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Database: PDB
Entry: 1US2
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Original site: 1US2 
HEADER    HYDROLASE                               17-NOV-03   1US2              
TITLE     XYLANASE10C (MUTANT E385A) FROM CELLVIBRIO JAPONICUS IN COMPLEX WITH  
TITLE    2 XYLOPENTAOSE                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDO-BETA-1,4-XYLANASE;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CARBOHYDRATE BINDING MODULE AND CATALYTIC MODULE, RESIDUES 
COMPND   5 (86-606);                                                            
COMPND   6 SYNONYM: XYLANASE10C;                                                
COMPND   7 EC: 3.2.1.8;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CELLVIBRIO JAPONICUS;                           
SOURCE   3 ORGANISM_TAXID: 155077;                                              
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: TUNER\:PLYSS;                              
SOURCE   7 EXPRESSION_SYSTEM_VECTOR: PET 22B                                    
KEYWDS    HYDROLASE, CARBOHYDRATE BINDING MODULE, XYLAN DEGRADATION             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.PELL,L.SZABO,S.J.CHARNOCK,H.XIE,T.M.GLOSTER,G.J.DAVIES,H.J.GILBERT  
REVDAT   5   30-AUG-17 1US2    1       REMARK                                   
REVDAT   4   13-JUL-11 1US2    1       VERSN                                    
REVDAT   3   24-FEB-09 1US2    1       VERSN                                    
REVDAT   2   18-MAR-04 1US2    1       JRNL                                     
REVDAT   1   18-DEC-03 1US2    0                                                
JRNL        AUTH   G.PELL,L.SZABO,S.J.CHARNOCK,H.XIE,T.M.GLOSTER,G.J.DAVIES,    
JRNL        AUTH 2 H.J.GILBERT                                                  
JRNL        TITL   STRUCTURAL AND BIOCHEMICAL ANALYSIS OF CELLVIBRIO JAPONICUS  
JRNL        TITL 2 XYLANASE 10C: HOW VARIATION IN SUBSTRATE-BINDING CLEFT       
JRNL        TITL 3 INFLUENCES THE CATALYTIC PROFILE OF FAMILY GH-10 XYLANASES   
JRNL        REF    J.BIOL.CHEM.                  V. 279 11777 2004              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   14670951                                                     
JRNL        DOI    10.1074/JBC.M311947200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 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) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 84.52                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 50495                          
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) : 0.181                           
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2682                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.85                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.90                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3559                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2060                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 189                          
REMARK   3   BIN FREE R VALUE                    : 0.2270                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3910                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 74                                      
REMARK   3   SOLVENT ATOMS            : 833                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.72                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.81000                                             
REMARK   3    B22 (A**2) : -0.52000                                             
REMARK   3    B33 (A**2) : 1.33000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.135         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.133         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.079         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.556         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.905                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4112 ; 0.017 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5617 ; 1.354 ; 1.941       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   504 ; 6.285 ; 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):   660 ; 0.101 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3094 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1543 ; 0.183 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   438 ; 0.142 ; 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):    35 ; 0.172 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    48 ; 0.141 ; 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):  2528 ; 0.597 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4086 ; 1.007 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1584 ; 1.697 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1531 ; 2.595 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   243        A   606                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.4190  62.5770 128.9480              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0353 T22:   0.0289                                     
REMARK   3      T33:   0.0192 T12:  -0.0096                                     
REMARK   3      T13:  -0.0025 T23:  -0.0191                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7423 L22:   0.4743                                     
REMARK   3      L33:   0.8178 L12:  -0.0472                                     
REMARK   3      L13:   0.1024 L23:  -0.1330                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0106 S12:   0.0192 S13:  -0.0699                       
REMARK   3      S21:  -0.0526 S22:  -0.0065 S23:   0.0031                       
REMARK   3      S31:   0.0268 S32:  -0.0059 S33:  -0.0040                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    97        A   238                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.0580  37.9710  82.5510              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3679 T22:   0.3444                                     
REMARK   3      T33:   0.2660 T12:   0.0136                                     
REMARK   3      T13:  -0.0480 T23:  -0.1692                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6062 L22:   1.7241                                     
REMARK   3      L33:   2.7774 L12:   0.5249                                     
REMARK   3      L13:  -0.2814 L23:   0.9890                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0350 S12:  -0.0983 S13:   0.1984                       
REMARK   3      S21:   0.3005 S22:   0.2122 S23:  -0.1624                       
REMARK   3      S31:  -0.0289 S32:   0.1946 S33:  -0.1772                       
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: ATOMS THAT COULD NOT BE PLACED RELIABLY   
REMARK   3  IN ELECTRON DENSITY HAVE BEEN SET TO ZERO OCCUPANCY                 
REMARK   4                                                                      
REMARK   4 1US2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-NOV-03.                  
REMARK 100 THE DEPOSITION ID IS D_1290013925.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAY-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX9.6                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8700                             
REMARK 200  MONOCHROMATOR                  : TRIANGULAR SINGLE CRYSTAL SI       
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : VERTICALLY FOCUSSING RH COATED     
REMARK 200                                   SI MIRROR                          
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 53227                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 4.400                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.92                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.800                              
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: PDB ENTRY 1CLX                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30 MG/ML PROTEIN 0.2 M SODIUM IODIDE,    
REMARK 280  20% PEG 3350, 20 MM (1 UL) XYLOPENTAOSE, PH 7.00                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       22.29850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       85.36350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.34300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       85.36350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.29850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.34300            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUES  GLU 385 ALA                                     
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     MET A    85                                                      
REMARK 465     VAL A    86                                                      
REMARK 465     ALA A    87                                                      
REMARK 465     ALA A    88                                                      
REMARK 465     SER A    89                                                      
REMARK 465     GLU A    90                                                      
REMARK 465     GLY A    91                                                      
REMARK 465     ASN A    92                                                      
REMARK 465     VAL A    93                                                      
REMARK 465     VAL A    94                                                      
REMARK 465     ALA A   192                                                      
REMARK 465     ASP A   193                                                      
REMARK 465     ALA A   240                                                      
REMARK 465     GLN A   241                                                      
REMARK 465     GLU A   242                                                      
REMARK 465     GLU A   607                                                      
REMARK 465     LEU A   608                                                      
REMARK 465     HIS A   609                                                      
REMARK 465     HIS A   610                                                      
REMARK 465     HIS A   611                                                      
REMARK 465     HIS A   612                                                      
REMARK 465     HIS A   613                                                      
REMARK 465     HIS A   614                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU A   96   CG   CD   OE1  OE2                                  
REMARK 480     VAL A  152   CB   CG1  CG2                                       
REMARK 480     LYS A  160   CG   CD   CE   NZ                                   
REMARK 480     LYS A  178   CB   CG   CD   CE   NZ                              
REMARK 480     LYS A  233   CB   CG   CD   CE   NZ                              
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 205   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A 249   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ASP A 562   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 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    SER A 119     -147.50   -147.53                                   
REMARK 500    ASP A 175       52.73   -142.75                                   
REMARK 500    THR A 225       71.68   -119.31                                   
REMARK 500    ASN A 267     -138.13   -129.53                                   
REMARK 500    ASN A 296      -32.41   -140.59                                   
REMARK 500    THR A 397      -97.95   -113.52                                   
REMARK 500    ASN A 435      -11.82     72.99                                   
REMARK 500    ASN A 440     -140.62   -116.02                                   
REMARK 500    GLU A 497       39.75   -142.86                                   
REMARK 500    ASN A 516      115.33   -164.10                                   
REMARK 500    THR A 554      -74.96   -100.10                                   
REMARK 500    TRP A 576       58.96     26.23                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2004        DISTANCE =  6.34 ANGSTROMS                       
REMARK 525    HOH A2044        DISTANCE =  9.70 ANGSTROMS                       
REMARK 525    HOH A2046        DISTANCE =  8.60 ANGSTROMS                       
REMARK 525    HOH A2047        DISTANCE = 11.11 ANGSTROMS                       
REMARK 525    HOH A2048        DISTANCE = 13.67 ANGSTROMS                       
REMARK 525    HOH A2049        DISTANCE = 13.46 ANGSTROMS                       
REMARK 525    HOH A2050        DISTANCE = 15.15 ANGSTROMS                       
REMARK 525    HOH A2051        DISTANCE = 16.94 ANGSTROMS                       
REMARK 525    HOH A2052        DISTANCE =  6.04 ANGSTROMS                       
REMARK 525    HOH A2053        DISTANCE =  8.28 ANGSTROMS                       
REMARK 525    HOH A2054        DISTANCE =  6.95 ANGSTROMS                       
REMARK 525    HOH A2059        DISTANCE =  7.82 ANGSTROMS                       
REMARK 525    HOH A2062        DISTANCE =  8.61 ANGSTROMS                       
REMARK 525    HOH A2064        DISTANCE =  6.49 ANGSTROMS                       
REMARK 525    HOH A2065        DISTANCE =  6.79 ANGSTROMS                       
REMARK 525    HOH A2066        DISTANCE =  8.68 ANGSTROMS                       
REMARK 525    HOH A2067        DISTANCE =  7.62 ANGSTROMS                       
REMARK 525    HOH A2068        DISTANCE =  8.94 ANGSTROMS                       
REMARK 525    HOH A2069        DISTANCE =  8.47 ANGSTROMS                       
REMARK 525    HOH A2070        DISTANCE = 10.05 ANGSTROMS                       
REMARK 525    HOH A2071        DISTANCE =  7.32 ANGSTROMS                       
REMARK 525    HOH A2072        DISTANCE =  9.24 ANGSTROMS                       
REMARK 525    HOH A2074        DISTANCE =  6.78 ANGSTROMS                       
REMARK 525    HOH A2075        DISTANCE =  8.80 ANGSTROMS                       
REMARK 525    HOH A2076        DISTANCE =  7.37 ANGSTROMS                       
REMARK 525    HOH A2077        DISTANCE = 11.06 ANGSTROMS                       
REMARK 525    HOH A2078        DISTANCE = 10.64 ANGSTROMS                       
REMARK 525    HOH A2079        DISTANCE = 12.68 ANGSTROMS                       
REMARK 525    HOH A2080        DISTANCE = 12.97 ANGSTROMS                       
REMARK 525    HOH A2081        DISTANCE = 10.31 ANGSTROMS                       
REMARK 525    HOH A2082        DISTANCE =  9.16 ANGSTROMS                       
REMARK 525    HOH A2083        DISTANCE =  8.24 ANGSTROMS                       
REMARK 525    HOH A2084        DISTANCE =  7.76 ANGSTROMS                       
REMARK 525    HOH A2087        DISTANCE =  6.46 ANGSTROMS                       
REMARK 525    HOH A2090        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH A2091        DISTANCE =  7.66 ANGSTROMS                       
REMARK 525    HOH A2092        DISTANCE =  6.62 ANGSTROMS                       
REMARK 525    HOH A2093        DISTANCE =  7.55 ANGSTROMS                       
REMARK 525    HOH A2097        DISTANCE =  6.09 ANGSTROMS                       
REMARK 525    HOH A2098        DISTANCE =  5.93 ANGSTROMS                       
REMARK 525    HOH A2102        DISTANCE =  6.62 ANGSTROMS                       
REMARK 525    HOH A2104        DISTANCE =  6.27 ANGSTROMS                       
REMARK 525    HOH A2109        DISTANCE =  6.18 ANGSTROMS                       
REMARK 525    HOH A2115        DISTANCE =  6.51 ANGSTROMS                       
REMARK 525    HOH A2120        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH A2126        DISTANCE =  6.05 ANGSTROMS                       
REMARK 525    HOH A2127        DISTANCE =  7.00 ANGSTROMS                       
REMARK 525    HOH A2129        DISTANCE =  7.15 ANGSTROMS                       
REMARK 525    HOH A2130        DISTANCE =  6.64 ANGSTROMS                       
REMARK 525    HOH A2133        DISTANCE =  6.72 ANGSTROMS                       
REMARK 525    HOH A2139        DISTANCE =  5.91 ANGSTROMS                       
REMARK 525    HOH A2142        DISTANCE =  6.80 ANGSTROMS                       
REMARK 525    HOH A2144        DISTANCE =  8.00 ANGSTROMS                       
REMARK 525    HOH A2146        DISTANCE =  9.12 ANGSTROMS                       
REMARK 525    HOH A2148        DISTANCE =  7.98 ANGSTROMS                       
REMARK 525    HOH A2149        DISTANCE =  6.36 ANGSTROMS                       
REMARK 525    HOH A2166        DISTANCE =  6.68 ANGSTROMS                       
REMARK 525    HOH A2191        DISTANCE =  6.86 ANGSTROMS                       
REMARK 525    HOH A2192        DISTANCE =  6.90 ANGSTROMS                       
REMARK 525    HOH A2316        DISTANCE =  6.71 ANGSTROMS                       
REMARK 525    HOH A2367        DISTANCE =  6.75 ANGSTROMS                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "AD" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  9-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A 10-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XYP A1609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF POLYSACCHARIDE         
REMARK 800  RESIDUES 1606 TO 1608                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF POLYSACCHARIDE         
REMARK 800  RESIDUES 1610 TO 1613                                               
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1GNY   RELATED DB: PDB                                   
REMARK 900 XYLAN-BINDING MODULE CBM15                                           
REMARK 900 RELATED ID: 1US3   RELATED DB: PDB                                   
REMARK 900 NATIVE XYLANASE10C FROM CELLVIBRIO JAPONICUS                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 NUMBERING IS CONSISTENT WITH THE SWISSPROT ENTRY FOR                 
REMARK 999 THE GENE.                                                            
REMARK 999 3 MISTAKES WERE DISCOVERED IN RESEQUENCING THE GENE                  
REMARK 999 (G186A, G536A, G594A) AND THE AUTHORS HAVE SENT                      
REMARK 999 CORRECTIONS TO GENBANK.                                              
REMARK 999 RESIDUE 85 (M) AND RESIDUES 607 TO 614 (ELHHHHHH)                    
REMARK 999 IN THE SEQUENCE CRYSTALLIZED HAVE RESULTED FROM CLONING              
REMARK 999 INTO PET VECTOR 22B WITH INCLUSION OF A HIS TAG.                     
REMARK 999 RESIDUES 1 TO 85 IN THE SWISSPROT ENTRY REFER TO A                   
REMARK 999 SIGNAL PEPTIDE WHICH WAS NOT CLONED.                                 
REMARK 999 E385A IS AN ENGINEERED MUTATION.                                     
DBREF  1US2 A   86   606  UNP    Q59675   Q59675_9GAMM    86    606             
SEQADV 1US2 MET A   85  UNP  Q59675              EXPRESSION TAG                 
SEQADV 1US2 ALA A  186  UNP  Q59675    GLY   186 SEE REMARK 999                 
SEQADV 1US2 ALA A  536  UNP  Q59675    GLY   536 SEE REMARK 999                 
SEQADV 1US2 ALA A  594  UNP  Q59675    GLY   594 SEE REMARK 999                 
SEQADV 1US2 ALA A  385  UNP  Q59675    GLU   385 ENGINEERED MUTATION            
SEQADV 1US2 GLU A  607  UNP  Q59675              EXPRESSION TAG                 
SEQADV 1US2 LEU A  608  UNP  Q59675              EXPRESSION TAG                 
SEQADV 1US2 HIS A  609  UNP  Q59675              EXPRESSION TAG                 
SEQADV 1US2 HIS A  610  UNP  Q59675              EXPRESSION TAG                 
SEQADV 1US2 HIS A  611  UNP  Q59675              EXPRESSION TAG                 
SEQADV 1US2 HIS A  612  UNP  Q59675              EXPRESSION TAG                 
SEQADV 1US2 HIS A  613  UNP  Q59675              EXPRESSION TAG                 
SEQADV 1US2 HIS A  614  UNP  Q59675              EXPRESSION TAG                 
SEQRES   1 A  530  MET VAL ALA ALA SER GLU GLY ASN VAL VAL ILE GLU VAL          
SEQRES   2 A  530  ASP MET ALA ASN GLY TRP ARG GLY ASN ALA SER GLY SER          
SEQRES   3 A  530  THR SER HIS SER GLY ILE THR TYR SER ALA ASP GLY VAL          
SEQRES   4 A  530  THR PHE ALA ALA LEU GLY ASP GLY VAL GLY ALA VAL PHE          
SEQRES   5 A  530  ASP ILE ALA ARG PRO THR THR LEU GLU ASP ALA VAL ILE          
SEQRES   6 A  530  ALA MET VAL VAL ASN VAL SER ALA GLU PHE LYS ALA SER          
SEQRES   7 A  530  GLU ALA ASN LEU GLN ILE PHE ALA GLN LEU LYS GLU ASP          
SEQRES   8 A  530  TRP SER LYS GLY GLU TRP ASP CYS LEU ALA ALA SER SER          
SEQRES   9 A  530  GLU LEU THR ALA ASP THR ASP LEU THR LEU THR CYS THR          
SEQRES  10 A  530  ILE ASP GLU ASP ASP ASP LYS PHE ASN GLN THR ALA ARG          
SEQRES  11 A  530  ASP VAL GLN VAL GLY ILE GLN ALA LYS GLY THR PRO ALA          
SEQRES  12 A  530  GLY THR ILE THR ILE LYS SER VAL THR ILE THR LEU ALA          
SEQRES  13 A  530  GLN GLU ALA TYR SER ALA ASN VAL ASP HIS LEU ARG ASP          
SEQRES  14 A  530  LEU ALA PRO SER ASP PHE PRO ILE GLY VAL ALA VAL SER          
SEQRES  15 A  530  ASN THR ASP SER ALA THR TYR ASN LEU LEU THR ASN SER          
SEQRES  16 A  530  ARG GLU GLN ALA VAL VAL LYS LYS HIS PHE ASN HIS LEU          
SEQRES  17 A  530  THR ALA GLY ASN ILE MET LYS MET SER TYR MET GLN PRO          
SEQRES  18 A  530  THR GLU GLY ASN PHE ASN PHE THR ASN ALA ASP ALA PHE          
SEQRES  19 A  530  VAL ASP TRP ALA THR GLU ASN ASN MET THR VAL HIS GLY          
SEQRES  20 A  530  HIS ALA LEU VAL TRP HIS SER ASP TYR GLN VAL PRO ASN          
SEQRES  21 A  530  PHE MET LYS ASN TRP ALA GLY SER ALA GLU ASP PHE LEU          
SEQRES  22 A  530  ALA ALA LEU ASP THR HIS ILE THR THR ILE VAL ASP HIS          
SEQRES  23 A  530  TYR GLU ALA LYS GLY ASN LEU VAL SER TRP ASP VAL VAL          
SEQRES  24 A  530  ASN ALA ALA ILE ASP ASP ASN SER PRO ALA ASN PHE ARG          
SEQRES  25 A  530  THR THR ASP SER ALA PHE TYR VAL LYS SER GLY ASN SER          
SEQRES  26 A  530  SER VAL TYR ILE GLU ARG ALA PHE GLN THR ALA ARG ALA          
SEQRES  27 A  530  ALA ASP PRO ALA VAL ILE LEU TYR TYR ASN ASP TYR ASN          
SEQRES  28 A  530  ILE GLU GLN ASN ASN ALA LYS THR THR LYS MET VAL ASP          
SEQRES  29 A  530  MET VAL LYS ASP PHE GLN ALA ARG SER ILE PRO ILE ASP          
SEQRES  30 A  530  GLY VAL GLY PHE GLN MET HIS VAL CYS MET ASN TYR PRO          
SEQRES  31 A  530  SER ILE ALA ASN ILE SER ALA ALA MET LYS LYS VAL VAL          
SEQRES  32 A  530  ASP LEU GLY LEU LEU VAL LYS ILE THR GLU LEU ASP VAL          
SEQRES  33 A  530  ALA VAL ASN GLN PRO HIS CYS ASP ALA TYR PRO ALA ASN          
SEQRES  34 A  530  LYS ILE ASN PRO LEU THR GLU ALA ALA GLN LEU ALA GLN          
SEQRES  35 A  530  LYS LYS ARG TYR CYS ASP VAL VAL LYS ALA TYR LEU ASP          
SEQRES  36 A  530  THR VAL PRO VAL ASN GLN ARG GLY GLY ILE SER VAL TRP          
SEQRES  37 A  530  GLY THR THR ASP ALA ASN THR TRP LEU ASP GLY LEU TYR          
SEQRES  38 A  530  ARG GLU GLN PHE GLU ASP GLU LYS ILE SER TRP PRO LEU          
SEQRES  39 A  530  LEU PHE ASP ASN ASN TYR ASN ASP LYS PRO ALA LEU ARG          
SEQRES  40 A  530  GLY PHE ALA ASP ALA LEU ILE GLY THR GLN CYS THR ASN          
SEQRES  41 A  530  THR HIS GLU LEU HIS HIS HIS HIS HIS HIS                      
HET    XYP  A1606       9                                                       
HET    XYP  A1607       9                                                       
HET    XYP  A1608       9                                                       
HET    XYP  A1609      10                                                       
HET    XYP  A1610      10                                                       
HET    XYP  A1611       9                                                       
HET    XYP  A1612       9                                                       
HET    XYP  A1613       9                                                       
HETNAM     XYP BETA-D-XYLOPYRANOSE                                              
FORMUL   2  XYP    8(C5 H10 O5)                                                 
FORMUL   4  HOH   *833(H2 O)                                                    
HELIX    1   1 SER A  156  SER A  162  1                                   7    
HELIX    2   2 ALA A  186  LEU A  190  5                                   5    
HELIX    3   3 HIS A  250  ALA A  255  5                                   6    
HELIX    4   4 ASN A  278  PHE A  289  1                                  12    
HELIX    5   5 LYS A  299  GLN A  304  1                                   6    
HELIX    6   6 PHE A  312  ASN A  325  1                                  14    
HELIX    7   7 SER A  338  VAL A  342  5                                   5    
HELIX    8   8 PRO A  343  ASN A  348  1                                   6    
HELIX    9   9 SER A  352  GLY A  375  1                                  24    
HELIX   10  10 SER A  400  SER A  406  1                                   7    
HELIX   11  11 VAL A  411  ASP A  424  1                                  14    
HELIX   12  12 ASN A  440  ARG A  456  1                                  17    
HELIX   13  13 SER A  475  ASP A  488  1                                  14    
HELIX   14  14 THR A  519  VAL A  541  1                                  23    
HELIX   15  15 PRO A  542  ASN A  544  5                                   3    
HELIX   16  16 ASP A  556  ASN A  558  5                                   3    
HELIX   17  17 THR A  559  TYR A  565  1                                   7    
HELIX   18  18 LYS A  587  GLY A  599  1                                  13    
SHEET    1  AA 5 ARG A 104  ALA A 107  0                                        
SHEET    2  AA 5 VAL A 132  ILE A 138 -1  O  GLY A 133   N  ASN A 106           
SHEET    3  AA 5 VAL A 216  LYS A 223 -1  O  VAL A 216   N  ILE A 138           
SHEET    4  AA 5 ASN A 165  LEU A 172 -1  O  ASN A 165   N  LYS A 223           
SHEET    5  AA 5 ASP A 175  GLU A 180 -1  N  ASP A 175   O  LEU A 172           
SHEET    1  AB 5 THR A 117  TYR A 118  0                                        
SHEET    2  AB 5 VAL A 123  ALA A 126 -1  O  THR A 124   N  THR A 117           
SHEET    3  AB 5 THR A 229  THR A 238 -1  O  ILE A 230   N  PHE A 125           
SHEET    4  AB 5 VAL A 148  VAL A 155 -1  O  VAL A 148   N  THR A 238           
SHEET    5  AB 5 LEU A 196  THR A 201 -1  O  LEU A 196   N  VAL A 153           
SHEET    1  AC 2 THR A 142  THR A 143  0                                        
SHEET    2  AC 2 ASN A 210  GLN A 211 -1  O  GLN A 211   N  THR A 142           
SHEET    1  AD10 ILE A 261  VAL A 265  0                                        
SHEET    2  AD10 ARG A 546  VAL A 551  1  O  ILE A 549   N  GLY A 262           
SHEET    3  AD10 LEU A 492  ALA A 501  1  O  VAL A 493   N  GLY A 547           
SHEET    4  AD10 GLY A 462  PHE A 465  1  O  VAL A 463   N  LYS A 494           
SHEET    5  AD10 ILE A 428  ASP A 433  1  O  TYR A 431   N  GLY A 464           
SHEET    6  AD10 SER A 379  ASN A 384  1  O  TRP A 380   N  TYR A 430           
SHEET    7  AD10 THR A 328  VAL A 335  1  O  GLY A 331   N  ASP A 381           
SHEET    8  AD10 HIS A 291  ALA A 294  1  O  LEU A 292   N  HIS A 330           
SHEET    9  AD10 ILE A 261  VAL A 265  1  O  VAL A 263   N  THR A 293           
SHEET   10  AD10 ILE A 261  VAL A 265  0                                        
SSBOND   1 CYS A  183    CYS A  200                          1555   1555  2.03  
SSBOND   2 CYS A  470    CYS A  507                          1555   1555  2.03  
SSBOND   3 CYS A  531    CYS A  602                          1555   1555  2.04  
LINK         C1B XYP A1606                 O4B XYP A1608     1555   1555  1.44  
LINK         C1B XYP A1607                 O4B XYP A1609     1555   1555  1.45  
LINK         O4B XYP A1607                 C1B XYP A1608     1555   1555  1.43  
LINK         O4B XYP A1610                 C1B XYP A1611     1555   1555  1.45  
LINK         O4B XYP A1611                 C1B XYP A1612     1555   1555  1.44  
LINK         O4B XYP A1612                 C1B XYP A1613     1555   1555  1.44  
CISPEP   1 ARG A  140    PRO A  141          0        -0.67                     
CISPEP   2 HIS A  332    ALA A  333          0        -1.82                     
CISPEP   3 SER A  391    PRO A  392          0        -2.71                     
CISPEP   4 TYR A  473    PRO A  474          0        -1.99                     
CISPEP   5 TYR A  510    PRO A  511          0        -0.11                     
CISPEP   6 ASN A  516    PRO A  517          0         5.71                     
SITE     1 AC1  9 LYS A 299  HIS A 332  ASN A 384  GLN A 466                    
SITE     2 AC1  9 GLU A 497  TRP A 552  TRP A 560  XYP A1607                    
SITE     3 AC1  9 HOH A2831                                                     
SITE     1 AC2 17 ASN A 296  LYS A 299  TYR A 340  VAL A 543                    
SITE     2 AC2 17 ASN A 544  TRP A 552  TRP A 560  XYP A1609                    
SITE     3 AC2 17 HOH A2306  HOH A2487  HOH A2822  HOH A2824                    
SITE     4 AC2 17 HOH A2826  HOH A2827  HOH A2828  HOH A2829                    
SITE     5 AC2 17 HOH A2830                                                     
SITE     1 AC3  8 ASN A 106  SER A 108  GLN A 171  TRP A 176                    
SITE     2 AC3  8 TRP A 181  GLN A 217  ALA A 350  HOH A2833                    
CRYST1   44.597   82.686  170.727  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.022423  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012094  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005857        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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