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Database: PDB
Entry: 3C5K
LinkDB: 3C5K
Original site: 3C5K 
HEADER    HYDROLASE                               31-JAN-08   3C5K              
TITLE     CRYSTAL STRUCTURE OF HUMAN HDAC6 ZINC FINGER DOMAIN                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE DEACETYLASE 6;                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 1109-1215;                                        
COMPND   5 SYNONYM: HD6;                                                        
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: HDAC6;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 ROSETTA-R3;                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET15-MHL                                 
KEYWDS    HDAC6, ZINC FINGER, ACTIN-BINDING, CHROMATIN REGULATOR,               
KEYWDS   2 CYTOPLASM, HYDROLASE, METAL-BINDING, NUCLEUS,                        
KEYWDS   3 PHOSPHOPROTEIN, REPRESSOR, TRANSCRIPTION, TRANSCRIPTION              
KEYWDS   4 REGULATION, UBL CONJUGATION, ZINC-FINGER, STRUCTURAL                 
KEYWDS   5 GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.DONG,M.RAVICHANDRAN,A.SCHUETZ,P.LOPPNAU,Y.LI,F.MACKENZIE,           
AUTHOR   2 I.KOZIERADZKI,A.M.EDWARDS,C.H.ARROWSMITH,J.WEIGELT,                  
AUTHOR   3 C.BOUNTRA,A.BOCHKAREV,S.DHE-PAGANON,J.MIN,H.OUYANG,                  
AUTHOR   4 STRUCTURAL GENOMICS CONSORTIUM (SGC)                                 
REVDAT   2   24-FEB-09 3C5K    1       VERSN                                    
REVDAT   1   19-FEB-08 3C5K    0                                                
JRNL        AUTH   A.DONG,M.RAVICHANDRAN,A.SCHUETZ,P.LOPPNAU,Y.LI,              
JRNL        AUTH 2 F.MACKENZIE,I.KOZIERADZKI,A.M.EDWARDS,                       
JRNL        AUTH 3 C.H.ARROWSMITH,J.WEIGELT,C.BOUNTRA,A.BOCHKAREV,              
JRNL        AUTH 4 S.DHE-PAGANON,J.MIN,H.OUYANG                                 
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN HDAC6 ZINC FINGER                 
JRNL        TITL 2 DOMAIN.                                                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.55 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) : 1.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.07                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 65.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 9546                           
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) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.173                           
REMARK   3   FREE R VALUE                     : 0.227                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 486                             
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) : 1.55                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.59                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 386                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 37.32                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1990                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 23                           
REMARK   3   BIN FREE R VALUE                    : 0.1860                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 840                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 3                                       
REMARK   3   SOLVENT ATOMS            : 156                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 12.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 10.93                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.01000                                             
REMARK   3    B22 (A**2) : 1.68000                                              
REMARK   3    B33 (A**2) : 0.33000                                              
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): 0.134         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.133         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.054         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.422         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
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):   872 ; 0.008 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1197 ; 1.151 ; 1.916       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   107 ; 6.122 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    39 ;35.236 ;24.103       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   117 ;11.759 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     1 ; 7.831 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   125 ; 0.099 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   690 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   407 ; 0.187 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   595 ; 0.302 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    96 ; 0.109 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     1 ; 0.023 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.159 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    20 ; 0.130 ; 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):   548 ; 0.604 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   872 ; 1.043 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   375 ; 1.500 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   325 ; 2.257 ; 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: THE FRIEDEL PAIRS WERE USED IN            
REMARK   3  PHASING. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.         
REMARK   3  PROGRAMS ARP/WARP 6.1.1, COOT 0.3.3 HAVE ALSO BEEN USED IN          
REMARK   3  REFINEMENT                                                          
REMARK   4                                                                      
REMARK   4 3C5K COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-FEB-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB046368.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-JAN-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.26000                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : SI(111)                            
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   : 15138                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 10.800                             
REMARK 200  R MERGE                    (I) : 0.07100                            
REMARK 200  R SYM                      (I) : 0.07100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.61                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.20100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.20100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.840                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.23                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.5M NA FORMATE, 100MM BIS-TRIS          
REMARK 280  PROPANE PH 7.0, VAPOR 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       20.25000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       27.87950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       22.55450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       27.87950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       20.25000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       22.55450            
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 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 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    -1                                                      
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     ILE A  14    CD1                                                 
REMARK 470     GLN A  85    CD   OE1  NE2                                       
REMARK 470     GLU A 101    CD   OE1  OE2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  27      -66.13    -91.42                                   
REMARK 500    ILE A  49     -102.22    -92.71                                   
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 109.3                                              
REMARK 620 3 CYS A  75   SG  114.1  99.1                                        
REMARK 620 4 CYS A  78   SG  114.5 103.7 114.2                                  
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  111.0                                              
REMARK 620 3 CYS A  45   SG  114.6 114.1                                        
REMARK 620 4 HIS A  52   ND1 104.2 110.8 101.2                                  
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  116.9                                              
REMARK 620 3 HIS A  56   NE2 115.2  98.3                                        
REMARK 620 4 HIS A  62   ND1 108.4 109.4 108.1                                  
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 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 202                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 203                  
DBREF  3C5K A    1   107  UNP    Q9UBN7   HDAC6_HUMAN   1109   1215             
SEQADV 3C5K GLY A   -1  UNP  Q9UBN7              EXPRESSION TAG                 
SEQADV 3C5K SER A    0  UNP  Q9UBN7              EXPRESSION TAG                 
SEQRES   1 A  109  GLY SER PRO LEU PRO TRP CYS PRO HIS LEU VAL ALA VAL          
SEQRES   2 A  109  CYS PRO ILE PRO ALA ALA GLY LEU ASP VAL THR GLN PRO          
SEQRES   3 A  109  CYS GLY ASP CYS GLY THR ILE GLN GLU ASN TRP VAL CYS          
SEQRES   4 A  109  LEU SER CYS TYR GLN VAL TYR CYS GLY ARG TYR ILE ASN          
SEQRES   5 A  109  GLY HIS MET LEU GLN HIS HIS GLY ASN SER GLY HIS PRO          
SEQRES   6 A  109  LEU VAL LEU SER TYR ILE ASP LEU SER ALA TRP CYS TYR          
SEQRES   7 A  109  TYR CYS GLN ALA TYR VAL HIS HIS GLN ALA LEU LEU ASP          
SEQRES   8 A  109  VAL LYS ASN ILE ALA HIS GLN ASN LYS PHE GLY GLU ASP          
SEQRES   9 A  109  MET PRO HIS PRO HIS                                          
HET     ZN  A 201       1                                                       
HET     ZN  A 202       1                                                       
HET     ZN  A 203       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   2   ZN    3(ZN 2+)                                                     
FORMUL   5  HOH   *156(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  GLY A  100  1                                  14    
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  2.36  
LINK         ND1 HIS A   7                ZN    ZN A 203     1555   1555  2.13  
LINK         SG  CYS A  25                ZN    ZN A 202     1555   1555  2.39  
LINK         SG  CYS A  28                ZN    ZN A 202     1555   1555  2.31  
LINK         SG  CYS A  37                ZN    ZN A 201     1555   1555  2.30  
LINK         SG  CYS A  40                ZN    ZN A 201     1555   1555  2.38  
LINK         SG  CYS A  45                ZN    ZN A 202     1555   1555  2.22  
LINK         ND1 HIS A  52                ZN    ZN A 202     1555   1555  2.11  
LINK         NE2 HIS A  56                ZN    ZN A 201     1555   1555  2.10  
LINK         ND1 HIS A  62                ZN    ZN A 201     1555   1555  2.04  
LINK         SG  CYS A  75                ZN    ZN A 203     1555   1555  2.38  
LINK         SG  CYS A  78                ZN    ZN A 203     1555   1555  2.35  
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                    
CRYST1   40.500   45.109   55.759  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      0.024691  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.022169  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017934        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system