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Database: PDB
Entry: 1GCB
LinkDB: 1GCB
Original site: 1GCB 
HEADER    DNA BINDING PROTEIN                     18-JUL-95   1GCB              
TITLE     GAL6, YEAST BLEOMYCIN HYDROLASE DNA-BINDING PROTEASE (THIOL)          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GAL6 HG (EMTS) DERIVATIVE;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 STRAIN: SC277;                                                       
SOURCE   6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   7 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 4932                                        
KEYWDS    DNA-BINDING, PEPTIDASE, CYSTEINE PROTEASE, REGULATORY FACTOR,         
KEYWDS   2 BLEOMYCIN HYDROLASE, RING PROTEIN, DNA-BINDING PROTEIN, DNA BINDING  
KEYWDS   3 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.JOSHUA-TOR,H.E.XU,S.A.JOHNSTON,D.C.REES                             
REVDAT   4   07-FEB-24 1GCB    1       KEYWDS REMARK LINK                       
REVDAT   3   13-JUL-11 1GCB    1       VERSN                                    
REVDAT   2   24-FEB-09 1GCB    1       VERSN                                    
REVDAT   1   15-OCT-95 1GCB    0                                                
JRNL        AUTH   L.JOSHUA-TOR,H.E.XU,S.A.JOHNSTON,D.C.REES                    
JRNL        TITL   CRYSTAL STRUCTURE OF A CONSERVED PROTEASE THAT BINDS DNA:    
JRNL        TITL 2 THE BLEOMYCIN HYDROLASE, GAL6.                               
JRNL        REF    SCIENCE                       V. 269   945 1995              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   7638617                                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   H.E.XU,S.A.JOHNSTON                                          
REMARK   1  TITL   YEAST BLEOMYCIN HYDROLASE IS A DNA-BINDING CYSTEINE          
REMARK   1  TITL 2 PROTEASE: IDENTIFICATION, PURIFICATION, BIOCHEMICAL          
REMARK   1  TITL 3 CHARACTERIZATION                                             
REMARK   1  REF    J.BIOL.CHEM.                  V. 269 21177 1994              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 30018                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.274                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
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           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
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            : 3653                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 25                                      
REMARK   3   SOLVENT ATOMS            : 238                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.380                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.180                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  FOR RESIDUE LEU 452 THE ELECTRON DENSITY IS LARGER THAN             
REMARK   3  EXPECTED.                                                           
REMARK   4                                                                      
REMARK   4 1GCB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000173513.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL; NULL                         
REMARK 200  TEMPERATURE           (KELVIN) : NULL; NULL                         
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; N                               
REMARK 200  RADIATION SOURCE               : SSRL; NULL                         
REMARK 200  BEAMLINE                       : BL7-1; NULL                        
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL; NULL                         
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.08; 1.54                         
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE; IMAGE PLATE           
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH; RIGAKU RAXIS II       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MSC, CCP4                          
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31451                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.200                              
REMARK 200  R MERGE                    (I) : 0.07400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL; NULL                                     
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z                                              
REMARK 290      10555   -Y,-X,-Z+1/2                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       44.94000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       44.94000            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       44.94000            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       44.94000            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       44.94000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       44.94000            
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 300 REMARK: SYMMETRY                                                     
REMARK 300  THE CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS PRESENTED             
REMARK 300  BELOW GENERATE THE SUBUNITS OF THE POLYMERIC MOLECULE.              
REMARK 300                                                                      
REMARK 300  APPLIED TO RESIDUES:           2 ..       453                       
REMARK 300                                                                      
REMARK 300   IDENTITY MATRIX                                                    
REMARK 300                                                                      
REMARK 300  SYMMETRY1   1  1.000000  0.000000  0.000000        0.00000          
REMARK 300  SYMMETRY2   1  0.000000  1.000000  0.000000        0.00000          
REMARK 300  SYMMETRY3   1  0.000000  0.000000  1.000000        0.00000          
REMARK 300  SYMMETRY1   2  1.000000  0.000000  0.000000        0.00000          
REMARK 300  SYMMETRY2   2  0.000000  1.000000  0.000000        0.00000          
REMARK 300  SYMMETRY3   2  0.000000  0.000000  1.000000        0.00000          
REMARK 300  APPLIED TO RESIDUES:           2 ..       453                       
REMARK 300                                                                      
REMARK 300   MONOMER 2 OF HEXAMER                                               
REMARK 300                                                                      
REMARK 300  SYMMETRY1   3  0.000000 -1.000000  0.000000        1.00000          
REMARK 300  SYMMETRY2   3  1.000000 -1.000000  0.000000        0.00000          
REMARK 300  SYMMETRY3   3  0.000000  0.000000  1.000000        0.00000          
REMARK 300  SYMMETRY1   4 -0.500000 -0.866000  0.000000      151.15000          
REMARK 300  SYMMETRY2   4  0.866000 -0.500000  0.000000        0.00000          
REMARK 300  SYMMETRY3   4  0.000000  0.000000  1.000000        0.00000          
REMARK 300  APPLIED TO RESIDUES:           2 ..       453                       
REMARK 300                                                                      
REMARK 300   MONOMER 3 OF HEXAMER                                               
REMARK 300                                                                      
REMARK 300  SYMMETRY1   5 -1.000000  1.000000  0.000000        1.00000          
REMARK 300  SYMMETRY2   5 -1.000000  0.000000  0.000000        1.00000          
REMARK 300  SYMMETRY3   5  0.000000  0.000000  1.000000        0.00000          
REMARK 300  SYMMETRY1   6 -0.500000  0.866000  0.000000       75.58000          
REMARK 300  SYMMETRY2   6 -0.866000 -0.500000  0.000000      130.90000          
REMARK 300  SYMMETRY3   6  0.000000  0.000000  1.000000        0.00000          
REMARK 300  APPLIED TO RESIDUES:           2 ..       453                       
REMARK 300                                                                      
REMARK 300   MONOMER 4 OF HEXAMER                                               
REMARK 300                                                                      
REMARK 300  SYMMETRY1   7  0.000000 -1.000000  0.000000        1.00000          
REMARK 300  SYMMETRY2   7 -1.000000  0.000000  0.000000        1.00000          
REMARK 300  SYMMETRY3   7  0.000000  0.000000 -1.000000        0.50000          
REMARK 300  SYMMETRY1   8  0.500000 -0.866000  0.000000       75.58000          
REMARK 300  SYMMETRY2   8 -0.866000 -0.500000  0.000000      130.90000          
REMARK 300  SYMMETRY3   8  0.000000  0.000000 -1.000000       44.94000          
REMARK 300  APPLIED TO RESIDUES:           2 ..       453                       
REMARK 300                                                                      
REMARK 300   MONOMER 5 OF HEXAMER (DIMER PARTNER OF MONOMER 1)                  
REMARK 300                                                                      
REMARK 300  SYMMETRY1   9  1.000000  0.000000  0.000000        0.00000          
REMARK 300  SYMMETRY2   9  1.000000 -1.000000  0.000000        0.00000          
REMARK 300  SYMMETRY3   9  0.000000  0.000000 -1.000000        0.50000          
REMARK 300  SYMMETRY1  10  0.500000  0.866000  0.000000        0.00000          
REMARK 300  SYMMETRY2  10  0.866000 -0.500000  0.000000        0.00000          
REMARK 300  SYMMETRY3  10  0.000000  0.000000 -1.000000       44.94000          
REMARK 300  APPLIED TO RESIDUES:           2 ..       453                       
REMARK 300                                                                      
REMARK 300   MONOMER 6 OF HEXAMER                                               
REMARK 300                                                                      
REMARK 300  SYMMETRY1  11 -1.000000  1.000000  0.000000        1.00000          
REMARK 300  SYMMETRY2  11  0.000000  1.000000  0.000000        0.00000          
REMARK 300  SYMMETRY3  11  0.000000  0.000000 -1.000000        0.50000          
REMARK 300  SYMMETRY1  12 -1.000000  0.000000  0.000000      151.15000          
REMARK 300  SYMMETRY2  12  0.000000  1.000000  0.000000        0.00000          
REMARK 300  SYMMETRY3  12  0.000000  0.000000 -1.000000       44.94000          
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 42180 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 95990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -742.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000      151.15000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000       75.57500            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000      130.89974            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.500000 -0.866025  0.000000       75.57500            
REMARK 350   BIOMT2   4 -0.866025 -0.500000  0.000000      130.89974            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000       44.94000            
REMARK 350   BIOMT1   5 -1.000000  0.000000  0.000000      151.15000            
REMARK 350   BIOMT2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   5  0.000000  0.000000 -1.000000       44.94000            
REMARK 350   BIOMT1   6  0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   6  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   6  0.000000  0.000000 -1.000000       44.94000            
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     1                                                      
REMARK 465     LYS A   454                                                      
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C  SSEQI                                                     
REMARK 475     GLU A   380                                                      
REMARK 475     THR A   381                                                      
REMARK 475     SER A   382                                                      
REMARK 475     LYS A   383                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU A   89   CD   OE1  OE2                                       
REMARK 480     LYS A   93   NZ                                                  
REMARK 480     ARG A  174   NE   CZ   NH1  NH2                                  
REMARK 480     GLU A  197   CB   CG   CD   OE1  OE2                             
REMARK 480     ARG A  198   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS A  281   CD   CE   NZ                                        
REMARK 480     LYS A  309   CE   NZ                                             
REMARK 480     LYS A  313   CG   CD   CE   NZ                                   
REMARK 480     ASN A  423   CG   OD1  ND2                                       
REMARK 480     LYS A  427   CD   CE   NZ                                        
REMARK 480     GLU A  428   CB   CG   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    SER A  61       91.03    -66.16                                   
REMARK 500    LYS A  68     -144.72     58.55                                   
REMARK 500    TYR A 163      101.53   -166.82                                   
REMARK 500    ALA A 172       68.43   -153.48                                   
REMARK 500    ARG A 287       -9.63     60.17                                   
REMARK 500    ASN A 290      -49.28   -139.50                                   
REMARK 500    GLU A 380       79.81    -66.95                                   
REMARK 500    THR A 381      -83.20   -174.30                                   
REMARK 500    SER A 382       18.40   -162.88                                   
REMARK 500    LYS A 383     -138.90    -97.79                                   
REMARK 500    SER A 435     -139.27    -83.47                                   
REMARK 500    GLU A 438       91.02    -58.87                                   
REMARK 500    LEU A 452     -159.39    -49.04                                   
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                              HG A 902  HG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  55   OG1                                                    
REMARK 620 2 CYS A 376   SG   50.0                                              
REMARK 620 3 VAL A 378   N   108.6 125.7                                        
REMARK 620 4  HG A 903  HG   113.6  64.8 118.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              HG A 904  HG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  73   SG                                                     
REMARK 620 2 ALA A 453   O    69.2                                              
REMARK 620 N                    1                                               
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 IN THE SHEET RECORDS BELOW STRAND 7 OF SHEET B IS REPEATED           
REMARK 700 IN SHEET C BECAUSE IT TAKES PART IN BOTH SHEETS.                     
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: CAT                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 901                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 902                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 903                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 904                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 851                 
DBREF  1GCB A    1   454  UNP    Q01532   BLH1_YEAST       1    454             
SEQRES   1 A  454  MET SER SER SER ILE ASP ILE SER LYS ILE ASN SER TRP          
SEQRES   2 A  454  ASN LYS GLU PHE GLN SER ASP LEU THR HIS GLN LEU ALA          
SEQRES   3 A  454  THR THR VAL LEU LYS ASN TYR ASN ALA ASP ASP ALA LEU          
SEQRES   4 A  454  LEU ASN LYS THR ARG LEU GLN LYS GLN ASP ASN ARG VAL          
SEQRES   5 A  454  PHE ASN THR VAL VAL SER THR ASP SER THR PRO VAL THR          
SEQRES   6 A  454  ASN GLN LYS SER SER GLY ARG CYS TRP LEU PHE ALA ALA          
SEQRES   7 A  454  THR ASN GLN LEU ARG LEU ASN VAL LEU SER GLU LEU ASN          
SEQRES   8 A  454  LEU LYS GLU PHE GLU LEU SER GLN ALA TYR LEU PHE PHE          
SEQRES   9 A  454  TYR ASP LYS LEU GLU LYS ALA ASN TYR PHE LEU ASP GLN          
SEQRES  10 A  454  ILE VAL SER SER ALA ASP GLN ASP ILE ASP SER ARG LEU          
SEQRES  11 A  454  VAL GLN TYR LEU LEU ALA ALA PRO THR GLU ASP GLY GLY          
SEQRES  12 A  454  GLN TYR SER MET PHE LEU ASN LEU VAL LYS LYS TYR GLY          
SEQRES  13 A  454  LEU ILE PRO LYS ASP LEU TYR GLY ASP LEU PRO TYR SER          
SEQRES  14 A  454  THR THR ALA SER ARG LYS TRP ASN SER LEU LEU THR THR          
SEQRES  15 A  454  LYS LEU ARG GLU PHE ALA GLU THR LEU ARG THR ALA LEU          
SEQRES  16 A  454  LYS GLU ARG SER ALA ASP ASP SER ILE ILE VAL THR LEU          
SEQRES  17 A  454  ARG GLU GLN MET GLN ARG GLU ILE PHE ARG LEU MET SER          
SEQRES  18 A  454  LEU PHE MET ASP ILE PRO PRO VAL GLN PRO ASN GLU GLN          
SEQRES  19 A  454  PHE THR TRP GLU TYR VAL ASP LYS ASP LYS LYS ILE HIS          
SEQRES  20 A  454  THR ILE LYS SER THR PRO LEU GLU PHE ALA SER LYS TYR          
SEQRES  21 A  454  ALA LYS LEU ASP PRO SER THR PRO VAL SER LEU ILE ASN          
SEQRES  22 A  454  ASP PRO ARG HIS PRO TYR GLY LYS LEU ILE LYS ILE ASP          
SEQRES  23 A  454  ARG LEU GLY ASN VAL LEU GLY GLY ASP ALA VAL ILE TYR          
SEQRES  24 A  454  LEU ASN VAL ASP ASN GLU THR LEU SER LYS LEU VAL VAL          
SEQRES  25 A  454  LYS ARG LEU GLN ASN ASN LYS ALA VAL PHE PHE GLY SER          
SEQRES  26 A  454  HIS THR PRO LYS PHE MET ASP LYS LYS THR GLY VAL MET          
SEQRES  27 A  454  ASP ILE GLU LEU TRP ASN TYR PRO ALA ILE GLY TYR ASN          
SEQRES  28 A  454  LEU PRO GLN GLN LYS ALA SER ARG ILE ARG TYR HIS GLU          
SEQRES  29 A  454  SER LEU MET THR HIS ALA MET LEU ILE THR GLY CYS HIS          
SEQRES  30 A  454  VAL ASP GLU THR SER LYS LEU PRO LEU ARG TYR ARG VAL          
SEQRES  31 A  454  GLU ASN SER TRP GLY LYS ASP SER GLY LYS ASP GLY LEU          
SEQRES  32 A  454  TYR VAL MET THR GLN LYS TYR PHE GLU GLU TYR CYS PHE          
SEQRES  33 A  454  GLN ILE VAL VAL ASP ILE ASN GLU LEU PRO LYS GLU LEU          
SEQRES  34 A  454  ALA SER LYS PHE THR SER GLY LYS GLU GLU PRO ILE VAL          
SEQRES  35 A  454  LEU PRO ILE TRP ASP PRO MET GLY ALA LEU ALA LYS              
HET    SO4  A 801       5                                                       
HET    SO4  A 802       5                                                       
HET    SO4  A 803       5                                                       
HET     HG  A 901       1                                                       
HET     HG  A 902       1                                                       
HET     HG  A 903       1                                                       
HET     HG  A 904       1                                                       
HET    GOL  A 851       6                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM      HG MERCURY (II) ION                                                 
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  SO4    3(O4 S 2-)                                                   
FORMUL   5   HG    4(HG 2+)                                                     
FORMUL   9  GOL    C3 H8 O3                                                     
FORMUL  10  HOH   *238(H2 O)                                                    
HELIX    1   1 ILE A    7  SER A   19  1                                  13    
HELIX    2   2 LEU A   21  LEU A   30  1                                  10    
HELIX    3   3 ALA A   35  LEU A   39  1                                   5    
HELIX    4   4 LYS A   42  GLN A   48  1                                   7    
HELIX    5   5 CYS A   73  GLU A   89  1                                  17    
HELIX    6   6 GLN A   99  SER A  121  1                                  23    
HELIX    7   7 ARG A  129  ALA A  136  1                                   8    
HELIX    8   8 TYR A  145  TYR A  155  1                                  11    
HELIX    9   9 LYS A  160  LEU A  162  5                                   3    
HELIX   10  10 TYR A  168  THR A  171  1                                   4    
HELIX   11  11 ARG A  174  GLU A  197  1                                  24    
HELIX   12  12 SER A  203  PHE A  223  1                                  21    
HELIX   13  13 PRO A  253  LYS A  259  1                                   7    
HELIX   14  14 ASN A  304  GLN A  316  1                                  13    
HELIX   15  15 TYR A  345  ILE A  348  5                                   4    
HELIX   16  16 LYS A  356  ARG A  361  1                                   6    
HELIX   17  17 GLN A  408  TYR A  414  1                                   7    
HELIX   18  18 ILE A  422  GLU A  424  5                                   3    
HELIX   19  19 LYS A  427  THR A  434  1                                   8    
SHEET    1   A 2 GLN A 234  VAL A 240  0                                        
SHEET    2   A 2 ILE A 246  THR A 252 -1  N  SER A 251   O  PHE A 235           
SHEET    1   B11 ILE A 441  LEU A 443  0                                        
SHEET    2   B11 LEU A 282  ILE A 285  1  N  LYS A 284   O  ILE A 441           
SHEET    3   B11 ILE A 298  ASN A 301 -1  N  TYR A 299   O  ILE A 283           
SHEET    4   B11 PRO A 268  ILE A 272  1  N  SER A 270   O  LEU A 300           
SHEET    5   B11 CYS A 415  ASP A 421 -1  N  VAL A 420   O  VAL A 269           
SHEET    6   B11 VAL A 321  SER A 325 -1  N  GLY A 324   O  PHE A 416           
SHEET    7   B11 HIS A 369  HIS A 377 -1  N  ILE A 373   O  VAL A 321           
SHEET    8   B11 ARG A 387  GLU A 391 -1  N  GLU A 391   O  LEU A 372           
SHEET    9   B11 LEU A 403  THR A 407 -1  N  MET A 406   O  TYR A 388           
SHEET   10   B11 GLY A 336  ASP A 339  1  N  MET A 338   O  VAL A 405           
SHEET   11   B11 PHE A 330  LYS A 333 -1  N  ASP A 332   O  VAL A 337           
SHEET    1   C 2 THR A  55  VAL A  57  0                                        
SHEET    2   C 2 HIS A 369  HIS A 377 -1  N  CYS A 376   O  THR A  55           
LINK         OG1 THR A  55                HG    HG A 902     1555   1555  3.24  
LINK         SG  CYS A  73                HG    HG A 904     1555   1555  2.12  
LINK         SG  CYS A 376                HG    HG A 902     1555   1555  2.19  
LINK         SG  CYS A 376                HG    HG A 903     1555   1555  2.61  
LINK         N   VAL A 378                HG    HG A 902     1555   1555  3.15  
LINK         SG  CYS A 415                HG    HG A 901     1555   1555  2.53  
LINK         O   ALA A 453                HG    HG A 904     1555   1555  3.52  
LINK        HG    HG A 902                HG    HG A 903     1555   1555  2.64  
CISPEP   1 THR A   62    PRO A   63          0        -0.03                     
CISPEP   2 THR A  327    PRO A  328          0        -0.52                     
SITE     1 CAT  3 CYS A  73  HIS A 369  ASN A 392                               
SITE     1 AC1  5 ASN A  66  GLY A 395  LYS A 396  HOH A 675                    
SITE     2 AC1  5 HOH A 714                                                     
SITE     1 AC2  6 ILE A 126  ARG A 192  LYS A 196  TYR A 362                    
SITE     2 AC2  6 HOH A 643  HOH A 644                                          
SITE     1 AC3  7 LYS A 175  SER A 178  PRO A 328  LYS A 329                    
SITE     2 AC3  7 HOH A 691  HOH A 697  HOH A 698                               
SITE     1 AC4  2 PHE A 411  CYS A 415                                          
SITE     1 AC5  4 THR A  55  CYS A 376  VAL A 378   HG A 903                    
SITE     1 AC6  4 VAL A 312  CYS A 376  PRO A 385   HG A 902                    
SITE     1 AC7  3 GLY A  71  CYS A  73  ALA A 453                               
SITE     1 AC8  8 GLN A  81  LEU A  82  ASN A  85  LYS A 262                    
SITE     2 AC8  8 ARG A 314  LYS A 319  ASP A 421  HOH A 684                    
CRYST1  151.150  151.150   89.880  90.00  90.00 120.00 P 63 2 2     12          
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      0.006616  0.003820  0.000000        0.00000                         
SCALE2      0.000000  0.007639  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011126        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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