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Database: PDB
Entry: 3H66
LinkDB: 3H66
Original site: 3H66 
HEADER    HYDROLASE                               23-APR-09   3H66              
TITLE     CATALYTIC DOMAIN OF HUMAN SERINE/THREONINE PHOSPHATASE 5              
TITLE    2 (PP5C) WITH TWO ZN2+ ATOMS                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN PHOSPHATASE 5;                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 176-490;                        
COMPND   5 SYNONYM: PP5C, PP5, PROTEIN PHOSPHATASE T, PP-T, PPT;                
COMPND   6 EC: 3.1.3.16;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PPP5C, PPP5;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIPL;                             
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PDEST30                                   
KEYWDS    METALLOENZYME, PHOSPHATASE, CYTOPLASM, HYDROLASE, IRON,               
KEYWDS   2 MANGANESE, METAL-BINDING, NUCLEUS, PROTEIN PHOSPHATASE, TPR          
KEYWDS   3 REPEAT                                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.BERTINI,V.CALDERONE,M.FRAGAI,C.LUCHINAT,E.TALLURI                   
REVDAT   1   29-SEP-09 3H66    0                                                
JRNL        AUTH   I.BERTINI,V.CALDERONE,M.FRAGAI,C.LUCHINAT,E.TALLURI          
JRNL        TITL   STRUCTURAL BASIS OF SERINE/THREONINE PHOSPHATASE             
JRNL        TITL 2 INHIBITION BY THE ARCHETYPAL SMALL MOLECULES                 
JRNL        TITL 3 CANTHARIDIN AND NORCANTHARIDIN                               
JRNL        REF    J.MED.CHEM.                   V.  52  4838 2009              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   19601647                                                     
JRNL        DOI    10.1021/JM900610K                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.59 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.4.0067                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.59                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.32                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 17919                          
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) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.291                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1822                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.59                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.65                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1004                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2700                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 119                          
REMARK   3   BIN FREE R VALUE                    : 0.3970                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5056                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 56                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 13.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 3.08                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.54000                                             
REMARK   3    B22 (A**2) : 0.12000                                              
REMARK   3    B33 (A**2) : 0.85000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.89000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.416         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.286         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.470        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.883                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.773                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5184 ; 0.052 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7012 ; 3.702 ; 1.955       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   628 ;10.405 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   256 ;38.341 ;24.688       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   894 ;21.289 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;24.676 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   744 ; 0.235 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3986 ; 0.019 ; 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):  3132 ; 0.569 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5064 ; 1.015 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2052 ; 2.885 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1948 ; 4.292 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
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          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 3H66 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-MAY-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB052741.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-AUG-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : SEALED TUBE                        
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : OXFORD DIFFRACTION ENHANCE         
REMARK 200                                   ULTRA                              
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54056                            
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : OXFORD ONYX CCD                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19742                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.590                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.21100                            
REMARK 200  R SYM                      (I) : 0.21100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.59                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.45300                            
REMARK 200  R SYM FOR SHELL            (I) : 0.45300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
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: 1S95                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10MM TRIS-HCL, 40% MPD, 20% PEG MME      
REMARK 280  5000, PH 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K       
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       77.12550            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       20.84200            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       77.12550            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       20.84200            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD2  ASP A   242     OD2  ASP A   271              1.97            
REMARK 500   NZ   LYS B   412     OE2  GLU B   416              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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   O    HOH A     1     O    HOH A    30     4445     2.09            
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 176   CB    TYR A 176   CG      0.104                       
REMARK 500    TYR A 176   CG    TYR A 176   CD2     0.086                       
REMARK 500    LYS A 180   CD    LYS A 180   CE      0.212                       
REMARK 500    LYS A 180   CE    LYS A 180   NZ      0.176                       
REMARK 500    GLU A 182   CG    GLU A 182   CD      0.120                       
REMARK 500    LYS A 185   CD    LYS A 185   CE      0.183                       
REMARK 500    PHE A 190   CG    PHE A 190   CD1     0.092                       
REMARK 500    GLU A 193   CB    GLU A 193   CG     -0.139                       
REMARK 500    GLU A 193   CG    GLU A 193   CD     -0.092                       
REMARK 500    GLN A 196   CB    GLN A 196   CG      0.163                       
REMARK 500    TRP A 197   CG    TRP A 197   CD1     0.095                       
REMARK 500    ARG A 206   CG    ARG A 206   CD      0.232                       
REMARK 500    ARG A 206   C     ARG A 206   O      -0.124                       
REMARK 500    VAL A 214   CA    VAL A 214   CB      0.183                       
REMARK 500    LYS A 217   CE    LYS A 217   NZ      0.161                       
REMARK 500    GLU A 218   CD    GLU A 218   OE2     0.069                       
REMARK 500    SER A 224   C     SER A 224   O      -0.116                       
REMARK 500    VAL A 227   CB    VAL A 227   CG1    -0.130                       
REMARK 500    GLU A 233   CG    GLU A 233   CD      0.287                       
REMARK 500    GLU A 233   CD    GLU A 233   OE1     0.068                       
REMARK 500    GLU A 233   CD    GLU A 233   OE2     0.089                       
REMARK 500    VAL A 239   CB    VAL A 239   CG1    -0.161                       
REMARK 500    HIS A 244   N     HIS A 244   CA      0.161                       
REMARK 500    TYR A 248   CD1   TYR A 248   CE1     0.104                       
REMARK 500    TYR A 248   CE2   TYR A 248   CD2     0.106                       
REMARK 500    LEU A 251   C     LEU A 251   O      -0.126                       
REMARK 500    PHE A 254   CZ    PHE A 254   CE2     0.179                       
REMARK 500    GLU A 255   CB    GLU A 255   CG     -0.236                       
REMARK 500    GLU A 262   CG    GLU A 262   CD      0.103                       
REMARK 500    GLU A 262   CD    GLU A 262   OE1     0.120                       
REMARK 500    GLU A 262   CD    GLU A 262   OE2     0.071                       
REMARK 500    TYR A 266   CB    TYR A 266   CG     -0.125                       
REMARK 500    ILE A 267   N     ILE A 267   CA     -0.123                       
REMARK 500    PHE A 268   CE1   PHE A 268   CZ     -0.188                       
REMARK 500    PHE A 268   CE2   PHE A 268   CD2    -0.151                       
REMARK 500    ARG A 275   NE    ARG A 275   CZ      0.090                       
REMARK 500    TYR A 293   CE2   TYR A 293   CD2    -0.141                       
REMARK 500    HIS A 296   CA    HIS A 296   C       0.160                       
REMARK 500    GLU A 305   CG    GLU A 305   CD      0.114                       
REMARK 500    GLN A 311   CG    GLN A 311   CD      0.151                       
REMARK 500    PHE A 315   CG    PHE A 315   CD1     0.116                       
REMARK 500    PHE A 315   CZ    PHE A 315   CE2     0.130                       
REMARK 500    GLU A 318   CB    GLU A 318   CG      0.115                       
REMARK 500    TYR A 323   CZ    TYR A 323   CE2    -0.119                       
REMARK 500    ALA A 325   C     ALA A 325   O       0.135                       
REMARK 500    GLN A 326   CD    GLN A 326   OE1     0.153                       
REMARK 500    LEU A 330   CG    LEU A 330   CD1     0.272                       
REMARK 500    PHE A 331   CZ    PHE A 331   CE2    -0.129                       
REMARK 500    LYS A 347   CD    LYS A 347   CE      0.164                       
REMARK 500    LYS A 347   C     LYS A 347   O      -0.119                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     155 BOND DEVIATIONS.                              
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    LYS A 180   CD  -  CE  -  NZ  ANGL. DEV. =  18.7 DEGREES          
REMARK 500    LEU A 181   CB  -  CG  -  CD1 ANGL. DEV. =  13.4 DEGREES          
REMARK 500    ASP A 183   CB  -  CG  -  OD1 ANGL. DEV. =  10.2 DEGREES          
REMARK 500    ASP A 183   CB  -  CG  -  OD2 ANGL. DEV. =  -8.3 DEGREES          
REMARK 500    MET A 195   CG  -  SD  -  CE  ANGL. DEV. =  10.2 DEGREES          
REMARK 500    LYS A 203   CB  -  CG  -  CD  ANGL. DEV. = -19.6 DEGREES          
REMARK 500    ARG A 206   CG  -  CD  -  NE  ANGL. DEV. = -16.1 DEGREES          
REMARK 500    LEU A 223   CB  -  CG  -  CD1 ANGL. DEV. = -11.0 DEGREES          
REMARK 500    VAL A 227   CG1 -  CB  -  CG2 ANGL. DEV. = -11.7 DEGREES          
REMARK 500    LEU A 231   CA  -  CB  -  CG  ANGL. DEV. = -13.8 DEGREES          
REMARK 500    LYS A 236   CD  -  CE  -  NZ  ANGL. DEV. = -13.9 DEGREES          
REMARK 500    ASP A 249   CB  -  CG  -  OD2 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    ASP A 271   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP A 271   CB  -  CG  -  OD2 ANGL. DEV. =  -9.1 DEGREES          
REMARK 500    ASP A 274   CB  -  CG  -  OD1 ANGL. DEV. =  -7.7 DEGREES          
REMARK 500    ARG A 275   NE  -  CZ  -  NH1 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    LEU A 291   CB  -  CG  -  CD2 ANGL. DEV. = -16.2 DEGREES          
REMARK 500    LEU A 299   CB  -  CG  -  CD1 ANGL. DEV. = -13.7 DEGREES          
REMARK 500    ARG A 301   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    LEU A 355   CB  -  CG  -  CD2 ANGL. DEV. = -13.5 DEGREES          
REMARK 500    GLU A 358   N   -  CA  -  C   ANGL. DEV. = -18.9 DEGREES          
REMARK 500    SER A 357   O   -  C   -  N   ANGL. DEV. =  -9.8 DEGREES          
REMARK 500    ASP A 359   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ARG A 367   NE  -  CZ  -  NH1 ANGL. DEV. =   7.7 DEGREES          
REMARK 500    ARG A 367   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.9 DEGREES          
REMARK 500    LYS A 368   CD  -  CE  -  NZ  ANGL. DEV. = -25.4 DEGREES          
REMARK 500    PRO A 376   C   -  N   -  CA  ANGL. DEV. =  -9.1 DEGREES          
REMARK 500    ASP A 377   CB  -  CA  -  C   ANGL. DEV. = -15.4 DEGREES          
REMARK 500    SER A 378   N   -  CA  -  C   ANGL. DEV. = -16.8 DEGREES          
REMARK 500    ASP A 383   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A 383   CB  -  CG  -  OD2 ANGL. DEV. =  -8.6 DEGREES          
REMARK 500    ARG A 395   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ARG A 400   NE  -  CZ  -  NH1 ANGL. DEV. =  -7.2 DEGREES          
REMARK 500    ARG A 400   NE  -  CZ  -  NH2 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    ASP A 421   CB  -  CG  -  OD1 ANGL. DEV. =  -6.8 DEGREES          
REMARK 500    ASP A 421   CB  -  CG  -  OD2 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    ARG A 425   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    ARG A 425   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ARG A 441   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    PHE A 446   CB  -  CA  -  C   ANGL. DEV. = -13.2 DEGREES          
REMARK 500    CYS A 452   CA  -  CB  -  SG  ANGL. DEV. =   6.9 DEGREES          
REMARK 500    PRO A 482   C   -  N   -  CA  ANGL. DEV. = -12.0 DEGREES          
REMARK 500    LEU B 181   CB  -  CG  -  CD2 ANGL. DEV. = -13.5 DEGREES          
REMARK 500    ASP B 183   N   -  CA  -  C   ANGL. DEV. = -19.6 DEGREES          
REMARK 500    LYS B 192   CD  -  CE  -  NZ  ANGL. DEV. =  14.7 DEGREES          
REMARK 500    LEU B 194   CB  -  CG  -  CD1 ANGL. DEV. = -19.3 DEGREES          
REMARK 500    TYR B 198   CG  -  CD1 -  CE1 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ASP B 200   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG B 206   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    LYS B 217   CD  -  CE  -  NZ  ANGL. DEV. =  14.1 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      86 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    ASP A 183       43.21     79.41                                   
REMARK 500    GLN A 201       10.72     58.27                                   
REMARK 500    HIS A 244       52.89     37.78                                   
REMARK 500    SER A 261      173.30    177.05                                   
REMARK 500    ASN A 264       65.32   -152.44                                   
REMARK 500    ASP A 274      142.74     88.11                                   
REMARK 500    ARG A 275      -45.77     81.50                                   
REMARK 500    LYS A 320      -29.69    -36.91                                   
REMARK 500    TYR A 323     -113.17   -124.60                                   
REMARK 500    GLU A 336       -2.48    -56.36                                   
REMARK 500    LEU A 355     -155.55    -95.49                                   
REMARK 500    ASP A 377      -23.33    -35.05                                   
REMARK 500    SER A 378      172.85    175.05                                   
REMARK 500    ASN A 393      153.49    -41.07                                   
REMARK 500    SER A 403     -157.16     49.48                                   
REMARK 500    TYR A 422     -176.10   -178.28                                   
REMARK 500    SER A 426     -119.72   -132.39                                   
REMARK 500    HIS A 427      -35.38     82.44                                   
REMARK 500    GLN A 454      -50.82   -125.92                                   
REMARK 500    ASP A 468       96.19   -167.87                                   
REMARK 500    LEU A 469       38.88    -84.99                                   
REMARK 500    MET A 487      -12.15     75.52                                   
REMARK 500    ALA A 488      -36.46    -34.03                                   
REMARK 500    ASP B 183       47.32    100.90                                   
REMARK 500    ASP B 200       40.67    -93.34                                   
REMARK 500    GLU B 233      -36.94    -30.94                                   
REMARK 500    SER B 261      177.37    166.39                                   
REMARK 500    ASP B 271       61.75     62.18                                   
REMARK 500    ASP B 274      147.51     73.25                                   
REMARK 500    ARG B 275      -61.88     81.22                                   
REMARK 500    TYR B 293       58.44   -144.79                                   
REMARK 500    PRO B 294       -3.77    -58.66                                   
REMARK 500    TYR B 323     -124.10   -121.37                                   
REMARK 500    ASN B 345       18.30     57.02                                   
REMARK 500    LEU B 355     -148.58    -89.29                                   
REMARK 500    ASP B 364      -48.76    -27.82                                   
REMARK 500    ASN B 372       72.22    -60.09                                   
REMARK 500    ASN B 393      138.14    -21.12                                   
REMARK 500    SER B 403     -157.69     55.09                                   
REMARK 500    SER B 426     -115.24   -127.15                                   
REMARK 500    HIS B 427      -25.85     56.34                                   
REMARK 500    ASN B 450       50.94     18.70                                   
REMARK 500    TYR B 451      127.10    -28.55                                   
REMARK 500    SER B 467       47.08   -101.06                                   
REMARK 500    ASP B 468       66.05    140.42                                   
REMARK 500    LEU B 469       27.83    -76.13                                   
REMARK 500    MET B 487      -12.65     74.47                                   
REMARK 500    ALA B 488      -44.75    -25.41                                   
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 LEU A  355     PHE A  356                 -148.34                    
REMARK 500 GLN A  454     MET A  455                 -147.88                    
REMARK 500 GLN B  465     GLY B  466                 -146.29                    
REMARK 500 THR B  477     ALA B  478                 -144.96                    
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 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: (11X,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     TYR A 176        21.0      L          L   OUTSIDE RANGE          
REMARK 500     VAL A 214        18.3      L          L   OUTSIDE RANGE          
REMARK 500     GLU A 233        21.3      L          L   OUTSIDE RANGE          
REMARK 500     PRO A 260        46.1      L          L   OUTSIDE RANGE          
REMARK 500     VAL A 282        23.9      L          L   OUTSIDE RANGE          
REMARK 500     ASP A 364        18.2      L          L   OUTSIDE RANGE          
REMARK 500     ASP A 365        22.9      L          L   OUTSIDE RANGE          
REMARK 500     TRP A 386        22.4      L          L   OUTSIDE RANGE          
REMARK 500     ASN A 419        22.7      L          L   OUTSIDE RANGE          
REMARK 500     SER A 447        23.8      L          L   OUTSIDE RANGE          
REMARK 500     GLU B 193        24.3      L          L   OUTSIDE RANGE          
REMARK 500     GLN B 201        24.6      L          L   OUTSIDE RANGE          
REMARK 500     ARG B 206        24.6      L          L   OUTSIDE RANGE          
REMARK 500     ASP B 364        22.2      L          L   OUTSIDE RANGE          
REMARK 500     TRP B 386        24.0      L          L   OUTSIDE RANGE          
REMARK 500     CYS B 442        19.1      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 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 242   OD2                                                    
REMARK 620 2 HIS A 244   NE2  90.7                                              
REMARK 620 3 ASP A 271   OD2  58.9  86.2                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 500  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 303   OD1                                                    
REMARK 620 2 HIS A 352   NE2  81.7                                              
REMARK 620 3 HIS A 427   ND1  92.9  82.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 242   OD2                                                    
REMARK 620 2 HIS B 244   NE2  96.8                                              
REMARK 620 3 ASP B 271   OD2  71.1  79.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 500  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 271   OD2                                                    
REMARK 620 2 ASN B 303   OD1 109.9                                              
REMARK 620 3 HIS B 352   NE2  92.5  66.7                                        
REMARK 620 4 HIS B 427   ND1 164.8  81.3  82.4                                  
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 500                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 501                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 500                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 501                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3H60   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3H61   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3H62   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3H63   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3H64   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3H67   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3H68   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3H69   RELATED DB: PDB                                   
DBREF  3H66 A  176   490  UNP    P53041   PPP5_HUMAN     176    490             
DBREF  3H66 B  176   490  UNP    P53041   PPP5_HUMAN     176    490             
SEQRES   1 A  315  TYR SER GLY PRO LYS LEU GLU ASP GLY LYS VAL THR ILE          
SEQRES   2 A  315  SER PHE MET LYS GLU LEU MET GLN TRP TYR LYS ASP GLN          
SEQRES   3 A  315  LYS LYS LEU HIS ARG LYS CYS ALA TYR GLN ILE LEU VAL          
SEQRES   4 A  315  GLN VAL LYS GLU VAL LEU SER LYS LEU SER THR LEU VAL          
SEQRES   5 A  315  GLU THR THR LEU LYS GLU THR GLU LYS ILE THR VAL CYS          
SEQRES   6 A  315  GLY ASP THR HIS GLY GLN PHE TYR ASP LEU LEU ASN ILE          
SEQRES   7 A  315  PHE GLU LEU ASN GLY LEU PRO SER GLU THR ASN PRO TYR          
SEQRES   8 A  315  ILE PHE ASN GLY ASP PHE VAL ASP ARG GLY SER PHE SER          
SEQRES   9 A  315  VAL GLU VAL ILE LEU THR LEU PHE GLY PHE LYS LEU LEU          
SEQRES  10 A  315  TYR PRO ASP HIS PHE HIS LEU LEU ARG GLY ASN HIS GLU          
SEQRES  11 A  315  THR ASP ASN MET ASN GLN ILE TYR GLY PHE GLU GLY GLU          
SEQRES  12 A  315  VAL LYS ALA LYS TYR THR ALA GLN MET TYR GLU LEU PHE          
SEQRES  13 A  315  SER GLU VAL PHE GLU TRP LEU PRO LEU ALA GLN CYS ILE          
SEQRES  14 A  315  ASN GLY LYS VAL LEU ILE MET HIS GLY GLY LEU PHE SER          
SEQRES  15 A  315  GLU ASP GLY VAL THR LEU ASP ASP ILE ARG LYS ILE GLU          
SEQRES  16 A  315  ARG ASN ARG GLN PRO PRO ASP SER GLY PRO MET CYS ASP          
SEQRES  17 A  315  LEU LEU TRP SER ASP PRO GLN PRO GLN ASN GLY ARG SER          
SEQRES  18 A  315  ILE SER LYS ARG GLY VAL SER CYS GLN PHE GLY PRO ASP          
SEQRES  19 A  315  VAL THR LYS ALA PHE LEU GLU GLU ASN ASN LEU ASP TYR          
SEQRES  20 A  315  ILE ILE ARG SER HIS GLU VAL LYS ALA GLU GLY TYR GLU          
SEQRES  21 A  315  VAL ALA HIS GLY GLY ARG CYS VAL THR VAL PHE SER ALA          
SEQRES  22 A  315  PRO ASN TYR CYS ASP GLN MET GLY ASN LYS ALA SER TYR          
SEQRES  23 A  315  ILE HIS LEU GLN GLY SER ASP LEU ARG PRO GLN PHE HIS          
SEQRES  24 A  315  GLN PHE THR ALA VAL PRO HIS PRO ASN VAL LYS PRO MET          
SEQRES  25 A  315  ALA TYR ALA                                                  
SEQRES   1 B  315  TYR SER GLY PRO LYS LEU GLU ASP GLY LYS VAL THR ILE          
SEQRES   2 B  315  SER PHE MET LYS GLU LEU MET GLN TRP TYR LYS ASP GLN          
SEQRES   3 B  315  LYS LYS LEU HIS ARG LYS CYS ALA TYR GLN ILE LEU VAL          
SEQRES   4 B  315  GLN VAL LYS GLU VAL LEU SER LYS LEU SER THR LEU VAL          
SEQRES   5 B  315  GLU THR THR LEU LYS GLU THR GLU LYS ILE THR VAL CYS          
SEQRES   6 B  315  GLY ASP THR HIS GLY GLN PHE TYR ASP LEU LEU ASN ILE          
SEQRES   7 B  315  PHE GLU LEU ASN GLY LEU PRO SER GLU THR ASN PRO TYR          
SEQRES   8 B  315  ILE PHE ASN GLY ASP PHE VAL ASP ARG GLY SER PHE SER          
SEQRES   9 B  315  VAL GLU VAL ILE LEU THR LEU PHE GLY PHE LYS LEU LEU          
SEQRES  10 B  315  TYR PRO ASP HIS PHE HIS LEU LEU ARG GLY ASN HIS GLU          
SEQRES  11 B  315  THR ASP ASN MET ASN GLN ILE TYR GLY PHE GLU GLY GLU          
SEQRES  12 B  315  VAL LYS ALA LYS TYR THR ALA GLN MET TYR GLU LEU PHE          
SEQRES  13 B  315  SER GLU VAL PHE GLU TRP LEU PRO LEU ALA GLN CYS ILE          
SEQRES  14 B  315  ASN GLY LYS VAL LEU ILE MET HIS GLY GLY LEU PHE SER          
SEQRES  15 B  315  GLU ASP GLY VAL THR LEU ASP ASP ILE ARG LYS ILE GLU          
SEQRES  16 B  315  ARG ASN ARG GLN PRO PRO ASP SER GLY PRO MET CYS ASP          
SEQRES  17 B  315  LEU LEU TRP SER ASP PRO GLN PRO GLN ASN GLY ARG SER          
SEQRES  18 B  315  ILE SER LYS ARG GLY VAL SER CYS GLN PHE GLY PRO ASP          
SEQRES  19 B  315  VAL THR LYS ALA PHE LEU GLU GLU ASN ASN LEU ASP TYR          
SEQRES  20 B  315  ILE ILE ARG SER HIS GLU VAL LYS ALA GLU GLY TYR GLU          
SEQRES  21 B  315  VAL ALA HIS GLY GLY ARG CYS VAL THR VAL PHE SER ALA          
SEQRES  22 B  315  PRO ASN TYR CYS ASP GLN MET GLY ASN LYS ALA SER TYR          
SEQRES  23 B  315  ILE HIS LEU GLN GLY SER ASP LEU ARG PRO GLN PHE HIS          
SEQRES  24 B  315  GLN PHE THR ALA VAL PRO HIS PRO ASN VAL LYS PRO MET          
SEQRES  25 B  315  ALA TYR ALA                                                  
HET     ZN  A 500       1                                                       
HET     ZN  A 501       1                                                       
HET     ZN  B 500       1                                                       
HET     ZN  B 501       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   3   ZN    4(ZN 2+)                                                     
FORMUL   7  HOH   *56(H2 O)                                                     
HELIX    1   1 THR A  187  ASP A  200  1                                  14    
HELIX    2   2 HIS A  205  LYS A  222  1                                  18    
HELIX    3   3 GLN A  246  GLY A  258  1                                  13    
HELIX    4   4 PHE A  278  TYR A  293  1                                  16    
HELIX    5   5 THR A  306  GLY A  314  1                                   9    
HELIX    6   6 GLY A  314  TYR A  323  1                                  10    
HELIX    7   7 THR A  324  GLU A  336  1                                  13    
HELIX    8   8 THR A  362  LYS A  368  1                                   7    
HELIX    9   9 GLY A  379  SER A  387  1                                   9    
HELIX   10  10 GLY A  407  ASN A  419  1                                  13    
HELIX   11  11 HIS A  438  GLY A  440  5                                   3    
HELIX   12  12 ASN A  450  MET A  455  1                                   6    
HELIX   13  13 THR B  187  ASP B  200  1                                  14    
HELIX   14  14 HIS B  205  LYS B  222  1                                  18    
HELIX   15  15 GLN B  246  GLY B  258  1                                  13    
HELIX   16  16 PHE B  278  TYR B  293  1                                  16    
HELIX   17  17 THR B  306  GLY B  314  1                                   9    
HELIX   18  18 GLY B  314  TYR B  323  1                                  10    
HELIX   19  19 THR B  324  GLU B  336  1                                  13    
HELIX   20  20 THR B  362  ILE B  369  1                                   8    
HELIX   21  21 GLY B  379  SER B  387  1                                   9    
HELIX   22  22 GLY B  407  ASN B  419  1                                  13    
HELIX   23  23 HIS B  438  GLY B  440  5                                   3    
HELIX   24  24 ASN B  450  MET B  455  1                                   6    
SHEET    1   A 6 LEU A 226  THR A 229  0                                        
SHEET    2   A 6 ALA A 341  ILE A 344  1  O  ALA A 341   N  VAL A 227           
SHEET    3   A 6 VAL A 348  ILE A 350 -1  O  ILE A 350   N  GLN A 342           
SHEET    4   A 6 TYR A 422  ARG A 425  1  O  ILE A 424   N  LEU A 349           
SHEET    5   A 6 CYS A 442  VAL A 445  1  O  VAL A 443   N  ILE A 423           
SHEET    6   A 6 TYR A 434  ALA A 437 -1  N  ALA A 437   O  CYS A 442           
SHEET    1   B 5 PHE A 297  LEU A 300  0                                        
SHEET    2   B 5 TYR A 266  ASN A 269  1  N  PHE A 268   O  HIS A 298           
SHEET    3   B 5 LYS A 236  CYS A 240  1  N  CYS A 240   O  ASN A 269           
SHEET    4   B 5 ALA A 459  GLN A 465 -1  O  LEU A 464   N  ILE A 237           
SHEET    5   B 5 ASP A 468  PHE A 476 -1  O  HIS A 474   N  TYR A 461           
SHEET    1   C 3 ASP A 388  PRO A 389  0                                        
SHEET    2   C 3 CYS A 404  PHE A 406  1  O  PHE A 406   N  ASP A 388           
SHEET    3   C 3 ARG A 395  ILE A 397 -1  N  SER A 396   O  GLN A 405           
SHEET    1   D10 LEU B 226  THR B 229  0                                        
SHEET    2   D10 ALA B 341  ILE B 344  1  O  ALA B 341   N  VAL B 227           
SHEET    3   D10 VAL B 348  MET B 351 -1  O  ILE B 350   N  GLN B 342           
SHEET    4   D10 TYR B 422  ARG B 425  1  O  ILE B 424   N  MET B 351           
SHEET    5   D10 CYS B 442  VAL B 445  1  O  VAL B 445   N  ARG B 425           
SHEET    6   D10 GLU B 432  ALA B 437 -1  N  GLU B 435   O  THR B 444           
SHEET    7   D10 LYS B 458  GLN B 465  1  N  SER B 460   O  GLY B 433           
SHEET    8   D10 LYS B 236  CYS B 240 -1  N  VAL B 239   O  ILE B 462           
SHEET    9   D10 TYR B 266  ASN B 269  1  O  ILE B 267   N  CYS B 240           
SHEET   10   D10 PHE B 297  LEU B 300  1  O  HIS B 298   N  PHE B 268           
SHEET    1   E 8 LEU B 226  THR B 229  0                                        
SHEET    2   E 8 ALA B 341  ILE B 344  1  O  ALA B 341   N  VAL B 227           
SHEET    3   E 8 VAL B 348  MET B 351 -1  O  ILE B 350   N  GLN B 342           
SHEET    4   E 8 TYR B 422  ARG B 425  1  O  ILE B 424   N  MET B 351           
SHEET    5   E 8 CYS B 442  VAL B 445  1  O  VAL B 445   N  ARG B 425           
SHEET    6   E 8 GLU B 432  ALA B 437 -1  N  GLU B 435   O  THR B 444           
SHEET    7   E 8 LYS B 458  GLN B 465  1  N  SER B 460   O  GLY B 433           
SHEET    8   E 8 ASP B 468  PHE B 476 -1  O  HIS B 474   N  TYR B 461           
SHEET    1   F 3 ASP B 388  PRO B 389  0                                        
SHEET    2   F 3 CYS B 404  PHE B 406  1  O  PHE B 406   N  ASP B 388           
SHEET    3   F 3 ARG B 395  ILE B 397 -1  N  SER B 396   O  GLN B 405           
LINK         OD2 ASP A 242                ZN    ZN A 501     1555   1555  2.00  
LINK         NE2 HIS A 244                ZN    ZN A 501     1555   1555  2.18  
LINK         OD2 ASP A 271                ZN    ZN A 501     1555   1555  2.01  
LINK         OD1 ASN A 303                ZN    ZN A 500     1555   1555  2.06  
LINK         NE2 HIS A 352                ZN    ZN A 500     1555   1555  2.20  
LINK         ND1 HIS A 427                ZN    ZN A 500     1555   1555  2.31  
LINK         OD2 ASP B 242                ZN    ZN B 501     1555   1555  1.92  
LINK         NE2 HIS B 244                ZN    ZN B 501     1555   1555  2.25  
LINK         OD2 ASP B 271                ZN    ZN B 500     1555   1555  2.13  
LINK         OD2 ASP B 271                ZN    ZN B 501     1555   1555  2.09  
LINK         OD1 ASN B 303                ZN    ZN B 500     1555   1555  2.07  
LINK         NE2 HIS B 352                ZN    ZN B 500     1555   1555  2.20  
LINK         ND1 HIS B 427                ZN    ZN B 500     1555   1555  2.34  
SITE     1 AC1  6 HOH A   5  ASP A 271  ASN A 303  HIS A 352                    
SITE     2 AC1  6 HIS A 427   ZN A 501                                          
SITE     1 AC2  4 ASP A 242  HIS A 244  ASP A 271   ZN A 500                    
SITE     1 AC3  6 ASP B 242  ASP B 271  ASN B 303  HIS B 352                    
SITE     2 AC3  6 HIS B 427   ZN B 501                                          
SITE     1 AC4  4 ASP B 242  HIS B 244  ASP B 271   ZN B 500                    
CRYST1  154.251   41.684  106.092  90.00  96.46  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      0.006483  0.000000  0.000734        0.00000                         
SCALE2      0.000000  0.023990  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009486        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system