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Database: PDB
Entry: 1W2P
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Original site: 1W2P 
HEADER    HYDROLASE                               07-JUL-04   1W2P              
TITLE     THE 3-DIMENSIONAL STRUCTURE OF A XYLANASE (XYN10A) FROM               
TITLE    2 CELLVIBRIO JAPONICUS                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDO-1,4-BETA-XYLANASE A PRECURSOR;                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 265-611;                        
COMPND   5 SYNONYM: XYLANASE A, 1,4-BETA-D-XYLAN XYLANOHYDROLASE A,             
COMPND   6  XYLA;                                                               
COMPND   7 EC: 3.2.1.8;                                                         
COMPND   8 ENGINEERED: 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: GM83 DE3;                                  
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PET-16B;                                  
SOURCE   8 OTHER_DETAILS: ORGANISM FORMERLY KNOWN AS PSEUDOMONAS                
SOURCE   9  FLUORESCENS                                                         
KEYWDS    XYLANASE, CALCIUM ION, THERMOSTABLE, GLYCOSYLE HYDROLASE,             
KEYWDS   2 FAMILY 10, ERROR PRONE PCR, HYDROLASE                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.J.TAYLOR,F.VINCENT,H.J.GILBERT,G.J.DAVIES                           
REVDAT   5   24-FEB-09 1W2P    1       VERSN                                    
REVDAT   4   30-OCT-06 1W2P    1       REMARK DBREF                             
REVDAT   3   22-DEC-04 1W2P    1       JRNL                                     
REVDAT   2   08-OCT-04 1W2P    1       SSBOND                                   
REVDAT   1   30-SEP-04 1W2P    0                                                
JRNL        AUTH   S.ANDREWS,E.J.TAYLOR,G.PELL,F.VINCENT,V.DUCROS,              
JRNL        AUTH 2 G.J.DAVIES,J.LAKEY,H.J.GILBERT                               
JRNL        TITL   THE USE OF FORCED PROTEIN EVOLUTION TO INVESTIGATE           
JRNL        TITL 2 AND IMPROVE STABILITY OF FAMILY 10 XYLANASES: THE            
JRNL        TITL 3 PRODUCTION OF CA2+-INDEPENDENT STABLE XYLANASES              
JRNL        REF    J.BIOL.CHEM.                  V. 279 54369 2004              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   15452124                                                     
JRNL        DOI    10.1074/JBC.M409044200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0003                                      
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) : 1.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.62                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 117100                         
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) : 0.129                           
REMARK   3   R VALUE            (WORKING SET) : 0.127                           
REMARK   3   FREE R VALUE                     : 0.152                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6186                            
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) : 1.45                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.49                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8479                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.63                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1010                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 476                          
REMARK   3   BIN FREE R VALUE                    : 0.1650                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7022                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 15                                      
REMARK   3   SOLVENT ATOMS            : 896                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 11.54                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : 0.01000                                              
REMARK   3    B33 (A**2) : -0.02000                                             
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): 0.078         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.058         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.032         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.765         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.975                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.971                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7256 ; 0.011 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  6113 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9968 ; 1.402 ; 1.906       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 14269 ; 0.779 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   958 ; 6.445 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   393 ;33.486 ;24.453       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1083 ;11.957 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    55 ;19.608 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1025 ; 0.091 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8765 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1582 ; 0.003 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1369 ; 0.259 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  5647 ; 0.238 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3103 ; 0.194 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  3263 ; 0.102 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   612 ; 0.172 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     1 ; 0.158 ; 0.200       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     3 ; 0.036 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    14 ; 0.198 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    48 ; 0.204 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    63 ; 0.173 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED 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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 1W2P COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JUL-04.                  
REMARK 100 THE PDBE ID CODE IS EBI-20352.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 120.0                              
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM14                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 123424                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 8.800                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 3.8500                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.760                              
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   (%): 44.5                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.2                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       75.10250            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       47.82650            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       47.82650            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      112.65375            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       47.82650            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       47.82650            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       37.55125            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       47.82650            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       47.82650            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      112.65375            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       47.82650            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       47.82650            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       37.55125            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       75.10250            
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 GENERATING THE BIOMOLECULE                                           
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE:  1                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 BIOMOLECULE:  2                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400  CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-BETA-D-XYLOSIDIC          
REMARK 400  LINKAGES IN XYLANS.                                                 
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     0                                                      
REMARK 465     ARG A   348                                                      
REMARK 465     MET B     0                                                      
REMARK 465     ARG B   348                                                      
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;                                
REMARK 480 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 480 I=INSERTION CODE):                                                   
REMARK 480   M RES CSSEQI  ATOMS                                                
REMARK 480     SER B  55    OG   OG                                             
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   OE1  GLN B   228  -  O    HOH B  2308              2.05            
REMARK 500   O    HOH A  2357  -  O    HOH A  2379              1.82            
REMARK 500   O    HOH B  2354  -  O    HOH B  2375              1.85            
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    SER B  26   C  A  SER B  27   N  A    0.262                       
REMARK 500    SER B  55   CB A  SER B  55   OG A    0.545                       
REMARK 500    SER B  86   C  A  TYR B  87   N  A    0.267                       
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    SER B  27   CA  -  C   -  N   ANGL. DEV. = -14.4 DEGREES          
REMARK 500    ALA B 105   CA  -  C   -  N   ANGL. DEV. = -24.6 DEGREES          
REMARK 500    ALA B 105   O   -  C   -  N   ANGL. DEV. =  22.4 DEGREES          
REMARK 500    ARG B 106   C   -  N   -  CA  ANGL. DEV. = -25.3 DEGREES          
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  16       33.44   -156.24                                   
REMARK 500    ASN A 182       -3.13     71.44                                   
REMARK 500    GLU A 246       40.36   -144.81                                   
REMARK 500    ASN B  44      -36.18   -136.00                                   
REMARK 500    GLU B 246       41.87   -146.05                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    SER B  27        -14.79                                           
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 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1348  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 253A  O                                                      
REMARK 620 2 ASN A 258A  O   141.3                                              
REMARK 620 3 ASN A 261A  OD1 148.3  69.4                                        
REMARK 620 4 ASP A 262A  OD1  97.5  95.1  83.3                                  
REMARK 620 5 HOH A2352   O    78.4  70.6 131.0  73.1                            
REMARK 620 6 HOH A2353   O    76.7 141.0  75.1  64.5 126.7                      
REMARK 620 7 ASP A 256A  OD1  80.4 106.0  82.8 148.7 135.5  84.8                
REMARK 620 8 ASP A 256A  OD2  77.8  77.3 111.6 158.8  85.7 132.5  51.7          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1348  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 253B  O                                                      
REMARK 620 2 ASP A 256B  OD1  77.8                                              
REMARK 620 3 ASP A 256B  OD2  77.6  50.1                                        
REMARK 620 4 ASN A 258B  O   145.6  78.8 105.6                                  
REMARK 620 5 ASN A 261B  OD1 146.1 110.2  83.1  66.7                            
REMARK 620 6 ASP A 262B  OD1 103.0 162.1 147.8  92.0  79.4                      
REMARK 620 7 HOH A2352   O    77.4  82.9 130.3  75.0 135.3  79.8                
REMARK 620 8 HOH A2353   O    76.7 121.9  73.8 137.6  71.2  75.1 138.4          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B1348  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B 261   OD1                                                    
REMARK 620 2 ASN B 258   O    67.8                                              
REMARK 620 3 ASP B 262   OD1  81.6  94.6                                        
REMARK 620 4 HOH B2350   O    73.1 139.5  69.3                                  
REMARK 620 5 ASN B 253   O   147.8 142.6 100.9  77.8                            
REMARK 620 6 ASP B 256   OD1 110.7  78.0 161.2 127.0  76.5                      
REMARK 620 7 ASP B 256   OD2  82.8 104.9 148.1  79.6  78.7  50.3                
REMARK 620 8 HOH B2349   O   131.1  71.3  76.2 133.8  79.6  85.0 133.8          
REMARK 620 9 HOH B2351   O   133.7  73.4  77.3 133.0  77.2  84.0 132.2   2.5    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN 10-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A 11-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 700                                                                      
REMARK 700 THE SHEETS PRESENTED AS "BA" 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  CA A1348                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B1348                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1349                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1350                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1351                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1CLX   RELATED DB: PDB                                   
REMARK 900  CATALYTIC CORE OF XYLANASE A                                        
REMARK 900 RELATED ID: 1E5N   RELATED DB: PDB                                   
REMARK 900  E246C MUTANT OF P FLUORESCENS SUBSP.                                
REMARK 900  CELLULOSA XYLANASE A IN COMPLEX WITH                                
REMARK 900  XYLOPENTAOSE                                                        
REMARK 900 RELATED ID: 1E8R   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF TYPE X CBD                                    
REMARK 900 RELATED ID: 1QLD   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF TYPE X CBM                                    
REMARK 900 RELATED ID: 1W2V   RELATED DB: PDB                                   
REMARK 900  THE 3-DIMENSIONAL STRUCTURE OF A                                    
REMARK 900  THERMOSTABLE MUTANT OF A XYLANASE (XYN10A)                          
REMARK 900  FROM CELLVIBRIO JAPONICUS                                           
REMARK 900 RELATED ID: 1W32   RELATED DB: PDB                                   
REMARK 900  THE 3-DIMENSIONAL STRUCTURE OF A                                    
REMARK 900  THERMOSTABLE MUTANT OF A XYLANASE (XYN10A)                          
REMARK 900  FROM CELLVIBRIO JAPONICUS                                           
REMARK 900 RELATED ID: 1W3H   RELATED DB: PDB                                   
REMARK 900  THE 3-DIMENSIONAL STRUCTURE OF A                                    
REMARK 900  THERMOSTABLE MUTANT OF A XYLANASE (XYN10A)                          
REMARK 900  FROM CELLVIBRIO JAPONICUS                                           
REMARK 900 RELATED ID: 1XYS   RELATED DB: PDB                                   
REMARK 900  CATALYTIC CORE OF XYLANASE A E246C MUTANT                           
DBREF  1W2P A    0     0  PDB    1W2P     1W2P             0      0             
DBREF  1W2P A    1   345  UNP    P14768   XYNA_PSEFL     265    609             
DBREF  1W2P A  347   348  UNP    P14768   XYNA_PSEFL     610    611             
DBREF  1W2P B    0     0  PDB    1W2P     1W2P             0      0             
DBREF  1W2P B    1   345  UNP    P14768   XYNA_PSEFL     265    609             
DBREF  1W2P B  347   348  UNP    P14768   XYNA_PSEFL     610    611             
SEQRES   1 A  348  MET GLY LEU ALA SER LEU ALA ASP PHE PRO ILE GLY VAL          
SEQRES   2 A  348  ALA VAL ALA ALA SER GLY GLY ASN ALA ASP ILE PHE THR          
SEQRES   3 A  348  SER SER ALA ARG GLN ASN ILE VAL ARG ALA GLU PHE ASN          
SEQRES   4 A  348  GLN ILE THR ALA GLU ASN ILE MET LYS MET SER TYR MET          
SEQRES   5 A  348  TYR SER GLY SER ASN PHE SER PHE THR ASN SER ASP ARG          
SEQRES   6 A  348  LEU VAL SER TRP ALA ALA GLN ASN GLY GLN THR VAL HIS          
SEQRES   7 A  348  GLY HIS ALA LEU VAL TRP HIS PRO SER TYR GLN LEU PRO          
SEQRES   8 A  348  ASN TRP ALA SER ASP SER ASN ALA ASN PHE ARG GLN ASP          
SEQRES   9 A  348  PHE ALA ARG HIS ILE ASP THR VAL ALA ALA HIS PHE ALA          
SEQRES  10 A  348  GLY GLN VAL LYS SER TRP ASP VAL VAL ASN GLU ALA LEU          
SEQRES  11 A  348  PHE ASP SER ALA ASP ASP PRO ASP GLY ARG GLY SER ALA          
SEQRES  12 A  348  ASN GLY TYR ARG GLN SER VAL PHE TYR ARG GLN PHE GLY          
SEQRES  13 A  348  GLY PRO GLU TYR ILE ASP GLU ALA PHE ARG ARG ALA ARG          
SEQRES  14 A  348  ALA ALA ASP PRO THR ALA GLU LEU TYR TYR ASN ASP PHE          
SEQRES  15 A  348  ASN THR GLU GLU ASN GLY ALA LYS THR THR ALA LEU VAL          
SEQRES  16 A  348  ASN LEU VAL GLN ARG LEU LEU ASN ASN GLY VAL PRO ILE          
SEQRES  17 A  348  ASP GLY VAL GLY PHE GLN MET HIS VAL MET ASN ASP TYR          
SEQRES  18 A  348  PRO SER ILE ALA ASN ILE ARG GLN ALA MET GLN LYS ILE          
SEQRES  19 A  348  VAL ALA LEU SER PRO THR LEU LYS ILE LYS ILE THR GLU          
SEQRES  20 A  348  LEU ASP VAL ARG LEU ASN ASN PRO TYR ASP GLY ASN SER          
SEQRES  21 A  348  SER ASN ASP TYR THR ASN ARG ASN ASP CYS ALA VAL SER          
SEQRES  22 A  348  CYS ALA GLY LEU ASP ARG GLN LYS ALA ARG TYR LYS GLU          
SEQRES  23 A  348  ILE VAL GLN ALA TYR LEU GLU VAL VAL PRO PRO GLY ARG          
SEQRES  24 A  348  ARG GLY GLY ILE THR VAL TRP GLY ILE ALA ASP PRO ASP          
SEQRES  25 A  348  SER TRP LEU TYR THR HIS GLN ASN LEU PRO ASP TRP PRO          
SEQRES  26 A  348  LEU LEU PHE ASN ASP ASN LEU GLN PRO LYS PRO ALA TYR          
SEQRES  27 A  348  GLN GLY VAL VAL GLU ALA LEU SER GLY ARG                      
SEQRES   1 B  348  MET GLY LEU ALA SER LEU ALA ASP PHE PRO ILE GLY VAL          
SEQRES   2 B  348  ALA VAL ALA ALA SER GLY GLY ASN ALA ASP ILE PHE THR          
SEQRES   3 B  348  SER SER ALA ARG GLN ASN ILE VAL ARG ALA GLU PHE ASN          
SEQRES   4 B  348  GLN ILE THR ALA GLU ASN ILE MET LYS MET SER TYR MET          
SEQRES   5 B  348  TYR SER GLY SER ASN PHE SER PHE THR ASN SER ASP ARG          
SEQRES   6 B  348  LEU VAL SER TRP ALA ALA GLN ASN GLY GLN THR VAL HIS          
SEQRES   7 B  348  GLY HIS ALA LEU VAL TRP HIS PRO SER TYR GLN LEU PRO          
SEQRES   8 B  348  ASN TRP ALA SER ASP SER ASN ALA ASN PHE ARG GLN ASP          
SEQRES   9 B  348  PHE ALA ARG HIS ILE ASP THR VAL ALA ALA HIS PHE ALA          
SEQRES  10 B  348  GLY GLN VAL LYS SER TRP ASP VAL VAL ASN GLU ALA LEU          
SEQRES  11 B  348  PHE ASP SER ALA ASP ASP PRO ASP GLY ARG GLY SER ALA          
SEQRES  12 B  348  ASN GLY TYR ARG GLN SER VAL PHE TYR ARG GLN PHE GLY          
SEQRES  13 B  348  GLY PRO GLU TYR ILE ASP GLU ALA PHE ARG ARG ALA ARG          
SEQRES  14 B  348  ALA ALA ASP PRO THR ALA GLU LEU TYR TYR ASN ASP PHE          
SEQRES  15 B  348  ASN THR GLU GLU ASN GLY ALA LYS THR THR ALA LEU VAL          
SEQRES  16 B  348  ASN LEU VAL GLN ARG LEU LEU ASN ASN GLY VAL PRO ILE          
SEQRES  17 B  348  ASP GLY VAL GLY PHE GLN MET HIS VAL MET ASN ASP TYR          
SEQRES  18 B  348  PRO SER ILE ALA ASN ILE ARG GLN ALA MET GLN LYS ILE          
SEQRES  19 B  348  VAL ALA LEU SER PRO THR LEU LYS ILE LYS ILE THR GLU          
SEQRES  20 B  348  LEU ASP VAL ARG LEU ASN ASN PRO TYR ASP GLY ASN SER          
SEQRES  21 B  348  SER ASN ASP TYR THR ASN ARG ASN ASP CYS ALA VAL SER          
SEQRES  22 B  348  CYS ALA GLY LEU ASP ARG GLN LYS ALA ARG TYR LYS GLU          
SEQRES  23 B  348  ILE VAL GLN ALA TYR LEU GLU VAL VAL PRO PRO GLY ARG          
SEQRES  24 B  348  ARG GLY GLY ILE THR VAL TRP GLY ILE ALA ASP PRO ASP          
SEQRES  25 B  348  SER TRP LEU TYR THR HIS GLN ASN LEU PRO ASP TRP PRO          
SEQRES  26 B  348  LEU LEU PHE ASN ASP ASN LEU GLN PRO LYS PRO ALA TYR          
SEQRES  27 B  348  GLN GLY VAL VAL GLU ALA LEU SER GLY ARG                      
HET     CA  A1348       2                                                       
HET     CA  B1348       1                                                       
HET    EDO  B1349       4                                                       
HET    EDO  B1350       4                                                       
HET    EDO  B1351       4                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
FORMUL   3   CA    2(CA 2+)                                                     
FORMUL   5  EDO    3(C2 H6 O2)                                                  
FORMUL   8  HOH   *896(H2 O1)                                                   
HELIX    1   1 GLY A    1  ALA A    6  5                                   6    
HELIX    2   2 SER A   26  PHE A   37  1                                  12    
HELIX    3   3 LYS A   47  TYR A   50  5                                   4    
HELIX    4   4 PHE A   59  ASN A   72  1                                  14    
HELIX    5   5 PRO A   85  LEU A   89  5                                   5    
HELIX    6   6 ASN A   99  PHE A  115  1                                  17    
HELIX    7   7 ASP A  131  ASP A  135  5                                   5    
HELIX    8   8 SER A  148  GLY A  155  1                                   8    
HELIX    9   9 PRO A  157  ASP A  171  1                                  15    
HELIX   10  10 GLY A  187  ASN A  203  1                                  17    
HELIX   11  11 SER A  222  ALA A  235  1                                  14    
HELIX   12  12 ASN A  265  ALA A  270  5                                   6    
HELIX   13  13 CYS A  273  VAL A  294  1                                  22    
HELIX   14  14 ASP A  309  SER A  312  5                                   4    
HELIX   15  15 LYS A  334  GLY A  347  1                                  13    
HELIX   16  16 GLY B    1  ALA B    6  5                                   6    
HELIX   17  17 SER B   26  PHE B   37  1                                  12    
HELIX   18  18 LYS B   47  TYR B   50  5                                   4    
HELIX   19  19 PHE B   59  ASN B   72  1                                  14    
HELIX   20  20 PRO B   85  LEU B   89  5                                   5    
HELIX   21  21 ASN B   99  PHE B  115  1                                  17    
HELIX   22  22 SER B  148  GLY B  155  1                                   8    
HELIX   23  23 PRO B  157  ASP B  171  1                                  15    
HELIX   24  24 GLY B  187  ASN B  203  1                                  17    
HELIX   25  25 SER B  222  ALA B  235  1                                  14    
HELIX   26  26 ASN B  258  ASP B  262  5                                   5    
HELIX   27  27 CYS B  273  VAL B  294  1                                  22    
HELIX   28  28 ASP B  309  SER B  312  5                                   4    
HELIX   29  29 LYS B  334  GLY B  347  1                                  13    
SHEET    1  AA11 ILE A  10  VAL A  14  0                                        
SHEET    2  AA11 ARG A 299  VAL A 304  1  O  ILE A 302   N  GLY A  11           
SHEET    3  AA11 LYS A 241  ARG A 250  1  O  ILE A 242   N  GLY A 300           
SHEET    4  AA11 GLY A 209  PHE A 212  1  O  VAL A 210   N  LYS A 243           
SHEET    5  AA11 GLU A 175  ASP A 180  1  O  TYR A 178   N  GLY A 211           
SHEET    6  AA11 SER A 121  ASN A 126  1  O  TRP A 122   N  TYR A 177           
SHEET    7  AA11 THR A  75  VAL A  82  1  O  GLY A  78   N  ASP A 123           
SHEET    8  AA11 GLN A  39  ALA A  42  1  O  ILE A  40   N  HIS A  77           
SHEET    9  AA11 ILE A  10  VAL A  14  1  O  VAL A  12   N  THR A  41           
SHEET   10  AA11 ARG A 299  VAL A 304  1  O  ILE A 302   N  GLY A  11           
SHEET   11  AA11 ILE A  10  VAL A  14  1  O  GLY A  11   N  VAL A 304           
SHEET    1  AB 2 TYR A  52  SER A  53  0                                        
SHEET    2  AB 2 ASN A  56  PHE A  57 -1  O  ASN A  56   N  SER A  53           
SHEET    1  AC 2 THR A 316  HIS A 317  0                                        
SHEET    2  AC 2 LEU A 320  PRO A 321 -1  O  LEU A 320   N  HIS A 317           
SHEET    1  BA10 ILE B  10  VAL B  14  0                                        
SHEET    2  BA10 ARG B 299  VAL B 304  1  O  ILE B 302   N  GLY B  11           
SHEET    3  BA10 LYS B 241  ARG B 250  1  O  ILE B 242   N  GLY B 300           
SHEET    4  BA10 GLY B 209  PHE B 212  1  O  VAL B 210   N  LYS B 243           
SHEET    5  BA10 GLU B 175  ASP B 180  1  O  TYR B 178   N  GLY B 211           
SHEET    6  BA10 SER B 121  ASN B 126  1  O  TRP B 122   N  TYR B 177           
SHEET    7  BA10 THR B  75  VAL B  82  1  O  VAL B  76   N  SER B 121           
SHEET    8  BA10 GLN B  39  ALA B  42  1  O  ILE B  40   N  HIS B  77           
SHEET    9  BA10 ILE B  10  VAL B  14  1  O  VAL B  12   N  THR B  41           
SHEET   10  BA10 ILE B  10  VAL B  14                                           
SHEET    1  BB 2 TYR B  52  SER B  53  0                                        
SHEET    2  BB 2 ASN B  56  PHE B  57 -1  O  ASN B  56   N  SER B  53           
SHEET    1  BC 2 THR B 316  HIS B 317  0                                        
SHEET    2  BC 2 LEU B 320  PRO B 321 -1  O  LEU B 320   N  HIS B 317           
SSBOND   1 CYS A  269    CYS A  273                          1555   1555  2.10  
SSBOND   2 CYS A  269    CYS A  273                          1555   1555  2.12  
SSBOND   3 CYS B  269    CYS B  273                          1555   1555  2.05  
LINK        CA  A CA A1348                 O  AASN A 253     1555   1555  2.32  
LINK        CA  A CA A1348                 O  AASN A 258     1555   1555  2.37  
LINK        CA  A CA A1348                 OD1AASN A 261     1555   1555  2.38  
LINK        CA  A CA A1348                 OD1AASP A 262     1555   1555  2.43  
LINK        CA  A CA A1348                 O   HOH A2352     1555   1555  2.53  
LINK        CA  A CA A1348                 O   HOH A2353     1555   1555  2.68  
LINK        CA  A CA A1348                 OD1AASP A 256     1555   1555  2.54  
LINK        CA  A CA A1348                 OD2AASP A 256     1555   1555  2.42  
LINK        CA  B CA A1348                 O  BASN A 253     1555   1555  2.56  
LINK        CA  B CA A1348                 OD1BASP A 256     1555   1555  2.45  
LINK        CA  B CA A1348                 OD2BASP A 256     1555   1555  2.60  
LINK        CA  B CA A1348                 O  BASN A 258     1555   1555  2.46  
LINK        CA  B CA A1348                 OD1BASN A 261     1555   1555  2.52  
LINK        CA  B CA A1348                 OD1BASP A 262     1555   1555  2.43  
LINK        CA  B CA A1348                 O   HOH A2352     1555   1555  2.50  
LINK        CA  B CA A1348                 O   HOH A2353     1555   1555  2.48  
LINK        CA    CA B1348                 O   ASN B 258     1555   1555  2.42  
LINK        CA    CA B1348                 OD1 ASP B 262     1555   1555  2.36  
LINK        CA    CA B1348                 O   HOH B2350     1555   1555  2.56  
LINK        CA    CA B1348                 O   ASN B 253     1555   1555  2.40  
LINK        CA    CA B1348                 OD1 ASP B 256     1555   1555  2.47  
LINK        CA    CA B1348                 OD2 ASP B 256     1555   1555  2.60  
LINK        CA    CA B1348                 O   HOH B2349     1555   1555  2.53  
LINK        CA    CA B1348                 O   HOH B2351     1555   1555  2.49  
LINK        CA    CA B1348                 OD1 ASN B 261     1555   1555  2.43  
CISPEP   1 HIS A   79    ALA A   80          0         6.90                     
CISPEP   2 TYR A  220    PRO A  221          0        -2.64                     
CISPEP   3 HIS B   79    ALA B   80          0         9.09                     
CISPEP   4 TYR B  220    PRO B  221          0        -5.06                     
SITE     1 AC1  7 ASN A 253  ASP A 256  ASN A 258  ASN A 261                    
SITE     2 AC1  7 ASP A 262  HOH A2352  HOH A2353                               
SITE     1 AC2  8 ASN B 253  ASP B 256  ASN B 258  ASN B 261                    
SITE     2 AC2  8 ASP B 262  HOH B2349  HOH B2350  HOH B2351                    
SITE     1 AC3  3 ASP B 131  SER B 132  HOH B2444                               
SITE     1 AC4  3 ARG B 168  HOH B2445  HOH B2447                               
SITE     1 AC5  8 TYR A  52  GLY A  54  PRO A  90  ASN A  91                    
SITE     2 AC5  8 TRP A  92  HOH B2448  HOH B2449  HOH B2450                    
CRYST1   95.653   95.653  150.205  90.00  90.00  90.00 P 43 21 2    16          
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      0.010454  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010454  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006658        0.00000                         
MTRIX1   1  0.997000 -0.054000  0.048000        7.73592    1                    
MTRIX2   1  0.057000  0.187000 -0.981000       68.59010    1                    
MTRIX3   1  0.044000  0.981000  0.190000      -30.83216    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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