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Database: PDB
Entry: 2WVJ
LinkDB: 2WVJ
Original site: 2WVJ 
HEADER    TRANSFERASE                             17-OCT-09   2WVJ              
TITLE     MUTATION OF THR163 TO SER IN HUMAN THYMIDINE KINASE SHIFTS            
TITLE    2 THE SPECIFICITY FROM THYMIDINE TOWARDS THE NUCLEOSIDE                
TITLE    3 ANALOGUE AZIDOTHYMIDINE                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THYMIDINE KINASE, CYTOSOLIC;                               
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 FRAGMENT: RESIDUES 1-193;                                            
COMPND   5 SYNONYM: THYMIDINE KINASE 1;                                         
COMPND   6 EC: 2.7.1.21;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 OTHER_DETAILS: TTP FEEDBACK INHIBITOR                                
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: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGEX-2THUTK1-CDELTA41                     
KEYWDS    ZINC-BINDING DOMAIN, DEOXYRIBONUCLEOSIDE KINASE, FEEDBACK             
KEYWDS   2 INHIBITOR, NUCLEOTIDE-BINDING, KINASE, CYTOPLASM,                    
KEYWDS   3 TRANSFERASE, ATP-BINDING, DNA SYNTHESIS, PHOSPHOPROTEIN,             
KEYWDS   4 PHOSPHORYLATION                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.SKOVGAARD,U.UHLIN,B.MUNCH-PETERSEN                                  
REVDAT   2   02-MAY-12 2WVJ    1       JRNL   REMARK VERSN                      
REVDAT   1   27-OCT-09 2WVJ    0                                                
JRNL        AUTH   T.SKOVGAARD,U.UHLIN,B.MUNCH-PETERSEN                         
JRNL        TITL   COMPARATIVE ACTIVE-SITE MUTATION STUDY OF HUMAN AND          
JRNL        TITL 2 CAENORHABDITIS ELEGANS THYMIDINE KINASE 1.                   
JRNL        REF    FEBS J.                       V. 279  1777 2012              
JRNL        REFN                   ISSN 1742-464X                               
JRNL        PMID   22385435                                                     
JRNL        DOI    10.1111/J.1742-4658.2012.08554.X                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.200                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.814                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.857                         
REMARK   3   NUMBER OF REFLECTIONS             : 85195                          
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) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.1733                          
REMARK   3   FREE R VALUE                     : 0.2209                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.04                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 4263                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.2                          
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.257                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5898                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.809                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.209                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 360                          
REMARK   3   BIN FREE R VALUE                    : 0.293                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9990                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 243                                     
REMARK   3   SOLVENT ATOMS            : 1074                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.5                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.101                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.232                                               
REMARK   3    B22 (A**2) : -0.069                                               
REMARK   3    B33 (A**2) : -0.065                                               
REMARK   3    B12 (A**2) : 0.000                                                
REMARK   3    B13 (A**2) : -0.268                                               
REMARK   3    B23 (A**2) : 0.000                                                
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.218         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.185         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.123         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.750         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.947                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.917                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10377 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13999 ; 1.215 ; 2.005       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1274 ; 5.919 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   420 ;33.468 ;22.881       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1856 ;15.446 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    88 ;20.350 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1586 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7508 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4926 ; 0.182 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  6930 ; 0.301 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   896 ; 0.150 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     1 ; 0.055 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    63 ; 0.208 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    30 ; 0.127 ; 0.200       
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):  6576 ; 0.441 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10216 ; 0.789 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4283 ; 1.115 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3783 ; 1.846 ; 4.500       
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 : MASK BULK SOLVENT                                    
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.200                                         
REMARK   3   ION PROBE RADIUS   : 0.800                                         
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3   RIDING POSITIONS. LOOP CONTAINING RESIDUES 64 TO 73 IS             
REMARK   3   MISSING IN THE STRUCTURE AS ARE RESIDUES BEFORE AMINO ACID         
REMARK   3   18 AND AFTER 192.                                                  
REMARK   4                                                                      
REMARK   4 2WVJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-OCT-09.                  
REMARK 100 THE PDBE ID CODE IS EBI-41398.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-APR-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8726                             
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 : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 85203                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.20                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 88.39                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.7                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 3.7                                
REMARK 200  R MERGE                    (I) : 0.10                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.56                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.22                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.7                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.37                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.40                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1XBT                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROPS WITH EQUAL                 
REMARK 280  AMOUNTS OF PROTEIN, 10 MG PER ML CONTAINING 5 MM TTP AND            
REMARK 280  TRAY SOLUTION COMPOSED OF SODIUM CITRATE PH 5.6,                    
REMARK 280  2-PROPANOL AND PEG 4000.                                            
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       78.45100            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       61.62600            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       78.45100            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       61.62600            
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: 11990 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 25830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.97 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, D                            
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                                                                      
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: 12250 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 26000 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -79.21 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, G, F, 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, THR 163 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, THR 163 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, THR 163 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, THR 163 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN E, THR 163 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN F, THR 163 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN G, THR 163 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN H, THR 163 TO SER                        
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     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     CYS A     3                                                      
REMARK 465     ILE A     4                                                      
REMARK 465     ASN A     5                                                      
REMARK 465     LEU A     6                                                      
REMARK 465     PRO A     7                                                      
REMARK 465     THR A     8                                                      
REMARK 465     VAL A     9                                                      
REMARK 465     LEU A    10                                                      
REMARK 465     PRO A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     SER A    13                                                      
REMARK 465     PRO A    14                                                      
REMARK 465     SER A    15                                                      
REMARK 465     LYS A    16                                                      
REMARK 465     THR A    17                                                      
REMARK 465     TYR A    61                                                      
REMARK 465     SER A    62                                                      
REMARK 465     SER A    63                                                      
REMARK 465     SER A    64                                                      
REMARK 465     PHE A    65                                                      
REMARK 465     CYS A    66                                                      
REMARK 465     THR A    67                                                      
REMARK 465     HIS A    68                                                      
REMARK 465     ASP A    69                                                      
REMARK 465     ARG A    70                                                      
REMARK 465     ASN A    71                                                      
REMARK 465     THR A    72                                                      
REMARK 465     MET A    73                                                      
REMARK 465     GLU A    74                                                      
REMARK 465     LYS A   192                                                      
REMARK 465     ALA A   193                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     CYS B     3                                                      
REMARK 465     ILE B     4                                                      
REMARK 465     ASN B     5                                                      
REMARK 465     LEU B     6                                                      
REMARK 465     PRO B     7                                                      
REMARK 465     THR B     8                                                      
REMARK 465     VAL B     9                                                      
REMARK 465     LEU B    10                                                      
REMARK 465     PRO B    11                                                      
REMARK 465     GLY B    12                                                      
REMARK 465     SER B    13                                                      
REMARK 465     PRO B    14                                                      
REMARK 465     SER B    15                                                      
REMARK 465     LYS B    16                                                      
REMARK 465     THR B    17                                                      
REMARK 465     TYR B    61                                                      
REMARK 465     SER B    62                                                      
REMARK 465     SER B    63                                                      
REMARK 465     SER B    64                                                      
REMARK 465     PHE B    65                                                      
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     MET B    73                                                      
REMARK 465     GLU B    74                                                      
REMARK 465     ALA B   193                                                      
REMARK 465     MET C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     CYS C     3                                                      
REMARK 465     ILE C     4                                                      
REMARK 465     ASN C     5                                                      
REMARK 465     LEU C     6                                                      
REMARK 465     PRO C     7                                                      
REMARK 465     THR C     8                                                      
REMARK 465     VAL C     9                                                      
REMARK 465     LEU C    10                                                      
REMARK 465     PRO C    11                                                      
REMARK 465     GLY C    12                                                      
REMARK 465     SER C    13                                                      
REMARK 465     PRO 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     MET D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     CYS D     3                                                      
REMARK 465     ILE D     4                                                      
REMARK 465     ASN D     5                                                      
REMARK 465     LEU D     6                                                      
REMARK 465     PRO D     7                                                      
REMARK 465     THR D     8                                                      
REMARK 465     VAL D     9                                                      
REMARK 465     LEU D    10                                                      
REMARK 465     PRO D    11                                                      
REMARK 465     GLY D    12                                                      
REMARK 465     SER D    13                                                      
REMARK 465     PRO D    14                                                      
REMARK 465     SER D    15                                                      
REMARK 465     LYS D    16                                                      
REMARK 465     THR D    17                                                      
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     MET E     1                                                      
REMARK 465     SER E     2                                                      
REMARK 465     CYS E     3                                                      
REMARK 465     ILE E     4                                                      
REMARK 465     ASN E     5                                                      
REMARK 465     LEU E     6                                                      
REMARK 465     PRO E     7                                                      
REMARK 465     THR E     8                                                      
REMARK 465     VAL E     9                                                      
REMARK 465     LEU E    10                                                      
REMARK 465     PRO E    11                                                      
REMARK 465     GLY E    12                                                      
REMARK 465     SER E    13                                                      
REMARK 465     PRO 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     MET F     1                                                      
REMARK 465     SER F     2                                                      
REMARK 465     CYS F     3                                                      
REMARK 465     ILE F     4                                                      
REMARK 465     ASN F     5                                                      
REMARK 465     LEU F     6                                                      
REMARK 465     PRO F     7                                                      
REMARK 465     THR F     8                                                      
REMARK 465     VAL F     9                                                      
REMARK 465     LEU F    10                                                      
REMARK 465     PRO F    11                                                      
REMARK 465     GLY F    12                                                      
REMARK 465     SER F    13                                                      
REMARK 465     PRO F    14                                                      
REMARK 465     SER F    15                                                      
REMARK 465     LYS F    16                                                      
REMARK 465     THR F    17                                                      
REMARK 465     TYR F    61                                                      
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     MET G     1                                                      
REMARK 465     SER G     2                                                      
REMARK 465     CYS G     3                                                      
REMARK 465     ILE G     4                                                      
REMARK 465     ASN G     5                                                      
REMARK 465     LEU G     6                                                      
REMARK 465     PRO G     7                                                      
REMARK 465     THR G     8                                                      
REMARK 465     VAL G     9                                                      
REMARK 465     LEU G    10                                                      
REMARK 465     PRO G    11                                                      
REMARK 465     GLY G    12                                                      
REMARK 465     SER G    13                                                      
REMARK 465     PRO G    14                                                      
REMARK 465     SER G    15                                                      
REMARK 465     LYS G    16                                                      
REMARK 465     THR G    17                                                      
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     MET H     1                                                      
REMARK 465     SER H     2                                                      
REMARK 465     CYS H     3                                                      
REMARK 465     ILE H     4                                                      
REMARK 465     ASN H     5                                                      
REMARK 465     LEU H     6                                                      
REMARK 465     PRO H     7                                                      
REMARK 465     THR H     8                                                      
REMARK 465     VAL H     9                                                      
REMARK 465     LEU H    10                                                      
REMARK 465     PRO H    11                                                      
REMARK 465     GLY H    12                                                      
REMARK 465     SER H    13                                                      
REMARK 465     PRO H    14                                                      
REMARK 465     SER H    15                                                      
REMARK 465     LYS H    16                                                      
REMARK 465     THR H    17                                                      
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     LYS H   192                                                      
REMARK 465     ALA H   193                                                      
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   NH2  ARG B   130     OE1  GLU D   110              2.18            
REMARK 500   NH2  ARG F   130     OE1  GLU H   110              2.19            
REMARK 500   O    HOH D  2056     O    HOH D  2074              1.88            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR B  59       46.72   -105.90                                   
REMARK 500    GLN C  47        4.51     84.99                                   
REMARK 500    ARG D 158     -168.71    -77.14                                   
REMARK 500    GLN E  47       14.38     80.20                                   
REMARK 500    GLN F  47        9.95     83.50                                   
REMARK 500    GLN G  47        6.38     84.99                                   
REMARK 500    GLN H  47       10.70     82.15                                   
REMARK 500    SER H  62      -61.01    -23.29                                   
REMARK 500    SER H  63      -24.68    130.97                                   
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    GLU C 144        24.8      L          L   OUTSIDE RANGE           
REMARK 500    SER H  62        24.5      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 THYMIDINE 5' TRIPHOSPHATE (TTP): TTP HAS TWO CONFORMATIONS           
REMARK 600  IN EACH SITE. IN PROTEIN CHAINS A,B,C,E AND F IS THE RATIO          
REMARK 600  1 TO 3 AND IN D, G AND H IS THE RATIO 3 TO 1  FOR                   
REMARK 600  RESPECTIVE CONFORMATION. MG HAS BEEN ASSIGNED FOR THE THE           
REMARK 600  3 TO 1 CONFORMATION.                                                
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 A1193  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 185   SG                                                     
REMARK 620 2 CYS A 153   SG  120.1                                              
REMARK 620 3 CYS A 156   SG  107.6 111.5                                        
REMARK 620 4 CYS A 188   SG  104.3 101.8 110.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1194  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 188   SG                                                     
REMARK 620 2 CYS B 153   SG   99.3                                              
REMARK 620 3 CYS B 156   SG  111.9 116.0                                        
REMARK 620 4 CYS B 185   SG  103.3 119.3 106.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C1193  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 153   SG                                                     
REMARK 620 2 CYS C 156   SG  115.9                                              
REMARK 620 3 CYS C 188   SG  103.6 106.9                                        
REMARK 620 4 CYS C 185   SG  120.7 107.7  99.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D1194  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 153   SG                                                     
REMARK 620 2 CYS D 188   SG  106.7                                              
REMARK 620 3 CYS D 185   SG  120.2 101.6                                        
REMARK 620 4 CYS D 156   SG  110.5 112.1 105.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E1193  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS E 153   SG                                                     
REMARK 620 2 CYS E 156   SG  110.1                                              
REMARK 620 3 CYS E 185   SG  120.3 107.4                                        
REMARK 620 4 CYS E 188   SG  103.7 109.2 105.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F1193  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F 156   SG                                                     
REMARK 620 2 CYS F 153   SG  115.8                                              
REMARK 620 3 CYS F 185   SG  105.2 116.7                                        
REMARK 620 4 CYS F 188   SG  112.9 102.7 103.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G1194  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS G 185   SG                                                     
REMARK 620 2 CYS G 188   SG  104.5                                              
REMARK 620 3 CYS G 153   SG  117.7 103.3                                        
REMARK 620 4 CYS G 156   SG  105.3 111.9 113.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN H1194  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS H 153   SG                                                     
REMARK 620 2 CYS H 156   SG  112.8                                              
REMARK 620 3 CYS H 185   SG  119.7 104.9                                        
REMARK 620 4 CYS H 188   SG  104.0 112.0 103.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D1193  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER D  33   OG                                                     
REMARK 620 2 HOH D2057   O    77.8                                              
REMARK 620 3 TTP D1192   O1B 145.9 111.9                                        
REMARK 620 4 TTP D1192   O1A 122.4 100.4  88.9                                  
REMARK 620 5 TTP D1192   O2G  77.1 146.2  78.9 112.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG G1193  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TTP G1192   O1A                                                    
REMARK 620 2 SER G  33   OG  110.7                                              
REMARK 620 3 HOH G2014   O   167.8  79.1                                        
REMARK 620 4 HOH G2092   O    83.1  82.2  91.2                                  
REMARK 620 5 TTP G1192   O3G  99.7  78.2  89.4 159.8                            
REMARK 620 6 TTP G1192   O1B  81.4 157.3  92.0 119.2  80.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG H1193  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TTP H1192   O2G                                                    
REMARK 620 2 TTP H1192   O1A 107.1                                              
REMARK 620 3 TTP H1192   O1B  87.1  83.8                                        
REMARK 620 4 SER H  33   OG   74.4 116.5 155.6                                  
REMARK 620 5 HOH H2013   O    84.2 160.0  80.2  82.1                            
REMARK 620 6 HOH H2077   O   155.0  90.1 113.2  81.8  85.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP A1192                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP B1193                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP C1192                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP D1192                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP E1192                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP F1192                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP G1192                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP H1192                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG D1193                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG G1193                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG H1193                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1193                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B1194                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN C1193                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN D1194                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN E1193                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN F1193                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN G1194                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN H1194                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1XBT   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN THYMIDINE KINASE 1                       
REMARK 900 RELATED ID: 1W4R   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF A TYPE II THYMIDINE KINASE                             
REMARK 900  WITH BOUND DTTP                                                     
REMARK 900 RELATED ID: 2WVL   RELATED DB: PDB                                   
REMARK 900  MANNOSYL-3-PHOSPHOGLYCERATE SYNTHASE FROM                           
REMARK 900  THERMUS THERMOPHILUS HB27 IN COMPLEX WITH                           
REMARK 900  GDP-ALPHA-D-MANNOSE AND MG(II)                                      
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 TRUNCATION AFTER AMINO ACID 193                                      
DBREF  2WVJ A    1   193  UNP    P04183   KITH_HUMAN       1    193             
DBREF  2WVJ B    1   193  UNP    P04183   KITH_HUMAN       1    193             
DBREF  2WVJ C    1   193  UNP    P04183   KITH_HUMAN       1    193             
DBREF  2WVJ D    1   193  UNP    P04183   KITH_HUMAN       1    193             
DBREF  2WVJ E    1   193  UNP    P04183   KITH_HUMAN       1    193             
DBREF  2WVJ F    1   193  UNP    P04183   KITH_HUMAN       1    193             
DBREF  2WVJ G    1   193  UNP    P04183   KITH_HUMAN       1    193             
DBREF  2WVJ H    1   193  UNP    P04183   KITH_HUMAN       1    193             
SEQADV 2WVJ SER A  163  UNP  P04183    THR   163 ENGINEERED MUTATION            
SEQADV 2WVJ SER B  163  UNP  P04183    THR   163 ENGINEERED MUTATION            
SEQADV 2WVJ SER C  163  UNP  P04183    THR   163 ENGINEERED MUTATION            
SEQADV 2WVJ SER D  163  UNP  P04183    THR   163 ENGINEERED MUTATION            
SEQADV 2WVJ SER E  163  UNP  P04183    THR   163 ENGINEERED MUTATION            
SEQADV 2WVJ SER F  163  UNP  P04183    THR   163 ENGINEERED MUTATION            
SEQADV 2WVJ SER G  163  UNP  P04183    THR   163 ENGINEERED MUTATION            
SEQADV 2WVJ SER H  163  UNP  P04183    THR   163 ENGINEERED MUTATION            
SEQRES   1 A  193  MET SER CYS ILE ASN LEU PRO THR VAL LEU PRO GLY SER          
SEQRES   2 A  193  PRO SER LYS THR ARG GLY GLN ILE GLN VAL ILE LEU GLY          
SEQRES   3 A  193  PRO MET PHE SER GLY LYS SER THR GLU LEU MET ARG ARG          
SEQRES   4 A  193  VAL ARG ARG PHE GLN ILE ALA GLN TYR LYS CYS LEU VAL          
SEQRES   5 A  193  ILE LYS TYR ALA LYS ASP THR ARG TYR SER SER SER PHE          
SEQRES   6 A  193  CYS THR HIS ASP ARG ASN THR MET GLU ALA LEU PRO ALA          
SEQRES   7 A  193  CYS LEU LEU ARG ASP VAL ALA GLN GLU ALA LEU GLY VAL          
SEQRES   8 A  193  ALA VAL ILE GLY ILE ASP GLU GLY GLN PHE PHE PRO ASP          
SEQRES   9 A  193  ILE VAL GLU PHE CYS GLU ALA MET ALA ASN ALA GLY LYS          
SEQRES  10 A  193  THR VAL ILE VAL ALA ALA LEU ASP GLY THR PHE GLN ARG          
SEQRES  11 A  193  LYS PRO PHE GLY ALA ILE LEU ASN LEU VAL PRO LEU ALA          
SEQRES  12 A  193  GLU SER VAL VAL LYS LEU THR ALA VAL CYS MET GLU CYS          
SEQRES  13 A  193  PHE ARG GLU ALA ALA TYR SER LYS ARG LEU GLY THR GLU          
SEQRES  14 A  193  LYS GLU VAL GLU VAL ILE GLY GLY ALA ASP LYS TYR HIS          
SEQRES  15 A  193  SER VAL CYS ARG LEU CYS TYR PHE LYS LYS ALA                  
SEQRES   1 B  193  MET SER CYS ILE ASN LEU PRO THR VAL LEU PRO GLY SER          
SEQRES   2 B  193  PRO SER LYS THR ARG GLY GLN ILE GLN VAL ILE LEU GLY          
SEQRES   3 B  193  PRO MET PHE SER GLY LYS SER THR GLU LEU MET ARG ARG          
SEQRES   4 B  193  VAL ARG ARG PHE GLN ILE ALA GLN TYR LYS CYS LEU VAL          
SEQRES   5 B  193  ILE LYS TYR ALA LYS ASP THR ARG TYR SER SER SER PHE          
SEQRES   6 B  193  CYS THR HIS ASP ARG ASN THR MET GLU ALA LEU PRO ALA          
SEQRES   7 B  193  CYS LEU LEU ARG ASP VAL ALA GLN GLU ALA LEU GLY VAL          
SEQRES   8 B  193  ALA VAL ILE GLY ILE ASP GLU GLY GLN PHE PHE PRO ASP          
SEQRES   9 B  193  ILE VAL GLU PHE CYS GLU ALA MET ALA ASN ALA GLY LYS          
SEQRES  10 B  193  THR VAL ILE VAL ALA ALA LEU ASP GLY THR PHE GLN ARG          
SEQRES  11 B  193  LYS PRO PHE GLY ALA ILE LEU ASN LEU VAL PRO LEU ALA          
SEQRES  12 B  193  GLU SER VAL VAL LYS LEU THR ALA VAL CYS MET GLU CYS          
SEQRES  13 B  193  PHE ARG GLU ALA ALA TYR SER LYS ARG LEU GLY THR GLU          
SEQRES  14 B  193  LYS GLU VAL GLU VAL ILE GLY GLY ALA ASP LYS TYR HIS          
SEQRES  15 B  193  SER VAL CYS ARG LEU CYS TYR PHE LYS LYS ALA                  
SEQRES   1 C  193  MET SER CYS ILE ASN LEU PRO THR VAL LEU PRO GLY SER          
SEQRES   2 C  193  PRO SER LYS THR ARG GLY GLN ILE GLN VAL ILE LEU GLY          
SEQRES   3 C  193  PRO MET PHE SER GLY LYS SER THR GLU LEU MET ARG ARG          
SEQRES   4 C  193  VAL ARG ARG PHE GLN ILE ALA GLN TYR LYS CYS LEU VAL          
SEQRES   5 C  193  ILE LYS TYR ALA LYS ASP THR ARG TYR SER SER SER PHE          
SEQRES   6 C  193  CYS THR HIS ASP ARG ASN THR MET GLU ALA LEU PRO ALA          
SEQRES   7 C  193  CYS LEU LEU ARG ASP VAL ALA GLN GLU ALA LEU GLY VAL          
SEQRES   8 C  193  ALA VAL ILE GLY ILE ASP GLU GLY GLN PHE PHE PRO ASP          
SEQRES   9 C  193  ILE VAL GLU PHE CYS GLU ALA MET ALA ASN ALA GLY LYS          
SEQRES  10 C  193  THR VAL ILE VAL ALA ALA LEU ASP GLY THR PHE GLN ARG          
SEQRES  11 C  193  LYS PRO PHE GLY ALA ILE LEU ASN LEU VAL PRO LEU ALA          
SEQRES  12 C  193  GLU SER VAL VAL LYS LEU THR ALA VAL CYS MET GLU CYS          
SEQRES  13 C  193  PHE ARG GLU ALA ALA TYR SER LYS ARG LEU GLY THR GLU          
SEQRES  14 C  193  LYS GLU VAL GLU VAL ILE GLY GLY ALA ASP LYS TYR HIS          
SEQRES  15 C  193  SER VAL CYS ARG LEU CYS TYR PHE LYS LYS ALA                  
SEQRES   1 D  193  MET SER CYS ILE ASN LEU PRO THR VAL LEU PRO GLY SER          
SEQRES   2 D  193  PRO SER LYS THR ARG GLY GLN ILE GLN VAL ILE LEU GLY          
SEQRES   3 D  193  PRO MET PHE SER GLY LYS SER THR GLU LEU MET ARG ARG          
SEQRES   4 D  193  VAL ARG ARG PHE GLN ILE ALA GLN TYR LYS CYS LEU VAL          
SEQRES   5 D  193  ILE LYS TYR ALA LYS ASP THR ARG TYR SER SER SER PHE          
SEQRES   6 D  193  CYS THR HIS ASP ARG ASN THR MET GLU ALA LEU PRO ALA          
SEQRES   7 D  193  CYS LEU LEU ARG ASP VAL ALA GLN GLU ALA LEU GLY VAL          
SEQRES   8 D  193  ALA VAL ILE GLY ILE ASP GLU GLY GLN PHE PHE PRO ASP          
SEQRES   9 D  193  ILE VAL GLU PHE CYS GLU ALA MET ALA ASN ALA GLY LYS          
SEQRES  10 D  193  THR VAL ILE VAL ALA ALA LEU ASP GLY THR PHE GLN ARG          
SEQRES  11 D  193  LYS PRO PHE GLY ALA ILE LEU ASN LEU VAL PRO LEU ALA          
SEQRES  12 D  193  GLU SER VAL VAL LYS LEU THR ALA VAL CYS MET GLU CYS          
SEQRES  13 D  193  PHE ARG GLU ALA ALA TYR SER LYS ARG LEU GLY THR GLU          
SEQRES  14 D  193  LYS GLU VAL GLU VAL ILE GLY GLY ALA ASP LYS TYR HIS          
SEQRES  15 D  193  SER VAL CYS ARG LEU CYS TYR PHE LYS LYS ALA                  
SEQRES   1 E  193  MET SER CYS ILE ASN LEU PRO THR VAL LEU PRO GLY SER          
SEQRES   2 E  193  PRO SER LYS THR ARG GLY GLN ILE GLN VAL ILE LEU GLY          
SEQRES   3 E  193  PRO MET PHE SER GLY LYS SER THR GLU LEU MET ARG ARG          
SEQRES   4 E  193  VAL ARG ARG PHE GLN ILE ALA GLN TYR LYS CYS LEU VAL          
SEQRES   5 E  193  ILE LYS TYR ALA LYS ASP THR ARG TYR SER SER SER PHE          
SEQRES   6 E  193  CYS THR HIS ASP ARG ASN THR MET GLU ALA LEU PRO ALA          
SEQRES   7 E  193  CYS LEU LEU ARG ASP VAL ALA GLN GLU ALA LEU GLY VAL          
SEQRES   8 E  193  ALA VAL ILE GLY ILE ASP GLU GLY GLN PHE PHE PRO ASP          
SEQRES   9 E  193  ILE VAL GLU PHE CYS GLU ALA MET ALA ASN ALA GLY LYS          
SEQRES  10 E  193  THR VAL ILE VAL ALA ALA LEU ASP GLY THR PHE GLN ARG          
SEQRES  11 E  193  LYS PRO PHE GLY ALA ILE LEU ASN LEU VAL PRO LEU ALA          
SEQRES  12 E  193  GLU SER VAL VAL LYS LEU THR ALA VAL CYS MET GLU CYS          
SEQRES  13 E  193  PHE ARG GLU ALA ALA TYR SER LYS ARG LEU GLY THR GLU          
SEQRES  14 E  193  LYS GLU VAL GLU VAL ILE GLY GLY ALA ASP LYS TYR HIS          
SEQRES  15 E  193  SER VAL CYS ARG LEU CYS TYR PHE LYS LYS ALA                  
SEQRES   1 F  193  MET SER CYS ILE ASN LEU PRO THR VAL LEU PRO GLY SER          
SEQRES   2 F  193  PRO SER LYS THR ARG GLY GLN ILE GLN VAL ILE LEU GLY          
SEQRES   3 F  193  PRO MET PHE SER GLY LYS SER THR GLU LEU MET ARG ARG          
SEQRES   4 F  193  VAL ARG ARG PHE GLN ILE ALA GLN TYR LYS CYS LEU VAL          
SEQRES   5 F  193  ILE LYS TYR ALA LYS ASP THR ARG TYR SER SER SER PHE          
SEQRES   6 F  193  CYS THR HIS ASP ARG ASN THR MET GLU ALA LEU PRO ALA          
SEQRES   7 F  193  CYS LEU LEU ARG ASP VAL ALA GLN GLU ALA LEU GLY VAL          
SEQRES   8 F  193  ALA VAL ILE GLY ILE ASP GLU GLY GLN PHE PHE PRO ASP          
SEQRES   9 F  193  ILE VAL GLU PHE CYS GLU ALA MET ALA ASN ALA GLY LYS          
SEQRES  10 F  193  THR VAL ILE VAL ALA ALA LEU ASP GLY THR PHE GLN ARG          
SEQRES  11 F  193  LYS PRO PHE GLY ALA ILE LEU ASN LEU VAL PRO LEU ALA          
SEQRES  12 F  193  GLU SER VAL VAL LYS LEU THR ALA VAL CYS MET GLU CYS          
SEQRES  13 F  193  PHE ARG GLU ALA ALA TYR SER LYS ARG LEU GLY THR GLU          
SEQRES  14 F  193  LYS GLU VAL GLU VAL ILE GLY GLY ALA ASP LYS TYR HIS          
SEQRES  15 F  193  SER VAL CYS ARG LEU CYS TYR PHE LYS LYS ALA                  
SEQRES   1 G  193  MET SER CYS ILE ASN LEU PRO THR VAL LEU PRO GLY SER          
SEQRES   2 G  193  PRO SER LYS THR ARG GLY GLN ILE GLN VAL ILE LEU GLY          
SEQRES   3 G  193  PRO MET PHE SER GLY LYS SER THR GLU LEU MET ARG ARG          
SEQRES   4 G  193  VAL ARG ARG PHE GLN ILE ALA GLN TYR LYS CYS LEU VAL          
SEQRES   5 G  193  ILE LYS TYR ALA LYS ASP THR ARG TYR SER SER SER PHE          
SEQRES   6 G  193  CYS THR HIS ASP ARG ASN THR MET GLU ALA LEU PRO ALA          
SEQRES   7 G  193  CYS LEU LEU ARG ASP VAL ALA GLN GLU ALA LEU GLY VAL          
SEQRES   8 G  193  ALA VAL ILE GLY ILE ASP GLU GLY GLN PHE PHE PRO ASP          
SEQRES   9 G  193  ILE VAL GLU PHE CYS GLU ALA MET ALA ASN ALA GLY LYS          
SEQRES  10 G  193  THR VAL ILE VAL ALA ALA LEU ASP GLY THR PHE GLN ARG          
SEQRES  11 G  193  LYS PRO PHE GLY ALA ILE LEU ASN LEU VAL PRO LEU ALA          
SEQRES  12 G  193  GLU SER VAL VAL LYS LEU THR ALA VAL CYS MET GLU CYS          
SEQRES  13 G  193  PHE ARG GLU ALA ALA TYR SER LYS ARG LEU GLY THR GLU          
SEQRES  14 G  193  LYS GLU VAL GLU VAL ILE GLY GLY ALA ASP LYS TYR HIS          
SEQRES  15 G  193  SER VAL CYS ARG LEU CYS TYR PHE LYS LYS ALA                  
SEQRES   1 H  193  MET SER CYS ILE ASN LEU PRO THR VAL LEU PRO GLY SER          
SEQRES   2 H  193  PRO SER LYS THR ARG GLY GLN ILE GLN VAL ILE LEU GLY          
SEQRES   3 H  193  PRO MET PHE SER GLY LYS SER THR GLU LEU MET ARG ARG          
SEQRES   4 H  193  VAL ARG ARG PHE GLN ILE ALA GLN TYR LYS CYS LEU VAL          
SEQRES   5 H  193  ILE LYS TYR ALA LYS ASP THR ARG TYR SER SER SER PHE          
SEQRES   6 H  193  CYS THR HIS ASP ARG ASN THR MET GLU ALA LEU PRO ALA          
SEQRES   7 H  193  CYS LEU LEU ARG ASP VAL ALA GLN GLU ALA LEU GLY VAL          
SEQRES   8 H  193  ALA VAL ILE GLY ILE ASP GLU GLY GLN PHE PHE PRO ASP          
SEQRES   9 H  193  ILE VAL GLU PHE CYS GLU ALA MET ALA ASN ALA GLY LYS          
SEQRES  10 H  193  THR VAL ILE VAL ALA ALA LEU ASP GLY THR PHE GLN ARG          
SEQRES  11 H  193  LYS PRO PHE GLY ALA ILE LEU ASN LEU VAL PRO LEU ALA          
SEQRES  12 H  193  GLU SER VAL VAL LYS LEU THR ALA VAL CYS MET GLU CYS          
SEQRES  13 H  193  PHE ARG GLU ALA ALA TYR SER LYS ARG LEU GLY THR GLU          
SEQRES  14 H  193  LYS GLU VAL GLU VAL ILE GLY GLY ALA ASP LYS TYR HIS          
SEQRES  15 H  193  SER VAL CYS ARG LEU CYS TYR PHE LYS LYS ALA                  
HET    TTP  A1192      29                                                       
HET    TTP  B1193      29                                                       
HET    TTP  C1192      29                                                       
HET    TTP  D1192      29                                                       
HET    TTP  E1192      29                                                       
HET    TTP  F1192      29                                                       
HET    TTP  G1192      29                                                       
HET    TTP  H1192      29                                                       
HET     MG  D1193       1                                                       
HET     MG  G1193       1                                                       
HET     MG  H1193       1                                                       
HET     ZN  A1193       1                                                       
HET     ZN  B1194       1                                                       
HET     ZN  C1193       1                                                       
HET     ZN  D1194       1                                                       
HET     ZN  E1193       1                                                       
HET     ZN  F1193       1                                                       
HET     ZN  G1194       1                                                       
HET     ZN  H1194       1                                                       
HETNAM     TTP THYMIDINE-5'-TRIPHOSPHATE                                        
HETNAM      ZN ZINC ION                                                         
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   9  TTP    8(C10 H17 N2 O14 P3)                                         
FORMUL  10   ZN    8(ZN 2+)                                                     
FORMUL  11   MG    3(MG 2+)                                                     
FORMUL  12  HOH   *1074(H2 O)                                                   
HELIX    1   1 GLY A   31  ALA A   46  1                                  16    
HELIX    2   2 LEU A   80  ASP A   83  5                                   4    
HELIX    3   3 VAL A   84  GLY A   90  1                                   7    
HELIX    4   4 GLU A   98  PHE A  102  5                                   5    
HELIX    5   5 ASP A  104  ALA A  115  1                                  12    
HELIX    6   6 ALA A  135  ALA A  143  5                                   9    
HELIX    7   7 CYS A  185  PHE A  190  1                                   6    
HELIX    8   8 GLY B   31  ALA B   46  1                                  16    
HELIX    9   9 LEU B   80  ASP B   83  5                                   4    
HELIX   10  10 VAL B   84  GLY B   90  1                                   7    
HELIX   11  11 GLU B   98  PHE B  102  5                                   5    
HELIX   12  12 ASP B  104  ALA B  115  1                                  12    
HELIX   13  13 ALA B  135  ALA B  143  5                                   9    
HELIX   14  14 CYS B  185  LYS B  191  1                                   7    
HELIX   15  15 GLY C   31  ILE C   45  1                                  15    
HELIX   16  16 LEU C   80  ASP C   83  5                                   4    
HELIX   17  17 VAL C   84  GLY C   90  1                                   7    
HELIX   18  18 GLU C   98  PHE C  102  5                                   5    
HELIX   19  19 ASP C  104  ALA C  115  1                                  12    
HELIX   20  20 ALA C  135  ALA C  143  5                                   9    
HELIX   21  21 CYS C  185  LYS C  191  1                                   7    
HELIX   22  22 GLY D   31  ILE D   45  1                                  15    
HELIX   23  23 LEU D   80  ASP D   83  5                                   4    
HELIX   24  24 VAL D   84  GLY D   90  1                                   7    
HELIX   25  25 GLY D   99  PHE D  102  5                                   4    
HELIX   26  26 ASP D  104  ALA D  115  1                                  12    
HELIX   27  27 ALA D  135  ALA D  143  5                                   9    
HELIX   28  28 CYS D  185  PHE D  190  1                                   6    
HELIX   29  29 GLY E   31  ALA E   46  1                                  16    
HELIX   30  30 LEU E   80  ASP E   83  5                                   4    
HELIX   31  31 VAL E   84  GLY E   90  1                                   7    
HELIX   32  32 GLU E   98  PHE E  102  5                                   5    
HELIX   33  33 ASP E  104  ALA E  115  1                                  12    
HELIX   34  34 ALA E  135  ALA E  143  5                                   9    
HELIX   35  35 CYS E  185  LYS E  191  1                                   7    
HELIX   36  36 GLY F   31  ILE F   45  1                                  15    
HELIX   37  37 LEU F   80  ASP F   83  5                                   4    
HELIX   38  38 VAL F   84  GLY F   90  1                                   7    
HELIX   39  39 GLU F   98  PHE F  102  5                                   5    
HELIX   40  40 ASP F  104  ALA F  115  1                                  12    
HELIX   41  41 ALA F  135  ALA F  143  5                                   9    
HELIX   42  42 CYS F  185  PHE F  190  1                                   6    
HELIX   43  43 GLY G   31  ILE G   45  1                                  15    
HELIX   44  44 LEU G   80  ASP G   83  5                                   4    
HELIX   45  45 VAL G   84  GLY G   90  1                                   7    
HELIX   46  46 GLY G   99  PHE G  102  5                                   4    
HELIX   47  47 ASP G  104  ALA G  115  1                                  12    
HELIX   48  48 ALA G  135  ALA G  143  5                                   9    
HELIX   49  49 CYS G  185  LYS G  191  1                                   7    
HELIX   50  50 GLY H   31  ILE H   45  1                                  15    
HELIX   51  51 LEU H   80  ASP H   83  5                                   4    
HELIX   52  52 VAL H   84  GLY H   90  1                                   7    
HELIX   53  53 GLU H   98  PHE H  102  5                                   5    
HELIX   54  54 ASP H  104  ALA H  115  1                                  12    
HELIX   55  55 ALA H  135  ALA H  143  5                                   9    
HELIX   56  56 CYS H  185  PHE H  190  1                                   6    
SHEET    1  AA 6 LEU A  76  ALA A  78  0                                        
SHEET    2  AA 6 CYS A  50  TYR A  55  1  O  VAL A  52   N  LEU A  76           
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  ALA A 122  1  O  THR A 118   N  ILE A  94           
SHEET    5  AA 6 GLN A  20  LEU A  25  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 LEU B  76  ALA B  78  0                                        
SHEET    2  BA 6 CYS B  50  TYR B  55  1  O  VAL B  52   N  LEU B  76           
SHEET    3  BA 6 VAL B  93  ILE B  96  1  O  VAL B  93   N  LEU B  51           
SHEET    4  BA 6 THR B 118  ALA B 122  1  O  THR B 118   N  ILE B  94           
SHEET    5  BA 6 GLN B  20  LEU B  25  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  ILE C  96  1  O  VAL C  93   N  LEU C  51           
SHEET    4  CA 6 THR C 118  ALA C 122  1  O  THR C 118   N  ILE C  94           
SHEET    5  CA 6 GLN C  20  LEU C  25  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  ASP D  97  1  O  VAL D  93   N  LEU D  51           
SHEET    4  DA 6 THR D 118  ALA D 122  1  O  THR D 118   N  ILE D  94           
SHEET    5  DA 6 GLN D  20  LEU D  25  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  ASP E  97  1  O  VAL E  93   N  LEU E  51           
SHEET    4  EA 6 THR E 118  ALA E 122  1  O  THR E 118   N  ILE E  94           
SHEET    5  EA 6 GLN E  20  LEU E  25  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  ALA F 122  1  O  THR F 118   N  ILE F  94           
SHEET    5  FA 6 GLN F  20  LEU F  25  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  ASP G  97  1  O  VAL G  93   N  LEU G  51           
SHEET    4  GA 6 THR G 118  ALA G 122  1  O  THR G 118   N  ILE G  94           
SHEET    5  GA 6 GLN G  20  LEU G  25  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 GLU H  74  ALA H  78  0                                        
SHEET    2  HA 6 CYS H  50  TYR H  55  1  O  CYS H  50   N  GLU H  74           
SHEET    3  HA 6 VAL H  93  ILE H  96  1  O  VAL H  93   N  LEU H  51           
SHEET    4  HA 6 THR H 118  ALA H 122  1  O  THR H 118   N  ILE H  94           
SHEET    5  HA 6 GLN H  20  LEU H  25  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        ZN    ZN A1193                 SG  CYS A 185     1555   1555  2.31  
LINK        ZN    ZN A1193                 SG  CYS A 153     1555   1555  2.28  
LINK        ZN    ZN A1193                 SG  CYS A 156     1555   1555  2.34  
LINK        ZN    ZN A1193                 SG  CYS A 188     1555   1555  2.44  
LINK        ZN    ZN B1194                 SG  CYS B 188     1555   1555  2.43  
LINK        ZN    ZN B1194                 SG  CYS B 153     1555   1555  2.19  
LINK        ZN    ZN B1194                 SG  CYS B 156     1555   1555  2.26  
LINK        ZN    ZN B1194                 SG  CYS B 185     1555   1555  2.42  
LINK        ZN    ZN C1193                 SG  CYS C 153     1555   1555  2.23  
LINK        ZN    ZN C1193                 SG  CYS C 156     1555   1555  2.35  
LINK        ZN    ZN C1193                 SG  CYS C 188     1555   1555  2.43  
LINK        ZN    ZN C1193                 SG  CYS C 185     1555   1555  2.45  
LINK        MG    MG D1193                 OG  SER D  33     1555   1555  2.59  
LINK        MG    MG D1193                 O2G TTP D1192     1555   1555  2.57  
LINK        MG    MG D1193                 O1A TTP D1192     1555   1555  1.93  
LINK        MG    MG D1193                 O1B TTP D1192     1555   1555  2.88  
LINK        MG    MG D1193                 O   HOH D2057     1555   1555  2.57  
LINK        ZN    ZN D1194                 SG  CYS D 156     1555   1555  2.39  
LINK        ZN    ZN D1194                 SG  CYS D 188     1555   1555  2.34  
LINK        ZN    ZN D1194                 SG  CYS D 185     1555   1555  2.44  
LINK        ZN    ZN D1194                 SG  CYS D 153     1555   1555  2.19  
LINK        ZN    ZN E1193                 SG  CYS E 156     1555   1555  2.17  
LINK        ZN    ZN E1193                 SG  CYS E 188     1555   1555  2.41  
LINK        ZN    ZN E1193                 SG  CYS E 185     1555   1555  2.39  
LINK        ZN    ZN E1193                 SG  CYS E 153     1555   1555  2.24  
LINK        ZN    ZN F1193                 SG  CYS F 188     1555   1555  2.42  
LINK        ZN    ZN F1193                 SG  CYS F 185     1555   1555  2.35  
LINK        ZN    ZN F1193                 SG  CYS F 153     1555   1555  2.33  
LINK        ZN    ZN F1193                 SG  CYS F 156     1555   1555  2.40  
LINK        MG    MG G1193                 O   HOH G2092     1555   1555  2.44  
LINK        MG    MG G1193                 O   HOH G2014     1555   1555  2.54  
LINK        MG    MG G1193                 O3G TTP G1192     1555   1555  2.55  
LINK        MG    MG G1193                 O1B TTP G1192     1555   1555  2.54  
LINK        MG    MG G1193                 O1A TTP G1192     1555   1555  2.24  
LINK        MG    MG G1193                 OG  SER G  33     1555   1555  2.59  
LINK        ZN    ZN G1194                 SG  CYS G 156     1555   1555  2.24  
LINK        ZN    ZN G1194                 SG  CYS G 153     1555   1555  2.32  
LINK        ZN    ZN G1194                 SG  CYS G 188     1555   1555  2.36  
LINK        ZN    ZN G1194                 SG  CYS G 185     1555   1555  2.34  
LINK        MG    MG H1193                 O1B TTP H1192     1555   1555  2.71  
LINK        MG    MG H1193                 OG  SER H  33     1555   1555  2.51  
LINK        MG    MG H1193                 O   HOH H2013     1555   1555  2.71  
LINK        MG    MG H1193                 O2G TTP H1192     1555   1555  2.66  
LINK        MG    MG H1193                 O1A TTP H1192     1555   1555  2.04  
LINK        MG    MG H1193                 O   HOH H2077     1555   1555  2.58  
LINK        ZN    ZN H1194                 SG  CYS H 188     1555   1555  2.38  
LINK        ZN    ZN H1194                 SG  CYS H 185     1555   1555  2.40  
LINK        ZN    ZN H1194                 SG  CYS H 156     1555   1555  2.29  
LINK        ZN    ZN H1194                 SG  CYS H 153     1555   1555  2.33  
CISPEP   1 SER H   62    SER H   63          0       -12.19                     
SITE     1 AC1 26 MET A  28  SER A  30  GLY A  31  LYS A  32                    
SITE     2 AC1 26 SER A  33  ASP A  58  ARG A  60  ASP A  97                    
SITE     3 AC1 26 GLU A  98  GLN A 100  PHE A 101  LEU A 124                    
SITE     4 AC1 26 THR A 127  PHE A 128  PHE A 133  SER A 163                    
SITE     5 AC1 26 VAL A 172  GLU A 173  VAL A 174  ILE A 175                    
SITE     6 AC1 26 GLY A 176  TYR A 181  HOH A2116  HOH A2117                    
SITE     7 AC1 26 HOH A2118  HOH A2119                                          
SITE     1 AC2 25 SER B  30  GLY B  31  LYS B  32  SER B  33                    
SITE     2 AC2 25 ASP B  58  ARG B  60  ASP B  97  GLU B  98                    
SITE     3 AC2 25 GLN B 100  PHE B 101  LEU B 124  THR B 127                    
SITE     4 AC2 25 PHE B 128  PHE B 133  SER B 163  VAL B 172                    
SITE     5 AC2 25 GLU B 173  VAL B 174  ILE B 175  GLY B 176                    
SITE     6 AC2 25 TYR B 181  HOH B2135  HOH B2136  HOH B2137                    
SITE     7 AC2 25 HOH B2139                                                     
SITE     1 AC3 26 MET C  28  SER C  30  GLY C  31  LYS C  32                    
SITE     2 AC3 26 SER C  33  ASP C  58  ARG C  60  ASP C  97                    
SITE     3 AC3 26 GLU C  98  GLN C 100  PHE C 101  LEU C 124                    
SITE     4 AC3 26 THR C 127  PHE C 128  PHE C 133  SER C 163                    
SITE     5 AC3 26 VAL C 172  GLU C 173  VAL C 174  ILE C 175                    
SITE     6 AC3 26 GLY C 176  TYR C 181  HOH C2119  HOH C2120                    
SITE     7 AC3 26 HOH C2121  HOH C2123                                          
SITE     1 AC4 28 MET D  28  PHE D  29  SER D  30  GLY D  31                    
SITE     2 AC4 28 LYS D  32  SER D  33  ASP D  58  ARG D  60                    
SITE     3 AC4 28 GLU D  98  PHE D 101  LEU D 124  THR D 127                    
SITE     4 AC4 28 PHE D 128  PHE D 133  SER D 163  ARG D 165                    
SITE     5 AC4 28 VAL D 172  GLU D 173  VAL D 174  ILE D 175                    
SITE     6 AC4 28 GLY D 176  TYR D 181   MG D1193  HOH D2056                    
SITE     7 AC4 28 HOH D2135  HOH D2136  HOH D2137  HOH D2138                    
SITE     1 AC5 26 MET E  28  SER E  30  GLY E  31  LYS E  32                    
SITE     2 AC5 26 SER E  33  ASP E  58  ARG E  60  ASP E  97                    
SITE     3 AC5 26 GLU E  98  GLN E 100  PHE E 101  LEU E 124                    
SITE     4 AC5 26 THR E 127  PHE E 128  PHE E 133  SER E 163                    
SITE     5 AC5 26 ARG E 165  VAL E 172  GLU E 173  VAL E 174                    
SITE     6 AC5 26 ILE E 175  GLY E 176  TYR E 181  HOH E2116                    
SITE     7 AC5 26 HOH E2117  HOH E2119                                          
SITE     1 AC6 24 MET F  28  SER F  30  GLY F  31  LYS F  32                    
SITE     2 AC6 24 SER F  33  ASP F  58  ASP F  97  GLU F  98                    
SITE     3 AC6 24 GLN F 100  PHE F 101  LEU F 124  THR F 127                    
SITE     4 AC6 24 PHE F 128  PHE F 133  SER F 163  VAL F 172                    
SITE     5 AC6 24 GLU F 173  VAL F 174  ILE F 175  GLY F 176                    
SITE     6 AC6 24 TYR F 181  HOH F2116  HOH F2117  HOH F2118                    
SITE     1 AC7 28 MET G  28  PHE G  29  SER G  30  GLY G  31                    
SITE     2 AC7 28 LYS G  32  SER G  33  ASP G  58  ARG G  60                    
SITE     3 AC7 28 GLU G  98  PHE G 101  LEU G 124  THR G 127                    
SITE     4 AC7 28 PHE G 128  PHE G 133  SER G 163  ARG G 165                    
SITE     5 AC7 28 VAL G 172  GLU G 173  VAL G 174  ILE G 175                    
SITE     6 AC7 28 GLY G 176  TYR G 181   MG G1193  HOH G2061                    
SITE     7 AC7 28 HOH G2093  HOH G2162  HOH G2163  HOH G2164                    
SITE     1 AC8 27 MET H  28  PHE H  29  SER H  30  GLY H  31                    
SITE     2 AC8 27 LYS H  32  SER H  33  ASP H  58  ARG H  60                    
SITE     3 AC8 27 GLU H  98  PHE H 101  LEU H 124  THR H 127                    
SITE     4 AC8 27 PHE H 128  PHE H 133  SER H 163  ARG H 165                    
SITE     5 AC8 27 VAL H 172  GLU H 173  VAL H 174  ILE H 175                    
SITE     6 AC8 27 GLY H 176  TYR H 181   MG H1193  HOH H2150                    
SITE     7 AC8 27 HOH H2151  HOH H2152  HOH H2153                               
SITE     1 AC9  5 SER D  33  TTP D1192  HOH D2009  HOH D2056                    
SITE     2 AC9  5 HOH D2057                                                     
SITE     1 BC1  4 SER G  33  TTP G1192  HOH G2014  HOH G2092                    
SITE     1 BC2  4 SER H  33  TTP H1192  HOH H2013  HOH H2077                    
SITE     1 BC3  4 CYS A 153  CYS A 156  CYS A 185  CYS A 188                    
SITE     1 BC4  4 CYS B 153  CYS B 156  CYS B 185  CYS B 188                    
SITE     1 BC5  4 CYS C 153  CYS C 156  CYS C 185  CYS C 188                    
SITE     1 BC6  4 CYS D 153  CYS D 156  CYS D 185  CYS D 188                    
SITE     1 BC7  4 CYS E 153  CYS E 156  CYS E 185  CYS E 188                    
SITE     1 BC8  4 CYS F 153  CYS F 156  CYS F 185  CYS F 188                    
SITE     1 BC9  4 CYS G 153  CYS G 156  CYS G 185  CYS G 188                    
SITE     1 CC1  4 CYS H 153  CYS H 156  CYS H 185  CYS H 188                    
CRYST1  156.902  123.252  121.024  90.00 132.98  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      0.006373  0.000000  0.005939        0.00000                         
SCALE2      0.000000  0.008113  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011294        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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