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Database: PDB
Entry: 2ORV
LinkDB: 2ORV
Original site: 2ORV 
HEADER    TRANSFERASE                             04-FEB-07   2ORV              
TITLE     HUMAN THYMIDINE KINASE 1 IN COMPLEX WITH TP4A                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THYMIDINE KINASE;                                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 2.7.1.21;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: TK1;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(D3);                                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET14B                                    
KEYWDS    TK-1 (THYMIDINE KINASE 1), TP4A (P1-(5'-ADENOSYL)P4-(5'-              
KEYWDS   2 (2'DEOXYTHYMIDIL))TETRAPHOSPHATE, TRANSFERASE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.SEGURA-PENA,S.LUTZ,C.MONNERJAHN,M.KONRAD,A.LAVIE                    
REVDAT   4   13-JUL-11 2ORV    1       VERSN                                    
REVDAT   3   24-FEB-09 2ORV    1       VERSN                                    
REVDAT   2   22-MAY-07 2ORV    1       JRNL                                     
REVDAT   1   27-MAR-07 2ORV    0                                                
JRNL        AUTH   D.SEGURA-PENA,S.LUTZ,C.MONNERJAHN,M.KONRAD,A.LAVIE           
JRNL        TITL   BINDING OF ATP TO TK1-LIKE ENZYMES IS ASSOCIATED WITH A      
JRNL        TITL 2 CONFORMATIONAL CHANGE IN THE QUATERNARY STRUCTURE.           
JRNL        REF    J.MOL.BIOL.                   V. 369   129 2007              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   17407781                                                     
JRNL        DOI    10.1016/J.JMB.2007.02.104                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 26191                          
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) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2604                            
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1768                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2840                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 184                          
REMARK   3   BIN FREE R VALUE                    : 0.3430                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2479                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 68                                      
REMARK   3   SOLVENT ATOMS            : 160                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 49.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.25                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.13000                                              
REMARK   3    B22 (A**2) : 4.13000                                              
REMARK   3    B33 (A**2) : -6.19000                                             
REMARK   3    B12 (A**2) : 2.06000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.219         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.203         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.164         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.168         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.935                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2583 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3493 ; 1.811 ; 2.008       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   319 ; 6.705 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   103 ;34.557 ;23.398       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   452 ;18.747 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    19 ;18.981 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   398 ; 0.122 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1865 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1207 ; 0.234 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1751 ; 0.312 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   148 ; 0.208 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    50 ; 0.309 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.225 ; 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):  1640 ; 0.938 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2554 ; 1.632 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1060 ; 2.127 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   939 ; 3.357 ; 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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B     18       B     191      4                      
REMARK   3           1     A     18       A     191      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   1228 ; 0.210 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   1228 ; 0.740 ; 2.000           
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                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2ORV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-FEB-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB041508.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-MAR-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.072                              
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 225 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34789                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.080                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.4                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : 0.07500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.5400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.08                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 79.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.18                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.35400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.8 M NACL, 0.1M MES, 0.1M NAH2PO4,      
REMARK 280  0.1M KH2PO4, PH 4.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE     
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       52.12000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      104.24000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      104.24000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       52.12000            
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: 11890 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 25460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      104.24000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     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     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     LYS A   192                                                      
REMARK 465     ALA A   193                                                      
REMARK 465     SER A   194                                                      
REMARK 465     GLY A   195                                                      
REMARK 465     GLN A   196                                                      
REMARK 465     PRO A   197                                                      
REMARK 465     ALA A   198                                                      
REMARK 465     GLY A   199                                                      
REMARK 465     PRO A   200                                                      
REMARK 465     ASP A   201                                                      
REMARK 465     ASN A   202                                                      
REMARK 465     ALA A   203                                                      
REMARK 465     ALA A   204                                                      
REMARK 465     ASN A   205                                                      
REMARK 465     CYS A   206                                                      
REMARK 465     PRO A   207                                                      
REMARK 465     VAL A   208                                                      
REMARK 465     PRO A   209                                                      
REMARK 465     GLY A   210                                                      
REMARK 465     LYS A   211                                                      
REMARK 465     PRO A   212                                                      
REMARK 465     GLY A   213                                                      
REMARK 465     GLU A   214                                                      
REMARK 465     ALA A   215                                                      
REMARK 465     VAL A   216                                                      
REMARK 465     ALA A   217                                                      
REMARK 465     ALA A   218                                                      
REMARK 465     ARG A   219                                                      
REMARK 465     LYS A   220                                                      
REMARK 465     LEU A   221                                                      
REMARK 465     PHE A   222                                                      
REMARK 465     ALA A   223                                                      
REMARK 465     PRO A   224                                                      
REMARK 465     GLN A   225                                                      
REMARK 465     GLN A   226                                                      
REMARK 465     ILE A   227                                                      
REMARK 465     LEU A   228                                                      
REMARK 465     GLN A   229                                                      
REMARK 465     CYS A   230                                                      
REMARK 465     SER A   231                                                      
REMARK 465     PRO A   232                                                      
REMARK 465     ALA A   233                                                      
REMARK 465     ASN A   234                                                      
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     THR B    59                                                      
REMARK 465     ARG B    60                                                      
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     LYS B   192                                                      
REMARK 465     ALA B   193                                                      
REMARK 465     SER B   194                                                      
REMARK 465     GLY B   195                                                      
REMARK 465     GLN B   196                                                      
REMARK 465     PRO B   197                                                      
REMARK 465     ALA B   198                                                      
REMARK 465     GLY B   199                                                      
REMARK 465     PRO B   200                                                      
REMARK 465     ASP B   201                                                      
REMARK 465     ASN B   202                                                      
REMARK 465     ALA B   203                                                      
REMARK 465     ALA B   204                                                      
REMARK 465     ASN B   205                                                      
REMARK 465     CYS B   206                                                      
REMARK 465     PRO B   207                                                      
REMARK 465     VAL B   208                                                      
REMARK 465     PRO B   209                                                      
REMARK 465     GLY B   210                                                      
REMARK 465     LYS B   211                                                      
REMARK 465     PRO B   212                                                      
REMARK 465     GLY B   213                                                      
REMARK 465     GLU B   214                                                      
REMARK 465     ALA B   215                                                      
REMARK 465     VAL B   216                                                      
REMARK 465     ALA B   217                                                      
REMARK 465     ALA B   218                                                      
REMARK 465     ARG B   219                                                      
REMARK 465     LYS B   220                                                      
REMARK 465     LEU B   221                                                      
REMARK 465     PHE B   222                                                      
REMARK 465     ALA B   223                                                      
REMARK 465     PRO B   224                                                      
REMARK 465     GLN B   225                                                      
REMARK 465     GLN B   226                                                      
REMARK 465     ILE B   227                                                      
REMARK 465     LEU B   228                                                      
REMARK 465     GLN B   229                                                      
REMARK 465     CYS B   230                                                      
REMARK 465     SER B   231                                                      
REMARK 465     PRO B   232                                                      
REMARK 465     ALA B   233                                                      
REMARK 465     ASN B   234                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  54    CG   CD   CE   NZ                                   
REMARK 470     TYR A  61    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG A  82    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  54    CG   CD   CE   NZ                                   
REMARK 470     ARG B  82    CG   CD   NE   CZ   NH1  NH2                        
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   CG1  ILE B   105     O    HOH B   865              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS A 109   CB    CYS A 109   SG     -0.110                       
REMARK 500    ASP B 104   CB    ASP B 104   CG      0.150                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP B 104   CB  -  CG  -  OD2 ANGL. DEV. =   9.8 DEGREES          
REMARK 500    LEU B 124   CA  -  CB  -  CG  ANGL. DEV. =  15.4 DEGREES          
REMARK 500    ARG B 130   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
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    GLN A  47       33.98     75.42                                   
REMARK 500    THR A  59       70.77   -118.22                                   
REMARK 500    GLU A  98       47.50     38.28                                   
REMARK 500    ALA A 123      148.10   -170.99                                   
REMARK 500    THR A 127     -173.71    -68.40                                   
REMARK 500    ILE B  45       -5.31    -59.25                                   
REMARK 500    GLN B  47       33.50     80.55                                   
REMARK 500    CYS B 156       -6.14   -147.07                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 854        DISTANCE =  6.04 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     4TA A  801                                                       
REMARK 610     4TA B  802                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 235  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 188   SG                                                     
REMARK 620 2 CYS A 156   SG  114.5                                              
REMARK 620 3 CYS A 153   SG   98.2 112.4                                        
REMARK 620 4 CYS A 185   SG  106.1 110.8 114.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 235  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 156   SG                                                     
REMARK 620 2 CYS B 185   SG  116.4                                              
REMARK 620 3 CYS B 188   SG  115.6  96.0                                        
REMARK 620 4 CYS B 153   SG  113.3 111.9 101.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 235                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 235                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4TA A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4TA B 802                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2ORW   RELATED DB: PDB                                   
REMARK 900 THERMOTOGA MARITIMA THYMIDINE KINASE 1 LIKE ENZYME IN                
REMARK 900 COMPLEX WITH TP4A                                                    
DBREF  2ORV A    1   234  UNP    P04183   KITH_HUMAN       1    234             
DBREF  2ORV B    1   234  UNP    P04183   KITH_HUMAN       1    234             
SEQADV 2ORV ALA A  203  UNP  P04183    LYS   203 ENGINEERED                     
SEQADV 2ORV ALA A  204  UNP  P04183    GLU   204 ENGINEERED                     
SEQADV 2ORV ALA B  203  UNP  P04183    LYS   203 ENGINEERED                     
SEQADV 2ORV ALA B  204  UNP  P04183    GLU   204 ENGINEERED                     
SEQRES   1 A  234  MET SER CYS ILE ASN LEU PRO THR VAL LEU PRO GLY SER          
SEQRES   2 A  234  PRO SER LYS THR ARG GLY GLN ILE GLN VAL ILE LEU GLY          
SEQRES   3 A  234  PRO MET PHE SER GLY LYS SER THR GLU LEU MET ARG ARG          
SEQRES   4 A  234  VAL ARG ARG PHE GLN ILE ALA GLN TYR LYS CYS LEU VAL          
SEQRES   5 A  234  ILE LYS TYR ALA LYS ASP THR ARG TYR SER SER SER PHE          
SEQRES   6 A  234  CYS THR HIS ASP ARG ASN THR MET GLU ALA LEU PRO ALA          
SEQRES   7 A  234  CYS LEU LEU ARG ASP VAL ALA GLN GLU ALA LEU GLY VAL          
SEQRES   8 A  234  ALA VAL ILE GLY ILE ASP GLU GLY GLN PHE PHE PRO ASP          
SEQRES   9 A  234  ILE VAL GLU PHE CYS GLU ALA MET ALA ASN ALA GLY LYS          
SEQRES  10 A  234  THR VAL ILE VAL ALA ALA LEU ASP GLY THR PHE GLN ARG          
SEQRES  11 A  234  LYS PRO PHE GLY ALA ILE LEU ASN LEU VAL PRO LEU ALA          
SEQRES  12 A  234  GLU SER VAL VAL LYS LEU THR ALA VAL CYS MET GLU CYS          
SEQRES  13 A  234  PHE ARG GLU ALA ALA TYR THR LYS ARG LEU GLY THR GLU          
SEQRES  14 A  234  LYS GLU VAL GLU VAL ILE GLY GLY ALA ASP LYS TYR HIS          
SEQRES  15 A  234  SER VAL CYS ARG LEU CYS TYR PHE LYS LYS ALA SER GLY          
SEQRES  16 A  234  GLN PRO ALA GLY PRO ASP ASN ALA ALA ASN CYS PRO VAL          
SEQRES  17 A  234  PRO GLY LYS PRO GLY GLU ALA VAL ALA ALA ARG LYS LEU          
SEQRES  18 A  234  PHE ALA PRO GLN GLN ILE LEU GLN CYS SER PRO ALA ASN          
SEQRES   1 B  234  MET SER CYS ILE ASN LEU PRO THR VAL LEU PRO GLY SER          
SEQRES   2 B  234  PRO SER LYS THR ARG GLY GLN ILE GLN VAL ILE LEU GLY          
SEQRES   3 B  234  PRO MET PHE SER GLY LYS SER THR GLU LEU MET ARG ARG          
SEQRES   4 B  234  VAL ARG ARG PHE GLN ILE ALA GLN TYR LYS CYS LEU VAL          
SEQRES   5 B  234  ILE LYS TYR ALA LYS ASP THR ARG TYR SER SER SER PHE          
SEQRES   6 B  234  CYS THR HIS ASP ARG ASN THR MET GLU ALA LEU PRO ALA          
SEQRES   7 B  234  CYS LEU LEU ARG ASP VAL ALA GLN GLU ALA LEU GLY VAL          
SEQRES   8 B  234  ALA VAL ILE GLY ILE ASP GLU GLY GLN PHE PHE PRO ASP          
SEQRES   9 B  234  ILE VAL GLU PHE CYS GLU ALA MET ALA ASN ALA GLY LYS          
SEQRES  10 B  234  THR VAL ILE VAL ALA ALA LEU ASP GLY THR PHE GLN ARG          
SEQRES  11 B  234  LYS PRO PHE GLY ALA ILE LEU ASN LEU VAL PRO LEU ALA          
SEQRES  12 B  234  GLU SER VAL VAL LYS LEU THR ALA VAL CYS MET GLU CYS          
SEQRES  13 B  234  PHE ARG GLU ALA ALA TYR THR LYS ARG LEU GLY THR GLU          
SEQRES  14 B  234  LYS GLU VAL GLU VAL ILE GLY GLY ALA ASP LYS TYR HIS          
SEQRES  15 B  234  SER VAL CYS ARG LEU CYS TYR PHE LYS LYS ALA SER GLY          
SEQRES  16 B  234  GLN PRO ALA GLY PRO ASP ASN ALA ALA ASN CYS PRO VAL          
SEQRES  17 B  234  PRO GLY LYS PRO GLY GLU ALA VAL ALA ALA ARG LYS LEU          
SEQRES  18 B  234  PHE ALA PRO GLN GLN ILE LEU GLN CYS SER PRO ALA ASN          
HET     ZN  A 235       1                                                       
HET     ZN  B 235       1                                                       
HET    4TA  A 801      33                                                       
HET    4TA  B 802      33                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     4TA P1-(5'-ADENOSYL)P4-(5'-(2'-DEOXY-THYMIDYL))                      
HETNAM   2 4TA  TETRAPHOSPHATE                                                  
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   5  4TA    2(C20 H25 N7 O20 P4 4-)                                      
FORMUL   7  HOH   *160(H2 O)                                                    
HELIX    1   1 GLY A   31  ILE A   45  1                                  15    
HELIX    2   2 LEU A   80  ASP A   83  5                                   4    
HELIX    3   3 VAL A   84  LEU A   89  1                                   6    
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  LYS A  191  1                                   7    
HELIX    8   8 GLY B   31  ILE B   45  1                                  15    
HELIX    9   9 LEU B   80  ASP B   83  5                                   4    
HELIX   10  10 VAL B   84  LEU B   89  1                                   6    
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  PHE B  190  1                                   6    
SHEET    1   A 6 GLU A  74  ALA A  78  0                                        
SHEET    2   A 6 CYS A  50  TYR A  55  1  N  VAL A  52   O  GLU A  74           
SHEET    3   A 6 VAL A  93  ILE A  96  1  O  GLY A  95   N  LEU A  51           
SHEET    4   A 6 THR A 118  ALA A 122  1  O  ILE A 120   N  ILE A  96           
SHEET    5   A 6 GLN A  20  LEU A  25  1  N  ILE A  24   O  VAL A 121           
SHEET    6   A 6 SER A 145  LYS A 148  1  O  VAL A 147   N  LEU A  25           
SHEET    1   B 2 ALA A 151  VAL A 152  0                                        
SHEET    2   B 2 GLU A 159  ALA A 160 -1  O  ALA A 160   N  ALA A 151           
SHEET    1   C 2 TYR A 162  ARG A 165  0                                        
SHEET    2   C 2 TYR A 181  VAL A 184 -1  O  VAL A 184   N  TYR A 162           
SHEET    1   D 6 GLU B  74  ALA B  78  0                                        
SHEET    2   D 6 CYS B  50  TYR B  55  1  N  LYS B  54   O  LEU B  76           
SHEET    3   D 6 VAL B  93  ILE B  96  1  O  GLY B  95   N  ILE B  53           
SHEET    4   D 6 THR B 118  ALA B 122  1  O  ALA B 122   N  ILE B  96           
SHEET    5   D 6 GLN B  20  LEU B  25  1  N  ILE B  24   O  VAL B 121           
SHEET    6   D 6 SER B 145  LYS B 148  1  O  SER B 145   N  VAL B  23           
SHEET    1   E 2 ALA B 151  VAL B 152  0                                        
SHEET    2   E 2 GLU B 159  ALA B 160 -1  O  ALA B 160   N  ALA B 151           
SHEET    1   F 2 TYR B 162  ARG B 165  0                                        
SHEET    2   F 2 TYR B 181  VAL B 184 -1  O  HIS B 182   N  LYS B 164           
LINK        ZN    ZN A 235                 SG  CYS A 188     1555   1555  2.30  
LINK        ZN    ZN A 235                 SG  CYS A 156     1555   1555  2.01  
LINK        ZN    ZN A 235                 SG  CYS A 153     1555   1555  2.45  
LINK        ZN    ZN A 235                 SG  CYS A 185     1555   1555  2.49  
LINK        ZN    ZN B 235                 SG  CYS B 156     1555   1555  2.26  
LINK        ZN    ZN B 235                 SG  CYS B 185     1555   1555  2.48  
LINK        ZN    ZN B 235                 SG  CYS B 188     1555   1555  2.43  
LINK        ZN    ZN B 235                 SG  CYS B 153     1555   1555  2.39  
SITE     1 AC1  4 CYS A 153  CYS A 156  CYS A 185  CYS A 188                    
SITE     1 AC2  4 CYS B 153  CYS B 156  CYS B 185  CYS B 188                    
SITE     1 AC3 30 MET A  28  PHE A  29  SER A  30  GLY A  31                    
SITE     2 AC3 30 LYS A  32  SER A  33  ASP A  58  ARG A  60                    
SITE     3 AC3 30 ASP A  97  GLU A  98  GLN A 100  PHE A 101                    
SITE     4 AC3 30 LEU A 124  THR A 127  PHE A 128  PHE A 133                    
SITE     5 AC3 30 VAL A 172  GLU A 173  VAL A 174  ILE A 175                    
SITE     6 AC3 30 GLY A 176  TYR A 181  HOH A 806  HOH A 810                    
SITE     7 AC3 30 HOH A 823  HOH A 831  HOH A 846  HOH A 863                    
SITE     8 AC3 30 HOH A 868  HOH A 880                                          
SITE     1 AC4 27 MET B  28  PHE B  29  SER B  30  GLY B  31                    
SITE     2 AC4 27 LYS B  32  SER B  33  ASP B  58  ASP B  97                    
SITE     3 AC4 27 GLU B  98  GLN B 100  PHE B 101  LEU B 124                    
SITE     4 AC4 27 THR B 127  PHE B 128  PHE B 133  THR B 163                    
SITE     5 AC4 27 ARG B 165  VAL B 172  GLU B 173  VAL B 174                    
SITE     6 AC4 27 ILE B 175  GLY B 176  TYR B 181  HOH B 808                    
SITE     7 AC4 27 HOH B 821  HOH B 834  HOH B 872                               
CRYST1   80.980   80.980  156.360  90.00  90.00 120.00 P 31 2 1     12          
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      0.012349  0.007130  0.000000        0.00000                         
SCALE2      0.000000  0.014259  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006395        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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