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Database: PDB
Entry: 1GOQ
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Original site: 1GOQ 
HEADER    HYDROLASE                               23-OCT-01   1GOQ              
TITLE     THERMOSTABLE XYLANASE I FROM THERMOASCUS AURANTIACUS - ROOM           
TITLE    2 TEMPERATURE XYLOBIOSE COMPLEX                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDO-1,4-BETA-XYLANASE;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: XYLANASE, 1,4-BETA-D-XYLAN XYLANOHYDROLASE;                 
COMPND   5 EC: 3.2.1.8                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOASCUS AURANTIACUS;                        
SOURCE   3 ORGANISM_TAXID: 5087                                                 
KEYWDS    XYLANASE, FAMILY 10, PLANT CELL WALL DEGRADATION, HYDROLASE           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.LO LEGGIO,S.LARSEN                                                  
REVDAT   3   22-OCT-14 1GOQ    1       REMARK VERSN  FORMUL                     
REVDAT   2   24-FEB-09 1GOQ    1       VERSN                                    
REVDAT   1   07-DEC-01 1GOQ    0                                                
JRNL        AUTH   L.LO LEGGIO,S.KALOGIANNIS,K.ECKERT,S.C.M.TEIXEIRA,           
JRNL        AUTH 2 M.K.BHAT,C.ANDREI,R.W.PICKERSGILL,S.LARSEN                   
JRNL        TITL   SUBSTRATE SPECIFICITY AND SUBSITE MOBILITY IN T.             
JRNL        TITL 2 AURANTIACUS XYLANASE 10A                                     
JRNL        REF    FEBS LETT.                    V. 509   303 2001              
JRNL        REFN                   ISSN 0014-5793                               
JRNL        PMID   11741607                                                     
JRNL        DOI    10.1016/S0014-5793(01)03177-5                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   S.TEIXEIRA,L.LO LEGGIO,R.PICKERSGILL,C.CARDIN                
REMARK   1  TITL   ANISOTROPIC REFINEMENT OF THE STRUCTURE OF                   
REMARK   1  TITL 2 THERMOASCUS AURANTIACUS XYLANASE I                           
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  57   385 2001              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1  PMID   11223515                                                     
REMARK   1  DOI    10.1107/S0907444900019089                                    
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   L.LO LEGGIO,S.KALOGIANNIS,M.K.BHAT,R.W.PICKERSGILL           
REMARK   1  TITL   HIGH RESOLUTION STRUCTURE AND SEQUENCE OF T.                 
REMARK   1  TITL 2 AURANTIACUS XYLANASE I: IMPLICATIONS FOR THE                 
REMARK   1  TITL 3 EVOLUTION OF THERMOSTABILITY IN FAMILY 10                    
REMARK   1  TITL 4 XYLANASES AND ENZYMES WITH BETA/ALPHA BARREL                 
REMARK   1  TITL 5 ARCHITECTURE                                                 
REMARK   1  REF    PROTEINS                      V.  36   295 1999              
REMARK   1  REFN                   ISSN 0887-3585                               
REMARK   1  PMID   10409823                                                     
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   R.PICKERSGILL,G.HARRIS,L.LO LEGGIO,O.MAYANS,                 
REMARK   1  AUTH 2 J.JENKINS                                                    
REMARK   1  TITL   SUPERFAMILIES: THE 4/7 SUPERFAMILY OF BETA/                  
REMARK   1  TITL 2 ALPHA-BARREL GLYCOSIDASES AND THE RIGHT-HANDED               
REMARK   1  TITL 3 PARALLEL BETA-HELIX SUPERFAMILY                              
REMARK   1  REF    BIOCHEM.SOC.TRANS.            V.  26   190 1998              
REMARK   1  REFN                   ISSN 0300-5127                               
REMARK   1  PMID   9649746                                                      
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   L.LO LEGGIO                                                  
REMARK   1  TITL   STRUCTURE SOLUTION OF THERMOASCUS AURANTIACUS                
REMARK   1  TITL 2 XYLANASE. STRUCTURAL STUDIES OF XYLANASES AND                
REMARK   1  TITL 3 ENDOGLUCANASES                                               
REMARK   1  EDIT   UNIVERSITY OF LONDON                                         
REMARK   1  REF    STRUCTURAL STUDIES OF                  194 1997              
REMARK   1  REF  2 XYLANASES AND ENDOGLUCANASES                                 
REMARK   1  PUBL   LONDON, UK : UNIVERSITY OF LONDON                            
REMARK   1  REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.8  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 5.0                            
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 100000.000                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.1000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 84.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 19293                          
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) : 0.167                           
REMARK   3   FREE R VALUE                     : 0.212                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.4                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1922                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.91                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 44.7                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1543                         
REMARK   3   BIN R VALUE           (WORKING SET) : .237                         
REMARK   3   BIN FREE R VALUE                    : .256                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.6                          
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 164                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.02                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2304                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 66                                      
REMARK   3   SOLVENT ATOMS            : 131                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.8                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.266                                                
REMARK   3    B22 (A**2) : -.115                                                
REMARK   3    B33 (A**2) : -1.151                                               
REMARK   3    B12 (A**2) : .000                                                 
REMARK   3    B13 (A**2) : .186                                                 
REMARK   3    B23 (A**2) : .000                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.18                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.16                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.0                             
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.22                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.13                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.0065                          
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.0                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.70                            
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) : 1.494 ; 1.50                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.116 ; 2.00                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.647 ; 2.00                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.728 ; 2.50                 
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  : PARAM19.SOL                                    
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH19.SOL                                     
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1GOQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-OCT-01.                  
REMARK 100 THE PDBE ID CODE IS EBI-8745.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 293.0                              
REMARK 200  PH                             : 7.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : R-AXIS                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20709                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.0                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : 0.17000                            
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) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.83                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 37.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER METHODS              
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: 1GOK                                                 
REMARK 200                                                                      
REMARK 200 REMARK: THE PH OF CRYSTALLIZATION WAS NOT BUFFERED                   
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 32.9                                       
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROPS CONTAINING 1:1             
REMARK 280  RATIO OF 20-30 MG/ML PROTEIN SOLUTION AND RESERVOIR                 
REMARK 280  SOLUTION (12 % TO 25 % PEG 6,000). THE CRYSTAL WAS SOAKED           
REMARK 280  IN 0.5 M XYLOBIOSE                                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       29.78000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 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 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     GLN A 303    N    CA   C    O    CB   CG   CD   OE1  NE2         
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    THR A  22     -175.62   -171.83                                   
REMARK 500    ASN A  47      -23.19   -143.85                                   
REMARK 500    ASP A 164       83.84   -153.55                                   
REMARK 500    GLU A 237       47.90   -140.98                                   
REMARK 500    VAL A 269      -65.54   -105.29                                   
REMARK 500    THR A 280       67.34     33.67                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN 10-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A 11-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XYP A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XYP A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XYP A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XYP A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XYP A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XYP A 406                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1FXM   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE THERMOASCUS                                
REMARK 900  AURANTIACUS XYLANASE I                                              
REMARK 900 RELATED ID: 1GOK   RELATED DB: PDB                                   
REMARK 900  THERMOSTABLE XYLANASE I FROM THERMOASCUS                            
REMARK 900  AURANTIACUS                                                         
REMARK 900 RELATED ID: 1GOM   RELATED DB: PDB                                   
REMARK 900  THERMOSTABLE XYLANASE I FROM THERMOASCUS                            
REMARK 900  AURANTIACUS                                                         
REMARK 900 RELATED ID: 1GOO   RELATED DB: PDB                                   
REMARK 900  THERMOSTABLE XYLANASE I FROM THERMOASCUS                            
REMARK 900  AURANTIACUS                                                         
REMARK 900 RELATED ID: 1GOQ   RELATED DB: PDB                                   
REMARK 900  THERMOSTABLE XYLANASE I FROM THERMOASCUS                            
REMARK 900  AURANTIACUS                                                         
REMARK 900 RELATED ID: 1GOR   RELATED DB: PDB                                   
REMARK 900  THERMOSTABLE XYLANASE I FROM THERMOASCUS                            
REMARK 900  AURANTIACUS - XYLOBIOSE COMPLEX AT 100 K                            
REMARK 900 RELATED ID: 1TAX   RELATED DB: PDB                                   
REMARK 900  THERMOSTABLE XYLANASE I FROM THERMOASCUS                            
REMARK 900  AURANTIACUS                                                         
REMARK 900 RELATED ID: 1TIX   RELATED DB: PDB                                   
REMARK 900  THERMOSTABLE XYLANASE I FROM THERMOASCUS                            
REMARK 900  AURANTIACUS                                                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 RESIDUES 1-26 REFER TO THE SIGNAL PEPTIDE                            
REMARK 999 IT IS NOT KNOWN IF GLN 303 IS PRESENT IN THE CRYSTAL                 
DBREF  1GOQ A    1   303  UNP    P23360   XYNA_THEAU      27    329             
SEQRES   1 A  303  PCA ALA ALA GLN SER VAL ASP GLN LEU ILE LYS ALA ARG          
SEQRES   2 A  303  GLY LYS VAL TYR PHE GLY VAL ALA THR ASP GLN ASN ARG          
SEQRES   3 A  303  LEU THR THR GLY LYS ASN ALA ALA ILE ILE GLN ALA ASP          
SEQRES   4 A  303  PHE GLY GLN VAL THR PRO GLU ASN SER MET LYS TRP ASP          
SEQRES   5 A  303  ALA THR GLU PRO SER GLN GLY ASN PHE ASN PHE ALA GLY          
SEQRES   6 A  303  ALA ASP TYR LEU VAL ASN TRP ALA GLN GLN ASN GLY LYS          
SEQRES   7 A  303  LEU ILE ARG GLY HIS THR LEU VAL TRP HIS SER GLN LEU          
SEQRES   8 A  303  PRO SER TRP VAL SER SER ILE THR ASP LYS ASN THR LEU          
SEQRES   9 A  303  THR ASN VAL MET LYS ASN HIS ILE THR THR LEU MET THR          
SEQRES  10 A  303  ARG TYR LYS GLY LYS ILE ARG ALA TRP ASP VAL VAL ASN          
SEQRES  11 A  303  GLU ALA PHE ASN GLU ASP GLY SER LEU ARG GLN THR VAL          
SEQRES  12 A  303  PHE LEU ASN VAL ILE GLY GLU ASP TYR ILE PRO ILE ALA          
SEQRES  13 A  303  PHE GLN THR ALA ARG ALA ALA ASP PRO ASN ALA LYS LEU          
SEQRES  14 A  303  TYR ILE ASN ASP TYR ASN LEU ASP SER ALA SER TYR PRO          
SEQRES  15 A  303  LYS THR GLN ALA ILE VAL ASN ARG VAL LYS GLN TRP ARG          
SEQRES  16 A  303  ALA ALA GLY VAL PRO ILE ASP GLY ILE GLY SER GLN THR          
SEQRES  17 A  303  HIS LEU SER ALA GLY GLN GLY ALA GLY VAL LEU GLN ALA          
SEQRES  18 A  303  LEU PRO LEU LEU ALA SER ALA GLY THR PRO GLU VAL ALA          
SEQRES  19 A  303  ILE THR GLU LEU ASP VAL ALA GLY ALA SER PRO THR ASP          
SEQRES  20 A  303  TYR VAL ASN VAL VAL ASN ALA CYS LEU ASN VAL GLN SER          
SEQRES  21 A  303  CYS VAL GLY ILE THR VAL TRP GLY VAL ALA ASP PRO ASP          
SEQRES  22 A  303  SER TRP ARG ALA SER THR THR PRO LEU LEU PHE ASP GLY          
SEQRES  23 A  303  ASN PHE ASN PRO LYS PRO ALA TYR ASN ALA ILE VAL GLN          
SEQRES  24 A  303  ASP LEU GLN GLN                                              
MODRES 1GOQ PCA A    1  GLN  PYROGLUTAMIC ACID                                  
HET    PCA  A   1       8                                                       
HET    XYP  A 401       9                                                       
HET    XYP  A 402      10                                                       
HET    XYP  A 403      10                                                       
HET    XYP  A 404      10                                                       
HET    XYP  A 405       9                                                       
HET    XYP  A 406      10                                                       
HETNAM     PCA PYROGLUTAMIC ACID                                                
HETNAM     XYP BETA-D-XYLOPYRANOSE                                              
FORMUL   1  PCA    C5 H7 N O3                                                   
FORMUL   2  XYP    6(C5 H10 O5)                                                 
FORMUL   6  HOH   *131(H2 O)                                                    
HELIX    1   1 SER A    5  ARG A   13  1                                   9    
HELIX    2   2 ASP A   23  THR A   28  1                                   6    
HELIX    3   3 LYS A   31  PHE A   40  1                                  10    
HELIX    4   4 LYS A   50  GLU A   55  1                                   6    
HELIX    5   5 PHE A   63  ASN A   76  1                                  14    
HELIX    6   6 PRO A   92  SER A   97  1                                   6    
HELIX    7   7 ASP A  100  TYR A  119  1                                  20    
HELIX    8   8 THR A  142  GLY A  149  1                                   8    
HELIX    9   9 ASP A  151  ASP A  164  1                                  14    
HELIX   10  10 TYR A  181  ALA A  197  1                                  17    
HELIX   11  11 GLN A  214  SER A  227  1                                  14    
HELIX   12  12 SER A  244  VAL A  258  1                                  15    
HELIX   13  13 ASP A  271  SER A  274  5                                   4    
HELIX   14  14 ARG A  276  THR A  280  5                                   5    
HELIX   15  15 LYS A  291  GLN A  302  1                                  12    
SHEET    1  AA11 TYR A  17  THR A  22  0                                        
SHEET    2  AA11 CYS A 261  VAL A 266  1  O  ILE A 264   N  GLY A  19           
SHEET    3  AA11 GLU A 232  VAL A 240  1  O  VAL A 233   N  VAL A 262           
SHEET    4  AA11 GLY A 203  SER A 206  1  O  ILE A 204   N  ALA A 234           
SHEET    5  AA11 LYS A 168  ASP A 173  1  O  LEU A 169   N  GLY A 203           
SHEET    6  AA11 ALA A 125  ASN A 130  1  O  TRP A 126   N  TYR A 170           
SHEET    7  AA11 LEU A  79  VAL A  86  1  O  GLY A  82   N  ASP A 127           
SHEET    8  AA11 GLN A  42  PRO A  45  1  O  VAL A  43   N  ARG A  81           
SHEET    9  AA11 TYR A  17  THR A  22  1  O  VAL A  20   N  THR A  44           
SHEET   10  AA11 CYS A 261  VAL A 266  1  O  ILE A 264   N  GLY A  19           
SHEET   11  AA11 TYR A  17  THR A  22  1  O  TYR A  17   N  ILE A 264           
SSBOND   1 CYS A  255    CYS A  261                          1555   1555  2.03  
LINK         C   PCA A   1                 N   ALA A   2     1555   1555  1.33  
LINK         C1B XYP A 401                 O4B XYP A 402     1555   1555  1.43  
LINK         C1B XYP A 405                 O4B XYP A 406     1555   1555  1.42  
CISPEP   1 HIS A   83    THR A   84          0        -1.66                     
SITE     1 AC1  8 GLU A  46  ASN A  47  LYS A  50  GLN A  90                    
SITE     2 AC1  8 TRP A 267  XYP A 402  HOH A2021  HOH A2128                    
SITE     1 AC2 10 LYS A  50  HIS A  83  ASN A 130  GLU A 131                    
SITE     2 AC2 10 GLN A 207  GLU A 237  TRP A 267  TRP A 275                    
SITE     3 AC2 10 XYP A 401  XYP A 403                                          
SITE     1 AC3  8 TRP A  87  GLU A 131  TYR A 174  GLN A 207                    
SITE     2 AC3  8 HIS A 209  TRP A 275  XYP A 402  HOH A2129                    
SITE     1 AC4  5 ASP A  23  GLN A  24  ASN A  25  ASN A  47                    
SITE     2 AC4  5 SER A  48                                                     
SITE     1 AC5  3 GLN A 259  XYP A 406  HOH A2130                               
SITE     1 AC6  6 ARG A  13  GLY A  14  LYS A  15  GLN A 259                    
SITE     2 AC6  6 XYP A 405  HOH A2131                                          
CRYST1   46.060   59.560   51.130  90.00 110.80  90.00 P 1 21 1      2          
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      0.021711  0.000000  0.008247        0.00000                         
SCALE2      0.000000  0.016790  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020921        0.00000                         
HETATM    1  N   PCA A   1      10.646   4.262  27.147  1.00 35.35           N  
HETATM    2  CA  PCA A   1      10.171   2.861  27.240  1.00 33.02           C  
HETATM    3  CB  PCA A   1      11.419   2.000  27.145  1.00 33.52           C  
HETATM    4  CG  PCA A   1      12.582   2.982  26.990  1.00 39.23           C  
HETATM    5  CD  PCA A   1      11.964   4.362  27.006  1.00 38.95           C  
HETATM    6  OE  PCA A   1      12.604   5.421  26.902  1.00 44.95           O  
HETATM    7  C   PCA A   1       9.392   2.559  28.548  1.00 32.21           C  
HETATM    8  O   PCA A   1       9.806   2.931  29.642  1.00 32.72           O  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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