GenomeNet

Database: PDB
Entry: 1XBT
LinkDB: 1XBT
Original site: 1XBT 
HEADER    TRANSFERASE                             31-AUG-04   1XBT              
TITLE     CRYSTAL STRUCTURE OF HUMAN THYMIDINE KINASE 1                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THYMIDINE KINASE, CYTOSOLIC;                               
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 FRAGMENT: TRUNCATION MUTANT(RESIDUES 1-193);                         
COMPND   5 SYNONYM: DEOXYRIBONUCLEOSIDE KINASE;                                 
COMPND   6 EC: 2.7.1.21;                                                        
COMPND   7 ENGINEERED: 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_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGEX-2T                                   
KEYWDS    DEOXYRIBONUCLEOSIDE KINASE, ZINC-BINDING DOMAIN, FEEDBACK             
KEYWDS   2 INHIBITOR, TRANSFERASE                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.WELIN,U.KOSINSKA,N.E.MIKKELSEN,C.CARNROT,C.ZHU,L.WANG,              
AUTHOR   2 S.ERIKSSON,B.MUNCH-PETERSEN,H.EKLUND                                 
REVDAT   3   24-FEB-09 1XBT    1       VERSN                                    
REVDAT   2   11-JAN-05 1XBT    1       JRNL                                     
REVDAT   1   14-DEC-04 1XBT    0                                                
JRNL        AUTH   M.WELIN,U.KOSINSKA,N.E.MIKKELSEN,C.CARNROT,C.ZHU,            
JRNL        AUTH 2 L.WANG,S.ERIKSSON,B.MUNCH-PETERSEN,H.EKLUND                  
JRNL        TITL   STRUCTURES OF THYMIDINE KINASE 1 OF HUMAN AND                
JRNL        TITL 2 MYCOPLASMIC ORIGIN                                           
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 101 17970 2004              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   15611477                                                     
JRNL        DOI    10.1073/PNAS.0406332102                                      
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.07                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 62088                          
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) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.232                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3317                            
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) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4560                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2410                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 246                          
REMARK   3   BIN FREE R VALUE                    : 0.2800                       
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          : 248                                     
REMARK   3   SOLVENT ATOMS            : 213                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.86000                                              
REMARK   3    B22 (A**2) : -0.50000                                             
REMARK   3    B33 (A**2) : -0.07000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.78000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.354         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.233         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.160         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.798         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.933                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.914                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10377 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14005 ; 1.259 ; 1.999       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1273 ; 5.619 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1593 ; 0.088 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7504 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4395 ; 0.184 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   482 ; 0.143 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     8 ; 0.235 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    55 ; 0.176 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    10 ; 0.110 ; 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):  6373 ; 0.519 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10216 ; 1.024 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4004 ; 1.461 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3789 ; 2.541 ; 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                    : A B C D E F G H                 
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     18       A      58      2                      
REMARK   3           1     B     18       B      58      2                      
REMARK   3           1     C     18       C      58      2                      
REMARK   3           1     D     18       D      58      2                      
REMARK   3           1     E     18       E      58      2                      
REMARK   3           1     F     18       F      58      2                      
REMARK   3           1     G     18       G      58      2                      
REMARK   3           1     H     18       H      58      2                      
REMARK   3           2     A     75       A     191      2                      
REMARK   3           2     B     75       B     191      2                      
REMARK   3           2     C     75       C     191      2                      
REMARK   3           2     D     75       D     191      2                      
REMARK   3           2     E     75       E     191      2                      
REMARK   3           2     F     75       F     192      2                      
REMARK   3           2     G     75       G     191      2                      
REMARK   3           2     H     75       H     191      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):    632 ;  0.03 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    B    (A):    632 ;  0.03 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    C    (A):    632 ;  0.03 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    D    (A):    632 ;  0.03 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    E    (A):    632 ;  0.03 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    F    (A):    632 ;  0.03 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    G    (A):    632 ;  0.03 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    H    (A):    632 ;  0.03 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    589 ;  0.44 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):    589 ;  0.41 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):    589 ;  0.48 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):    589 ;  0.39 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    E    (A):    589 ;  0.44 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    F    (A):    589 ;  0.41 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    G    (A):    589 ;  0.38 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    H    (A):    589 ;  0.43 ;  0.50           
REMARK   3   TIGHT THERMAL      1    A (A**2):    632 ;  0.05 ;  0.50           
REMARK   3   TIGHT THERMAL      1    B (A**2):    632 ;  0.06 ;  0.50           
REMARK   3   TIGHT THERMAL      1    C (A**2):    632 ;  0.08 ;  0.50           
REMARK   3   TIGHT THERMAL      1    D (A**2):    632 ;  0.06 ;  0.50           
REMARK   3   TIGHT THERMAL      1    E (A**2):    632 ;  0.05 ;  0.50           
REMARK   3   TIGHT THERMAL      1    F (A**2):    632 ;  0.06 ;  0.50           
REMARK   3   TIGHT THERMAL      1    G (A**2):    632 ;  0.08 ;  0.50           
REMARK   3   TIGHT THERMAL      1    H (A**2):    632 ;  0.06 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    589 ;  0.41 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):    589 ;  0.40 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    C (A**2):    589 ;  0.59 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    D (A**2):    589 ;  0.40 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    E (A**2):    589 ;  0.46 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    F (A**2):    589 ;  0.43 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    G (A**2):    589 ;  0.50 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    H (A**2):    589 ;  0.42 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1XBT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-SEP-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB030179.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-DEC-03                          
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                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 77566                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 87.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 28.4                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.37                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.43400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS                        
REMARK 200 SOFTWARE USED: AUTOSHARP                                             
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, 2-PROPANOL, PEG          
REMARK 280  4000, PH 5.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 288.0K     
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       78.83600            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       61.58850            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       78.83600            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       61.58850            
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: 12360 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 25830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -93.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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: 12430 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 26040 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -98.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     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     LYS B   192                                                      
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     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     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     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     SER H    62                                                      
REMARK 465     SER H    63                                                      
REMARK 465     SER H    64                                                      
REMARK 465     PHE H    65                                                      
REMARK 465     CYS H    66                                                      
REMARK 465     THR H    67                                                      
REMARK 465     HIS H    68                                                      
REMARK 465     ASP H    69                                                      
REMARK 465     ARG H    70                                                      
REMARK 465     ASN H    71                                                      
REMARK 465     THR H    72                                                      
REMARK 465     MET H    73                                                      
REMARK 465     GLU H    74                                                      
REMARK 465     LYS H   192                                                      
REMARK 465     ALA H   193                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 104   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP B 104   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP B 125   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP C 104   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP C 125   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP D 104   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP E 104   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ASP E 179   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP G  97   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 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  20      145.05   -171.11                                   
REMARK 500    GLN B  47        6.70     82.99                                   
REMARK 500    THR B  59       58.79   -114.91                                   
REMARK 500    GLN C  47        9.08     83.87                                   
REMARK 500    GLN E  47        7.26     83.02                                   
REMARK 500    GLN F  47        7.68     82.33                                   
REMARK 500    SER G  63       33.37    -96.38                                   
REMARK 500    GLN H  47        6.57     82.88                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1193  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 153   SG                                                     
REMARK 620 2 CYS A 156   SG  111.5                                              
REMARK 620 3 CYS A 185   SG  118.7 109.7                                        
REMARK 620 4 CYS A 188   SG  105.2 108.7 102.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B2193  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 153   SG                                                     
REMARK 620 2 CYS B 156   SG  114.3                                              
REMARK 620 3 CYS B 185   SG  119.5 108.5                                        
REMARK 620 4 CYS B 188   SG   99.2 112.8 101.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C3193  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 153   SG                                                     
REMARK 620 2 CYS C 156   SG  118.5                                              
REMARK 620 3 CYS C 185   SG  120.4 107.4                                        
REMARK 620 4 CYS C 188   SG   98.0 111.7  98.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D4193  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 153   SG                                                     
REMARK 620 2 CYS D 156   SG  110.7                                              
REMARK 620 3 CYS D 185   SG  121.3 108.1                                        
REMARK 620 4 CYS D 188   SG  102.8 112.9 100.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E5193  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS E 153   SG                                                     
REMARK 620 2 CYS E 156   SG  114.6                                              
REMARK 620 3 CYS E 185   SG  118.8 103.2                                        
REMARK 620 4 CYS E 188   SG  102.3 118.0  99.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F6193  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F 153   SG                                                     
REMARK 620 2 CYS F 156   SG  110.8                                              
REMARK 620 3 CYS F 185   SG  118.9 108.8                                        
REMARK 620 4 CYS F 188   SG  103.8 111.9 102.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G7193  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS G 153   SG                                                     
REMARK 620 2 CYS G 156   SG  112.4                                              
REMARK 620 3 CYS G 185   SG  120.4 107.3                                        
REMARK 620 4 CYS G 188   SG  101.2 115.1 100.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN H8193  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS H 153   SG                                                     
REMARK 620 2 CYS H 156   SG  111.9                                              
REMARK 620 3 CYS H 185   SG  118.3 108.7                                        
REMARK 620 4 CYS H 188   SG  103.4 113.7 100.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1194  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TTP A1195   O1A                                                    
REMARK 620 2 TTP A1195   O1B  84.1                                              
REMARK 620 3 TTP A1195   O1G  77.1  67.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B2194  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TTP B2195   O1B                                                    
REMARK 620 2 TTP B2195   O1A  92.5                                              
REMARK 620 3 SER B  33   OG  139.6 118.7                                        
REMARK 620 4 TTP B2195   O3B  55.7  70.1 109.0                                  
REMARK 620 5 TTP B2195   O1G  87.8 107.1  60.0  51.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C3194  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TTP C3195   O1A                                                    
REMARK 620 2 TTP C3195   O3B  70.8                                              
REMARK 620 3 TTP C3195   O1G 117.4  54.2                                        
REMARK 620 4 HOH C3215   O    62.0  97.2  95.3                                  
REMARK 620 5 SER C  33   OG  127.1 129.4  78.9  66.9                            
REMARK 620 6 TTP C3195   O1B  87.7  54.4  83.6 145.3 145.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D4194  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TTP D4195   O1G                                                    
REMARK 620 2 TTP D4195   O1A 103.3                                              
REMARK 620 3 SER D  33   OG   91.7 129.1                                        
REMARK 620 4 HOH D4229   O   164.0  92.7  78.8                                  
REMARK 620 5 TTP D4195   O1B  82.1  71.3 159.6 102.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E5194  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER E  33   OG                                                     
REMARK 620 2 TTP E5195   O1A 144.8                                              
REMARK 620 3 TTP E5195   O1G  81.0 101.1                                        
REMARK 620 4 TTP E5195   O1B 138.3  74.3  75.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG F6194  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TTP F6195   O1B                                                    
REMARK 620 2 TTP F6195   O1G  75.8                                              
REMARK 620 3 HOH F6219   O   127.7  89.1                                        
REMARK 620 4 SER F  33   OG  152.6  88.2  73.0                                  
REMARK 620 5 TTP F6195   O1A  72.4  94.3  59.0 131.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG G7194  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TTP G7195   O1G                                                    
REMARK 620 2 HOH G7228   O    88.1                                              
REMARK 620 3 TTP G7195   O1A  92.6 151.6                                        
REMARK 620 4 TTP G7195   O1B  77.1  73.6  78.9                                  
REMARK 620 5 SER G  33   OG   83.4  82.7 125.7 149.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG H8194  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TTP H8195   O1B                                                    
REMARK 620 2 TTP H8195   O1A  73.7                                              
REMARK 620 3 HOH H8217   O    86.8 152.3                                        
REMARK 620 4 TTP H8195   O1G  89.5  95.3 104.1                                  
REMARK 620 5 SER H  33   OG  171.6 113.8  87.3  86.0                            
REMARK 620 N                    1     2     3     4                             
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 1193                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 2193                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 3193                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 4193                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 5193                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 6193                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN G 7193                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 8193                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1194                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 2194                 
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 3194                 
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 4194                 
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 5194                 
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 6194                 
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 7194                 
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 8194                 
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP A 1195                
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP B 2195                
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP C 3195                
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP D 4195                
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP E 5195                
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP F 6195                
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP G 7195                
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP H 8195                
DBREF  1XBT A    1   193  UNP    P04183   KITH_HUMAN       1    193             
DBREF  1XBT B    1   193  UNP    P04183   KITH_HUMAN       1    193             
DBREF  1XBT C    1   193  UNP    P04183   KITH_HUMAN       1    193             
DBREF  1XBT D    1   193  UNP    P04183   KITH_HUMAN       1    193             
DBREF  1XBT E    1   193  UNP    P04183   KITH_HUMAN       1    193             
DBREF  1XBT F    1   193  UNP    P04183   KITH_HUMAN       1    193             
DBREF  1XBT G    1   193  UNP    P04183   KITH_HUMAN       1    193             
DBREF  1XBT H    1   193  UNP    P04183   KITH_HUMAN       1    193             
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 THR 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 THR 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 THR 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 THR 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 THR 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 THR 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 THR 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 THR 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     ZN  A1193       1                                                       
HET     ZN  B2193       1                                                       
HET     ZN  C3193       1                                                       
HET     ZN  D4193       1                                                       
HET     ZN  E5193       1                                                       
HET     ZN  F6193       1                                                       
HET     ZN  G7193       1                                                       
HET     ZN  H8193       1                                                       
HET     MG  A1194       1                                                       
HET     MG  B2194       1                                                       
HET     MG  C3194       1                                                       
HET     MG  D4194       1                                                       
HET     MG  E5194       1                                                       
HET     MG  F6194       1                                                       
HET     MG  G7194       1                                                       
HET     MG  H8194       1                                                       
HET    TTP  A1195      29                                                       
HET    TTP  B2195      29                                                       
HET    TTP  C3195      29                                                       
HET    TTP  D4195      29                                                       
HET    TTP  E5195      29                                                       
HET    TTP  F6195      29                                                       
HET    TTP  G7195      29                                                       
HET    TTP  H8195      29                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     TTP THYMIDINE-5'-TRIPHOSPHATE                                        
FORMUL   9   ZN    8(ZN 2+)                                                     
FORMUL  17   MG    8(MG 2+)                                                     
FORMUL  25  TTP    8(C10 H17 N2 O14 P3)                                         
FORMUL  33  HOH   *213(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  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  ILE B   45  1                                  15    
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  LYS D  191  1                                   7    
HELIX   29  29 GLY E   31  ILE E   45  1                                  15    
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 GLY F   99  PHE F  102  5                                   4    
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  LYS F  191  1                                   7    
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 GLY H   99  PHE H  102  5                                   4    
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  LYS H  191  1                                   7    
SHEET    1   A 6 LEU A  76  ALA A  78  0                                        
SHEET    2   A 6 CYS A  50  TYR A  55  1  N  LYS A  54   O  LEU A  76           
SHEET    3   A 6 VAL A  93  ILE A  96  1  O  GLY A  95   N  ILE A  53           
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  HIS A 182   N  LYS A 164           
SHEET    1   D 6 LEU B  76  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  LEU B  51           
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  VAL B 147   N  LEU B  25           
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           
SHEET    1   G 6 LEU C  76  ALA C  78  0                                        
SHEET    2   G 6 CYS C  50  TYR C  55  1  N  LYS C  54   O  LEU C  76           
SHEET    3   G 6 VAL C  93  ILE C  96  1  O  GLY C  95   N  ILE C  53           
SHEET    4   G 6 THR C 118  ALA C 122  1  O  ILE C 120   N  ILE C  96           
SHEET    5   G 6 GLN C  20  LEU C  25  1  N  ILE C  24   O  VAL C 121           
SHEET    6   G 6 SER C 145  LYS C 148  1  O  VAL C 147   N  LEU C  25           
SHEET    1   H 2 ALA C 151  VAL C 152  0                                        
SHEET    2   H 2 GLU C 159  ALA C 160 -1  O  ALA C 160   N  ALA C 151           
SHEET    1   I 2 TYR C 162  ARG C 165  0                                        
SHEET    2   I 2 TYR C 181  VAL C 184 -1  O  HIS C 182   N  LYS C 164           
SHEET    1   J 6 LEU D  76  ALA D  78  0                                        
SHEET    2   J 6 CYS D  50  TYR D  55  1  N  LYS D  54   O  LEU D  76           
SHEET    3   J 6 VAL D  93  ASP D  97  1  O  GLY D  95   N  LEU D  51           
SHEET    4   J 6 THR D 118  ALA D 122  1  O  THR D 118   N  ILE D  94           
SHEET    5   J 6 GLN D  20  LEU D  25  1  N  ILE D  24   O  VAL D 121           
SHEET    6   J 6 SER D 145  LYS D 148  1  O  VAL D 147   N  LEU D  25           
SHEET    1   K 2 ALA D 151  VAL D 152  0                                        
SHEET    2   K 2 GLU D 159  ALA D 160 -1  O  ALA D 160   N  ALA D 151           
SHEET    1   L 2 TYR D 162  ARG D 165  0                                        
SHEET    2   L 2 TYR D 181  VAL D 184 -1  O  HIS D 182   N  LYS D 164           
SHEET    1   M 6 LEU E  76  ALA E  78  0                                        
SHEET    2   M 6 CYS E  50  TYR E  55  1  N  LYS E  54   O  LEU E  76           
SHEET    3   M 6 VAL E  93  ILE E  96  1  O  GLY E  95   N  LEU E  51           
SHEET    4   M 6 THR E 118  ALA E 122  1  O  THR E 118   N  ILE E  94           
SHEET    5   M 6 GLN E  20  LEU E  25  1  N  ILE E  24   O  VAL E 121           
SHEET    6   M 6 SER E 145  LYS E 148  1  O  VAL E 147   N  LEU E  25           
SHEET    1   N 2 ALA E 151  VAL E 152  0                                        
SHEET    2   N 2 GLU E 159  ALA E 160 -1  O  ALA E 160   N  ALA E 151           
SHEET    1   O 2 TYR E 162  ARG E 165  0                                        
SHEET    2   O 2 TYR E 181  VAL E 184 -1  O  HIS E 182   N  LYS E 164           
SHEET    1   P 6 LEU F  76  ALA F  78  0                                        
SHEET    2   P 6 CYS F  50  TYR F  55  1  N  LYS F  54   O  LEU F  76           
SHEET    3   P 6 VAL F  93  ASP F  97  1  O  GLY F  95   N  ILE F  53           
SHEET    4   P 6 THR F 118  ALA F 122  1  O  ILE F 120   N  ILE F  96           
SHEET    5   P 6 GLN F  20  LEU F  25  1  N  ILE F  24   O  VAL F 121           
SHEET    6   P 6 SER F 145  LYS F 148  1  O  VAL F 147   N  LEU F  25           
SHEET    1   Q 2 ALA F 151  VAL F 152  0                                        
SHEET    2   Q 2 GLU F 159  ALA F 160 -1  O  ALA F 160   N  ALA F 151           
SHEET    1   R 2 TYR F 162  ARG F 165  0                                        
SHEET    2   R 2 TYR F 181  VAL F 184 -1  O  HIS F 182   N  LYS F 164           
SHEET    1   S 6 ALA G  75  ALA G  78  0                                        
SHEET    2   S 6 CYS G  50  TYR G  55  1  N  LYS G  54   O  LEU G  76           
SHEET    3   S 6 VAL G  93  ASP G  97  1  O  GLY G  95   N  ILE G  53           
SHEET    4   S 6 THR G 118  LEU G 124  1  O  ILE G 120   N  ILE G  94           
SHEET    5   S 6 GLN G  20  GLY G  26  1  N  ILE G  24   O  VAL G 121           
SHEET    6   S 6 SER G 145  LYS G 148  1  O  VAL G 147   N  LEU G  25           
SHEET    1   T 2 ALA G 151  VAL G 152  0                                        
SHEET    2   T 2 GLU G 159  ALA G 160 -1  O  ALA G 160   N  ALA G 151           
SHEET    1   U 2 TYR G 162  ARG G 165  0                                        
SHEET    2   U 2 TYR G 181  VAL G 184 -1  O  HIS G 182   N  LYS G 164           
SHEET    1   V 6 LEU H  76  ALA H  78  0                                        
SHEET    2   V 6 CYS H  50  TYR H  55  1  N  LYS H  54   O  LEU H  76           
SHEET    3   V 6 VAL H  93  ASP H  97  1  O  GLY H  95   N  LEU H  51           
SHEET    4   V 6 THR H 118  LEU H 124  1  O  ILE H 120   N  ILE H  94           
SHEET    5   V 6 GLN H  20  GLY H  26  1  N  ILE H  24   O  VAL H 121           
SHEET    6   V 6 SER H 145  LYS H 148  1  O  VAL H 147   N  LEU H  25           
SHEET    1   W 2 ALA H 151  VAL H 152  0                                        
SHEET    2   W 2 GLU H 159  ALA H 160 -1  O  ALA H 160   N  ALA H 151           
SHEET    1   X 2 TYR H 162  ARG H 165  0                                        
SHEET    2   X 2 TYR H 181  VAL H 184 -1  O  HIS H 182   N  LYS H 164           
LINK        ZN    ZN A1193                 SG  CYS A 153     1555   1555  2.29  
LINK        ZN    ZN A1193                 SG  CYS A 156     1555   1555  2.38  
LINK        ZN    ZN A1193                 SG  CYS A 185     1555   1555  2.34  
LINK        ZN    ZN A1193                 SG  CYS A 188     1555   1555  2.42  
LINK        ZN    ZN B2193                 SG  CYS B 153     1555   1555  2.34  
LINK        ZN    ZN B2193                 SG  CYS B 156     1555   1555  2.18  
LINK        ZN    ZN B2193                 SG  CYS B 185     1555   1555  2.37  
LINK        ZN    ZN B2193                 SG  CYS B 188     1555   1555  2.21  
LINK        ZN    ZN C3193                 SG  CYS C 153     1555   1555  2.25  
LINK        ZN    ZN C3193                 SG  CYS C 156     1555   1555  2.04  
LINK        ZN    ZN C3193                 SG  CYS C 185     1555   1555  2.38  
LINK        ZN    ZN C3193                 SG  CYS C 188     1555   1555  2.46  
LINK        ZN    ZN D4193                 SG  CYS D 153     1555   1555  2.29  
LINK        ZN    ZN D4193                 SG  CYS D 156     1555   1555  2.37  
LINK        ZN    ZN D4193                 SG  CYS D 185     1555   1555  2.34  
LINK        ZN    ZN D4193                 SG  CYS D 188     1555   1555  2.35  
LINK        ZN    ZN E5193                 SG  CYS E 153     1555   1555  2.32  
LINK        ZN    ZN E5193                 SG  CYS E 156     1555   1555  2.30  
LINK        ZN    ZN E5193                 SG  CYS E 185     1555   1555  2.36  
LINK        ZN    ZN E5193                 SG  CYS E 188     1555   1555  2.26  
LINK        ZN    ZN F6193                 SG  CYS F 153     1555   1555  2.24  
LINK        ZN    ZN F6193                 SG  CYS F 156     1555   1555  2.27  
LINK        ZN    ZN F6193                 SG  CYS F 185     1555   1555  2.35  
LINK        ZN    ZN F6193                 SG  CYS F 188     1555   1555  2.41  
LINK        ZN    ZN G7193                 SG  CYS G 153     1555   1555  2.32  
LINK        ZN    ZN G7193                 SG  CYS G 156     1555   1555  2.31  
LINK        ZN    ZN G7193                 SG  CYS G 185     1555   1555  2.31  
LINK        ZN    ZN G7193                 SG  CYS G 188     1555   1555  2.27  
LINK        ZN    ZN H8193                 SG  CYS H 153     1555   1555  2.34  
LINK        ZN    ZN H8193                 SG  CYS H 156     1555   1555  2.15  
LINK        ZN    ZN H8193                 SG  CYS H 185     1555   1555  2.29  
LINK        ZN    ZN H8193                 SG  CYS H 188     1555   1555  2.34  
LINK        MG    MG A1194                 O1A TTP A1195     1555   1555  2.03  
LINK        MG    MG A1194                 O1B TTP A1195     1555   1555  2.40  
LINK        MG    MG A1194                 O1G TTP A1195     1555   1555  2.97  
LINK        MG    MG B2194                 O1B TTP B2195     1555   1555  2.57  
LINK        MG    MG B2194                 O1A TTP B2195     1555   1555  2.10  
LINK        MG    MG B2194                 OG  SER B  33     1555   1555  2.74  
LINK        MG    MG B2194                 O3B TTP B2195     1555   1555  2.83  
LINK        MG    MG B2194                 O1G TTP B2195     1555   1555  2.77  
LINK        MG    MG C3194                 O1A TTP C3195     1555   1555  2.08  
LINK        MG    MG C3194                 O3B TTP C3195     1555   1555  2.83  
LINK        MG    MG C3194                 O1G TTP C3195     1555   1555  2.38  
LINK        MG    MG C3194                 O   HOH C3215     1555   1555  2.89  
LINK        MG    MG C3194                 OG  SER C  33     1555   1555  2.64  
LINK        MG    MG C3194                 O1B TTP C3195     1555   1555  2.67  
LINK        MG    MG D4194                 O1G TTP D4195     1555   1555  2.06  
LINK        MG    MG D4194                 O1A TTP D4195     1555   1555  2.16  
LINK        MG    MG D4194                 OG  SER D  33     1555   1555  2.24  
LINK        MG    MG D4194                 O   HOH D4229     1555   1555  2.04  
LINK        MG    MG D4194                 O1B TTP D4195     1555   1555  2.40  
LINK        MG    MG E5194                 OG  SER E  33     1555   1555  2.29  
LINK        MG    MG E5194                 O1A TTP E5195     1555   1555  2.12  
LINK        MG    MG E5194                 O1G TTP E5195     1555   1555  2.49  
LINK        MG    MG E5194                 O1B TTP E5195     1555   1555  3.00  
LINK        MG    MG F6194                 O1B TTP F6195     1555   1555  2.69  
LINK        MG    MG F6194                 O1G TTP F6195     1555   1555  2.24  
LINK        MG    MG F6194                 O   HOH F6219     1555   1555  3.13  
LINK        MG    MG F6194                 OG  SER F  33     1555   1555  2.59  
LINK        MG    MG F6194                 O1A TTP F6195     1555   1555  2.07  
LINK        MG    MG G7194                 O1G TTP G7195     1555   1555  2.04  
LINK        MG    MG G7194                 O   HOH G7228     1555   1555  2.08  
LINK        MG    MG G7194                 O1A TTP G7195     1555   1555  2.04  
LINK        MG    MG G7194                 O1B TTP G7195     1555   1555  2.26  
LINK        MG    MG G7194                 OG  SER G  33     1555   1555  2.25  
LINK        MG    MG H8194                 O1B TTP H8195     1555   1555  2.32  
LINK        MG    MG H8194                 O1A TTP H8195     1555   1555  2.33  
LINK        MG    MG H8194                 O   HOH H8217     1555   1555  2.40  
LINK        MG    MG H8194                 O1G TTP H8195     1555   1555  2.12  
LINK        MG    MG H8194                 OG  SER H  33     1555   1555  2.47  
SITE     1 AC1  4 CYS A 153  CYS A 156  CYS A 185  CYS A 188                    
SITE     1 AC2  4 CYS B 153  CYS B 156  CYS B 185  CYS B 188                    
SITE     1 AC3  4 CYS C 153  CYS C 156  CYS C 185  CYS C 188                    
SITE     1 AC4  4 CYS D 153  CYS D 156  CYS D 185  CYS D 188                    
SITE     1 AC5  4 CYS E 153  CYS E 156  CYS E 185  CYS E 188                    
SITE     1 AC6  4 CYS F 153  CYS F 156  CYS F 185  CYS F 188                    
SITE     1 AC7  4 CYS G 153  CYS G 156  CYS G 185  CYS G 188                    
SITE     1 AC8  4 CYS H 153  CYS H 156  CYS H 185  CYS H 188                    
SITE     1 AC9  3 SER A  33  ARG A  60  TTP A1195                               
SITE     1 BC1  2 SER B  33  TTP B2195                                          
SITE     1 BC2  3 SER C  33  TTP C3195  HOH C3215                               
SITE     1 BC3  3 SER D  33  TTP D4195  HOH D4229                               
SITE     1 BC4  2 SER E  33  TTP E5195                                          
SITE     1 BC5  2 SER F  33  TTP F6195                                          
SITE     1 BC6  3 SER G  33  TTP G7195  HOH G7228                               
SITE     1 BC7  3 SER H  33  TTP H8195  HOH H8217                               
SITE     1 BC8 25 MET A  28  PHE A  29  SER A  30  GLY A  31                    
SITE     2 BC8 25 LYS A  32  SER A  33  ASP A  58  ARG A  60                    
SITE     3 BC8 25 GLU A  98  PHE A 101  LEU A 124  THR A 127                    
SITE     4 BC8 25 PHE A 128  PHE A 133  ARG A 165  VAL A 172                    
SITE     5 BC8 25 GLU A 173  VAL A 174  ILE A 175  GLY A 176                    
SITE     6 BC8 25 TYR A 181   MG A1194  HOH A1202  HOH A1214                    
SITE     7 BC8 25 HOH A1218                                                     
SITE     1 BC9 23 MET B  28  PHE B  29  SER B  30  GLY B  31                    
SITE     2 BC9 23 LYS B  32  SER B  33  ASP B  58  ARG B  60                    
SITE     3 BC9 23 GLU B  98  PHE B 101  LEU B 124  THR B 127                    
SITE     4 BC9 23 PHE B 128  PHE B 133  THR B 163  VAL B 172                    
SITE     5 BC9 23 GLU B 173  VAL B 174  ILE B 175  GLY B 176                    
SITE     6 BC9 23 TYR B 181   MG B2194  HOH B2226                               
SITE     1 CC1 26 MET C  28  PHE C  29  SER C  30  GLY C  31                    
SITE     2 CC1 26 LYS C  32  SER C  33  ASP C  58  ARG C  60                    
SITE     3 CC1 26 GLU C  98  PHE C 101  LEU C 124  THR C 127                    
SITE     4 CC1 26 PHE C 128  PHE C 133  THR C 163  ARG C 165                    
SITE     5 CC1 26 VAL C 172  GLU C 173  VAL C 174  ILE C 175                    
SITE     6 CC1 26 GLY C 176  TYR C 181   MG C3194  HOH C3200                    
SITE     7 CC1 26 HOH C3207  HOH C3215                                          
SITE     1 CC2 25 MET D  28  PHE D  29  SER D  30  GLY D  31                    
SITE     2 CC2 25 LYS D  32  SER D  33  ASP D  58  ARG D  60                    
SITE     3 CC2 25 GLU D  98  PHE D 101  LEU D 124  THR D 127                    
SITE     4 CC2 25 PHE D 128  PHE D 133  ARG D 165  VAL D 172                    
SITE     5 CC2 25 GLU D 173  VAL D 174  GLY D 176  TYR D 181                    
SITE     6 CC2 25  MG D4194  HOH D4212  HOH D4225  HOH D4229                    
SITE     7 CC2 25 HOH D4230                                                     
SITE     1 CC3 24 MET E  28  PHE E  29  SER E  30  GLY E  31                    
SITE     2 CC3 24 LYS E  32  SER E  33  ASP E  58  ARG E  60                    
SITE     3 CC3 24 GLU E  98  PHE E 101  LEU E 124  THR E 127                    
SITE     4 CC3 24 PHE E 128  PHE E 133  ARG E 165  VAL E 172                    
SITE     5 CC3 24 GLU E 173  VAL E 174  ILE E 175  GLY E 176                    
SITE     6 CC3 24 TYR E 181   MG E5194  HOH E5214  HOH E5215                    
SITE     1 CC4 25 MET F  28  PHE F  29  SER F  30  GLY F  31                    
SITE     2 CC4 25 LYS F  32  SER F  33  ASP F  58  ARG F  60                    
SITE     3 CC4 25 PHE F 101  LEU F 124  THR F 127  PHE F 128                    
SITE     4 CC4 25 PHE F 133  THR F 163  ARG F 165  VAL F 172                    
SITE     5 CC4 25 GLU F 173  VAL F 174  ILE F 175  GLY F 176                    
SITE     6 CC4 25 TYR F 181   MG F6194  HOH F6210  HOH F6219                    
SITE     7 CC4 25 HOH F6220                                                     
SITE     1 CC5 25 MET G  28  PHE G  29  SER G  30  GLY G  31                    
SITE     2 CC5 25 LYS G  32  SER G  33  ASP G  58  ARG G  60                    
SITE     3 CC5 25 GLU G  98  PHE G 101  LEU G 124  THR G 127                    
SITE     4 CC5 25 PHE G 128  PHE G 133  ARG G 165  VAL G 172                    
SITE     5 CC5 25 GLU G 173  VAL G 174  GLY G 176  TYR G 181                    
SITE     6 CC5 25  MG G7194  HOH G7202  HOH G7214  HOH G7216                    
SITE     7 CC5 25 HOH G7228                                                     
SITE     1 CC6 25 MET H  28  PHE H  29  SER H  30  GLY H  31                    
SITE     2 CC6 25 LYS H  32  SER H  33  ASP H  58  ARG H  60                    
SITE     3 CC6 25 GLU H  98  PHE H 101  LEU H 124  THR H 127                    
SITE     4 CC6 25 PHE H 128  PHE H 133  ARG H 165  VAL H 172                    
SITE     5 CC6 25 GLU H 173  VAL H 174  ILE H 175  GLY H 176                    
SITE     6 CC6 25 TYR H 181   MG H8194  HOH H8204  HOH H8205                    
SITE     7 CC6 25 HOH H8208                                                     
CRYST1  157.672  123.177  116.000  90.00 130.20  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      0.006342  0.000000  0.005360        0.00000                         
SCALE2      0.000000  0.008118  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011287        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system