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Database: PDB
Entry: 1UKR
LinkDB: 1UKR
Original site: 1UKR 
HEADER    HYDROLASE                               23-AUG-96   1UKR              
TITLE     STRUCTURE OF ENDO-1,4-BETA-XYLANASE C                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDO-1,4-B-XYLANASE I;                                     
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: XYLANASE;                                                   
COMPND   5 EC: 3.2.1.8;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ASPERGILLUS NIGER;                              
SOURCE   3 ORGANISM_TAXID: 5061;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    XYLAN DEGRADATION, HYDROLASE, GLYCOSIDASE, SIGNAL                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    U.KRENGEL,B.W.DIJKSTRA                                                
REVDAT   2   24-FEB-09 1UKR    1       VERSN                                    
REVDAT   1   24-DEC-97 1UKR    0                                                
JRNL        AUTH   U.KRENGEL,B.W.DIJKSTRA                                       
JRNL        TITL   THREE-DIMENSIONAL STRUCTURE OF                               
JRNL        TITL 2 ENDO-1,4-BETA-XYLANASE I FROM ASPERGILLUS NIGER:             
JRNL        TITL 3 MOLECULAR BASIS FOR ITS LOW PH OPTIMUM.                      
JRNL        REF    J.MOL.BIOL.                   V. 263    70 1996              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   8890913                                                      
JRNL        DOI    10.1006/JMBI.1996.0556                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   U.KRENGEL,H.J.ROZEBOOM,K.H.KALK,B.W.DIJKSTRA                 
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC             
REMARK   1  TITL 2 ANALYSIS OF ENDO-1,4-BETA-XYALANASE I FROM                   
REMARK   1  TITL 3 ASPERGILLUS NIGER                                            
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  52   571 1996              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 28728                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5556                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 288                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.24                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.29                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 27.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.88                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: REFINEMENT INCLUDED NCS-RESTRAINTS        
REMARK   3  AT PLACES WITHOUT CRYSTAL CONTACTS. ONLY IN THE FINAL               
REMARK   3  REFINEMENT CYCLE ALL DATA WERE INCLUDED. IN THE EARLIER STAGES      
REMARK   3  OF REFINEMENT, 10% OF THE DATA WERE TAKEN TO CALCULATE A FREE       
REMARK   3  R-FACTOR (R=17.7 AND RFREE=21.9 %, RESPECTIVELY).                   
REMARK   4                                                                      
REMARK   4 1UKR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-OCT-94                          
REMARK 200  TEMPERATURE           (KELVIN) : 295                                
REMARK 200  PH                             : 4.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X31                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33131                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.060                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.3                               
REMARK 200  DATA REDUNDANCY                : 4.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08200                            
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) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: BRUTE                                                 
REMARK 200 STARTING MODEL: TRICHODERMA HARZIANUM XYLANASE, PDB ENTRY 1XND.      
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SITTING DROP SETUP USING                 
REMARK 280  SILICONIZED GLASS WELLS USING 15 MICROLITER DROPS AT ROOM           
REMARK 280  TEMPERATURE AND MACROSEEDING. PROTEIN SOLUTION: 4.5 MG/ML IN        
REMARK 280  10 MM NA ACETATE PH 4.7. RESERVOIR SOLUTION: 1.5 ML 1.8 M           
REMARK 280  NA2S2O3 (PH 8.0)., VAPOR DIFFUSION - SITTING DROP -                 
REMARK 280  MACROSEEDING                                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       42.15000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       56.90000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.65000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       56.90000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       42.15000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.65000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     SER A   184                                                      
REMARK 465     SER B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     SER B   184                                                      
REMARK 465     SER C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     SER C   184                                                      
REMARK 465     SER D     1                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     SER D   184                                                      
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    VAL A  34   CG1 -  CB  -  CG2 ANGL. DEV. = -11.4 DEGREES          
REMARK 500    ARG A 134   CD  -  NE  -  CZ  ANGL. DEV. =   8.7 DEGREES          
REMARK 500    ARG A 134   NE  -  CZ  -  NH1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ARG A 134   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.4 DEGREES          
REMARK 500    ARG A 138   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES          
REMARK 500    VAL B  34   CG1 -  CB  -  CG2 ANGL. DEV. = -12.1 DEGREES          
REMARK 500    ARG B 134   NE  -  CZ  -  NH1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ARG B 134   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.7 DEGREES          
REMARK 500    ARG B 138   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    VAL C  34   CG1 -  CB  -  CG2 ANGL. DEV. = -11.3 DEGREES          
REMARK 500    ARG C 134   CD  -  NE  -  CZ  ANGL. DEV. =   8.6 DEGREES          
REMARK 500    ARG C 134   NE  -  CZ  -  NH1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ARG C 134   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.5 DEGREES          
REMARK 500    ARG C 138   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    VAL D  34   CG1 -  CB  -  CG2 ANGL. DEV. = -11.5 DEGREES          
REMARK 500    ARG D 134   CD  -  NE  -  CZ  ANGL. DEV. =   8.7 DEGREES          
REMARK 500    ARG D 134   NE  -  CZ  -  NH1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG D 134   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.5 DEGREES          
REMARK 500    ARG D 138   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 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    ALA A  60       37.16   -148.36                                   
REMARK 500    ASN A 163     -143.48    -97.29                                   
REMARK 500    ALA B  60       30.95   -145.01                                   
REMARK 500    ASN B 163     -143.31    -97.43                                   
REMARK 500    ALA C  60       45.71   -146.56                                   
REMARK 500    ASN C 163     -143.81    -97.23                                   
REMARK 500    ALA D  60       30.83   -146.42                                   
REMARK 500    ASN D 117       63.48     36.21                                   
REMARK 500    ASN D 163     -143.61    -97.92                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1261        DISTANCE =  5.37 ANGSTROMS                       
REMARK 525    HOH A1264        DISTANCE = 10.33 ANGSTROMS                       
REMARK 525    HOH A1268        DISTANCE =  7.16 ANGSTROMS                       
REMARK 525    HOH A1271        DISTANCE =  8.38 ANGSTROMS                       
REMARK 525    HOH A1276        DISTANCE =  9.23 ANGSTROMS                       
REMARK 525    HOH A1284        DISTANCE = 12.25 ANGSTROMS                       
REMARK 525    HOH A1285        DISTANCE =  5.51 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: EA                                                  
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: GLU A 79 AND GLU A 170 REFER TO THE CATALYTIC      
REMARK 800  ACIDIC RESIDUES.                                                    
REMARK 800 SITE_IDENTIFIER: EB                                                  
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: GLU B 79 AND GLU B 170 REFER TO THE CATALYTIC      
REMARK 800  ACIDIC RESIDUES.                                                    
REMARK 800 SITE_IDENTIFIER: EC                                                  
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: GLU C 79 AND GLU C 170 REFER TO THE CATALYTIC      
REMARK 800  ACIDIC RESIDUES.                                                    
REMARK 800 SITE_IDENTIFIER: ED                                                  
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: GLU D 79 AND GLU D 170 REFER TO THE CATALYTIC      
REMARK 800  ACIDIC RESIDUES.                                                    
DBREF  1UKR A    1   184  UNP    P55329   XYN1_ASPNG      28    211             
DBREF  1UKR B    1   184  UNP    P55329   XYN1_ASPNG      28    211             
DBREF  1UKR C    1   184  UNP    P55329   XYN1_ASPNG      28    211             
DBREF  1UKR D    1   184  UNP    P55329   XYN1_ASPNG      28    211             
SEQRES   1 A  184  SER ALA GLY ILE ASN TYR VAL GLN ASN TYR ASN GLY ASN          
SEQRES   2 A  184  LEU GLY ASP PHE THR TYR ASP GLU SER ALA GLY THR PHE          
SEQRES   3 A  184  SER MET TYR TRP GLU ASP GLY VAL SER SER ASP PHE VAL          
SEQRES   4 A  184  VAL GLY LEU GLY TRP THR THR GLY SER SER ASN ALA ILE          
SEQRES   5 A  184  THR TYR SER ALA GLU TYR SER ALA SER GLY SER ALA SER          
SEQRES   6 A  184  TYR LEU ALA VAL TYR GLY TRP VAL ASN TYR PRO GLN ALA          
SEQRES   7 A  184  GLU TYR TYR ILE VAL GLU ASP TYR GLY ASP TYR ASN PRO          
SEQRES   8 A  184  CYS SER SER ALA THR SER LEU GLY THR VAL TYR SER ASP          
SEQRES   9 A  184  GLY SER THR TYR GLN VAL CYS THR ASP THR ARG THR ASN          
SEQRES  10 A  184  GLU PRO SER ILE THR GLY THR SER THR PHE THR GLN TYR          
SEQRES  11 A  184  PHE SER VAL ARG GLU SER THR ARG THR SER GLY THR VAL          
SEQRES  12 A  184  THR VAL ALA ASN HIS PHE ASN PHE TRP ALA HIS HIS GLY          
SEQRES  13 A  184  PHE GLY ASN SER ASP PHE ASN TYR GLN VAL VAL ALA VAL          
SEQRES  14 A  184  GLU ALA TRP SER GLY ALA GLY SER ALA SER VAL THR ILE          
SEQRES  15 A  184  SER SER                                                      
SEQRES   1 B  184  SER ALA GLY ILE ASN TYR VAL GLN ASN TYR ASN GLY ASN          
SEQRES   2 B  184  LEU GLY ASP PHE THR TYR ASP GLU SER ALA GLY THR PHE          
SEQRES   3 B  184  SER MET TYR TRP GLU ASP GLY VAL SER SER ASP PHE VAL          
SEQRES   4 B  184  VAL GLY LEU GLY TRP THR THR GLY SER SER ASN ALA ILE          
SEQRES   5 B  184  THR TYR SER ALA GLU TYR SER ALA SER GLY SER ALA SER          
SEQRES   6 B  184  TYR LEU ALA VAL TYR GLY TRP VAL ASN TYR PRO GLN ALA          
SEQRES   7 B  184  GLU TYR TYR ILE VAL GLU ASP TYR GLY ASP TYR ASN PRO          
SEQRES   8 B  184  CYS SER SER ALA THR SER LEU GLY THR VAL TYR SER ASP          
SEQRES   9 B  184  GLY SER THR TYR GLN VAL CYS THR ASP THR ARG THR ASN          
SEQRES  10 B  184  GLU PRO SER ILE THR GLY THR SER THR PHE THR GLN TYR          
SEQRES  11 B  184  PHE SER VAL ARG GLU SER THR ARG THR SER GLY THR VAL          
SEQRES  12 B  184  THR VAL ALA ASN HIS PHE ASN PHE TRP ALA HIS HIS GLY          
SEQRES  13 B  184  PHE GLY ASN SER ASP PHE ASN TYR GLN VAL VAL ALA VAL          
SEQRES  14 B  184  GLU ALA TRP SER GLY ALA GLY SER ALA SER VAL THR ILE          
SEQRES  15 B  184  SER SER                                                      
SEQRES   1 C  184  SER ALA GLY ILE ASN TYR VAL GLN ASN TYR ASN GLY ASN          
SEQRES   2 C  184  LEU GLY ASP PHE THR TYR ASP GLU SER ALA GLY THR PHE          
SEQRES   3 C  184  SER MET TYR TRP GLU ASP GLY VAL SER SER ASP PHE VAL          
SEQRES   4 C  184  VAL GLY LEU GLY TRP THR THR GLY SER SER ASN ALA ILE          
SEQRES   5 C  184  THR TYR SER ALA GLU TYR SER ALA SER GLY SER ALA SER          
SEQRES   6 C  184  TYR LEU ALA VAL TYR GLY TRP VAL ASN TYR PRO GLN ALA          
SEQRES   7 C  184  GLU TYR TYR ILE VAL GLU ASP TYR GLY ASP TYR ASN PRO          
SEQRES   8 C  184  CYS SER SER ALA THR SER LEU GLY THR VAL TYR SER ASP          
SEQRES   9 C  184  GLY SER THR TYR GLN VAL CYS THR ASP THR ARG THR ASN          
SEQRES  10 C  184  GLU PRO SER ILE THR GLY THR SER THR PHE THR GLN TYR          
SEQRES  11 C  184  PHE SER VAL ARG GLU SER THR ARG THR SER GLY THR VAL          
SEQRES  12 C  184  THR VAL ALA ASN HIS PHE ASN PHE TRP ALA HIS HIS GLY          
SEQRES  13 C  184  PHE GLY ASN SER ASP PHE ASN TYR GLN VAL VAL ALA VAL          
SEQRES  14 C  184  GLU ALA TRP SER GLY ALA GLY SER ALA SER VAL THR ILE          
SEQRES  15 C  184  SER SER                                                      
SEQRES   1 D  184  SER ALA GLY ILE ASN TYR VAL GLN ASN TYR ASN GLY ASN          
SEQRES   2 D  184  LEU GLY ASP PHE THR TYR ASP GLU SER ALA GLY THR PHE          
SEQRES   3 D  184  SER MET TYR TRP GLU ASP GLY VAL SER SER ASP PHE VAL          
SEQRES   4 D  184  VAL GLY LEU GLY TRP THR THR GLY SER SER ASN ALA ILE          
SEQRES   5 D  184  THR TYR SER ALA GLU TYR SER ALA SER GLY SER ALA SER          
SEQRES   6 D  184  TYR LEU ALA VAL TYR GLY TRP VAL ASN TYR PRO GLN ALA          
SEQRES   7 D  184  GLU TYR TYR ILE VAL GLU ASP TYR GLY ASP TYR ASN PRO          
SEQRES   8 D  184  CYS SER SER ALA THR SER LEU GLY THR VAL TYR SER ASP          
SEQRES   9 D  184  GLY SER THR TYR GLN VAL CYS THR ASP THR ARG THR ASN          
SEQRES  10 D  184  GLU PRO SER ILE THR GLY THR SER THR PHE THR GLN TYR          
SEQRES  11 D  184  PHE SER VAL ARG GLU SER THR ARG THR SER GLY THR VAL          
SEQRES  12 D  184  THR VAL ALA ASN HIS PHE ASN PHE TRP ALA HIS HIS GLY          
SEQRES  13 D  184  PHE GLY ASN SER ASP PHE ASN TYR GLN VAL VAL ALA VAL          
SEQRES  14 D  184  GLU ALA TRP SER GLY ALA GLY SER ALA SER VAL THR ILE          
SEQRES  15 D  184  SER SER                                                      
FORMUL   5  HOH   *288(H2 O)                                                    
HELIX    1   1 GLY A   12  LEU A   14  5                                   3    
HELIX    2   2 PRO A   91  SER A   94  1                                   4    
HELIX    3   3 VAL A  145  HIS A  155  1                                  11    
HELIX    4   4 GLY B   12  LEU B   14  5                                   3    
HELIX    5   5 PRO B   91  SER B   93  5                                   3    
HELIX    6   6 VAL B  145  HIS B  155  1                                  11    
HELIX    7   7 GLY C   12  LEU C   14  5                                   3    
HELIX    8   8 PRO C   91  SER C   94  1                                   4    
HELIX    9   9 VAL C  145  HIS C  155  1                                  11    
HELIX   10  10 GLY D   12  LEU D   14  5                                   3    
HELIX   11  11 PRO D   91  SER D   94  1                                   4    
HELIX   12  12 VAL D  145  HIS D  155  1                                  11    
SHEET    1   A 8 TYR A   6  TYR A  10  0                                        
SHEET    2   A 8 PHE A  38  TRP A  44 -1  N  GLY A  43   O  TYR A   6           
SHEET    3   A 8 GLN A 165  SER A 173 -1  N  ALA A 171   O  PHE A  38           
SHEET    4   A 8 ALA A  64  VAL A  73 -1  N  TYR A  70   O  VAL A 166           
SHEET    5   A 8 ALA A  78  TYR A  86 -1  N  ASP A  85   O  LEU A  67           
SHEET    6   A 8 PHE A 127  ARG A 134  1  N  THR A 128   O  GLU A  79           
SHEET    7   A 8 SER A 106  ARG A 115 -1  N  ARG A 115   O  PHE A 127           
SHEET    8   A 8 THR A  96  SER A 103 -1  N  SER A 103   O  SER A 106           
SHEET    1   B 5 ASP A  16  ASP A  20  0                                        
SHEET    2   B 5 THR A  25  TYR A  29 -1  N  TYR A  29   O  ASP A  16           
SHEET    3   B 5 SER A 177  ILE A 182 -1  N  VAL A 180   O  PHE A  26           
SHEET    4   B 5 ILE A  52  SER A  59 -1  N  SER A  59   O  SER A 177           
SHEET    5   B 5 SER A 140  VAL A 143 -1  N  VAL A 143   O  ILE A  52           
SHEET    1   C 2 GLU A 118  SER A 120  0                                        
SHEET    2   C 2 GLY A 123  SER A 125 -1  N  SER A 125   O  GLU A 118           
SHEET    1   D 8 TYR B   6  TYR B  10  0                                        
SHEET    2   D 8 PHE B  38  TRP B  44 -1  N  GLY B  43   O  TYR B   6           
SHEET    3   D 8 GLN B 165  ALA B 171 -1  N  ALA B 171   O  PHE B  38           
SHEET    4   D 8 SER B  65  VAL B  73 -1  N  TYR B  70   O  VAL B 166           
SHEET    5   D 8 ALA B  78  TYR B  86 -1  N  ASP B  85   O  LEU B  67           
SHEET    6   D 8 PHE B 127  ARG B 134  1  N  THR B 128   O  GLU B  79           
SHEET    7   D 8 SER B 106  ARG B 115 -1  N  ARG B 115   O  PHE B 127           
SHEET    8   D 8 THR B  96  SER B 103 -1  N  SER B 103   O  SER B 106           
SHEET    1   E 5 ASP B  16  ASP B  20  0                                        
SHEET    2   E 5 THR B  25  TYR B  29 -1  N  TYR B  29   O  ASP B  16           
SHEET    3   E 5 SER B 177  ILE B 182 -1  N  VAL B 180   O  PHE B  26           
SHEET    4   E 5 ILE B  52  SER B  59 -1  N  SER B  59   O  SER B 177           
SHEET    5   E 5 SER B 140  VAL B 143 -1  N  VAL B 143   O  ILE B  52           
SHEET    1   F 2 GLU B 118  SER B 120  0                                        
SHEET    2   F 2 GLY B 123  SER B 125 -1  N  SER B 125   O  GLU B 118           
SHEET    1   G 8 TYR C   6  TYR C  10  0                                        
SHEET    2   G 8 PHE C  38  TRP C  44 -1  N  GLY C  43   O  TYR C   6           
SHEET    3   G 8 GLN C 165  SER C 173 -1  N  ALA C 171   O  PHE C  38           
SHEET    4   G 8 ALA C  64  VAL C  73 -1  N  TYR C  70   O  VAL C 166           
SHEET    5   G 8 ALA C  78  TYR C  86 -1  N  ASP C  85   O  LEU C  67           
SHEET    6   G 8 PHE C 127  ARG C 134  1  N  THR C 128   O  GLU C  79           
SHEET    7   G 8 SER C 106  ARG C 115 -1  N  ARG C 115   O  PHE C 127           
SHEET    8   G 8 THR C  96  SER C 103 -1  N  SER C 103   O  SER C 106           
SHEET    1   H 5 ASP C  16  ASP C  20  0                                        
SHEET    2   H 5 THR C  25  TYR C  29 -1  N  TYR C  29   O  ASP C  16           
SHEET    3   H 5 SER C 177  ILE C 182 -1  N  VAL C 180   O  PHE C  26           
SHEET    4   H 5 ILE C  52  SER C  59 -1  N  SER C  59   O  SER C 177           
SHEET    5   H 5 SER C 140  VAL C 143 -1  N  VAL C 143   O  ILE C  52           
SHEET    1   I 2 GLU C 118  SER C 120  0                                        
SHEET    2   I 2 GLY C 123  SER C 125 -1  N  SER C 125   O  GLU C 118           
SHEET    1   J 8 TYR D   6  TYR D  10  0                                        
SHEET    2   J 8 PHE D  38  TRP D  44 -1  N  GLY D  43   O  TYR D   6           
SHEET    3   J 8 GLN D 165  SER D 173 -1  N  ALA D 171   O  PHE D  38           
SHEET    4   J 8 ALA D  64  VAL D  73 -1  N  TYR D  70   O  VAL D 166           
SHEET    5   J 8 ALA D  78  TYR D  86 -1  N  ASP D  85   O  LEU D  67           
SHEET    6   J 8 PHE D 127  ARG D 134  1  N  THR D 128   O  GLU D  79           
SHEET    7   J 8 SER D 106  ARG D 115 -1  N  ARG D 115   O  PHE D 127           
SHEET    8   J 8 THR D  96  SER D 103 -1  N  SER D 103   O  SER D 106           
SHEET    1   K 5 ASP D  16  ASP D  20  0                                        
SHEET    2   K 5 THR D  25  TYR D  29 -1  N  TYR D  29   O  ASP D  16           
SHEET    3   K 5 SER D 177  ILE D 182 -1  N  VAL D 180   O  PHE D  26           
SHEET    4   K 5 ILE D  52  SER D  59 -1  N  SER D  59   O  SER D 177           
SHEET    5   K 5 SER D 140  VAL D 143 -1  N  VAL D 143   O  ILE D  52           
SHEET    1   L 2 GLU D 118  SER D 120  0                                        
SHEET    2   L 2 GLY D 123  SER D 125 -1  N  SER D 125   O  GLU D 118           
SSBOND   1 CYS A   92    CYS A  111                          1555   1555  2.02  
SSBOND   2 CYS B   92    CYS B  111                          1555   1555  1.99  
SSBOND   3 CYS C   92    CYS C  111                          1555   1555  2.02  
SSBOND   4 CYS D   92    CYS D  111                          1555   1555  2.01  
CISPEP   1 TYR A   75    PRO A   76          0       -16.01                     
CISPEP   2 TYR B   75    PRO B   76          0       -16.05                     
CISPEP   3 TYR C   75    PRO C   76          0       -15.96                     
CISPEP   4 TYR D   75    PRO D   76          0       -15.62                     
SITE     1  EA  2 GLU A  79  GLU A 170                                          
SITE     1  EB  2 GLU B  79  GLU B 170                                          
SITE     1  EC  2 GLU C  79  GLU C 170                                          
SITE     1  ED  2 GLU D  79  GLU D 170                                          
CRYST1   84.300   85.300  113.800  90.00  90.00  90.00 P 21 21 21   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      0.011862  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011723  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008787        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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