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Database: PDB
Entry: 1BG4
LinkDB: 1BG4
Original site: 1BG4 
HEADER    FAMILY 10 XYLANASE                      05-JUN-98   1BG4              
TITLE     XYLANASE FROM PENICILLIUM SIMPLICISSIMUM                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDO-1,4-BETA-XYLANASE;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.2.1.8                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PENICILLIUM SIMPLICISSIMUM;                     
SOURCE   3 ORGANISM_TAXID: 69488;                                               
SOURCE   4 COLLECTION: BT 2246, CULTURE COLLECTION OF THE INSTITUTE OF          
SOURCE   5 BIOTECHNOLOGY, UNIVERSITY OF TECHNOLOGY, GRAZ, AUSTRIA;              
SOURCE   6 CELLULAR_LOCATION: SECRETED;                                         
SOURCE   7 OTHER_DETAILS: PENICILLIUM SIMPLICISSIMUM (OUDEM.) THOM              
KEYWDS    FAMILY 10 XYLANASE, PENICILLIUM SIMPLICISSIMUM, TIM-BARREL, GLYCOSYL  
KEYWDS   2 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.SCHMIDT,C.KRATKY                                                    
REVDAT   4   13-JUL-11 1BG4    1       VERSN                                    
REVDAT   3   24-FEB-09 1BG4    1       VERSN                                    
REVDAT   2   30-MAR-99 1BG4    1       JRNL                                     
REVDAT   1   12-AUG-98 1BG4    0                                                
JRNL        AUTH   A.SCHMIDT,A.SCHLACHER,W.STEINER,H.SCHWAB,C.KRATKY            
JRNL        TITL   STRUCTURE OF THE XYLANASE FROM PENICILLIUM SIMPLICISSIMUM.   
JRNL        REF    PROTEIN SCI.                  V.   7  2081 1998              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   9792094                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 100000.000                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 43712                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : FREE R THROUGHOUT               
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.229                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 4462                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.75                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.83                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4840                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2680                       
REMARK   3   BIN FREE R VALUE                    : 0.2850                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.00                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 548                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.011                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2298                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 64                                      
REMARK   3   SOLVENT ATOMS            : 316                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 11.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 10.00                          
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) : NULL                            
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) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 2.532 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.844 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.441 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.923 ; 2.500                
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  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : PARAM.PYQ                                      
REMARK   3  PARAMETER FILE  3  : PARAM19.SOL                                    
REMARK   3  PARAMETER FILE  4  : PARAM.GLY                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH19.SOL                                     
REMARK   3  TOPOLOGY FILE  3   : TOP.GLYC                                       
REMARK   3  TOPOLOGY FILE  4   : TOP.PYQ                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: PARAMETER/TOPOLOGY FILES FOR HET GROUPS   
REMARK   3  EXCEPT WATER SELF-SETUP                                             
REMARK   4                                                                      
REMARK   4 1BG4 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        : JUL-97                             
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ELETTRA                            
REMARK 200  BEAMLINE                       : 5.2R                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.850                              
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : TOROIDAL MIRROR                    
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE AREA DETECTOR          
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43712                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 10.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.79                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.23200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR 3.851                                          
REMARK 200 STARTING MODEL: PDB ENTRY 1XYZ                                       
REMARK 200                                                                      
REMARK 200 REMARK: DATA WERE COLLECTED AT THE ELETTRA SYNCHROTRON LIGHT         
REMARK 200  SOURCE, TRIESTE, ITALY                                              
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 1.9M       
REMARK 280  (NH4)2SO4, 0.1M TRISHCL PH 8.4 AT 4 C, TEMPERATURE 277K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.80000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       75.60000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       75.60000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       37.80000            
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 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 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  48      -25.54   -149.53                                   
REMARK 500    LEU A 177       49.96   -108.49                                   
REMARK 500    GLU A 238       54.92   -142.54                                   
REMARK 500    VAL A 270      -61.96   -100.44                                   
REMARK 500    SER A 281       63.35     37.62                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A 125         0.07    SIDE CHAIN                              
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 A 547        DISTANCE =  5.06 ANGSTROMS                       
REMARK 525    HOH A 574        DISTANCE =  6.21 ANGSTROMS                       
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                              NA A 623  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 561   O                                                      
REMARK 620 2 SER A  49   O    94.4                                              
REMARK 620 3 THR A  63   O   119.1 131.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 624  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  84   O                                                      
REMARK 620 2 PRO A  46   O   107.0                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 621  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A  17   OH                                                     
REMARK 620 2 ILE A 236   O   131.7                                              
REMARK 620 3 THR A 266   OG1 107.7  98.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 622  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A 143   OG                                                     
REMARK 620 2 TYR A 153   OH   97.9                                              
REMARK 620 3 HOH A 550   O   117.9 128.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 620  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG A 162   NH1                                                    
REMARK 620 2 ASP A 165   O   160.1                                              
REMARK 620 3 ALA A 168   O    86.5  97.2                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 619  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU A 226   O                                                      
REMARK 620 2 THR A 231   N   141.7                                              
REMARK 620 3 THR A 231   OG1 127.3  61.5                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: ACT                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE.                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 619                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 620                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 621                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 622                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 623                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 624                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 632                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 633                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 625                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 626                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 627                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 628                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 629                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 630                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 631                 
DBREF  1BG4 A    2   302  UNP    P56588   XYNA_PENSI       2    302             
SEQRES   1 A  302  PCA ALA SER VAL SER ILE ASP ALA LYS PHE LYS ALA HIS          
SEQRES   2 A  302  GLY LYS LYS TYR LEU GLY THR ILE GLY ASP GLN TYR THR          
SEQRES   3 A  302  LEU THR LYS ASN THR LYS ASN PRO ALA ILE ILE LYS ALA          
SEQRES   4 A  302  ASP PHE GLY GLN LEU THR PRO GLU ASN SER MET LYS TRP          
SEQRES   5 A  302  ASP ALA THR GLU PRO ASN ARG GLY GLN PHE THR PHE SER          
SEQRES   6 A  302  GLY SER ASP TYR LEU VAL ASN PHE ALA GLN SER ASN GLY          
SEQRES   7 A  302  LYS LEU ILE ARG GLY HIS THR LEU VAL TRP HIS SER GLN          
SEQRES   8 A  302  LEU PRO GLY TRP VAL SER SER ILE THR ASP LYS ASN THR          
SEQRES   9 A  302  LEU ILE SER VAL LEU LYS ASN HIS ILE THR THR VAL MET          
SEQRES  10 A  302  THR ARG TYR LYS GLY LYS ILE TYR ALA TRP ASP VAL LEU          
SEQRES  11 A  302  ASN GLU ILE PHE ASN GLU ASP GLY SER LEU ARG ASN SER          
SEQRES  12 A  302  VAL PHE TYR ASN VAL ILE GLY GLU ASP TYR VAL ARG ILE          
SEQRES  13 A  302  ALA PHE GLU THR ALA ARG SER VAL ASP PRO ASN ALA LYS          
SEQRES  14 A  302  LEU TYR ILE ASN ASP TYR ASN LEU ASP SER ALA GLY TYR          
SEQRES  15 A  302  SER LYS VAL ASN GLY MET VAL SER HIS VAL LYS LYS TRP          
SEQRES  16 A  302  LEU ALA ALA GLY ILE PRO ILE ASP GLY ILE GLY SER GLN          
SEQRES  17 A  302  THR HIS LEU GLY ALA GLY ALA GLY SER ALA VAL ALA GLY          
SEQRES  18 A  302  ALA LEU ASN ALA LEU ALA SER ALA GLY THR LYS GLU ILE          
SEQRES  19 A  302  ALA ILE THR GLU LEU ASP ILE ALA GLY ALA SER SER THR          
SEQRES  20 A  302  ASP TYR VAL ASN VAL VAL ASN ALA CYS LEU ASN GLN ALA          
SEQRES  21 A  302  LYS CYS VAL GLY ILE THR VAL TRP GLY VAL ALA ASP PRO          
SEQRES  22 A  302  ASP SER TRP ARG SER SER SER SER PRO LEU LEU PHE ASP          
SEQRES  23 A  302  GLY ASN TYR ASN PRO LYS ALA ALA TYR ASN ALA ILE ALA          
SEQRES  24 A  302  ASN ALA LEU                                                  
MODRES 1BG4 PCA A    1  GLU  PYROGLUTAMIC ACID                                  
HET    PCA  A   1       8                                                       
HET     NA  A 619       1                                                       
HET     NA  A 620       1                                                       
HET     NA  A 621       1                                                       
HET     NA  A 622       1                                                       
HET     NA  A 623       1                                                       
HET     NA  A 624       1                                                       
HET    TRS  A 632       8                                                       
HET    TRS  A 633       8                                                       
HET    GOL  A 625       6                                                       
HET    GOL  A 626       6                                                       
HET    GOL  A 627       6                                                       
HET    GOL  A 628       6                                                       
HET    GOL  A 629       6                                                       
HET    GOL  A 630       6                                                       
HET    GOL  A 631       6                                                       
HETNAM     PCA PYROGLUTAMIC ACID                                                
HETNAM      NA SODIUM ION                                                       
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETNAM     GOL GLYCEROL                                                         
HETSYN     TRS TRIS BUFFER                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  PCA    C5 H7 N O3                                                   
FORMUL   2   NA    6(NA 1+)                                                     
FORMUL   8  TRS    2(C4 H12 N O3 1+)                                            
FORMUL  10  GOL    7(C3 H8 O3)                                                  
FORMUL  17  HOH   *316(H2 O)                                                    
HELIX    1 A'' SER A    5  ALA A   12  1                                   8    
HELIX    2  B1 GLN A   24  LYS A   29  1                                   6    
HELIX    3   B LYS A   32  ASP A   40  1                                   9    
HELIX    4  C1 TRP A   52  GLU A   56  1                                   5    
HELIX    5   C SER A   65  SER A   76  1                                  12    
HELIX    6  D1 GLY A   94  SER A   97  1                                   4    
HELIX    7   D LYS A  102  ARG A  119  1                                  18    
HELIX    8  E1 SER A  143  GLU A  151  1                                   9    
HELIX    9   E ASP A  152  VAL A  164  1                                  13    
HELIX   10   F TYR A  182  ALA A  197  1                                  16    
HELIX   11   G VAL A  219  ALA A  225  1                                   7    
HELIX   12   H SER A  246  LEU A  257  1                                  12    
HELIX   13  A1 ASP A  272  ASP A  274  5                                   3    
HELIX   14  A2 SER A  278  SER A  280  5                                   3    
HELIX   15  A' ALA A  293  LEU A  302  1                                  10    
SHEET    1   1 8 TYR A  17  GLY A  22  0                                        
SHEET    2   1 8 GLN A  43  GLU A  47  1                                        
SHEET    3   1 8 LEU A  80  GLN A  91  1                                        
SHEET    4   1 8 ALA A 126  GLU A 132  1                                        
SHEET    5   1 8 LYS A 169  ASP A 174  1                                        
SHEET    6   1 8 GLY A 204  LEU A 211  1                                        
SHEET    7   1 8 GLU A 233  ILE A 241  1                                        
SHEET    8   1 8 CYS A 262  VAL A 267  1                                        
SSBOND   1 CYS A  256    CYS A  262                          1555   1555  2.04  
LINK         C   PCA A   1                 N   ALA A   2     1555   1555  1.33  
LINK        NA    NA A 623                 O   HOH A 561     1555   1555  2.38  
LINK        NA    NA A 624                 O   HIS A  84     1555   1555  2.58  
LINK         OH  TYR A  17                NA    NA A 621     1555   1555  2.70  
LINK         O   PRO A  46                NA    NA A 624     1555   1555  2.73  
LINK         O   SER A  49                NA    NA A 623     1555   1555  2.80  
LINK         O   THR A  63                NA    NA A 623     1555   1555  2.85  
LINK         OG  SER A 143                NA    NA A 622     1555   1555  2.67  
LINK         OH  TYR A 153                NA    NA A 622     1555   1555  2.79  
LINK         NH1 ARG A 162                NA    NA A 620     1555   1555  2.82  
LINK         O   ASP A 165                NA    NA A 620     1555   1555  2.67  
LINK         O   ALA A 168                NA    NA A 620     1555   1555  2.72  
LINK         O   LEU A 226                NA    NA A 619     1555   1555  2.84  
LINK         N   THR A 231                NA    NA A 619     1555   1555  2.97  
LINK         OG1 THR A 231                NA    NA A 619     1555   1555  2.66  
LINK         O   ILE A 236                NA    NA A 621     1555   1555  2.84  
LINK         OG1 THR A 266                NA    NA A 621     1555   1555  2.64  
LINK        NA    NA A 622                 O   HOH A 550     1555   1555  2.62  
CISPEP   1 HIS A   84    THR A   85          0       -18.28                     
SITE     1 ACT  2 GLU A 132  GLU A 238                                          
SITE     1 AC1  5 LEU A 226  ALA A 227  GLY A 230  THR A 231                    
SITE     2 AC1  5 LYS A 261                                                     
SITE     1 AC2  5 ARG A 162  ASP A 165  PRO A 166  ALA A 168                    
SITE     2 AC2  5 LEU A 170                                                     
SITE     1 AC3  5 TYR A  17  ARG A  82  ILE A 236  THR A 237                    
SITE     2 AC3  5 THR A 266                                                     
SITE     1 AC4  3 SER A 143  TYR A 153  HOH A 550                               
SITE     1 AC5  5 SER A  49  ALA A  54  THR A  63  SER A  67                    
SITE     2 AC5  5 HOH A 561                                                     
SITE     1 AC6  7 PRO A  46  GLU A  47  ASN A  48  SER A  49                    
SITE     2 AC6  7 MET A  50  LYS A  51  HIS A  84                               
SITE     1 AC7 15 TYR A 146  ILE A 149  GLY A 150  GLU A 151                    
SITE     2 AC7 15 GLY A 214  SER A 217  THR A 247  ASP A 248                    
SITE     3 AC7 15 ASN A 251  HOH A 327  HOH A 339  HOH A 367                    
SITE     4 AC7 15 HOH A 474  HOH A 499  HOH A 533                               
SITE     1 AC8  8 GLN A  24  TYR A  69  GLY A 221  HOH A 331                    
SITE     2 AC8  8 HOH A 381  HOH A 396  HOH A 600  HOH A 610                    
SITE     1 AC9  7 ASP A  68  ASN A  72  ARG A 119  TYR A 120                    
SITE     2 AC9  7 LYS A 123  HOH A 433  HOH A 563                               
SITE     1 BC1 10 THR A  26  GLU A  47  ASN A  48  LYS A 193                    
SITE     2 BC1 10 SER A 228  ASP A 274  HOH A 386  HOH A 429                    
SITE     3 BC1 10 HOH A 535  GOL A 627                                          
SITE     1 BC2  9 ASN A  48  SER A  49  ALA A  54  ALA A 227                    
SITE     2 BC2  9 HOH A 479  HOH A 510  HOH A 535  HOH A 561                    
SITE     3 BC2  9 GOL A 626                                                     
SITE     1 BC3  6 HIS A  13  GLN A  61  PHE A  62  THR A  63                    
SITE     2 BC3  6 LEU A 257  HOH A 588                                          
SITE     1 BC4  9 LYS A  51  HIS A  84  GLU A 132  GLN A 208                    
SITE     2 BC4  9 GLU A 238  TRP A 268  HOH A 340  HOH A 412                    
SITE     3 BC4  9 GOL A 631                                                     
SITE     1 BC5  9 SER A   5  ASP A   7  ALA A   8  LYS A  11                    
SITE     2 BC5  9 ALA A  39  ASP A  40  PHE A  41  HOH A 434                    
SITE     3 BC5  9 HOH A 607                                                     
SITE     1 BC6  8 GLU A  47  ASN A  48  LYS A  51  GLN A  91                    
SITE     2 BC6  8 TRP A 268  TRP A 276  HOH A 353  GOL A 629                    
CRYST1   81.020   81.020  113.400  90.00  90.00 120.00 P 31 2 1      6          
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      0.012343  0.007126  0.000000        0.00000                         
SCALE2      0.000000  0.014252  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008818        0.00000                         
HETATM    1  N   PCA A   1      61.703  61.494  21.209  1.00 28.13           N  
HETATM    2  CA  PCA A   1      62.144  61.814  22.563  1.00 28.28           C  
HETATM    3  CB  PCA A   1      62.811  63.189  22.450  1.00 26.96           C  
HETATM    4  CG  PCA A   1      62.646  63.602  20.997  1.00 28.29           C  
HETATM    5  CD  PCA A   1      61.942  62.438  20.324  1.00 29.24           C  
HETATM    6  OE  PCA A   1      61.659  62.387  19.119  1.00 31.43           O  
HETATM    7  C   PCA A   1      60.981  61.866  23.538  1.00 28.21           C  
HETATM    8  O   PCA A   1      59.936  62.456  23.242  1.00 28.34           O  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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