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Database: PDB
Entry: 1XYP
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Original site: 1XYP 
HEADER    HYDROLASE                               09-AUG-94   1XYP              
TITLE     STRUCTURAL COMPARISON OF TWO MAJOR ENDO-1,4-BETA-XYLANASES            
TITLE    2 FROM TRICHODREMA REESEI                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDO-1,4-BETA-XYLANASE II;                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.2.1.8;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HYPOCREA JECORINA;                              
SOURCE   3 ORGANISM_TAXID: 51453                                                
KEYWDS    XYLANASE, HYDROLASE                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.ROUVINEN,A.TORRONEN                                                 
REVDAT   3   24-FEB-09 1XYP    1       VERSN                                    
REVDAT   2   01-APR-03 1XYP    1       JRNL                                     
REVDAT   1   08-AUG-95 1XYP    0                                                
JRNL        AUTH   A.TORRONEN,J.ROUVINEN                                        
JRNL        TITL   STRUCTURAL COMPARISON OF TWO MAJOR                           
JRNL        TITL 2 ENDO-1,4-XYLANASES FROM TRICHODERMA REESEI.                  
JRNL        REF    BIOCHEMISTRY                  V.  34   847 1995              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   7827044                                                      
JRNL        DOI    10.1021/BI00003A019                                          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.TORRONEN,A.HARKKI,J.ROUVINEN                               
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF                               
REMARK   1  TITL 2 ENDO-1,4-BETA-XYLANASE II FROM TRICHODERMA REESEI:           
REMARK   1  TITL 3 TWO CONFORMATIONAL STATES IN THE ACTIVE SITE                 
REMARK   1  REF    EMBO J.                       V.  13  2493 1994              
REMARK   1  REFN                   ISSN 0261-4189                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
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             : 39560                          
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) : 0.189                           
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            : 2960                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 328                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.26                          
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) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.60                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.20                            
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: NULL                                      
REMARK   4                                                                      
REMARK   4 1XYP 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-JUL-94                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41141                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 68.0                               
REMARK 200  DATA REDUNDANCY                : 2.250                              
REMARK 200  R MERGE                    (I) : 0.08550                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 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: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       30.45000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK:                                                              
REMARK 300 MTRIX                                                                
REMARK 300  THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW                
REMARK 300  DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE               
REMARK 300  VARIOUS DOMAINS IN THIS ENTRY.  APPLYING THE APPROPRIATE            
REMARK 300  MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL              
REMARK 300  YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED               
REMARK 300  SECOND.                                                             
REMARK 300                                                                      
REMARK 300            APPLIED TO           TRANSFORMED TO                       
REMARK 300  MTRIX      RESIDUES               RESIDUES         RMSD             
REMARK 300    M1   A    1  ..  A  190     B    1  ..  B  190   0.243            
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 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    ASP A 170     -139.35    -98.01                                   
REMARK 500    ASN B  57       17.66   -143.21                                   
REMARK 500    ASP B 170     -139.46   -100.85                                   
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 534        DISTANCE =  5.09 ANGSTROMS                       
REMARK 525    HOH B 615        DISTANCE =  5.38 ANGSTROMS                       
REMARK 525    HOH B 618        DISTANCE =  6.89 ANGSTROMS                       
REMARK 525    HOH B 621        DISTANCE =  5.92 ANGSTROMS                       
REMARK 525    HOH A 567        DISTANCE =  6.34 ANGSTROMS                       
REMARK 525    HOH A 669        DISTANCE =  5.74 ANGSTROMS                       
REMARK 525    HOH A 674        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH B 714        DISTANCE =  7.22 ANGSTROMS                       
REMARK 525    HOH A 686        DISTANCE =  6.49 ANGSTROMS                       
REMARK 525    HOH A 690        DISTANCE =  8.80 ANGSTROMS                       
REMARK 525    HOH B 758        DISTANCE =  5.87 ANGSTROMS                       
REMARK 525    HOH A 739        DISTANCE =  5.40 ANGSTROMS                       
REMARK 525    HOH A 778        DISTANCE =  5.44 ANGSTROMS                       
DBREF  1XYP A    2   190  UNP    P36217   XYN2_TRIRE      34    222             
DBREF  1XYP B    2   190  UNP    P36217   XYN2_TRIRE      34    222             
SEQRES   1 A  190  PCA THR ILE GLN PRO GLY THR GLY TYR ASN ASN GLY TYR          
SEQRES   2 A  190  PHE TYR SER TYR TRP ASN ASP GLY HIS GLY GLY VAL THR          
SEQRES   3 A  190  TYR THR ASN GLY PRO GLY GLY GLN PHE SER VAL ASN TRP          
SEQRES   4 A  190  SER ASN SER GLY ASN PHE VAL GLY GLY LYS GLY TRP GLN          
SEQRES   5 A  190  PRO GLY THR LYS ASN LYS VAL ILE ASN PHE SER GLY SER          
SEQRES   6 A  190  TYR ASN PRO ASN GLY ASN SER TYR LEU SER VAL TYR GLY          
SEQRES   7 A  190  TRP SER ARG ASN PRO LEU ILE GLU TYR TYR ILE VAL GLU          
SEQRES   8 A  190  ASN PHE GLY THR TYR ASN PRO SER THR GLY ALA THR LYS          
SEQRES   9 A  190  LEU GLY GLU VAL THR SER ASP GLY SER VAL TYR ASP ILE          
SEQRES  10 A  190  TYR ARG THR GLN ARG VAL ASN GLN PRO SER ILE ILE GLY          
SEQRES  11 A  190  THR ALA THR PHE TYR GLN TYR TRP SER VAL ARG ARG ASN          
SEQRES  12 A  190  HIS ARG SER SER GLY SER VAL ASN THR ALA ASN HIS PHE          
SEQRES  13 A  190  ASN ALA TRP ALA GLN GLN GLY LEU THR LEU GLY THR MET          
SEQRES  14 A  190  ASP TYR GLN ILE VAL ALA VAL GLU GLY TYR PHE SER SER          
SEQRES  15 A  190  GLY SER ALA SER ILE THR VAL SER                              
SEQRES   1 B  190  PCA THR ILE GLN PRO GLY THR GLY TYR ASN ASN GLY TYR          
SEQRES   2 B  190  PHE TYR SER TYR TRP ASN ASP GLY HIS GLY GLY VAL THR          
SEQRES   3 B  190  TYR THR ASN GLY PRO GLY GLY GLN PHE SER VAL ASN TRP          
SEQRES   4 B  190  SER ASN SER GLY ASN PHE VAL GLY GLY LYS GLY TRP GLN          
SEQRES   5 B  190  PRO GLY THR LYS ASN LYS VAL ILE ASN PHE SER GLY SER          
SEQRES   6 B  190  TYR ASN PRO ASN GLY ASN SER TYR LEU SER VAL TYR GLY          
SEQRES   7 B  190  TRP SER ARG ASN PRO LEU ILE GLU TYR TYR ILE VAL GLU          
SEQRES   8 B  190  ASN PHE GLY THR TYR ASN PRO SER THR GLY ALA THR LYS          
SEQRES   9 B  190  LEU GLY GLU VAL THR SER ASP GLY SER VAL TYR ASP ILE          
SEQRES  10 B  190  TYR ARG THR GLN ARG VAL ASN GLN PRO SER ILE ILE GLY          
SEQRES  11 B  190  THR ALA THR PHE TYR GLN TYR TRP SER VAL ARG ARG ASN          
SEQRES  12 B  190  HIS ARG SER SER GLY SER VAL ASN THR ALA ASN HIS PHE          
SEQRES  13 B  190  ASN ALA TRP ALA GLN GLN GLY LEU THR LEU GLY THR MET          
SEQRES  14 B  190  ASP TYR GLN ILE VAL ALA VAL GLU GLY TYR PHE SER SER          
SEQRES  15 B  190  GLY SER ALA SER ILE THR VAL SER                              
MODRES 1XYP PCA A    1  GLU  PYROGLUTAMIC ACID                                  
MODRES 1XYP PCA B    1  GLU  PYROGLUTAMIC ACID                                  
HET    PCA  A   1       8                                                       
HET    PCA  B   1       8                                                       
HETNAM     PCA PYROGLUTAMIC ACID                                                
FORMUL   1  PCA    2(C5 H7 N O3)                                                
FORMUL   3  HOH   *328(H2 O)                                                    
HELIX    1   1 THR A  152  GLN A  162  1                                  11    
HELIX    2   2 THR B  152  GLN B  162  1                                  11    
SHEET    1   A 9 GLY A   6  ASN A  10  0                                        
SHEET    2   A 9 TYR A  13  ASN A  19 -1  O  TYR A  13   N  ASN A  10           
SHEET    3   A 9 ASN A  44  TRP A  51 -1  O  VAL A  46   N  TRP A  18           
SHEET    4   A 9 THR A 168  TYR A 179 -1  O  GLN A 172   N  TRP A  51           
SHEET    5   A 9 SER A  72  ARG A  81 -1  O  TYR A  73   N  GLU A 177           
SHEET    6   A 9 ILE A  85  PHE A  93 -1  O  ILE A  85   N  SER A  80           
SHEET    7   A 9 ALA A 132  ARG A 141  1  O  TYR A 135   N  GLU A  86           
SHEET    8   A 9 SER A 113  GLN A 125 -1  O  ASP A 116   N  VAL A 140           
SHEET    9   A 9 THR A 103  SER A 110 -1  N  THR A 103   O  ARG A 119           
SHEET    1   B 5 VAL A  25  ASN A  29  0                                        
SHEET    2   B 5 GLN A  34  TRP A  39 -1  O  SER A  36   N  THR A  28           
SHEET    3   B 5 SER A 182  SER A 190 -1  N  GLY A 183   O  TRP A  39           
SHEET    4   B 5 VAL A  59  ASN A  69 -1  N  ASN A  61   O  SER A 190           
SHEET    5   B 5 GLY A 148  ASN A 151 -1  N  GLY A 148   O  PHE A  62           
SHEET    1   C 6 THR B   2  ILE B   3  0                                        
SHEET    2   C 6 VAL B  25  ASN B  29 -1  O  TYR B  27   N  ILE B   3           
SHEET    3   C 6 GLN B  34  TRP B  39 -1  O  SER B  36   N  THR B  28           
SHEET    4   C 6 SER B 182  SER B 190 -1  N  GLY B 183   O  TRP B  39           
SHEET    5   C 6 VAL B  59  ASN B  69 -1  N  ASN B  61   O  SER B 190           
SHEET    6   C 6 GLY B 148  ASN B 151 -1  N  GLY B 148   O  PHE B  62           
SHEET    1   D 9 GLY B   6  ASN B  10  0                                        
SHEET    2   D 9 TYR B  13  ASN B  19 -1  O  TYR B  13   N  ASN B  10           
SHEET    3   D 9 ASN B  44  TRP B  51 -1  O  VAL B  46   N  TRP B  18           
SHEET    4   D 9 THR B 168  TYR B 179 -1  O  GLN B 172   N  TRP B  51           
SHEET    5   D 9 SER B  72  ARG B  81 -1  O  TYR B  73   N  GLU B 177           
SHEET    6   D 9 ILE B  85  PHE B  93 -1  O  ILE B  85   N  SER B  80           
SHEET    7   D 9 ALA B 132  ARG B 141  1  O  TYR B 135   N  GLU B  86           
SHEET    8   D 9 SER B 113  GLN B 125 -1  O  ASP B 116   N  VAL B 140           
SHEET    9   D 9 THR B 103  SER B 110 -1  N  THR B 103   O  ARG B 119           
LINK         C   PCA A   1                 N   THR A   2     1555   1555  1.33  
LINK         C   PCA B   1                 N   THR B   2     1555   1555  1.33  
CISPEP   1 GLN A   52    PRO A   53          0        -0.56                     
CISPEP   2 ASN A   82    PRO A   83          0         0.47                     
CISPEP   3 GLN B   52    PRO B   53          0         0.37                     
CISPEP   4 ASN B   82    PRO B   83          0         0.35                     
CRYST1   81.820   60.900   38.130  90.00  94.43  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012222  0.000000  0.000947        0.00000                         
SCALE2      0.000000  0.016420  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.026305        0.00000                         
MTRIX1   1  0.986800 -0.024399  0.160100       40.12830    1                    
MTRIX2   1 -0.025399 -0.999699  0.004100       58.04710    1                    
MTRIX3   1  0.160000 -0.008099 -0.987099       12.70670    1                    
HETATM    1  N   PCA A   1      48.005  14.771  14.152  1.00 20.70           N  
HETATM    2  CA  PCA A   1      48.964  15.185  15.223  1.00 19.59           C  
HETATM    3  CB  PCA A   1      50.375  15.147  14.639  1.00 21.55           C  
HETATM    4  CG  PCA A   1      50.221  15.042  13.175  1.00 22.16           C  
HETATM    5  CD  PCA A   1      48.778  14.662  12.895  1.00 23.41           C  
HETATM    6  OE  PCA A   1      48.386  14.314  11.782  1.00 27.62           O  
HETATM    7  C   PCA A   1      48.651  16.598  15.681  1.00 17.73           C  
HETATM    8  O   PCA A   1      47.982  17.360  14.981  1.00 15.48           O  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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