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Database: PDB
Entry: 3KZ8
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Original site: 3KZ8 
HEADER    TRANSCRIPTION/DNA                       08-DEC-09   3KZ8              
TITLE     DIVERSITY IN DNA RECOGNITION BY P53 REVEALED BY CRYSTAL STRUCTURES    
TITLE    2 WITH HOOGSTEEN BASE PAIRS (P53-DNA COMPLEX 3)                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELLULAR TUMOR ANTIGEN P53;                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: P53 CORE DOMAIN, UNP RESIDUES 94-293;                      
COMPND   5 SYNONYM: TUMOR SUPPRESSOR P53, PHOSPHOPROTEIN P53, ANTIGEN NY-CO-13; 
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: DNA (5'-                                                   
COMPND   9 D(*TP*GP*GP*GP*CP*AP*TP*GP*CP*CP*CP*GP*GP*GP*CP*AP*TP*GP*CP*CP*C)-   
COMPND  10 3');                                                                 
COMPND  11 CHAIN: C;                                                            
COMPND  12 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: TP53;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET27-B;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 OTHER_DETAILS: SYNTHETIC DNA FRAGMENT.                               
KEYWDS    P53, MUTANT PROTEIN, LOOP-SHEET-HELIX MOTIF, DNA TARGET, ACTIVATOR,   
KEYWDS   2 ANTI-ONCOGENE APOPTOSIS, CELL CYCLE, COVALENT PROTEIN-RNA LINKAGE,   
KEYWDS   3 DISEASE MUTATION, DNA-BINDING, ENDOPLASMIC RETICULUM, GLYCOPROTEIN,  
KEYWDS   4 HOST-VIRUS INTERACTION, LI-FRAUMENI SYNDROME, METHYLATION, NUCLEUS,  
KEYWDS   5 PHOSPHOPROTEIN, TRANSCRIPTION, TRANSCRIPTION REGULATION,             
KEYWDS   6 TRANSCRIPTION/DNA COMPLE, APOPTOSIS, ISOPEPTIDE BOND, TUMOR          
KEYWDS   7 SUPPRESSOR, TRANSCRIPTION-DNA COMPLEX                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.ROZENBERG,O.SUAD,Z.SHAKKED                                          
REVDAT   3   08-JUN-11 3KZ8    1       JRNL                                     
REVDAT   2   14-APR-10 3KZ8    1       TITLE                                    
REVDAT   1   31-MAR-10 3KZ8    0                                                
JRNL        AUTH   M.KITAYNER,H.ROZENBERG,R.ROHS,O.SUAD,D.RABINOVICH,B.HONIG,   
JRNL        AUTH 2 Z.SHAKKED                                                    
JRNL        TITL   DIVERSITY IN DNA RECOGNITION BY P53 REVEALED BY CRYSTAL      
JRNL        TITL 2 STRUCTURES WITH HOOGSTEEN BASE PAIRS                         
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  17   423 2010              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   20364130                                                     
JRNL        DOI    10.1038/NSMB.1800                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.91 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.4.0078                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.91                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.54                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 34235                          
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) : 0.223                           
REMARK   3   R VALUE            (WORKING SET) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1828                            
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) : 1.91                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.96                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2495                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.47                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2910                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 132                          
REMARK   3   BIN FREE R VALUE                    : 0.3200                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2972                                    
REMARK   3   NUCLEIC ACID ATOMS       : 410                                     
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 311                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.81                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.71000                                             
REMARK   3    B22 (A**2) : 0.50000                                              
REMARK   3    B33 (A**2) : 0.16000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.45000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.191         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.172         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.114         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.908         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.957                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3599 ; 0.031 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4990 ; 2.819 ; 2.102       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   414 ; 7.467 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   130 ;32.386 ;22.154       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   506 ;14.782 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    30 ;13.662 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   554 ; 0.192 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2646 ; 0.016 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2016 ; 2.447 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3286 ; 3.890 ; 3.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1583 ; 4.925 ; 4.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1698 ; 6.507 ; 5.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3KZ8 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-DEC-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB056632.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-NOV-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.1                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97620                            
REMARK 200  MONOCHROMATOR                  : SILICON (1 1 1) CHANNEL-CUT        
REMARK 200  OPTICS                         : SILICON TOROIDAL MIRROR COATED     
REMARK 200                                   WITH RHODIUM                       
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37958                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.880                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 34.540                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 25.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.88                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.91                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.48600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.670                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: CHAIN A OF 2AC0                                      
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.20M AMMONIUM IODIDE, 20% PEG 3350,     
REMARK 280  PH 6.1, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K             
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       69.21100            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.90600            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       69.21100            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       24.90600            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE HEXAMER IS FORMED BY CHAINS (A, B, C, A', B', C')        
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: HEXAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       -4.13101            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       67.93051            
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     SER A    94                                                      
REMARK 465     SER A   185                                                      
REMARK 465     ASP A   186                                                      
REMARK 465     GLY A   187                                                      
REMARK 465     GLY A   293                                                      
REMARK 465     SER B    94                                                      
REMARK 465     SER B   185                                                      
REMARK 465     ASP B   186                                                      
REMARK 465     GLY B   187                                                      
REMARK 465     GLY B   293                                                      
REMARK 465      DT C     0                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 101    CE   NZ                                             
REMARK 470     GLN A 104    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 110    CD   NE   CZ   NH1  NH2                             
REMARK 470     ASP A 148    CG   OD1  OD2                                       
REMARK 470     LEU A 188    CG   CD1  CD2                                       
REMARK 470     LEU A 201    CG   CD1  CD2                                       
REMARK 470     ARG A 202    NE   CZ   NH1  NH2                                  
REMARK 470     GLU A 204    CD   OE1  OE2                                       
REMARK 470     GLU A 221    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 224    CG   CD   OE1  OE2                                  
REMARK 470     VAL A 225    CG1  CG2                                            
REMARK 470     ASP A 228    CG   OD1  OD2                                       
REMARK 470     GLU A 287    CD   OE1  OE2                                       
REMARK 470     ARG A 290    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 291    CD   CE   NZ                                        
REMARK 470     LYS A 292    CD   CE   NZ                                        
REMARK 470     LYS B 101    CE   NZ                                             
REMARK 470     GLN B 104    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 110    CD   NE   CZ   NH1  NH2                             
REMARK 470     ASP B 148    CG   OD1  OD2                                       
REMARK 470     LEU B 188    CG   CD1  CD2                                       
REMARK 470     LEU B 201    CG   CD1  CD2                                       
REMARK 470     ARG B 202    NE   CZ   NH1  NH2                                  
REMARK 470     GLU B 204    CD   OE1  OE2                                       
REMARK 470     GLU B 221    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 224    CG   CD   OE1  OE2                                  
REMARK 470     VAL B 225    CG1  CG2                                            
REMARK 470     ASP B 228    CG   OD1  OD2                                       
REMARK 470     GLU B 287    CD   OE1  OE2                                       
REMARK 470     ARG B 290    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS B 291    CD   CE   NZ                                        
REMARK 470     LYS B 292    CD   CE   NZ                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NH1  ARG A   209     O    ARG A   290     1545     1.83            
REMARK 500   P     DG C     1     O3'   DC C    20     1554     2.01            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TYR A 107   CB    TYR A 107   CG      0.102                       
REMARK 500    MET A 133   C     MET A 133   O       0.138                       
REMARK 500    TYR B 107   CB    TYR B 107   CG      0.102                       
REMARK 500    TYR B 107   CD1   TYR B 107   CE1     0.095                       
REMARK 500    PHE B 134   CZ    PHE B 134   CE2     0.125                       
REMARK 500    ALA B 161   CA    ALA B 161   CB      0.184                       
REMARK 500    GLU B 180   CG    GLU B 180   CD      0.121                       
REMARK 500    ARG B 181   CZ    ARG B 181   NH2    -0.129                       
REMARK 500    TYR B 234   CD1   TYR B 234   CE1     0.090                       
REMARK 500     DG C   1   P      DG C   1   O5'     0.073                       
REMARK 500     DG C   1   N3     DG C   1   C4     -0.060                       
REMARK 500     DG C   3   N7     DG C   3   C8      0.037                       
REMARK 500     DC C   4   C5'    DC C   4   C4'     0.047                       
REMARK 500     DC C   4   C1'    DC C   4   N1      0.091                       
REMARK 500     DA C   5   C2'    DA C   5   C1'     0.068                       
REMARK 500     DT C   6   C3'    DT C   6   C2'     0.073                       
REMARK 500     DT C   6   O3'    DT C   6   C3'    -0.039                       
REMARK 500     DT C   6   C5     DT C   6   C6      0.061                       
REMARK 500     DG C   7   C6     DG C   7   N1      0.053                       
REMARK 500     DG C   7   N7     DG C   7   C8      0.041                       
REMARK 500     DC C   8   O3'    DC C   8   C3'    -0.048                       
REMARK 500     DC C  10   N3     DC C  10   C4     -0.057                       
REMARK 500     DG C  11   N3     DG C  11   C4     -0.058                       
REMARK 500     DG C  13   N7     DG C  13   C8      0.042                       
REMARK 500     DC C  14   O3'    DC C  14   C3'    -0.043                       
REMARK 500     DC C  14   C1'    DC C  14   N1      0.083                       
REMARK 500     DA C  15   C2'    DA C  15   C1'     0.072                       
REMARK 500     DA C  15   N1     DA C  15   C2      0.062                       
REMARK 500     DA C  15   C5     DA C  15   N7      0.056                       
REMARK 500     DT C  16   C5     DT C  16   C6      0.058                       
REMARK 500     DT C  16   C2     DT C  16   O2      0.054                       
REMARK 500     DG C  17   C6     DG C  17   N1      0.072                       
REMARK 500     DG C  17   C5     DG C  17   N7      0.045                       
REMARK 500     DG C  17   N7     DG C  17   C8      0.039                       
REMARK 500     DC C  18   O3'    DC C  18   C3'    -0.055                       
REMARK 500     DC C  18   N1     DC C  18   C6     -0.038                       
REMARK 500     DC C  20   N3     DC C  20   C4     -0.043                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS A 124   CA  -  CB  -  SG  ANGL. DEV. =   7.1 DEGREES          
REMARK 500    LEU A 137   CB  -  CG  -  CD1 ANGL. DEV. = -10.5 DEGREES          
REMARK 500    LEU A 137   CB  -  CG  -  CD2 ANGL. DEV. = -11.9 DEGREES          
REMARK 500    ARG A 174   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ARG A 175   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ARG A 196   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    LEU A 206   CB  -  CG  -  CD1 ANGL. DEV. =  10.8 DEGREES          
REMARK 500    ASP A 207   CB  -  CG  -  OD2 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    ARG A 209   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ARG A 213   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG A 267   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A 267   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    LEU B 137   CB  -  CG  -  CD1 ANGL. DEV. = -10.5 DEGREES          
REMARK 500    LEU B 137   CB  -  CG  -  CD2 ANGL. DEV. = -11.9 DEGREES          
REMARK 500    ARG B 174   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG B 175   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG B 175   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ARG B 181   NE  -  CZ  -  NH1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG B 181   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.5 DEGREES          
REMARK 500    ARG B 196   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    LEU B 206   CB  -  CG  -  CD1 ANGL. DEV. =  10.3 DEGREES          
REMARK 500    ASP B 207   CB  -  CG  -  OD2 ANGL. DEV. =  -7.2 DEGREES          
REMARK 500    ARG B 209   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ARG B 213   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG B 267   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG B 267   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500     DG C   1   C4  -  C5  -  N7  ANGL. DEV. =  -3.4 DEGREES          
REMARK 500     DG C   1   N9  -  C4  -  C5  ANGL. DEV. =   3.7 DEGREES          
REMARK 500     DG C   1   N3  -  C4  -  N9  ANGL. DEV. =  -5.1 DEGREES          
REMARK 500     DG C   1   C6  -  C5  -  N7  ANGL. DEV. =   4.3 DEGREES          
REMARK 500     DG C   1   N1  -  C6  -  O6  ANGL. DEV. =  -6.4 DEGREES          
REMARK 500     DG C   1   C5  -  C6  -  O6  ANGL. DEV. =   5.0 DEGREES          
REMARK 500     DG C   2   O4' -  C1' -  N9  ANGL. DEV. =   2.5 DEGREES          
REMARK 500     DG C   2   C4  -  C5  -  N7  ANGL. DEV. =  -3.4 DEGREES          
REMARK 500     DG C   2   C5  -  N7  -  C8  ANGL. DEV. =   4.0 DEGREES          
REMARK 500     DG C   2   N7  -  C8  -  N9  ANGL. DEV. =  -4.7 DEGREES          
REMARK 500     DG C   1   C3' -  O3' -  P   ANGL. DEV. =   9.0 DEGREES          
REMARK 500     DG C   3   O4' -  C1' -  C2' ANGL. DEV. =  -5.9 DEGREES          
REMARK 500     DG C   3   O4' -  C1' -  N9  ANGL. DEV. =   7.4 DEGREES          
REMARK 500     DG C   3   C6  -  N1  -  C2  ANGL. DEV. =  -4.5 DEGREES          
REMARK 500     DG C   3   C5  -  C6  -  N1  ANGL. DEV. =   3.3 DEGREES          
REMARK 500     DG C   3   C4  -  C5  -  N7  ANGL. DEV. =  -4.2 DEGREES          
REMARK 500     DG C   3   C5  -  N7  -  C8  ANGL. DEV. =   5.3 DEGREES          
REMARK 500     DG C   3   N7  -  C8  -  N9  ANGL. DEV. =  -6.2 DEGREES          
REMARK 500     DG C   3   N9  -  C4  -  C5  ANGL. DEV. =   2.9 DEGREES          
REMARK 500     DC C   4   O4' -  C1' -  C2' ANGL. DEV. =  -6.0 DEGREES          
REMARK 500     DC C   4   C2  -  N3  -  C4  ANGL. DEV. =  -5.0 DEGREES          
REMARK 500     DC C   4   N3  -  C4  -  C5  ANGL. DEV. =   5.8 DEGREES          
REMARK 500     DC C   4   C4  -  C5  -  C6  ANGL. DEV. =  -4.0 DEGREES          
REMARK 500     DA C   5   C5' -  C4' -  O4' ANGL. DEV. =   9.3 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     122 ANGLE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 116        3.17   -151.38                                   
REMARK 500    SER A 183     -134.99    -48.35                                   
REMARK 500    GLU A 224      137.07    -28.48                                   
REMARK 500    VAL A 225       91.06    -46.30                                   
REMARK 500    SER B 116        1.83   -154.18                                   
REMARK 500    SER B 183     -131.47    -47.74                                   
REMARK 500    GLU B 224      136.07    -26.45                                   
REMARK 500    VAL B 225       92.35    -46.74                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ALA A  119     LYS A  120                 -149.50                    
REMARK 500 ALA B  119     LYS B  120                 -148.54                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    MET B 160         10.82                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASP B 228        24.8      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A   1  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 179   ND1                                                    
REMARK 620 2 CYS A 176   SG  106.5                                              
REMARK 620 3 CYS A 242   SG  102.1 115.7                                        
REMARK 620 4 CYS A 238   SG  112.0 107.5 112.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B   1  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 179   ND1                                                    
REMARK 620 2 CYS B 176   SG  106.5                                              
REMARK 620 3 CYS B 242   SG  102.1 115.8                                        
REMARK 620 4 CYS B 238   SG  112.0 107.8 112.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 2                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3IGK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3IGL   RELATED DB: PDB                                   
DBREF  3KZ8 A   94   293  UNP    P04637   P53_HUMAN       94    293             
DBREF  3KZ8 B   94   293  UNP    P04637   P53_HUMAN       94    293             
DBREF  3KZ8 C    0    20  PDB    3KZ8     3KZ8             0     20             
SEQRES   1 A  200  SER SER SER VAL PRO SER GLN LYS THR TYR GLN GLY SER          
SEQRES   2 A  200  TYR GLY PHE ARG LEU GLY PHE LEU HIS SER GLY THR ALA          
SEQRES   3 A  200  LYS SER VAL THR CYS THR TYR SER PRO ALA LEU ASN LYS          
SEQRES   4 A  200  MET PHE CYS GLN LEU ALA LYS THR CYS PRO VAL GLN LEU          
SEQRES   5 A  200  TRP VAL ASP SER THR PRO PRO PRO GLY THR ARG VAL ARG          
SEQRES   6 A  200  ALA MET ALA ILE TYR LYS GLN SER GLN HIS MET THR GLU          
SEQRES   7 A  200  VAL VAL ARG ARG CYS PRO HIS HIS GLU ARG CYS SER ASP          
SEQRES   8 A  200  SER ASP GLY LEU ALA PRO PRO GLN HIS LEU ILE ARG VAL          
SEQRES   9 A  200  GLU GLY ASN LEU ARG VAL GLU TYR LEU ASP ASP ARG ASN          
SEQRES  10 A  200  THR PHE ARG HIS SER VAL VAL VAL PRO TYR GLU PRO PRO          
SEQRES  11 A  200  GLU VAL GLY SER ASP CYS THR THR ILE HIS TYR ASN TYR          
SEQRES  12 A  200  MET CYS ASN SER SER CYS MET GLY GLY MET ASN ARG ARG          
SEQRES  13 A  200  PRO ILE LEU THR ILE ILE THR LEU GLU ASP SER SER GLY          
SEQRES  14 A  200  ASN LEU LEU GLY ARG ASN SER PHE GLU VAL ARG VAL CYS          
SEQRES  15 A  200  ALA CYS PRO GLY ARG ASP ARG ARG THR GLU GLU GLU ASN          
SEQRES  16 A  200  LEU ARG LYS LYS GLY                                          
SEQRES   1 B  200  SER SER SER VAL PRO SER GLN LYS THR TYR GLN GLY SER          
SEQRES   2 B  200  TYR GLY PHE ARG LEU GLY PHE LEU HIS SER GLY THR ALA          
SEQRES   3 B  200  LYS SER VAL THR CYS THR TYR SER PRO ALA LEU ASN LYS          
SEQRES   4 B  200  MET PHE CYS GLN LEU ALA LYS THR CYS PRO VAL GLN LEU          
SEQRES   5 B  200  TRP VAL ASP SER THR PRO PRO PRO GLY THR ARG VAL ARG          
SEQRES   6 B  200  ALA MET ALA ILE TYR LYS GLN SER GLN HIS MET THR GLU          
SEQRES   7 B  200  VAL VAL ARG ARG CYS PRO HIS HIS GLU ARG CYS SER ASP          
SEQRES   8 B  200  SER ASP GLY LEU ALA PRO PRO GLN HIS LEU ILE ARG VAL          
SEQRES   9 B  200  GLU GLY ASN LEU ARG VAL GLU TYR LEU ASP ASP ARG ASN          
SEQRES  10 B  200  THR PHE ARG HIS SER VAL VAL VAL PRO TYR GLU PRO PRO          
SEQRES  11 B  200  GLU VAL GLY SER ASP CYS THR THR ILE HIS TYR ASN TYR          
SEQRES  12 B  200  MET CYS ASN SER SER CYS MET GLY GLY MET ASN ARG ARG          
SEQRES  13 B  200  PRO ILE LEU THR ILE ILE THR LEU GLU ASP SER SER GLY          
SEQRES  14 B  200  ASN LEU LEU GLY ARG ASN SER PHE GLU VAL ARG VAL CYS          
SEQRES  15 B  200  ALA CYS PRO GLY ARG ASP ARG ARG THR GLU GLU GLU ASN          
SEQRES  16 B  200  LEU ARG LYS LYS GLY                                          
SEQRES   1 C   21   DT  DG  DG  DG  DC  DA  DT  DG  DC  DC  DC  DG  DG          
SEQRES   2 C   21   DG  DC  DA  DT  DG  DC  DC  DC                              
HET     ZN  A   1       1                                                       
HET    IOD  A   2       1                                                       
HET     ZN  B   1       1                                                       
HET    IOD  B   2       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     IOD IODIDE ION                                                       
FORMUL   4   ZN    2(ZN 2+)                                                     
FORMUL   5  IOD    2(I 1-)                                                      
FORMUL   8  HOH   *311(H2 O)                                                    
HELIX    1   1 GLN A  104  GLY A  108  5                                   5    
HELIX    2   2 GLN A  165  MET A  169  5                                   5    
HELIX    3   3 CYS A  176  CYS A  182  1                                   7    
HELIX    4   4 CYS A  277  LYS A  292  1                                  16    
HELIX    5   5 GLN B  165  MET B  169  5                                   5    
HELIX    6   6 CYS B  176  CYS B  182  1                                   7    
HELIX    7   7 CYS B  277  LYS B  292  1                                  16    
SHEET    1   A 4 ARG A 110  GLY A 112  0                                        
SHEET    2   A 4 THR A 140  TRP A 146 -1  O  GLN A 144   N  GLY A 112           
SHEET    3   A 4 THR A 230  TYR A 236 -1  O  THR A 230   N  LEU A 145           
SHEET    4   A 4 ILE A 195  VAL A 197 -1  N  ARG A 196   O  ASN A 235           
SHEET    1   B 7 CYS A 124  SER A 127  0                                        
SHEET    2   B 7 LYS A 132  CYS A 135 -1  O  LYS A 132   N  SER A 127           
SHEET    3   B 7 LEU A 264  VAL A 274  1  O  ARG A 273   N  MET A 133           
SHEET    4   B 7 ILE A 251  GLU A 258 -1  N  THR A 253   O  PHE A 270           
SHEET    5   B 7 ARG A 156  TYR A 163 -1  N  ARG A 156   O  GLU A 258           
SHEET    6   B 7 HIS A 214  PRO A 219 -1  O  VAL A 218   N  VAL A 157           
SHEET    7   B 7 GLU A 204  ASP A 207 -1  N  GLU A 204   O  VAL A 217           
SHEET    1   C 4 ARG B 110  GLY B 112  0                                        
SHEET    2   C 4 THR B 140  TRP B 146 -1  O  GLN B 144   N  GLY B 112           
SHEET    3   C 4 THR B 230  TYR B 236 -1  O  THR B 230   N  LEU B 145           
SHEET    4   C 4 ILE B 195  VAL B 197 -1  N  ARG B 196   O  ASN B 235           
SHEET    1   D 7 CYS B 124  SER B 127  0                                        
SHEET    2   D 7 LYS B 132  CYS B 135 -1  O  LYS B 132   N  SER B 127           
SHEET    3   D 7 LEU B 264  VAL B 274  1  O  GLU B 271   N  MET B 133           
SHEET    4   D 7 ILE B 251  GLU B 258 -1  N  ILE B 255   O  ASN B 268           
SHEET    5   D 7 ARG B 156  TYR B 163 -1  N  MET B 160   O  ILE B 254           
SHEET    6   D 7 HIS B 214  PRO B 219 -1  O  VAL B 218   N  VAL B 157           
SHEET    7   D 7 GLU B 204  ASP B 207 -1  N  GLU B 204   O  VAL B 217           
LINK         ND1 HIS A 179                ZN    ZN A   1     1555   1555  1.96  
LINK         ND1 HIS B 179                ZN    ZN B   1     1555   1555  1.97  
LINK         SG  CYS B 176                ZN    ZN B   1     1555   1555  2.30  
LINK         SG  CYS A 176                ZN    ZN A   1     1555   1555  2.30  
LINK         SG  CYS A 242                ZN    ZN A   1     1555   1555  2.34  
LINK         SG  CYS A 238                ZN    ZN A   1     1555   1555  2.34  
LINK         SG  CYS B 242                ZN    ZN B   1     1555   1555  2.35  
LINK         SG  CYS B 238                ZN    ZN B   1     1555   1555  2.35  
SITE     1 AC1  4 CYS A 176  HIS A 179  CYS A 238  CYS A 242                    
SITE     1 AC2  3 HOH A  52  MET A 160  HOH A 309                               
SITE     1 AC3  4 CYS B 176  HIS B 179  CYS B 238  CYS B 242                    
SITE     1 AC4  3 HOH B  51  MET B 160  HOH B 308                               
CRYST1  138.422   49.812   68.056  90.00  93.48  90.00 C 1 2 1       8          
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      0.007224  0.000000  0.000439        0.00000                         
SCALE2      0.000000  0.020075  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014721        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system