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Database: PDB
Entry: 2B42
LinkDB: 2B42
Original site: 2B42 
HEADER    HYDROLASE INHIBITOR/HYDROLASE           22-SEP-05   2B42              
TITLE     CRYSTAL STRUCTURE OF THE TRITICUM XYLANSE INHIBITOR-I IN COMPLEX WITH 
TITLE    2 BACILLUS SUBTILIS XYLANASE                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: XYLANASE INHIBITOR-I;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: ENDO-1,4-BETA-XYLANASE A;                                  
COMPND   6 CHAIN: B;                                                            
COMPND   7 SYNONYM: XYLANASE A; 1,4- BETA-D-XYLAN XYLANOHYDROLASE A;            
COMPND   8 EC: 3.2.1.8;                                                         
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: TRITICUM AESTIVUM;                              
SOURCE   3 ORGANISM_COMMON: BREAD WHEAT;                                        
SOURCE   4 ORGANISM_TAXID: 4565;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   7 ORGANISM_TAXID: 1423;                                                
SOURCE   8 GENE: XYNA;                                                          
SOURCE   9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PROTEIN-PROTEIN COMPLEX; TWO BETA-BARREL DOMAIN; BETA-JELLY ROLL; X-  
KEYWDS   2 RAY CRYSTALLOGRAPHY, HYDROLASE INHIBITOR-HYDROLASE COMPLEX           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.SANSEN,M.DEWILDE,C.J.DE RANTER,K.GEBRUERS,K.BRIJS,C.M.COURTIN,      
AUTHOR   2 J.A.DELCOUR,A.RABIJNS                                                
REVDAT   3   23-JUN-10 2B42    1       JRNL                                     
REVDAT   2   24-FEB-09 2B42    1       VERSN                                    
REVDAT   1   19-SEP-06 2B42    0                                                
JRNL        AUTH   A.POLLET,S.SANSEN,G.RAEDSCHELDERS,K.GEBRUERS,A.RABIJNS,      
JRNL        AUTH 2 J.A.DELCOUR,C.M.COURTIN                                      
JRNL        TITL   IDENTIFICATION OF STRUCTURAL DETERMINANTS FOR INHIBITION     
JRNL        TITL 2 STRENGTH AND SPECIFICITY OF WHEAT XYLANASE INHIBITORS        
JRNL        TITL 3 TAXI-IA AND TAXI-IIA.                                        
JRNL        REF    FEBS J.                       V. 276  3916 2009              
JRNL        REFN                   ISSN 1742-464X                               
JRNL        PMID   19769747                                                     
JRNL        DOI    10.1111/J.1742-4658.2009.07105.X                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.36                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 18166                          
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) : 0.188                           
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1968                            
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) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1376                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2560                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 140                          
REMARK   3   BIN FREE R VALUE                    : 0.3080                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4047                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 65                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.36                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.41000                                              
REMARK   3    B22 (A**2) : 0.91000                                              
REMARK   3    B33 (A**2) : 0.09000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.32000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.731         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.295         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.207         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.333         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.901                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4163 ; 0.013 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  3675 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5699 ; 1.425 ; 1.945       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8548 ; 0.808 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   543 ; 7.171 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   633 ; 0.083 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4713 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   840 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   719 ; 0.201 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4070 ; 0.242 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2487 ; 0.083 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   105 ; 0.143 ; 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):     3 ; 0.149 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    39 ; 0.269 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.258 ; 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):  2710 ; 0.693 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4349 ; 1.285 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1453 ; 1.455 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1350 ; 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 : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2B42 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-OCT-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB034648.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-NOV-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
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                  : SAGITALLY FOCUSING GE(220) AND A   
REMARK 200                                   MULTILAYER                         
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18166                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.360                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.700                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.1                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
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) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.22 M AMMONIUM SULPHATE, 0.1 M SODIUM   
REMARK 280  ACETATE BUFFER, 25 % (W/V) POLYETHYLENE GLYCOL 4000, PH 4.6,        
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                     
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       53.94500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.67000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       53.94500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       47.67000            
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 300 REMARK: THE ASYMMMETRIC UNIT CONTAINS ONE COPY OF THE PROTEIN-       
REMARK 300 PROTEIN COMPLEX                                                      
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2520 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21260 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLY A    42                                                      
REMARK 465     GLN A    43                                                      
REMARK 465     PRO A    44                                                      
REMARK 465     PRO A    45                                                      
REMARK 465     ALA A    46                                                      
REMARK 465     PRO A    69                                                      
REMARK 465     SER A    70                                                      
REMARK 465     CYS A    71                                                      
REMARK 465     GLY A    72                                                      
REMARK 465     SER A    73                                                      
REMARK 465     ASP A    74                                                      
REMARK 465     LYS A    75                                                      
REMARK 465     HIS A    76                                                      
REMARK 465     ASP A    77                                                      
REMARK 465     HIS A   263                                                      
REMARK 465     ALA A   264                                                      
REMARK 465     ASN A   265                                                      
REMARK 465     ALA B     1                                                      
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    ASP A 355   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP B 106   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 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                                                                      
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    PHE A  20      -71.32   -111.83                                   
REMARK 500    LYS A  40      119.88    -26.08                                   
REMARK 500    PRO A  67      -93.47    -81.28                                   
REMARK 500    LYS A 115      150.54    -45.78                                   
REMARK 500    SER A 132       -7.94     81.67                                   
REMARK 500    GLU A 224      106.60    -58.24                                   
REMARK 500    VAL A 321      -52.46   -120.96                                   
REMARK 500    ALA A 329       31.29    -83.51                                   
REMARK 500    ASN B   8       86.70   -161.09                                   
REMARK 500    ALA B 165     -154.23   -107.25                                   
REMARK 500    GLN B 175       47.73     37.22                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 THR B   33     GLY B   34                  148.81                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1T6E   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF TRITICUM AESTIVUM XYLANASE INHIBITOR-I                  
REMARK 900 RELATED ID: 1T6G   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF TRITICUM AESTIVUM XYLANASE INHIBITOR-I IN               
REMARK 900 COMPLEX WITH ASPERGILLUS NIGER XYLANASE-I                            
REMARK 900 RELATED ID: 2B45   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF AN ENGINEERED UNINHIBITED BACILLUS SUBTILIS             
REMARK 900 XYLANASE IN FREE STATE                                               
REMARK 900 RELATED ID: 2B46   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF AN ENGINEERED UNINHIBITED BACILLUS SUBTILIS             
REMARK 900 XYLANASE WITH XYLOBIOSE                                              
DBREF  2B42 A    1   381  GB     23954367 CAD27730        22    402             
DBREF  2B42 B    1   185  UNP    P18429   XYNA_BACSU      29    213             
SEQADV 2B42 LYS A   40  GB   23954367  ASP    61 CONFLICT                       
SEQADV 2B42 VAL A  274  GB   23954367  GLU   295 CONFLICT                       
SEQADV 2B42 THR B  147  UNP  P18429    SER   175 CONFLICT                       
SEQRES   1 A  381  LEU PRO VAL LEU ALA PRO VAL THR LYS ASP PRO ALA THR          
SEQRES   2 A  381  SER LEU TYR THR ILE PRO PHE HIS ASP GLY ALA SER LEU          
SEQRES   3 A  381  VAL LEU ASP VAL ALA GLY PRO LEU VAL TRP SER THR CYS          
SEQRES   4 A  381  LYS GLY GLY GLN PRO PRO ALA GLU ILE PRO CYS SER SER          
SEQRES   5 A  381  PRO THR CYS LEU LEU ALA ASN ALA TYR PRO ALA PRO GLY          
SEQRES   6 A  381  CYS PRO ALA PRO SER CYS GLY SER ASP LYS HIS ASP LYS          
SEQRES   7 A  381  PRO CYS THR ALA TYR PRO TYR ASN PRO VAL SER GLY ALA          
SEQRES   8 A  381  CYS ALA ALA GLY SER LEU SER HIS THR ARG PHE VAL ALA          
SEQRES   9 A  381  ASN THR THR ASP GLY SER LYS PRO VAL SER LYS VAL ASN          
SEQRES  10 A  381  VAL GLY VAL LEU ALA ALA CYS ALA PRO SER LYS LEU LEU          
SEQRES  11 A  381  ALA SER LEU PRO ARG GLY SER THR GLY VAL ALA GLY LEU          
SEQRES  12 A  381  ALA ASN SER GLY LEU ALA LEU PRO ALA GLN VAL ALA SER          
SEQRES  13 A  381  ALA GLN LYS VAL ALA ASN ARG PHE LEU LEU CYS LEU PRO          
SEQRES  14 A  381  THR GLY GLY PRO GLY VAL ALA ILE PHE GLY GLY GLY PRO          
SEQRES  15 A  381  VAL PRO TRP PRO GLN PHE THR GLN SER MET PRO TYR THR          
SEQRES  16 A  381  PRO LEU VAL THR LYS GLY GLY SER PRO ALA HIS TYR ILE          
SEQRES  17 A  381  SER ALA ARG SER ILE VAL VAL GLY ASP THR ARG VAL PRO          
SEQRES  18 A  381  VAL PRO GLU GLY ALA LEU ALA THR GLY GLY VAL MET LEU          
SEQRES  19 A  381  SER THR ARG LEU PRO TYR VAL LEU LEU ARG PRO ASP VAL          
SEQRES  20 A  381  TYR ARG PRO LEU MET ASP ALA PHE THR LYS ALA LEU ALA          
SEQRES  21 A  381  ALA GLN HIS ALA ASN GLY ALA PRO VAL ALA ARG ALA VAL          
SEQRES  22 A  381  VAL ALA VAL ALA PRO PHE GLY VAL CYS TYR ASP THR LYS          
SEQRES  23 A  381  THR LEU GLY ASN ASN LEU GLY GLY TYR ALA VAL PRO ASN          
SEQRES  24 A  381  VAL GLN LEU GLY LEU ASP GLY GLY SER ASP TRP THR MET          
SEQRES  25 A  381  THR GLY LYS ASN SER MET VAL ASP VAL LYS GLN GLY THR          
SEQRES  26 A  381  ALA CYS VAL ALA PHE VAL GLU MET LYS GLY VAL ALA ALA          
SEQRES  27 A  381  GLY ASP GLY ARG ALA PRO ALA VAL ILE LEU GLY GLY ALA          
SEQRES  28 A  381  GLN MET GLU ASP PHE VAL LEU ASP PHE ASP MET GLU LYS          
SEQRES  29 A  381  LYS ARG LEU GLY PHE SER ARG LEU PRO HIS PHE THR GLY          
SEQRES  30 A  381  CYS GLY GLY LEU                                              
SEQRES   1 B  185  ALA SER THR ASP TYR TRP GLN ASN TRP THR ASP GLY GLY          
SEQRES   2 B  185  GLY ILE VAL ASN ALA VAL ASN GLY SER GLY GLY ASN TYR          
SEQRES   3 B  185  SER VAL ASN TRP SER ASN THR GLY ASN PHE VAL VAL GLY          
SEQRES   4 B  185  LYS GLY TRP THR THR GLY SER PRO PHE ARG THR ILE ASN          
SEQRES   5 B  185  TYR ASN ALA GLY VAL TRP ALA PRO ASN GLY ASN GLY TYR          
SEQRES   6 B  185  LEU THR LEU TYR GLY TRP THR ARG SER PRO LEU ILE GLU          
SEQRES   7 B  185  TYR TYR VAL VAL ASP SER TRP GLY THR TYR ARG PRO THR          
SEQRES   8 B  185  GLY THR TYR LYS GLY THR VAL LYS SER ASP GLY GLY THR          
SEQRES   9 B  185  TYR ASP ILE TYR THR THR THR ARG TYR ASN ALA PRO SER          
SEQRES  10 B  185  ILE ASP GLY ASP ARG THR THR PHE THR GLN TYR TRP SER          
SEQRES  11 B  185  VAL ARG GLN SER LYS ARG PRO THR GLY SER ASN ALA THR          
SEQRES  12 B  185  ILE THR PHE THR ASN HIS VAL ASN ALA TRP LYS SER HIS          
SEQRES  13 B  185  GLY MET ASN LEU GLY SER ASN TRP ALA TYR GLN VAL MET          
SEQRES  14 B  185  ALA THR GLU GLY TYR GLN SER SER GLY SER SER ASN VAL          
SEQRES  15 B  185  THR VAL TRP                                                  
FORMUL   3  HOH   *65(H2 O)                                                     
HELIX    1   1 SER A   52  ASN A   59  1                                   8    
HELIX    2   2 PRO A  126  ALA A  131  5                                   6    
HELIX    3   3 ALA A  149  LYS A  159  1                                  11    
HELIX    4   4 TRP A  185  GLN A  190  1                                   6    
HELIX    5   5 ARG A  244  ALA A  261  1                                  18    
HELIX    6   6 LYS A  286  LEU A  288  5                                   3    
HELIX    7   7 THR A  313  SER A  317  1                                   5    
HELIX    8   8 GLY A  349  GLU A  354  1                                   6    
HELIX    9   9 PHE B  146  HIS B  156  1                                  11    
SHEET    1   A 8 THR A  81  ALA A  82  0                                        
SHEET    2   A 8 GLY A  95  THR A 107 -1  O  GLY A  95   N  ALA A  82           
SHEET    3   A 8 VAL A   3  LYS A   9 -1  N  LEU A   4   O  ASN A 105           
SHEET    4   A 8 GLY A 174  PHE A 178 -1  O  GLY A 174   N  VAL A   7           
SHEET    5   A 8 ARG A 163  CYS A 167 -1  N  LEU A 165   O  ILE A 177           
SHEET    6   A 8 PHE A 356  ASP A 361 -1  O  LEU A 358   N  LEU A 166           
SHEET    7   A 8 ARG A 366  ARG A 371 -1  O  SER A 370   N  VAL A 357           
SHEET    8   A 8 TYR A 194  PRO A 196 -1  N  THR A 195   O  LEU A 367           
SHEET    1   B13 THR A  81  ALA A  82  0                                        
SHEET    2   B13 GLY A  95  THR A 107 -1  O  GLY A  95   N  ALA A  82           
SHEET    3   B13 PRO A 112  CYS A 124 -1  O  VAL A 113   N  THR A 106           
SHEET    4   B13 VAL A  35  SER A  37  1  N  VAL A  35   O  ALA A 123           
SHEET    5   B13 SER A 137  GLY A 142 -1  O  VAL A 140   N  TRP A  36           
SHEET    6   B13 ALA A  24  ASP A  29  1  N  VAL A  27   O  GLY A 139           
SHEET    7   B13 TYR A  16  HIS A  21 -1  N  PHE A  20   O  ALA A  24           
SHEET    8   B13 VAL A   3  LYS A   9 -1  N  THR A   8   O  THR A  17           
SHEET    9   B13 GLY A 174  PHE A 178 -1  O  GLY A 174   N  VAL A   7           
SHEET   10   B13 ARG A 163  CYS A 167 -1  N  LEU A 165   O  ILE A 177           
SHEET   11   B13 PHE A 356  ASP A 361 -1  O  LEU A 358   N  LEU A 166           
SHEET   12   B13 ARG A 366  ARG A 371 -1  O  SER A 370   N  VAL A 357           
SHEET   13   B13 TYR A 194  PRO A 196 -1  N  THR A 195   O  LEU A 367           
SHEET    1   C 5 TYR A 207  ILE A 208  0                                        
SHEET    2   C 5 VAL A 232  LEU A 234 -1  O  VAL A 232   N  ILE A 208           
SHEET    3   C 5 VAL A 346  LEU A 348  1  O  VAL A 346   N  MET A 233           
SHEET    4   C 5 VAL A 241  LEU A 243 -1  N  LEU A 242   O  ILE A 347           
SHEET    5   C 5 PHE A 330  GLU A 332  1  O  VAL A 331   N  VAL A 241           
SHEET    1   D 4 THR A 218  ARG A 219  0                                        
SHEET    2   D 4 ALA A 210  VAL A 215 -1  N  VAL A 215   O  THR A 218           
SHEET    3   D 4 VAL A 300  LEU A 304 -1  O  GLY A 303   N  SER A 212           
SHEET    4   D 4 SER A 308  MET A 312 -1  O  TRP A 310   N  LEU A 302           
SHEET    1   E 4 ALA A 272  VAL A 273  0                                        
SHEET    2   E 4 CYS A 282  ASP A 284 -1  O  CYS A 282   N  VAL A 273           
SHEET    3   E 4 THR A 325  VAL A 328 -1  O  ALA A 326   N  TYR A 283           
SHEET    4   E 4 MET A 318  LYS A 322 -1  N  VAL A 319   O  CYS A 327           
SHEET    1   F 2 ASN A 290  ASN A 291  0                                        
SHEET    2   F 2 GLY A 294  TYR A 295 -1  O  GLY A 294   N  ASN A 291           
SHEET    1   G 8 TYR B   5  THR B  10  0                                        
SHEET    2   G 8 ASN B  35  TRP B  42 -1  O  GLY B  39   N  GLN B   7           
SHEET    3   G 8 ASN B 163  TRP B 185 -1  O  THR B 171   N  VAL B  38           
SHEET    4   G 8 THR B  50  ARG B  73 -1  N  THR B  67   O  ALA B 170           
SHEET    5   G 8 ILE B  77  TRP B  85 -1  O  SER B  84   N  LEU B  66           
SHEET    6   G 8 GLY B 120  ARG B 132  1  O  ARG B 132   N  VAL B  82           
SHEET    7   G 8 GLY B 103  SER B 117 -1  N  ARG B 112   O  PHE B 125           
SHEET    8   G 8 THR B  93  SER B 100 -1  N  GLY B  96   O  ILE B 107           
SHEET    1   H 5 ILE B  15  ASN B  20  0                                        
SHEET    2   H 5 ASN B  25  SER B  31 -1  O  ASN B  29   N  ASN B  17           
SHEET    3   H 5 ASN B 163  TRP B 185 -1  O  GLY B 178   N  TRP B  30           
SHEET    4   H 5 THR B  50  ARG B  73 -1  N  THR B  67   O  ALA B 170           
SHEET    5   H 5 ALA B 142  THR B 145 -1  O  ALA B 142   N  TYR B  53           
SSBOND   1 CYS A   39    CYS A  124                          1555   1555  2.05  
SSBOND   2 CYS A   55    CYS A   80                          1555   1555  2.02  
SSBOND   3 CYS A   66    CYS A   92                          1555   1555  2.04  
SSBOND   4 CYS A  167    CYS A  378                          1555   1555  2.10  
SSBOND   5 CYS A  282    CYS A  327                          1555   1555  2.06  
CISPEP   1 ALA A  277    PRO A  278          0        -2.31                     
CISPEP   2 SER B   74    PRO B   75          0        -3.33                     
CRYST1  107.890   95.340   69.310  90.00 122.24  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      0.009269  0.000000  0.005846        0.00000                         
SCALE2      0.000000  0.010489  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017058        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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