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Database: PDB
Entry: 1W4R
LinkDB: 1W4R
Original site: 1W4R 
HEADER    TRANSFERASE                             27-JUL-04   1W4R              
TITLE     STRUCTURE OF A TYPE II THYMIDINE KINASE WITH BOUND DTTP               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THYMIDINE KINASE;                                          
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 EC: 2.7.1.21;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TRANSFERASE, TYPE II,  TRANSFERASE                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.S.BIRRINGER,M.T.CLAUS,G.FOLKERS,D.P.KLOER,G.E.SCHULZ, L.SCAPOZZA    
REVDAT   4   06-MAR-13 1W4R    1       KEYWDS AUTHOR JRNL   REMARK              
REVDAT   4 2                           VERSN  DBREF  SEQADV FORMUL              
REVDAT   4 3                           SITE   MASTER                            
REVDAT   3   24-FEB-09 1W4R    1       VERSN                                    
REVDAT   2   02-MAR-05 1W4R    1       JRNL                                     
REVDAT   1   01-FEB-05 1W4R    0                                                
JRNL        AUTH   M.S.BIRRINGER,M.T.CLAUS,G.FOLKERS,D.P.KLOER,G.E.SCHULZ,      
JRNL        AUTH 2 L.SCAPOZZA                                                   
JRNL        TITL   STRUCTURE OF A TYPE II THYMIDINE KINASE WITH BOUND DTTP      
JRNL        REF    FEBS LETT.                    V. 579  1376 2005              
JRNL        REFN                   ISSN 0014-5793                               
JRNL        PMID   15733844                                                     
JRNL        DOI    10.1016/J.FEBSLET.2005.01.034                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.83 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.0                                           
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.83                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 140080                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.160                           
REMARK   3   R VALUE            (WORKING SET) : 0.159                           
REMARK   3   FREE R VALUE                     : 0.189                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7423                            
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   REFLECTION IN BIN     (WORKING SET) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE SET COUNT          : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10203                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 480                                     
REMARK   3   SOLVENT ATOMS            : 794                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.50                          
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.969                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.957                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : NULL                                          
REMARK   3   ION PROBE RADIUS   : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS.                                                   
REMARK   4                                                                      
REMARK   4 1W4R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-JUL-04.                  
REMARK 100 THE PDBE ID CODE IS EBI-20600.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.20                               
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9794, 1.277, 0.9196              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 140080                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.830                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 7.100                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.83                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 7.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.4                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       78.74800            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       61.46000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       78.74800            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       61.46000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE:  1                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10450 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 31630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.2 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, C                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 BIOMOLECULE:  2                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8850 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.7 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     0                                                      
REMARK 465     ARG A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     HIS A     4                                                      
REMARK 465     HIS A     5                                                      
REMARK 465     HIS A     6                                                      
REMARK 465     HIS A     7                                                      
REMARK 465     HIS A     8                                                      
REMARK 465     HIS A     9                                                      
REMARK 465     LEU A    10                                                      
REMARK 465     VAL A    11                                                      
REMARK 465     PRO A    12                                                      
REMARK 465     ARG A    13                                                      
REMARK 465     GLY A    14                                                      
REMARK 465     SER A    15                                                      
REMARK 465     LYS A    16                                                      
REMARK 465     THR A    17                                                      
REMARK 465     LYS A   192                                                      
REMARK 465     ALA A   193                                                      
REMARK 465     SER A   194                                                      
REMARK 465     MET B     0                                                      
REMARK 465     ARG B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     HIS B     4                                                      
REMARK 465     HIS B     5                                                      
REMARK 465     HIS B     6                                                      
REMARK 465     HIS B     7                                                      
REMARK 465     HIS B     8                                                      
REMARK 465     HIS B     9                                                      
REMARK 465     LEU B    10                                                      
REMARK 465     VAL B    11                                                      
REMARK 465     PRO B    12                                                      
REMARK 465     ARG B    13                                                      
REMARK 465     GLY B    14                                                      
REMARK 465     SER B    15                                                      
REMARK 465     LYS B    16                                                      
REMARK 465     THR B    17                                                      
REMARK 465     CYS B    66                                                      
REMARK 465     THR B    67                                                      
REMARK 465     HIS B    68                                                      
REMARK 465     ASP B    69                                                      
REMARK 465     ARG B    70                                                      
REMARK 465     ASN B    71                                                      
REMARK 465     THR B    72                                                      
REMARK 465     LYS B   192                                                      
REMARK 465     ALA B   193                                                      
REMARK 465     SER B   194                                                      
REMARK 465     MET C     0                                                      
REMARK 465     ARG C     1                                                      
REMARK 465     GLY C     2                                                      
REMARK 465     SER C     3                                                      
REMARK 465     HIS C     4                                                      
REMARK 465     HIS C     5                                                      
REMARK 465     HIS C     6                                                      
REMARK 465     HIS C     7                                                      
REMARK 465     HIS C     8                                                      
REMARK 465     HIS C     9                                                      
REMARK 465     LEU C    10                                                      
REMARK 465     VAL C    11                                                      
REMARK 465     PRO C    12                                                      
REMARK 465     ARG C    13                                                      
REMARK 465     GLY C    14                                                      
REMARK 465     SER C    15                                                      
REMARK 465     LYS C    16                                                      
REMARK 465     THR C    17                                                      
REMARK 465     TYR C    61                                                      
REMARK 465     SER C    62                                                      
REMARK 465     SER C    63                                                      
REMARK 465     SER C    64                                                      
REMARK 465     PHE C    65                                                      
REMARK 465     CYS C    66                                                      
REMARK 465     THR C    67                                                      
REMARK 465     HIS C    68                                                      
REMARK 465     ASP C    69                                                      
REMARK 465     ARG C    70                                                      
REMARK 465     ASN C    71                                                      
REMARK 465     THR C    72                                                      
REMARK 465     MET C    73                                                      
REMARK 465     GLU C    74                                                      
REMARK 465     LYS C   192                                                      
REMARK 465     ALA C   193                                                      
REMARK 465     SER C   194                                                      
REMARK 465     MET D     0                                                      
REMARK 465     ARG D     1                                                      
REMARK 465     GLY D     2                                                      
REMARK 465     SER D     3                                                      
REMARK 465     HIS D     4                                                      
REMARK 465     HIS D     5                                                      
REMARK 465     HIS D     6                                                      
REMARK 465     HIS D     7                                                      
REMARK 465     HIS D     8                                                      
REMARK 465     HIS D     9                                                      
REMARK 465     LEU D    10                                                      
REMARK 465     VAL D    11                                                      
REMARK 465     PRO D    12                                                      
REMARK 465     ARG D    13                                                      
REMARK 465     GLY D    14                                                      
REMARK 465     SER D    15                                                      
REMARK 465     LYS D    16                                                      
REMARK 465     THR D    17                                                      
REMARK 465     TYR D    61                                                      
REMARK 465     SER D    62                                                      
REMARK 465     SER D    63                                                      
REMARK 465     SER D    64                                                      
REMARK 465     PHE D    65                                                      
REMARK 465     CYS D    66                                                      
REMARK 465     THR D    67                                                      
REMARK 465     HIS D    68                                                      
REMARK 465     ASP D    69                                                      
REMARK 465     ARG D    70                                                      
REMARK 465     ASN D    71                                                      
REMARK 465     THR D    72                                                      
REMARK 465     MET D    73                                                      
REMARK 465     GLU D    74                                                      
REMARK 465     LYS D   192                                                      
REMARK 465     ALA D   193                                                      
REMARK 465     SER D   194                                                      
REMARK 465     MET E     0                                                      
REMARK 465     ARG E     1                                                      
REMARK 465     GLY E     2                                                      
REMARK 465     SER E     3                                                      
REMARK 465     HIS E     4                                                      
REMARK 465     HIS E     5                                                      
REMARK 465     HIS E     6                                                      
REMARK 465     HIS E     7                                                      
REMARK 465     HIS E     8                                                      
REMARK 465     HIS E     9                                                      
REMARK 465     LEU E    10                                                      
REMARK 465     VAL E    11                                                      
REMARK 465     PRO E    12                                                      
REMARK 465     ARG E    13                                                      
REMARK 465     GLY E    14                                                      
REMARK 465     SER E    15                                                      
REMARK 465     LYS E    16                                                      
REMARK 465     THR E    17                                                      
REMARK 465     TYR E    61                                                      
REMARK 465     SER E    62                                                      
REMARK 465     SER E    63                                                      
REMARK 465     SER E    64                                                      
REMARK 465     PHE E    65                                                      
REMARK 465     CYS E    66                                                      
REMARK 465     THR E    67                                                      
REMARK 465     HIS E    68                                                      
REMARK 465     ASP E    69                                                      
REMARK 465     ARG E    70                                                      
REMARK 465     ASN E    71                                                      
REMARK 465     THR E    72                                                      
REMARK 465     MET E    73                                                      
REMARK 465     GLU E    74                                                      
REMARK 465     LYS E   192                                                      
REMARK 465     ALA E   193                                                      
REMARK 465     SER E   194                                                      
REMARK 465     MET F     0                                                      
REMARK 465     ARG F     1                                                      
REMARK 465     GLY F     2                                                      
REMARK 465     SER F     3                                                      
REMARK 465     HIS F     4                                                      
REMARK 465     HIS F     5                                                      
REMARK 465     HIS F     6                                                      
REMARK 465     HIS F     7                                                      
REMARK 465     HIS F     8                                                      
REMARK 465     HIS F     9                                                      
REMARK 465     LEU F    10                                                      
REMARK 465     VAL F    11                                                      
REMARK 465     PRO F    12                                                      
REMARK 465     ARG F    13                                                      
REMARK 465     GLY F    14                                                      
REMARK 465     SER F    15                                                      
REMARK 465     LYS F    16                                                      
REMARK 465     THR F    17                                                      
REMARK 465     SER F    62                                                      
REMARK 465     SER F    63                                                      
REMARK 465     SER F    64                                                      
REMARK 465     PHE F    65                                                      
REMARK 465     CYS F    66                                                      
REMARK 465     THR F    67                                                      
REMARK 465     HIS F    68                                                      
REMARK 465     ASP F    69                                                      
REMARK 465     ARG F    70                                                      
REMARK 465     ASN F    71                                                      
REMARK 465     THR F    72                                                      
REMARK 465     MET F    73                                                      
REMARK 465     GLU F    74                                                      
REMARK 465     LYS F   192                                                      
REMARK 465     ALA F   193                                                      
REMARK 465     SER F   194                                                      
REMARK 465     MET G     0                                                      
REMARK 465     ARG G     1                                                      
REMARK 465     GLY G     2                                                      
REMARK 465     SER G     3                                                      
REMARK 465     HIS G     4                                                      
REMARK 465     HIS G     5                                                      
REMARK 465     HIS G     6                                                      
REMARK 465     HIS G     7                                                      
REMARK 465     HIS G     8                                                      
REMARK 465     HIS G     9                                                      
REMARK 465     LEU G    10                                                      
REMARK 465     VAL G    11                                                      
REMARK 465     PRO G    12                                                      
REMARK 465     ARG G    13                                                      
REMARK 465     GLY G    14                                                      
REMARK 465     SER G    15                                                      
REMARK 465     LYS G    16                                                      
REMARK 465     THR G    17                                                      
REMARK 465     TYR G    61                                                      
REMARK 465     SER G    62                                                      
REMARK 465     SER G    63                                                      
REMARK 465     SER G    64                                                      
REMARK 465     PHE G    65                                                      
REMARK 465     CYS G    66                                                      
REMARK 465     THR G    67                                                      
REMARK 465     HIS G    68                                                      
REMARK 465     ASP G    69                                                      
REMARK 465     ARG G    70                                                      
REMARK 465     ASN G    71                                                      
REMARK 465     THR G    72                                                      
REMARK 465     MET G    73                                                      
REMARK 465     GLU G    74                                                      
REMARK 465     LYS G   192                                                      
REMARK 465     ALA G   193                                                      
REMARK 465     SER G   194                                                      
REMARK 465     MET H     0                                                      
REMARK 465     ARG H     1                                                      
REMARK 465     GLY H     2                                                      
REMARK 465     SER H     3                                                      
REMARK 465     HIS H     4                                                      
REMARK 465     HIS H     5                                                      
REMARK 465     HIS H     6                                                      
REMARK 465     HIS H     7                                                      
REMARK 465     HIS H     8                                                      
REMARK 465     HIS H     9                                                      
REMARK 465     LEU H    10                                                      
REMARK 465     VAL H    11                                                      
REMARK 465     PRO H    12                                                      
REMARK 465     ARG H    13                                                      
REMARK 465     GLY H    14                                                      
REMARK 465     SER H    15                                                      
REMARK 465     LYS H    16                                                      
REMARK 465     THR H    17                                                      
REMARK 465     TYR H    61                                                      
REMARK 465     SER H    62                                                      
REMARK 465     SER H    63                                                      
REMARK 465     SER H    64                                                      
REMARK 465     PHE H    65                                                      
REMARK 465     CYS H    66                                                      
REMARK 465     THR H    67                                                      
REMARK 465     HIS H    68                                                      
REMARK 465     ASP H    69                                                      
REMARK 465     ARG H    70                                                      
REMARK 465     ASN H    71                                                      
REMARK 465     THR H    72                                                      
REMARK 465     MET H    73                                                      
REMARK 465     LYS H   192                                                      
REMARK 465     ALA H   193                                                      
REMARK 465     SER H   194                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NZ B LYS A    54     O    HOH A  2020              1.79            
REMARK 500   OG B SER C    33     O1BB TTP C   300              2.07            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     106 CLOSE CONTACTS                                
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH F  2048     O    HOH A  2049     1556     1.32            
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    ASP A  58   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG B  42   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ASP B  58   CB  -  CG  -  OD2 ANGL. DEV. =   7.7 DEGREES          
REMARK 500    CYS B  79   CA  -  CB  -  SG  ANGL. DEV. =  -7.4 DEGREES          
REMARK 500    ARG C 130   NE  -  CZ  -  NH1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG C 130   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ARG D 130   NE  -  CZ  -  NH1 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ARG D 130   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.9 DEGREES          
REMARK 500    ASP F  97   CB  -  CG  -  OD2 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    CYS G  79   CA  -  CB  -  SG  ANGL. DEV. =  -7.0 DEGREES          
REMARK 500    ARG H  42   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ASP H  58   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ARG B   18     GLY B   19                   50.12                    
REMARK 500 SER B   64     PHE B   65                   44.54                    
REMARK 500 PHE B  190     LYS B  191                  109.26                    
REMARK 500 PHE H  190     LYS H  191                  144.20                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ALA H  75        11.8      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 400  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 153   SG                                                     
REMARK 620 2 CYS A 185   SG  116.7                                              
REMARK 620 3 CYS A 156   SG  112.8 107.2                                        
REMARK 620 4 CYS A 188   SG  102.4 104.5 113.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 400  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 185   SG                                                     
REMARK 620 2 CYS B 188   SG  102.1                                              
REMARK 620 3 CYS B 153   SG  117.4 105.9                                        
REMARK 620 4 CYS B 156   SG  107.6 110.1 113.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 400  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 153   SG                                                     
REMARK 620 2 CYS C 156   SG  113.3                                              
REMARK 620 3 CYS C 185   SG  116.7 107.5                                        
REMARK 620 4 CYS C 188   SG  103.3 111.8 103.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 400  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 156   SG                                                     
REMARK 620 2 CYS D 185   SG  107.6                                              
REMARK 620 3 CYS D 188   SG  112.6 103.0                                        
REMARK 620 4 CYS D 153   SG  112.3 116.0 105.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E 400  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS E 156   SG                                                     
REMARK 620 2 CYS E 185   SG  107.0                                              
REMARK 620 3 CYS E 188   SG  110.7 103.7                                        
REMARK 620 4 CYS E 153   SG  115.5 117.5 101.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F 400  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F 153   SG                                                     
REMARK 620 2 CYS F 156   SG  112.7                                              
REMARK 620 3 CYS F 185   SG  117.2 106.6                                        
REMARK 620 4 CYS F 188   SG  104.4 111.5 104.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G 400  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS G 188   SG                                                     
REMARK 620 2 CYS G 153   SG  106.0                                              
REMARK 620 3 CYS G 156   SG  111.1 112.9                                        
REMARK 620 4 CYS G 185   SG  102.0 117.8 106.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN H 400  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS H 185   SG                                                     
REMARK 620 2 CYS H 188   SG  102.2                                              
REMARK 620 3 CYS H 153   SG  118.4 104.0                                        
REMARK 620 4 CYS H 156   SG  107.9 113.1 111.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN C 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN D 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN E 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN F 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN G 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN H 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP A 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP B 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP C 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP D 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP E 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTU E1193                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP F 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP G 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP H 300                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 CONSTRUCT CONSISTS OF RESIDUES 15-194 OF THE NATIVE                  
REMARK 999 PROTEIN PLUS AN N-TERMINAL EXTENSION OF 15 RESIDUES                  
REMARK 999 CONTAINING A HIS6-TAG                                                
DBREF  1W4R A   15   194  UNP    P04183   KITH_HUMAN      15    194             
DBREF  1W4R B   15   194  UNP    P04183   KITH_HUMAN      15    194             
DBREF  1W4R C   15   194  UNP    P04183   KITH_HUMAN      15    194             
DBREF  1W4R D   15   194  UNP    P04183   KITH_HUMAN      15    194             
DBREF  1W4R E   15   194  UNP    P04183   KITH_HUMAN      15    194             
DBREF  1W4R F   15   194  UNP    P04183   KITH_HUMAN      15    194             
DBREF  1W4R G   15   194  UNP    P04183   KITH_HUMAN      15    194             
DBREF  1W4R H   15   194  UNP    P04183   KITH_HUMAN      15    194             
SEQADV 1W4R MET A    0  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R ARG A    1  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R GLY A    2  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R SER A    3  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS A    4  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS A    5  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS A    6  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS A    7  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS A    8  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS A    9  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R LEU A   10  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R VAL A   11  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R PRO A   12  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R ARG A   13  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R GLY A   14  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R MET B    0  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R ARG B    1  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R GLY B    2  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R SER B    3  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS B    4  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS B    5  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS B    6  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS B    7  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS B    8  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS B    9  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R LEU B   10  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R VAL B   11  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R PRO B   12  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R ARG B   13  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R GLY B   14  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R MET C    0  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R ARG C    1  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R GLY C    2  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R SER C    3  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS C    4  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS C    5  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS C    6  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS C    7  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS C    8  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS C    9  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R LEU C   10  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R VAL C   11  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R PRO C   12  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R ARG C   13  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R GLY C   14  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R MET D    0  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R ARG D    1  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R GLY D    2  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R SER D    3  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS D    4  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS D    5  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS D    6  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS D    7  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS D    8  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS D    9  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R LEU D   10  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R VAL D   11  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R PRO D   12  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R ARG D   13  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R GLY D   14  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R MET E    0  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R ARG E    1  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R GLY E    2  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R SER E    3  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS E    4  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS E    5  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS E    6  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS E    7  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS E    8  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS E    9  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R LEU E   10  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R VAL E   11  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R PRO E   12  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R ARG E   13  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R GLY E   14  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R MET F    0  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R ARG F    1  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R GLY F    2  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R SER F    3  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS F    4  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS F    5  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS F    6  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS F    7  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS F    8  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS F    9  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R LEU F   10  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R VAL F   11  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R PRO F   12  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R ARG F   13  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R GLY F   14  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R MET G    0  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R ARG G    1  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R GLY G    2  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R SER G    3  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS G    4  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS G    5  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS G    6  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS G    7  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS G    8  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS G    9  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R LEU G   10  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R VAL G   11  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R PRO G   12  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R ARG G   13  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R GLY G   14  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R MET H    0  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R ARG H    1  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R GLY H    2  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R SER H    3  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS H    4  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS H    5  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS H    6  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS H    7  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS H    8  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R HIS H    9  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R LEU H   10  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R VAL H   11  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R PRO H   12  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R ARG H   13  UNP  P04183              EXPRESSION TAG                 
SEQADV 1W4R GLY H   14  UNP  P04183              EXPRESSION TAG                 
SEQRES   1 A  195  MET ARG GLY SER HIS HIS HIS HIS HIS HIS LEU VAL PRO          
SEQRES   2 A  195  ARG GLY SER LYS THR ARG GLY GLN ILE GLN VAL ILE LEU          
SEQRES   3 A  195  GLY PRO MET PHE SER GLY LYS SER THR GLU LEU MET ARG          
SEQRES   4 A  195  ARG VAL ARG ARG PHE GLN ILE ALA GLN TYR LYS CYS LEU          
SEQRES   5 A  195  VAL ILE LYS TYR ALA LYS ASP THR ARG TYR SER SER SER          
SEQRES   6 A  195  PHE CYS THR HIS ASP ARG ASN THR MET GLU ALA LEU PRO          
SEQRES   7 A  195  ALA CYS LEU LEU ARG ASP VAL ALA GLN GLU ALA LEU GLY          
SEQRES   8 A  195  VAL ALA VAL ILE GLY ILE ASP GLU GLY GLN PHE PHE PRO          
SEQRES   9 A  195  ASP ILE VAL GLU PHE CYS GLU ALA MET ALA ASN ALA GLY          
SEQRES  10 A  195  LYS THR VAL ILE VAL ALA ALA LEU ASP GLY THR PHE GLN          
SEQRES  11 A  195  ARG LYS PRO PHE GLY ALA ILE LEU ASN LEU VAL PRO LEU          
SEQRES  12 A  195  ALA GLU SER VAL VAL LYS LEU THR ALA VAL CYS MET GLU          
SEQRES  13 A  195  CYS PHE ARG GLU ALA ALA TYR THR LYS ARG LEU GLY THR          
SEQRES  14 A  195  GLU LYS GLU VAL GLU VAL ILE GLY GLY ALA ASP LYS TYR          
SEQRES  15 A  195  HIS SER VAL CYS ARG LEU CYS TYR PHE LYS LYS ALA SER          
SEQRES   1 B  195  MET ARG GLY SER HIS HIS HIS HIS HIS HIS LEU VAL PRO          
SEQRES   2 B  195  ARG GLY SER LYS THR ARG GLY GLN ILE GLN VAL ILE LEU          
SEQRES   3 B  195  GLY PRO MET PHE SER GLY LYS SER THR GLU LEU MET ARG          
SEQRES   4 B  195  ARG VAL ARG ARG PHE GLN ILE ALA GLN TYR LYS CYS LEU          
SEQRES   5 B  195  VAL ILE LYS TYR ALA LYS ASP THR ARG TYR SER SER SER          
SEQRES   6 B  195  PHE CYS THR HIS ASP ARG ASN THR MET GLU ALA LEU PRO          
SEQRES   7 B  195  ALA CYS LEU LEU ARG ASP VAL ALA GLN GLU ALA LEU GLY          
SEQRES   8 B  195  VAL ALA VAL ILE GLY ILE ASP GLU GLY GLN PHE PHE PRO          
SEQRES   9 B  195  ASP ILE VAL GLU PHE CYS GLU ALA MET ALA ASN ALA GLY          
SEQRES  10 B  195  LYS THR VAL ILE VAL ALA ALA LEU ASP GLY THR PHE GLN          
SEQRES  11 B  195  ARG LYS PRO PHE GLY ALA ILE LEU ASN LEU VAL PRO LEU          
SEQRES  12 B  195  ALA GLU SER VAL VAL LYS LEU THR ALA VAL CYS MET GLU          
SEQRES  13 B  195  CYS PHE ARG GLU ALA ALA TYR THR LYS ARG LEU GLY THR          
SEQRES  14 B  195  GLU LYS GLU VAL GLU VAL ILE GLY GLY ALA ASP LYS TYR          
SEQRES  15 B  195  HIS SER VAL CYS ARG LEU CYS TYR PHE LYS LYS ALA SER          
SEQRES   1 C  195  MET ARG GLY SER HIS HIS HIS HIS HIS HIS LEU VAL PRO          
SEQRES   2 C  195  ARG GLY SER LYS THR ARG GLY GLN ILE GLN VAL ILE LEU          
SEQRES   3 C  195  GLY PRO MET PHE SER GLY LYS SER THR GLU LEU MET ARG          
SEQRES   4 C  195  ARG VAL ARG ARG PHE GLN ILE ALA GLN TYR LYS CYS LEU          
SEQRES   5 C  195  VAL ILE LYS TYR ALA LYS ASP THR ARG TYR SER SER SER          
SEQRES   6 C  195  PHE CYS THR HIS ASP ARG ASN THR MET GLU ALA LEU PRO          
SEQRES   7 C  195  ALA CYS LEU LEU ARG ASP VAL ALA GLN GLU ALA LEU GLY          
SEQRES   8 C  195  VAL ALA VAL ILE GLY ILE ASP GLU GLY GLN PHE PHE PRO          
SEQRES   9 C  195  ASP ILE VAL GLU PHE CYS GLU ALA MET ALA ASN ALA GLY          
SEQRES  10 C  195  LYS THR VAL ILE VAL ALA ALA LEU ASP GLY THR PHE GLN          
SEQRES  11 C  195  ARG LYS PRO PHE GLY ALA ILE LEU ASN LEU VAL PRO LEU          
SEQRES  12 C  195  ALA GLU SER VAL VAL LYS LEU THR ALA VAL CYS MET GLU          
SEQRES  13 C  195  CYS PHE ARG GLU ALA ALA TYR THR LYS ARG LEU GLY THR          
SEQRES  14 C  195  GLU LYS GLU VAL GLU VAL ILE GLY GLY ALA ASP LYS TYR          
SEQRES  15 C  195  HIS SER VAL CYS ARG LEU CYS TYR PHE LYS LYS ALA SER          
SEQRES   1 D  195  MET ARG GLY SER HIS HIS HIS HIS HIS HIS LEU VAL PRO          
SEQRES   2 D  195  ARG GLY SER LYS THR ARG GLY GLN ILE GLN VAL ILE LEU          
SEQRES   3 D  195  GLY PRO MET PHE SER GLY LYS SER THR GLU LEU MET ARG          
SEQRES   4 D  195  ARG VAL ARG ARG PHE GLN ILE ALA GLN TYR LYS CYS LEU          
SEQRES   5 D  195  VAL ILE LYS TYR ALA LYS ASP THR ARG TYR SER SER SER          
SEQRES   6 D  195  PHE CYS THR HIS ASP ARG ASN THR MET GLU ALA LEU PRO          
SEQRES   7 D  195  ALA CYS LEU LEU ARG ASP VAL ALA GLN GLU ALA LEU GLY          
SEQRES   8 D  195  VAL ALA VAL ILE GLY ILE ASP GLU GLY GLN PHE PHE PRO          
SEQRES   9 D  195  ASP ILE VAL GLU PHE CYS GLU ALA MET ALA ASN ALA GLY          
SEQRES  10 D  195  LYS THR VAL ILE VAL ALA ALA LEU ASP GLY THR PHE GLN          
SEQRES  11 D  195  ARG LYS PRO PHE GLY ALA ILE LEU ASN LEU VAL PRO LEU          
SEQRES  12 D  195  ALA GLU SER VAL VAL LYS LEU THR ALA VAL CYS MET GLU          
SEQRES  13 D  195  CYS PHE ARG GLU ALA ALA TYR THR LYS ARG LEU GLY THR          
SEQRES  14 D  195  GLU LYS GLU VAL GLU VAL ILE GLY GLY ALA ASP LYS TYR          
SEQRES  15 D  195  HIS SER VAL CYS ARG LEU CYS TYR PHE LYS LYS ALA SER          
SEQRES   1 E  195  MET ARG GLY SER HIS HIS HIS HIS HIS HIS LEU VAL PRO          
SEQRES   2 E  195  ARG GLY SER LYS THR ARG GLY GLN ILE GLN VAL ILE LEU          
SEQRES   3 E  195  GLY PRO MET PHE SER GLY LYS SER THR GLU LEU MET ARG          
SEQRES   4 E  195  ARG VAL ARG ARG PHE GLN ILE ALA GLN TYR LYS CYS LEU          
SEQRES   5 E  195  VAL ILE LYS TYR ALA LYS ASP THR ARG TYR SER SER SER          
SEQRES   6 E  195  PHE CYS THR HIS ASP ARG ASN THR MET GLU ALA LEU PRO          
SEQRES   7 E  195  ALA CYS LEU LEU ARG ASP VAL ALA GLN GLU ALA LEU GLY          
SEQRES   8 E  195  VAL ALA VAL ILE GLY ILE ASP GLU GLY GLN PHE PHE PRO          
SEQRES   9 E  195  ASP ILE VAL GLU PHE CYS GLU ALA MET ALA ASN ALA GLY          
SEQRES  10 E  195  LYS THR VAL ILE VAL ALA ALA LEU ASP GLY THR PHE GLN          
SEQRES  11 E  195  ARG LYS PRO PHE GLY ALA ILE LEU ASN LEU VAL PRO LEU          
SEQRES  12 E  195  ALA GLU SER VAL VAL LYS LEU THR ALA VAL CYS MET GLU          
SEQRES  13 E  195  CYS PHE ARG GLU ALA ALA TYR THR LYS ARG LEU GLY THR          
SEQRES  14 E  195  GLU LYS GLU VAL GLU VAL ILE GLY GLY ALA ASP LYS TYR          
SEQRES  15 E  195  HIS SER VAL CYS ARG LEU CYS TYR PHE LYS LYS ALA SER          
SEQRES   1 F  195  MET ARG GLY SER HIS HIS HIS HIS HIS HIS LEU VAL PRO          
SEQRES   2 F  195  ARG GLY SER LYS THR ARG GLY GLN ILE GLN VAL ILE LEU          
SEQRES   3 F  195  GLY PRO MET PHE SER GLY LYS SER THR GLU LEU MET ARG          
SEQRES   4 F  195  ARG VAL ARG ARG PHE GLN ILE ALA GLN TYR LYS CYS LEU          
SEQRES   5 F  195  VAL ILE LYS TYR ALA LYS ASP THR ARG TYR SER SER SER          
SEQRES   6 F  195  PHE CYS THR HIS ASP ARG ASN THR MET GLU ALA LEU PRO          
SEQRES   7 F  195  ALA CYS LEU LEU ARG ASP VAL ALA GLN GLU ALA LEU GLY          
SEQRES   8 F  195  VAL ALA VAL ILE GLY ILE ASP GLU GLY GLN PHE PHE PRO          
SEQRES   9 F  195  ASP ILE VAL GLU PHE CYS GLU ALA MET ALA ASN ALA GLY          
SEQRES  10 F  195  LYS THR VAL ILE VAL ALA ALA LEU ASP GLY THR PHE GLN          
SEQRES  11 F  195  ARG LYS PRO PHE GLY ALA ILE LEU ASN LEU VAL PRO LEU          
SEQRES  12 F  195  ALA GLU SER VAL VAL LYS LEU THR ALA VAL CYS MET GLU          
SEQRES  13 F  195  CYS PHE ARG GLU ALA ALA TYR THR LYS ARG LEU GLY THR          
SEQRES  14 F  195  GLU LYS GLU VAL GLU VAL ILE GLY GLY ALA ASP LYS TYR          
SEQRES  15 F  195  HIS SER VAL CYS ARG LEU CYS TYR PHE LYS LYS ALA SER          
SEQRES   1 G  195  MET ARG GLY SER HIS HIS HIS HIS HIS HIS LEU VAL PRO          
SEQRES   2 G  195  ARG GLY SER LYS THR ARG GLY GLN ILE GLN VAL ILE LEU          
SEQRES   3 G  195  GLY PRO MET PHE SER GLY LYS SER THR GLU LEU MET ARG          
SEQRES   4 G  195  ARG VAL ARG ARG PHE GLN ILE ALA GLN TYR LYS CYS LEU          
SEQRES   5 G  195  VAL ILE LYS TYR ALA LYS ASP THR ARG TYR SER SER SER          
SEQRES   6 G  195  PHE CYS THR HIS ASP ARG ASN THR MET GLU ALA LEU PRO          
SEQRES   7 G  195  ALA CYS LEU LEU ARG ASP VAL ALA GLN GLU ALA LEU GLY          
SEQRES   8 G  195  VAL ALA VAL ILE GLY ILE ASP GLU GLY GLN PHE PHE PRO          
SEQRES   9 G  195  ASP ILE VAL GLU PHE CYS GLU ALA MET ALA ASN ALA GLY          
SEQRES  10 G  195  LYS THR VAL ILE VAL ALA ALA LEU ASP GLY THR PHE GLN          
SEQRES  11 G  195  ARG LYS PRO PHE GLY ALA ILE LEU ASN LEU VAL PRO LEU          
SEQRES  12 G  195  ALA GLU SER VAL VAL LYS LEU THR ALA VAL CYS MET GLU          
SEQRES  13 G  195  CYS PHE ARG GLU ALA ALA TYR THR LYS ARG LEU GLY THR          
SEQRES  14 G  195  GLU LYS GLU VAL GLU VAL ILE GLY GLY ALA ASP LYS TYR          
SEQRES  15 G  195  HIS SER VAL CYS ARG LEU CYS TYR PHE LYS LYS ALA SER          
SEQRES   1 H  195  MET ARG GLY SER HIS HIS HIS HIS HIS HIS LEU VAL PRO          
SEQRES   2 H  195  ARG GLY SER LYS THR ARG GLY GLN ILE GLN VAL ILE LEU          
SEQRES   3 H  195  GLY PRO MET PHE SER GLY LYS SER THR GLU LEU MET ARG          
SEQRES   4 H  195  ARG VAL ARG ARG PHE GLN ILE ALA GLN TYR LYS CYS LEU          
SEQRES   5 H  195  VAL ILE LYS TYR ALA LYS ASP THR ARG TYR SER SER SER          
SEQRES   6 H  195  PHE CYS THR HIS ASP ARG ASN THR MET GLU ALA LEU PRO          
SEQRES   7 H  195  ALA CYS LEU LEU ARG ASP VAL ALA GLN GLU ALA LEU GLY          
SEQRES   8 H  195  VAL ALA VAL ILE GLY ILE ASP GLU GLY GLN PHE PHE PRO          
SEQRES   9 H  195  ASP ILE VAL GLU PHE CYS GLU ALA MET ALA ASN ALA GLY          
SEQRES  10 H  195  LYS THR VAL ILE VAL ALA ALA LEU ASP GLY THR PHE GLN          
SEQRES  11 H  195  ARG LYS PRO PHE GLY ALA ILE LEU ASN LEU VAL PRO LEU          
SEQRES  12 H  195  ALA GLU SER VAL VAL LYS LEU THR ALA VAL CYS MET GLU          
SEQRES  13 H  195  CYS PHE ARG GLU ALA ALA TYR THR LYS ARG LEU GLY THR          
SEQRES  14 H  195  GLU LYS GLU VAL GLU VAL ILE GLY GLY ALA ASP LYS TYR          
SEQRES  15 H  195  HIS SER VAL CYS ARG LEU CYS TYR PHE LYS LYS ALA SER          
HET     ZN  A 400       1                                                       
HET     ZN  B 400       1                                                       
HET     ZN  C 400       1                                                       
HET     ZN  D 400       1                                                       
HET     ZN  E 400       1                                                       
HET     ZN  F 400       1                                                       
HET     ZN  G 400       1                                                       
HET     ZN  H 400       1                                                       
HET    TTP  A 300      58                                                       
HET    TTP  B 300      58                                                       
HET    TTP  C 300      58                                                       
HET    TTP  D 300      58                                                       
HET    TTP  E 300      58                                                       
HET    DTU  E1193       8                                                       
HET    TTP  F 300      58                                                       
HET    TTP  G 300      58                                                       
HET    TTP  H 300      58                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     TTP THYMIDINE-5'-TRIPHOSPHATE                                        
HETNAM     DTU (2R,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL                            
FORMUL   9   ZN    8(ZN 2+)                                                     
FORMUL  10  TTP    8(C10 H17 N2 O14 P3)                                         
FORMUL  11  DTU    C4 H10 O2 S2                                                 
FORMUL  12  HOH   *794(H2 O1)                                                   
HELIX    1   1 GLY A   31  ALA A   46  1                                  16    
HELIX    2   2 ARG A   60  SER A   64  5                                   5    
HELIX    3   3 CYS A   66  MET A   73  1                                   8    
HELIX    4   4 LEU A   80  ASP A   83  5                                   4    
HELIX    5   5 VAL A   84  GLY A   90  1                                   7    
HELIX    6   6 GLU A   98  PHE A  102  5                                   5    
HELIX    7   7 ASP A  104  ALA A  115  1                                  12    
HELIX    8   8 ALA A  135  ALA A  143  5                                   9    
HELIX    9   9 CYS A  185  PHE A  190  1                                   6    
HELIX   10  10 GLY B   31  ILE B   45  1                                  15    
HELIX   11  11 ARG B   60  SER B   64  5                                   5    
HELIX   12  12 LEU B   80  ASP B   83  5                                   4    
HELIX   13  13 VAL B   84  GLY B   90  1                                   7    
HELIX   14  14 GLY B   99  PHE B  102  5                                   4    
HELIX   15  15 ASP B  104  ALA B  115  1                                  12    
HELIX   16  16 ALA B  135  ALA B  143  5                                   9    
HELIX   17  17 CYS B  185  LYS B  191  1                                   7    
HELIX   18  18 GLY C   31  ILE C   45  1                                  15    
HELIX   19  19 LEU C   80  ASP C   83  5                                   4    
HELIX   20  20 VAL C   84  GLY C   90  1                                   7    
HELIX   21  21 GLU C   98  PHE C  102  5                                   5    
HELIX   22  22 ASP C  104  ALA C  115  1                                  12    
HELIX   23  23 ALA C  135  ALA C  143  5                                   9    
HELIX   24  24 CYS C  185  PHE C  190  1                                   6    
HELIX   25  25 GLY D   31  ALA D   46  1                                  16    
HELIX   26  26 LEU D   80  ASP D   83  5                                   4    
HELIX   27  27 VAL D   84  GLY D   90  1                                   7    
HELIX   28  28 GLU D   98  PHE D  102  5                                   5    
HELIX   29  29 ASP D  104  ALA D  115  1                                  12    
HELIX   30  30 ALA D  135  ALA D  143  5                                   9    
HELIX   31  31 CYS D  185  PHE D  190  1                                   6    
HELIX   32  32 GLY E   31  ILE E   45  1                                  15    
HELIX   33  33 LEU E   80  ASP E   83  5                                   4    
HELIX   34  34 VAL E   84  GLY E   90  1                                   7    
HELIX   35  35 GLU E   98  PHE E  102  5                                   5    
HELIX   36  36 ASP E  104  ALA E  115  1                                  12    
HELIX   37  37 ALA E  135  ALA E  143  5                                   9    
HELIX   38  38 CYS E  185  PHE E  190  1                                   6    
HELIX   39  39 GLY F   31  ALA F   46  1                                  16    
HELIX   40  40 LEU F   80  ASP F   83  5                                   4    
HELIX   41  41 VAL F   84  GLY F   90  1                                   7    
HELIX   42  42 GLU F   98  PHE F  102  5                                   5    
HELIX   43  43 ASP F  104  ALA F  115  1                                  12    
HELIX   44  44 ALA F  135  ALA F  143  5                                   9    
HELIX   45  45 CYS F  185  PHE F  190  1                                   6    
HELIX   46  46 GLY G   31  ALA G   46  1                                  16    
HELIX   47  47 LEU G   80  ASP G   83  5                                   4    
HELIX   48  48 VAL G   84  GLY G   90  1                                   7    
HELIX   49  49 GLU G   98  PHE G  102  5                                   5    
HELIX   50  50 ASP G  104  ALA G  115  1                                  12    
HELIX   51  51 ALA G  135  ALA G  143  5                                   9    
HELIX   52  52 CYS G  185  PHE G  190  1                                   6    
HELIX   53  53 GLY H   31  ALA H   46  1                                  16    
HELIX   54  54 LEU H   80  ASP H   83  5                                   4    
HELIX   55  55 VAL H   84  GLY H   90  1                                   7    
HELIX   56  56 GLU H   98  PHE H  102  5                                   5    
HELIX   57  57 ASP H  104  ALA H  115  1                                  12    
HELIX   58  58 ALA H  135  ALA H  143  5                                   9    
HELIX   59  59 CYS H  185  PHE H  190  1                                   6    
SHEET    1  AA 6 GLU A  74  ALA A  78  0                                        
SHEET    2  AA 6 CYS A  50  TYR A  55  1  O  CYS A  50   N  GLU A  74           
SHEET    3  AA 6 VAL A  93  ILE A  96  1  O  VAL A  93   N  LEU A  51           
SHEET    4  AA 6 THR A 118  LEU A 124  1  O  THR A 118   N  ILE A  94           
SHEET    5  AA 6 GLN A  20  GLY A  26  1  O  GLN A  20   N  VAL A 119           
SHEET    6  AA 6 SER A 145  LYS A 148  1  O  SER A 145   N  VAL A  23           
SHEET    1  AB 2 ALA A 151  VAL A 152  0                                        
SHEET    2  AB 2 GLU A 159  ALA A 160 -1  O  ALA A 160   N  ALA A 151           
SHEET    1  AC 2 TYR A 162  ARG A 165  0                                        
SHEET    2  AC 2 TYR A 181  VAL A 184 -1  O  HIS A 182   N  LYS A 164           
SHEET    1  BA 6 GLU B  74  ALA B  78  0                                        
SHEET    2  BA 6 CYS B  50  TYR B  55  1  O  CYS B  50   N  GLU B  74           
SHEET    3  BA 6 VAL B  93  ASP B  97  1  O  VAL B  93   N  LEU B  51           
SHEET    4  BA 6 THR B 118  LEU B 124  1  O  THR B 118   N  ILE B  94           
SHEET    5  BA 6 GLN B  20  GLY B  26  1  O  GLN B  20   N  VAL B 119           
SHEET    6  BA 6 SER B 145  LYS B 148  1  O  SER B 145   N  VAL B  23           
SHEET    1  BB 2 ALA B 151  VAL B 152  0                                        
SHEET    2  BB 2 GLU B 159  ALA B 160 -1  O  ALA B 160   N  ALA B 151           
SHEET    1  BC 2 TYR B 162  ARG B 165  0                                        
SHEET    2  BC 2 TYR B 181  VAL B 184 -1  O  HIS B 182   N  LYS B 164           
SHEET    1  CA 6 LEU C  76  ALA C  78  0                                        
SHEET    2  CA 6 CYS C  50  TYR C  55  1  O  VAL C  52   N  LEU C  76           
SHEET    3  CA 6 VAL C  93  ASP C  97  1  O  VAL C  93   N  LEU C  51           
SHEET    4  CA 6 THR C 118  LEU C 124  1  O  THR C 118   N  ILE C  94           
SHEET    5  CA 6 GLN C  20  GLY C  26  1  O  GLN C  20   N  VAL C 119           
SHEET    6  CA 6 SER C 145  LYS C 148  1  O  SER C 145   N  VAL C  23           
SHEET    1  CB 2 ALA C 151  VAL C 152  0                                        
SHEET    2  CB 2 GLU C 159  ALA C 160 -1  O  ALA C 160   N  ALA C 151           
SHEET    1  CC 2 TYR C 162  ARG C 165  0                                        
SHEET    2  CC 2 TYR C 181  VAL C 184 -1  O  HIS C 182   N  LYS C 164           
SHEET    1  DA 6 LEU D  76  ALA D  78  0                                        
SHEET    2  DA 6 CYS D  50  TYR D  55  1  O  VAL D  52   N  LEU D  76           
SHEET    3  DA 6 VAL D  93  ILE D  96  1  O  VAL D  93   N  LEU D  51           
SHEET    4  DA 6 THR D 118  LEU D 124  1  O  THR D 118   N  ILE D  94           
SHEET    5  DA 6 GLN D  20  GLY D  26  1  O  GLN D  20   N  VAL D 119           
SHEET    6  DA 6 SER D 145  LYS D 148  1  O  SER D 145   N  VAL D  23           
SHEET    1  DB 2 ALA D 151  VAL D 152  0                                        
SHEET    2  DB 2 GLU D 159  ALA D 160 -1  O  ALA D 160   N  ALA D 151           
SHEET    1  DC 2 TYR D 162  ARG D 165  0                                        
SHEET    2  DC 2 TYR D 181  VAL D 184 -1  O  HIS D 182   N  LYS D 164           
SHEET    1  EA 6 LEU E  76  ALA E  78  0                                        
SHEET    2  EA 6 CYS E  50  TYR E  55  1  O  VAL E  52   N  LEU E  76           
SHEET    3  EA 6 VAL E  93  ILE E  96  1  O  VAL E  93   N  LEU E  51           
SHEET    4  EA 6 THR E 118  LEU E 124  1  O  THR E 118   N  ILE E  94           
SHEET    5  EA 6 GLN E  20  GLY E  26  1  O  GLN E  20   N  VAL E 119           
SHEET    6  EA 6 SER E 145  LYS E 148  1  O  SER E 145   N  VAL E  23           
SHEET    1  EB 2 ALA E 151  VAL E 152  0                                        
SHEET    2  EB 2 GLU E 159  ALA E 160 -1  O  ALA E 160   N  ALA E 151           
SHEET    1  EC 2 TYR E 162  ARG E 165  0                                        
SHEET    2  EC 2 TYR E 181  VAL E 184 -1  O  HIS E 182   N  LYS E 164           
SHEET    1  FA 6 LEU F  76  ALA F  78  0                                        
SHEET    2  FA 6 CYS F  50  TYR F  55  1  O  VAL F  52   N  LEU F  76           
SHEET    3  FA 6 VAL F  93  ILE F  96  1  O  VAL F  93   N  LEU F  51           
SHEET    4  FA 6 THR F 118  LEU F 124  1  O  THR F 118   N  ILE F  94           
SHEET    5  FA 6 GLN F  20  GLY F  26  1  O  GLN F  20   N  VAL F 119           
SHEET    6  FA 6 SER F 145  LYS F 148  1  O  SER F 145   N  VAL F  23           
SHEET    1  FB 2 ALA F 151  VAL F 152  0                                        
SHEET    2  FB 2 GLU F 159  ALA F 160 -1  O  ALA F 160   N  ALA F 151           
SHEET    1  FC 2 TYR F 162  ARG F 165  0                                        
SHEET    2  FC 2 TYR F 181  VAL F 184 -1  O  HIS F 182   N  LYS F 164           
SHEET    1  GA 6 LEU G  76  ALA G  78  0                                        
SHEET    2  GA 6 CYS G  50  TYR G  55  1  O  VAL G  52   N  LEU G  76           
SHEET    3  GA 6 VAL G  93  ILE G  96  1  O  VAL G  93   N  LEU G  51           
SHEET    4  GA 6 THR G 118  LEU G 124  1  O  THR G 118   N  ILE G  94           
SHEET    5  GA 6 GLN G  20  GLY G  26  1  O  GLN G  20   N  VAL G 119           
SHEET    6  GA 6 SER G 145  LYS G 148  1  O  SER G 145   N  VAL G  23           
SHEET    1  GB 2 ALA G 151  VAL G 152  0                                        
SHEET    2  GB 2 GLU G 159  ALA G 160 -1  O  ALA G 160   N  ALA G 151           
SHEET    1  GC 2 TYR G 162  ARG G 165  0                                        
SHEET    2  GC 2 TYR G 181  VAL G 184 -1  O  HIS G 182   N  LYS G 164           
SHEET    1  HA 6 ALA H  75  ALA H  78  0                                        
SHEET    2  HA 6 CYS H  50  TYR H  55  1  O  VAL H  52   N  LEU H  76           
SHEET    3  HA 6 VAL H  93  ASP H  97  1  O  VAL H  93   N  LEU H  51           
SHEET    4  HA 6 THR H 118  LEU H 124  1  O  THR H 118   N  ILE H  94           
SHEET    5  HA 6 GLN H  20  GLY H  26  1  O  GLN H  20   N  VAL H 119           
SHEET    6  HA 6 SER H 145  LYS H 148  1  O  SER H 145   N  VAL H  23           
SHEET    1  HB 2 ALA H 151  VAL H 152  0                                        
SHEET    2  HB 2 GLU H 159  ALA H 160 -1  O  ALA H 160   N  ALA H 151           
SHEET    1  HC 2 TYR H 162  ARG H 165  0                                        
SHEET    2  HC 2 TYR H 181  VAL H 184 -1  O  HIS H 182   N  LYS H 164           
LINK         OG BSER A  33                 O1BBTTP A 300     1555   1555  2.03  
LINK        ZN    ZN A 400                 SG  CYS A 185     1555   1555  2.32  
LINK        ZN    ZN A 400                 SG  CYS A 156     1555   1555  2.27  
LINK        ZN    ZN A 400                 SG  CYS A 188     1555   1555  2.32  
LINK        ZN    ZN A 400                 SG  CYS A 153     1555   1555  2.35  
LINK        ZN    ZN B 400                 SG  CYS B 188     1555   1555  2.35  
LINK        ZN    ZN B 400                 SG  CYS B 153     1555   1555  2.32  
LINK        ZN    ZN B 400                 SG  CYS B 156     1555   1555  2.27  
LINK        ZN    ZN B 400                 SG  CYS B 185     1555   1555  2.31  
LINK        ZN    ZN C 400                 SG  CYS C 156     1555   1555  2.27  
LINK        ZN    ZN C 400                 SG  CYS C 185     1555   1555  2.40  
LINK        ZN    ZN C 400                 SG  CYS C 188     1555   1555  2.31  
LINK        ZN    ZN C 400                 SG  CYS C 153     1555   1555  2.26  
LINK        ZN    ZN D 400                 SG  CYS D 185     1555   1555  2.43  
LINK        ZN    ZN D 400                 SG  CYS D 188     1555   1555  2.29  
LINK        ZN    ZN D 400                 SG  CYS D 153     1555   1555  2.32  
LINK        ZN    ZN D 400                 SG  CYS D 156     1555   1555  2.28  
LINK        ZN    ZN E 400                 SG  CYS E 188     1555   1555  2.38  
LINK        ZN    ZN E 400                 SG  CYS E 153     1555   1555  2.31  
LINK        ZN    ZN E 400                 SG  CYS E 185     1555   1555  2.36  
LINK        ZN    ZN E 400                 SG  CYS E 156     1555   1555  2.28  
LINK        ZN    ZN F 400                 SG  CYS F 185     1555   1555  2.38  
LINK        ZN    ZN F 400                 SG  CYS F 188     1555   1555  2.29  
LINK        ZN    ZN F 400                 SG  CYS F 156     1555   1555  2.32  
LINK        ZN    ZN F 400                 SG  CYS F 153     1555   1555  2.29  
LINK        ZN    ZN G 400                 SG  CYS G 156     1555   1555  2.28  
LINK        ZN    ZN G 400                 SG  CYS G 185     1555   1555  2.39  
LINK        ZN    ZN G 400                 SG  CYS G 153     1555   1555  2.29  
LINK        ZN    ZN G 400                 SG  CYS G 188     1555   1555  2.35  
LINK        ZN    ZN H 400                 SG  CYS H 153     1555   1555  2.31  
LINK        ZN    ZN H 400                 SG  CYS H 156     1555   1555  2.33  
LINK        ZN    ZN H 400                 SG  CYS H 188     1555   1555  2.38  
LINK        ZN    ZN H 400                 SG  CYS H 185     1555   1555  2.33  
SITE     1 AC1  4 CYS A 153  CYS A 156  CYS A 185  CYS A 188                    
SITE     1 AC2  4 CYS B 153  CYS B 156  CYS B 185  CYS B 188                    
SITE     1 AC3  4 CYS C 153  CYS C 156  CYS C 185  CYS C 188                    
SITE     1 AC4  4 CYS D 153  CYS D 156  CYS D 185  CYS D 188                    
SITE     1 AC5  4 CYS E 153  CYS E 156  CYS E 185  CYS E 188                    
SITE     1 AC6  4 CYS F 153  CYS F 156  CYS F 185  CYS F 188                    
SITE     1 AC7  4 CYS G 153  CYS G 156  CYS G 185  CYS G 188                    
SITE     1 AC8  4 CYS H 153  CYS H 156  CYS H 185  CYS H 188                    
SITE     1 AC9 25 MET A  28  PHE A  29  SER A  30  GLY A  31                    
SITE     2 AC9 25 LYS A  32  SER A  33  ASP A  58  ARG A  60                    
SITE     3 AC9 25 GLU A  98  PHE A 101  LEU A 124  THR A 127                    
SITE     4 AC9 25 PHE A 128  PHE A 133  VAL A 172  GLU A 173                    
SITE     5 AC9 25 VAL A 174  ILE A 175  GLY A 176  TYR A 181                    
SITE     6 AC9 25 HOH A2104  HOH A2105  HOH A2108  HOH A2109                    
SITE     7 AC9 25 HOH A2110                                                     
SITE     1 BC1 30 MET B  28  PHE B  29  SER B  30  GLY B  31                    
SITE     2 BC1 30 LYS B  32  SER B  33  ASP B  58  ARG B  60                    
SITE     3 BC1 30 GLU B  98  PHE B 101  LEU B 124  THR B 127                    
SITE     4 BC1 30 PHE B 128  PHE B 133  ARG B 165  VAL B 172                    
SITE     5 BC1 30 GLU B 173  VAL B 174  ILE B 175  GLY B 176                    
SITE     6 BC1 30 TYR B 181  HOH B2034  HOH B2100  HOH B2102                    
SITE     7 BC1 30 HOH B2103  HOH B2104  HOH B2105  HOH B2106                    
SITE     8 BC1 30 HOH B2107  HOH B2108                                          
SITE     1 BC2 27 PRO C  27  MET C  28  PHE C  29  SER C  30                    
SITE     2 BC2 27 GLY C  31  LYS C  32  SER C  33  ASP C  58                    
SITE     3 BC2 27 ARG C  60  GLU C  98  PHE C 101  LEU C 124                    
SITE     4 BC2 27 THR C 127  PHE C 128  PHE C 133  ARG C 165                    
SITE     5 BC2 27 VAL C 172  GLU C 173  VAL C 174  ILE C 175                    
SITE     6 BC2 27 GLY C 176  TYR C 181  HOH C2080  HOH C2081                    
SITE     7 BC2 27 HOH C2083  HOH C2084  HOH C2085                               
SITE     1 BC3 28 MET D  28  SER D  30  GLY D  31  LYS D  32                    
SITE     2 BC3 28 SER D  33  ASP D  58  ARG D  60  ASP D  97                    
SITE     3 BC3 28 GLU D  98  GLN D 100  PHE D 101  LEU D 124                    
SITE     4 BC3 28 THR D 127  PHE D 128  PHE D 133  VAL D 172                    
SITE     5 BC3 28 GLU D 173  VAL D 174  ILE D 175  GLY D 176                    
SITE     6 BC3 28 TYR D 181  HOH D2088  HOH D2089  HOH D2090                    
SITE     7 BC3 28 HOH D2092  HOH D2093  HOH D2094  HOH D2095                    
SITE     1 BC4 27 MET E  28  GLY E  31  LYS E  32  SER E  33                    
SITE     2 BC4 27 ASP E  58  ASP E  97  GLU E  98  GLN E 100                    
SITE     3 BC4 27 PHE E 101  LEU E 124  THR E 127  PHE E 128                    
SITE     4 BC4 27 PHE E 133  ARG E 165  VAL E 172  GLU E 173                    
SITE     5 BC4 27 VAL E 174  ILE E 175  GLY E 176  TYR E 181                    
SITE     6 BC4 27 HOH E2075  HOH E2076  HOH E2077  HOH E2078                    
SITE     7 BC4 27 HOH E2079  HOH E2080  HOH E2081                               
SITE     1 BC5  9 ARG B  82  ASP B 104  GLU B 107  ALA B 111                    
SITE     2 BC5  9 GLU E 110  ALA E 111  ASN E 114  HOH E2082                    
SITE     3 BC5  9 HOH E2083                                                     
SITE     1 BC6 29 MET F  28  SER F  30  GLY F  31  LYS F  32                    
SITE     2 BC6 29 SER F  33  ASP F  58  ARG F  60  ASP F  97                    
SITE     3 BC6 29 GLU F  98  GLN F 100  PHE F 101  LEU F 124                    
SITE     4 BC6 29 THR F 127  PHE F 128  PHE F 133  VAL F 172                    
SITE     5 BC6 29 GLU F 173  VAL F 174  ILE F 175  GLY F 176                    
SITE     6 BC6 29 TYR F 181  HOH F2109  HOH F2110  HOH F2111                    
SITE     7 BC6 29 HOH F2112  HOH F2113  HOH F2115  HOH F2116                    
SITE     8 BC6 29 HOH F2117                                                     
SITE     1 BC7 28 MET G  28  SER G  30  GLY G  31  LYS G  32                    
SITE     2 BC7 28 SER G  33  ASP G  58  ARG G  60  ASP G  97                    
SITE     3 BC7 28 GLU G  98  GLN G 100  PHE G 101  LEU G 124                    
SITE     4 BC7 28 THR G 127  PHE G 128  PHE G 133  VAL G 172                    
SITE     5 BC7 28 GLU G 173  VAL G 174  ILE G 175  GLY G 176                    
SITE     6 BC7 28 TYR G 181  HOH G2100  HOH G2101  HOH G2102                    
SITE     7 BC7 28 HOH G2103  HOH G2106  HOH G2107  HOH G2108                    
SITE     1 BC8 29 MET H  28  GLY H  31  LYS H  32  SER H  33                    
SITE     2 BC8 29 ASP H  58  ARG H  60  ASP H  97  GLU H  98                    
SITE     3 BC8 29 GLN H 100  PHE H 101  LEU H 124  THR H 127                    
SITE     4 BC8 29 PHE H 128  PHE H 133  ARG H 165  VAL H 172                    
SITE     5 BC8 29 GLU H 173  VAL H 174  ILE H 175  GLY H 176                    
SITE     6 BC8 29 TYR H 181  HOH H2081  HOH H2082  HOH H2083                    
SITE     7 BC8 29 HOH H2084  HOH H2085  HOH H2086  HOH H2087                    
SITE     8 BC8 29 HOH H2088                                                     
CRYST1  157.496  122.920  115.274  90.00 130.00  90.00 C 1 2 1      32          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006349  0.000000  0.005328        0.00000                         
SCALE2      0.000000  0.008135  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011324        0.00000                         
MTRIX1   1  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   1  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   1  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   2 -0.545498 -0.763843  0.344928      113.44400    1                    
MTRIX2   2 -0.755071  0.269291 -0.597788       83.06100    1                    
MTRIX3   2  0.363730 -0.586537 -0.723653       32.64100    1                    
MTRIX1   3 -0.873078  0.269500  0.406331       41.84300    1                    
MTRIX2   3  0.262291 -0.442909  0.857342      107.86600    1                    
MTRIX3   3  0.411021  0.855103  0.316007      -83.11700    1                    
MTRIX1   4  0.424704  0.487538 -0.762845      -20.77200    1                    
MTRIX2   4  0.485981 -0.833694 -0.262254      130.29900    1                    
MTRIX3   4 -0.763838 -0.259348 -0.591008       44.40900    1                    
MTRIX1   5 -0.261718 -0.138417 -0.955167       90.74300    1                    
MTRIX2   5  0.112513 -0.987290  0.112243      137.54600    1                    
MTRIX3   5 -0.958564 -0.078093  0.273966       -4.79000    1                    
MTRIX1   6 -0.283160  0.790217  0.543486      -42.47800    1                    
MTRIX2   6  0.798022 -0.120184  0.590522       54.69300    1                    
MTRIX3   6  0.531959  0.600926 -0.596580      -13.33100    1                    
MTRIX1   7 -0.141097 -0.171068  0.975104       -2.74100    1                    
MTRIX2   7 -0.942272  0.325330 -0.079272       68.10700    1                    
MTRIX3   7 -0.303669 -0.929998 -0.207096       70.16200    1                    
MTRIX1   8  0.674675 -0.480474 -0.560320       88.57000    1                    
MTRIX2   8  0.032427  0.777684 -0.627819       60.82600    1                    
MTRIX3   8  0.737402  0.405404  0.540264      -57.87200    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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