GenomeNet

Database: PDB
Entry: 3C0Z
LinkDB: 3C0Z
Original site: 3C0Z 
HEADER    HYDROLASE                               21-JAN-08   3C0Z              
TITLE     CRYSTAL STRUCTURE OF CATALYTIC DOMAIN OF HUMAN HISTONE                
TITLE    2 DEACETYLASE HDAC7 IN COMPLEX WITH SAHA                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE DEACETYLASE 7A;                                    
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: CATALYTIC DOMAIN: RESIDUES 482-903;                        
COMPND   5 SYNONYM: HD7A, HDAC7;                                                
COMPND   6 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: HDAC7A, HDAC7;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A-MHL                                
KEYWDS    HDAC, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM,            
KEYWDS   2 SGC, ALTERNATIVE SPLICING, CHROMATIN REGULATOR, CYTOPLASM,           
KEYWDS   3 HYDROLASE, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM,                    
KEYWDS   4 REPRESSOR, TRANSCRIPTION, TRANSCRIPTION REGULATION                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.MIN,A.SCHUETZ,P.LOPPNAU,J.WEIGELT,M.SUNDSTROM,                      
AUTHOR   2 C.H.ARROWSMITH,A.M.EDWARDS,A.BOCHKAREV,A.N.PLOTNIKOV,                
AUTHOR   3 STRUCTURAL GENOMICS CONSORTIUM (SGC)                                 
REVDAT   3   27-OCT-09 3C0Z    1       JRNL                                     
REVDAT   2   24-FEB-09 3C0Z    1       VERSN                                    
REVDAT   1   19-FEB-08 3C0Z    0                                                
SPRSDE     19-FEB-08 3C0Z      2PQO                                             
JRNL        AUTH   A.SCHUETZ,J.MIN,A.ALLALI-HASSANI,M.SCHAPIRA,                 
JRNL        AUTH 2 M.SHUEN,P.LOPPNAU,R.MAZITSCHEK,N.P.KWIATKOWSKI,              
JRNL        AUTH 3 T.A.LEWIS,R.L.MAGLATHIN,T.H.MCLEAN,A.BOCHKAREV,              
JRNL        AUTH 4 A.N.PLOTNIKOV,M.VEDADI,C.H.ARROWSMITH                        
JRNL        TITL   HUMAN HDAC7 HARBORS A CLASS IIA HISTONE                      
JRNL        TITL 2 DEACETYLASE-SPECIFIC ZINC BINDING MOTIF AND CRYPTIC          
JRNL        TITL 3 DEACETYLASE ACTIVITY.                                        
JRNL        REF    J.BIOL.CHEM.                  V. 283 11355 2008              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   18285338                                                     
JRNL        DOI    10.1074/JBC.M707362200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 57634                          
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) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3080                            
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3775                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 83.02                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2570                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 190                          
REMARK   3   BIN FREE R VALUE                    : 0.3220                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8400                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 37                                      
REMARK   3   SOLVENT ATOMS            : 332                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.02                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.67000                                              
REMARK   3    B22 (A**2) : 1.67000                                              
REMARK   3    B33 (A**2) : -2.50000                                             
REMARK   3    B12 (A**2) : 0.83000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.268         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.207         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.155         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.826         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.937                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8657 ; 0.018 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11698 ; 1.707 ; 1.936       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1104 ; 6.858 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   394 ;39.383 ;23.782       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1313 ;18.055 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    54 ;17.684 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1258 ; 0.123 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6705 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4222 ; 0.225 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5749 ; 0.307 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   464 ; 0.179 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    10 ; 0.338 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    84 ; 0.236 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    17 ; 0.147 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5499 ; 0.996 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8710 ; 1.715 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3182 ; 2.637 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2988 ; 3.972 ; 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   : 1.40                                          
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 3C0Z COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JAN-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB046204.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-SEP-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X25                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.10000                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 60749                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.5                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.04900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.27700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP, ARP/WARP                                      
REMARK 200 STARTING MODEL: PDB ENTRY 2NVR                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.62                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 % PEG 3350, 0.1 M HEPES PH 7.5,       
REMARK 280  10 % ISOPROPANOL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE        
REMARK 280  300K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       99.24467            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       49.62233            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLY A   481                                                      
REMARK 465     SER A   482                                                      
REMARK 465     ARG A   483                                                      
REMARK 465     ALA A   484                                                      
REMARK 465     GLN A   485                                                      
REMARK 465     SER A   486                                                      
REMARK 465     SER A   487                                                      
REMARK 465     PRO A   488                                                      
REMARK 465     ALA A   489                                                      
REMARK 465     ALA A   490                                                      
REMARK 465     PRO A   491                                                      
REMARK 465     ALA A   492                                                      
REMARK 465     SER A   493                                                      
REMARK 465     LEU A   494                                                      
REMARK 465     SER A   495                                                      
REMARK 465     ALA A   496                                                      
REMARK 465     PRO A   497                                                      
REMARK 465     GLU A   498                                                      
REMARK 465     PRO A   499                                                      
REMARK 465     ALA A   500                                                      
REMARK 465     SER A   501                                                      
REMARK 465     GLN A   502                                                      
REMARK 465     ALA A   503                                                      
REMARK 465     ARG A   504                                                      
REMARK 465     VAL A   505                                                      
REMARK 465     LEU A   506                                                      
REMARK 465     SER A   507                                                      
REMARK 465     SER A   508                                                      
REMARK 465     SER A   509                                                      
REMARK 465     GLU A   510                                                      
REMARK 465     THR A   511                                                      
REMARK 465     PRO A   512                                                      
REMARK 465     ALA A   513                                                      
REMARK 465     ARG A   514                                                      
REMARK 465     ARG A   611                                                      
REMARK 465     MET A   612                                                      
REMARK 465     PHE A   613                                                      
REMARK 465     LEU A   901                                                      
REMARK 465     ALA A   902                                                      
REMARK 465     SER A   903                                                      
REMARK 465     GLY B   481                                                      
REMARK 465     SER B   482                                                      
REMARK 465     ARG B   483                                                      
REMARK 465     ALA B   484                                                      
REMARK 465     GLN B   485                                                      
REMARK 465     SER B   486                                                      
REMARK 465     SER B   487                                                      
REMARK 465     PRO B   488                                                      
REMARK 465     ALA B   489                                                      
REMARK 465     ALA B   490                                                      
REMARK 465     PRO B   491                                                      
REMARK 465     ALA B   492                                                      
REMARK 465     SER B   493                                                      
REMARK 465     LEU B   494                                                      
REMARK 465     SER B   495                                                      
REMARK 465     ALA B   496                                                      
REMARK 465     PRO B   497                                                      
REMARK 465     GLU B   498                                                      
REMARK 465     PRO B   499                                                      
REMARK 465     ALA B   500                                                      
REMARK 465     SER B   501                                                      
REMARK 465     GLN B   502                                                      
REMARK 465     ALA B   503                                                      
REMARK 465     ARG B   504                                                      
REMARK 465     VAL B   505                                                      
REMARK 465     LEU B   506                                                      
REMARK 465     SER B   507                                                      
REMARK 465     SER B   508                                                      
REMARK 465     SER B   509                                                      
REMARK 465     GLU B   510                                                      
REMARK 465     THR B   511                                                      
REMARK 465     PRO B   512                                                      
REMARK 465     ALA B   513                                                      
REMARK 465     ARG B   514                                                      
REMARK 465     THR B   515                                                      
REMARK 465     ARG B   596                                                      
REMARK 465     LEU B   597                                                      
REMARK 465     LYS B   598                                                      
REMARK 465     LEU B   599                                                      
REMARK 465     ASP B   600                                                      
REMARK 465     ASN B   601                                                      
REMARK 465     GLY B   602                                                      
REMARK 465     LYS B   603                                                      
REMARK 465     LEU B   604                                                      
REMARK 465     ALA B   605                                                      
REMARK 465     GLY B   606                                                      
REMARK 465     LEU B   607                                                      
REMARK 465     LEU B   608                                                      
REMARK 465     ALA B   609                                                      
REMARK 465     GLN B   610                                                      
REMARK 465     ARG B   611                                                      
REMARK 465     MET B   612                                                      
REMARK 465     PHE B   613                                                      
REMARK 465     ALA B   902                                                      
REMARK 465     SER B   903                                                      
REMARK 465     GLY C   481                                                      
REMARK 465     SER C   482                                                      
REMARK 465     ARG C   483                                                      
REMARK 465     ALA C   484                                                      
REMARK 465     GLN C   485                                                      
REMARK 465     SER C   486                                                      
REMARK 465     SER C   487                                                      
REMARK 465     PRO C   488                                                      
REMARK 465     ALA C   489                                                      
REMARK 465     ALA C   490                                                      
REMARK 465     PRO C   491                                                      
REMARK 465     ALA C   492                                                      
REMARK 465     SER C   493                                                      
REMARK 465     LEU C   494                                                      
REMARK 465     SER C   495                                                      
REMARK 465     ALA C   496                                                      
REMARK 465     PRO C   497                                                      
REMARK 465     GLU C   498                                                      
REMARK 465     PRO C   499                                                      
REMARK 465     ALA C   500                                                      
REMARK 465     SER C   501                                                      
REMARK 465     GLN C   502                                                      
REMARK 465     ALA C   503                                                      
REMARK 465     ARG C   504                                                      
REMARK 465     VAL C   505                                                      
REMARK 465     LEU C   506                                                      
REMARK 465     SER C   507                                                      
REMARK 465     SER C   508                                                      
REMARK 465     SER C   509                                                      
REMARK 465     GLU C   510                                                      
REMARK 465     THR C   511                                                      
REMARK 465     PRO C   512                                                      
REMARK 465     ALA C   513                                                      
REMARK 465     ARG C   514                                                      
REMARK 465     THR C   515                                                      
REMARK 465     LEU C   516                                                      
REMARK 465     PRO C   517                                                      
REMARK 465     PHE C   518                                                      
REMARK 465     LEU C   594                                                      
REMARK 465     SER C   595                                                      
REMARK 465     ARG C   596                                                      
REMARK 465     LEU C   597                                                      
REMARK 465     LYS C   598                                                      
REMARK 465     LEU C   599                                                      
REMARK 465     ASP C   600                                                      
REMARK 465     ASN C   601                                                      
REMARK 465     GLY C   602                                                      
REMARK 465     LYS C   603                                                      
REMARK 465     LEU C   604                                                      
REMARK 465     ALA C   605                                                      
REMARK 465     GLY C   606                                                      
REMARK 465     LEU C   607                                                      
REMARK 465     LEU C   608                                                      
REMARK 465     ALA C   609                                                      
REMARK 465     GLN C   610                                                      
REMARK 465     ARG C   611                                                      
REMARK 465     MET C   612                                                      
REMARK 465     PHE C   613                                                      
REMARK 465     VAL C   614                                                      
REMARK 465     MET C   615                                                      
REMARK 465     ARG C   900                                                      
REMARK 465     LEU C   901                                                      
REMARK 465     ALA C   902                                                      
REMARK 465     SER C   903                                                      
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     ARG A 596    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     LYS A 598    CG   CD   CE   NZ                                   
REMARK 470     ARG A 655    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 658    CG   CD   CE   NZ                                   
REMARK 470     LYS A 818    CD   CE   NZ                                        
REMARK 470     ARG A 900    NE   CZ   NH1  NH2                                  
REMARK 470     LEU B 810    CG   CD1  CD2                                       
REMARK 470     LEU B 867    CG   CD1  CD2                                       
REMARK 470     GLU B 870    CB   CG   CD   OE1  OE2                             
REMARK 470     LYS C 697    CG   CD   CE   NZ                                   
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   SG   CYS A   566     O    HOH A   997              2.03            
REMARK 500   K    K   C   202     O    HOH C   905              2.08            
REMARK 500   OD1  ASP B   733     O    HOH B   982              2.09            
REMARK 500   O    THR A   519     N    LYS A   658              2.09            
REMARK 500   O    HOH B   954     O    HOH B   986              2.14            
REMARK 500   N    VAL B   614     O    HOH B  1009              2.15            
REMARK 500   O    VAL A   724     K    K   A   202              2.15            
REMARK 500   OD1  ASP A   721     OG   SER A   723              2.16            
REMARK 500   NH2  ARG B   568     O    HOH B   995              2.16            
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    ARG B 690   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A 596        4.26    -67.35                                   
REMARK 500    ARG A 655       14.14     80.20                                   
REMARK 500    PHE A 679       -0.28     79.85                                   
REMARK 500    SER A 790       74.24     61.74                                   
REMARK 500    ALA A 808      -68.99    -15.95                                   
REMARK 500    GLU A 840     -112.66   -118.85                                   
REMARK 500    PHE B 518       59.95    -59.07                                   
REMARK 500    THR B 519     -163.19   -120.94                                   
REMARK 500    HIS B 531       95.43    -63.86                                   
REMARK 500    PRO B 617      -30.06    -34.43                                   
REMARK 500    ASP B 624     -158.97   -144.34                                   
REMARK 500    PHE B 679       -1.03     73.28                                   
REMARK 500    ASP B 733       57.93     24.28                                   
REMARK 500    PRO B 809       56.85   -114.55                                   
REMARK 500    GLU B 840     -113.27   -115.66                                   
REMARK 500    SER B 868       20.19    -79.43                                   
REMARK 500    ASN C 592      -87.37    -72.73                                   
REMARK 500    THR C 625      -38.03    -39.94                                   
REMARK 500    ALA C 698      134.21   -176.11                                   
REMARK 500    VAL C 781      -60.09   -107.53                                   
REMARK 500    SER C 790       77.99     40.40                                   
REMARK 500    PRO C 809       62.59   -112.48                                   
REMARK 500    GLU C 840     -103.63   -112.63                                   
REMARK 500    HIS C 843      -15.22   -141.11                                   
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     ARG A 900        21.2      L          L   OUTSIDE RANGE          
REMARK 500     HIS B 843        24.8      L          L   OUTSIDE RANGE          
REMARK 500     HIS C 669        24.7      L          L   OUTSIDE RANGE          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     SHH A  301                                                       
REMARK 610     SHH B  301                                                       
REMARK 610     SHH C  301                                                       
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 102  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 533   SG                                                     
REMARK 620 2 CYS A 535   SG  109.9                                              
REMARK 620 3 HIS A 541   NE2 108.1 100.2                                        
REMARK 620 4 CYS A 618   SG   98.5 121.9 117.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 201   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 705   O                                                      
REMARK 620 2 ASP A 705   OD1  71.1                                              
REMARK 620 3 ASP A 707   O    98.5  96.6                                        
REMARK 620 4 HIS A 709   O   164.7  94.7  77.1                                  
REMARK 620 5 SER A 728   OG   82.7 109.8 152.2 108.2                            
REMARK 620 6 LEU A 729   O    74.9 139.8  67.8 115.7  86.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 101  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 707   OD1                                                    
REMARK 620 2 HIS A 709   ND1 107.4                                              
REMARK 620 3 ASP A 801   OD2 107.1  98.5                                        
REMARK 620 4 SHH A 301   O1   91.1  87.5 157.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 202   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE A 718   O                                                      
REMARK 620 2 ASP A 721   O    88.7                                              
REMARK 620 3 HOH A 915   O    84.4 159.9                                        
REMARK 620 4 HOH A 908   O    71.0 102.4  93.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 102  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 533   SG                                                     
REMARK 620 2 CYS B 535   SG  109.8                                              
REMARK 620 3 HIS B 541   NE2 113.2 101.5                                        
REMARK 620 4 CYS B 618   SG  113.2 108.9 109.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B 201   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 705   O                                                      
REMARK 620 2 ASP B 705   OD1  67.3                                              
REMARK 620 3 ASP B 707   O   102.4  94.0                                        
REMARK 620 4 HIS B 709   O   155.6  89.7  70.0                                  
REMARK 620 5 SER B 728   OG   87.8 112.1 153.8 109.2                            
REMARK 620 6 LEU B 729   O    77.9 136.1  67.6 117.5  91.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 101  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 707   OD1                                                    
REMARK 620 2 HIS B 709   ND1 104.3                                              
REMARK 620 3 ASP B 801   OD2 111.8 103.8                                        
REMARK 620 4 SHH B 301   O1   84.5 107.6 139.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B 202   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE B 718   O                                                      
REMARK 620 2 ASP B 721   O    97.1                                              
REMARK 620 3 VAL B 724   O   147.7  81.0                                        
REMARK 620 4 HOH B 906   O    86.5 158.8  84.8                                  
REMARK 620 5 HOH B 907   O    81.9 111.6 129.0  89.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 102  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 533   SG                                                     
REMARK 620 2 CYS C 535   SG  107.9                                              
REMARK 620 3 HIS C 541   NE2 102.5  93.0                                        
REMARK 620 4 CYS C 618   SG  104.7 127.2 118.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C 201   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 705   O                                                      
REMARK 620 2 ASP C 705   OD1  71.7                                              
REMARK 620 3 ASP C 707   O    98.0  99.7                                        
REMARK 620 4 HIS C 709   O   157.7  87.7  76.7                                  
REMARK 620 5 SER C 728   OG   86.9 111.4 148.4 109.1                            
REMARK 620 6 LEU C 729   O    81.4 145.7  62.8 113.7  87.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 101  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 707   OD1                                                    
REMARK 620 2 HIS C 709   ND1  99.5                                              
REMARK 620 3 ASP C 801   OD2 105.3  89.2                                        
REMARK 620 4 SHH C 301   O1   85.7 102.9 162.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C 202   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE C 718   O                                                      
REMARK 620 2 ASP C 721   O    88.5                                              
REMARK 620 3 VAL C 724   O   151.2  82.8                                        
REMARK 620 4 HOH C 913   O    76.2  85.2 129.9                                  
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 101                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 102                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 201                   
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 202                   
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 101                  
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 102                  
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 201                   
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 202                   
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 101                  
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 102                  
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 201                   
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 202                   
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SHH A 301                 
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SHH B 301                 
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SHH C 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2NVR   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF CATALYTIC DOMAIN OF HUMAN HISTONE               
REMARK 900 DEACETYLASE HDAC7                                                    
REMARK 900 RELATED ID: 3C0Y   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF CATALYTIC DOMAIN OF HUMAN HISTONE               
REMARK 900 DEACETYLASE HDAC7                                                    
REMARK 900 RELATED ID: 3C10   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF CATALYTIC DOMAIN OF HUMAN HISTONE               
REMARK 900 DEACETYLASE HDAC7 IN COMPLEX WITH TRICHOSTATIN A (TSA)               
DBREF  3C0Z A  482   903  UNP    Q8WUI4   HDAC7_HUMAN    482    903             
DBREF  3C0Z B  482   903  UNP    Q8WUI4   HDAC7_HUMAN    482    903             
DBREF  3C0Z C  482   903  UNP    Q8WUI4   HDAC7_HUMAN    482    903             
SEQADV 3C0Z GLY A  481  UNP  Q8WUI4              EXPRESSION TAG                 
SEQADV 3C0Z GLY B  481  UNP  Q8WUI4              EXPRESSION TAG                 
SEQADV 3C0Z GLY C  481  UNP  Q8WUI4              EXPRESSION TAG                 
SEQRES   1 A  423  GLY SER ARG ALA GLN SER SER PRO ALA ALA PRO ALA SER          
SEQRES   2 A  423  LEU SER ALA PRO GLU PRO ALA SER GLN ALA ARG VAL LEU          
SEQRES   3 A  423  SER SER SER GLU THR PRO ALA ARG THR LEU PRO PHE THR          
SEQRES   4 A  423  THR GLY LEU ILE TYR ASP SER VAL MET LEU LYS HIS GLN          
SEQRES   5 A  423  CYS SER CYS GLY ASP ASN SER ARG HIS PRO GLU HIS ALA          
SEQRES   6 A  423  GLY ARG ILE GLN SER ILE TRP SER ARG LEU GLN GLU ARG          
SEQRES   7 A  423  GLY LEU ARG SER GLN CYS GLU CYS LEU ARG GLY ARG LYS          
SEQRES   8 A  423  ALA SER LEU GLU GLU LEU GLN SER VAL HIS SER GLU ARG          
SEQRES   9 A  423  HIS VAL LEU LEU TYR GLY THR ASN PRO LEU SER ARG LEU          
SEQRES  10 A  423  LYS LEU ASP ASN GLY LYS LEU ALA GLY LEU LEU ALA GLN          
SEQRES  11 A  423  ARG MET PHE VAL MET LEU PRO CYS GLY GLY VAL GLY VAL          
SEQRES  12 A  423  ASP THR ASP THR ILE TRP ASN GLU LEU HIS SER SER ASN          
SEQRES  13 A  423  ALA ALA ARG TRP ALA ALA GLY SER VAL THR ASP LEU ALA          
SEQRES  14 A  423  PHE LYS VAL ALA SER ARG GLU LEU LYS ASN GLY PHE ALA          
SEQRES  15 A  423  VAL VAL ARG PRO PRO GLY HIS HIS ALA ASP HIS SER THR          
SEQRES  16 A  423  ALA MET GLY PHE CYS PHE PHE ASN SER VAL ALA ILE ALA          
SEQRES  17 A  423  CYS ARG GLN LEU GLN GLN GLN SER LYS ALA SER LYS ILE          
SEQRES  18 A  423  LEU ILE VAL ASP TRP ASP VAL HIS HIS GLY ASN GLY THR          
SEQRES  19 A  423  GLN GLN THR PHE TYR GLN ASP PRO SER VAL LEU TYR ILE          
SEQRES  20 A  423  SER LEU HIS ARG HIS ASP ASP GLY ASN PHE PHE PRO GLY          
SEQRES  21 A  423  SER GLY ALA VAL ASP GLU VAL GLY ALA GLY SER GLY GLU          
SEQRES  22 A  423  GLY PHE ASN VAL ASN VAL ALA TRP ALA GLY GLY LEU ASP          
SEQRES  23 A  423  PRO PRO MET GLY ASP PRO GLU TYR LEU ALA ALA PHE ARG          
SEQRES  24 A  423  ILE VAL VAL MET PRO ILE ALA ARG GLU PHE SER PRO ASP          
SEQRES  25 A  423  LEU VAL LEU VAL SER ALA GLY PHE ASP ALA ALA GLU GLY          
SEQRES  26 A  423  HIS PRO ALA PRO LEU GLY GLY TYR HIS VAL SER ALA LYS          
SEQRES  27 A  423  CYS PHE GLY TYR MET THR GLN GLN LEU MET ASN LEU ALA          
SEQRES  28 A  423  GLY GLY ALA VAL VAL LEU ALA LEU GLU GLY GLY HIS ASP          
SEQRES  29 A  423  LEU THR ALA ILE CYS ASP ALA SER GLU ALA CYS VAL ALA          
SEQRES  30 A  423  ALA LEU LEU GLY ASN ARG VAL ASP PRO LEU SER GLU GLU          
SEQRES  31 A  423  GLY TRP LYS GLN LYS PRO ASN LEU ASN ALA ILE ARG SER          
SEQRES  32 A  423  LEU GLU ALA VAL ILE ARG VAL HIS SER LYS TYR TRP GLY          
SEQRES  33 A  423  CYS MET GLN ARG LEU ALA SER                                  
SEQRES   1 B  423  GLY SER ARG ALA GLN SER SER PRO ALA ALA PRO ALA SER          
SEQRES   2 B  423  LEU SER ALA PRO GLU PRO ALA SER GLN ALA ARG VAL LEU          
SEQRES   3 B  423  SER SER SER GLU THR PRO ALA ARG THR LEU PRO PHE THR          
SEQRES   4 B  423  THR GLY LEU ILE TYR ASP SER VAL MET LEU LYS HIS GLN          
SEQRES   5 B  423  CYS SER CYS GLY ASP ASN SER ARG HIS PRO GLU HIS ALA          
SEQRES   6 B  423  GLY ARG ILE GLN SER ILE TRP SER ARG LEU GLN GLU ARG          
SEQRES   7 B  423  GLY LEU ARG SER GLN CYS GLU CYS LEU ARG GLY ARG LYS          
SEQRES   8 B  423  ALA SER LEU GLU GLU LEU GLN SER VAL HIS SER GLU ARG          
SEQRES   9 B  423  HIS VAL LEU LEU TYR GLY THR ASN PRO LEU SER ARG LEU          
SEQRES  10 B  423  LYS LEU ASP ASN GLY LYS LEU ALA GLY LEU LEU ALA GLN          
SEQRES  11 B  423  ARG MET PHE VAL MET LEU PRO CYS GLY GLY VAL GLY VAL          
SEQRES  12 B  423  ASP THR ASP THR ILE TRP ASN GLU LEU HIS SER SER ASN          
SEQRES  13 B  423  ALA ALA ARG TRP ALA ALA GLY SER VAL THR ASP LEU ALA          
SEQRES  14 B  423  PHE LYS VAL ALA SER ARG GLU LEU LYS ASN GLY PHE ALA          
SEQRES  15 B  423  VAL VAL ARG PRO PRO GLY HIS HIS ALA ASP HIS SER THR          
SEQRES  16 B  423  ALA MET GLY PHE CYS PHE PHE ASN SER VAL ALA ILE ALA          
SEQRES  17 B  423  CYS ARG GLN LEU GLN GLN GLN SER LYS ALA SER LYS ILE          
SEQRES  18 B  423  LEU ILE VAL ASP TRP ASP VAL HIS HIS GLY ASN GLY THR          
SEQRES  19 B  423  GLN GLN THR PHE TYR GLN ASP PRO SER VAL LEU TYR ILE          
SEQRES  20 B  423  SER LEU HIS ARG HIS ASP ASP GLY ASN PHE PHE PRO GLY          
SEQRES  21 B  423  SER GLY ALA VAL ASP GLU VAL GLY ALA GLY SER GLY GLU          
SEQRES  22 B  423  GLY PHE ASN VAL ASN VAL ALA TRP ALA GLY GLY LEU ASP          
SEQRES  23 B  423  PRO PRO MET GLY ASP PRO GLU TYR LEU ALA ALA PHE ARG          
SEQRES  24 B  423  ILE VAL VAL MET PRO ILE ALA ARG GLU PHE SER PRO ASP          
SEQRES  25 B  423  LEU VAL LEU VAL SER ALA GLY PHE ASP ALA ALA GLU GLY          
SEQRES  26 B  423  HIS PRO ALA PRO LEU GLY GLY TYR HIS VAL SER ALA LYS          
SEQRES  27 B  423  CYS PHE GLY TYR MET THR GLN GLN LEU MET ASN LEU ALA          
SEQRES  28 B  423  GLY GLY ALA VAL VAL LEU ALA LEU GLU GLY GLY HIS ASP          
SEQRES  29 B  423  LEU THR ALA ILE CYS ASP ALA SER GLU ALA CYS VAL ALA          
SEQRES  30 B  423  ALA LEU LEU GLY ASN ARG VAL ASP PRO LEU SER GLU GLU          
SEQRES  31 B  423  GLY TRP LYS GLN LYS PRO ASN LEU ASN ALA ILE ARG SER          
SEQRES  32 B  423  LEU GLU ALA VAL ILE ARG VAL HIS SER LYS TYR TRP GLY          
SEQRES  33 B  423  CYS MET GLN ARG LEU ALA SER                                  
SEQRES   1 C  423  GLY SER ARG ALA GLN SER SER PRO ALA ALA PRO ALA SER          
SEQRES   2 C  423  LEU SER ALA PRO GLU PRO ALA SER GLN ALA ARG VAL LEU          
SEQRES   3 C  423  SER SER SER GLU THR PRO ALA ARG THR LEU PRO PHE THR          
SEQRES   4 C  423  THR GLY LEU ILE TYR ASP SER VAL MET LEU LYS HIS GLN          
SEQRES   5 C  423  CYS SER CYS GLY ASP ASN SER ARG HIS PRO GLU HIS ALA          
SEQRES   6 C  423  GLY ARG ILE GLN SER ILE TRP SER ARG LEU GLN GLU ARG          
SEQRES   7 C  423  GLY LEU ARG SER GLN CYS GLU CYS LEU ARG GLY ARG LYS          
SEQRES   8 C  423  ALA SER LEU GLU GLU LEU GLN SER VAL HIS SER GLU ARG          
SEQRES   9 C  423  HIS VAL LEU LEU TYR GLY THR ASN PRO LEU SER ARG LEU          
SEQRES  10 C  423  LYS LEU ASP ASN GLY LYS LEU ALA GLY LEU LEU ALA GLN          
SEQRES  11 C  423  ARG MET PHE VAL MET LEU PRO CYS GLY GLY VAL GLY VAL          
SEQRES  12 C  423  ASP THR ASP THR ILE TRP ASN GLU LEU HIS SER SER ASN          
SEQRES  13 C  423  ALA ALA ARG TRP ALA ALA GLY SER VAL THR ASP LEU ALA          
SEQRES  14 C  423  PHE LYS VAL ALA SER ARG GLU LEU LYS ASN GLY PHE ALA          
SEQRES  15 C  423  VAL VAL ARG PRO PRO GLY HIS HIS ALA ASP HIS SER THR          
SEQRES  16 C  423  ALA MET GLY PHE CYS PHE PHE ASN SER VAL ALA ILE ALA          
SEQRES  17 C  423  CYS ARG GLN LEU GLN GLN GLN SER LYS ALA SER LYS ILE          
SEQRES  18 C  423  LEU ILE VAL ASP TRP ASP VAL HIS HIS GLY ASN GLY THR          
SEQRES  19 C  423  GLN GLN THR PHE TYR GLN ASP PRO SER VAL LEU TYR ILE          
SEQRES  20 C  423  SER LEU HIS ARG HIS ASP ASP GLY ASN PHE PHE PRO GLY          
SEQRES  21 C  423  SER GLY ALA VAL ASP GLU VAL GLY ALA GLY SER GLY GLU          
SEQRES  22 C  423  GLY PHE ASN VAL ASN VAL ALA TRP ALA GLY GLY LEU ASP          
SEQRES  23 C  423  PRO PRO MET GLY ASP PRO GLU TYR LEU ALA ALA PHE ARG          
SEQRES  24 C  423  ILE VAL VAL MET PRO ILE ALA ARG GLU PHE SER PRO ASP          
SEQRES  25 C  423  LEU VAL LEU VAL SER ALA GLY PHE ASP ALA ALA GLU GLY          
SEQRES  26 C  423  HIS PRO ALA PRO LEU GLY GLY TYR HIS VAL SER ALA LYS          
SEQRES  27 C  423  CYS PHE GLY TYR MET THR GLN GLN LEU MET ASN LEU ALA          
SEQRES  28 C  423  GLY GLY ALA VAL VAL LEU ALA LEU GLU GLY GLY HIS ASP          
SEQRES  29 C  423  LEU THR ALA ILE CYS ASP ALA SER GLU ALA CYS VAL ALA          
SEQRES  30 C  423  ALA LEU LEU GLY ASN ARG VAL ASP PRO LEU SER GLU GLU          
SEQRES  31 C  423  GLY TRP LYS GLN LYS PRO ASN LEU ASN ALA ILE ARG SER          
SEQRES  32 C  423  LEU GLU ALA VAL ILE ARG VAL HIS SER LYS TYR TRP GLY          
SEQRES  33 C  423  CYS MET GLN ARG LEU ALA SER                                  
HET     ZN  A 101       1                                                       
HET     ZN  A 102       1                                                       
HET      K  A 201       1                                                       
HET      K  A 202       1                                                       
HET     ZN  B 101       1                                                       
HET     ZN  B 102       1                                                       
HET      K  B 201       1                                                       
HET      K  B 202       1                                                       
HET     ZN  C 101       1                                                       
HET     ZN  C 102       1                                                       
HET      K  C 201       1                                                       
HET      K  C 202       1                                                       
HET    SHH  A 301       8                                                       
HET    SHH  B 301       9                                                       
HET    SHH  C 301       8                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM       K POTASSIUM ION                                                    
HETNAM     SHH OCTANEDIOIC ACID HYDROXYAMIDE PHENYLAMIDE                        
HETSYN     SHH SAHA                                                             
FORMUL   4   ZN    6(ZN 2+)                                                     
FORMUL   6    K    6(K 1+)                                                      
FORMUL  16  SHH    3(C14 H20 N2 O3)                                             
FORMUL  19  HOH   *332(H2 O)                                                    
HELIX    1   1 ASP A  525  HIS A  531  5                                   7    
HELIX    2   2 ASP A  537  HIS A  541  5                                   5    
HELIX    3   3 ALA A  545  ARG A  558  1                                  14    
HELIX    4   4 LEU A  560  CYS A  564  5                                   5    
HELIX    5   5 SER A  573  GLN A  578  1                                   6    
HELIX    6   6 SER A  582  THR A  591  1                                  10    
HELIX    7   7 ASP A  600  GLN A  610  1                                  11    
HELIX    8   8 HIS A  633  SER A  654  1                                  22    
HELIX    9   9 ASN A  683  SER A  696  1                                  14    
HELIX   10  10 GLY A  711  TYR A  719  1                                   9    
HELIX   11  11 ALA A  749  GLU A  753  5                                   5    
HELIX   12  12 GLY A  770  VAL A  781  1                                  12    
HELIX   13  13 VAL A  781  SER A  790  1                                  10    
HELIX   14  14 PRO A  807  GLY A  811  5                                   5    
HELIX   15  15 SER A  816  MET A  828  1                                  13    
HELIX   16  16 ASN A  829  GLY A  833  5                                   5    
HELIX   17  17 ASP A  844  GLY A  861  1                                  18    
HELIX   18  18 ASP A  865  LYS A  873  5                                   9    
HELIX   19  19 ASN A  877  SER A  892  1                                  16    
HELIX   20  20 LYS A  893  TYR A  894  5                                   2    
HELIX   21  21 TRP A  895  GLN A  899  5                                   5    
HELIX   22  22 ASP B  525  HIS B  531  5                                   7    
HELIX   23  23 ALA B  545  ARG B  558  1                                  14    
HELIX   24  24 LEU B  560  CYS B  564  5                                   5    
HELIX   25  25 SER B  573  SER B  579  1                                   7    
HELIX   26  26 SER B  582  THR B  591  1                                  10    
HELIX   27  27 HIS B  633  SER B  654  1                                  22    
HELIX   28  28 ASN B  683  GLN B  695  1                                  13    
HELIX   29  29 GLY B  711  TYR B  719  1                                   9    
HELIX   30  30 ALA B  749  GLU B  753  5                                   5    
HELIX   31  31 GLY B  770  VAL B  781  1                                  12    
HELIX   32  32 VAL B  781  SER B  790  1                                  10    
HELIX   33  33 SER B  816  MET B  828  1                                  13    
HELIX   34  34 ASN B  829  GLY B  833  5                                   5    
HELIX   35  35 ASP B  844  LEU B  860  1                                  17    
HELIX   36  36 ASN B  877  SER B  892  1                                  16    
HELIX   37  37 LYS B  893  TYR B  894  5                                   2    
HELIX   38  38 TRP B  895  GLN B  899  5                                   5    
HELIX   39  39 ASP C  525  HIS C  531  5                                   7    
HELIX   40  40 ALA C  545  ARG C  558  1                                  14    
HELIX   41  41 LEU C  560  CYS C  564  5                                   5    
HELIX   42  42 SER C  573  SER C  579  1                                   7    
HELIX   43  43 SER C  582  THR C  591  1                                  10    
HELIX   44  44 HIS C  633  SER C  654  1                                  22    
HELIX   45  45 ASN C  683  GLN C  695  1                                  13    
HELIX   46  46 GLY C  711  TYR C  719  1                                   9    
HELIX   47  47 ASP C  733  ASN C  736  5                                   4    
HELIX   48  48 ALA C  749  GLU C  753  5                                   5    
HELIX   49  49 GLY C  770  VAL C  781  1                                  12    
HELIX   50  50 VAL C  781  SER C  790  1                                  10    
HELIX   51  51 SER C  816  ASN C  829  1                                  14    
HELIX   52  52 LEU C  830  GLY C  833  5                                   4    
HELIX   53  53 ASP C  844  LEU C  860  1                                  17    
HELIX   54  54 ASP C  865  LYS C  873  5                                   9    
HELIX   55  55 ASN C  877  SER C  892  1                                  16    
HELIX   56  56 LYS C  893  TYR C  894  5                                   2    
HELIX   57  57 TRP C  895  GLN C  899  5                                   5    
SHEET    1   A 8 GLU A 565  LEU A 567  0                                        
SHEET    2   A 8 THR A 520  ILE A 523  1  N  LEU A 522   O  LEU A 567           
SHEET    3   A 8 ASN A 659  ALA A 662  1  O  PHE A 661   N  GLY A 521           
SHEET    4   A 8 VAL A 835  LEU A 839  1  O  LEU A 837   N  ALA A 662           
SHEET    5   A 8 LEU A 793  ALA A 798  1  N  VAL A 796   O  VAL A 836           
SHEET    6   A 8 ILE A 701  ASP A 705  1  N  VAL A 704   O  SER A 797           
SHEET    7   A 8 VAL A 724  ARG A 731  1  O  LEU A 725   N  ILE A 703           
SHEET    8   A 8 ASN A 756  TRP A 761  1  O  VAL A 757   N  TYR A 726           
SHEET    1   B 8 GLU B 565  LEU B 567  0                                        
SHEET    2   B 8 THR B 520  ILE B 523  1  N  LEU B 522   O  LEU B 567           
SHEET    3   B 8 ASN B 659  ALA B 662  1  O  PHE B 661   N  GLY B 521           
SHEET    4   B 8 VAL B 835  LEU B 839  1  O  LEU B 839   N  ALA B 662           
SHEET    5   B 8 LEU B 793  ALA B 798  1  N  VAL B 796   O  VAL B 836           
SHEET    6   B 8 ILE B 701  ASP B 705  1  N  VAL B 704   O  SER B 797           
SHEET    7   B 8 VAL B 724  ARG B 731  1  O  LEU B 725   N  ILE B 703           
SHEET    8   B 8 ASN B 756  TRP B 761  1  O  VAL B 759   N  SER B 728           
SHEET    1   C 8 GLU C 565  LEU C 567  0                                        
SHEET    2   C 8 THR C 520  ILE C 523  1  N  LEU C 522   O  LEU C 567           
SHEET    3   C 8 ASN C 659  ALA C 662  1  O  PHE C 661   N  ILE C 523           
SHEET    4   C 8 VAL C 835  LEU C 839  1  O  LEU C 837   N  ALA C 662           
SHEET    5   C 8 LEU C 793  ALA C 798  1  N  VAL C 796   O  VAL C 836           
SHEET    6   C 8 ILE C 701  ASP C 705  1  N  LEU C 702   O  LEU C 795           
SHEET    7   C 8 VAL C 724  ARG C 731  1  O  LEU C 725   N  ILE C 703           
SHEET    8   C 8 ASN C 756  TRP C 761  1  O  VAL C 757   N  TYR C 726           
LINK         SG  CYS A 533                ZN    ZN A 102     1555   1555  2.40  
LINK         SG  CYS A 535                ZN    ZN A 102     1555   1555  2.29  
LINK         NE2 HIS A 541                ZN    ZN A 102     1555   1555  1.98  
LINK         SG  CYS A 618                ZN    ZN A 102     1555   1555  2.21  
LINK         O   ASP A 705                 K     K A 201     1555   1555  2.88  
LINK         OD1 ASP A 705                 K     K A 201     1555   1555  2.72  
LINK         O   ASP A 707                 K     K A 201     1555   1555  2.54  
LINK         OD1 ASP A 707                ZN    ZN A 101     1555   1555  2.05  
LINK         O   HIS A 709                 K     K A 201     1555   1555  2.65  
LINK         ND1 HIS A 709                ZN    ZN A 101     1555   1555  2.03  
LINK         O   PHE A 718                 K     K A 202     1555   1555  2.69  
LINK         O   ASP A 721                 K     K A 202     1555   1555  2.56  
LINK         OG  SER A 728                 K     K A 201     1555   1555  2.76  
LINK         O   LEU A 729                 K     K A 201     1555   1555  2.75  
LINK         OD2 ASP A 801                ZN    ZN A 101     1555   1555  2.04  
LINK         SG  CYS B 533                ZN    ZN B 102     1555   1555  2.28  
LINK         SG  CYS B 535                ZN    ZN B 102     1555   1555  2.40  
LINK         NE2 HIS B 541                ZN    ZN B 102     1555   1555  2.06  
LINK         SG  CYS B 618                ZN    ZN B 102     1555   1555  2.44  
LINK         O   ASP B 705                 K     K B 201     1555   1555  2.65  
LINK         OD1 ASP B 705                 K     K B 201     1555   1555  2.68  
LINK         O   ASP B 707                 K     K B 201     1555   1555  2.54  
LINK         OD1 ASP B 707                ZN    ZN B 101     1555   1555  2.04  
LINK         O   HIS B 709                 K     K B 201     1555   1555  2.69  
LINK         ND1 HIS B 709                ZN    ZN B 101     1555   1555  2.03  
LINK         O   PHE B 718                 K     K B 202     1555   1555  2.55  
LINK         O   ASP B 721                 K     K B 202     1555   1555  2.43  
LINK         O   VAL B 724                 K     K B 202     1555   1555  2.50  
LINK         OG  SER B 728                 K     K B 201     1555   1555  2.61  
LINK         O   LEU B 729                 K     K B 201     1555   1555  2.71  
LINK         OD2 ASP B 801                ZN    ZN B 101     1555   1555  2.01  
LINK         SG  CYS C 533                ZN    ZN C 102     1555   1555  2.51  
LINK         SG  CYS C 535                ZN    ZN C 102     1555   1555  2.31  
LINK         NE2 HIS C 541                ZN    ZN C 102     1555   1555  2.08  
LINK         SG  CYS C 618                ZN    ZN C 102     1555   1555  2.14  
LINK         O   ASP C 705                 K     K C 201     1555   1555  2.68  
LINK         OD1 ASP C 705                 K     K C 201     1555   1555  2.59  
LINK         O   ASP C 707                 K     K C 201     1555   1555  2.60  
LINK         OD1 ASP C 707                ZN    ZN C 101     1555   1555  2.05  
LINK         O   HIS C 709                 K     K C 201     1555   1555  2.68  
LINK         ND1 HIS C 709                ZN    ZN C 101     1555   1555  2.09  
LINK         O   PHE C 718                 K     K C 202     1555   1555  2.52  
LINK         O   ASP C 721                 K     K C 202     1555   1555  2.55  
LINK         O   VAL C 724                 K     K C 202     1555   1555  2.48  
LINK         OG  SER C 728                 K     K C 201     1555   1555  2.61  
LINK         O   LEU C 729                 K     K C 201     1555   1555  2.63  
LINK         OD2 ASP C 801                ZN    ZN C 101     1555   1555  1.94  
LINK        ZN    ZN A 101                 O1  SHH A 301     1555   1555  2.07  
LINK        ZN    ZN B 101                 O1  SHH B 301     1555   1555  2.33  
LINK        ZN    ZN C 101                 O1  SHH C 301     1555   1555  1.98  
LINK         K     K A 202                 O   HOH A 915     1555   1555  2.36  
LINK         K     K A 202                 O   HOH A 908     1555   1555  2.56  
LINK         K     K B 202                 O   HOH B 906     1555   1555  2.50  
LINK         K     K B 202                 O   HOH B 907     1555   1555  2.48  
LINK         K     K C 202                 O   HOH C 913     1555   1555  2.53  
CISPEP   1 PRO A  593    LEU A  594          0         7.68                     
CISPEP   2 ARG A  665    PRO A  666          0        -1.70                     
CISPEP   3 PHE A  738    PRO A  739          0        -2.33                     
CISPEP   4 ASP A  766    PRO A  767          0         2.32                     
CISPEP   5 ARG B  665    PRO B  666          0        -1.48                     
CISPEP   6 PHE B  738    PRO B  739          0        -1.07                     
CISPEP   7 ASP B  766    PRO B  767          0         5.62                     
CISPEP   8 ALA B  808    PRO B  809          0        -4.57                     
CISPEP   9 ASN C  592    PRO C  593          0       -20.40                     
CISPEP  10 ARG C  665    PRO C  666          0        -2.56                     
CISPEP  11 PHE C  738    PRO C  739          0        -1.74                     
CISPEP  12 ASP C  766    PRO C  767          0         8.35                     
CISPEP  13 ALA C  808    PRO C  809          0        10.99                     
SITE     1 AC1  4 SHH A 301  ASP A 707  HIS A 709  ASP A 801                    
SITE     1 AC2  4 CYS A 533  CYS A 535  HIS A 541  CYS A 618                    
SITE     1 AC3  5 ASP A 705  ASP A 707  HIS A 709  SER A 728                    
SITE     2 AC3  5 LEU A 729                                                     
SITE     1 AC4  6 PHE A 718  ASP A 721  VAL A 724  PHE A 755                    
SITE     2 AC4  6 HOH A 908  HOH A 915                                          
SITE     1 AC5  4 SHH B 301  ASP B 707  HIS B 709  ASP B 801                    
SITE     1 AC6  4 CYS B 533  CYS B 535  HIS B 541  CYS B 618                    
SITE     1 AC7  5 ASP B 705  ASP B 707  HIS B 709  SER B 728                    
SITE     2 AC7  5 LEU B 729                                                     
SITE     1 AC8  5 PHE B 718  ASP B 721  VAL B 724  HOH B 906                    
SITE     2 AC8  5 HOH B 907                                                     
SITE     1 AC9  4 SHH C 301  ASP C 707  HIS C 709  ASP C 801                    
SITE     1 BC1  4 CYS C 533  CYS C 535  HIS C 541  CYS C 618                    
SITE     1 BC2  5 ASP C 705  ASP C 707  HIS C 709  SER C 728                    
SITE     2 BC2  5 LEU C 729                                                     
SITE     1 BC3  6 PHE C 718  ASP C 721  VAL C 724  PHE C 755                    
SITE     2 BC3  6 HOH C 905  HOH C 913                                          
SITE     1 BC4  9  ZN A 101  HIS A 669  HIS A 670  GLY A 678                    
SITE     2 BC4  9 ASP A 707  HIS A 709  PHE A 738  ASP A 801                    
SITE     3 BC4  9 HOH A1010                                                     
SITE     1 BC5  9  ZN B 101  HIS B 669  HIS B 670  GLY B 678                    
SITE     2 BC5  9 PHE B 679  ASP B 707  HIS B 709  ASP B 801                    
SITE     3 BC5  9 HOH B 986                                                     
SITE     1 BC6  9  ZN C 101  HIS C 669  HIS C 670  PHE C 679                    
SITE     2 BC6  9 ASP C 707  HIS C 709  PHE C 738  ASP C 801                    
SITE     3 BC6  9 HOH C 966                                                     
CRYST1   81.825   81.825  148.867  90.00  90.00 120.00 P 32          9          
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      0.012221  0.007056  0.000000        0.00000                         
SCALE2      0.000000  0.014112  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006717        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system