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Database: PDB
Entry: 1HIZ
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Original site: 1HIZ 
HEADER    GLYCOSIDASE                             05-JAN-01   1HIZ              
TITLE     XYLANASE T6 (XT6) FROM BACILLUS STEAROTHERMOPHILUS                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDO-1,4-BETA-XYLANASE;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.2.1.8;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS STEAROTHERMOPHILUS;                    
SOURCE   3 ORGANISM_TAXID: 1422;                                                
SOURCE   4 STRAIN: NCIMB40221;                                                  
SOURCE   5 CELL: BACTERIA;                                                      
SOURCE   6 CELLULAR_LOCATION: EXTRA CELLULAR;                                   
SOURCE   7 GENE: XYNA;                                                          
SOURCE   8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  10 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  11 EXPRESSION_SYSTEM_CELL: BACTERIA;                                    
SOURCE  12 EXPRESSION_SYSTEM_CELLULAR_LOCATION: EXTRACELLULAR;                  
SOURCE  13 EXPRESSION_SYSTEM_VECTOR: PET9D                                      
KEYWDS    GLYCOSIDASE, XYLAN DEGRADATION, FAMILY 10, THERMOPHILE                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.SAINZ,A.TEPPLITSKY,V.STOJANOFF,A.THOMPSON,Y.SHOHAM,                 
AUTHOR   2 G.SHOHAM                                                             
REVDAT   4   24-FEB-09 1HIZ    1       VERSN                                    
REVDAT   3   06-MAY-04 1HIZ    1       JRNL                                     
REVDAT   2   23-MAR-04 1HIZ    1       AUTHOR JRNL                              
REVDAT   1   04-JAN-02 1HIZ    0                                                
JRNL        AUTH   A.TEPLITSKY,A.MECHALY,V.STOJANOFF,G.SAINZ,G.GOLAN,           
JRNL        AUTH 2 H.FEINBERG,R.GILBOA,V.REILAND,G.ZOLOTNITSKY,                 
JRNL        AUTH 3 D.SHALLOM,A.THOMPSON,Y.SHOHAM,G.SHOHAM                       
JRNL        TITL   STRUCTURE DETERMINATION OF THE EXTRACELLULAR                 
JRNL        TITL 2 XYLANASE FROM GEOBACILLUS STEAROTHERMOPHILUS BY              
JRNL        TITL 3 SELENOMETHIONYL MAD PHASING                                  
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  60   836 2004              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   15103129                                                     
JRNL        DOI    10.1107/S0907444904004123                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.4  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.44                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2184699.83                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 35080                          
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 SET) : 0.158                           
REMARK   3   FREE R VALUE                     : 0.188                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.9                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 3461                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.55                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.0                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5046                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.188                        
REMARK   3   BIN FREE R VALUE                    : 0.221                        
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.4                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 584                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.009                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3071                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 29                                      
REMARK   3   SOLVENT ATOMS            : 630                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 28.4                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.9                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.62                                                 
REMARK   3    B22 (A**2) : 5.62                                                 
REMARK   3    B33 (A**2) : -11.24                                               
REMARK   3    B12 (A**2) : 4.47                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.20                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.18                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.25                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.23                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.3                             
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.5                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.90                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.20  ; 1.50                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.92  ; 2.00                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.25  ; 2.00                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.32  ; 2.50                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.375956                                             
REMARK   3   BSOL        : 60                                                   
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : M                                              
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : M                                              
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1HIZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  05-JAN-01.                 
REMARK 100 THE PDBE ID CODE IS EBI-5406.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-APR-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM14                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.88,0.9791,0.97                   
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35080                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.45                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.21200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 75.86                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS:                                          
REMARK 280  RESERVOIR: 1.5 M AMMONIUM SULFATE.                                  
REMARK 280  DROP : 5-6 MG/ML PROTEIN, 0.75 AMMONIUM SULFATE,                    
REMARK 280  8% (W/V) MPD                                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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       81.82000            
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       40.91000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       40.91000            
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       81.82000            
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 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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400  ENDOHYDROLYSIS OF 1,4-BETA-D-XYLOSIDIC LINKAGES IN XYLANS           
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     LYS A     2                                                      
REMARK 465     ASN A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     ASP A     5                                                      
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     SER A   6    OG                                                  
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    PRO A 360   C   -  N   -  CA  ANGL. DEV. =   9.8 DEGREES          
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  27       -1.31     76.90                                   
REMARK 500    ASN A  60      -30.25   -146.53                                   
REMARK 500    THR A  97      133.56     38.55                                   
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 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLA A1381                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A1382                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1383                 
DBREF  1HIZ A    2   380  UNP    P40943   XYN1_BACST      29    407             
SEQRES   1 A  379  LYS ASN ALA ASP SER TYR ALA LYS LYS PRO HIS ILE SER          
SEQRES   2 A  379  ALA LEU ASN ALA PRO GLN LEU ASP GLN ARG TYR LYS ASN          
SEQRES   3 A  379  GLU PHE THR ILE GLY ALA ALA VAL GLU PRO TYR GLN LEU          
SEQRES   4 A  379  GLN ASN GLU LYS ASP VAL GLN MET LEU LYS ARG HIS PHE          
SEQRES   5 A  379  ASN SER ILE VAL ALA GLU ASN VAL MET LYS PRO ILE SER          
SEQRES   6 A  379  ILE GLN PRO GLU GLU GLY LYS PHE ASN PHE GLU GLN ALA          
SEQRES   7 A  379  ASP ARG ILE VAL LYS PHE ALA LYS ALA ASN GLY MET ASP          
SEQRES   8 A  379  ILE ARG PHE HIS THR LEU VAL TRP HIS SER GLN VAL PRO          
SEQRES   9 A  379  GLN TRP PHE PHE LEU ASP LYS GLU GLY LYS PRO MET VAL          
SEQRES  10 A  379  ASN GLU THR ASP PRO VAL LYS ARG GLU GLN ASN LYS GLN          
SEQRES  11 A  379  LEU LEU LEU LYS ARG LEU GLU THR HIS ILE LYS THR ILE          
SEQRES  12 A  379  VAL GLU ARG TYR LYS ASP ASP ILE LYS TYR TRP ASP VAL          
SEQRES  13 A  379  VAL ASN GLU VAL VAL GLY ASP ASP GLY LYS LEU ARG ASN          
SEQRES  14 A  379  SER PRO TRP TYR GLN ILE ALA GLY ILE ASP TYR ILE LYS          
SEQRES  15 A  379  VAL ALA PHE GLN ALA ALA ARG LYS TYR GLY GLY ASP ASN          
SEQRES  16 A  379  ILE LYS LEU TYR MET ASN ASP TYR ASN THR GLU VAL GLU          
SEQRES  17 A  379  PRO LYS ARG THR ALA LEU TYR ASN LEU VAL LYS GLN LEU          
SEQRES  18 A  379  LYS GLU GLU GLY VAL PRO ILE ASP GLY ILE GLY HIS GLN          
SEQRES  19 A  379  SER HIS ILE GLN ILE GLY TRP PRO SER GLU ALA GLU ILE          
SEQRES  20 A  379  GLU LYS THR ILE ASN MET PHE ALA ALA LEU GLY LEU ASP          
SEQRES  21 A  379  ASN GLN ILE THR GLU LEU ASP VAL SER MET TYR GLY TRP          
SEQRES  22 A  379  PRO PRO ARG ALA TYR PRO THR TYR ASP ALA ILE PRO LYS          
SEQRES  23 A  379  GLN LYS PHE LEU ASP GLN ALA ALA ARG TYR ASP ARG LEU          
SEQRES  24 A  379  PHE LYS LEU TYR GLU LYS LEU SER ASP LYS ILE SER ASN          
SEQRES  25 A  379  VAL THR PHE TRP GLY ILE ALA ASP ASN HIS THR TRP LEU          
SEQRES  26 A  379  ASP SER ARG ALA ASP VAL TYR TYR ASP ALA ASN GLY ASN          
SEQRES  27 A  379  VAL VAL VAL ASP PRO ASN ALA PRO TYR ALA LYS VAL GLU          
SEQRES  28 A  379  LYS GLY LYS GLY LYS ASP ALA PRO PHE VAL PHE GLY PRO          
SEQRES  29 A  379  ASP TYR LYS VAL LYS PRO ALA TYR TRP ALA ILE ILE ASP          
SEQRES  30 A  379  HIS LYS                                                      
HET    GLA  A1381      12                                                       
HET    GLC  A1382      12                                                       
HET    SO4  A1383       5                                                       
HETNAM     GLA ALPHA D-GALACTOSE                                                
HETNAM     GLC ALPHA-D-GLUCOSE                                                  
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2  GLA    C6 H12 O6                                                    
FORMUL   3  GLC    C6 H12 O6                                                    
FORMUL   4  SO4    O4 S 2-                                                      
FORMUL   5  HOH   *630(H2 O1)                                                   
HELIX    1   1 GLN A   20  TYR A   25  1                                   6    
HELIX    2   2 GLU A   36  GLN A   41  5                                   6    
HELIX    3   3 ASN A   42  PHE A   53  1                                  12    
HELIX    4   4 LYS A   63  GLN A   68  1                                   6    
HELIX    5   5 PHE A   76  ASN A   89  1                                  14    
HELIX    6   6 PRO A  105  PHE A  109  5                                   5    
HELIX    7   7 MET A  117  GLU A  120  5                                   4    
HELIX    8   8 ASP A  122  LYS A  149  1                                  28    
HELIX    9   9 SER A  171  GLY A  178  1                                   8    
HELIX   10  10 ILE A  179  GLY A  194  1                                  16    
HELIX   11  11 PRO A  210  GLU A  225  1                                  16    
HELIX   12  12 SER A  244  ALA A  257  1                                  14    
HELIX   13  13 THR A  281  ILE A  285  5                                   5    
HELIX   14  14 PRO A  286  LEU A  307  1                                  22    
HELIX   15  15 THR A  324  ALA A  330  5                                   7    
HELIX   16  16 LYS A  370  ASP A  378  1                                   9    
SHEET    1  AA 7 VAL A  99  TRP A 100  0                                        
SHEET    2  AA 7 TYR A 154  ASN A 159  1  O  VAL A 157   N  VAL A  99           
SHEET    3  AA 7 ASP A  92  PHE A  95  1  O  ILE A  93   N  TYR A 154           
SHEET    4  AA 7 SER A  55  ALA A  58  1  O  ILE A  56   N  ARG A  94           
SHEET    5  AA 7 THR A  30  VAL A  35  1  O  ALA A  33   N  VAL A  57           
SHEET    6  AA 7 ILE A 311  PHE A 316  1  O  SER A 312   N  THR A  30           
SHEET    7  AA 7 ASP A 261  VAL A 269  1  O  ASN A 262   N  SER A 312           
SHEET    1  AB 5 VAL A  99  TRP A 100  0                                        
SHEET    2  AB 5 TYR A 154  ASN A 159  1  O  VAL A 157   N  VAL A  99           
SHEET    3  AB 5 LYS A 198  ASP A 203  1  O  LYS A 198   N  TRP A 155           
SHEET    4  AB 5 GLY A 231  HIS A 234  1  O  GLY A 231   N  MET A 201           
SHEET    5  AB 5 ASP A 261  VAL A 269  1  O  ASP A 261   N  ILE A 232           
SHEET    1  AC 3 VAL A 340  VAL A 341  0                                        
SHEET    2  AC 3 VAL A 332  TYR A 334 -1  O  TYR A 333   N  VAL A 341           
SHEET    3  AC 3 LYS A 350  GLU A 352 -1  O  LYS A 350   N  TYR A 334           
CISPEP   1 GLU A  209    PRO A  210          0         0.36                     
CISPEP   2 TRP A  242    PRO A  243          0        -0.39                     
CISPEP   3 TRP A  274    PRO A  275          0        -0.14                     
SITE     1 AC1  8 TRP A 100  GLU A 266  TRP A 325  HOH A2358                    
SITE     2 AC1  8 HOH A2472  HOH A2616  HOH A2617  HOH A2618                    
SITE     1 AC2 14 TYR A 204  ASN A 205  GLN A 239  TRP A 242                    
SITE     2 AC2 14 TRP A 274  ARG A 329  HOH A2442  HOH A2620                    
SITE     3 AC2 14 HOH A2621  HOH A2622  HOH A2623  HOH A2624                    
SITE     4 AC2 14 HOH A2625  HOH A2626                                          
SITE     1 AC3  3 ARG A 147  HOH A2628  HOH A2629                               
CRYST1  112.870  112.870  122.730  90.00  90.00 120.00 P 32 2 1      6          
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      0.008860  0.005115  0.000000        0.00000                         
SCALE2      0.000000  0.010230  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008148        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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