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Database: PDB
Entry: 4PUD
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Original site: 4PUD 
HEADER    HYDROLASE                               13-MAR-14   4PUD              
TITLE     EXTRACELLULR XYLANASE FROM GEOBACILLUS STEAROTHERMOPHILUS: E159Q      
TITLE    2 MUTANT, WITH XYLOPENTAOSE IN ACTIVE SITE                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDO-1,4-BETA-XYLANASE;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: XYLANASE, 1,4-BETA-D-XYLAN XYLANOHYDROLASE;                 
COMPND   5 EC: 3.2.1.8;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: GEOBACILLUS STEAROTHERMOPHILUS;                 
SOURCE   3 ORGANISM_TAXID: 1422;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TIM BARREL, HYDROLASE                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.D.DANN,H.V.SOLOMON,S.LANSKY,A.BEN-DAVID,N.LAVID,R.SALAMA,Y.SHOHAM,  
AUTHOR   2 G.SHOHAM                                                             
REVDAT   1   18-MAR-15 4PUD    0                                                
JRNL        AUTH   R.D.DANN,H.V.SOLOMON,S.LANSKY,A.BEN-DAVID,N.LAVID,R.SALAMA,  
JRNL        AUTH 2 Y.SHOHAM,G.SHOHAM                                            
JRNL        TITL   EXTRACELLULR XYLANASE FROM GEOBACILLUS STEAROTHERMOPHILUS:   
JRNL        TITL 2 E159Q MUTANT, WITH XYLOPENTAOSE IN ACTIVE SITE.              
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.01 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.01                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 36157                          
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) : 0.148                           
REMARK   3   R VALUE            (WORKING SET) : 0.146                           
REMARK   3   FREE R VALUE                     : 0.183                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1901                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.01                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2546                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.54                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2140                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 136                          
REMARK   3   BIN FREE R VALUE                    : 0.2450                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3036                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 58                                      
REMARK   3   SOLVENT ATOMS            : 354                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.83                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.98000                                              
REMARK   3    B22 (A**2) : 1.37000                                              
REMARK   3    B33 (A**2) : -1.25000                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -0.54000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.121         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.118         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.071         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.518         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.974                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.959                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3282 ; 0.020 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3073 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4472 ; 2.029 ; 1.959       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7098 ; 0.928 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   391 ; 6.551 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   169 ;34.061 ;25.207       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   559 ;15.210 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;15.574 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   475 ; 0.129 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3748 ; 0.011 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   768 ; 0.003 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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 RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4PUD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-APR-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB085229.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-SEP-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : A HOME SOURCE WAS USED             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS HTC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36157                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.010                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 5.700                              
REMARK 200  R MERGE                    (I) : 0.09800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.01                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC 5.7.0032                                       
REMARK 200 STARTING MODEL: 1R86                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG 4000, 0.1M MES, 10MM ZINC        
REMARK 280  CHLORIDE, PH 6.7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       60.69700            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       30.83200            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       60.69700            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       30.83200            
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 515  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 742  LIES ON A SPECIAL POSITION.                          
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 114    CG   CD   CE   NZ                                   
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   NZ   LYS A   182     OE1  GLU A   224              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CE1  HIS A   378    CL     CL A   409     4445     2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 104   C   -  N   -  CA  ANGL. DEV. =  -9.4 DEGREES          
REMARK 500    LEU A 214   CA  -  CB  -  CG  ANGL. DEV. =  14.0 DEGREES          
REMARK 500    ASP A 377   CB  -  CG  -  OD1 ANGL. DEV. =   8.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  59      -31.28   -136.29                                   
REMARK 500    GLN A 102       74.46     19.95                                   
REMARK 500    ASN A 169       56.61    -94.99                                   
REMARK 500    GLU A 265       45.56   -141.96                                   
REMARK 500    TRP A 316       57.08    -90.14                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                              ZN A 417  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 365   OD1                                                    
REMARK 620 2 HIS A  11   NE2 120.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 410  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 322   NE2                                                    
REMARK 620 2 HOH A 843   O   113.6                                              
REMARK 620 3 GLU A  58   OE1  97.1 109.2                                        
REMARK 620 4 GLU A  58   OE2 120.9 124.0  54.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 413  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 282   OD2                                                    
REMARK 620 2 HOH A 844   O   112.6                                              
REMARK 620 3 HOH A 760   O    92.1  89.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 406  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 746   O                                                      
REMARK 620 2 ASP A  21   OD2 177.3                                              
REMARK 620 3 HOH A 795   O    90.4  91.9                                        
REMARK 620 4 HOH A 745   O    85.3  93.3  90.3                                  
REMARK 620 5 HOH A 772   O    90.0  91.2  91.1 175.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 411  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 297   OD1                                                    
REMARK 620 2 ALA A 374   O    97.5                                              
REMARK 620 3 ASP A 377   OD1 150.4  82.2                                        
REMARK 620 4 LYS A 379   O    92.2 167.1  85.2                                  
REMARK 620 5 HOH A 532   O   140.0  88.4  69.6  89.7                            
REMARK 620 6 HOH A 531   O    73.9  91.9  76.5  82.5 145.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 412  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  27   O                                                      
REMARK 620 2 ILE A 310   O    96.2                                              
REMARK 620 3 SER A 307   O   100.8  83.1                                        
REMARK 620 4 HOH A 533   O    89.2 107.0 165.0                                  
REMARK 620 5 HOH A 624   O   169.1  84.7  90.1  80.1                            
REMARK 620 6 HOH A 588   O    80.6 166.6  84.7  86.0 100.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 406                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 407                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 408                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 409                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 410                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 411                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 412                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 413                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 414                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 415                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 416                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 417                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF POLYSACCHARIDE         
REMARK 800  RESIDUES 401 TO 405                                                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1R86   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1HIZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3MMD   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1R85   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1R87   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4PRW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4PUE   RELATED DB: PDB                                   
DBREF  4PUD A    9   379  UNP    P40943   XYN1_GEOSE      37    407             
SEQADV 4PUD GLN A  159  UNP  P40943    GLU   187 ENGINEERED MUTATION            
SEQRES   1 A  371  LYS PRO HIS ILE SER ALA LEU ASN ALA PRO GLN LEU ASP          
SEQRES   2 A  371  GLN ARG TYR LYS ASN GLU PHE THR ILE GLY ALA ALA VAL          
SEQRES   3 A  371  GLU PRO TYR GLN LEU GLN ASN GLU LYS ASP VAL GLN MET          
SEQRES   4 A  371  LEU LYS ARG HIS PHE ASN SER ILE VAL ALA GLU ASN VAL          
SEQRES   5 A  371  MET LYS PRO ILE SER ILE GLN PRO GLU GLU GLY LYS PHE          
SEQRES   6 A  371  ASN PHE GLU GLN ALA ASP ARG ILE VAL LYS PHE ALA LYS          
SEQRES   7 A  371  ALA ASN GLY MET ASP ILE ARG PHE HIS THR LEU VAL TRP          
SEQRES   8 A  371  HIS SER GLN VAL PRO GLN TRP PHE PHE LEU ASP LYS GLU          
SEQRES   9 A  371  GLY LYS PRO MET VAL ASN GLU THR ASP PRO VAL LYS ARG          
SEQRES  10 A  371  GLU GLN ASN LYS GLN LEU LEU LEU LYS ARG LEU GLU THR          
SEQRES  11 A  371  HIS ILE LYS THR ILE VAL GLU ARG TYR LYS ASP ASP ILE          
SEQRES  12 A  371  LYS TYR TRP ASP VAL VAL ASN GLN VAL VAL GLY ASP ASP          
SEQRES  13 A  371  GLY LYS LEU ARG ASN SER PRO TRP TYR GLN ILE ALA GLY          
SEQRES  14 A  371  ILE ASP TYR ILE LYS VAL ALA PHE GLN ALA ALA ARG LYS          
SEQRES  15 A  371  TYR GLY GLY ASP ASN ILE LYS LEU TYR MET ASN ASP TYR          
SEQRES  16 A  371  ASN THR GLU VAL GLU PRO LYS ARG THR ALA LEU TYR ASN          
SEQRES  17 A  371  LEU VAL LYS GLN LEU LYS GLU GLU GLY VAL PRO ILE ASP          
SEQRES  18 A  371  GLY ILE GLY HIS GLN SER HIS ILE GLN ILE GLY TRP PRO          
SEQRES  19 A  371  SER GLU ALA GLU ILE GLU LYS THR ILE ASN MET PHE ALA          
SEQRES  20 A  371  ALA LEU GLY LEU ASP ASN GLN ILE THR GLU LEU ASP VAL          
SEQRES  21 A  371  SER MET TYR GLY TRP PRO PRO ARG ALA TYR PRO THR TYR          
SEQRES  22 A  371  ASP ALA ILE PRO LYS GLN LYS PHE LEU ASP GLN ALA ALA          
SEQRES  23 A  371  ARG TYR ASP ARG LEU PHE LYS LEU TYR GLU LYS LEU SER          
SEQRES  24 A  371  ASP LYS ILE SER ASN VAL THR PHE TRP GLY ILE ALA ASP          
SEQRES  25 A  371  ASN HIS THR TRP LEU ASP SER ARG ALA ASP VAL TYR TYR          
SEQRES  26 A  371  ASP ALA ASN GLY ASN VAL VAL VAL ASP PRO ASN ALA PRO          
SEQRES  27 A  371  TYR ALA LYS VAL GLU LYS GLY LYS GLY LYS ASP ALA PRO          
SEQRES  28 A  371  PHE VAL PHE GLY PRO ASP TYR LYS VAL LYS PRO ALA TYR          
SEQRES  29 A  371  TRP ALA ILE ILE ASP HIS LYS                                  
HET    XYP  A 401       9                                                       
HET    XYP  A 402       9                                                       
HET    XYP  A 403       9                                                       
HET    XYP  A 404       9                                                       
HET    XYP  A 405      10                                                       
HET     ZN  A 406       1                                                       
HET     ZN  A 407       1                                                       
HET     CL  A 408       1                                                       
HET     CL  A 409       1                                                       
HET     ZN  A 410       1                                                       
HET     ZN  A 411       1                                                       
HET     ZN  A 412       1                                                       
HET     ZN  A 413       1                                                       
HET     CL  A 414       1                                                       
HET     ZN  A 415       1                                                       
HET     ZN  A 416       1                                                       
HET     ZN  A 417       1                                                       
HETNAM     XYP BETA-D-XYLOPYRANOSE                                              
HETNAM      ZN ZINC ION                                                         
HETNAM      CL CHLORIDE ION                                                     
FORMUL   2  XYP    5(C5 H10 O5)                                                 
FORMUL   3   ZN    9(ZN 2+)                                                     
FORMUL   5   CL    3(CL 1-)                                                     
FORMUL  15  HOH   *354(H2 O)                                                    
HELIX    1   1 SER A   13  ALA A   17  5                                   5    
HELIX    2   2 GLN A   19  TYR A   24  1                                   6    
HELIX    3   3 GLU A   35  GLN A   40  5                                   6    
HELIX    4   4 ASN A   41  PHE A   52  1                                  12    
HELIX    5   5 LYS A   62  GLN A   67  1                                   6    
HELIX    6   6 PHE A   75  ASN A   88  1                                  14    
HELIX    7   7 PRO A  104  LEU A  109  5                                   6    
HELIX    8   8 PRO A  115  GLU A  119  5                                   5    
HELIX    9   9 ASP A  121  LYS A  148  1                                  28    
HELIX   10  10 SER A  170  GLY A  177  1                                   8    
HELIX   11  11 ILE A  178  GLY A  193  1                                  16    
HELIX   12  12 PRO A  209  GLU A  224  1                                  16    
HELIX   13  13 SER A  243  LEU A  257  1                                  15    
HELIX   14  14 THR A  280  ILE A  284  5                                   5    
HELIX   15  15 PRO A  285  LEU A  306  1                                  22    
HELIX   16  16 THR A  323  ALA A  329  5                                   7    
HELIX   17  17 LYS A  369  ASP A  377  1                                   9    
SHEET    1   A10 HIS A 236  GLN A 238  0                                        
SHEET    2   A10 ASP A 260  SER A 269  1  O  SER A 269   N  ILE A 237           
SHEET    3   A10 ILE A 310  PHE A 315  1  O  THR A 314   N  ILE A 263           
SHEET    4   A10 THR A  29  VAL A  34  1  N  GLY A  31   O  PHE A 315           
SHEET    5   A10 SER A  54  ALA A  57  1  O  VAL A  56   N  VAL A  34           
SHEET    6   A10 ASP A  91  VAL A  98  1  O  ARG A  93   N  ILE A  55           
SHEET    7   A10 TYR A 153  ASN A 158  1  O  ASP A 155   N  PHE A  94           
SHEET    8   A10 LYS A 197  ASP A 202  1  O  TYR A 199   N  TRP A 154           
SHEET    9   A10 GLY A 230  HIS A 233  1  O  GLY A 232   N  MET A 200           
SHEET   10   A10 ASP A 260  SER A 269  1  O  GLN A 262   N  HIS A 233           
SHEET    1   B 3 VAL A 339  VAL A 340  0                                        
SHEET    2   B 3 VAL A 331  TYR A 333 -1  N  TYR A 332   O  VAL A 340           
SHEET    3   B 3 LYS A 349  GLU A 351 -1  O  GLU A 351   N  VAL A 331           
LINK         C1B XYP A 401                 O4B XYP A 402     1555   1555  1.40  
LINK         C1B XYP A 404                 O4B XYP A 405     1555   1555  1.43  
LINK         C1B XYP A 403                 O4B XYP A 404     1555   1555  1.44  
LINK         C1B XYP A 402                 O4B XYP A 403     1555   1555  1.47  
LINK         OD1 ASP A 365                ZN    ZN A 417     1555   1555  1.89  
LINK         NE2 HIS A 322                ZN    ZN A 410     1555   1555  1.96  
LINK        ZN    ZN A 410                 O   HOH A 843     1555   1555  1.99  
LINK         OD2 ASP A 282                ZN    ZN A 413     1555   1555  1.99  
LINK         NE2 HIS A  11                ZN    ZN A 417     1555   1555  2.02  
LINK        ZN    ZN A 406                 O   HOH A 746     1555   1555  2.03  
LINK         OD2 ASP A  21                ZN    ZN A 406     1555   1555  2.05  
LINK        ZN    ZN A 406                 O   HOH A 795     1555   1555  2.11  
LINK        ZN    ZN A 406                 O   HOH A 745     1555   1555  2.12  
LINK        ZN    ZN A 406                 O   HOH A 772     1555   1555  2.14  
LINK         OD1 ASP A 282                ZN    ZN A 416     1555   1555  2.21  
LINK         OD1 ASP A 297                ZN    ZN A 411     1555   1555  2.21  
LINK        ZN    ZN A 413                 O   HOH A 844     1555   1555  2.21  
LINK         OE1 GLU A  58                ZN    ZN A 410     1555   1555  2.25  
LINK         O   GLU A  27                ZN    ZN A 412     1555   1555  2.29  
LINK         O   ALA A 374                ZN    ZN A 411     1555   1555  2.30  
LINK         O   ILE A 310                ZN    ZN A 412     1555   1555  2.30  
LINK         O   SER A 307                ZN    ZN A 412     1555   1555  2.31  
LINK         OD1 ASP A 377                ZN    ZN A 411     1555   1555  2.32  
LINK         O   LYS A 379                ZN    ZN A 411     1555   1555  2.34  
LINK        ZN    ZN A 411                 O   HOH A 532     1555   1555  2.36  
LINK        ZN    ZN A 411                 O   HOH A 531     1555   1555  2.38  
LINK        ZN    ZN A 412                 O   HOH A 533     1555   1555  2.38  
LINK        ZN    ZN A 413                 O   HOH A 760     1555   1555  2.45  
LINK         OE2 GLU A  58                ZN    ZN A 410     1555   1555  2.52  
LINK        ZN    ZN A 412                 O   HOH A 624     1555   1555  2.53  
LINK        ZN    ZN A 412                 O   HOH A 588     1555   1555  2.65  
CISPEP   1 HIS A   95    THR A   96          0         0.39                     
CISPEP   2 GLU A  208    PRO A  209          0         2.02                     
CISPEP   3 TRP A  241    PRO A  242          0        -3.66                     
CISPEP   4 TRP A  273    PRO A  274          0        -6.82                     
SITE     1 AC1  6 ASP A  21   ZN A 415  HOH A 745  HOH A 746                    
SITE     2 AC1  6 HOH A 772  HOH A 795                                          
SITE     1 AC2  5 HIS A  11  ASN A  26  GLU A  27  ASP A 365                    
SITE     2 AC2  5  ZN A 417                                                     
SITE     1 AC3  6 GLU A  58  HIS A 322  TRP A 324  XYP A 401                    
SITE     2 AC3  6  ZN A 410  HOH A 843                                          
SITE     1 AC4  5 ASP A 282  HIS A 378   ZN A 416  HOH A 719                    
SITE     2 AC4  5 HOH A 845                                                     
SITE     1 AC5  5 GLU A  58  HIS A 322  XYP A 401   CL A 408                    
SITE     2 AC5  5 HOH A 843                                                     
SITE     1 AC6  7 ASP A 297  ALA A 374  ASP A 377  LYS A 379                    
SITE     2 AC6  7  CL A 414  HOH A 531  HOH A 532                               
SITE     1 AC7  6 GLU A  27  SER A 307  ILE A 310  HOH A 533                    
SITE     2 AC7  6 HOH A 588  HOH A 624                                          
SITE     1 AC8  5 ASP A 282  HIS A 378  HOH A 577  HOH A 760                    
SITE     2 AC8  5 HOH A 844                                                     
SITE     1 AC9  7 ASP A 297  LYS A 301  ALA A 374  LYS A 379                    
SITE     2 AC9  7  ZN A 411  HOH A 532  HOH A 583                               
SITE     1 BC1  7 ASP A  21  LYS A  49  PHE A  52   ZN A 406                    
SITE     2 BC1  7 HOH A 745  HOH A 746  HOH A 772                               
SITE     1 BC2  4 ARG A  23  ASP A 282   CL A 409  HOH A 824                    
SITE     1 BC3  4 HIS A  11  GLU A  27  ASP A 365   ZN A 407                    
SITE     1 BC4 25 GLU A  58  ASN A  59  LYS A  62  HIS A  95                    
SITE     2 BC4 25 GLN A 102  ASN A 158  GLN A 159  ASN A 204                    
SITE     3 BC4 25 GLN A 234  HIS A 236  GLN A 238  TRP A 241                    
SITE     4 BC4 25 GLU A 265  TRP A 273  TRP A 316  TRP A 324                    
SITE     5 BC4 25 ARG A 328   CL A 408   ZN A 410  HOH A 550                    
SITE     6 BC4 25 HOH A 574  HOH A 697  HOH A 737  HOH A 793                    
SITE     7 BC4 25 HOH A 838                                                     
CRYST1  121.394   61.664   89.321  90.00 119.37  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008238  0.000000  0.004637        0.00000                         
SCALE2      0.000000  0.016217  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012847        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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