GenomeNet

Database: PDB
Entry: 2BNJ
LinkDB: 2BNJ
Original site: 2BNJ 
HEADER    HYDROLASE                               25-MAR-05   2BNJ              
TITLE     THE XYLANASE TA FROM THERMOASCUS AURANTIACUS UTILIZES                 
TITLE    2 ARABINOSE DECORATIONS OF XYLAN AS SIGNIFICANT SUBSTRATE              
TITLE    3 SPECIFICITY DETERMINANTS.                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDO-1,4-BETA-XYLANASE;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: FAMILY 10 XYLANASE, 1,4-BETA-D-XYLAN                        
COMPND   5  XYLANOHYDROLASE, TAXI;                                              
COMPND   6 EC: 3.2.1.8                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOASCUS AURANTIACUS;                        
SOURCE   3 ORGANISM_TAXID: 5087;                                                
SOURCE   4 VARIANT: MIECHE, IMI 216529                                          
KEYWDS    XYLANASE, GLYCOSIDASE, HYDROLASE, PYRROLIDONE CARBOXYLIC              
KEYWDS   2 ACID, XYLAN DEGRADATION                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.VARDAKOU,J.W.MURRAY,J.FLINT,P.CHRISTAKOPOULOS,R.J.LEWIS,            
AUTHOR   2 H.J.GILBERT                                                          
REVDAT   4   24-FEB-09 2BNJ    1       VERSN                                    
REVDAT   3   20-DEC-06 2BNJ    1       JRNL                                     
REVDAT   2   14-SEP-05 2BNJ    1       REMARK                                   
REVDAT   1   07-SEP-05 2BNJ    0                                                
JRNL        AUTH   M.VARDAKOU,J.FLINT,P.CHRISTAKOPOULOS,R.J.LEWIS,              
JRNL        AUTH 2 H.J.GILBERT,J.W.MURRAY                                       
JRNL        TITL   A FAMILY 10 THERMOASCUS AURANTIACUS XYLANASE                 
JRNL        TITL 2 UTILIZES ARABINOSE DECORATIONS OF XYLAN AS                   
JRNL        TITL 3 SIGNIFICANT SUBSTRATE SPECIFICITY DETERMINANTS.              
JRNL        REF    J.MOL.BIOL.                   V. 352  1060 2005              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   16140328                                                     
JRNL        DOI    10.1016/J.JMB.2005.07.051                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.6  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 63.12                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 34409                          
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) : 0.117                           
REMARK   3   R VALUE            (WORKING SET) : 0.115                           
REMARK   3   FREE R VALUE                     : 0.147                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1689                            
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) : 7.11                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 63.12                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 392                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1320                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 17                           
REMARK   3   BIN FREE R VALUE                    : 0.1440                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2313                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 49                                      
REMARK   3   SOLVENT ATOMS            : 596                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 12.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 7.60                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.09500                                              
REMARK   3    B22 (A**2) : -0.03700                                             
REMARK   3    B33 (A**2) : -0.05300                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00500                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.072         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.073         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.040         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.097         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.978                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.964                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2421 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3313 ; 1.409 ; 1.948       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   307 ; 6.181 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   108 ;34.519 ;25.370       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   364 ;11.513 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ;19.362 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   381 ; 0.078 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2724 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   513 ; 0.232 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1231 ; 0.179 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   422 ; 0.163 ; 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):     6 ; 0.166 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    50 ; 0.154 ; 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):  1941 ; 0.774 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2440 ; 0.979 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1082 ; 1.890 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   870 ; 2.473 ; 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 : MASK BULK SOLVENT                                    
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS.                                                   
REMARK   4                                                                      
REMARK   4 2BNJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-MAR-05.                  
REMARK 100 THE PDBE ID CODE IS EBI-22718.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-FEB-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : NULL                               
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          : RIGAKU                             
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 (RAXIS IV)             
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34409                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.450                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY                : 2.640                              
REMARK 200  R MERGE                    (I) : 0.03000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 25.1200                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.61                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.44                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.07000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 9.310                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1I1X                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 13.5% PEG 6K, 2.5MM FAX2,                
REMARK 280  4MG/ML TA PROTEIN.                                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       44.11200            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.73100            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       44.11200            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       24.73100            
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375      HOH A2295  LIES ON A SPECIAL POSITION.                          
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400  CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-BETA-D-XYLOSIDIC          
REMARK 400  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     GLN A   303                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLN A   302  -  O    HOH A  2586              2.12            
REMARK 500   O    HOH A  2360  -  O    HOH A  2364              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500                                                                      
REMARK 500   O    HOH A  2353     O    HOH A  2534     3445      2.14           
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 161   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 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  47      -24.26   -149.45                                   
REMARK 500    GLU A 237       43.51   -145.04                                   
REMARK 500    VAL A 269      -66.85   -100.30                                   
REMARK 500    THR A 280       61.40     36.21                                   
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 XYP 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 AHR A1305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FER A1306                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
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: 1I1W   RELATED DB: PDB                                   
REMARK 900  0.89 A ULTRA HIGH RESOLUTION STRUCTURE OF                           
REMARK 900   A THERMOSTABLEXYLANASE FROM THERMOASCUS                            
REMARK 900  AURANTIACUS                                                         
REMARK 900 RELATED ID: 1I1X   RELATED DB: PDB                                   
REMARK 900  1.11 A ATOMIC RESOLUTION STRUCTURE OF A                             
REMARK 900  THERMOSTABLEXYLANASE FROM THERMOASCUS AURANTIACUS                   
REMARK 900 RELATED ID: 1K6A   RELATED DB: PDB                                   
REMARK 900  STRUCTURAL STUDIES ON THE MOBILITY IN THE                           
REMARK 900  ACTIVE SITE OFTHE THERMOASCUS AURANTIACUS                           
REMARK 900  XYLANASE I                                                          
REMARK 900 RELATED ID: 1TUX   RELATED DB: PDB                                   
REMARK 900  HIGH RESOLUTION CRYSTAL STRUCTURE OF A                              
REMARK 900  THERMOSTABLE XYLANASE FROM THERMOASCUS                              
REMARK 900  AURANTIACUS                                                         
DBREF  2BNJ A    1   303  UNP    P23360   XYNA_THEAU      27    329             
SEQADV 2BNJ LYS A  193  UNP  P23360    GLN   219 CONFLICT                       
SEQADV 2BNJ SER A  259  UNP  P23360    GLN   285 CONFLICT                       
SEQADV 2BNJ ASN A  300  UNP  P23360    ASP   326 CONFLICT                       
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 ASN          
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 LYS 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 SER 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  ASN LEU GLN GLN                                              
MODRES 2BNJ PCA A    1  GLU  PYROGLUTAMATE                                      
HET    PCA  A   1       8                                                       
HET    XYP  A1303      10                                                       
HET    XYP  A1304       9                                                       
HET    AHR  A1305       8                                                       
HET    FER  A1306      14                                                       
HETNAM     PCA PYROGLUTAMIC ACID                                                
HETNAM     XYP BETA-D-XYLOPYRANOSE                                              
HETNAM     AHR ALPHA-L-ARABINOFURANOSE                                          
HETNAM     FER 3-(4-HYDROXY-3-METHOXYPHENYL)-2-PROPENOIC                        
HETNAM   2 FER  ACID                                                            
HETSYN     FER FERULIC ACID                                                     
FORMUL   1  PCA    C5 H7 N O3                                                   
FORMUL   2  XYP    2(C5 H10 O5)                                                 
FORMUL   2  AHR    C5 H10 O5                                                    
FORMUL   3  FER    C10 H10 O4                                                   
FORMUL   4  HOH   *596(H2 O1)                                                   
HELIX    1   1 SER A    5  ALA A   12  1                                   8    
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  ILE A  148  1                                   7    
HELIX    9   9 ASP A  151  ASP A  164  1                                  14    
HELIX   10  10 TYR A  181  GLY A  198  1                                  18    
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  LEU A  301  1                                  11    
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  2.11  
LINK         C   PCA A   1                 N   ALA A   2     1555   1555  1.33  
LINK         O4B XYP A1303                 C1B XYP A1304     1555   1555  1.42  
LINK         O3B XYP A1304                 C1' AHR A1305     1555   1555  1.35  
LINK         C5' AHR A1305                 O2  FER A1306     1555   1555  1.35  
CISPEP   1 HIS A   83    THR A   84          0        -3.61                     
SITE     1 AC1 11 LYS A  50  HIS A  83  ASN A 130  GLU A 131                    
SITE     2 AC1 11 GLN A 207  GLU A 237  TRP A 267  TRP A 275                    
SITE     3 AC1 11 XYP A1304  HOH A2588  HOH A2589                               
SITE     1 AC2 10 GLU A  46  ASN A  47  LYS A  50  GLN A  90                    
SITE     2 AC2 10 TRP A 267  TRP A 275  XYP A1303  AHR A1305                    
SITE     3 AC2 10 FER A1306  HOH A2591                                          
SITE     1 AC3 10 ASN A  25  GLU A  46  ASP A 273  TRP A 275                    
SITE     2 AC3 10 XYP A1304  FER A1306  HOH A2095  HOH A2592                    
SITE     3 AC3 10 HOH A2593  HOH A2594                                          
SITE     1 AC4  4 TRP A 275  XYP A1304  AHR A1305  HOH A2596                    
CRYST1   88.224   49.462   77.384  90.00 125.38  90.00 C 1 2 1       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      0.011335  0.000000  0.008049        0.00000                         
SCALE2      0.000000  0.020218  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015849        0.00000                         
HETATM    1  N   PCA A   1      27.578  22.427  21.802  1.00 12.72           N  
HETATM    2  CA  PCA A   1      27.842  22.372  20.384  1.00 13.08           C  
HETATM    3  CB  PCA A   1      26.797  23.209  19.650  1.00 13.57           C  
HETATM    4  CG  PCA A   1      25.592  23.158  20.566  1.00 14.60           C  
HETATM    5  CD  PCA A   1      26.221  22.912  21.922  1.00 13.71           C  
HETATM    6  OE  PCA A   1      25.672  23.084  23.017  1.00 15.97           O  
HETATM    7  C   PCA A   1      29.268  22.844  20.140  1.00 13.17           C  
HETATM    8  O   PCA A   1      29.629  23.959  20.526  1.00 13.82           O  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system