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Database: PDB
Entry: 2B46
LinkDB: 2B46
Original site: 2B46 
HEADER    HYDROLASE                               22-SEP-05   2B46              
TITLE     CRYSTAL STRUCTURE OF AN ENGINEERED UNINHIBITED BACILLUS               
TITLE    2 SUBTILIS XYLANASE IN SUBSTRATE BOUND STATE                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDO-1,4-BETA-XYLANASE A;                                  
COMPND   3 CHAIN: X;                                                            
COMPND   4 SYNONYM: XYLANASE A; 1,4- BETA-D-XYLAN XYLANOHYDROLASE A;            
COMPND   5 EC: 3.2.1.8;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 GENE: XYNA;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    BETA-JELLY ROLL STRUCTURE, HYDROLASE                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.SANSEN,M.DEWILDE,C.J.DE RANTER,J.F.SORENSEN,O.SIBBESEN,             
AUTHOR   2 K.GEBRUERS,K.BRIJS,C.M.COURTIN,J.A.DELCOUR,A.RABIJNS                 
REVDAT   2   24-FEB-09 2B46    1       VERSN                                    
REVDAT   1   19-SEP-06 2B46    0                                                
JRNL        AUTH   S.SANSEN,M.DEWILDE,C.J.DE RANTER,K.GEBRUERS,                 
JRNL        AUTH 2 K.BRIJS,C.M.COURTIN,J.A.DELCOUR,A.RABIJNS                    
JRNL        TITL   CRYSTAL STRUCTURE OF THE TRITICUM XYLANSE                    
JRNL        TITL 2 INHIBITOR-I IN COMPLEX WITH BACILLUS SUBTILIS                
JRNL        TITL 3 XYLANASE                                                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.21 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.19                                        
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) : 2.21                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 52.70                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 8903                           
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) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.198                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 968                             
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) : 2.21                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.27                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 586                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3260                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 70                           
REMARK   3   BIN FREE R VALUE                    : 0.3490                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1447                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 19                                      
REMARK   3   SOLVENT ATOMS            : 75                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.44                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.77000                                             
REMARK   3    B22 (A**2) : -0.77000                                             
REMARK   3    B33 (A**2) : 1.16000                                              
REMARK   3    B12 (A**2) : -0.39000                                             
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): 0.291         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.190         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.126         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.036         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.946                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.930                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1516 ; 0.014 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  1202 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2080 ; 1.488 ; 1.887       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2786 ; 0.782 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   184 ; 8.584 ; 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):   216 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1733 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   346 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   295 ; 0.317 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1474 ; 0.264 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):   876 ; 0.090 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    91 ; 0.381 ; 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):     8 ; 0.153 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    39 ; 0.237 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 0.185 ; 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):   906 ; 0.561 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1456 ; 1.075 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   610 ; 1.804 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   624 ; 2.752 ; 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          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 2B46 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 RCSB034652.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-MAR-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X13                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8000                             
REMARK 200  MONOCHROMATOR                  : TRIANGULAR MONOCHROMATOR           
REMARK 200  OPTICS                         : BENT MIRROR                        
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 8893                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.215                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 52.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.700                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.8                               
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) : 2.21                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.1                               
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   (%): 49.83                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 % (W/V) POLYETHYLENE GLYCOL           
REMARK 280  8000, 0.1 M HEPES BUFFER, PH 7.5, VAPOR DIFFUSION, HANGING DROP     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       31.83767            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       63.67533            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       47.75650            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       79.59417            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       15.91883            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X                                     
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 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   O5B  XYP X   501     O    HOH X   525              0.69            
REMARK 500   C1B  XYP X   501     O    HOH X   525              0.81            
REMARK 500   O3B  XYP X   502     O    HOH X   510              1.09            
REMARK 500   O2B  XYP X   502     O    HOH X   547              1.35            
REMARK 500   O3B  XYP X   501     O    HOH X   544              1.58            
REMARK 500   C3B  XYP X   501     O    HOH X   544              1.60            
REMARK 500   C5B  XYP X   501     O    HOH X   525              1.74            
REMARK 500   O4B  XYP X   502     O    HOH X   525              1.99            
REMARK 500   C2B  XYP X   501     O    HOH X   525              2.02            
REMARK 500   C2B  XYP X   502     O    HOH X   547              2.07            
REMARK 500   C3B  XYP X   502     O    HOH X   510              2.10            
REMARK 500   OE1  GLU X    78     O    HOH X   547              2.13            
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    ASP X 119   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 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    ASN X   8       82.19   -159.62                                   
REMARK 500    ALA X 165     -151.11   -100.29                                   
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 X   33     GLY X   34                  148.51                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XYP X 502                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XYP X 501                 
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: 2B42   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF TRITICUM AESTIVUM XYLANASE INHIBITOR-I IN               
REMARK 900 COMPLEX WITH BACILLUS SUBTILIS XYLANASE                              
REMARK 900 RELATED ID: 2B45   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF AN ENGINEERED UNINHIBITED BACILLUS SUBTILIS             
REMARK 900 XYLANASE IN FREE STATE                                               
DBREF  2B46 X    1   185  UNP    P18429   XYNA_BACSU      29    213             
SEQADV 2B46 PHE X   11  UNP  P18429    ASP    39 ENGINEERED                     
SEQADV 2B46 ASP X  122  UNP  P18429    ARG   150 ENGINEERED                     
SEQRES   1 X  185  ALA SER THR ASP TYR TRP GLN ASN TRP THR PHE GLY GLY          
SEQRES   2 X  185  GLY ILE VAL ASN ALA VAL ASN GLY SER GLY GLY ASN TYR          
SEQRES   3 X  185  SER VAL ASN TRP SER ASN THR GLY ASN PHE VAL VAL GLY          
SEQRES   4 X  185  LYS GLY TRP THR THR GLY SER PRO PHE ARG THR ILE ASN          
SEQRES   5 X  185  TYR ASN ALA GLY VAL TRP ALA PRO ASN GLY ASN GLY TYR          
SEQRES   6 X  185  LEU THR LEU TYR GLY TRP THR ARG SER PRO LEU ILE GLU          
SEQRES   7 X  185  TYR TYR VAL VAL ASP SER TRP GLY THR TYR ARG PRO THR          
SEQRES   8 X  185  GLY THR TYR LYS GLY THR VAL LYS SER ASP GLY GLY THR          
SEQRES   9 X  185  TYR ASP ILE TYR THR THR THR ARG TYR ASN ALA PRO SER          
SEQRES  10 X  185  ILE ASP GLY ASP ASP THR THR PHE THR GLN TYR TRP SER          
SEQRES  11 X  185  VAL ARG GLN SER LYS ARG PRO THR GLY SER ASN ALA THR          
SEQRES  12 X  185  ILE THR PHE SER ASN HIS VAL ASN ALA TRP LYS SER HIS          
SEQRES  13 X  185  GLY MET ASN LEU GLY SER ASN TRP ALA TYR GLN VAL MET          
SEQRES  14 X  185  ALA THR GLU GLY TYR GLN SER SER GLY SER SER ASN VAL          
SEQRES  15 X  185  THR VAL TRP                                                  
HET    XYP  X 502      10                                                       
HET    XYP  X 501       9                                                       
HETNAM     XYP BETA-D-XYLOPYRANOSE                                              
FORMUL   2  XYP    2(C5 H10 O5)                                                 
FORMUL   3  HOH   *75(H2 O)                                                     
HELIX    1   1 PHE X  146  HIS X  156  1                                  11    
SHEET    1   A 8 TYR X   5  PHE X  11  0                                        
SHEET    2   A 8 ASN X  35  TRP X  42 -1  O  GLY X  39   N  GLN X   7           
SHEET    3   A 8 ASN X 163  TYR X 174 -1  O  THR X 171   N  VAL X  38           
SHEET    4   A 8 GLY X  64  ARG X  73 -1  N  THR X  67   O  ALA X 170           
SHEET    5   A 8 ILE X  77  TRP X  85 -1  O  TYR X  79   N  GLY X  70           
SHEET    6   A 8 GLY X 120  ARG X 132  1  O  SER X 130   N  VAL X  82           
SHEET    7   A 8 GLY X 103  SER X 117 -1  N  THR X 110   O  GLN X 127           
SHEET    8   A 8 THR X  93  SER X 100 -1  N  GLY X  96   O  ILE X 107           
SHEET    1   B 5 ILE X  15  ASN X  20  0                                        
SHEET    2   B 5 ASN X  25  SER X  31 -1  O  ASN X  29   N  ASN X  17           
SHEET    3   B 5 SER X 177  TRP X 185 -1  O  GLY X 178   N  TRP X  30           
SHEET    4   B 5 THR X  50  ASN X  61 -1  N  ASN X  61   O  SER X 177           
SHEET    5   B 5 ALA X 142  THR X 145 -1  O  ALA X 142   N  TYR X  53           
LINK         O4B XYP X 502                 C1B XYP X 501     1555   1555  1.44  
CISPEP   1 SER X   74    PRO X   75          0        -0.53                     
SITE     1 AC1 14 TRP X   9  VAL X  37  TYR X  69  TRP X  71                    
SITE     2 AC1 14 GLU X  78  TYR X  80  ARG X 112  PRO X 116                    
SITE     3 AC1 14 GLN X 127  GLU X 172  XYP X 501  HOH X 510                    
SITE     4 AC1 14 HOH X 525  HOH X 547                                          
SITE     1 AC2  9 GLN X   7  TRP X   9  TYR X  69  PRO X 116                    
SITE     2 AC2  9 SER X 117  TYR X 166  XYP X 502  HOH X 525                    
SITE     3 AC2  9 HOH X 544                                                     
CRYST1   60.653   60.653   95.513  90.00  90.00 120.00 P 61          6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016487  0.009519  0.000000        0.00000                         
SCALE2      0.000000  0.019038  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010470        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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