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Database: PDB
Entry: 1OHZ
LinkDB: 1OHZ
Original site: 1OHZ 
HEADER    CELL ADHESION                           04-JUN-03   1OHZ              
TITLE     COHESIN-DOCKERIN COMPLEX FROM THE CELLULOSOME OF                      
TITLE    2 CLOSTRIDIUM THERMOCELLUM                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELLULOSOMAL SCAFFOLDING PROTEIN A;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 181-340;                                          
COMPND   5 SYNONYM: CELLULOSOMAL GLYCOPROTEIN S1/SL, CELLULOSE                  
COMPND   6  INTEGRATING PROTEIN A, COHESIN;                                     
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: ENDO-1,4-BETA-XYLANASE Y;                                  
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: RESIDUES 733-791;                                          
COMPND  12 SYNONYM: XYLANASE Y, XYLY, 1,4-BETA-D-XYLAN                          
COMPND  13  XYLANOHYDROLASE Y;                                                  
COMPND  14 EC: 3.2.1.8;                                                         
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM THERMOCELLUM;                       
SOURCE   3 ORGANISM_TAXID: 1515;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: CLOSTRIDIUM THERMOCELLUM;                       
SOURCE   8 ORGANISM_TAXID: 1515;                                                
SOURCE   9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CELL ADHESION, COHESIN/DOCKERIN COMPLEX, COHESIN, DOCKERIN,           
KEYWDS   2 CELLULOSOME, CLOSTRIDIUM THERMOCELLUM, CELLULOSE                     
KEYWDS   3 DEGRADATION                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.L.CARVALHO,F.M.V.DIAS,J.A.M.PRATES,L.M.A.FERREIRA,                  
AUTHOR   2 H.J.GILBERT,G.J.DAVIES,M.J.ROMAO,C.M.G.A.FONTES                      
REVDAT   3   24-FEB-09 1OHZ    1       VERSN                                    
REVDAT   2   04-DEC-03 1OHZ    1       JRNL                                     
REVDAT   1   20-NOV-03 1OHZ    0                                                
JRNL        AUTH   A.L.CARVALHO,F.M.V.DIAS,J.A.M.PRATES,                        
JRNL        AUTH 2 L.M.A.FERREIRA,H.J.GILBERT,G.J.DAVIES,M.J.ROMAO,             
JRNL        AUTH 3 C.M.G.A.FONTES                                               
JRNL        TITL   CELLULOSOME ASSEMBLY REVEALED BY THE CRYSTAL                 
JRNL        TITL 2 STRUCTURE OF THE COHESIN-DOCKERIN COMPLEX                    
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 100 13809 2003              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   14623971                                                     
JRNL        DOI    10.1073/PNAS.1936124100                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.2  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.2                            
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 17                             
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100                            
REMARK   3   NUMBER OF REFLECTIONS             : 15291                          
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) : 0.21132                         
REMARK   3   R VALUE            (WORKING SET) : 0.20974                         
REMARK   3   FREE R VALUE                     : 0.24175                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 810                             
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1469                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 15                                      
REMARK   3   SOLVENT ATOMS            : 115                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1OHZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  04-JUN-03.                 
REMARK 100 THE PDBE ID CODE IS EBI-12841.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 110.0                              
REMARK 200  PH                             : 7.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM30A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.976288                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16170                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.201                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 17.040                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 11.900                             
REMARK 200  R MERGE                    (I) : 0.07200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 12.00                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.30900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1ANU                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 3                           
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z+1/2,-X+1/2,-Y                                         
REMARK 290       7555   -Z+1/2,-X,Y+1/2                                         
REMARK 290       8555   -Z,X+1/2,-Y+1/2                                         
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z+1/2,-X+1/2                                         
REMARK 290      11555   Y+1/2,-Z+1/2,-X                                         
REMARK 290      12555   -Y+1/2,-Z,X+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       48.95300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       48.95300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       48.95300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       48.95300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       48.95300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       48.95300            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000       48.95300            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000       48.95300            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000       48.95300            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000       48.95300            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000       48.95300            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000       48.95300            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000       48.95300            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000       48.95300            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000       48.95300            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000       48.95300            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000       48.95300            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000       48.95300            
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 300 DETAILS:THIS MAY BE THE RESULT OF CRYSTAL PACKING                    
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000      -48.95300            
REMARK 350   BIOMT3   2  0.000000 -1.000000  0.000000      -48.95300            
REMARK 350   BIOMT1   3  0.000000  1.000000  0.000000       48.95300            
REMARK 350   BIOMT2   3  0.000000  0.000000 -1.000000      -48.95300            
REMARK 350   BIOMT3   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375      HOH B2009  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B2014  LIES ON A SPECIAL POSITION.                          
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     ALA A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     ASP A     4                                                      
REMARK 465     ASN A   145                                                      
REMARK 465     ALA A   146                                                      
REMARK 465     THR A   147                                                      
REMARK 465     PRO A   148                                                      
REMARK 465     THR A   149                                                      
REMARK 465     LYS A   150                                                      
REMARK 465     GLY A   151                                                      
REMARK 465     ALA A   152                                                      
REMARK 465     THR A   153                                                      
REMARK 465     PRO A   154                                                      
REMARK 465     THR A   155                                                      
REMARK 465     ASN A   156                                                      
REMARK 465     THR A   157                                                      
REMARK 465     ALA A   158                                                      
REMARK 465     THR A   159                                                      
REMARK 465     PRO A   160                                                      
REMARK 465     THR A   161                                                      
REMARK 465     LYS A   162                                                      
REMARK 465     MET B     0                                                      
REMARK 465     ARG B    57                                                      
REMARK 465     VAL B    58                                                      
REMARK 465     ILE B    59                                                      
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     GLU A  22    OE1  OE2                                            
REMARK 470     SER A  32    OG                                                  
REMARK 470     LYS A  33    CD   CE   NZ                                        
REMARK 470     ASP A  76    OD1  OD2                                            
REMARK 470     LYS A  78    CE   NZ                                             
REMARK 470     LYS A  97    CE   NZ                                             
REMARK 470     LYS A 103    CE   NZ                                             
REMARK 470     LYS A 109    CD   CE   NZ                                        
REMARK 470     LEU A 129    CD1  CD2                                            
REMARK 470     LYS A 133    CG   CD   CE   NZ                                   
REMARK 470     SER B  42    OG                                                  
REMARK 470     LEU B  56    CD1  CD2                                            
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 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    ASN A  64       77.64   -114.34                                   
REMARK 500    PHE A 124       77.82   -162.97                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
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                              CA B1057  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B   4   OD1                                                    
REMARK 620 2 HOH B2004   O    84.6                                              
REMARK 620 3 ASP B  13   OD1  80.2  94.8                                        
REMARK 620 4 ASP B  13   OD2 125.0  81.4  48.7                                  
REMARK 620 5 ASP B   6   OD1  79.6  84.9 159.7 150.2                            
REMARK 620 6 ASP B   2   OD1  91.4 173.3  89.8 105.3  89.1                      
REMARK 620 7 THR B   8   O   158.5  96.7 120.9  76.3  79.1  85.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B1058  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B  42   O                                                      
REMARK 620 2 ASP B  47   OD2  77.5                                              
REMARK 620 3 HOH B2036   O   107.2  81.2                                        
REMARK 620 4 ASP B  36   OD1  84.5 112.2 164.3                                  
REMARK 620 5 ASP B  38   OD1 160.6 121.9  79.3  86.4                            
REMARK 620 6 ASP B  47   OD1 121.2  49.2  89.3  93.6  76.4                      
REMARK 620 7 ASN B  40   OD1  85.0 151.3  82.6  88.2  77.6 153.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A1145                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A1146                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B1057                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B1058                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1059                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1147                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1ANU   RELATED DB: PDB                                   
REMARK 900  COHESIN-2 DOMAIN OF THE CELLULOSOME FROM                            
REMARK 900  CLOSTRIDIUM THERMOCELLUM                                            
REMARK 900 RELATED ID: 1AOH   RELATED DB: PDB                                   
REMARK 900  SINGLE COHESIN DOMAIN FROM THE SCAFFOLDING                          
REMARK 900  PROTEIN CIPA OFTHE CLOSTRIDIUM THERMOCELLUM                         
REMARK 900  CELLULOSOME                                                         
REMARK 900 RELATED ID: 1NBC   RELATED DB: PDB                                   
REMARK 900  BACTERIAL TYPE 3A CELLULOSE-BINDING DOMAIN                          
REMARK 900 RELATED ID: 1DYO   RELATED DB: PDB                                   
REMARK 900  XYLAN-BINDING DOMAIN FROM CBM 22, FORMALLY                          
REMARK 900  X6B DOMAIN                                                          
REMARK 900 RELATED ID: 1GKK   RELATED DB: PDB                                   
REMARK 900  FERULOYL ESTERASE DOMAIN OF XYNY FROM                               
REMARK 900  CLOSTRIDIUM THERMOCELLUM                                            
REMARK 900 RELATED ID: 1GKL   RELATED DB: PDB                                   
REMARK 900  S954A MUTANT OF THE FERULOYL ESTERASE MODULE                        
REMARK 900   FROM CLOSTRIDIUM THERMOCELLUM COMPLEXED WITH                       
REMARK 900  FERULIC ACID                                                        
REMARK 900 RELATED ID: 1H6X   RELATED DB: PDB                                   
REMARK 900  THE ROLE OF CONSERVED AMONI ACIDS IN THE                            
REMARK 900  CLEFT OF THE C-TERMINAL FAMILY 22                                   
REMARK 900  CARBOHYDRATE BINDING MODULE OF CLOSTRIDIUM                          
REMARK 900  THERMOCELLUM XYN10B IN LIGAND BINDING                               
REMARK 900 RELATED ID: 1H6Y   RELATED DB: PDB                                   
REMARK 900  THE ROLE OF CONSERVED AMONI ACIDS IN THE                            
REMARK 900  CLEFT OF THE C-TERMINAL FAMILY 22                                   
REMARK 900  CARBOHYDRATE BINDING MODULE OF CLOSTRIDIUM                          
REMARK 900  THERMOCELLUM XYN10B IN LIGAND BINDING                               
DBREF  1OHZ A    1     2  PDB    1OHZ     1OHZ             1      2             
DBREF  1OHZ A    3   162  UNP    Q06851   CIPA_CLOTM     181    340             
DBREF  1OHZ B    0     0  PDB    1OHZ     1OHZ             0      0             
DBREF  1OHZ B    1    59  UNP    P51584   XYNY_CLOTM     733    791             
SEQRES   1 A  162  MET ALA SER ASP GLY VAL VAL VAL GLU ILE GLY LYS VAL          
SEQRES   2 A  162  THR GLY SER VAL GLY THR THR VAL GLU ILE PRO VAL TYR          
SEQRES   3 A  162  PHE ARG GLY VAL PRO SER LYS GLY ILE ALA ASN CYS ASP          
SEQRES   4 A  162  PHE VAL PHE ARG TYR ASP PRO ASN VAL LEU GLU ILE ILE          
SEQRES   5 A  162  GLY ILE ASP PRO GLY ASP ILE ILE VAL ASP PRO ASN PRO          
SEQRES   6 A  162  THR LYS SER PHE ASP THR ALA ILE TYR PRO ASP ARG LYS          
SEQRES   7 A  162  ILE ILE VAL PHE LEU PHE ALA GLU ASP SER GLY THR GLY          
SEQRES   8 A  162  ALA TYR ALA ILE THR LYS ASP GLY VAL PHE ALA LYS ILE          
SEQRES   9 A  162  ARG ALA THR VAL LYS SER SER ALA PRO GLY TYR ILE THR          
SEQRES  10 A  162  PHE ASP GLU VAL GLY GLY PHE ALA ASP ASN ASP LEU VAL          
SEQRES  11 A  162  GLU GLN LYS VAL SER PHE ILE ASP GLY GLY VAL ASN VAL          
SEQRES  12 A  162  GLY ASN ALA THR PRO THR LYS GLY ALA THR PRO THR ASN          
SEQRES  13 A  162  THR ALA THR PRO THR LYS                                      
SEQRES   1 B   60  MET GLY ASP VAL ASN GLY ASP GLY THR ILE ASN SER THR          
SEQRES   2 B   60  ASP LEU THR MET LEU LYS ARG SER VAL LEU ARG ALA ILE          
SEQRES   3 B   60  THR LEU THR ASP ASP ALA LYS ALA ARG ALA ASP VAL ASP          
SEQRES   4 B   60  LYS ASN GLY SER ILE ASN SER THR ASP VAL LEU LEU LEU          
SEQRES   5 B   60  SER ARG TYR LEU LEU ARG VAL ILE                              
HET    NO3  A1145       4                                                       
HET    NO3  A1146       4                                                       
HET     CA  B1057       1                                                       
HET     CA  B1058       1                                                       
HET     CL  B1059       1                                                       
HET    EDO  A1147       4                                                       
HETNAM     NO3 NITRATE ION                                                      
HETNAM      CA CALCIUM ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  NO3    2(N O3 1-)                                                   
FORMUL   5   CA    2(CA 2+)                                                     
FORMUL   7   CL    CL 1-                                                        
FORMUL   8  EDO    C2 H6 O2                                                     
FORMUL   9  HOH   *115(H2 O1)                                                   
HELIX    1   1 ASN A   64  SER A   68  1                                   5    
HELIX    2   2 ASN B   10  LEU B   22  1                                  13    
HELIX    3   3 THR B   28  ASP B   36  1                                   9    
HELIX    4   4 ASN B   44  LEU B   55  1                                  12    
SHEET    1  AA 5 LEU A  49  PRO A  56  0                                        
SHEET    2  AA 5 GLY A  99  VAL A 108 -1  O  LYS A 103   N  ASP A  55           
SHEET    3  AA 5 THR A  20  ARG A  28 -1  O  VAL A  21   N  ALA A 106           
SHEET    4  AA 5 VAL A   6  ILE A  10 -1  O  VAL A   7   N  ARG A  28           
SHEET    5  AA 5 VAL A 134  ILE A 137  1  O  SER A 135   N  VAL A   8           
SHEET    1  AB 6 LYS A  12  VAL A  13  0                                        
SHEET    2  AB 6 GLY A 139  VAL A 141  1  O  GLY A 140   N  VAL A  13           
SHEET    3  AB 6 GLY A 114  ALA A 125 -1  O  GLY A 114   N  VAL A 141           
SHEET    4  AB 6 ASN A  37  ARG A  43 -1  O  ASN A  37   N  ALA A 125           
SHEET    5  AB 6 ILE A  79  ALA A  85 -1  O  ILE A  80   N  PHE A  42           
SHEET    6  AB 6 PHE A  69  TYR A  74 -1  O  ASP A  70   N  LEU A  83           
LINK        CA    CA B1057                 OD1 ASN B   4     1555   1555  2.42  
LINK        CA    CA B1057                 O   HOH B2004     1555   1555  2.53  
LINK        CA    CA B1057                 OD1 ASP B  13     1555   1555  2.71  
LINK        CA    CA B1057                 OD2 ASP B  13     1555   1555  2.47  
LINK        CA    CA B1057                 OD1 ASP B   6     1555   1555  2.50  
LINK        CA    CA B1057                 OD1 ASP B   2     1555   1555  2.33  
LINK        CA    CA B1057                 O   THR B   8     1555   1555  2.31  
LINK        CA    CA B1058                 OD2 ASP B  47     1555   1555  2.57  
LINK        CA    CA B1058                 O   HOH B2036     1555   1555  2.40  
LINK        CA    CA B1058                 OD1 ASP B  36     1555   1555  2.39  
LINK        CA    CA B1058                 OD1 ASP B  38     1555   1555  2.38  
LINK        CA    CA B1058                 OD1 ASP B  47     1555   1555  2.60  
LINK        CA    CA B1058                 OD1 ASN B  40     1555   1555  2.38  
LINK        CA    CA B1058                 O   SER B  42     1555   1555  2.23  
SITE     1 AC1  6 TYR A  74  PRO A  75  ASP A  76  ARG A  77                    
SITE     2 AC1  6 EDO A1147  THR B  26                                          
SITE     1 AC2  8 THR A  14  ASN A 142  VAL A 143  GLY A 144                    
SITE     2 AC2  8 HOH A2072  ALA B  33  ARG B  34  LYS B  39                    
SITE     1 AC3  6 ASP B   2  ASN B   4  ASP B   6  THR B   8                    
SITE     2 AC3  6 ASP B  13  HOH B2004                                          
SITE     1 AC4  6 ASP B  36  ASP B  38  ASN B  40  SER B  42                    
SITE     2 AC4  6 ASP B  47  HOH B2036                                          
SITE     1 AC5  2 ARG B  19  HOH B2014                                          
SITE     1 AC6  3 ARG A  77  NO3 A1145  HOH A2073                               
CRYST1   97.906   97.906   97.906  90.00  90.00  90.00 P 21 3       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      0.010214  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010214  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010214        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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