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Database: PDB
Entry: 1BK1
LinkDB: 1BK1
Original site: 1BK1 
HEADER    HYDROLASE                               14-JUL-98   1BK1              
TITLE     ENDO-1,4-BETA-XYLANASE C                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDO-1,4-B-XYLANASE C;                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: XYLANASE;                                                   
COMPND   5 EC: 3.2.1.8;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ASPERGILLUS KAWACHII;                           
SOURCE   3 ORGANISM_TAXID: 40384;                                               
SOURCE   4 STRAIN: IFO 4308;                                                    
SOURCE   5 CELLULAR_LOCATION: EXTRACELLULAR;                                    
SOURCE   6 GENE: XYNC;                                                          
SOURCE   7 EXPRESSION_SYSTEM: ASPERGILLUS KAWACHII;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 40384;                                      
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: IFO 4308;                                  
SOURCE  10 EXPRESSION_SYSTEM_CELLULAR_LOCATION: EXTRACELLULAR;                  
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  12 EXPRESSION_SYSTEM_VECTOR: PUAMD3;                                    
SOURCE  13 EXPRESSION_SYSTEM_PLASMID: PUAMXC1;                                  
SOURCE  14 EXPRESSION_SYSTEM_GENE: XYNC                                         
KEYWDS    HYDROLASE, XYLAN DEGRADATION, GLYCOSIDASE, SIGNAL                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.FUSHINOBU,K.ITO,M.KONNO,T.WAKAGI,H.MATSUZAWA                        
REVDAT   5   24-FEB-09 1BK1    1       VERSN                                    
REVDAT   4   01-APR-03 1BK1    1       JRNL                                     
REVDAT   3   26-MAR-99 1BK1    1       JRNL                                     
REVDAT   2   16-FEB-99 1BK1    3       REMARK HETATM DBREF  SEQADV              
REVDAT   2 2                   3       JRNL                                     
REVDAT   1   13-JAN-99 1BK1    0                                                
JRNL        AUTH   S.FUSHINOBU,K.ITO,M.KONNO,T.WAKAGI,H.MATSUZAWA               
JRNL        TITL   CRYSTALLOGRAPHIC AND MUTATIONAL ANALYSES OF AN               
JRNL        TITL 2 EXTREMELY ACIDOPHILIC AND ACID-STABLE XYLANASE:              
JRNL        TITL 3 BIASED DISTRIBUTION OF ACIDIC RESIDUES AND                   
JRNL        TITL 4 IMPORTANCE OF ASP37 FOR CATALYSIS AT LOW PH.                 
JRNL        REF    PROTEIN ENG.                  V.  11  1121 1998              
JRNL        REFN                   ISSN 0269-2139                               
JRNL        PMID   9930661                                                      
JRNL        DOI    10.1093/PROTEIN/11.12.1121                                   
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   K.ITO,H.OGASAWARA,T.SUGIMOTO,T.ISHIKAWA                      
REMARK   1  TITL   PURIFICATION AND PROPERTIES OF ACID STABLE                   
REMARK   1  TITL 2 XYLANASES FROM ASPERGILLUS KAWACHII                          
REMARK   1  REF    BIOSCI.BIOTECHNOL.BIOCHEM.    V.  56   547 1992              
REMARK   1  REFN                   ISSN 0916-8451                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   K.ITO,K.IWASHITA,K.IWANO                                     
REMARK   1  TITL   CLONING AND SEQUENCING OF THE XYNC GENE ENCODING             
REMARK   1  TITL 2 ACID XYLANASE OF ASPERGILLUS KAWACHII                        
REMARK   1  REF    BIOSCI.BIOTECHNOL.BIOCHEM.    V.  56  1338 1992              
REMARK   1  REFN                   ISSN 0916-8451                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 3.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 83.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 12530                          
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 SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.260                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 637                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.010                           
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.09                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 60.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1031                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3090                       
REMARK   3   BIN FREE R VALUE                    : 0.2610                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 3.68                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 67                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.032                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1394                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 111                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.10                          
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) : 0.27                            
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) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.90                            
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  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : PARAM19.SOL                                    
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH19.SOL                                     
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1BK1 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        : 04-JUL-96                          
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-6A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : FUJI                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15428                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 34.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.100                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 8.700                              
REMARK 200  R MERGE                    (I) : 0.07300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39700                            
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: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: TRICHODERMA REESEI XYNI, PDB ENTRY 1XYN              
REMARK 200                                                                      
REMARK 200 REMARK: DATA WERE COLLECTED USING THE WEISSENBERG METHOD             
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.5                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       56.64550            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       31.03250            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       31.03250            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       84.96825            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       31.03250            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       31.03250            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       28.32275            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       31.03250            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       31.03250            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       84.96825            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       31.03250            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       31.03250            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       28.32275            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       56.64550            
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 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     SER A   184                                                      
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    TRP A  30       47.04   -144.56                                   
REMARK 500    ALA A  60       30.95   -143.41                                   
REMARK 500    ILE A 121        4.92    -64.82                                   
REMARK 500    ASN A 163     -143.55    -97.56                                   
REMARK 500    TRP A 172       13.16   -140.82                                   
REMARK 500    SER A 173      144.09   -171.74                                   
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 262        DISTANCE =  5.33 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AS                                                  
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: GLU 79 AND GLU 170 REFER TO THE CATALYTIC          
REMARK 800  ACIDIC RESIDUES.                                                    
DBREF  1BK1 A    1   184  UNP    P33557   XYN3_ASPKA      28    211             
SEQADV 1BK1 GLY A   15  UNP  P33557    ALA    42 CONFLICT                       
SEQADV 1BK1 THR A   53  UNP  P33557    SER    80 CONFLICT                       
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 SER 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 GLN HIS GLY          
SEQRES  13 A  184  PHE GLY ASN SER ASP PHE ASN TYR GLN VAL MET 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                                                      
FORMUL   2  HOH   *111(H2 O)                                                    
HELIX    1   1 GLY A   12  LEU A   14  5                                   3    
HELIX    2   2 GLU A   21  ALA A   23  5                                   3    
HELIX    3   3 VAL A  145  HIS A  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  ALA A 171 -1  N  ALA A 171   O  PHE A  38           
SHEET    4   A 8 SER A  65  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  TRP A  30 -1  N  TYR A  29   O  ASP A  16           
SHEET    3   B 5 GLY A 176  SER A 183 -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           
SSBOND   1 CYS A   92    CYS A  111                          1555   1555  2.02  
HYDBND       OD1 ASP A   37                 OE2 GLU A  170 1555    1555         
CISPEP   1 TYR A   75    PRO A   76          0        -0.97                     
SITE     1  AS  2 GLU A  79  GLU A 170                                          
CRYST1   62.065   62.065  113.291  90.00  90.00  90.00 P 43 21 2     8          
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      0.016112  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016112  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008827        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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