GenomeNet

Database: PDB
Entry: 3GV4
LinkDB: 3GV4
Original site: 3GV4 
HEADER    HYDROLASE                               30-MAR-09   3GV4              
TITLE     CRYSTAL STRUCTURE OF HUMAN HDAC6 ZINC FINGER DOMAIN AND UBIQUITIN C-  
TITLE    2 TERMINAL PEPTIDE RLRGG                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE DEACETYLASE 6;                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 1109-1215;                                    
COMPND   5 SYNONYM: HD6;                                                        
COMPND   6 EC: 3.5.1.98;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: UBIQUITIN C-TERMINAL PEPTIDE RLRGG;                        
COMPND  10 CHAIN: H;                                                            
COMPND  11 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: HDAC6, KIAA0901, JM21;                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: P28A-LIC;                                 
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 OTHER_DETAILS: UBIQUITIN C-TERMINAL PEPTIDE                          
KEYWDS    HDAC6, ZINC FINGER, UBIQUITIN C-TERMINAL PEPTIDE RLRGG, SGC, ACTIN-   
KEYWDS   2 BINDING, CHROMATIN REGULATOR, CYTOPLASM, HYDROLASE, METAL-BINDING,   
KEYWDS   3 NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, REPRESSOR, TRANSCRIPTION,     
KEYWDS   4 TRANSCRIPTION REGULATION, UBL CONJUGATION, ZINC, ZINC-FINGER,        
KEYWDS   5 STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.DONG,M.RAVICHANDRAN,P.LOPPNAU,Y.LI,F.MACKENZIE,I.KOZIERADZKI,       
AUTHOR   2 A.M.EDWARDS,C.H.ARROWSMITH,J.WEIGELT,C.BOUNTRA,A.BOCHKAREV,S.DHE-    
AUTHOR   3 PAGANON,J.MIN,H.OUYANG,STRUCTURAL GENOMICS CONSORTIUM (SGC)          
REVDAT   2   01-NOV-17 3GV4    1       REMARK                                   
REVDAT   1   28-APR-09 3GV4    0                                                
JRNL        AUTH   A.DONG,M.RAVICHANDRAN,P.LOPPNAU,Y.LI,F.MACKENZIE,            
JRNL        AUTH 2 I.KOZIERADZKI,A.M.EDWARDS,C.H.ARROWSMITH,J.WEIGELT,          
JRNL        AUTH 3 C.BOUNTRA,A.BOCHKAREV,S.DHE-PAGANON,J.MIN,H.OUYANG           
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN HDAC6 ZINC FINGER DOMAIN AND      
JRNL        TITL 2 UBIQUITIN C-TERMINAL PEPTIDE RLRGG                           
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.72 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) : 1.72                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.45                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 10213                          
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) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 609                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.72                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.76                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 523                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 67.68                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3780                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 34                           
REMARK   3   BIN FREE R VALUE                    : 0.4770                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 799                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 205                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.96                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : -1.31000                                             
REMARK   3    B33 (A**2) : 1.30000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
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): 0.125         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.129         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.082         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.510         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.938                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):   825 ; 0.010 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1128 ; 1.191 ; 1.921       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   101 ; 5.813 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    36 ;36.527 ;23.889       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   116 ;11.322 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     2 ;16.224 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   120 ; 0.093 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   640 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   438 ; 0.193 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   551 ; 0.303 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   121 ; 0.153 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     3 ; 0.037 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    33 ; 0.208 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    26 ; 0.162 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):     1 ; 0.039 ; 0.200       
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):   520 ; 0.612 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   821 ; 1.020 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   355 ; 1.595 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   307 ; 2.470 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3GV4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAR-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000052344.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-APR-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E SUPERBRIGHT            
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : VARIMAX HR                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10865                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.720                              
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     (%) : 94.5                               
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : 0.07300                            
REMARK 200  R SYM                      (I) : 0.07300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.72                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.78                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 72.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.23100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.23100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.260                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASES                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3C5K                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 0.2 M NACL, VAPOR           
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 297K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       15.82850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       44.49900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       18.04650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       44.49900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       15.82850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       18.04650            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 680 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 5500 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   100                                                      
REMARK 465     GLU A   101                                                      
REMARK 465     ASP A   102                                                      
REMARK 465     MET A   103                                                      
REMARK 465     PRO A   104                                                      
REMARK 465     HIS A   105                                                      
REMARK 465     PRO A   106                                                      
REMARK 465     HIS A   107                                                      
REMARK 465     ARG H    72                                                      
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     GLN A  96    OE1  NE2                                            
REMARK 470     PHE A  99    CD1  CD2  CE1  CE2  CZ                              
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   O    HOH A   241     O    HOH A   297              2.07            
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    ILE A  49     -100.30   -102.57                                   
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 203  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A   5   SG                                                     
REMARK 620 2 HIS A   7   ND1 111.4                                              
REMARK 620 3 CYS A  75   SG  116.8  97.4                                        
REMARK 620 4 CYS A  78   SG  113.1 100.7 114.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  25   SG                                                     
REMARK 620 2 CYS A  28   SG  110.8                                              
REMARK 620 3 CYS A  45   SG  112.0 114.8                                        
REMARK 620 4 HIS A  52   ND1 105.7 112.0 100.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  37   SG                                                     
REMARK 620 2 CYS A  40   SG  113.7                                              
REMARK 620 3 HIS A  56   NE2 111.9  97.5                                        
REMARK 620 4 HIS A  62   ND1 107.2 117.1 109.1                                  
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 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 300                  
DBREF  3GV4 A    1   107  UNP    Q9UBN7   HDAC6_HUMAN   1109   1215             
DBREF  3GV4 H   72    76  PDB    3GV4     3GV4            72     76             
SEQRES   1 A  107  PRO LEU PRO TRP CYS PRO HIS LEU VAL ALA VAL CYS PRO          
SEQRES   2 A  107  ILE PRO ALA ALA GLY LEU ASP VAL THR GLN PRO CYS GLY          
SEQRES   3 A  107  ASP CYS GLY THR ILE GLN GLU ASN TRP VAL CYS LEU SER          
SEQRES   4 A  107  CYS TYR GLN VAL TYR CYS GLY ARG TYR ILE ASN GLY HIS          
SEQRES   5 A  107  MET LEU GLN HIS HIS GLY ASN SER GLY HIS PRO LEU VAL          
SEQRES   6 A  107  LEU SER TYR ILE ASP LEU SER ALA TRP CYS TYR TYR CYS          
SEQRES   7 A  107  GLN ALA TYR VAL HIS HIS GLN ALA LEU LEU ASP VAL LYS          
SEQRES   8 A  107  ASN ILE ALA HIS GLN ASN LYS PHE GLY GLU ASP MET PRO          
SEQRES   9 A  107  HIS PRO HIS                                                  
SEQRES   1 H    5  ARG LEU ARG GLY GLY                                          
HET     ZN  A 201       1                                                       
HET     ZN  A 202       1                                                       
HET     ZN  A 203       1                                                       
HET     CA  A 300       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CA CALCIUM ION                                                      
FORMUL   3   ZN    3(ZN 2+)                                                     
FORMUL   6   CA    CA 2+                                                        
FORMUL   7  HOH   *205(H2 O)                                                    
HELIX    1   1 HIS A    7  VAL A   11  5                                   5    
HELIX    2   2 GLY A   51  GLY A   61  1                                  11    
HELIX    3   3 HIS A   84  ALA A   86  5                                   3    
HELIX    4   4 LEU A   87  PHE A   99  1                                  13    
SHEET    1   A 5 VAL A  43  CYS A  45  0                                        
SHEET    2   A 5 ASN A  34  CYS A  37 -1  N  TRP A  35   O  TYR A  44           
SHEET    3   A 5 LEU A  64  SER A  67 -1  O  LEU A  66   N  VAL A  36           
SHEET    4   A 5 ALA A  73  CYS A  75 -1  O  TRP A  74   N  VAL A  65           
SHEET    5   A 5 ALA A  80  TYR A  81 -1  O  ALA A  80   N  CYS A  75           
LINK         SG  CYS A   5                ZN    ZN A 203     1555   1555  2.35  
LINK         ND1 HIS A   7                ZN    ZN A 203     1555   1555  2.14  
LINK         SG  CYS A  25                ZN    ZN A 202     1555   1555  2.37  
LINK         SG  CYS A  28                ZN    ZN A 202     1555   1555  2.34  
LINK         SG  CYS A  37                ZN    ZN A 201     1555   1555  2.35  
LINK         SG  CYS A  40                ZN    ZN A 201     1555   1555  2.27  
LINK         SG  CYS A  45                ZN    ZN A 202     1555   1555  2.39  
LINK         ND1 HIS A  52                ZN    ZN A 202     1555   1555  2.02  
LINK         NE2 HIS A  56                ZN    ZN A 201     1555   1555  2.04  
LINK         ND1 HIS A  62                ZN    ZN A 201     1555   1555  2.11  
LINK         SG  CYS A  75                ZN    ZN A 203     1555   1555  2.35  
LINK         SG  CYS A  78                ZN    ZN A 203     1555   1555  2.27  
SITE     1 AC1  4 CYS A  37  CYS A  40  HIS A  56  HIS A  62                    
SITE     1 AC2  4 CYS A  25  CYS A  28  CYS A  45  HIS A  52                    
SITE     1 AC3  4 CYS A   5  HIS A   7  CYS A  75  CYS A  78                    
SITE     1 AC4  7 ALA A  17  GLY A  26  HOH A 205  HOH A 212                    
SITE     2 AC4  7 HOH A 225  HOH A 228  HOH A 282                               
CRYST1   31.657   36.093   88.998  90.00  90.00  90.00 P 21 21 21    4          
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      0.031589  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.027706  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011236        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system