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Database: PDB
Entry: 4HK9
LinkDB: 4HK9
Original site: 4HK9 
HEADER    HYDROLASE                               15-OCT-12   4HK9              
TITLE     CRYSTAL STRUCTURES OF MUTANT ENDO-BETA-1,4-XYLANASE II COMPLEXED WITH 
TITLE    2 SUBSTRATE (1.15 A) AND PRODUCTS (1.6 A)                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDO-1,4-BETA-XYLANASE 2;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: XYLANASE 2, 1,4-BETA-D-XYLAN XYLANOHYDROLASE 2;             
COMPND   5 EC: 3.2.1.8;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: TRICHODERMA REESEI;                             
SOURCE   3 ORGANISM_TAXID: 51453;                                               
SOURCE   4 GENE: XYN2;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PJEXPRESS401                              
KEYWDS    XYLANASE II, XYLOHEXAOSE, XYLOTRIOSE, INDUCED FIT MECHANISM,          
KEYWDS   2 OXOCARBENIUM ION, HYDROLASE                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.LANGAN,Q.WAN,L.COATES,A.KOVALEVSKY                                  
REVDAT   3   15-NOV-17 4HK9    1       REMARK                                   
REVDAT   2   12-FEB-14 4HK9    1       JRNL                                     
REVDAT   1   08-JAN-14 4HK9    0                                                
JRNL        AUTH   Q.WAN,Q.ZHANG,S.HAMILTON-BREHM,K.WEISS,M.MUSTYAKIMOV,        
JRNL        AUTH 2 L.COATES,P.LANGAN,D.GRAHAM,A.KOVALEVSKY                      
JRNL        TITL   X-RAY CRYSTALLOGRAPHIC STUDIES OF FAMILY 11 XYLANASE         
JRNL        TITL 2 MICHAELIS AND PRODUCT COMPLEXES: IMPLICATIONS FOR THE        
JRNL        TITL 3 CATALYTIC MECHANISM.                                         
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  70    11 2014              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   24419374                                                     
JRNL        DOI    10.1107/S1399004713023626                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8_1069                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.97                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 23165                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.150                           
REMARK   3   R VALUE            (WORKING SET) : 0.149                           
REMARK   3   FREE R VALUE                     : 0.179                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.170                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1198                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 19.9730 -  3.2180    0.96     2530   137  0.1328 0.1429        
REMARK   3     2  3.2180 -  2.5559    0.97     2452   127  0.1504 0.1882        
REMARK   3     3  2.5559 -  2.2333    0.98     2413   148  0.1535 0.1812        
REMARK   3     4  2.2333 -  2.0293    0.98     2429   132  0.1395 0.1643        
REMARK   3     5  2.0293 -  1.8840    0.99     2427   126  0.1410 0.1950        
REMARK   3     6  1.8840 -  1.7730    0.99     2440   131  0.1536 0.1874        
REMARK   3     7  1.7730 -  1.6842    1.00     2449   128  0.1740 0.2183        
REMARK   3     8  1.6842 -  1.6110    1.00     2421   139  0.1750 0.2292        
REMARK   3     9  1.6110 -  1.5490    1.00     2406   130  0.1868 0.2092        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.080            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.540           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.72                          
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           1544                                  
REMARK   3   ANGLE     :  1.179           2110                                  
REMARK   3   CHIRALITY :  0.077            214                                  
REMARK   3   PLANARITY :  0.005            272                                  
REMARK   3   DIHEDRAL  : 13.329            512                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4HK9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-NOV-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000075570.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-JUN-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23195                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.09900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.58                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 35.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15-20 % PEG 8,000, 0.2 M CACL2, 0.1 M    
REMARK 280  MES, PH6.0 , VAPOR DIFFUSION, TEMPERATURE 298K                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       21.19800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       31.05850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       29.78750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       31.05850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       21.19800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       29.78750            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.                         
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   407     O    HOH A   473              2.06            
REMARK 500   O    HOH A   466     O    HOH A   475              2.09            
REMARK 500   O    HOH A   507     O    HOH A   549              2.13            
REMARK 500   O    HOH A   316     O    HOH A   348              2.15            
REMARK 500   O    HOH A   458     O    HOH A   553              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   316     O    HOH A   454     4455     2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 170     -141.63    -99.27                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XYP A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XYP A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XYP A 203                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2DFB   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4HK8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4HKL   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4HKO   RELATED DB: PDB                                   
DBREF  4HK9 A    3   190  UNP    P36217   XYN2_HYPJE      35    222             
SEQADV 4HK9 HIS A   44  UNP  P36217    ASN    76 ENGINEERED MUTATION            
SEQRES   1 A  188  ILE GLN PRO GLY THR GLY TYR ASN ASN GLY TYR PHE TYR          
SEQRES   2 A  188  SER TYR TRP ASN ASP GLY HIS GLY GLY VAL THR TYR THR          
SEQRES   3 A  188  ASN GLY PRO GLY GLY GLN PHE SER VAL ASN TRP SER ASN          
SEQRES   4 A  188  SER GLY HIS PHE VAL GLY GLY LYS GLY TRP GLN PRO GLY          
SEQRES   5 A  188  THR LYS ASN LYS VAL ILE ASN PHE SER GLY SER TYR ASN          
SEQRES   6 A  188  PRO ASN GLY ASN SER TYR LEU SER VAL TYR GLY TRP SER          
SEQRES   7 A  188  ARG ASN PRO LEU ILE GLU TYR TYR ILE VAL GLU ASN PHE          
SEQRES   8 A  188  GLY THR TYR ASN PRO SER THR GLY ALA THR LYS LEU GLY          
SEQRES   9 A  188  GLU VAL THR SER ASP GLY SER VAL TYR ASP ILE TYR ARG          
SEQRES  10 A  188  THR GLN ARG VAL ASN GLN PRO SER ILE ILE GLY THR ALA          
SEQRES  11 A  188  THR PHE TYR GLN TYR TRP SER VAL ARG ARG ASN HIS ARG          
SEQRES  12 A  188  SER SER GLY SER VAL ASN THR ALA ASN HIS PHE ASN ALA          
SEQRES  13 A  188  TRP ALA GLN GLN GLY LEU THR LEU GLY THR MET ASP TYR          
SEQRES  14 A  188  GLN ILE VAL ALA VAL GLU GLY TYR PHE SER SER GLY SER          
SEQRES  15 A  188  ALA SER ILE THR VAL SER                                      
HET    XYP  A 201       9                                                       
HET    XYP  A 202       9                                                       
HET    XYP  A 203      10                                                       
HETNAM     XYP BETA-D-XYLOPYRANOSE                                              
FORMUL   2  XYP    3(C5 H10 O5)                                                 
FORMUL   3  HOH   *256(H2 O)                                                    
HELIX    1   1 THR A  152  GLN A  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  15   N  GLY A   8           
SHEET    3   A 9 HIS 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  N  TYR A  77   O  ILE A 173           
SHEET    6   A 9 ILE A  85  PHE A  93 -1  O  TYR A  87   N  GLY A  78           
SHEET    7   A 9 ALA A 132  ARG A 141  1  O  SER A 139   N  VAL A  90           
SHEET    8   A 9 SER A 113  GLN A 125 -1  N  ASP A 116   O  VAL A 140           
SHEET    9   A 9 THR A 103  SER A 110 -1  N  LEU A 105   O  ILE A 117           
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  O  GLY A 183   N  TRP A  39           
SHEET    4   B 5 VAL A  59  ASN A  69 -1  N  ASN A  69   O  SER A 182           
SHEET    5   B 5 GLY A 148  ASN A 151 -1  O  GLY A 148   N  PHE A  62           
LINK         C1B XYP A 201                 O4B XYP A 202     1555   1555  1.42  
LINK         C1B XYP A 202                 O4B XYP A 203     1555   1555  1.43  
CISPEP   1 GLN A   52    PRO A   53          0         2.67                     
CISPEP   2 ASN A   82    PRO A   83          0         7.00                     
SITE     1 AC1  8 SER A  40  ASN A  41  SER A 127  ILE A 128                    
SITE     2 AC1  8 XYP A 202  HOH A 339  HOH A 390  HOH A 402                    
SITE     1 AC2  8 TRP A  18  TYR A  77  PRO A 126  SER A 127                    
SITE     2 AC2  8 TYR A 171  XYP A 201  XYP A 203  HOH A 307                    
SITE     1 AC3 12 HIS A  44  VAL A  46  TYR A  77  TRP A  79                    
SITE     2 AC3 12 GLU A  86  TYR A  88  ARG A 122  PRO A 126                    
SITE     3 AC3 12 GLN A 136  GLU A 177  XYP A 202  HOH A 310                    
CRYST1   42.396   59.575   62.117  90.00  90.00  90.00 P 21 21 21    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      0.023587  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016786  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016099        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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