GenomeNet

Database: PDB
Entry: 3PHD
LinkDB: 3PHD
Original site: 3PHD 
HEADER    PROTEIN BINDING                         03-NOV-10   3PHD              
TITLE     CRYSTAL STRUCTURE OF HUMAN HDAC6 IN COMPLEX WITH UBIQUITIN            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE DEACETYLASE 6;                                     
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: HD6;                                                        
COMPND   5 EC: 3.5.1.98;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: POLYUBIQUITIN;                                             
COMPND   9 CHAIN: E, F, G, H;                                                   
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HDAC6, KIAA0901, JM21;                                         
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;                                
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: UBB, UBA52, UBCEP2, UBC, RPS27A, UBA80, UBCEP1;                
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HDAC6, UBIQUITIN, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS            
KEYWDS   2 CONSORTIUM, SGC, PROTEIN BINDING                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.DONG,W.QUI,M.RAVICHANDRAN,A.SCHUETZ,P.LOPPNAU,F.LI,F.MACKENZIE,     
AUTHOR   2 I.KOZIERADZKI,H.OUYANG,STRUCTURAL GENOMICS CONSORTIUM (SGC)          
REVDAT   4   08-FEB-12 3PHD    1       JRNL                                     
REVDAT   3   23-NOV-11 3PHD    1       JRNL                                     
REVDAT   2   16-NOV-11 3PHD    1       JRNL                                     
REVDAT   1   23-FEB-11 3PHD    0                                                
JRNL        AUTH   H.OUYANG,Y.O.ALI,M.RAVICHANDRAN,A.DONG,W.QIU,F.MACKENZIE,    
JRNL        AUTH 2 S.DHE-PAGANON,C.H.ARROWSMITH,R.G.ZHAI                        
JRNL        TITL   PROTEIN AGGREGATES ARE RECRUITED TO AGGRESOME BY HISTONE     
JRNL        TITL 2 DEACETYLASE 6 VIA UNANCHORED UBIQUITIN C TERMINI.            
JRNL        REF    J.BIOL.CHEM.                  V. 287  2317 2012              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   22069321                                                     
JRNL        DOI    10.1074/JBC.M111.273730                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.8.0                                         
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.72                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 22135                          
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)  : 0.235                          
REMARK   3   R VALUE            (WORKING SET)  : 0.235                          
REMARK   3   FREE R VALUE                      : 0.265                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 2.090                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 463                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 11                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.00                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.15                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2894                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2593                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2823                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2585                   
REMARK   3   BIN FREE R VALUE                        : 0.2907                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 2.45                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 71                       
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3307                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 12                                      
REMARK   3   SOLVENT ATOMS            : 2                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 92.68                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 72.86                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.45780                                             
REMARK   3    B22 (A**2) : -3.45780                                             
REMARK   3    B33 (A**2) : 6.91570                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.42                
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.907                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.856                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3400   ; 2.000  ; NULL                
REMARK   3    BOND ANGLES               : 4648   ; 2.000  ; NULL                
REMARK   3    TORSION ANGLES            : 950    ; 2.000  ; NULL                
REMARK   3    TRIGONAL CARBON PLANES    : 55     ; 2.000  ; NULL                
REMARK   3    GENERAL PLANES            : 530    ; 5.000  ; NULL                
REMARK   3    ISOTROPIC THERMAL FACTORS : 3400   ; 20.000 ; NULL                
REMARK   3    BAD NON-BONDED CONTACTS   : 6      ; 5.000  ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 451    ; 5.000  ; NULL                
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 3660   ; 4.000  ; NULL                
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.12                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.88                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 19.83                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3PHD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-NOV-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB062375.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-MAR-08                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.03317                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000                            
REMARK 200  DATA SCALING SOFTWARE          : HKL2000                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22204                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 16.200                             
REMARK 200  R MERGE                    (I) : 0.09100                            
REMARK 200  R SYM                      (I) : 0.09100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 45.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.76700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP 9.2                                            
REMARK 200 STARTING MODEL: PDB ENTRY 3C5K                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.84                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.22                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 3350, 0.1M AMMONIUM SULPHATE,    
REMARK 280  0.1M BIS-TRIS, PH 5.6, TEMPERATURE 297K                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       59.38400            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       66.87400            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       66.87400            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       89.07600            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       66.87400            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       66.87400            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       29.69200            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       66.87400            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       66.87400            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       89.07600            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       66.87400            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       66.87400            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       29.69200            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       59.38400            
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: OCTAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H                
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   103                                                      
REMARK 465     PRO A   104                                                      
REMARK 465     HIS A   105                                                      
REMARK 465     PRO A   106                                                      
REMARK 465     HIS A   107                                                      
REMARK 465     GLU B   101                                                      
REMARK 465     ASP B   102                                                      
REMARK 465     MET B   103                                                      
REMARK 465     PRO B   104                                                      
REMARK 465     HIS B   105                                                      
REMARK 465     PRO B   106                                                      
REMARK 465     HIS B   107                                                      
REMARK 465     PRO C     1                                                      
REMARK 465     LEU C     2                                                      
REMARK 465     LEU C    88                                                      
REMARK 465     ASP C    89                                                      
REMARK 465     VAL C    90                                                      
REMARK 465     LYS C    91                                                      
REMARK 465     ASN C    92                                                      
REMARK 465     ILE C    93                                                      
REMARK 465     ALA C    94                                                      
REMARK 465     HIS C    95                                                      
REMARK 465     GLN C    96                                                      
REMARK 465     ASN C    97                                                      
REMARK 465     LYS C    98                                                      
REMARK 465     PHE C    99                                                      
REMARK 465     GLY C   100                                                      
REMARK 465     GLU C   101                                                      
REMARK 465     ASP C   102                                                      
REMARK 465     MET C   103                                                      
REMARK 465     PRO C   104                                                      
REMARK 465     HIS C   105                                                      
REMARK 465     PRO C   106                                                      
REMARK 465     HIS C   107                                                      
REMARK 465     PRO D     1                                                      
REMARK 465     LEU D     2                                                      
REMARK 465     PRO D     3                                                      
REMARK 465     LEU D    88                                                      
REMARK 465     ASP D    89                                                      
REMARK 465     VAL D    90                                                      
REMARK 465     LYS D    91                                                      
REMARK 465     ASN D    92                                                      
REMARK 465     ILE D    93                                                      
REMARK 465     ALA D    94                                                      
REMARK 465     HIS D    95                                                      
REMARK 465     GLN D    96                                                      
REMARK 465     ASN D    97                                                      
REMARK 465     LYS D    98                                                      
REMARK 465     PHE D    99                                                      
REMARK 465     GLY D   100                                                      
REMARK 465     GLU D   101                                                      
REMARK 465     ASP D   102                                                      
REMARK 465     MET D   103                                                      
REMARK 465     PRO D   104                                                      
REMARK 465     HIS D   105                                                      
REMARK 465     PRO D   106                                                      
REMARK 465     HIS D   107                                                      
REMARK 465     MET E     1                                                      
REMARK 465     GLN E     2                                                      
REMARK 465     ILE E     3                                                      
REMARK 465     PHE E     4                                                      
REMARK 465     VAL E     5                                                      
REMARK 465     LYS E     6                                                      
REMARK 465     THR E     7                                                      
REMARK 465     LEU E     8                                                      
REMARK 465     THR E     9                                                      
REMARK 465     GLY E    10                                                      
REMARK 465     LYS E    11                                                      
REMARK 465     THR E    12                                                      
REMARK 465     ILE E    13                                                      
REMARK 465     THR E    14                                                      
REMARK 465     LEU E    15                                                      
REMARK 465     GLU E    16                                                      
REMARK 465     VAL E    17                                                      
REMARK 465     GLU E    18                                                      
REMARK 465     PRO E    19                                                      
REMARK 465     SER E    20                                                      
REMARK 465     ASP E    21                                                      
REMARK 465     THR E    22                                                      
REMARK 465     ALA E    28                                                      
REMARK 465     LYS E    29                                                      
REMARK 465     ILE E    30                                                      
REMARK 465     GLN E    31                                                      
REMARK 465     ASP E    32                                                      
REMARK 465     LYS E    33                                                      
REMARK 465     GLU E    34                                                      
REMARK 465     GLY E    35                                                      
REMARK 465     ILE E    36                                                      
REMARK 465     PRO E    37                                                      
REMARK 465     PRO E    38                                                      
REMARK 465     ASP E    39                                                      
REMARK 465     GLN E    40                                                      
REMARK 465     GLN E    41                                                      
REMARK 465     ARG E    42                                                      
REMARK 465     LEU E    43                                                      
REMARK 465     ILE E    44                                                      
REMARK 465     PHE E    45                                                      
REMARK 465     ALA E    46                                                      
REMARK 465     GLY E    47                                                      
REMARK 465     LYS E    48                                                      
REMARK 465     GLN E    49                                                      
REMARK 465     LEU E    50                                                      
REMARK 465     GLU E    51                                                      
REMARK 465     ASP E    52                                                      
REMARK 465     GLY E    53                                                      
REMARK 465     ARG E    54                                                      
REMARK 465     THR E    55                                                      
REMARK 465     LEU E    56                                                      
REMARK 465     SER E    57                                                      
REMARK 465     ASP E    58                                                      
REMARK 465     TYR E    59                                                      
REMARK 465     ASN E    60                                                      
REMARK 465     ILE E    61                                                      
REMARK 465     GLN E    62                                                      
REMARK 465     LYS E    63                                                      
REMARK 465     GLU E    64                                                      
REMARK 465     SER E    65                                                      
REMARK 465     THR E    66                                                      
REMARK 465     VAL E    70                                                      
REMARK 465     MET F     1                                                      
REMARK 465     GLN F     2                                                      
REMARK 465     ILE F     3                                                      
REMARK 465     PHE F     4                                                      
REMARK 465     VAL F     5                                                      
REMARK 465     LYS F     6                                                      
REMARK 465     THR F     7                                                      
REMARK 465     LEU F     8                                                      
REMARK 465     THR F     9                                                      
REMARK 465     GLY F    10                                                      
REMARK 465     LYS F    11                                                      
REMARK 465     THR F    12                                                      
REMARK 465     ILE F    13                                                      
REMARK 465     THR F    14                                                      
REMARK 465     LEU F    15                                                      
REMARK 465     GLU F    16                                                      
REMARK 465     VAL F    17                                                      
REMARK 465     GLU F    18                                                      
REMARK 465     PRO F    19                                                      
REMARK 465     SER F    20                                                      
REMARK 465     ASP F    21                                                      
REMARK 465     THR F    22                                                      
REMARK 465     ILE F    23                                                      
REMARK 465     GLU F    24                                                      
REMARK 465     ASN F    25                                                      
REMARK 465     VAL F    26                                                      
REMARK 465     LYS F    27                                                      
REMARK 465     ALA F    28                                                      
REMARK 465     LYS F    29                                                      
REMARK 465     ILE F    30                                                      
REMARK 465     GLN F    31                                                      
REMARK 465     ASP F    32                                                      
REMARK 465     LYS F    33                                                      
REMARK 465     GLU F    34                                                      
REMARK 465     GLY F    35                                                      
REMARK 465     ILE F    36                                                      
REMARK 465     PRO F    37                                                      
REMARK 465     PRO F    38                                                      
REMARK 465     ASP F    39                                                      
REMARK 465     GLN F    40                                                      
REMARK 465     GLN F    41                                                      
REMARK 465     ARG F    42                                                      
REMARK 465     LEU F    43                                                      
REMARK 465     ILE F    44                                                      
REMARK 465     PHE F    45                                                      
REMARK 465     ALA F    46                                                      
REMARK 465     GLY F    47                                                      
REMARK 465     LYS F    48                                                      
REMARK 465     GLN F    49                                                      
REMARK 465     LEU F    50                                                      
REMARK 465     GLU F    51                                                      
REMARK 465     ASP F    52                                                      
REMARK 465     GLY F    53                                                      
REMARK 465     ARG F    54                                                      
REMARK 465     THR F    55                                                      
REMARK 465     LEU F    56                                                      
REMARK 465     SER F    57                                                      
REMARK 465     ASP F    58                                                      
REMARK 465     TYR F    59                                                      
REMARK 465     ASN F    60                                                      
REMARK 465     ILE F    61                                                      
REMARK 465     GLN F    62                                                      
REMARK 465     LYS F    63                                                      
REMARK 465     GLU F    64                                                      
REMARK 465     SER F    65                                                      
REMARK 465     THR F    66                                                      
REMARK 465     LEU F    67                                                      
REMARK 465     HIS F    68                                                      
REMARK 465     LEU F    69                                                      
REMARK 465     VAL F    70                                                      
REMARK 465     LEU F    71                                                      
REMARK 465     MET G     1                                                      
REMARK 465     GLN G     2                                                      
REMARK 465     ILE G     3                                                      
REMARK 465     PHE G     4                                                      
REMARK 465     LEU G    15                                                      
REMARK 465     GLU G    16                                                      
REMARK 465     SER G    20                                                      
REMARK 465     ASP G    21                                                      
REMARK 465     GLN G    31                                                      
REMARK 465     ASP G    32                                                      
REMARK 465     LYS G    33                                                      
REMARK 465     GLU G    34                                                      
REMARK 465     GLY G    35                                                      
REMARK 465     ILE G    36                                                      
REMARK 465     PRO G    37                                                      
REMARK 465     PRO G    38                                                      
REMARK 465     ASP G    39                                                      
REMARK 465     ARG G    42                                                      
REMARK 465     ALA G    46                                                      
REMARK 465     GLY G    47                                                      
REMARK 465     LYS G    48                                                      
REMARK 465     GLN G    49                                                      
REMARK 465     LEU G    50                                                      
REMARK 465     GLU G    51                                                      
REMARK 465     ASP G    52                                                      
REMARK 465     GLY G    53                                                      
REMARK 465     ARG G    54                                                      
REMARK 465     THR G    55                                                      
REMARK 465     LEU G    56                                                      
REMARK 465     SER G    57                                                      
REMARK 465     ASP G    58                                                      
REMARK 465     TYR G    59                                                      
REMARK 465     ASN G    60                                                      
REMARK 465     ILE G    61                                                      
REMARK 465     GLN G    62                                                      
REMARK 465     LYS G    63                                                      
REMARK 465     MET H     1                                                      
REMARK 465     GLN H     2                                                      
REMARK 465     ILE H     3                                                      
REMARK 465     PHE H     4                                                      
REMARK 465     ILE H    13                                                      
REMARK 465     THR H    14                                                      
REMARK 465     LEU H    15                                                      
REMARK 465     GLU H    16                                                      
REMARK 465     VAL H    17                                                      
REMARK 465     GLU H    18                                                      
REMARK 465     ASP H    21                                                      
REMARK 465     GLN H    31                                                      
REMARK 465     ASP H    32                                                      
REMARK 465     LYS H    33                                                      
REMARK 465     GLU H    34                                                      
REMARK 465     GLY H    35                                                      
REMARK 465     ILE H    36                                                      
REMARK 465     PRO H    37                                                      
REMARK 465     PRO H    38                                                      
REMARK 465     ASP H    39                                                      
REMARK 465     LYS H    48                                                      
REMARK 465     GLN H    49                                                      
REMARK 465     LEU H    50                                                      
REMARK 465     GLU H    51                                                      
REMARK 465     ASP H    52                                                      
REMARK 465     GLY H    53                                                      
REMARK 465     ARG H    54                                                      
REMARK 465     THR H    55                                                      
REMARK 465     LEU H    56                                                      
REMARK 465     SER H    57                                                      
REMARK 465     ASP H    58                                                      
REMARK 465     TYR H    59                                                      
REMARK 465     ASN H    60                                                      
REMARK 465     SER H    65                                                      
REMARK 465     THR H    66                                                      
REMARK 465     LEU H    67                                                      
REMARK 465     HIS H    68                                                      
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     PRO A   1    CG   CD                                             
REMARK 470     ILE A  14    CG1  CG2  CD1                                       
REMARK 470     LEU A  19    CG   CD1  CD2                                       
REMARK 470     VAL A  21    CG1  CG2                                            
REMARK 470     ILE A  31    CD1                                                 
REMARK 470     GLN A  32    CG   CD   OE1  NE2                                  
REMARK 470     ILE A  49    CD1                                                 
REMARK 470     LEU A  54    CD1  CD2                                            
REMARK 470     ASN A  59    CG   OD1  ND2                                       
REMARK 470     GLN A  85    CG   CD   OE1  NE2                                  
REMARK 470     LEU A  88    CG   CD1  CD2                                       
REMARK 470     VAL A  90    CG1  CG2                                            
REMARK 470     ILE A  93    CD1                                                 
REMARK 470     GLU A 101    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 102    CG   OD1  OD2                                       
REMARK 470     VAL B   9    CG1  CG2                                            
REMARK 470     ILE B  14    CG1  CD1                                            
REMARK 470     ILE B  31    CD1                                                 
REMARK 470     ILE B  49    CD1                                                 
REMARK 470     ILE B  69    CD1                                                 
REMARK 470     HIS B  83    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN B  85    CG   CD   OE1  NE2                                  
REMARK 470     LEU B  88    CG   CD1  CD2                                       
REMARK 470     VAL B  90    CG1  CG2                                            
REMARK 470     ILE B  93    CG1  CG2  CD1                                       
REMARK 470     LEU C   8    CG   CD1  CD2                                       
REMARK 470     ILE C  14    CG1  CD1                                            
REMARK 470     LEU C  19    CG   CD1  CD2                                       
REMARK 470     ILE C  31    CG1  CG2  CD1                                       
REMARK 470     GLN C  32    CG   CD   OE1  NE2                                  
REMARK 470     VAL C  43    CG1  CG2                                            
REMARK 470     ILE C  49    CD1                                                 
REMARK 470     LEU C  54    CD1  CD2                                            
REMARK 470     GLN C  55    CG   CD   OE1  NE2                                  
REMARK 470     ILE C  69    CD1                                                 
REMARK 470     LEU C  71    CG   CD1  CD2                                       
REMARK 470     GLN C  85    CD   OE1  NE2                                       
REMARK 470     LEU C  87    CG   CD1  CD2                                       
REMARK 470     TRP D   4    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP D   4    CZ3  CH2                                            
REMARK 470     ILE D  14    CG1  CD1                                            
REMARK 470     VAL D  21    CG1  CG2                                            
REMARK 470     ILE D  31    CD1                                                 
REMARK 470     GLN D  32    CG   CD   OE1  NE2                                  
REMARK 470     TYR D  48    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ILE D  49    CD1                                                 
REMARK 470     ILE D  69    CG2  CD1                                            
REMARK 470     LEU D  71    CD1  CD2                                            
REMARK 470     GLN D  85    CD   OE1  NE2                                       
REMARK 470     ILE E  23    CG1  CG2  CD1                                       
REMARK 470     GLU E  24    CG   CD   OE1  OE2                                  
REMARK 470     ASN E  25    CG   OD1  ND2                                       
REMARK 470     VAL E  26    CG1  CG2                                            
REMARK 470     LYS E  27    CG   CD   CE   NZ                                   
REMARK 470     LEU E  67    CG   CD1  CD2                                       
REMARK 470     LEU E  69    CG   CD1  CD2                                       
REMARK 470     LEU E  71    CG   CD1  CD2                                       
REMARK 470     ARG E  72    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU E  73    CG   CD1  CD2                                       
REMARK 470     ARG E  74    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG F  72    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU F  73    CG   CD1  CD2                                       
REMARK 470     VAL G   5    CG1  CG2                                            
REMARK 470     LYS G   6    CG   CD   CE   NZ                                   
REMARK 470     THR G   7    OG1  CG2                                            
REMARK 470     LEU G   8    CG   CD1  CD2                                       
REMARK 470     THR G   9    OG1  CG2                                            
REMARK 470     LYS G  11    CG   CD   CE   NZ                                   
REMARK 470     ILE G  13    CG1  CG2  CD1                                       
REMARK 470     VAL G  17    CG1  CG2                                            
REMARK 470     GLU G  18    CG   CD   OE1  OE2                                  
REMARK 470     PRO G  19    CG   CD                                             
REMARK 470     THR G  22    OG1  CG2                                            
REMARK 470     ILE G  23    CG1  CG2  CD1                                       
REMARK 470     GLU G  24    CG   CD   OE1  OE2                                  
REMARK 470     ASN G  25    CG   OD1  ND2                                       
REMARK 470     VAL G  26    CG1  CG2                                            
REMARK 470     LYS G  27    CG   CD   CE   NZ                                   
REMARK 470     LYS G  29    CG   CD   CE   NZ                                   
REMARK 470     ILE G  30    CG1  CG2  CD1                                       
REMARK 470     GLN G  40    CG   CD   OE1  NE2                                  
REMARK 470     GLN G  41    CG   CD   OE1  NE2                                  
REMARK 470     LEU G  43    CG   CD1  CD2                                       
REMARK 470     ILE G  44    CG1  CG2  CD1                                       
REMARK 470     GLU G  64    CG   CD   OE1  OE2                                  
REMARK 470     SER G  65    OG                                                  
REMARK 470     THR G  66    OG1  CG2                                            
REMARK 470     LEU G  67    CG   CD1  CD2                                       
REMARK 470     HIS G  68    CG   ND1  CD2  CE1  NE2                             
REMARK 470     VAL G  70    CG1  CG2                                            
REMARK 470     LEU G  71    CG   CD1  CD2                                       
REMARK 470     LEU G  73    CG   CD1  CD2                                       
REMARK 470     VAL H   5    CG1  CG2                                            
REMARK 470     LYS H   6    CG   CD   CE   NZ                                   
REMARK 470     THR H   7    OG1  CG2                                            
REMARK 470     LEU H   8    CG   CD1  CD2                                       
REMARK 470     THR H   9    OG1  CG2                                            
REMARK 470     LYS H  11    CG   CD   CE   NZ                                   
REMARK 470     PRO H  19    CG   CD                                             
REMARK 470     SER H  20    OG                                                  
REMARK 470     THR H  22    OG1  CG2                                            
REMARK 470     ILE H  23    CG1  CG2  CD1                                       
REMARK 470     GLU H  24    CG   CD   OE1  OE2                                  
REMARK 470     ASN H  25    CG   OD1  ND2                                       
REMARK 470     VAL H  26    CG1  CG2                                            
REMARK 470     LYS H  27    CG   CD   CE   NZ                                   
REMARK 470     LYS H  29    CG   CD   CE   NZ                                   
REMARK 470     ILE H  30    CG1  CG2  CD1                                       
REMARK 470     GLN H  40    CG   CD   OE1  NE2                                  
REMARK 470     GLN H  41    CG   CD   OE1  NE2                                  
REMARK 470     ARG H  42    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU H  43    CG   CD1  CD2                                       
REMARK 470     ILE H  44    CG1  CG2  CD1                                       
REMARK 470     ILE H  61    CG1  CG2  CD1                                       
REMARK 470     GLN H  62    CG   CD   OE1  NE2                                  
REMARK 470     LYS H  63    CG   CD   CE   NZ                                   
REMARK 470     GLU H  64    CG   CD   OE1  OE2                                  
REMARK 470     VAL H  70    CG1  CG2                                            
REMARK 470     LEU H  71    CG   CD1  CD2                                       
REMARK 470     ARG H  72    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU H  73    CG   CD1  CD2                                       
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    LEU H  73   C   -  N   -  CA  ANGL. DEV. =  16.1 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    ILE A  49      -99.61    -99.35                                   
REMARK 500    PHE A  99      -50.37   -126.18                                   
REMARK 500    ILE B  49      -98.93   -100.12                                   
REMARK 500    PHE B  99      -52.46   -126.08                                   
REMARK 500    PRO C   6        2.28    -69.11                                   
REMARK 500    ILE C  49      -95.54    -95.20                                   
REMARK 500    LEU C  71       26.71     49.37                                   
REMARK 500    ILE D  49     -100.36   -107.66                                   
REMARK 500    HIS E  68      114.96   -165.58                                   
REMARK 500    LEU E  73     -163.26     55.68                                   
REMARK 500    LEU G  71     -114.03   -124.73                                   
REMARK 500    ARG G  72       99.22   -175.10                                   
REMARK 500    LEU G  73      -57.09    -15.00                                   
REMARK 500    ILE H  23      -83.12   -136.52                                   
REMARK 500    LEU H  71     -158.75   -114.29                                   
REMARK 500    ARG H  72       55.77   -141.15                                   
REMARK 500    LEU H  73      -94.36     55.31                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU G   18     PRO G   19                  121.21                    
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 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
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: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    TYR A  41        24.9      L          L   OUTSIDE RANGE           
REMARK 500    LEU B  54        24.7      L          L   OUTSIDE RANGE           
REMARK 500    TYR C  41        24.7      L          L   OUTSIDE RANGE           
REMARK 500    VAL C  82        24.4      L          L   OUTSIDE RANGE           
REMARK 500    LEU G  73        23.2      L          L   OUTSIDE RANGE           
REMARK 500    LEU H  73        22.2      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1000  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  62   ND1                                                    
REMARK 620 2 HIS A  56   NE2 115.6                                              
REMARK 620 3 CYS A  37   SG  104.6 116.5                                        
REMARK 620 4 CYS A  40   SG  116.6  95.4 108.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C2001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  52   ND1                                                    
REMARK 620 2 CYS C  45   SG  103.8                                              
REMARK 620 3 CYS C  25   SG  104.2 115.0                                        
REMARK 620 4 CYS C  28   SG  111.7 116.0 105.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B2000  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  62   ND1                                                    
REMARK 620 2 HIS B  56   NE2 110.7                                              
REMARK 620 3 CYS B  37   SG  102.2 115.9                                        
REMARK 620 4 CYS B  40   SG  117.9  97.5 113.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D2002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D   7   ND1                                                    
REMARK 620 2 CYS D  78   SG  106.6                                              
REMARK 620 3 CYS D  75   SG  100.0 108.7                                        
REMARK 620 4 CYS D   5   SG  116.0 115.0 109.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D2000  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  62   ND1                                                    
REMARK 620 2 HIS D  56   NE2 109.0                                              
REMARK 620 3 CYS D  37   SG  105.7 118.5                                        
REMARK 620 4 CYS D  40   SG  113.8  94.5 115.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B2002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B   7   ND1                                                    
REMARK 620 2 CYS B  78   SG  102.8                                              
REMARK 620 3 CYS B  75   SG  102.3 112.6                                        
REMARK 620 4 CYS B   5   SG  114.6 113.6 110.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C2000  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  62   ND1                                                    
REMARK 620 2 HIS C  56   NE2 108.0                                              
REMARK 620 3 CYS C  37   SG  104.8 119.9                                        
REMARK 620 4 CYS C  40   SG  115.2  93.8 115.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D2001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  52   ND1                                                    
REMARK 620 2 CYS D  45   SG  101.1                                              
REMARK 620 3 CYS D  25   SG  103.1 126.7                                        
REMARK 620 4 CYS D  28   SG  112.8 110.3 102.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A   7   ND1                                                    
REMARK 620 2 CYS A  78   SG  100.8                                              
REMARK 620 3 CYS A  75   SG   98.9 107.7                                        
REMARK 620 4 CYS A   5   SG  117.4 117.2 112.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B2001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  52   ND1                                                    
REMARK 620 2 CYS B  45   SG  101.2                                              
REMARK 620 3 CYS B  25   SG  101.7 122.8                                        
REMARK 620 4 CYS B  28   SG  102.3 114.1 110.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C2002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C   7   ND1                                                    
REMARK 620 2 CYS C   5   SG  119.3                                              
REMARK 620 3 CYS C  78   SG   99.3 117.2                                        
REMARK 620 4 CYS C  75   SG   97.5 114.8 105.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  52   ND1                                                    
REMARK 620 2 CYS A  45   SG  113.7                                              
REMARK 620 3 CYS A  28   SG  105.5 120.2                                        
REMARK 620 4 CYS A  25   SG   90.3 117.7 105.0                                  
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 1000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 2000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 2000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 2000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 2002                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3C5K   RELATED DB: PDB                                   
REMARK 900 HIGH RESOLUTION STRUCTURE OF HDAC6                                   
REMARK 900 RELATED ID: 3GV4   RELATED DB: PDB                                   
REMARK 900 HIGH RESOLUTION STRUCTURE OF HDAC6                                   
REMARK 900 RELATED ID: 2ZNV   RELATED DB: PDB                                   
REMARK 900 HIGH RESOLUTION STRUCTURE OF UBIQUITIN                               
REMARK 900 RELATED ID: 3NHE   RELATED DB: PDB                                   
REMARK 900 HIGH RESOLUTION STRUCTURE OF UBIQUITIN                               
DBREF  3PHD A    1   107  UNP    Q9UBN7   HDAC6_HUMAN   1109   1215             
DBREF  3PHD B    1   107  UNP    Q9UBN7   HDAC6_HUMAN   1109   1215             
DBREF  3PHD C    1   107  UNP    Q9UBN7   HDAC6_HUMAN   1109   1215             
DBREF  3PHD D    1   107  UNP    Q9UBN7   HDAC6_HUMAN   1109   1215             
DBREF  3PHD E    1    76  UNP    P62988   UBB_HUMAN        1     76             
DBREF  3PHD F    1    76  UNP    P62988   UBB_HUMAN        1     76             
DBREF  3PHD G    1    76  UNP    P62988   UBB_HUMAN        1     76             
DBREF  3PHD H    1    76  UNP    P62988   UBB_HUMAN        1     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 B  107  PRO LEU PRO TRP CYS PRO HIS LEU VAL ALA VAL CYS PRO          
SEQRES   2 B  107  ILE PRO ALA ALA GLY LEU ASP VAL THR GLN PRO CYS GLY          
SEQRES   3 B  107  ASP CYS GLY THR ILE GLN GLU ASN TRP VAL CYS LEU SER          
SEQRES   4 B  107  CYS TYR GLN VAL TYR CYS GLY ARG TYR ILE ASN GLY HIS          
SEQRES   5 B  107  MET LEU GLN HIS HIS GLY ASN SER GLY HIS PRO LEU VAL          
SEQRES   6 B  107  LEU SER TYR ILE ASP LEU SER ALA TRP CYS TYR TYR CYS          
SEQRES   7 B  107  GLN ALA TYR VAL HIS HIS GLN ALA LEU LEU ASP VAL LYS          
SEQRES   8 B  107  ASN ILE ALA HIS GLN ASN LYS PHE GLY GLU ASP MET PRO          
SEQRES   9 B  107  HIS PRO HIS                                                  
SEQRES   1 C  107  PRO LEU PRO TRP CYS PRO HIS LEU VAL ALA VAL CYS PRO          
SEQRES   2 C  107  ILE PRO ALA ALA GLY LEU ASP VAL THR GLN PRO CYS GLY          
SEQRES   3 C  107  ASP CYS GLY THR ILE GLN GLU ASN TRP VAL CYS LEU SER          
SEQRES   4 C  107  CYS TYR GLN VAL TYR CYS GLY ARG TYR ILE ASN GLY HIS          
SEQRES   5 C  107  MET LEU GLN HIS HIS GLY ASN SER GLY HIS PRO LEU VAL          
SEQRES   6 C  107  LEU SER TYR ILE ASP LEU SER ALA TRP CYS TYR TYR CYS          
SEQRES   7 C  107  GLN ALA TYR VAL HIS HIS GLN ALA LEU LEU ASP VAL LYS          
SEQRES   8 C  107  ASN ILE ALA HIS GLN ASN LYS PHE GLY GLU ASP MET PRO          
SEQRES   9 C  107  HIS PRO HIS                                                  
SEQRES   1 D  107  PRO LEU PRO TRP CYS PRO HIS LEU VAL ALA VAL CYS PRO          
SEQRES   2 D  107  ILE PRO ALA ALA GLY LEU ASP VAL THR GLN PRO CYS GLY          
SEQRES   3 D  107  ASP CYS GLY THR ILE GLN GLU ASN TRP VAL CYS LEU SER          
SEQRES   4 D  107  CYS TYR GLN VAL TYR CYS GLY ARG TYR ILE ASN GLY HIS          
SEQRES   5 D  107  MET LEU GLN HIS HIS GLY ASN SER GLY HIS PRO LEU VAL          
SEQRES   6 D  107  LEU SER TYR ILE ASP LEU SER ALA TRP CYS TYR TYR CYS          
SEQRES   7 D  107  GLN ALA TYR VAL HIS HIS GLN ALA LEU LEU ASP VAL LYS          
SEQRES   8 D  107  ASN ILE ALA HIS GLN ASN LYS PHE GLY GLU ASP MET PRO          
SEQRES   9 D  107  HIS PRO HIS                                                  
SEQRES   1 E   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 E   76  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 E   76  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 E   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 E   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 E   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
SEQRES   1 F   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 F   76  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 F   76  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 F   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 F   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 F   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
SEQRES   1 G   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 G   76  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 G   76  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 G   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 G   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 G   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
SEQRES   1 H   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 H   76  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 H   76  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 H   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 H   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 H   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
HET     ZN  A1000       1                                                       
HET     ZN  A1001       1                                                       
HET     ZN  A1002       1                                                       
HET     ZN  B2000       1                                                       
HET     ZN  B2001       1                                                       
HET     ZN  B2002       1                                                       
HET     ZN  C2000       1                                                       
HET     ZN  C2001       1                                                       
HET     ZN  C2002       1                                                       
HET     ZN  D2000       1                                                       
HET     ZN  D2001       1                                                       
HET     ZN  D2002       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   9   ZN    12(ZN 2+)                                                    
FORMUL  21  HOH   *2(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    
HELIX    5   5 HIS B    7  VAL B   11  5                                   5    
HELIX    6   6 GLY B   51  GLY B   61  1                                  11    
HELIX    7   7 HIS B   84  ALA B   86  5                                   3    
HELIX    8   8 LEU B   87  PHE B   99  1                                  13    
HELIX    9   9 HIS C    7  VAL C   11  5                                   5    
HELIX   10  10 GLY C   51  GLY C   61  1                                  11    
HELIX   11  11 HIS D    7  VAL D   11  5                                   5    
HELIX   12  12 GLY D   51  GLY D   61  1                                  11    
HELIX   13  13 GLU G   24  ILE G   30  1                                   7    
HELIX   14  14 GLU H   24  ILE H   30  1                                   7    
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  VAL A  82 -1  O  VAL A  82   N  ALA A  73           
SHEET    1   B 5 VAL B  43  CYS B  45  0                                        
SHEET    2   B 5 ASN B  34  CYS B  37 -1  N  TRP B  35   O  TYR B  44           
SHEET    3   B 5 LEU B  64  SER B  67 -1  O  LEU B  66   N  VAL B  36           
SHEET    4   B 5 ALA B  73  CYS B  75 -1  O  TRP B  74   N  VAL B  65           
SHEET    5   B 5 ALA B  80  TYR B  81 -1  O  ALA B  80   N  CYS B  75           
SHEET    1   C 5 VAL C  43  CYS C  45  0                                        
SHEET    2   C 5 ASN C  34  CYS C  37 -1  N  TRP C  35   O  TYR C  44           
SHEET    3   C 5 LEU C  64  SER C  67 -1  O  LEU C  66   N  VAL C  36           
SHEET    4   C 5 ALA C  73  CYS C  75 -1  O  TRP C  74   N  VAL C  65           
SHEET    5   C 5 ALA C  80  HIS C  83 -1  O  VAL C  82   N  ALA C  73           
SHEET    1   D 5 VAL D  43  CYS D  45  0                                        
SHEET    2   D 5 ASN D  34  CYS D  37 -1  N  TRP D  35   O  TYR D  44           
SHEET    3   D 5 LEU D  64  SER D  67 -1  O  LEU D  66   N  VAL D  36           
SHEET    4   D 5 ALA D  73  CYS D  75 -1  O  TRP D  74   N  VAL D  65           
SHEET    5   D 5 ALA D  80  TYR D  81 -1  O  ALA D  80   N  CYS D  75           
LINK         ND1 HIS A  62                ZN    ZN A1000     1555   1555  1.91  
LINK         ND1 HIS C  52                ZN    ZN C2001     1555   1555  1.93  
LINK         ND1 HIS B  62                ZN    ZN B2000     1555   1555  1.95  
LINK         ND1 HIS D   7                ZN    ZN D2002     1555   1555  1.97  
LINK         ND1 HIS D  62                ZN    ZN D2000     1555   1555  1.98  
LINK         ND1 HIS B   7                ZN    ZN B2002     1555   1555  1.99  
LINK         NE2 HIS A  56                ZN    ZN A1000     1555   1555  1.99  
LINK         ND1 HIS C  62                ZN    ZN C2000     1555   1555  2.01  
LINK         ND1 HIS D  52                ZN    ZN D2001     1555   1555  2.01  
LINK         ND1 HIS A   7                ZN    ZN A1002     1555   1555  2.02  
LINK         NE2 HIS B  56                ZN    ZN B2000     1555   1555  2.04  
LINK         NE2 HIS D  56                ZN    ZN D2000     1555   1555  2.04  
LINK         NE2 HIS C  56                ZN    ZN C2000     1555   1555  2.05  
LINK         ND1 HIS B  52                ZN    ZN B2001     1555   1555  2.05  
LINK         ND1 HIS C   7                ZN    ZN C2002     1555   1555  2.09  
LINK         ND1 HIS A  52                ZN    ZN A1001     1555   1555  2.10  
LINK         SG  CYS D  37                ZN    ZN D2000     1555   1555  2.14  
LINK         SG  CYS C  37                ZN    ZN C2000     1555   1555  2.14  
LINK         SG  CYS D  78                ZN    ZN D2002     1555   1555  2.16  
LINK         SG  CYS B  45                ZN    ZN B2001     1555   1555  2.17  
LINK         SG  CYS B  78                ZN    ZN B2002     1555   1555  2.18  
LINK         SG  CYS B  37                ZN    ZN B2000     1555   1555  2.20  
LINK         SG  CYS A  37                ZN    ZN A1000     1555   1555  2.21  
LINK         SG  CYS B  40                ZN    ZN B2000     1555   1555  2.21  
LINK         SG  CYS B  25                ZN    ZN B2001     1555   1555  2.22  
LINK         SG  CYS B  75                ZN    ZN B2002     1555   1555  2.22  
LINK         SG  CYS D  45                ZN    ZN D2001     1555   1555  2.23  
LINK         SG  CYS A  78                ZN    ZN A1002     1555   1555  2.24  
LINK         SG  CYS C   5                ZN    ZN C2002     1555   1555  2.25  
LINK         SG  CYS C  78                ZN    ZN C2002     1555   1555  2.25  
LINK         SG  CYS D  40                ZN    ZN D2000     1555   1555  2.25  
LINK         SG  CYS C  40                ZN    ZN C2000     1555   1555  2.26  
LINK         SG  CYS A  75                ZN    ZN A1002     1555   1555  2.27  
LINK         SG  CYS C  75                ZN    ZN C2002     1555   1555  2.28  
LINK         SG  CYS C  45                ZN    ZN C2001     1555   1555  2.29  
LINK         SG  CYS D  75                ZN    ZN D2002     1555   1555  2.29  
LINK         SG  CYS A  40                ZN    ZN A1000     1555   1555  2.31  
LINK         SG  CYS A   5                ZN    ZN A1002     1555   1555  2.31  
LINK         SG  CYS C  25                ZN    ZN C2001     1555   1555  2.31  
LINK         SG  CYS A  45                ZN    ZN A1001     1555   1555  2.32  
LINK         SG  CYS A  28                ZN    ZN A1001     1555   1555  2.33  
LINK         SG  CYS D  25                ZN    ZN D2001     1555   1555  2.34  
LINK         SG  CYS D  28                ZN    ZN D2001     1555   1555  2.35  
LINK         SG  CYS A  25                ZN    ZN A1001     1555   1555  2.36  
LINK         SG  CYS C  28                ZN    ZN C2001     1555   1555  2.39  
LINK         SG  CYS B   5                ZN    ZN B2002     1555   1555  2.39  
LINK         SG  CYS D   5                ZN    ZN D2002     1555   1555  2.41  
LINK         SG  CYS B  28                ZN    ZN B2001     1555   1555  2.42  
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  4 CYS B  37  CYS B  40  HIS B  56  HIS B  62                    
SITE     1 AC5  4 CYS B  25  CYS B  28  CYS B  45  HIS B  52                    
SITE     1 AC6  4 CYS B   5  HIS B   7  CYS B  75  CYS B  78                    
SITE     1 AC7  4 CYS C  37  CYS C  40  HIS C  56  HIS C  62                    
SITE     1 AC8  4 CYS C  25  CYS C  28  CYS C  45  HIS C  52                    
SITE     1 AC9  4 CYS C   5  HIS C   7  CYS C  75  CYS C  78                    
SITE     1 BC1  4 CYS D  37  CYS D  40  HIS D  56  HIS D  62                    
SITE     1 BC2  4 CYS D  25  CYS D  28  CYS D  45  HIS D  52                    
SITE     1 BC3  4 CYS D   5  HIS D   7  CYS D  75  CYS D  78                    
CRYST1  133.748  133.748  118.768  90.00  90.00  90.00 P 43 21 2    32          
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      0.007477  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007477  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008420        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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