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Database: PDB
Entry: 1V0M
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Original site: 1V0M 
HEADER    HYDROLASE                               31-MAR-04   1V0M              
TITLE     XYLANASE XYN10A FROM STREPTOMYCES LIVIDANS IN COMPLEX                 
TITLE    2 WITH XYLOBIO-DEOXYNOJIRIMYCIN AT PH 7.5                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDO-1,4-BETA-XYLANASE A;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CATALYTIC MODULE, RESIDUES 42-354;                         
COMPND   5 SYNONYM: XYLANASE A, 1,4-BETA-D-XYLAN XYLANOHYDROLASE A;             
COMPND   6 EC: 3.2.1.8;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOMYCES LIVIDANS;                          
SOURCE   3 ORGANISM_TAXID: 1916;                                                
SOURCE   4 EXPRESSION_SYSTEM: STREPTOMYCES LIVIDANS;                            
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 1916;                                       
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: IAF 19                                     
KEYWDS    GLYCOSIDE HYDROLASE FAMILY 10, XYLANASE, XYLAN DEGRADATION,           
KEYWDS   2 DEOXYNOJIRIMYCIN, HYDROLASE                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.M.GLOSTER,S.J.WILLIAMS,S.ROBERTS,C.A.TARLING,J.WICKI,               
AUTHOR   2 S.G.WITHERS,G.J.DAVIES                                               
REVDAT   2   24-FEB-09 1V0M    1       VERSN                                    
REVDAT   1   16-AUG-04 1V0M    0                                                
JRNL        AUTH   T.M.GLOSTER,S.J.WILLIAMS,S.ROBERTS,C.A.TARLING,              
JRNL        AUTH 2 J.WICKI,S.G.WITHERS,G.J.DAVIES                               
JRNL        TITL   ATOMIC RESOLUTION ANALYSES OF THE BINDING OF                 
JRNL        TITL 2 XYLOBIOSE-DERIVED DEOXYNOJIRIMYCIN AND ISOFAGOMINE           
JRNL        TITL 3 TO XYLANASE XYN10A                                           
JRNL        REF    CHEM.COMMUN.(CAMB.)           V.  16  1794 2004              
JRNL        REFN                   ISSN 1359-7345                               
JRNL        PMID   15306887                                                     
JRNL        DOI    10.1039/B405152A                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.07 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0000                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.07                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.65                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 105254                         
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) : 0.099                           
REMARK   3   R VALUE            (WORKING SET) : 0.098                           
REMARK   3   FREE R VALUE                     : 0.121                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5530                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.07                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.10                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6306                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1940                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 325                          
REMARK   3   BIN FREE R VALUE                    : 0.2200                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2386                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 23                                      
REMARK   3   SOLVENT ATOMS            : 568                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 7.70                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.92000                                              
REMARK   3    B22 (A**2) : -0.95000                                             
REMARK   3    B33 (A**2) : 0.03000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.021         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.023         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.014         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.627         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.986                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.980                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2464 ; 0.014 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2120 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3351 ; 1.652 ; 1.907       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4936 ; 1.100 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   301 ; 6.293 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   125 ;32.261 ;24.240       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   392 ;10.979 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;14.688 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   370 ; 0.122 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2781 ; 0.011 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   526 ; 0.000 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   528 ; 0.231 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2234 ; 0.220 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1281 ; 0.095 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   286 ; 0.160 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    10 ; 0.113 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    39 ; 0.310 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.215 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1936 ; 1.653 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   623 ; 0.644 ; 1.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2434 ; 1.995 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1130 ; 2.672 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   917 ; 3.377 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS THE LAST 11 AMINO ACIDS ARE TOO DISORDERED TO      
REMARK   3  BE BUILT IN DENSITY.                                                
REMARK   4                                                                      
REMARK   4 1V0M COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-MAR-04.                  
REMARK 100 THE PDBE ID CODE IS EBI-11791.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-SEP-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934                              
REMARK 200  MONOCHROMATOR                  : DIAMOND (111), GE(220)             
REMARK 200  OPTICS                         : SAGITALLY FOCUSING GE(220)         
REMARK 200                                   AND A MULTILAYER                   
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 117436                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.070                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.4                               
REMARK 200  DATA REDUNDANCY                : 5.700                              
REMARK 200  R MERGE                    (I) : 0.06300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 25.5400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.07                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.93                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.940                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1OD8                                       
REMARK 200                                                                      
REMARK 200 REMARK: STRUCTURE ISOMORPHOUS WITH STARTING MODEL                    
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 36.5                                       
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.0                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM IMIDAZOLE, PH 7.5                 
REMARK 280  16% PEG 5K MME, 5% ISOPROPANOL                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
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                                                                      
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       33.44200            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       42.89450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       23.04050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       42.89450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       33.44200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       23.04050            
REMARK 290   SMTRY3   4  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 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  CONTRIBUTES TO THE HYDROLYSIS OF HEMICELLULOSE, WHICH IS            
REMARK 400  THE MAJOR COMPONENT OF PLANT CELL-WALLS.                            
REMARK 400  XLNA AND XLNB SEEM TO ACT SEQUENTIALLY ON THE SUBSTRATE             
REMARK 400  TO YIELD XYLOBIOSE AND XYLOSE AS CARBON SOURCES.                    
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     ASP A   304                                                      
REMARK 465     SER A   305                                                      
REMARK 465     SER A   306                                                      
REMARK 465     GLU A   307                                                      
REMARK 465     PRO A   308                                                      
REMARK 465     PRO A   309                                                      
REMARK 465     ALA A   310                                                      
REMARK 465     ASP A   311                                                      
REMARK 465     GLY A   312                                                      
REMARK 465     GLY A   313                                                      
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     ARG A  66    CZ   NH1  NH2                                       
REMARK 470     GLY A 303    CA   C    O                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG A 190   CZ A  ARG A 190   NH2A    3.183                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    ARG A  79   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ARG A 102   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES          
REMARK 500    ARG A 102   NH1 -  CZ  -  NH2 ANGL. DEV. =  -7.7 DEGREES          
REMARK 500    ARG A 190   NE  -  CZ  -  NH2 ANGL. DEV. = -62.2 DEGREES          
REMARK 500    ARG A 190   NH1 -  CZ  -  NH2 ANGL. DEV. = -39.6 DEGREES          
REMARK 500    ARG A 259   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500 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  45      -22.09   -141.37                                   
REMARK 500    GLU A 236       40.68   -146.13                                   
REMARK 500    VAL A 268      -76.00   -100.09                                   
REMARK 500    THR A 279       62.15     34.68                                   
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 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 XDN A1303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XYP A1304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A1305                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1E0V   RELATED DB: PDB                                   
REMARK 900  XYLANASE 10A FROM SREPTOMYCES LIVIDANS.                             
REMARK 900  CELLOBIOSYL-ENZYME INTERMEDIATE AT 1.7 A                            
REMARK 900 RELATED ID: 1E0W   RELATED DB: PDB                                   
REMARK 900  XYLANASE 10A FROM SREPTOMYCES LIVIDANS. NATIVE                      
REMARK 900   STRUCTURE AT 1.2 ANGSTROM RESOLUTION                               
REMARK 900 RELATED ID: 1E0X   RELATED DB: PDB                                   
REMARK 900  XYLANASE 10A FROM SREPTOMYCES LIVIDANS.                             
REMARK 900  XYLOBIOSYL-ENZYME INTERMEDIATE AT 1.65 A                            
REMARK 900 RELATED ID: 1KNL   RELATED DB: PDB                                   
REMARK 900  STREPTOMYCES LIVIDANS XYLAN BINDING DOMAIN                          
REMARK 900  CBM13                                                               
REMARK 900 RELATED ID: 1KNM   RELATED DB: PDB                                   
REMARK 900  STREPTOMYCES LIVIDANS XYLAN BINDING DOMAIN                          
REMARK 900  CBM13 IN COMPLEXWITH LACTOSE                                        
REMARK 900 RELATED ID: 1MC9   RELATED DB: PDB                                   
REMARK 900  STREPROMYCES LIVIDANS XYLAN BINDING DOMAIN                          
REMARK 900  CBM13 IN COMPLEXWITH XYLOPENTAOSE                                   
REMARK 900 RELATED ID: 1OD8   RELATED DB: PDB                                   
REMARK 900  XYLANASE XYN10A FROM STREPTOMYCES LIVIDANS IN                       
REMARK 900   COMPLEX WITH XYLOBIO-ISOFAGOMINE LACTAM                            
REMARK 900 RELATED ID: 1V0L   RELATED DB: PDB                                   
REMARK 900  XYLANASE XYN10A FROM STREPTOMYCES LIVIDANS IN                       
REMARK 900   COMPLEX WITH XYLOBIO-ISOFAGOMINE AT PH 5.8                         
REMARK 900 RELATED ID: 1V0K   RELATED DB: PDB                                   
REMARK 900  XYLANASE XYN10A FROM STREPTOMYCES LIVIDANS IN                       
REMARK 900   COMPLEX WITH XYLOBIO-DEOXYNOJIRIMYCIN AT PH 5.8                    
REMARK 900 RELATED ID: 1V0N   RELATED DB: PDB                                   
REMARK 900  XYLANASE XYN10A FROM STREPTOMYCES LIVIDANS IN                       
REMARK 900   COMPLEX WITH XYLOBIO-ISOFAGOMINE AT PH 7.5                         
REMARK 900 RELATED ID: 1XAS   RELATED DB: PDB                                   
REMARK 900  1,4-BETA-D-XYLAN XYLANOHYDROLASE                                    
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE FIRST 41 RESIDUES IN THE DATABASE CORRESPOND                     
REMARK 999 TO THE SIGNAL PEPTIDE. THE NUMBERING USED IN THE                     
REMARK 999 PDB FILE IF AFTER CLEAVAGE OF THE SIGNAL PEPTIDE.                    
DBREF  1V0M A    1   313  UNP    P26514   XYNA_STRLI      42    354             
SEQRES   1 A  313  ALA GLU SER THR LEU GLY ALA ALA ALA ALA GLN SER GLY          
SEQRES   2 A  313  ARG TYR PHE GLY THR ALA ILE ALA SER GLY ARG LEU SER          
SEQRES   3 A  313  ASP SER THR TYR THR SER ILE ALA GLY ARG GLU PHE ASN          
SEQRES   4 A  313  MET VAL THR ALA GLU ASN GLU MET LYS ILE ASP ALA THR          
SEQRES   5 A  313  GLU PRO GLN ARG GLY GLN PHE ASN PHE SER SER ALA ASP          
SEQRES   6 A  313  ARG VAL TYR ASN TRP ALA VAL GLN ASN GLY LYS GLN VAL          
SEQRES   7 A  313  ARG GLY HIS THR LEU ALA TRP HIS SER GLN GLN PRO GLY          
SEQRES   8 A  313  TRP MET GLN SER LEU SER GLY SER ALA LEU ARG GLN ALA          
SEQRES   9 A  313  MET ILE ASP HIS ILE ASN GLY VAL MET ALA HIS TYR LYS          
SEQRES  10 A  313  GLY LYS ILE VAL GLN TRP ASP VAL VAL ASN GLU ALA PHE          
SEQRES  11 A  313  ALA ASP GLY SER SER GLY ALA ARG ARG ASP SER ASN LEU          
SEQRES  12 A  313  GLN ARG SER GLY ASN ASP TRP ILE GLU VAL ALA PHE ARG          
SEQRES  13 A  313  THR ALA ARG ALA ALA ASP PRO SER ALA LYS LEU CYS TYR          
SEQRES  14 A  313  ASN ASP TYR ASN VAL GLU ASN TRP THR TRP ALA LYS THR          
SEQRES  15 A  313  GLN ALA MET TYR ASN MET VAL ARG ASP PHE LYS GLN ARG          
SEQRES  16 A  313  GLY VAL PRO ILE ASP CYS VAL GLY PHE GLN SER HIS PHE          
SEQRES  17 A  313  ASN SER GLY SER PRO TYR ASN SER ASN PHE ARG THR THR          
SEQRES  18 A  313  LEU GLN ASN PHE ALA ALA LEU GLY VAL ASP VAL ALA ILE          
SEQRES  19 A  313  THR GLU LEU ASP ILE GLN GLY ALA PRO ALA SER THR TYR          
SEQRES  20 A  313  ALA ASN VAL THR ASN ASP CYS LEU ALA VAL SER ARG CYS          
SEQRES  21 A  313  LEU GLY ILE THR VAL TRP GLY VAL ARG ASP SER ASP SER          
SEQRES  22 A  313  TRP ARG SER GLU GLN THR PRO LEU LEU PHE ASN ASN ASP          
SEQRES  23 A  313  GLY SER LYS LYS ALA ALA TYR THR ALA VAL LEU ASP ALA          
SEQRES  24 A  313  LEU ASN GLY GLY ASP SER SER GLU PRO PRO ALA ASP GLY          
SEQRES  25 A  313  GLY                                                          
HET    XDN  A1303       9                                                       
HET    XYP  A1304       9                                                       
HET    IMD  A1305       5                                                       
HETNAM     XDN PIPERIDINE-3,4,5-TRIOL                                           
HETNAM     XYP BETA-D-XYLOPYRANOSE                                              
HETNAM     IMD IMIDAZOLE                                                        
HETSYN     XDN XYLOSE-DERIVED 1-DEOXY-NOJIRIMYCIN                               
FORMUL   2  XDN    C5 H11 N O3                                                  
FORMUL   2  XYP    C5 H10 O5                                                    
FORMUL   3  IMD    C3 H5 N2 1+                                                  
FORMUL   4  HOH   *568(H2 O1)                                                   
HELIX    1   1 THR A    4  GLN A   11  1                                   8    
HELIX    2   2 ALA A   21  LEU A   25  5                                   5    
HELIX    3   3 ASP A   27  PHE A   38  1                                  12    
HELIX    4   4 LYS A   48  GLU A   53  1                                   6    
HELIX    5   5 PHE A   61  ASN A   74  1                                  14    
HELIX    6   6 PRO A   90  SER A   95  1                                   6    
HELIX    7   7 SER A   97  TYR A  116  1                                  20    
HELIX    8   8 SER A  141  SER A  146  1                                   6    
HELIX    9   9 ASP A  149  ASP A  162  1                                  14    
HELIX   10  10 TRP A  179  GLY A  196  1                                  18    
HELIX   11  11 ASN A  217  ALA A  227  1                                  11    
HELIX   12  12 PRO A  243  ALA A  256  1                                  14    
HELIX   13  13 ASP A  270  SER A  273  5                                   4    
HELIX   14  14 ARG A  275  THR A  279  5                                   5    
HELIX   15  15 LYS A  290  ASN A  301  1                                  12    
SHEET    1  AA11 TYR A  15  ILE A  20  0                                        
SHEET    2  AA11 CYS A 260  VAL A 265  1  O  LEU A 261   N  TYR A  15           
SHEET    3  AA11 ASP A 231  ILE A 239  1  O  VAL A 232   N  LEU A 261           
SHEET    4  AA11 CYS A 201  PHE A 204  1  O  VAL A 202   N  ALA A 233           
SHEET    5  AA11 LYS A 166  ASP A 171  1  O  TYR A 169   N  GLY A 203           
SHEET    6  AA11 GLN A 122  ASN A 127  1  O  TRP A 123   N  CYS A 168           
SHEET    7  AA11 GLN A  77  ALA A  84  1  O  GLY A  80   N  ASP A 124           
SHEET    8  AA11 MET A  40  ALA A  43  1  O  VAL A  41   N  ARG A  79           
SHEET    9  AA11 TYR A  15  ILE A  20  1  O  THR A  18   N  THR A  42           
SHEET   10  AA11 CYS A 260  VAL A 265  1  O  LEU A 261   N  TYR A  15           
SHEET   11  AA11 TYR A  15  ILE A  20  1  O  TYR A  15   N  ILE A 263           
SSBOND   1 CYS A  168    CYS A  201                          1555   1555  2.02  
SSBOND   2 CYS A  168    CYS A  201                          1555   1555  2.03  
SSBOND   3 CYS A  254    CYS A  260                          1555   1555  2.09  
LINK         O4  XDN A1303                 C1B XYP A1304     1555   1555  1.42  
CISPEP   1 HIS A   81    THR A   82          0         0.68                     
SITE     1 AC1 13 LYS A  48  HIS A  81  TRP A  85  ASN A 127                    
SITE     2 AC1 13 GLU A 128  GLN A 205  GLU A 236  TRP A 266                    
SITE     3 AC1 13 TRP A 274  XYP A1304  HOH A2294  HOH A2414                    
SITE     4 AC1 13 HOH A2562                                                     
SITE     1 AC2 11 GLU A  44  ASN A  45  LYS A  48  GLN A  88                    
SITE     2 AC2 11 TRP A 266  TRP A 274  XDN A1303  HOH A2563                    
SITE     3 AC2 11 HOH A2564  HOH A2567  HOH A2568                               
SITE     1 AC3  9 SER A  12  GLY A  13  ARG A  14  LYS A 193                    
SITE     2 AC3  9 GLN A 194  GLY A 196  SER A 258  CYS A 260                    
SITE     3 AC3  9 HOH A2402                                                     
CRYST1   66.884   46.081   85.789  90.00  90.00  90.00 P 21 21 21    4          
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      0.014951  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.021701  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011656        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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