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Database: PDB
Entry: 4HKW
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Original site: 4HKW 
HEADER    HYDROLASE                               15-OCT-12   4HKW              
TITLE     CRYSTAL STRUCTURES OF MUTANT ENDO-BETA-1,4-XYLANASE II COMPLEXED WITH 
TITLE    2 SUBSTRATE AND PRODUCTS                                               
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                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: TRICHODERMA REESEI;                             
SOURCE   3 ORGANISM_TAXID: 51453                                                
KEYWDS    XYLANASE II, XYLOPENTAOSE, INDUCED FIT MECHANISM, OXOCARBENIUM ION,   
KEYWDS   2 GLYCOSIDASE, HYDROLASE                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.Y.KOVALEVSKY,Q.WAN,P.LANGAN,L.COATES                                
REVDAT   2   12-FEB-14 4HKW    1       JRNL                                     
REVDAT   1   08-JAN-14 4HKW    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.    1.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.8                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R                         
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.159                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.159                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.219                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 944                    
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 18694                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.145                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 16432                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 1480                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 55                                            
REMARK   3   SOLVENT ATOMS      : 248                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 1778.00                 
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 0.00                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 0                       
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 7135                    
REMARK   3   NUMBER OF RESTRAINTS                     : 6377                    
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.008                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.025                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.032                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.047                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.062                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.044                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.000                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.057                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.000                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4HKW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-OCT-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB075593.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JUN-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5417                             
REMARK 200  MONOCHROMATOR                  : NONE                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16432                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 84.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
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: 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   (%): 41.18                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS, 0.1M CACL2, PH=8.5, 15%       
REMARK 280  PEG4000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K            
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       19.21400            
REMARK 290   SMTRY3   2  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 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: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    TYR A  87   CB  -  CG  -  CD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 170     -138.09   -104.62                                   
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 A1155        DISTANCE =  5.05 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                              CA A 407  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A1108   O                                                      
REMARK 620 2 PHE A  93   O   139.2                                              
REMARK 620 3 ASN A  92   OD1 135.1  75.5                                        
REMARK 620 4 HOH A1101   O    68.0  73.3 145.2                                  
REMARK 620 5 HOH A1096   O   129.9  75.1  77.0 109.1                            
REMARK 620 6 HOH A1181   O    72.8 148.0  77.4 136.7  82.5                      
REMARK 620 N                    1     2     3     4     5                       
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 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XYP A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XYS A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XYP A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XYP A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 407                  
DBREF  4HKW A    2   190  UNP    P36217   XYN2_HYPJE      34    222             
SEQADV 4HKW PCA A    1  UNP  P36217              EXPRESSION TAG                 
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                              
MODRES 4HKW PCA A    1  GLU  PYROGLUTAMIC ACID                                  
HET    PCA  A   1       8                                                       
HET    XYP  A 401       9                                                       
HET    XYP  A 402       9                                                       
HET    XYS  A 403      10                                                       
HET    XYP  A 404       9                                                       
HET    XYP  A 405       9                                                       
HET    TRS  A 406       8                                                       
HET     CA  A 407       1                                                       
HETNAM     PCA PYROGLUTAMIC ACID                                                
HETNAM     XYP BETA-D-XYLOPYRANOSE                                              
HETNAM     XYS XYLOPYRANOSE                                                     
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETNAM      CA CALCIUM ION                                                      
HETSYN     TRS TRIS BUFFER                                                      
FORMUL   1  PCA    C5 H7 N O3                                                   
FORMUL   2  XYP    4(C5 H10 O5)                                                 
FORMUL   2  XYS    C5 H10 O5                                                    
FORMUL   4  TRS    C4 H12 N O3 1+                                               
FORMUL   5   CA    CA 2+                                                        
FORMUL   6  HOH   *248(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  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  N  TRP A  79   O  ASP A 170           
SHEET    6   A 9 ILE A  85  PHE A  93 -1  O  ILE A  89   N  VAL A  76           
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  ARG A 122   O  PHE A 134           
SHEET    9   A 9 LYS A 104  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  61   O  SER A 190           
SHEET    5   B 5 GLY A 148  ASN A 151 -1  O  GLY A 148   N  PHE A  62           
LINK         C   PCA A   1                 N   THR A   2     1555   1555  1.32  
LINK         C1B XYP A 404                 O4B XYP A 405     1555   1555  1.43  
LINK         C1B XYP A 405                 O1  TRS A 406     1555   1555  1.44  
LINK         C1B XYP A 401                 O4B XYP A 402     1555   1555  1.44  
LINK         C1B XYP A 402                 O4  XYS A 403     1555   1555  1.44  
LINK        CA    CA A 407                 O   HOH A1108     1555   1555  2.39  
LINK         O   PHE A  93                CA    CA A 407     1555   1555  2.44  
LINK         OD1 ASN A  92                CA    CA A 407     1555   1555  2.46  
LINK        CA    CA A 407                 O   HOH A1101     1555   1555  2.53  
LINK        CA    CA A 407                 O   HOH A1096     1555   1555  2.55  
LINK        CA    CA A 407                 O   HOH A1181     1555   1555  2.63  
CISPEP   1 GLN A   52    PRO A   53          0        -3.58                     
CISPEP   2 ASN A   82    PRO A   83          0         1.95                     
SITE     1 AC1 12 ASN A  44  TYR A  73  TYR A  88  ARG A 122                    
SITE     2 AC1 12 GLN A 136  TRP A 138  GLU A 177  TYR A 179                    
SITE     3 AC1 12 XYP A 402  TRS A 406  HOH A1006  HOH A1147                    
SITE     1 AC2  7 ASN A  71  TYR A  73  TYR A  96  TYR A 179                    
SITE     2 AC2  7 XYP A 401  XYS A 403  HOH A1147                               
SITE     1 AC3  5 ASN A  71  TYR A  96  XYP A 402  HOH A1170                    
SITE     2 AC3  5 HOH A1206                                                     
SITE     1 AC4  7 TRP A  18  SER A 127  ILE A 128  XYP A 405                    
SITE     2 AC4  7 HOH A1095  HOH A1104  HOH A1138                               
SITE     1 AC5  9 TRP A  18  TYR A  77  PRO A 126  SER A 127                    
SITE     2 AC5  9 TYR A 171  XYP A 404  TRS A 406  HOH A1011                    
SITE     3 AC5  9 HOH A1014                                                     
SITE     1 AC6  8 ASN A  44  TYR A  77  GLU A  86  ARG A 122                    
SITE     2 AC6  8 PRO A 126  XYP A 401  XYP A 405  HOH A1183                    
SITE     1 AC7  7 ASN A  92  PHE A  93  HIS A 144  HOH A1096                    
SITE     2 AC7  7 HOH A1101  HOH A1108  HOH A1181                               
CRYST1   41.879   38.428   56.315  90.00 105.93  90.00 P 1 21 1      2          
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      0.023878  0.000000  0.006815        0.00000                         
SCALE2      0.000000  0.026023  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018466        0.00000                         
HETATM    1  N   PCA A   1      18.200 -21.830  12.266  1.00 31.48           N  
HETATM    2  CA  PCA A   1      19.461 -21.285  12.703  1.00 25.70           C  
HETATM    3  CB  PCA A   1      20.326 -21.370  11.436  1.00 20.63           C  
HETATM    4  CG  PCA A   1      19.393 -21.685  10.304  1.00 31.44           C  
HETATM    5  CD  PCA A   1      18.153 -22.219  10.970  1.00 37.58           C  
HETATM    6  OE  PCA A   1      17.282 -22.880  10.412  1.00 43.91           O  
HETATM    7  C   PCA A   1      19.336 -19.788  12.964  1.00 26.53           C  
HETATM    8  O   PCA A   1      18.293 -19.229  12.555  1.00 19.68           O  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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