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Database: PDB
Entry: 3VD1
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Original site: 3VD1 
HEADER    ANTITUMOR PROTEIN/DNA                   04-JAN-12   3VD1              
TITLE     STRUCTURE OF P73 DNA BINDING DOMAIN TETRAMER MODULATES P73            
TITLE    2 TRANSACTIVATION                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUMOR PROTEIN P73;                                         
COMPND   3 CHAIN: A, B, C, D, I, J, K, L;                                       
COMPND   4 FRAGMENT: UNP RESIDUE 115-312;                                       
COMPND   5 SYNONYM: P53-LIKE TRANSCRIPTION FACTOR, P53-RELATED PROTEIN;         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: DNA (5'-D(*CP*GP*GP*GP*CP*AP*TP*GP*CP*CP*CP*G)-3');        
COMPND   9 CHAIN: E, F, G, H, M, N, O, P;                                       
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES                                                       
KEYWDS    PROTEIN DNA COMPLEX, BETA-IMMUNOGLOBULIN-LIKE FOLD, TUMOUR            
KEYWDS   2 SUPPRESSOR, ANTITUMOR PROTEIN-DNA COMPLEX                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.S.ETHAYATHULLA,P.W.TSE,S.NGUYEN,H.VIADIU                            
REVDAT   6   13-SEP-23 3VD1    1       REMARK SEQADV LINK                       
REVDAT   5   08-OCT-14 3VD1    1       AUTHOR                                   
REVDAT   4   22-AUG-12 3VD1    1       REMARK                                   
REVDAT   3   25-JUL-12 3VD1    1       JRNL                                     
REVDAT   2   16-MAY-12 3VD1    1                                                
REVDAT   1   18-APR-12 3VD1    0                                                
JRNL        AUTH   A.S.ETHAYATHULLA,P.W.TSE,P.MONTI,S.NGUYEN,A.INGA,G.FRONZA,   
JRNL        AUTH 2 H.VIADIU                                                     
JRNL        TITL   STRUCTURE OF P73 DNA-BINDING DOMAIN TETRAMER MODULATES P73   
JRNL        TITL 2 TRANSACTIVATION.                                             
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 109  6066 2012              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   22474346                                                     
JRNL        DOI    10.1073/PNAS.1115463109                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.3                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.99                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1510416.310                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 41779                          
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 SET) : 0.239                           
REMARK   3   FREE R VALUE                     : 0.285                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 843                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.010                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.95                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.13                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.20                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 6596                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3620                       
REMARK   3   BIN FREE R VALUE                    : 0.4310                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 1.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 125                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.039                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12576                                   
REMARK   3   NUCLEIC ACID ATOMS       : 1944                                    
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 188                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 35.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 74.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.31000                                              
REMARK   3    B22 (A**2) : 12.41000                                             
REMARK   3    B33 (A**2) : -17.72000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -8.29000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.43                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.58                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.52                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.71                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.700                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.380                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.28                                                 
REMARK   3   BSOL        : 36.51                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : DNA-RNA_REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : CARBOHYDRATE.TOP                               
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 3VD1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JAN-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000069891.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 200.0                              
REMARK 200  PH                             : 6.1                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : RH COATED FLAT MIRROR              
REMARK 200  OPTICS                         : MIRROR                             
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          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41946                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY                : 6.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.40000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3KMD                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES, 0.1M NA ACETATE, PH 6.1,       
REMARK 280  TEMPERATURE 298.0K                                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       52.10000            
REMARK 290   SMTRY3   2  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 300 REMARK: THE OCTAMER IN THE ASU CORRESPONDS TO A TETRAMER P73DBD      
REMARK 300 PLUS FOUR CHAINS OF TWO CONTINUOUS DNA DOUBLE STRANDS.               
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: OCTAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J, K, L, M, N, O, P                
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   103                                                      
REMARK 465     GLY A   104                                                      
REMARK 465     HIS A   105                                                      
REMARK 465     HIS A   106                                                      
REMARK 465     HIS A   107                                                      
REMARK 465     HIS A   108                                                      
REMARK 465     HIS A   109                                                      
REMARK 465     HIS A   110                                                      
REMARK 465     MET B   103                                                      
REMARK 465     GLY B   104                                                      
REMARK 465     HIS B   105                                                      
REMARK 465     HIS B   106                                                      
REMARK 465     HIS B   107                                                      
REMARK 465     HIS B   108                                                      
REMARK 465     HIS B   109                                                      
REMARK 465     HIS B   110                                                      
REMARK 465     HIS B   111                                                      
REMARK 465     HIS B   112                                                      
REMARK 465     GLU B   113                                                      
REMARK 465     MET C   103                                                      
REMARK 465     GLY C   104                                                      
REMARK 465     HIS C   105                                                      
REMARK 465     HIS C   106                                                      
REMARK 465     HIS C   107                                                      
REMARK 465     HIS C   108                                                      
REMARK 465     HIS C   109                                                      
REMARK 465     HIS C   110                                                      
REMARK 465     HIS C   111                                                      
REMARK 465     MET D   103                                                      
REMARK 465     GLY D   104                                                      
REMARK 465     HIS D   105                                                      
REMARK 465     HIS D   106                                                      
REMARK 465     HIS D   107                                                      
REMARK 465     HIS D   108                                                      
REMARK 465     HIS D   109                                                      
REMARK 465     HIS D   110                                                      
REMARK 465     HIS D   111                                                      
REMARK 465     HIS D   112                                                      
REMARK 465     GLU D   113                                                      
REMARK 465     MET I   103                                                      
REMARK 465     GLY I   104                                                      
REMARK 465     HIS I   105                                                      
REMARK 465     HIS I   106                                                      
REMARK 465     HIS I   107                                                      
REMARK 465     HIS I   108                                                      
REMARK 465     HIS I   109                                                      
REMARK 465     HIS I   110                                                      
REMARK 465     HIS I   111                                                      
REMARK 465     HIS I   112                                                      
REMARK 465     GLU I   113                                                      
REMARK 465     MET J   103                                                      
REMARK 465     GLY J   104                                                      
REMARK 465     HIS J   105                                                      
REMARK 465     HIS J   106                                                      
REMARK 465     HIS J   107                                                      
REMARK 465     HIS J   108                                                      
REMARK 465     HIS J   109                                                      
REMARK 465     HIS J   110                                                      
REMARK 465     HIS J   111                                                      
REMARK 465     HIS J   112                                                      
REMARK 465     GLU J   113                                                      
REMARK 465     MET K   103                                                      
REMARK 465     GLY K   104                                                      
REMARK 465     HIS K   105                                                      
REMARK 465     HIS K   106                                                      
REMARK 465     HIS K   107                                                      
REMARK 465     HIS K   108                                                      
REMARK 465     HIS K   109                                                      
REMARK 465     HIS K   110                                                      
REMARK 465     MET L   103                                                      
REMARK 465     GLY L   104                                                      
REMARK 465     HIS L   105                                                      
REMARK 465     HIS L   106                                                      
REMARK 465     HIS L   107                                                      
REMARK 465     HIS L   108                                                      
REMARK 465     HIS L   109                                                      
REMARK 465     HIS L   110                                                      
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     HIS A 111    CG   ND1  CD2  CE1  NE2                             
REMARK 470     HIS A 112    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A 113    CG   CD   OE1  OE2                                  
REMARK 470     PHE B 114    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU C 113    CG   CD   OE1  OE2                                  
REMARK 470     PHE C 114    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PHE D 114    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PHE I 114    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PHE J 114    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     HIS K 112    CG   ND1  CD2  CE1  NE2                             
REMARK 470     HIS L 111    CG   ND1  CD2  CE1  NE2                             
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    PRO B 168   C   -  N   -  CD  ANGL. DEV. = -15.6 DEGREES          
REMARK 500    PRO B 169   C   -  N   -  CD  ANGL. DEV. = -20.3 DEGREES          
REMARK 500    PRO B 170   C   -  N   -  CD  ANGL. DEV. = -13.7 DEGREES          
REMARK 500    PRO B 171   C   -  N   -  CD  ANGL. DEV. = -12.9 DEGREES          
REMARK 500     DA F 415   C3' -  O3' -  P   ANGL. DEV. =  12.3 DEGREES          
REMARK 500     DC O 710   C3' -  C2' -  C1' ANGL. DEV. =  -4.9 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    THR A 119      126.33    -33.30                                   
REMARK 500    ALA A 140      148.46    -33.82                                   
REMARK 500    TRP A 142      142.96   -171.11                                   
REMARK 500    LYS A 149       46.22     31.32                                   
REMARK 500    PHE A 203        8.22   -178.98                                   
REMARK 500    SER A 208      -45.77   -137.86                                   
REMARK 500    ALA A 211        5.06    -68.67                                   
REMARK 500    ASN A 220      120.99    -38.53                                   
REMARK 500    ASP A 227       74.41   -150.41                                   
REMARK 500    PRO A 243      137.40    -33.15                                   
REMARK 500    VAL A 245      123.25    -38.38                                   
REMARK 500    SER A 260      -19.16    -37.63                                   
REMARK 500    MET A 266       95.13    -64.35                                   
REMARK 500    ARG A 268       19.95     56.59                                   
REMARK 500    PHE A 290      125.38   -178.84                                   
REMARK 500    ARG A 310       31.41    -78.28                                   
REMARK 500    ILE B 115       71.78     65.97                                   
REMARK 500    ASN B 118       21.63    -76.29                                   
REMARK 500    TYR B 121       97.14   -172.09                                   
REMARK 500    SER B 139       30.24    -93.89                                   
REMARK 500    LYS B 149       54.87    -98.27                                   
REMARK 500    ALA B 156       10.51     55.10                                   
REMARK 500    PRO B 169        5.98   -158.16                                   
REMARK 500    LYS B 192     -165.73   -107.12                                   
REMARK 500    SER B 223      150.38    -43.55                                   
REMARK 500    VAL B 245      114.42    -36.51                                   
REMARK 500    ARG B 268        2.17     81.39                                   
REMARK 500    GLN B 283       95.97   -167.47                                   
REMARK 500    VAL B 284      103.36    -57.24                                   
REMARK 500    ARG B 287      162.51    179.72                                   
REMARK 500    PHE B 290      135.78   -172.29                                   
REMARK 500    GLU B 311      -35.90    -39.35                                   
REMARK 500    PRO C 116      122.37    -39.14                                   
REMARK 500    TYR C 121       91.40   -171.69                                   
REMARK 500    GLN C 132      -77.84    -94.48                                   
REMARK 500    LYS C 149       51.36     37.19                                   
REMARK 500    ALA C 156       18.89     53.59                                   
REMARK 500    PRO C 170      161.44    -49.76                                   
REMARK 500    ASP C 202      107.71    -41.21                                   
REMARK 500    PHE C 203       -3.36     83.47                                   
REMARK 500    ASN C 220       93.48   -161.44                                   
REMARK 500    PRO C 243     -114.21    -31.07                                   
REMARK 500    CYS C 262      107.55    -51.84                                   
REMARK 500    ARG C 268       -3.44     73.00                                   
REMARK 500    ILE C 271     -168.61   -102.27                                   
REMARK 500    LEU C 272      114.14   -160.53                                   
REMARK 500    ARG C 287      145.99   -176.13                                   
REMARK 500    CYS C 297       94.51   -168.06                                   
REMARK 500    ILE D 115     -106.15   -132.94                                   
REMARK 500    SER D 117     -151.31    -56.91                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     149 RAMACHANDRAN OUTLIERS.                        
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 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 194   SG                                                     
REMARK 620 2 HIS A 197   ND1  82.3                                              
REMARK 620 3 CYS A 258   SG  107.3 102.3                                        
REMARK 620 4 CYS A 262   SG   88.5  96.8 156.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 194   SG                                                     
REMARK 620 2 HIS B 197   ND1  84.5                                              
REMARK 620 3 CYS B 258   SG   96.6  98.7                                        
REMARK 620 4 CYS B 262   SG   98.8 123.4 136.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 194   SG                                                     
REMARK 620 2 HIS C 197   ND1 110.8                                              
REMARK 620 3 CYS C 258   SG  117.5 113.5                                        
REMARK 620 4 CYS C 262   SG  122.8  99.0  91.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 194   SG                                                     
REMARK 620 2 HIS D 197   ND1  97.0                                              
REMARK 620 3 CYS D 258   SG  110.7  97.6                                        
REMARK 620 4 CYS D 262   SG  118.3 101.7 123.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN I 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS I 194   SG                                                     
REMARK 620 2 HIS I 197   ND1  96.6                                              
REMARK 620 3 CYS I 258   SG  106.2 120.5                                        
REMARK 620 4 CYS I 262   SG  133.4 104.4  98.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN J 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS J 194   SG                                                     
REMARK 620 2 HIS J 197   ND1 158.5                                              
REMARK 620 3 CYS J 258   SG   86.4  99.1                                        
REMARK 620 4 CYS J 262   SG   82.9 115.1 105.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN K 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS K 194   SG                                                     
REMARK 620 2 HIS K 197   ND1  98.1                                              
REMARK 620 3 CYS K 258   SG  104.4 112.9                                        
REMARK 620 4 CYS K 262   SG  105.0  79.4 145.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN L 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS L 194   SG                                                     
REMARK 620 2 HIS L 197   ND1  94.2                                              
REMARK 620 3 CYS L 258   SG  112.4 102.0                                        
REMARK 620 4 CYS L 262   SG  122.5 102.1 117.2                                  
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 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN J 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN K 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN L 401                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3VD0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3VD2   RELATED DB: PDB                                   
DBREF  3VD1 A  115   312  UNP    O15350   P73_HUMAN      115    312             
DBREF  3VD1 B  115   312  UNP    O15350   P73_HUMAN      115    312             
DBREF  3VD1 C  115   312  UNP    O15350   P73_HUMAN      115    312             
DBREF  3VD1 D  115   312  UNP    O15350   P73_HUMAN      115    312             
DBREF  3VD1 I  115   312  UNP    O15350   P73_HUMAN      115    312             
DBREF  3VD1 J  115   312  UNP    O15350   P73_HUMAN      115    312             
DBREF  3VD1 K  115   312  UNP    O15350   P73_HUMAN      115    312             
DBREF  3VD1 L  115   312  UNP    O15350   P73_HUMAN      115    312             
DBREF  3VD1 E  398   409  PDB    3VD1     3VD1           398    409             
DBREF  3VD1 F  410   421  PDB    3VD1     3VD1           410    421             
DBREF  3VD1 G  500   511  PDB    3VD1     3VD1           500    511             
DBREF  3VD1 H  512   523  PDB    3VD1     3VD1           512    523             
DBREF  3VD1 M  600   611  PDB    3VD1     3VD1           600    611             
DBREF  3VD1 N  612   623  PDB    3VD1     3VD1           612    623             
DBREF  3VD1 O  700   711  PDB    3VD1     3VD1           700    711             
DBREF  3VD1 P  712   723  PDB    3VD1     3VD1           712    723             
SEQADV 3VD1 MET A  103  UNP  O15350              INITIATING METHIONINE          
SEQADV 3VD1 GLY A  104  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS A  105  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS A  106  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS A  107  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS A  108  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS A  109  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS A  110  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS A  111  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS A  112  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 GLU A  113  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 PHE A  114  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 MET B  103  UNP  O15350              INITIATING METHIONINE          
SEQADV 3VD1 GLY B  104  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS B  105  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS B  106  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS B  107  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS B  108  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS B  109  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS B  110  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS B  111  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS B  112  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 GLU B  113  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 PHE B  114  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 MET C  103  UNP  O15350              INITIATING METHIONINE          
SEQADV 3VD1 GLY C  104  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS C  105  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS C  106  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS C  107  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS C  108  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS C  109  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS C  110  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS C  111  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS C  112  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 GLU C  113  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 PHE C  114  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 MET D  103  UNP  O15350              INITIATING METHIONINE          
SEQADV 3VD1 GLY D  104  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS D  105  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS D  106  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS D  107  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS D  108  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS D  109  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS D  110  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS D  111  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS D  112  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 GLU D  113  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 PHE D  114  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 MET I  103  UNP  O15350              INITIATING METHIONINE          
SEQADV 3VD1 GLY I  104  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS I  105  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS I  106  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS I  107  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS I  108  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS I  109  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS I  110  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS I  111  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS I  112  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 GLU I  113  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 PHE I  114  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 MET J  103  UNP  O15350              INITIATING METHIONINE          
SEQADV 3VD1 GLY J  104  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS J  105  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS J  106  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS J  107  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS J  108  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS J  109  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS J  110  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS J  111  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS J  112  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 GLU J  113  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 PHE J  114  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 MET K  103  UNP  O15350              INITIATING METHIONINE          
SEQADV 3VD1 GLY K  104  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS K  105  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS K  106  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS K  107  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS K  108  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS K  109  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS K  110  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS K  111  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS K  112  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 GLU K  113  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 PHE K  114  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 MET L  103  UNP  O15350              INITIATING METHIONINE          
SEQADV 3VD1 GLY L  104  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS L  105  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS L  106  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS L  107  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS L  108  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS L  109  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS L  110  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS L  111  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 HIS L  112  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 GLU L  113  UNP  O15350              EXPRESSION TAG                 
SEQADV 3VD1 PHE L  114  UNP  O15350              EXPRESSION TAG                 
SEQRES   1 A  210  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS GLU PHE ILE          
SEQRES   2 A  210  PRO SER ASN THR ASP TYR PRO GLY PRO HIS HIS PHE GLU          
SEQRES   3 A  210  VAL THR PHE GLN GLN SER SER THR ALA LYS SER ALA THR          
SEQRES   4 A  210  TRP THR TYR SER PRO LEU LEU LYS LYS LEU TYR CYS GLN          
SEQRES   5 A  210  ILE ALA LYS THR CYS PRO ILE GLN ILE LYS VAL SER THR          
SEQRES   6 A  210  PRO PRO PRO PRO GLY THR ALA ILE ARG ALA MET PRO VAL          
SEQRES   7 A  210  TYR LYS LYS ALA GLU HIS VAL THR ASP VAL VAL LYS ARG          
SEQRES   8 A  210  CYS PRO ASN HIS GLU LEU GLY ARG ASP PHE ASN GLU GLY          
SEQRES   9 A  210  GLN SER ALA PRO ALA SER HIS LEU ILE ARG VAL GLU GLY          
SEQRES  10 A  210  ASN ASN LEU SER GLN TYR VAL ASP ASP PRO VAL THR GLY          
SEQRES  11 A  210  ARG GLN SER VAL VAL VAL PRO TYR GLU PRO PRO GLN VAL          
SEQRES  12 A  210  GLY THR GLU PHE THR THR ILE LEU TYR ASN PHE MET CYS          
SEQRES  13 A  210  ASN SER SER CYS VAL GLY GLY MET ASN ARG ARG PRO ILE          
SEQRES  14 A  210  LEU ILE ILE ILE THR LEU GLU MET ARG ASP GLY GLN VAL          
SEQRES  15 A  210  LEU GLY ARG ARG SER PHE GLU GLY ARG ILE CYS ALA CYS          
SEQRES  16 A  210  PRO GLY ARG ASP ARG LYS ALA ASP GLU ASP HIS TYR ARG          
SEQRES  17 A  210  GLU GLN                                                      
SEQRES   1 B  210  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS GLU PHE ILE          
SEQRES   2 B  210  PRO SER ASN THR ASP TYR PRO GLY PRO HIS HIS PHE GLU          
SEQRES   3 B  210  VAL THR PHE GLN GLN SER SER THR ALA LYS SER ALA THR          
SEQRES   4 B  210  TRP THR TYR SER PRO LEU LEU LYS LYS LEU TYR CYS GLN          
SEQRES   5 B  210  ILE ALA LYS THR CYS PRO ILE GLN ILE LYS VAL SER THR          
SEQRES   6 B  210  PRO PRO PRO PRO GLY THR ALA ILE ARG ALA MET PRO VAL          
SEQRES   7 B  210  TYR LYS LYS ALA GLU HIS VAL THR ASP VAL VAL LYS ARG          
SEQRES   8 B  210  CYS PRO ASN HIS GLU LEU GLY ARG ASP PHE ASN GLU GLY          
SEQRES   9 B  210  GLN SER ALA PRO ALA SER HIS LEU ILE ARG VAL GLU GLY          
SEQRES  10 B  210  ASN ASN LEU SER GLN TYR VAL ASP ASP PRO VAL THR GLY          
SEQRES  11 B  210  ARG GLN SER VAL VAL VAL PRO TYR GLU PRO PRO GLN VAL          
SEQRES  12 B  210  GLY THR GLU PHE THR THR ILE LEU TYR ASN PHE MET CYS          
SEQRES  13 B  210  ASN SER SER CYS VAL GLY GLY MET ASN ARG ARG PRO ILE          
SEQRES  14 B  210  LEU ILE ILE ILE THR LEU GLU MET ARG ASP GLY GLN VAL          
SEQRES  15 B  210  LEU GLY ARG ARG SER PHE GLU GLY ARG ILE CYS ALA CYS          
SEQRES  16 B  210  PRO GLY ARG ASP ARG LYS ALA ASP GLU ASP HIS TYR ARG          
SEQRES  17 B  210  GLU GLN                                                      
SEQRES   1 C  210  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS GLU PHE ILE          
SEQRES   2 C  210  PRO SER ASN THR ASP TYR PRO GLY PRO HIS HIS PHE GLU          
SEQRES   3 C  210  VAL THR PHE GLN GLN SER SER THR ALA LYS SER ALA THR          
SEQRES   4 C  210  TRP THR TYR SER PRO LEU LEU LYS LYS LEU TYR CYS GLN          
SEQRES   5 C  210  ILE ALA LYS THR CYS PRO ILE GLN ILE LYS VAL SER THR          
SEQRES   6 C  210  PRO PRO PRO PRO GLY THR ALA ILE ARG ALA MET PRO VAL          
SEQRES   7 C  210  TYR LYS LYS ALA GLU HIS VAL THR ASP VAL VAL LYS ARG          
SEQRES   8 C  210  CYS PRO ASN HIS GLU LEU GLY ARG ASP PHE ASN GLU GLY          
SEQRES   9 C  210  GLN SER ALA PRO ALA SER HIS LEU ILE ARG VAL GLU GLY          
SEQRES  10 C  210  ASN ASN LEU SER GLN TYR VAL ASP ASP PRO VAL THR GLY          
SEQRES  11 C  210  ARG GLN SER VAL VAL VAL PRO TYR GLU PRO PRO GLN VAL          
SEQRES  12 C  210  GLY THR GLU PHE THR THR ILE LEU TYR ASN PHE MET CYS          
SEQRES  13 C  210  ASN SER SER CYS VAL GLY GLY MET ASN ARG ARG PRO ILE          
SEQRES  14 C  210  LEU ILE ILE ILE THR LEU GLU MET ARG ASP GLY GLN VAL          
SEQRES  15 C  210  LEU GLY ARG ARG SER PHE GLU GLY ARG ILE CYS ALA CYS          
SEQRES  16 C  210  PRO GLY ARG ASP ARG LYS ALA ASP GLU ASP HIS TYR ARG          
SEQRES  17 C  210  GLU GLN                                                      
SEQRES   1 D  210  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS GLU PHE ILE          
SEQRES   2 D  210  PRO SER ASN THR ASP TYR PRO GLY PRO HIS HIS PHE GLU          
SEQRES   3 D  210  VAL THR PHE GLN GLN SER SER THR ALA LYS SER ALA THR          
SEQRES   4 D  210  TRP THR TYR SER PRO LEU LEU LYS LYS LEU TYR CYS GLN          
SEQRES   5 D  210  ILE ALA LYS THR CYS PRO ILE GLN ILE LYS VAL SER THR          
SEQRES   6 D  210  PRO PRO PRO PRO GLY THR ALA ILE ARG ALA MET PRO VAL          
SEQRES   7 D  210  TYR LYS LYS ALA GLU HIS VAL THR ASP VAL VAL LYS ARG          
SEQRES   8 D  210  CYS PRO ASN HIS GLU LEU GLY ARG ASP PHE ASN GLU GLY          
SEQRES   9 D  210  GLN SER ALA PRO ALA SER HIS LEU ILE ARG VAL GLU GLY          
SEQRES  10 D  210  ASN ASN LEU SER GLN TYR VAL ASP ASP PRO VAL THR GLY          
SEQRES  11 D  210  ARG GLN SER VAL VAL VAL PRO TYR GLU PRO PRO GLN VAL          
SEQRES  12 D  210  GLY THR GLU PHE THR THR ILE LEU TYR ASN PHE MET CYS          
SEQRES  13 D  210  ASN SER SER CYS VAL GLY GLY MET ASN ARG ARG PRO ILE          
SEQRES  14 D  210  LEU ILE ILE ILE THR LEU GLU MET ARG ASP GLY GLN VAL          
SEQRES  15 D  210  LEU GLY ARG ARG SER PHE GLU GLY ARG ILE CYS ALA CYS          
SEQRES  16 D  210  PRO GLY ARG ASP ARG LYS ALA ASP GLU ASP HIS TYR ARG          
SEQRES  17 D  210  GLU GLN                                                      
SEQRES   1 I  210  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS GLU PHE ILE          
SEQRES   2 I  210  PRO SER ASN THR ASP TYR PRO GLY PRO HIS HIS PHE GLU          
SEQRES   3 I  210  VAL THR PHE GLN GLN SER SER THR ALA LYS SER ALA THR          
SEQRES   4 I  210  TRP THR TYR SER PRO LEU LEU LYS LYS LEU TYR CYS GLN          
SEQRES   5 I  210  ILE ALA LYS THR CYS PRO ILE GLN ILE LYS VAL SER THR          
SEQRES   6 I  210  PRO PRO PRO PRO GLY THR ALA ILE ARG ALA MET PRO VAL          
SEQRES   7 I  210  TYR LYS LYS ALA GLU HIS VAL THR ASP VAL VAL LYS ARG          
SEQRES   8 I  210  CYS PRO ASN HIS GLU LEU GLY ARG ASP PHE ASN GLU GLY          
SEQRES   9 I  210  GLN SER ALA PRO ALA SER HIS LEU ILE ARG VAL GLU GLY          
SEQRES  10 I  210  ASN ASN LEU SER GLN TYR VAL ASP ASP PRO VAL THR GLY          
SEQRES  11 I  210  ARG GLN SER VAL VAL VAL PRO TYR GLU PRO PRO GLN VAL          
SEQRES  12 I  210  GLY THR GLU PHE THR THR ILE LEU TYR ASN PHE MET CYS          
SEQRES  13 I  210  ASN SER SER CYS VAL GLY GLY MET ASN ARG ARG PRO ILE          
SEQRES  14 I  210  LEU ILE ILE ILE THR LEU GLU MET ARG ASP GLY GLN VAL          
SEQRES  15 I  210  LEU GLY ARG ARG SER PHE GLU GLY ARG ILE CYS ALA CYS          
SEQRES  16 I  210  PRO GLY ARG ASP ARG LYS ALA ASP GLU ASP HIS TYR ARG          
SEQRES  17 I  210  GLU GLN                                                      
SEQRES   1 J  210  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS GLU PHE ILE          
SEQRES   2 J  210  PRO SER ASN THR ASP TYR PRO GLY PRO HIS HIS PHE GLU          
SEQRES   3 J  210  VAL THR PHE GLN GLN SER SER THR ALA LYS SER ALA THR          
SEQRES   4 J  210  TRP THR TYR SER PRO LEU LEU LYS LYS LEU TYR CYS GLN          
SEQRES   5 J  210  ILE ALA LYS THR CYS PRO ILE GLN ILE LYS VAL SER THR          
SEQRES   6 J  210  PRO PRO PRO PRO GLY THR ALA ILE ARG ALA MET PRO VAL          
SEQRES   7 J  210  TYR LYS LYS ALA GLU HIS VAL THR ASP VAL VAL LYS ARG          
SEQRES   8 J  210  CYS PRO ASN HIS GLU LEU GLY ARG ASP PHE ASN GLU GLY          
SEQRES   9 J  210  GLN SER ALA PRO ALA SER HIS LEU ILE ARG VAL GLU GLY          
SEQRES  10 J  210  ASN ASN LEU SER GLN TYR VAL ASP ASP PRO VAL THR GLY          
SEQRES  11 J  210  ARG GLN SER VAL VAL VAL PRO TYR GLU PRO PRO GLN VAL          
SEQRES  12 J  210  GLY THR GLU PHE THR THR ILE LEU TYR ASN PHE MET CYS          
SEQRES  13 J  210  ASN SER SER CYS VAL GLY GLY MET ASN ARG ARG PRO ILE          
SEQRES  14 J  210  LEU ILE ILE ILE THR LEU GLU MET ARG ASP GLY GLN VAL          
SEQRES  15 J  210  LEU GLY ARG ARG SER PHE GLU GLY ARG ILE CYS ALA CYS          
SEQRES  16 J  210  PRO GLY ARG ASP ARG LYS ALA ASP GLU ASP HIS TYR ARG          
SEQRES  17 J  210  GLU GLN                                                      
SEQRES   1 K  210  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS GLU PHE ILE          
SEQRES   2 K  210  PRO SER ASN THR ASP TYR PRO GLY PRO HIS HIS PHE GLU          
SEQRES   3 K  210  VAL THR PHE GLN GLN SER SER THR ALA LYS SER ALA THR          
SEQRES   4 K  210  TRP THR TYR SER PRO LEU LEU LYS LYS LEU TYR CYS GLN          
SEQRES   5 K  210  ILE ALA LYS THR CYS PRO ILE GLN ILE LYS VAL SER THR          
SEQRES   6 K  210  PRO PRO PRO PRO GLY THR ALA ILE ARG ALA MET PRO VAL          
SEQRES   7 K  210  TYR LYS LYS ALA GLU HIS VAL THR ASP VAL VAL LYS ARG          
SEQRES   8 K  210  CYS PRO ASN HIS GLU LEU GLY ARG ASP PHE ASN GLU GLY          
SEQRES   9 K  210  GLN SER ALA PRO ALA SER HIS LEU ILE ARG VAL GLU GLY          
SEQRES  10 K  210  ASN ASN LEU SER GLN TYR VAL ASP ASP PRO VAL THR GLY          
SEQRES  11 K  210  ARG GLN SER VAL VAL VAL PRO TYR GLU PRO PRO GLN VAL          
SEQRES  12 K  210  GLY THR GLU PHE THR THR ILE LEU TYR ASN PHE MET CYS          
SEQRES  13 K  210  ASN SER SER CYS VAL GLY GLY MET ASN ARG ARG PRO ILE          
SEQRES  14 K  210  LEU ILE ILE ILE THR LEU GLU MET ARG ASP GLY GLN VAL          
SEQRES  15 K  210  LEU GLY ARG ARG SER PHE GLU GLY ARG ILE CYS ALA CYS          
SEQRES  16 K  210  PRO GLY ARG ASP ARG LYS ALA ASP GLU ASP HIS TYR ARG          
SEQRES  17 K  210  GLU GLN                                                      
SEQRES   1 L  210  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS GLU PHE ILE          
SEQRES   2 L  210  PRO SER ASN THR ASP TYR PRO GLY PRO HIS HIS PHE GLU          
SEQRES   3 L  210  VAL THR PHE GLN GLN SER SER THR ALA LYS SER ALA THR          
SEQRES   4 L  210  TRP THR TYR SER PRO LEU LEU LYS LYS LEU TYR CYS GLN          
SEQRES   5 L  210  ILE ALA LYS THR CYS PRO ILE GLN ILE LYS VAL SER THR          
SEQRES   6 L  210  PRO PRO PRO PRO GLY THR ALA ILE ARG ALA MET PRO VAL          
SEQRES   7 L  210  TYR LYS LYS ALA GLU HIS VAL THR ASP VAL VAL LYS ARG          
SEQRES   8 L  210  CYS PRO ASN HIS GLU LEU GLY ARG ASP PHE ASN GLU GLY          
SEQRES   9 L  210  GLN SER ALA PRO ALA SER HIS LEU ILE ARG VAL GLU GLY          
SEQRES  10 L  210  ASN ASN LEU SER GLN TYR VAL ASP ASP PRO VAL THR GLY          
SEQRES  11 L  210  ARG GLN SER VAL VAL VAL PRO TYR GLU PRO PRO GLN VAL          
SEQRES  12 L  210  GLY THR GLU PHE THR THR ILE LEU TYR ASN PHE MET CYS          
SEQRES  13 L  210  ASN SER SER CYS VAL GLY GLY MET ASN ARG ARG PRO ILE          
SEQRES  14 L  210  LEU ILE ILE ILE THR LEU GLU MET ARG ASP GLY GLN VAL          
SEQRES  15 L  210  LEU GLY ARG ARG SER PHE GLU GLY ARG ILE CYS ALA CYS          
SEQRES  16 L  210  PRO GLY ARG ASP ARG LYS ALA ASP GLU ASP HIS TYR ARG          
SEQRES  17 L  210  GLU GLN                                                      
SEQRES   1 E   12   DC  DG  DG  DG  DC  DA  DT  DG  DC  DC  DC  DG              
SEQRES   1 F   12   DC  DG  DG  DG  DC  DA  DT  DG  DC  DC  DC  DG              
SEQRES   1 G   12   DC  DG  DG  DG  DC  DA  DT  DG  DC  DC  DC  DG              
SEQRES   1 H   12   DC  DG  DG  DG  DC  DA  DT  DG  DC  DC  DC  DG              
SEQRES   1 M   12   DC  DG  DG  DG  DC  DA  DT  DG  DC  DC  DC  DG              
SEQRES   1 N   12   DC  DG  DG  DG  DC  DA  DT  DG  DC  DC  DC  DG              
SEQRES   1 O   12   DC  DG  DG  DG  DC  DA  DT  DG  DC  DC  DC  DG              
SEQRES   1 P   12   DC  DG  DG  DG  DC  DA  DT  DG  DC  DC  DC  DG              
HET     ZN  A 401       1                                                       
HET     ZN  B 401       1                                                       
HET     ZN  C 401       1                                                       
HET     ZN  D 401       1                                                       
HET     ZN  I 401       1                                                       
HET     ZN  J 401       1                                                       
HET     ZN  K 401       1                                                       
HET     ZN  L 401       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL  17   ZN    8(ZN 2+)                                                     
FORMUL  25  HOH   *188(H2 O)                                                    
HELIX    1   1 LYS A  183  THR A  188  1                                   6    
HELIX    2   2 CYS A  194  GLY A  200  1                                   7    
HELIX    3   3 CYS A  297  ARG A  310  1                                  14    
HELIX    4   4 LYS B  183  THR B  188  1                                   6    
HELIX    5   5 CYS B  194  GLY B  200  1                                   7    
HELIX    6   6 CYS B  297  GLN B  312  1                                  16    
HELIX    7   7 CYS C  194  LEU C  199  1                                   6    
HELIX    8   8 CYS C  297  GLN C  312  1                                  16    
HELIX    9   9 GLU D  185  ASP D  189  5                                   5    
HELIX   10  10 CYS D  194  LEU D  199  1                                   6    
HELIX   11  11 CYS D  297  GLN D  312  1                                  16    
HELIX   12  12 CYS I  194  LEU I  199  1                                   6    
HELIX   13  13 CYS I  297  GLU I  311  1                                  15    
HELIX   14  14 PRO J  122  HIS J  126  5                                   5    
HELIX   15  15 LYS J  183  THR J  188  1                                   6    
HELIX   16  16 CYS J  194  GLY J  200  1                                   7    
HELIX   17  17 CYS J  297  GLN J  312  1                                  16    
HELIX   18  18 CYS K  194  LEU K  199  1                                   6    
HELIX   19  19 CYS K  297  GLU K  311  1                                  15    
HELIX   20  20 LYS L  183  VAL L  187  5                                   5    
HELIX   21  21 CYS L  194  GLY L  200  1                                   7    
HELIX   22  22 GLY L  299  GLU L  311  1                                  13    
SHEET    1   A 4 GLU A 128  THR A 130  0                                        
SHEET    2   A 4 CYS A 159  LYS A 164 -1  O  GLN A 162   N  THR A 130           
SHEET    3   A 4 THR A 250  PHE A 256 -1  O  THR A 250   N  ILE A 163           
SHEET    4   A 4 ILE A 215  VAL A 217 -1  N  ARG A 216   O  ASN A 255           
SHEET    1   B 7 TRP A 142  THR A 143  0                                        
SHEET    2   B 7 LYS A 150  CYS A 153 -1  O  TYR A 152   N  THR A 143           
SHEET    3   B 7 GLU A 291  ILE A 294  1  O  ARG A 293   N  CYS A 153           
SHEET    4   B 7 ILE A 271  GLU A 278 -1  N  ILE A 271   O  GLY A 292           
SHEET    5   B 7 ALA A 174  TYR A 181 -1  N  VAL A 180   O  LEU A 272           
SHEET    6   B 7 ARG A 233  PRO A 239 -1  O  VAL A 238   N  ILE A 175           
SHEET    7   B 7 GLN A 224  ASP A 228 -1  N  GLN A 224   O  VAL A 237           
SHEET    1   C 5 TRP A 142  THR A 143  0                                        
SHEET    2   C 5 LYS A 150  CYS A 153 -1  O  TYR A 152   N  THR A 143           
SHEET    3   C 5 GLU A 291  ILE A 294  1  O  ARG A 293   N  CYS A 153           
SHEET    4   C 5 ILE A 271  GLU A 278 -1  N  ILE A 271   O  GLY A 292           
SHEET    5   C 5 GLY A 286  ARG A 288 -1  O  GLY A 286   N  LEU A 277           
SHEET    1   D 4 PHE B 127  PHE B 131  0                                        
SHEET    2   D 4 CYS B 159  VAL B 165 -1  O  GLN B 162   N  THR B 130           
SHEET    3   D 4 THR B 250  PHE B 256 -1  O  THR B 250   N  ILE B 163           
SHEET    4   D 4 ILE B 215  VAL B 217 -1  N  ARG B 216   O  ASN B 255           
SHEET    1   E 7 TRP B 142  SER B 145  0                                        
SHEET    2   E 7 LYS B 150  CYS B 153 -1  O  TYR B 152   N  THR B 143           
SHEET    3   E 7 VAL B 284  ILE B 294  1  O  ARG B 293   N  CYS B 153           
SHEET    4   E 7 ILE B 271  GLU B 278 -1  N  ILE B 271   O  GLY B 292           
SHEET    5   E 7 ALA B 174  TYR B 181 -1  N  VAL B 180   O  LEU B 272           
SHEET    6   E 7 GLN B 234  PRO B 239 -1  O  VAL B 238   N  ILE B 175           
SHEET    7   E 7 GLN B 224  ASP B 227 -1  N  VAL B 226   O  SER B 235           
SHEET    1   F 4 GLU C 128  THR C 130  0                                        
SHEET    2   F 4 CYS C 159  LYS C 164 -1  O  GLN C 162   N  THR C 130           
SHEET    3   F 4 THR C 250  PHE C 256 -1  O  THR C 250   N  ILE C 163           
SHEET    4   F 4 ILE C 215  VAL C 217 -1  N  ARG C 216   O  ASN C 255           
SHEET    1   G 7 TRP C 142  SER C 145  0                                        
SHEET    2   G 7 LYS C 150  GLN C 154 -1  O  TYR C 152   N  THR C 143           
SHEET    3   G 7 VAL C 284  CYS C 295  1  O  GLU C 291   N  LEU C 151           
SHEET    4   G 7 ILE C 271  GLU C 278 -1  N  LEU C 277   O  LEU C 285           
SHEET    5   G 7 ALA C 174  TYR C 181 -1  N  ARG C 176   O  THR C 276           
SHEET    6   G 7 GLN C 234  PRO C 239 -1  O  VAL C 236   N  ALA C 177           
SHEET    7   G 7 GLN C 224  ASP C 227 -1  N  VAL C 226   O  SER C 235           
SHEET    1   H 4 GLU D 128  THR D 130  0                                        
SHEET    2   H 4 CYS D 159  LYS D 164 -1  O  GLN D 162   N  THR D 130           
SHEET    3   H 4 THR D 250  PHE D 256 -1  O  THR D 250   N  ILE D 163           
SHEET    4   H 4 ILE D 215  VAL D 217 -1  N  ARG D 216   O  ASN D 255           
SHEET    1   I 7 TRP D 142  SER D 145  0                                        
SHEET    2   I 7 LYS D 150  CYS D 153 -1  O  TYR D 152   N  THR D 143           
SHEET    3   I 7 ARG D 288  ILE D 294  1  O  GLU D 291   N  LEU D 151           
SHEET    4   I 7 ILE D 271  MET D 279 -1  N  ILE D 271   O  GLY D 292           
SHEET    5   I 7 THR D 173  TYR D 181 -1  N  MET D 178   O  ILE D 274           
SHEET    6   I 7 GLN D 234  PRO D 239 -1  O  VAL D 238   N  ILE D 175           
SHEET    7   I 7 GLN D 224  ASP D 227 -1  N  VAL D 226   O  SER D 235           
SHEET    1   J 4 GLU I 128  PHE I 131  0                                        
SHEET    2   J 4 THR I 158  LYS I 164 -1  O  LYS I 164   N  GLU I 128           
SHEET    3   J 4 THR I 250  PHE I 256 -1  O  TYR I 254   N  CYS I 159           
SHEET    4   J 4 ILE I 215  VAL I 217 -1  N  ARG I 216   O  ASN I 255           
SHEET    1   K 7 TRP I 142  SER I 145  0                                        
SHEET    2   K 7 LYS I 150  CYS I 153 -1  O  LYS I 150   N  SER I 145           
SHEET    3   K 7 VAL I 284  ILE I 294  1  O  ARG I 293   N  LEU I 151           
SHEET    4   K 7 ILE I 271  GLU I 278 -1  N  ILE I 273   O  PHE I 290           
SHEET    5   K 7 ALA I 174  TYR I 181 -1  N  VAL I 180   O  LEU I 272           
SHEET    6   K 7 GLN I 234  PRO I 239 -1  O  VAL I 236   N  ALA I 177           
SHEET    7   K 7 GLN I 224  ASP I 227 -1  N  VAL I 226   O  SER I 235           
SHEET    1   L 4 GLU J 128  PHE J 131  0                                        
SHEET    2   L 4 CYS J 159  LYS J 164 -1  N  LYS J 164   O  GLU J 128           
SHEET    3   L 4 ILE J 252  PHE J 256 -1  O  ILE J 252   N  ILE J 161           
SHEET    4   L 4 ILE J 215  VAL J 217 -1  N  ARG J 216   O  ASN J 255           
SHEET    1   M 6 TRP J 142  SER J 145  0                                        
SHEET    2   M 6 LYS J 150  CYS J 153 -1  O  TYR J 152   N  THR J 143           
SHEET    3   M 6 VAL J 284  GLY J 292  1  O  GLU J 291   N  LEU J 151           
SHEET    4   M 6 ILE J 271  MET J 279 -1  N  ILE J 273   O  PHE J 290           
SHEET    5   M 6 THR J 173  TYR J 181 -1  N  VAL J 180   O  LEU J 272           
SHEET    6   M 6 VAL J 236  VAL J 238 -1  O  VAL J 238   N  ILE J 175           
SHEET    1   N 7 TRP K 142  SER K 145  0                                        
SHEET    2   N 7 LYS K 150  GLN K 154 -1  O  TYR K 152   N  THR K 143           
SHEET    3   N 7 ARG K 288  CYS K 295  1  O  GLU K 291   N  LEU K 151           
SHEET    4   N 7 ILE K 271  GLU K 278 -1  N  ILE K 273   O  PHE K 290           
SHEET    5   N 7 ALA K 174  TYR K 181 -1  N  ALA K 174   O  GLU K 278           
SHEET    6   N 7 GLN K 234  PRO K 239 -1  O  VAL K 238   N  ILE K 175           
SHEET    7   N 7 TYR K 225  ASP K 227 -1  N  VAL K 226   O  SER K 235           
SHEET    1   O 3 CYS K 159  ILE K 163  0                                        
SHEET    2   O 3 THR K 250  PHE K 256 -1  O  TYR K 254   N  CYS K 159           
SHEET    3   O 3 ILE K 215  VAL K 217 -1  N  ARG K 216   O  ASN K 255           
SHEET    1   P 4 GLU L 128  THR L 130  0                                        
SHEET    2   P 4 CYS L 159  LYS L 164 -1  O  LYS L 164   N  GLU L 128           
SHEET    3   P 4 THR L 250  PHE L 256 -1  O  TYR L 254   N  CYS L 159           
SHEET    4   P 4 ILE L 215  VAL L 217 -1  N  ARG L 216   O  ASN L 255           
SHEET    1   Q 7 TRP L 142  TYR L 144  0                                        
SHEET    2   Q 7 LEU L 151  GLN L 154 -1  O  TYR L 152   N  THR L 143           
SHEET    3   Q 7 VAL L 284  CYS L 295  1  O  ARG L 293   N  LEU L 151           
SHEET    4   Q 7 ILE L 271  GLU L 278 -1  N  LEU L 277   O  GLY L 286           
SHEET    5   Q 7 ALA L 174  TYR L 181 -1  N  ALA L 174   O  GLU L 278           
SHEET    6   Q 7 GLN L 234  PRO L 239 -1  O  VAL L 238   N  ILE L 175           
SHEET    7   Q 7 GLN L 224  ASP L 227 -1  N  VAL L 226   O  SER L 235           
LINK         SG  CYS A 194                ZN    ZN A 401     1555   1555  2.29  
LINK         ND1 HIS A 197                ZN    ZN A 401     1555   1555  2.02  
LINK         SG  CYS A 258                ZN    ZN A 401     1555   1555  2.28  
LINK         SG  CYS A 262                ZN    ZN A 401     1555   1555  2.35  
LINK         SG  CYS B 194                ZN    ZN B 401     1555   1555  2.27  
LINK         ND1 HIS B 197                ZN    ZN B 401     1555   1555  2.05  
LINK         SG  CYS B 258                ZN    ZN B 401     1555   1555  2.28  
LINK         SG  CYS B 262                ZN    ZN B 401     1555   1555  2.34  
LINK         SG  CYS C 194                ZN    ZN C 401     1555   1555  2.32  
LINK         ND1 HIS C 197                ZN    ZN C 401     1555   1555  2.05  
LINK         SG  CYS C 258                ZN    ZN C 401     1555   1555  2.28  
LINK         SG  CYS C 262                ZN    ZN C 401     1555   1555  2.32  
LINK         SG  CYS D 194                ZN    ZN D 401     1555   1555  2.35  
LINK         ND1 HIS D 197                ZN    ZN D 401     1555   1555  2.01  
LINK         SG  CYS D 258                ZN    ZN D 401     1555   1555  2.30  
LINK         SG  CYS D 262                ZN    ZN D 401     1555   1555  2.31  
LINK         SG  CYS I 194                ZN    ZN I 401     1555   1555  2.26  
LINK         ND1 HIS I 197                ZN    ZN I 401     1555   1555  2.03  
LINK         SG  CYS I 258                ZN    ZN I 401     1555   1555  2.29  
LINK         SG  CYS I 262                ZN    ZN I 401     1555   1555  2.31  
LINK         SG  CYS J 194                ZN    ZN J 401     1555   1555  2.30  
LINK         ND1 HIS J 197                ZN    ZN J 401     1555   1555  2.03  
LINK         SG  CYS J 258                ZN    ZN J 401     1555   1555  2.33  
LINK         SG  CYS J 262                ZN    ZN J 401     1555   1555  2.33  
LINK         SG  CYS K 194                ZN    ZN K 401     1555   1555  2.31  
LINK         ND1 HIS K 197                ZN    ZN K 401     1555   1555  2.05  
LINK         SG  CYS K 258                ZN    ZN K 401     1555   1555  2.26  
LINK         SG  CYS K 262                ZN    ZN K 401     1555   1555  2.32  
LINK         SG  CYS L 194                ZN    ZN L 401     1555   1555  2.28  
LINK         ND1 HIS L 197                ZN    ZN L 401     1555   1555  2.04  
LINK         SG  CYS L 258                ZN    ZN L 401     1555   1555  2.30  
LINK         SG  CYS L 262                ZN    ZN L 401     1555   1555  2.31  
SITE     1 AC1  4 CYS A 194  HIS A 197  CYS A 258  CYS A 262                    
SITE     1 AC2  4 CYS B 194  HIS B 197  CYS B 258  CYS B 262                    
SITE     1 AC3  4 CYS C 194  HIS C 197  CYS C 258  CYS C 262                    
SITE     1 AC4  4 CYS D 194  HIS D 197  CYS D 258  CYS D 262                    
SITE     1 AC5  4 CYS I 194  HIS I 197  CYS I 258  CYS I 262                    
SITE     1 AC6  4 CYS J 194  HIS J 197  CYS J 258  CYS J 262                    
SITE     1 AC7  4 CYS K 194  HIS K 197  CYS K 258  CYS K 262                    
SITE     1 AC8  4 CYS L 194  HIS L 197  CYS L 258  CYS L 262                    
CRYST1   82.540  104.200  123.223  90.00  96.55  90.00 P 1 21 1     16          
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      0.012115  0.000000  0.001391        0.00000                         
SCALE2      0.000000  0.009597  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008169        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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