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Database: PDB
Entry: 1E0X
LinkDB: 1E0X
Original site: 1E0X 
HEADER    HYDROLASE                               10-APR-00   1E0X              
TITLE     XYLANASE 10A FROM SREPTOMYCES LIVIDANS. XYLOBIOSYL-ENZYME             
TITLE    2 INTERMEDIATE AT 1.65 A                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDO-1,4-BETA-XYLANASE A;                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CATALYTIC MODULE, RESIDUES 32-450;                         
COMPND   5 SYNONYM: XYLANASE A, 1,4-BETA-D-XYLAN XYLANOHYDROLASE A;             
COMPND   6 EC: 3.2.1.8;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 OTHER_DETAILS: GLYCOSYL ENXYME INTERMEDIATE. COVALENT LINK           
COMPND   9  BETWEEN GLU 236 AND THE SUBSTRATE                                   
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOMYCES LIVIDANS;                          
SOURCE   3 ORGANISM_TAXID: 1916;                                                
SOURCE   4 EXPRESSION_SYSTEM: STREPTOMYCES LIVIDANS;                            
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 1916;                                       
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: IAF 19                                     
KEYWDS    GLYCOSIDE HYDROLASE FAMILY 10, HYDROLASE, XYLAN DEGRADATION,          
KEYWDS   2 GLYCOSYL-ENZYME INTERMEDIATE                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.DUCROS,S.J.CHARNOCK,U.DEREWENDA,Z.S.DEREWENDA,Z.DAUTER,             
AUTHOR   2 C.DUPONT,F.SHARECK,R.MOROSOLI,D.KLUEPFEL,G.J.DAVIES                  
REVDAT   5   31-AUG-11 1E0X    1       HEADER COMPND KEYWDS REMARK              
REVDAT   5 2                           HETSYN FORMUL SITE   ATOM                
REVDAT   5 3                           TER    HETATM VERSN                      
REVDAT   4   24-FEB-09 1E0X    1       VERSN                                    
REVDAT   3   24-JUN-03 1E0X    1       COMPND REMARK HET    HETNAM              
REVDAT   3 2                           FORMUL ATOM   TER    HETATM              
REVDAT   2   25-MAY-01 1E0X    1       JRNL   REMARK                            
REVDAT   1   05-APR-01 1E0X    0                                                
JRNL        AUTH   V.DUCROS,S.J.CHARNOCK,U.DEREWENDA,Z.S.DEREWENDA,             
JRNL        AUTH 2 Z.DAUTER,C.DUPONT,F.SHARECK,R.MOROSOLI,D.KLUEPFEL,           
JRNL        AUTH 3 G.J.DAVIES                                                   
JRNL        TITL   SUBSTRATE SPECIFICITY IN GLYCOSIDE HYDROLASE                 
JRNL        TITL 2 FAMILY 10. STRUCTURAL AND KINETIC ANALYSIS OF THE            
JRNL        TITL 3 STREPTOMYCES LIVIDANS XYLANASE 10A                           
JRNL        REF    J.BIOL.CHEM.                  V. 275 23020 2000              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   10930426                                                     
JRNL        DOI    10.1074/JBC.M000129200                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   U.DEREWENDA,L.SWENSON,R.GREEN,Y.WEI,R.MOROSOLI,              
REMARK   1  AUTH 2 F.SHARECK,D.KLUEPFEL,Z.S.DEREWENDA                           
REMARK   1  TITL   CRYSTAL STRUCTURE, AT 2.6 A RESOLUTION, OF THE               
REMARK   1  TITL 2 STREPTOMYCES LIVIDANS XYLANASE A, A MEMBER OF THE            
REMARK   1  TITL 3 F FAMILY OF B-1,4-D-GLYCANASES                               
REMARK   1  REF    J.BIOL.CHEM.                  V. 269 20811 1994              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1  PMID   8063693                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15                             
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99                             
REMARK   3   NUMBER OF REFLECTIONS             : 63415                          
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) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.126                           
REMARK   3   FREE R VALUE                     : 0.162                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 3381                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4823                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 54                                      
REMARK   3   SOLVENT ATOMS            : 717                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 11.8                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.012 ; 0.02                
REMARK   3    ANGLE DISTANCE                  (A) : 0.028 ; 0.04                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.034 ; 0.05                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.026 ; 0.03                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.121 ; 0.150               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : 0.16  ; 0.30                
REMARK   3    MULTIPLE TORSION                (A) : 0.26  ; 0.30                
REMARK   3    H-BOND (X...Y)                  (A) : 0.14  ; 0.30                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : 4.7   ; 7.0                 
REMARK   3    STAGGERED                 (DEGREES) : 12.3  ; 15.0                
REMARK   3    TRANSVERSE                (DEGREES) : 27.8  ; 20.0                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.448 ; 3.000                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.994 ; 5.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.301 ; 4.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.885 ; 6.000                
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: DOUBLY CONFIGURATED DISULPHIDE BOND       
REMARK   3  BETWEEN CYS168 AND CYS201                                           
REMARK   4                                                                      
REMARK   4 1E0X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-APR-00.                  
REMARK 100 THE PDBE ID CODE IS EBI-4843.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-NOV-97                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : LONG MIRRORS (MSC)                 
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66881                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.03300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 35.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.71                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.09700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 12.900                             
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NATIVE STRUCTURE AT 1.2                              
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.0                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.7                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLISED WITH            
REMARK 280  18 % PEG 5000 AS PRECIPITANT, 100MM HEPES PH 7.5 AS BUFFER,         
REMARK 280  10% ISOPROPANOL, CRYSTAL WERE SOAKED IN PRESENCE                    
REMARK 280  OF POWDERED SUBSTRATE FOR 12 HOURS.                                 
REMARK 280  15% GLYCEROL WAS ADDED AS CRYOPROTECTANT                            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       40.53000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     ASP A   311                                                      
REMARK 465     GLY A   312                                                      
REMARK 465     GLY A   313                                                      
REMARK 465     ASP B   311                                                      
REMARK 465     GLY B   312                                                      
REMARK 465     GLY B   313                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ALA A 310    CA   C    O    CB                                   
REMARK 470     ALA B 310    CA   C    O    CB                                   
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   C    GLU B   277     O    HOH B  2313              0.42            
REMARK 500   CA   ALA A   160     O    HOH A  2229              0.64            
REMARK 500   CA   ALA B   292     O    HOH B  2329              0.68            
REMARK 500   CB   ALA A   100     O    HOH A  2151              0.78            
REMARK 500   OG1  THR B   279     O    HOH B  2318              0.79            
REMARK 500   CG   ASP B   162     O    HOH B  2219              0.98            
REMARK 500   O    ARG B   159     O    HOH B  2213              1.05            
REMARK 500   O    SER B   276     O    HOH B  2310              1.15            
REMARK 500   CB   ASP B   162     O    HOH B  2219              1.17            
REMARK 500   CB   ALA B   292     O    HOH B  2329              1.22            
REMARK 500   N    ASN B   215     O    HOH B  2261              1.24            
REMARK 500   CA   GLU B   277     O    HOH B  2313              1.27            
REMARK 500   CA   ASN A    60     O    HOH A  2084              1.36            
REMARK 500   O    GLU B   277     O    HOH B  2313              1.39            
REMARK 500   C    ALA A   160     O    HOH A  2229              1.42            
REMARK 500   N    ALA B   292     O    HOH B  2329              1.47            
REMARK 500   C    GLN B   278     O    HOH B  2315              1.48            
REMARK 500   O    GLN B   278     O    HOH B  2315              1.49            
REMARK 500   CA   ASN B   215     O    HOH B  2261              1.49            
REMARK 500   OD1  ASP B   162     O    HOH B  2219              1.50            
REMARK 500   CG2  ILE B   239     O    HOH B  2281              1.51            
REMARK 500   O    ALA B   160     O    HOH B  2215              1.51            
REMARK 500   C    PRO B   163     O    HOH B  2220              1.54            
REMARK 500   N    GLN B   278     O    HOH B  2313              1.55            
REMARK 500   CB   ASN B   215     O    HOH B  2261              1.56            
REMARK 500   N    SER B   271     O    HOH B  2305              1.58            
REMARK 500   NE2  GLN B    11     O    HOH B  2013              1.62            
REMARK 500   O    PHE A    59     O    HOH A  2084              1.62            
REMARK 500   C    SER B   276     O    HOH B  2310              1.63            
REMARK 500   CD1  LEU A    96     O    HOH A  2149              1.63            
REMARK 500   CA   SER B   271     O    HOH B  2305              1.64            
REMARK 500   CB   ALA A   160     O    HOH A  2229              1.73            
REMARK 500   N    GLN B   278     O    HOH B  2316              1.74            
REMARK 500   N    ASN A    60     O    HOH A  2084              1.79            
REMARK 500   CA   GLN B   278     O    HOH B  2316              1.84            
REMARK 500   CB   PRO B   163     O    HOH B  2220              1.85            
REMARK 500   CA   GLN B   278     O    HOH B  2315              1.85            
REMARK 500   CA   ASP B   162     O    HOH B  2219              1.88            
REMARK 500   CG   GLN B   278     O    HOH B  2316              1.89            
REMARK 500   C    PHE A    59     O    HOH A  2084              1.90            
REMARK 500   CD   GLN B    11     O    HOH B  2013              1.95            
REMARK 500   OE1  GLN B    11     O    HOH B  2013              1.96            
REMARK 500   CD   PRO B   198     O    HOH B  2210              1.96            
REMARK 500   CA   PRO B   163     O    HOH B  2220              1.96            
REMARK 500   CB   THR B   279     O    HOH B  2318              1.97            
REMARK 500   C    ASP B   270     O    HOH B  2305              1.99            
REMARK 500   O    ALA A   160     O    HOH A  2229              2.01            
REMARK 500   O    PRO B   163     O    HOH B  2220              2.03            
REMARK 500   OD2  ASP B   162     O    HOH B  2219              2.03            
REMARK 500   N    ALA A   160     O    HOH A  2229              2.03            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      56 CLOSE CONTACTS                                
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   OG   SER B    97     O    HOH B  2013     2647     2.04            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 236   CD    GLU A 236   OE1     0.119                       
REMARK 500    GLU B 236   CD    GLU B 236   OE1     0.112                       
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  36   CD  -  NE  -  CZ  ANGL. DEV. =  15.8 DEGREES          
REMARK 500    ASP A  50   CB  -  CG  -  OD1 ANGL. DEV. =   8.2 DEGREES          
REMARK 500    ARG A  56   NE  -  CZ  -  NH2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ARG A  66   CD  -  NE  -  CZ  ANGL. DEV. =  30.7 DEGREES          
REMARK 500    ARG A  66   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG A  79   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG A  79   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ASP A 132   N   -  CA  -  CB  ANGL. DEV. =  17.3 DEGREES          
REMARK 500    ASP A 132   CB  -  CG  -  OD1 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ASP A 132   CB  -  CG  -  OD2 ANGL. DEV. = -10.6 DEGREES          
REMARK 500    ARG A 138   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG A 159   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG A 159   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ARG A 195   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    ARG A 195   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    CYS A 201   CA  -  CB  -  SG  ANGL. DEV. =  10.8 DEGREES          
REMARK 500    GLU B   2   OE1 -  CD  -  OE2 ANGL. DEV. =  11.0 DEGREES          
REMARK 500    ARG B  36   CD  -  NE  -  CZ  ANGL. DEV. =  10.5 DEGREES          
REMARK 500    ARG B  56   NE  -  CZ  -  NH2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP B 132   CB  -  CG  -  OD2 ANGL. DEV. =  -9.0 DEGREES          
REMARK 500    ARG B 145   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG B 159   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    PHE B 192   CB  -  CG  -  CD2 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    ARG B 195   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    CYS B 201   CA  -  CB  -  SG  ANGL. DEV. =   8.2 DEGREES          
REMARK 500    ARG B 269   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 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 A  45      -15.37   -142.50                                   
REMARK 500    GLN A  58       78.16   -115.85                                   
REMARK 500    GLU A 236       38.70   -142.60                                   
REMARK 500    VAL A 268      -75.63   -100.95                                   
REMARK 500    THR A 279       66.80     31.87                                   
REMARK 500    ASN B  45      -15.61   -142.43                                   
REMARK 500    GLN B  58       74.69   -104.44                                   
REMARK 500    ASP B 149        3.46    -68.80                                   
REMARK 500    GLU B 236       40.67   -140.91                                   
REMARK 500    VAL B 268      -76.71   -101.51                                   
REMARK 500    THR B 279       66.85     28.44                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASP A 132        21.3      L          L   OUTSIDE RANGE           
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 GOL A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF POLYSACCHARIDE         
REMARK 800   RESIDUES  701 TO  702                                              
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF DI-SACCHARIDE X2F B    
REMARK 800   701 AND XYP B 702                                                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1XAS   RELATED DB: PDB                                   
REMARK 900  XYLANASE A                                                          
REMARK 900 RELATED ID: 1E0V   RELATED DB: PDB                                   
REMARK 900  XYLANASE 10A FROM SREPTOMYCES LIVIDANS. CELLOBIOSYL-ENZYME          
REMARK 900  INTERMEDIATE AT 1.7 A                                               
REMARK 900 RELATED ID: 1E0W   RELATED DB: PDB                                   
REMARK 900  XYLANASE 10A FROM SREPTOMYCES LIVIDANS. NATIVE STRUCTURE            
REMARK 900  AT 1.2 ANGSTROM RESOLUTION                                          
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE FIRST 41 RESIDUES IN THE DATABASE CORRESPOND                     
REMARK 999 TO THE SIGNAL PEPTIDE. THE NUMBERING USED IN THE PDB FILE            
REMARK 999 IF AFTER CLEAVAGE OF THE SIGNAL PEPTIDE.                             
REMARK 999 THE LAST 4 RESIDUES ARE INVISIBLE IN DENSITY.                        
DBREF  1E0X A    1   309  UNP    P26514   XYNA_STRLI      42    350             
DBREF  1E0X B    1   309  UNP    P26514   XYNA_STRLI      42    350             
SEQRES   1 A  313  ALA GLU SER THR LEU GLY ALA ALA ALA ALA GLN SER GLY          
SEQRES   2 A  313  ARG TYR PHE GLY THR ALA ILE ALA SER GLY ARG LEU SER          
SEQRES   3 A  313  ASP SER THR TYR THR SER ILE ALA GLY ARG GLU PHE ASN          
SEQRES   4 A  313  MET VAL THR ALA GLU ASN GLU MET LYS ILE ASP ALA THR          
SEQRES   5 A  313  GLU PRO GLN ARG GLY GLN PHE ASN PHE SER SER ALA ASP          
SEQRES   6 A  313  ARG VAL TYR ASN TRP ALA VAL GLN ASN GLY LYS GLN VAL          
SEQRES   7 A  313  ARG GLY HIS THR LEU ALA TRP HIS SER GLN GLN PRO GLY          
SEQRES   8 A  313  TRP MET GLN SER LEU SER GLY SER ALA LEU ARG GLN ALA          
SEQRES   9 A  313  MET ILE ASP HIS ILE ASN GLY VAL MET ALA HIS TYR LYS          
SEQRES  10 A  313  GLY LYS ILE VAL GLN TRP ASP VAL VAL ASN GLU ALA PHE          
SEQRES  11 A  313  ALA ASP GLY SER SER GLY ALA ARG ARG ASP SER ASN LEU          
SEQRES  12 A  313  GLN ARG SER GLY ASN ASP TRP ILE GLU VAL ALA PHE ARG          
SEQRES  13 A  313  THR ALA ARG ALA ALA ASP PRO SER ALA LYS LEU CYS TYR          
SEQRES  14 A  313  ASN ASP TYR ASN VAL GLU ASN TRP THR TRP ALA LYS THR          
SEQRES  15 A  313  GLN ALA MET TYR ASN MET VAL ARG ASP PHE LYS GLN ARG          
SEQRES  16 A  313  GLY VAL PRO ILE ASP CYS VAL GLY PHE GLN SER HIS PHE          
SEQRES  17 A  313  ASN SER GLY SER PRO TYR ASN SER ASN PHE ARG THR THR          
SEQRES  18 A  313  LEU GLN ASN PHE ALA ALA LEU GLY VAL ASP VAL ALA ILE          
SEQRES  19 A  313  THR GLU LEU ASP ILE GLN GLY ALA PRO ALA SER THR TYR          
SEQRES  20 A  313  ALA ASN VAL THR ASN ASP CYS LEU ALA VAL SER ARG CYS          
SEQRES  21 A  313  LEU GLY ILE THR VAL TRP GLY VAL ARG ASP SER ASP SER          
SEQRES  22 A  313  TRP ARG SER GLU GLN THR PRO LEU LEU PHE ASN ASN ASP          
SEQRES  23 A  313  GLY SER LYS LYS ALA ALA TYR THR ALA VAL LEU ASP ALA          
SEQRES  24 A  313  LEU ASN GLY GLY ASP SER SER GLU PRO PRO ALA ASP GLY          
SEQRES  25 A  313  GLY                                                          
SEQRES   1 B  313  ALA GLU SER THR LEU GLY ALA ALA ALA ALA GLN SER GLY          
SEQRES   2 B  313  ARG TYR PHE GLY THR ALA ILE ALA SER GLY ARG LEU SER          
SEQRES   3 B  313  ASP SER THR TYR THR SER ILE ALA GLY ARG GLU PHE ASN          
SEQRES   4 B  313  MET VAL THR ALA GLU ASN GLU MET LYS ILE ASP ALA THR          
SEQRES   5 B  313  GLU PRO GLN ARG GLY GLN PHE ASN PHE SER SER ALA ASP          
SEQRES   6 B  313  ARG VAL TYR ASN TRP ALA VAL GLN ASN GLY LYS GLN VAL          
SEQRES   7 B  313  ARG GLY HIS THR LEU ALA TRP HIS SER GLN GLN PRO GLY          
SEQRES   8 B  313  TRP MET GLN SER LEU SER GLY SER ALA LEU ARG GLN ALA          
SEQRES   9 B  313  MET ILE ASP HIS ILE ASN GLY VAL MET ALA HIS TYR LYS          
SEQRES  10 B  313  GLY LYS ILE VAL GLN TRP ASP VAL VAL ASN GLU ALA PHE          
SEQRES  11 B  313  ALA ASP GLY SER SER GLY ALA ARG ARG ASP SER ASN LEU          
SEQRES  12 B  313  GLN ARG SER GLY ASN ASP TRP ILE GLU VAL ALA PHE ARG          
SEQRES  13 B  313  THR ALA ARG ALA ALA ASP PRO SER ALA LYS LEU CYS TYR          
SEQRES  14 B  313  ASN ASP TYR ASN VAL GLU ASN TRP THR TRP ALA LYS THR          
SEQRES  15 B  313  GLN ALA MET TYR ASN MET VAL ARG ASP PHE LYS GLN ARG          
SEQRES  16 B  313  GLY VAL PRO ILE ASP CYS VAL GLY PHE GLN SER HIS PHE          
SEQRES  17 B  313  ASN SER GLY SER PRO TYR ASN SER ASN PHE ARG THR THR          
SEQRES  18 B  313  LEU GLN ASN PHE ALA ALA LEU GLY VAL ASP VAL ALA ILE          
SEQRES  19 B  313  THR GLU LEU ASP ILE GLN GLY ALA PRO ALA SER THR TYR          
SEQRES  20 B  313  ALA ASN VAL THR ASN ASP CYS LEU ALA VAL SER ARG CYS          
SEQRES  21 B  313  LEU GLY ILE THR VAL TRP GLY VAL ARG ASP SER ASP SER          
SEQRES  22 B  313  TRP ARG SER GLU GLN THR PRO LEU LEU PHE ASN ASN ASP          
SEQRES  23 B  313  GLY SER LYS LYS ALA ALA TYR THR ALA VAL LEU ASP ALA          
SEQRES  24 B  313  LEU ASN GLY GLY ASP SER SER GLU PRO PRO ALA ASP GLY          
SEQRES  25 B  313  GLY                                                          
HET    X2F  A 701       9                                                       
HET    XYP  A 702       9                                                       
HET    X2F  B 701       9                                                       
HET    XYP  B 702       9                                                       
HET    GOL  A 400       6                                                       
HET    GOL  A 401       6                                                       
HET    GOL  B 400       6                                                       
HETNAM     X2F 2-DEOXY-2-FLUORO XYLOPYRANOSE                                    
HETNAM     XYP BETA-D-XYLOPYRANOSE                                              
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  X2F    2(C5 H9 F O4)                                                
FORMUL   4  XYP    2(C5 H10 O5)                                                 
FORMUL   5  GOL    3(C3 H8 O3)                                                  
FORMUL   6  HOH   *717(H2 O)                                                    
HELIX    1   1 THR A    4  GLN A   11  1                                   8    
HELIX    2   2 ALA A   21  LEU A   25  5                                   5    
HELIX    3   3 ASP A   27  PHE A   38  1                                  12    
HELIX    4   4 LYS A   48  GLU A   53  1                                   6    
HELIX    5   5 PHE A   61  ASN A   74  1                                  14    
HELIX    6   6 PRO A   90  SER A   95  1                                   6    
HELIX    7   7 SER A   97  TYR A  116  1                                  20    
HELIX    8   8 SER A  141  SER A  146  1                                   6    
HELIX    9   9 ASP A  149  ASP A  162  1                                  14    
HELIX   10  10 TRP A  179  GLY A  196  1                                  18    
HELIX   11  11 ASN A  217  ALA A  227  1                                  11    
HELIX   12  12 PRO A  243  ALA A  256  1                                  14    
HELIX   13  13 ASP A  270  SER A  273  5                                   4    
HELIX   14  14 ARG A  275  THR A  279  5                                   5    
HELIX   15  15 LYS A  290  ASN A  301  1                                  12    
HELIX   16  16 THR B    4  GLN B   11  1                                   8    
HELIX   17  17 ALA B   21  LEU B   25  5                                   5    
HELIX   18  18 ASP B   27  PHE B   38  1                                  12    
HELIX   19  19 LYS B   48  GLU B   53  1                                   6    
HELIX   20  20 PHE B   61  ASN B   74  1                                  14    
HELIX   21  21 PRO B   90  SER B   95  1                                   6    
HELIX   22  22 SER B   97  TYR B  116  1                                  20    
HELIX   23  23 SER B  141  GLY B  147  1                                   7    
HELIX   24  24 ASP B  149  ASP B  162  1                                  14    
HELIX   25  25 TRP B  179  GLY B  196  1                                  18    
HELIX   26  26 ASN B  217  ALA B  227  1                                  11    
HELIX   27  27 PRO B  243  ALA B  256  1                                  14    
HELIX   28  28 ASP B  270  SER B  273  5                                   4    
HELIX   29  29 ARG B  275  THR B  279  5                                   5    
HELIX   30  30 LYS B  290  GLY B  302  1                                  13    
SHEET    1   A 4 GLY A 262  VAL A 265  0                                        
SHEET    2   A 4 TYR A  15  ILE A  20  1  N  TYR A  15   O  ILE A 263           
SHEET    3   A 4 MET A  40  ALA A  43  1  N  MET A  40   O  THR A  18           
SHEET    4   A 4 GLN A  77  ARG A  79  1  N  GLN A  77   O  VAL A  41           
SHEET    1   B 4 ASP A 231  ILE A 234  0                                        
SHEET    2   B 4 CYS A 201  PHE A 204  1  N  VAL A 202   O  ASP A 231           
SHEET    3   B 4 LYS A 166  ASP A 171  1  N  TYR A 169   O  CYS A 201           
SHEET    4   B 4 GLN A 122  ASN A 127  1  N  TRP A 123   O  LYS A 166           
SHEET    1   C 4 GLY B 262  VAL B 265  0                                        
SHEET    2   C 4 TYR B  15  ILE B  20  1  N  TYR B  15   O  ILE B 263           
SHEET    3   C 4 MET B  40  ALA B  43  1  N  MET B  40   O  THR B  18           
SHEET    4   C 4 GLN B  77  ARG B  79  1  N  GLN B  77   O  VAL B  41           
SHEET    1   D 4 ASP B 231  ILE B 234  0                                        
SHEET    2   D 4 CYS B 201  PHE B 204  1  N  VAL B 202   O  ASP B 231           
SHEET    3   D 4 LYS B 166  ASP B 171  1  N  TYR B 169   O  CYS B 201           
SHEET    4   D 4 GLN B 122  ASN B 127  1  N  TRP B 123   O  LYS B 166           
SSBOND   1 CYS A  168    CYS A  201                          1555   1555  1.97  
SSBOND   2 CYS A  168    CYS A  201                          1555   1555  2.06  
SSBOND   3 CYS A  254    CYS A  260                          1555   1555  2.05  
SSBOND   4 CYS B  168    CYS B  201                          1555   1555  1.99  
SSBOND   5 CYS B  168    CYS B  201                          1555   1555  2.05  
SSBOND   6 CYS B  254    CYS B  260                          1555   1555  2.06  
LINK         OE1 GLU A 236                 C1  X2F A 701     1555   1555  1.50  
LINK         O4  X2F A 701                 C1B XYP A 702     1555   1555  1.44  
LINK         OE1 GLU B 236                 C1  X2F B 701     1555   1555  1.49  
LINK         O4  X2F B 701                 C1B XYP B 702     1555   1555  1.43  
CISPEP   1 HIS A   81    THR A   82          0         6.79                     
CISPEP   2 HIS B   81    THR B   82          0         1.84                     
SITE     1 AC1  4 GLN A  73  HOH A2361  HOH A2362  HOH A2363                    
SITE     1 AC2  8 HIS A  86  GLN A  89  GLN A  94  SER A 141                    
SITE     2 AC2  8 ASN A 142  HOH A2364  HOH A2365  HOH A2366                    
SITE     1 AC3  5 TYR B  68  ASN B  69  VAL B  72  GLN B  73                    
SITE     2 AC3  5 HOH B2345                                                     
SITE     1 AC4 15 GLU A  44  ASN A  45  LYS A  48  HIS A  81                    
SITE     2 AC4 15 TRP A  85  GLN A  88  ASN A 127  GLN A 205                    
SITE     3 AC4 15 HIS A 207  GLU A 236  TRP A 266  TRP A 274                    
SITE     4 AC4 15 HOH A2367  HOH A2368  HOH A2369                               
SITE     1 AC5 15 GLU B  44  ASN B  45  LYS B  48  HIS B  81                    
SITE     2 AC5 15 TRP B  85  GLN B  88  ASN B 127  GLN B 205                    
SITE     3 AC5 15 HIS B 207  GLU B 236  TRP B 266  TRP B 274                    
SITE     4 AC5 15 HOH B2346  HOH B2347  HOH B2348                               
CRYST1   49.210   81.060   72.810  90.00 102.79  90.00 P 1 21 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      0.020320  0.000000  0.004610        0.00000                         
SCALE2      0.000000  0.012340  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014080        0.00000                         
MTRIX1   1  0.999080 -0.041440  0.011400       15.98502    1                    
MTRIX2   1  0.042110  0.996900 -0.066520        2.67231    1                    
MTRIX3   1 -0.008610  0.066940  0.997720       35.57695    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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