  1.00 16.00           C  
ATOM   1260  CZ3 TRP A 158      -9.737  13.231  21.039  1.00 20.10           C  
ATOM   1261  CH2 TRP A 158     -10.308  14.108  19.937  1.00 18.70           C  
ATOM   1262  N   GLN A 159      -8.663  14.780  27.538  1.00 12.20           N  
ATOM   1263  CA  GLN A 159      -7.923  14.332  28.752  1.00 13.90           C  
ATOM   1264  C   GLN A 159      -7.506  12.888  28.416  1.00 13.30           C  
ATOM   1265  O   GLN A 159      -8.091  12.086  27.715  1.00 12.20           O  
ATOM   1266  CB  GLN A 159      -8.875  14.264  29.919  1.00 12.30           C  
ATOM   1267  CG  GLN A 159      -8.835  15.801  30.675  1.00 24.50           C  
ATOM   1268  CD  GLN A 159     -10.068  15.608  31.404  1.00 33.20           C  
ATOM   1269  OE1 GLN A 159     -10.635  14.587  31.973  1.00 42.20           O  
ATOM   1270  NE2 GLN A 159     -10.682  16.797  31.852  1.00 38.70           N  
ATOM   1271  N   LYS A 160      -6.266  12.583  28.882  1.00 10.80           N  
ATOM   1272  CA  LYS A 160      -5.469  11.351  28.677  1.00 10.00           C  
ATOM   1273  C   LYS A 160      -6.212  10.125  29.349  1.00 10.90           C  
ATOM   1274  O   LYS A 160      -6.740  10.343  30.479  1.00 15.30           O  
ATOM   1275  CB  LYS A 160      -4.024  11.476  29.265  1.00 13.50           C  
ATOM   1276  CG  LYS A 160      -3.032  10.505  28.677  1.00 17.80           C  
ATOM   1277  CD  LYS A 160      -1.664  10.698  29.377  1.00 28.60           C  
ATOM   1278  CE  LYS A 160      -0.776   9.646  28.612  1.00 50.40           C  
ATOM   1279  NZ  LYS A 160       0.384   9.391  29.517  1.00 76.60           N  
ATOM   1280  N   LYS A 161      -6.511   9.061  28.612  1.00 18.80           N  
ATOM   1281  CA  LYS A 161      -7.164   7.829  29.172  1.00 16.70           C  
ATOM   1282  C   LYS A 161      -6.406   7.151  30.349  1.00 25.90           C  
ATOM   1283  O   LYS A 161      -5.131   7.468  30.320  1.00 23.50           O  
ATOM   1284  CB  LYS A 161      -7.412   6.964  27.893  1.00 16.90           C  
ATOM   1285  CG  LYS A 161      -8.382   7.524  26.856  1.00 21.00           C  
ATOM   1286  CD  LYS A 161      -8.081   6.342  25.782  1.00 20.40           C  
ATOM   1287  CE  LYS A 161      -9.198   6.696  25.017  1.00 31.00           C  
ATOM   1288  NZ  LYS A 161      -9.777   6.541  23.653  1.00 49.50           N  
ATOM   1289  N   ALA A 162      -6.805   6.335  31.469  1.00 51.00           N  
ATOM   1290  CA  ALA A 162      -5.957   5.501  32.394  1.00 40.70           C  
ATOM   1291  C   ALA A 162      -5.005   4.487  31.460  1.00 97.90           C  
ATOM   1292  O   ALA A 162      -3.629   4.294  31.469  1.00 82.40           O  
ATOM   1293  CB  ALA A 162      -6.751   4.400  33.019  1.00 37.10           C  
ATOM   1294  OXT ALA A 162      -5.778   3.908  30.489  1.00 59.50           O  
TER    1295      ALA A 162                                                      
HETATM 1296  PA  NDP A 163       9.248  28.142  19.825  1.00 13.00           P  
HETATM 1297  O1A NDP A 163       8.957  26.741  20.217  1.00 11.70           O  
HETATM 1298  O2A NDP A 163       8.293  29.175  20.245  1.00 13.90           O  
HETATM 1299  O5B NDP A 163      10.754  28.695  20.207  1.00 16.00           O  
HETATM 1300  C5B NDP A 163      12.008  27.905  19.937  1.00 12.50           C  
HETATM 1301  C4B NDP A 163      13.165  28.552  20.833  1.00 11.70           C  
HETATM 1302  O4B NDP A 163      12.935  27.905  21.954  1.00 17.30           O  
HETATM 1303  C3B NDP A 163      14.498  27.874  20.291  1.00 11.70           C  
HETATM 1304  O3B NDP A 163      14.825  28.776  19.162  1.00 14.00           O  
HETATM 1305  C2B NDP A 163      15.195  28.086  21.711  1.00 17.90           C  
HETATM 1306  O2B NDP A 163      15.450  29.486  21.832  1.00 23.50           O  
HETATM 1307  C1B NDP A 163      14.178  27.606  22.701  1.00 17.30           C  
HETATM 1308  N9A NDP A 163      14.225  26.206  22.915  1.00 17.40           N  
HETATM 1309  C8A NDP A 163      13.679  25.161  22.252  1.00 14.60           C  
HETATM 1310  N7A NDP A 163      13.664  24.003  22.757  1.00 20.20           N  
HETATM 1311  C5A NDP A 163      14.570  24.202  23.849  1.00 18.40           C  
HETATM 1312  C6A NDP A 163      14.994  23.219  25.007  1.00 22.70           C  
HETATM 1313  N6A NDP A 163      14.638  21.931  25.017  1.00 27.30           N  
HETATM 1314  N1A NDP A 163      15.590  23.879  25.904  1.00 29.30           N  
HETATM 1315  C2A NDP A 163      15.752  25.266  25.866  1.00 25.00           C  
HETATM 1316  N3A NDP A 163      15.533  26.219  24.923  1.00 17.70           N  
HETATM 1317  C4A NDP A 163      14.717  25.553  23.980  1.00 16.10           C  
HETATM 1318  O3  NDP A 163       9.349  28.316  18.237  1.00 16.90           O  
HETATM 1319  PN  NDP A 163       8.875  27.457  16.958  1.00 15.60           P  
HETATM 1320  O1N NDP A 163       8.839  26.038  17.163  1.00 14.10           O  
HETATM 1321  O2N NDP A 163       9.378  28.266  15.763  1.00 14.40           O  
HETATM 1322  O5D NDP A 163       7.337  28.030  16.976  1.00 14.90           O  
HETATM 1323  C5D NDP A 163       6.895  29.467  16.902  1.00 14.30           C  
HETATM 1324  C4D NDP A 163       5.842  29.448  15.772  1.00 13.00           C  
HETATM 1325  O4D NDP A 163       4.628  28.839  16.388  1.00 16.60           O  
HETATM 1326  C3D NDP A 163       5.436  30.898  15.436  1.00 12.40           C  
HETATM 1327  O3D NDP A 163       4.901  31.042  14.119  1.00 14.80           O  
HETATM 1328  C2D NDP A 163       4.301  31.110  16.435  1.00 14.60           C  
HETATM 1329  O2D NDP A 163       3.431  32.180  15.968  1.00 14.50           O  
HETATM 1330  C1D NDP A 163       3.571  29.772  16.463  1.00 17.10           C  
HETATM 1331  N1N NDP A 163       2.583  29.529  17.611  1.00 16.70           N  
HETATM 1332  C2N NDP A 163       1.272  29.336  17.583  1.00 14.30           C  
HETATM 1333  C3N NDP A 163       0.564  28.758  18.489  1.00 14.30           C  
HETATM 1334  C7N NDP A 163      -0.801  28.720  18.050  1.00 10.80           C  
HETATM 1335  O7N NDP A 163      -1.423  28.204  19.087  1.00 12.10           O  
HETATM 1336  N7N NDP A 163      -1.304  28.708  16.790  1.00 16.50           N  
HETATM 1337  C4N NDP A 163       1.150  28.789  19.862  1.00 13.40           C  
HETATM 1338  C5N NDP A 163       2.526  29.181  19.983  1.00 17.80           C  
HETATM 1339  C6N NDP A 163       3.291  29.548  18.881  1.00 11.10           C  
HETATM 1340  P2B NDP A 163      16.898  30.289  21.617  1.00 17.70           P  
HETATM 1341  O1X NDP A 163      16.535  31.664  22.187  1.00 18.30           O  
HETATM 1342  O2X NDP A 163      17.879  29.212  22.066  1.00 19.10           O  
HETATM 1343  O3X NDP A 163      16.869  30.351  20.039  1.00 22.60           O  
HETATM 1344  N1  MTX A 164      -4.322  30.550  21.011  1.00 12.40           N  
HETATM 1345  C2  MTX A 164      -4.394  29.355  21.739  1.00  7.80           C  
HETATM 1346  NA2 MTX A 164      -5.645  28.807  21.860  1.00  9.00           N  
HETATM 1347  N3  MTX A 164      -3.288  28.783  22.252  1.00 12.10           N  
HETATM 1348  C4  MTX A 164      -2.019  29.274  22.234  1.00  8.20           C  
HETATM 1349  NA4 MTX A 164      -0.974  28.708  22.785  1.00  9.10           N  
HETATM 1350  C4A MTX A 164      -1.933  30.569  21.533  1.00 12.70           C  
HETATM 1351  N5  MTX A 164      -0.758  31.235  21.496  1.00 13.70           N  
HETATM 1352  C6  MTX A 164      -0.765  32.405  20.842  1.00 13.40           C  
HETATM 1353  C7  MTX A 164      -1.944  32.803  20.217  1.00 14.60           C  
HETATM 1354  N8  MTX A 164      -3.054  32.324  20.235  1.00 12.30           N  
HETATM 1355  C8A MTX A 164      -3.083  31.116  20.898  1.00 11.90           C  
HETATM 1356  C9  MTX A 164       0.640  33.021  20.684  1.00 16.00           C  
HETATM 1357  N10 MTX A 164       0.578  34.384  20.488  1.00 18.40           N  
HETATM 1358  CM  MTX A 164       1.308  34.813  19.227  1.00 17.40           C  
HETATM 1359  C11 MTX A 164      -1.279  37.203  22.934  1.00 21.20           C  
HETATM 1360  C12 MTX A 164      -0.862  37.551  21.655  1.00 17.90           C  
HETATM 1361  C13 MTX A 164      -0.194  36.854  20.712  1.00 18.50           C  
HETATM 1362  C14 MTX A 164       0.032  35.404  21.207  1.00 17.70           C  
HETATM 1363  C15 MTX A 164      -0.553  35.049  22.533  1.00 15.00           C  
HETATM 1364  C16 MTX A 164      -1.229  35.834  23.289  1.00 18.00           C  
HETATM 1365  C   MTX A 164      -1.965  38.130  23.541  1.00 28.80           C  
HETATM 1366  O   MTX A 164      -2.138  39.337  23.429  1.00 26.60           O  
HETATM 1367  N   MTX A 164      -2.925  37.974  24.419  1.00 22.60           N  
HETATM 1368  CA  MTX A 164      -3.571  38.572  25.455  1.00 31.40           C  
HETATM 1369  CT  MTX A 164      -3.410  37.769  26.744  1.00 24.60           C  
HETATM 1370  O1  MTX A 164      -3.349  36.580  27.005  1.00 22.80           O  
HETATM 1371  O2  MTX A 164      -3.607  38.634  27.799  1.00 21.60           O  
HETATM 1372  CB  MTX A 164      -5.120  38.852  25.539  1.00 27.70           C  
HETATM 1373  CG  MTX A 164      -5.745  39.848  24.643  1.00 54.70           C  
HETATM 1374  CD  MTX A 164      -7.132  39.910  23.719  1.00 37.70           C  
HETATM 1375  OE1 MTX A 164      -7.290  40.706  22.617  1.00 55.60           O  
HETATM 1376  OE2 MTX A 164      -7.707  39.325  24.755  1.00 31.50           O  
HETATM 1377  O   HOH A 201      -7.261  26.119  22.915  1.00 12.50           O  
HETATM 1378  O   HOH A 202      -3.104  18.408  15.604  1.00 28.30           O  
HETATM 1379  O   HOH A 203      -2.964  24.737   6.228  0.95 27.50           O  
HETATM 1380  O   HOH A 204      -5.303  18.135  12.410  1.00 71.30           O  
HETATM 1381  O   HOH A 205      -8.275  20.045  12.905  1.00 45.50           O  
HETATM 1382  O   HOH A 207       7.797  37.962  10.785  0.80 69.40           O  
HETATM 1383  O   HOH A 208       6.697  30.482  12.130  0.90 13.40           O  
HETATM 1384  O   HOH A 209       0.363  36.885  15.034  0.95 29.60           O  
HETATM 1385  O   HOH A 211      -4.883  34.944   7.424  1.00 44.20           O  
HETATM 1386  O   HOH A 212      -7.348  36.387  10.132  0.75 18.00           O  
HETATM 1387  O   HOH A 213      -9.518  38.254  10.748  0.75 20.10           O  
HETATM 1388  O   HOH A 214     -10.847  38.466  13.325  0.80 29.00           O  
HETATM 1389  O   HOH A 215      -3.683  37.819  16.967  0.65 37.50           O  
HETATM 1390  O   HOH A 216     -10.463  41.646  14.212  1.00 51.50           O  
HETATM 1391  O   HOH A 217      -5.264  35.504  16.846  0.70 13.80           O  
HETATM 1392  O   HOH A 218     -13.046  36.848  17.257  1.00 20.20           O  
HETATM 1393  O   HOH A 219     -14.544  39.244  19.050  1.00 59.40           O  
HETATM 1394  O   HOH A 220     -13.140  25.011  26.576  1.00 29.10           O  
HETATM 1395  O   HOH A 222      10.420  40.401  29.247  1.00 24.90           O  
HETATM 1396  O   HOH A 223       1.168  33.998  38.258  1.00 61.10           O  
HETATM 1397  O   HOH A 224      22.043  27.140  27.790  0.65 40.30           O  
HETATM 1398  O   HOH A 225      22.945  31.664  32.608  0.85 49.50           O  
HETATM 1399  O   HOH A 226      19.409  33.979  31.011  0.55 17.70           O  
HETATM 1400  O   HOH A 227      16.000  38.553  32.562  0.70 24.30           O  
HETATM 1401  O   HOH A 228      18.245  39.132  25.838  0.75 37.10           O  
HETATM 1402  O   HOH A 229      12.428  39.661  26.212  0.95 51.50           O  
HETATM 1403  O   HOH A 230      14.138  37.420  34.383  0.70 11.60           O  
HETATM 1404  O   HOH A 232      11.587  37.321  36.997  1.00 18.10           O  
HETATM 1405  O   HOH A 233      14.404  34.757  35.391  1.00 17.60           O  
HETATM 1406  O   HOH A 235      17.972  26.636  33.271  0.55 15.40           O  
HETATM 1407  O   HOH A 236      19.952  24.688  27.099  0.85 33.40           O  
HETATM 1408  O   HOH A 237       4.667  31.508  39.845  1.00 26.10           O  
HETATM 1409  O   HOH A 238       8.781  33.743  39.855  1.00 24.10           O  
HETATM 1410  O   HOH A 239      12.047  22.348  42.768  0.80 31.30           O  
HETATM 1411  O   HOH A 240       3.022  23.605  39.444  1.00 30.00           O  
HETATM 1412  O   HOH A 241      -3.147  27.669  38.501  1.00 34.90           O  
HETATM 1413  O   HOH A 242      -0.352  20.985  36.549  1.00 30.90           O  
HETATM 1414  O   HOH A 243       3.773  16.367  33.523  1.00 51.20           O  
HETATM 1415  O   HOH A 246       9.866  30.618   9.263  0.90 68.50           O  
HETATM 1416  O   HOH A 247       9.834  30.189   5.706  1.00 57.50           O  
HETATM 1417  O   HOH A 248      -0.115  18.458  13.008  1.00 27.00           O  
HETATM 1418  O   HOH A 249      -1.164  16.641  16.388  0.90 25.90           O  
HETATM 1419  O   HOH A 250     -13.068  37.358  14.418  0.85 22.30           O  
HETATM 1420  O   HOH A 251     -14.649  23.007  25.129  1.00 18.20           O  
HETATM 1421  O   HOH A 252      -9.493  24.457  24.213  1.00 19.80           O  
HETATM 1422  O   HOH A 253      -5.267  32.784  17.817  1.00 19.50           O  
HETATM 1423  O   HOH A 254     -13.287  33.419  23.915  0.90 32.00           O  
HETATM 1424  O   HOH A 255      -6.672  30.463  33.981  1.00 28.40           O  
HETATM 1425  O   HOH A 256       2.939  37.427  16.444  0.85 55.30           O  
HETATM 1426  O   HOH A 257       1.326  39.947  18.900  1.00 66.20           O  
HETATM 1427  O   HOH A 258      -7.775  42.355  18.424  1.00 64.90           O  
HETATM 1428  O   HOH A 260       1.135  41.086  36.372  1.00 33.20           O  
HETATM 1429  O   HOH A 261      11.447  44.110  25.045  0.95 50.30           O  
HETATM 1430  O   HOH A 262       3.510  38.678  34.345  1.00 30.20           O  
HETATM 1431  O   HOH A 263       6.079  36.344  34.672  1.00 19.90           O  
HETATM 1432  O   HOH A 264      13.377  42.623  29.405  0.80 28.40           O  
HETATM 1433  O   HOH A 265      17.469  43.102  31.590  0.95 60.80           O  
HETATM 1434  O   HOH A 266      15.820  19.958  27.454  1.00 33.80           O  
HETATM 1435  O   HOH A 267      18.058  21.881  35.074  0.55 24.90           O  
HETATM 1436  O   HOH A 268      19.920  29.610  35.102  0.70 47.70           O  
HETATM 1437  O   HOH A 269      13.459  18.993  37.371  0.95 34.10           O  
HETATM 1438  O   HOH A 271       7.348  35.541  37.417  0.65 22.40           O  
HETATM 1439  O   HOH A 272       9.834  43.320  35.858  1.00 30.00           O  
HETATM 1440  O   HOH A 273      14.235  26.324  37.791  0.80 21.80           O  
HETATM 1441  O   HOH A 274       9.076  37.688  38.080  0.75 26.60           O  
HETATM 1442  O   HOH A 275       6.536  39.686  36.362  0.75 25.70           O  
HETATM 1443  O   HOH A 276       9.658  24.893  14.913  0.80 18.70           O  
HETATM 1444  O   HOH A 277       8.778  15.253  27.062  1.00 32.90           O  
HETATM 1445  O   HOH A 278      -5.713  16.803  14.969  1.00 37.50           O  
HETATM 1446  O   HOH A 279      12.838  21.290  21.524  1.00 36.00           O  
HETATM 1447  O   HOH A 280       1.480  11.974  28.247  0.85 48.90           O  
HETATM 1448  O   HOH A 281      12.277  16.797  26.669  1.00 34.50           O  
HETATM 1449  O   HOH A 283      16.319  24.482  19.955  0.85 36.90           O  
HETATM 1450  O   HOH A 284     -17.024  27.295   8.451  0.80 22.20           O  
HETATM 1451  O   HOH A 287       0.679  11.606  22.271  0.65 21.00           O  
HETATM 1452  O   HOH A 288      -3.435   9.609  16.612  0.70 32.10           O  
HETATM 1453  O   HOH A 289     -13.255  11.059  22.393  0.95 26.10           O  
HETATM 1454  O   HOH A 290      -7.513  14.805  16.491  0.95 46.50           O  
HETATM 1455  O   HOH A 291       7.624  15.708  18.769  0.85 41.20           O  
HETATM 1456  O   HOH A 292     -10.136  27.712   3.903  1.00 42.00           O  
HETATM 1457  O   HOH A 293       5.490  23.014   7.863  1.00 27.10           O  
HETATM 1458  O   HOH A 294       0.165  11.165  15.305  0.70 17.00           O  
HETATM 1459  O   HOH A 295      -9.759   9.472  21.123  0.70 23.60           O  
HETATM 1460  O   HOH A 297      -6.119   8.594  16.201  1.00 89.90           O  
HETATM 1461  O   HOH A 299       0.223   9.422  24.391  0.55 29.40           O  
HETATM 1462  O   HOH A 301       8.850  26.990  13.064  1.00 27.50           O  
HETATM 1463  O   HOH A 302       9.141  30.108  13.858  0.75 20.10           O  
HETATM 1464  O   HOH A 303     -12.360  16.965  16.836  1.00 29.20           O  
HETATM 1465  O   HOH A 305     -14.063  20.624  30.199  0.50 17.20           O  
HETATM 1466  O   HOH A 306     -19.036  21.794  19.246  0.90 28.30           O  
HETATM 1467  O   HOH A 307     -15.382  18.912  18.302  1.00 26.50           O  
HETATM 1468  O   HOH A 308     -21.493  30.979  17.527  1.00 37.50           O  
HETATM 1469  O   HOH A 310     -13.549  37.819  11.243  0.80 26.10           O  
HETATM 1470  O   HOH A 312     -20.545  32.212   9.796  0.60 46.00           O  
HETATM 1471  O   HOH A 314     -20.696  33.718   6.079  0.45 19.60           O  
HETATM 1472  O   HOH A 315     -14.429  24.072  13.839  1.00 36.30           O  
HETATM 1473  O   HOH A 316     -14.329  29.772   3.623  0.45 16.30           O  
HETATM 1474  O   HOH A 317      -5.742  14.600  32.197  0.90 34.90           O  
HETATM 1475  O   HOH A 318      18.148  22.547  26.529  0.75 25.40           O  
HETATM 1476  O   HOH A 319       0.359   6.870  29.667  1.00 88.90           O  
HETATM 1477  O   HOH A 321      -6.974  11.955  32.524  0.60 19.10           O  
HETATM 1478  O   HOH A 322      -3.266  40.918  21.692  0.85 33.10           O  
HETATM 1479  O   HOH A 323      -3.209   6.827  28.061  0.70 36.10           O  
HETATM 1480  O   HOH A 324      -3.604   8.582  32.188  0.60 47.10           O  
HETATM 1481  O   HOH A 326      18.533  27.457  19.731  0.85 39.30           O  
HETATM 1482  O   HOH A 329      -8.907  42.374  23.719  0.95 63.40           O  
HETATM 1483  O   HOH A 331      -2.781  41.098  28.360  1.00 61.90           O  
HETATM 1484  O   HOH A 332      -5.817  26.256  31.628  0.95 30.90           O  
HETATM 1485  O   HOH A 335      -7.481  21.084   3.259  1.00 91.30           O  
HETATM 1486  O   HOH A 337       3.334  21.557   3.287  1.00 54.40           O  
HETATM 1487  O   HOH A 338       0.582  26.374   4.099  0.90 44.50           O  
HETATM 1488  O   HOH A 339      -0.679  23.244  -0.084  0.95131.90           O  
HETATM 1489  O   HOH A 341     -10.876  21.962  11.514  0.85 66.80           O  
HETATM 1490  O   HOH A 343      14.598  17.270  16.379  0.90 92.20           O  
HETATM 1491  O   HOH A 344       9.888  28.142  10.477  0.85 39.30           O  
HETATM 1492  O   HOH A 345      -1.775  32.709   6.621  1.00 27.40           O  
HETATM 1493  O   HOH A 346      -5.098  38.254   9.375  0.60 31.70           O  
HETATM 1494  O   HOH A 347      -2.483  37.396  14.296  1.00 35.10           O  
HETATM 1495  O   HOH A 348     -10.086  39.947  32.272  1.00 64.70           O  
HETATM 1496  O   HOH A 351     -10.524  36.250  28.742  0.95 37.50           O  
HETATM 1497  O   HOH A 352      -8.932  42.343  11.122  0.95 73.30           O  
HETATM 1498  O   HOH A 353     -12.518  42.069  19.012  1.00 57.80           O  
HETATM 1499  O   HOH A 354     -15.227  34.415  16.164  0.75 18.20           O  
HETATM 1500  O   HOH A 355     -14.746  36.643  23.569  1.00 59.30           O  
HETATM 1501  O   HOH A 356      16.582  36.624  20.207  0.65 28.90           O  
HETATM 1502  O   HOH A 357     -12.414  29.741  28.901  0.55 24.80           O  
HETATM 1503  O   HOH A 358     -11.005  34.023  32.804  0.95 84.20           O  
HETATM 1504  O   HOH A 359     -15.015  37.172  30.619  0.80102.10           O  
HETATM 1505  O   HOH A 360      -9.992  30.861  37.847  0.90 63.30           O  
HETATM 1506  O   HOH A 361      23.225  33.232  20.077  1.00151.30           O  
HETATM 1507  O   HOH A 362       9.953  41.198  20.562  0.75 29.90           O  
HETATM 1508  O   HOH A 364       9.654  35.865  17.527  0.90 52.80           O  
HETATM 1509  O   HOH A 365      13.858  34.309  15.632  1.00 37.80           O  
HETATM 1510  O   HOH A 366      15.651  32.610  15.389  1.00 37.00           O  
HETATM 1511  O   HOH A 368       6.281  44.770  26.427  0.95 41.20           O  
HETATM 1512  O   HOH A 370       3.270  42.990  33.019  1.00 57.80           O  
HETATM 1513  O   HOH A 373      20.318  29.455  21.197  0.50 19.30           O  
HETATM 1514  O   HOH A 374      17.994  32.871  33.589  0.55 19.20           O  
HETATM 1515  O   HOH A 378     -15.953  32.485  22.794  1.00 36.00           O  
HETATM 1516  O   HOH A 379       5.587  14.307  17.920  0.70 28.60           O  
HETATM 1517  O   HOH A 380       1.552  11.961  31.264  1.00 83.00           O  
HETATM 1518  O   HOH A 381      -3.302  19.025  33.682  1.00 62.70           O  
HETATM 1519  O   HOH A 384       5.594  23.729   5.033  1.00 80.40           O  
HETATM 1520  O   HOH A 388      -9.748  12.030  16.285  0.50 86.70           O  
HETATM 1521  O   HOH A 390     -22.018  29.623  24.503  1.00 70.40           O  
HETATM 1522  O   HOH A 391     -19.438  29.075  10.038  0.60 19.60           O  
HETATM 1523  O   HOH A 393     -20.045  33.973  17.294  0.70 40.60           O  
HETATM 1524  O   HOH A 394     -12.543  24.252  29.657  0.80 52.50           O  
HETATM 1525  O   HOH A 399      -3.288   4.450  21.235  0.50 36.60           O  
HETATM 1526  O   HOH A 400       0.471   4.475  18.993  1.00 65.30           O  
HETATM 1527  O   HOH A 401      15.626  27.264  16.771  0.85 37.50           O  
HETATM 1528  O   HOH A 402      -2.321  39.941  18.807  1.00 49.60           O  
HETATM 1529  O   HOH A 403       5.770  38.211  13.830  1.00 61.90           O  
HETATM 1530  O   HOH A 404       1.937  39.449  13.167  0.80 53.30           O  
HETATM 1531  O   HOH A 405       0.589  36.232   7.274  1.00101.10           O  
HETATM 1532  O   HOH A 406      -0.539  18.271  10.122  1.00 32.00           O  
HETATM 1533  O   HOH A 408      -6.000  42.667  11.495  0.85 71.50           O  
HETATM 1534  O   HOH A 409      16.337  18.850  31.114  1.00 32.00           O  
HETATM 1535  O   HOH A 410      17.534  31.004  37.165  0.45 18.80           O  
HETATM 1536  O   HOH A 411       2.220  37.937  37.445  0.60 47.60           O  
HETATM 1537  O   HOH A 413       5.756  44.870  30.414  0.90 79.40           O  
HETATM 1538  O   HOH A 414      10.739  15.365  23.196  1.00 42.30           O  
HETATM 1539  O   HOH A 416       4.383  35.099  38.435  0.75 55.90           O  
HETATM 1540  O   HOH A 417      22.061  39.816  28.079  0.80 61.70           O  
HETATM 1541  O   HOH A 419      13.143  39.580  36.110  1.00 19.40           O  
HETATM 1542  O   HOH A 421       3.058  32.479  47.129  1.00 80.40           O  
HETATM 1543  O   HOH A 423       3.834  20.244  41.041  0.75 38.80           O  
HETATM 1544  O   HOH A 424      -6.058  30.954  37.389  0.95 61.70           O  
HETATM 1545  O   HOH A 425      16.531  26.990  12.494  0.75 43.30           O  
HETATM 1546  O   HOH A 426      -4.786  23.611  32.048  1.00 61.80           O  
HETATM 1547  O   HOH A 427      -6.194  17.674   8.675  1.00117.50           O  
HETATM 1548  O   HOH A 428       5.504  26.474   4.389  0.90 66.30           O  
HETATM 1549  O   HOH A 429     -17.293  24.874  10.337  0.60 41.20           O  
HETATM 1550  O   HOH A 432     -17.448  35.597  17.621  0.50 40.70           O  
HETATM 1551  O   HOH A 433     -23.383  37.103  10.739  0.60 64.70           O  
HETATM 1552  O   HOH A 434     -19.607  29.193  27.146  0.70 59.30           O  
HETATM 1553  O   HOH A 435       5.853  31.322   5.332  1.00 64.80           O  
HETATM 1554  O   HOH A 436      -1.376  36.723  10.431  0.95 67.00           O  
HETATM 1555  O   HOH A 437      -9.029  26.965  36.717  1.00 85.60           O  
HETATM 1556  O   HOH A 438      -0.938  18.464  22.084  1.00 94.40           O  
HETATM 1557  O   HOH A 439       3.730  32.896  18.853  1.00 78.70           O  
HETATM 1558  O   HOH A 440       8.408  43.501  33.243  1.00 32.10           O  
HETATM 1559  O   HOH A 441     -13.898  14.127  17.453  0.95 48.70           O  
HETATM 1560  O   HOH A 443      -9.938  39.455  27.062  1.00 63.40           O  
HETATM 1561  O   HOH A 444     -12.640  28.901   1.121  0.40 33.70           O  
HETATM 1562  O   HOH A 446     -14.200  40.974  15.100  0.85 59.30           O  
HETATM 1563  O   HOH A 447       6.848  41.248  18.788  0.70 43.40           O  
HETATM 1564  O   HOH A 450      -9.773  18.570   9.655  1.00 70.20           O  
HETATM 1565  O   HOH A 456      -1.505  14.071  15.034  0.55 26.30           O  
HETATM 1566  O   HOH A 458      -4.746  13.498  10.216  0.20 41.70           O  
HETATM 1567  O   HOH A 459      -4.340  13.355  13.736  0.45 37.30           O  
HETATM 1568  O   HOH A 470     -13.197  27.799   5.407  0.40 12.30           O  
HETATM 1569  O   HOH A 471     -16.312  20.923  15.454  1.00 90.10           O  
HETATM 1570  O   HOH A 472     -18.723  18.153  16.575  1.00109.60           O  
HETATM 1571  O   HOH A 475     -20.182  36.649  14.306  0.55 31.50           O  
HETATM 1572  O   HOH A 478     -21.522  22.404  15.763  0.85 73.00           O  
HETATM 1573  O   HOH A 485     -17.645  26.965   2.082  0.65 68.10           O  
HETATM 1574  O   HOH A 501      -7.330  16.044  34.616  0.75 31.80           O  
HETATM 1575  O   HOH A 502      -8.321  14.401  37.483  1.00 59.20           O  
HETATM 1576  O   HOH A 503      -5.932  13.498  36.605  0.60 42.00           O  
HETATM 1577  O   HOH A 504      -3.489  12.067  33.243  0.35 33.60           O  
HETATM 1578  O   HOH A 505     -14.785  12.353  19.516  1.00 87.90           O  
HETATM 1579  O   HOH A 507     -12.407  26.443  31.544  0.70 41.80           O  
HETATM 1580  O   HOH A 508      -9.787  24.283  30.675  1.00 57.90           O  
HETATM 1581  O   HOH A 509      -8.242  18.732  32.496  1.00 55.60           O  
HETATM 1582  O   HOH A 510     -10.229  20.692  33.663  1.00137.00           O  
HETATM 1583  O   HOH A 511      19.797  36.219  37.249  0.40 19.00           O  
HETATM 1584  O   HOH A 514      12.152  23.897  14.128  0.60 37.90           O  
HETATM 1585  O   HOH A 515      13.280  28.079  12.345  0.85 98.90           O  
HETATM 1586  O   HOH A 516      10.844  32.199  14.175  0.85 68.00           O  
HETATM 1587  O   HOH A 518       1.685  24.040   6.191  0.80 95.10           O  
HETATM 1588  O   HOH A 519      -1.049  20.462   5.986  0.85 67.80           O  
HETATM 1589  O   HOH A 521      -5.404  40.215   5.855  0.50 32.20           O  
HETATM 1590  O   HOH A 524       3.615  39.431   8.983  1.00 75.80           O  
HETATM 1591  O   HOH A 525     -14.322  41.173   2.110  0.65 46.70           O  
HETATM 1592  O   HOH A 526     -11.857  29.797  31.703  0.55 39.10           O  
HETATM 1593  O   HOH A 535     -15.227  33.867  30.573  0.55 61.50           O  
HETATM 1594  O   HOH A 537     -11.404   6.198  28.331  0.50 40.30           O  
HETATM 1595  O   HOH A 538     -13.111   7.872  23.448  1.00 46.50           O  
HETATM 1596  O   HOH A 539     -13.308   8.078  28.714  0.50 24.30           O  
HETATM 1597  O   HOH A 543     -10.826   3.753  24.979  0.60 41.50           O  
HETATM 1598  O   HOH A 545       2.781  30.009  43.450  0.90 52.40           O  
HETATM 1599  O   HOH A 547      16.172  24.501  38.743  0.45 33.90           O  
HETATM 1600  O   HOH A 549      11.814  18.595  39.687  1.00 50.70           O  
HETATM 1601  O   HOH A 550      13.247  19.809  42.077  0.85 66.60           O  
HETATM 1602  O   HOH A 551      13.237  16.429  44.878  1.00129.90           O  
HETATM 1603  O   HOH A 552      10.366  19.858  46.232  1.00100.60           O  
HETATM 1604  O   HOH A 553      10.621  23.661  45.738  0.75 47.40           O  
HETATM 1605  O   HOH A 554      11.929  17.985  47.661  1.00 90.00           O  
HETATM 1606  O   HOH A 555      -2.167  31.110  40.630  1.00 80.10           O  
HETATM 1607  O   HOH A 556      -1.103  22.037  39.416  0.90 76.70           O  
HETATM 1608  O   HOH A 559      -7.387  40.339  27.136  1.00 93.80           O  
HETATM 1609  O   HOH A 560      -8.106  26.548  33.925  1.00109.10           O  
HETATM 1610  O   HOH A 561      -9.058  29.056  33.383  1.00 82.10           O  
HETATM 1611  O   HOH A 562       9.845  19.952  16.631  0.55 40.40           O  
HETATM 1612  O   HOH A 563     -12.619  22.155   8.115  1.00 67.80           O  
HETATM 1613  O   HOH A 564      -2.052  25.123   2.904  1.00 54.60           O  
HETATM 1614  O   HOH A 565       2.231   6.640  20.039  0.70 52.70           O  
HETATM 1615  O   HOH A 567      -1.929   6.005  32.552  0.80 52.20           O  
HETATM 1616  O   HOH A 569       7.488  19.180  38.687  0.20 11.70           O  
HETATM 1617  O   HOH A 571       4.495  28.422  46.064  0.45 62.60           O  
HETATM 1618  O   HOH A 572       2.088  19.535  35.802  0.50 42.80           O  
HETATM 1619  O   HOH A 573       0.431  20.250  41.993  0.40 49.50           O  
HETATM 1620  O   HOH A 575       3.431  21.091  37.950  0.20 14.40           O  
HETATM 1621  O   HOH A 576      10.678  29.921  42.170  0.25 14.00           O  
HETATM 1622  O   HOH A 577     -17.947  34.346  21.972  0.55 40.90           O  
HETATM 1623  O   HOH A 578     -20.451  29.486  22.346  1.00 69.30           O  
HETATM 1624  O   HOH A 579      14.354  18.863  24.848  0.80 62.70           O  
HETATM 1625  O   HOH A 580      21.533  36.923  24.512  0.80 92.00           O  
HETATM 1626  O   HOH A 581      19.054  37.545  22.383  0.40 33.70           O  
HETATM 1627  O   HOH A 601     -21.590  31.670  22.813  1.00 88.50           O  
HETATM 1628  O   HOH A 602     -10.344   6.229  21.151  1.00 72.40           O  
HETATM 1629  O   HOH A 604      12.342  36.114  17.555  1.00 76.40           O  
HETATM 1630  O   HOH A 606      -1.814  41.864  23.980  0.70 51.50           O  
HETATM 1631  O   HOH A 607     -16.312  23.499   0.532  0.80 77.10           O  
HETATM 1632  O   HOH A 608     -15.806  23.505   7.041  1.00 96.50           O  
HETATM 1633  O   HOH A 610      21.429  38.335  33.916  0.70 62.70           O  
HETATM 1634  O   HOH A 611      24.461  30.842  25.409  1.00 59.60           O  
HETATM 1635  O   HOH A 616     -13.222   6.783  26.165  0.90 85.90           O  
HETATM 1636  O   HOH A 619      -2.734  23.393  41.433  0.90 72.30           O  
HETATM 1637  O   HOH A 620      -3.974  24.856  44.710  1.00107.30           O  
HETATM 1638  O   HOH A 621      -8.753  41.559  20.917  1.00 72.60           O  
HETATM 1639  O   HOH A 622      -7.466  27.208  45.457  0.70 58.50           O  
HETATM 1640  O   HOH A 623      -0.180   5.389  26.034  0.50 42.00           O  
CONECT 1296 1297 1298 1299 1318                                                 
CONECT 1297 1296                                                                
CONECT 1298 1296                                                                
CONECT 1299 1296 1300                                                           
CONECT 1300 1299 1301                                                           
CONECT 1301 1300 1302 1303                                                      
CONECT 1302 1301 1307                                                           
CONECT 1303 1301 1304 1305                                                      
CONECT 1304 1303                                                                
CONECT 1305 1303 1306 1307                                                      
CONECT 1306 1305 1340                                                           
CONECT 1307 1302 1305 1308                                                      
CONECT 1308 1307 1309 1317                                                      
CONECT 1309 1308 1310                                                           
CONECT 1310 1309 1311                                                           
CONECT 1311 1310 1312 1317                                                      
CONECT 1312 1311 1313 1314                                                      
CONECT 1313 1312                                                                
CONECT 1314 1312 1315                                                           
CONECT 1315 1314 1316                                                           
CONECT 1316 1315 1317                                                           
CONECT 1317 1308 1311 1316                                                      
CONECT 1318 1296 1319                                                           
CONECT 1319 1318 1320 1321 1322                                                 
CONECT 1320 1319                                                                
CONECT 1321 1319                                                                
CONECT 1322 1319 1323                                                           
CONECT 1323 1322 1324                                                           
CONECT 1324 1323 1325 1326                                                      
CONECT 1325 1324 1330                                                           
CONECT 1326 1324 1327 1328                                                      
CONECT 1327 1326                                                                
CONECT 1328 1326 1329 1330                                                      
CONECT 1329 1328                                                                
CONECT 1330 1325 1328 1331                                                      
CONECT 1331 1330 1332 1339                                                      
CONECT 1332 1331 1333                                                           
CONECT 1333 1332 1334 1337                                                      
CONECT 1334 1333 1335 1336                                                      
CONECT 1335 1334                                                                
CONECT 1336 1334                                                                
CONECT 1337 1333 1338                                                           
CONECT 1338 1337 1339                                                           
CONECT 1339 1331 1338                                                           
CONECT 1340 1306 1341 1342 1343                                                 
CONECT 1341 1340                                                                
CONECT 1342 1340                                                                
CONECT 1343 1340                                                                
CONECT 1344 1345 1355                                                           
CONECT 1345 1344 1346 1347                                                      
CONECT 1346 1345                                                                
CONECT 1347 1345 1348                                                           
CONECT 1348 1347 1349 1350                                                      
CONECT 1349 1348                                                                
CONECT 1350 1348 1351 1355                                                      
CONECT 1351 1350 1352                                                           
CONECT 1352 1351 1353 1356                                                      
CONECT 1353 1352 1354                                                           
CONECT 1354 1353 1355                                                           
CONECT 1355 1344 1350 1354                                                      
CONECT 1356 1352 1357                                                           
CONECT 1357 1356 1358 1362                                                      
CONECT 1358 1357                                                                
CONECT 1359 1360 1364 1365                                                      
CONECT 1360 1359 1361                                                           
CONECT 1361 1360 1362                                                           
CONECT 1362 1357 1361 1363                                                      
CONECT 1363 1362 1364                                                           
CONECT 1364 1359 1363                                                           
CONECT 1365 1359 1366 1367                                                      
CONECT 1366 1365                                                                
CONECT 1367 1365 1368                                                           
CONECT 1368 1367 1369 1372                                                      
CONECT 1369 1368 1370 1371                                                      
CONECT 1370 1369                                                                
CONECT 1371 1369                                                                
CONECT 1372 1368 1373                                                           
CONECT 1373 1372 1374                                                           
CONECT 1374 1373 1375 1376                                                      
CONECT 1375 1374                                                                
CONECT 1376 1374                                                                
MASTER      512    0    2    4    8    0   36    6 1639    1   81   13          
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.