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Database: PDB
Entry: 3HD8
LinkDB: 3HD8
Original site: 3HD8 
HEADER    HYDROLASE INHIBITOR/HYDROLASE           07-MAY-09   3HD8              
TITLE     CRYSTAL STRUCTURE OF THE TRITICUM AESTIVUM XYLANASE INHIBITOR-IIA IN  
TITLE    2 COMPLEX WITH BACILLUS SUBTILIS XYLANASE                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: XYLANASE INHIBITOR;                                        
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: XYLANASE INHIBITOR IIA;                                     
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: ENDO-1,4-BETA-XYLANASE A;                                  
COMPND   8 CHAIN: B, D;                                                         
COMPND   9 SYNONYM: XYLANASE A, 1,4-BETA-D-XYLAN XYLANOHYDROLASE A;             
COMPND  10 EC: 3.2.1.8;                                                         
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: TRITICUM AESTIVUM;                              
SOURCE   3 ORGANISM_COMMON: WHEAT;                                              
SOURCE   4 ORGANISM_TAXID: 4565;                                                
SOURCE   5 GENE: XYNA;                                                          
SOURCE   6 EXPRESSION_SYSTEM: PICHIA PASTORIS;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PPICZAC;                                  
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE  12 ORGANISM_TAXID: 1423;                                                
SOURCE  13 GENE: XYNA;                                                          
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TWO BETA-BARREL DOMAIN, BETA-JELLY ROLL, HYDROLASE INHIBITOR-         
KEYWDS   2 HYDROLASE COMPLEX, PROTEIN-PROTEIN COMPLEX, XYLAN DEGRADATION,       
KEYWDS   3 GLYCOSIDASE, HYDROLASE                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.SANSEN,A.POLLET,G.RAEDSCHELDERS,K.GEBRUERS,A.RABIJNS,C.M.COURTIN    
REVDAT   2   30-JUN-10 3HD8    1       JRNL                                     
REVDAT   1   30-JUN-09 3HD8    0                                                
JRNL        AUTH   A.POLLET,S.SANSEN,G.RAEDSCHELDERS,K.GEBRUERS,A.RABIJNS,      
JRNL        AUTH 2 J.A.DELCOUR,C.M.COURTIN                                      
JRNL        TITL   IDENTIFICATION OF STRUCTURAL DETERMINANTS FOR INHIBITION     
JRNL        TITL 2 STRENGTH AND SPECIFICITY OF WHEAT XYLANASE INHIBITORS        
JRNL        TITL 3 TAXI-IA AND TAXI-IIA                                         
JRNL        REF    FEBS J.                       V. 276  3916 2009              
JRNL        REFN                   ISSN 1742-464X                               
JRNL        PMID   19769747                                                     
JRNL        DOI    10.1111/J.1742-4658.2009.07105.X                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.39 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.19                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.39                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.52                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 44570                          
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 + TEST SET) : 0.226                           
REMARK   3   R VALUE            (WORKING SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2427                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.39                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.45                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2935                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3640                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 153                          
REMARK   3   BIN FREE R VALUE                    : 0.4030                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8240                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 42                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.73                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.58000                                              
REMARK   3    B22 (A**2) : 0.58000                                              
REMARK   3    B33 (A**2) : -0.71000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.15000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.444         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.285         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.219         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.539         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.916                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.880                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8474 ; 0.027 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  7450 ; 0.004 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11588 ; 2.237 ; 1.942       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 17328 ; 1.222 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1096 ; 9.191 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1280 ; 0.128 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9586 ; 0.010 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1736 ; 0.009 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1672 ; 0.242 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  8523 ; 0.265 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  5130 ; 0.100 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   178 ; 0.213 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    34 ; 0.347 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    83 ; 0.351 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     4 ; 0.068 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5468 ; 1.063 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8768 ; 1.951 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3006 ; 2.631 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2820 ; 4.310 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A     389      0                      
REMARK   3           1     C      1       C     389      0                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   5199 ; 0.070 ; 0.050           
REMARK   3   TIGHT THERMAL      1    A (A**2):   5199 ; 0.400 ; 0.500           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : B D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B      1       B     185      0                      
REMARK   3           1     D      1       D     185      0                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    B    (A):   2636 ; 0.080 ; 0.050           
REMARK   3   TIGHT THERMAL      2    B (A**2):   2636 ; 0.370 ; 0.500           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3HD8 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-MAY-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB052991.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-NOV-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : BW7A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.811                              
REMARK 200  MONOCHROMATOR                  : SI [111], HORIZONTALLY FOCUSSING   
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45604                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.380                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.38                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.44                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.34100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRIES 1T6E FOR CHAINS A AND C; 1C5H FOR THE    
REMARK 200  CHAINS B AND D                                                      
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% (W/V) POLYETHYLENE GLYCOL 4000,      
REMARK 280  0.18M AMMONIUM SULFATE, 0.1M SODIUM ACETATE BUFFER , PH 4.6,        
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                     
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       30.15000            
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 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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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     GLY A    44                                                      
REMARK 465     GLN A    45                                                      
REMARK 465     SER A    46                                                      
REMARK 465     PRO A    47                                                      
REMARK 465     PRO A    71                                                      
REMARK 465     SER A    72                                                      
REMARK 465     CYS A    73                                                      
REMARK 465     GLY A    74                                                      
REMARK 465     SER A    75                                                      
REMARK 465     ASP A    76                                                      
REMARK 465     ARG A    77                                                      
REMARK 465     HIS A    78                                                      
REMARK 465     ASP A    79                                                      
REMARK 465     PRO A   265                                                      
REMARK 465     ALA A   266                                                      
REMARK 465     ASN A   267                                                      
REMARK 465     ARG A   387                                                      
REMARK 465     SER A   388                                                      
REMARK 465     THR A   389                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     GLY C    44                                                      
REMARK 465     GLN C    45                                                      
REMARK 465     SER C    46                                                      
REMARK 465     PRO C    47                                                      
REMARK 465     ALA C    48                                                      
REMARK 465     PRO C    71                                                      
REMARK 465     SER C    72                                                      
REMARK 465     CYS C    73                                                      
REMARK 465     GLY C    74                                                      
REMARK 465     SER C    75                                                      
REMARK 465     ASP C    76                                                      
REMARK 465     ARG C    77                                                      
REMARK 465     HIS C    78                                                      
REMARK 465     ASP C    79                                                      
REMARK 465     PRO C   265                                                      
REMARK 465     ALA C   266                                                      
REMARK 465     ASN C   267                                                      
REMARK 465     ALA C   386                                                      
REMARK 465     ARG C   387                                                      
REMARK 465     SER C   388                                                      
REMARK 465     THR C   389                                                      
REMARK 465     ALA D     1                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ALA A 143    CB                                                  
REMARK 470     PRO A 277    CG   CD                                             
REMARK 470     GLU A 282    CB   CG   CD   OE1  OE2                             
REMARK 470     ALA C 143    CB                                                  
REMARK 470     PRO C 277    CG   CD                                             
REMARK 470     GLU C 282    CB   CG   CD   OE1  OE2                             
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   NH2  ARG C   213     OD1  ASP C   307              2.05            
REMARK 500   ND2  ASN A   107     O    HOH A   396              2.11            
REMARK 500   ND2  ASN C   107     O    HOH C   395              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    SER A 148   CA    SER A 148   CB      0.096                       
REMARK 500    LYS A 165   CE    LYS A 165   NZ      0.169                       
REMARK 500    ASP A 195   CB    ASP A 195   CG      0.136                       
REMARK 500    ASN A 384   CB    ASN A 384   CG     -0.149                       
REMARK 500    ASN A 384   CA    ASN A 384   C       0.167                       
REMARK 500    PHE A 385   CD1   PHE A 385   CE1     0.147                       
REMARK 500    VAL B  82   CB    VAL B  82   CG2    -0.135                       
REMARK 500    SER B 130   CB    SER B 130   OG     -0.088                       
REMARK 500    ASN B 163   CB    ASN B 163   CG     -0.169                       
REMARK 500    TRP B 164   CB    TRP B 164   CG     -0.158                       
REMARK 500    SER C 148   CA    SER C 148   CB      0.110                       
REMARK 500    ASP C 195   CB    ASP C 195   CG      0.181                       
REMARK 500    ARG C 213   CZ    ARG C 213   NH2     0.083                       
REMARK 500    PHE C 385   CD1   PHE C 385   CE1     0.127                       
REMARK 500    PHE D  48   CD1   PHE D  48   CE1     0.124                       
REMARK 500    TYR D 174   CE1   TYR D 174   CZ     -0.084                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    ASP A 110   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ARG A 213   CA  -  CB  -  CG  ANGL. DEV. =  26.1 DEGREES          
REMARK 500    ASP A 248   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ARG A 273   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ASP A 307   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP A 357   CB  -  CG  -  OD2 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    ASP A 361   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASN A 384   N   -  CA  -  C   ANGL. DEV. =  23.5 DEGREES          
REMARK 500    ASN B 163   CB  -  CA  -  C   ANGL. DEV. =  17.2 DEGREES          
REMARK 500    TRP B 185   CA  -  C   -  O   ANGL. DEV. =  12.9 DEGREES          
REMARK 500    LYS C 165   CD  -  CE  -  NZ  ANGL. DEV. =  17.4 DEGREES          
REMARK 500    ASP C 195   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ARG C 213   CA  -  CB  -  CG  ANGL. DEV. =  32.5 DEGREES          
REMARK 500    ARG C 273   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ASP C 286   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP C 307   CB  -  CG  -  OD2 ANGL. DEV. =   9.1 DEGREES          
REMARK 500    ASP C 342   CB  -  CG  -  OD2 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    ASP C 361   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASN C 384   N   -  CA  -  C   ANGL. DEV. =  23.0 DEGREES          
REMARK 500    ASP D   4   CB  -  CG  -  OD2 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    ASP D 101   CB  -  CG  -  OD2 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ASP D 121   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    TYR D 174   CE1 -  CZ  -  OH  ANGL. DEV. = -16.8 DEGREES          
REMARK 500    TRP D 185   CA  -  C   -  O   ANGL. DEV. =  14.9 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    PHE A  22      -70.38   -114.54                                   
REMARK 500    GLU A  49      -84.43    -86.62                                   
REMARK 500    ILE A  50      119.42     53.11                                   
REMARK 500    PRO A  66      -71.84    -22.72                                   
REMARK 500    PRO A  69     -116.15    -97.95                                   
REMARK 500    ALA A 106     -152.92   -152.85                                   
REMARK 500    VAL A 115      -82.26    -96.88                                   
REMARK 500    SER A 134        7.07     80.14                                   
REMARK 500    SER A 148     -144.88    179.36                                   
REMARK 500    SER A 205      110.58   -160.69                                   
REMARK 500    ALA A 207     -179.60    -55.65                                   
REMARK 500    GLU A 218     -108.89     54.84                                   
REMARK 500    SER A 225      148.25    -39.08                                   
REMARK 500    GLU A 226       98.77    -21.60                                   
REMARK 500    ALA A 230     -169.62    -46.32                                   
REMARK 500    LYS A 276      105.80    -52.51                                   
REMARK 500    PRO A 277      122.72    -39.25                                   
REMARK 500    LEU A 283       91.57    174.11                                   
REMARK 500    ALA A 331       38.76    -87.81                                   
REMARK 500    ASN A 384     -156.22    145.28                                   
REMARK 500    PHE A 385       54.05    -95.54                                   
REMARK 500    ASN B 114       48.10     37.33                                   
REMARK 500    ALA B 165     -150.07   -107.32                                   
REMARK 500    GLN B 175       59.20     37.29                                   
REMARK 500    PHE C  22      -70.38   -117.14                                   
REMARK 500    ILE C  50      122.25     61.29                                   
REMARK 500    PRO C  66      -69.29    -27.31                                   
REMARK 500    PRO C  69     -118.49   -101.97                                   
REMARK 500    ALA C 106     -151.99   -154.95                                   
REMARK 500    VAL C 115      -70.56   -109.50                                   
REMARK 500    SER C 134        8.74     84.83                                   
REMARK 500    SER C 148     -144.72    175.82                                   
REMARK 500    SER C 205      118.60   -161.46                                   
REMARK 500    ALA C 207      176.24    -59.97                                   
REMARK 500    GLU C 218     -115.83     50.81                                   
REMARK 500    SER C 225      143.14    -34.33                                   
REMARK 500    GLU C 226      100.46    -20.46                                   
REMARK 500    ALA C 230     -169.50    -51.49                                   
REMARK 500    LEU C 283       93.01   -173.00                                   
REMARK 500    ALA C 331       38.91    -89.57                                   
REMARK 500    ASN C 384     -153.41    140.78                                   
REMARK 500    SER D  74       62.54     62.55                                   
REMARK 500    ASN D 114       55.65     27.99                                   
REMARK 500    ALA D 165     -144.87   -112.60                                   
REMARK 500    GLN D 175       57.60     38.91                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU A    1     GLY A    2                  149.86                    
REMARK 500 ALA A   48     GLU A   49                 -116.98                    
REMARK 500 ALA A  146     GLY A  147                 -145.98                    
REMARK 500 SER A  225     GLU A  226                  129.90                    
REMARK 500 ASN A  384     PHE A  385                 -139.15                    
REMARK 500 THR B   33     GLY B   34                  147.64                    
REMARK 500 GLU C    1     GLY C    2                  145.80                    
REMARK 500 LEU C   36     VAL C   37                  148.82                    
REMARK 500 ALA C  146     GLY C  147                 -145.10                    
REMARK 500 SER C  225     GLU C  226                  129.62                    
REMARK 500 ASN C  384     PHE C  385                 -135.08                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASN A 384        17.1      L          L   OUTSIDE RANGE           
REMARK 500    ASN C 384        17.1      L          L   OUTSIDE RANGE           
REMARK 500    ASN D 163        24.4      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1T6E   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE TRITICUM AESTIVUM XYLANASE                  
REMARK 900 INHIBITOR I                                                          
REMARK 900 RELATED ID: 1T6G   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE TRITICUM AESTIVUM XYLANASE                  
REMARK 900 INHIBITOR-I IN COMPLEX WITH ASPERGILLUS NIGER XYLANASE-I             
REMARK 900 RELATED ID: 2B42   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE TRITICUM XYLANSE INHIBITOR-I IN             
REMARK 900 COMPLEX WITH BACILLUS SUBTILIS XYLANASE                              
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 BASED ON THE PAPER (PMID: 16084833) DESCRIBING THE TAXI-IIA          
REMARK 999 SEQUENCE (CHAINS A AND C) THE CORRECT SEQUENCE SHOULD BE GLU1,       
REMARK 999 PRO163 AND LEU314. FOR THE XYLANASE (CHAINS B AND D) RESIDUE 147     
REMARK 999 SHOULD BE SERINE.                                                    
DBREF  3HD8 A    1   389  UNP    Q53IQ4   Q53IQ4_WHEAT     1    389             
DBREF  3HD8 B    1   185  UNP    P18429   XYNA_BACSU      29    213             
DBREF  3HD8 C    1   389  UNP    Q53IQ4   Q53IQ4_WHEAT     1    389             
DBREF  3HD8 D    1   185  UNP    P18429   XYNA_BACSU      29    213             
SEQADV 3HD8 GLU A    1  UNP  Q53IQ4    LYS     1 SEE REMARK 999                 
SEQADV 3HD8 PRO A  163  UNP  Q53IQ4    ALA   163 SEE REMARK 999                 
SEQADV 3HD8 MET A  314  UNP  Q53IQ4    LEU   314 SEE REMARK 999                 
SEQADV 3HD8 THR B  147  UNP  P18429    SER   175 SEE REMARK 999                 
SEQADV 3HD8 GLU C    1  UNP  Q53IQ4    LYS     1 SEE REMARK 999                 
SEQADV 3HD8 PRO C  163  UNP  Q53IQ4    ALA   163 SEE REMARK 999                 
SEQADV 3HD8 MET C  314  UNP  Q53IQ4    LEU   314 SEE REMARK 999                 
SEQADV 3HD8 THR D  147  UNP  P18429    SER   175 SEE REMARK 999                 
SEQRES   1 A  389  GLU GLY LEU PRO VAL LEU ALA PRO VAL THR LYS ASP THR          
SEQRES   2 A  389  ALA THR SER LEU TYR THR ILE PRO PHE HIS ASP GLY ALA          
SEQRES   3 A  389  SER LEU VAL LEU ASP VAL ALA GLY LEU LEU VAL TRP SER          
SEQRES   4 A  389  THR CYS GLU GLY GLY GLN SER PRO ALA GLU ILE ALA CYS          
SEQRES   5 A  389  SER SER PRO THR CYS LEU LEU ALA ASN ALA TYR PRO ALA          
SEQRES   6 A  389  PRO GLY CYS PRO ALA PRO SER CYS GLY SER ASP ARG HIS          
SEQRES   7 A  389  ASP LYS PRO CYS THR ALA TYR PRO SER ASN PRO VAL THR          
SEQRES   8 A  389  GLY ALA CYS ALA ALA GLY SER LEU PHE HIS THR ARG PHE          
SEQRES   9 A  389  ALA ALA ASN THR THR ASP GLY ASN LYS PRO VAL SER GLU          
SEQRES  10 A  389  VAL ASN VAL ARG VAL LEU ALA ALA CYS ALA PRO SER LYS          
SEQRES  11 A  389  LEU LEU ALA SER LEU PRO ARG GLY SER THR GLY VAL ALA          
SEQRES  12 A  389  GLY LEU ALA GLY SER GLY LEU ALA LEU PRO SER GLN VAL          
SEQRES  13 A  389  ALA SER ALA GLN LYS VAL PRO ASN LYS PHE LEU LEU CYS          
SEQRES  14 A  389  LEU PRO THR GLY GLY PRO GLY VAL ALA ILE PHE GLY GLY          
SEQRES  15 A  389  GLY PRO LEU PRO TRP PRO GLN PHE THR GLN SER MET ASP          
SEQRES  16 A  389  TYR THR PRO LEU VAL ALA LYS GLY GLY SER PRO ALA HIS          
SEQRES  17 A  389  TYR ILE SER ALA ARG SER ILE LYS VAL GLU ASN THR ARG          
SEQRES  18 A  389  VAL PRO ILE SER GLU ARG ALA LEU ALA THR GLY GLY VAL          
SEQRES  19 A  389  MET LEU SER THR ARG LEU PRO TYR VAL LEU LEU ARG ARG          
SEQRES  20 A  389  ASP VAL TYR ARG PRO LEU VAL ASP ALA PHE THR LYS ALA          
SEQRES  21 A  389  LEU ALA ALA GLN PRO ALA ASN GLY ALA PRO VAL ALA ARG          
SEQRES  22 A  389  ALA VAL LYS PRO VAL ALA PRO PHE GLU LEU CYS TYR ASP          
SEQRES  23 A  389  THR LYS THR LEU GLY ASN ASN PRO GLY GLY TYR TRP VAL          
SEQRES  24 A  389  PRO ASN VAL LEU LEU GLU LEU ASP GLY GLY SER ASP TRP          
SEQRES  25 A  389  ALA MET THR GLY LYS ASN SER MET VAL ASP VAL LYS PRO          
SEQRES  26 A  389  GLY THR ALA CYS VAL ALA PHE VAL GLU MET LYS GLY VAL          
SEQRES  27 A  389  ASP ALA GLY ASP GLY SER ALA PRO ALA VAL ILE LEU GLY          
SEQRES  28 A  389  GLY ALA GLN MET GLU ASP PHE VAL LEU ASP PHE ASP MET          
SEQRES  29 A  389  GLU LYS LYS ARG LEU GLY PHE LEU ARG LEU PRO HIS PHE          
SEQRES  30 A  389  THR GLY CYS SER SER PHE ASN PHE ALA ARG SER THR              
SEQRES   1 B  185  ALA SER THR ASP TYR TRP GLN ASN TRP THR ASP GLY GLY          
SEQRES   2 B  185  GLY ILE VAL ASN ALA VAL ASN GLY SER GLY GLY ASN TYR          
SEQRES   3 B  185  SER VAL ASN TRP SER ASN THR GLY ASN PHE VAL VAL GLY          
SEQRES   4 B  185  LYS GLY TRP THR THR GLY SER PRO PHE ARG THR ILE ASN          
SEQRES   5 B  185  TYR ASN ALA GLY VAL TRP ALA PRO ASN GLY ASN GLY TYR          
SEQRES   6 B  185  LEU THR LEU TYR GLY TRP THR ARG SER PRO LEU ILE GLU          
SEQRES   7 B  185  TYR TYR VAL VAL ASP SER TRP GLY THR TYR ARG PRO THR          
SEQRES   8 B  185  GLY THR TYR LYS GLY THR VAL LYS SER ASP GLY GLY THR          
SEQRES   9 B  185  TYR ASP ILE TYR THR THR THR ARG TYR ASN ALA PRO SER          
SEQRES  10 B  185  ILE ASP GLY ASP ARG THR THR PHE THR GLN TYR TRP SER          
SEQRES  11 B  185  VAL ARG GLN SER LYS ARG PRO THR GLY SER ASN ALA THR          
SEQRES  12 B  185  ILE THR PHE THR ASN HIS VAL ASN ALA TRP LYS SER HIS          
SEQRES  13 B  185  GLY MET ASN LEU GLY SER ASN TRP ALA TYR GLN VAL MET          
SEQRES  14 B  185  ALA THR GLU GLY TYR GLN SER SER GLY SER SER ASN VAL          
SEQRES  15 B  185  THR VAL TRP                                                  
SEQRES   1 C  389  GLU GLY LEU PRO VAL LEU ALA PRO VAL THR LYS ASP THR          
SEQRES   2 C  389  ALA THR SER LEU TYR THR ILE PRO PHE HIS ASP GLY ALA          
SEQRES   3 C  389  SER LEU VAL LEU ASP VAL ALA GLY LEU LEU VAL TRP SER          
SEQRES   4 C  389  THR CYS GLU GLY GLY GLN SER PRO ALA GLU ILE ALA CYS          
SEQRES   5 C  389  SER SER PRO THR CYS LEU LEU ALA ASN ALA TYR PRO ALA          
SEQRES   6 C  389  PRO GLY CYS PRO ALA PRO SER CYS GLY SER ASP ARG HIS          
SEQRES   7 C  389  ASP LYS PRO CYS THR ALA TYR PRO SER ASN PRO VAL THR          
SEQRES   8 C  389  GLY ALA CYS ALA ALA GLY SER LEU PHE HIS THR ARG PHE          
SEQRES   9 C  389  ALA ALA ASN THR THR ASP GLY ASN LYS PRO VAL SER GLU          
SEQRES  10 C  389  VAL ASN VAL ARG VAL LEU ALA ALA CYS ALA PRO SER LYS          
SEQRES  11 C  389  LEU LEU ALA SER LEU PRO ARG GLY SER THR GLY VAL ALA          
SEQRES  12 C  389  GLY LEU ALA GLY SER GLY LEU ALA LEU PRO SER GLN VAL          
SEQRES  13 C  389  ALA SER ALA GLN LYS VAL PRO ASN LYS PHE LEU LEU CYS          
SEQRES  14 C  389  LEU PRO THR GLY GLY PRO GLY VAL ALA ILE PHE GLY GLY          
SEQRES  15 C  389  GLY PRO LEU PRO TRP PRO GLN PHE THR GLN SER MET ASP          
SEQRES  16 C  389  TYR THR PRO LEU VAL ALA LYS GLY GLY SER PRO ALA HIS          
SEQRES  17 C  389  TYR ILE SER ALA ARG SER ILE LYS VAL GLU ASN THR ARG          
SEQRES  18 C  389  VAL PRO ILE SER GLU ARG ALA LEU ALA THR GLY GLY VAL          
SEQRES  19 C  389  MET LEU SER THR ARG LEU PRO TYR VAL LEU LEU ARG ARG          
SEQRES  20 C  389  ASP VAL TYR ARG PRO LEU VAL ASP ALA PHE THR LYS ALA          
SEQRES  21 C  389  LEU ALA ALA GLN PRO ALA ASN GLY ALA PRO VAL ALA ARG          
SEQRES  22 C  389  ALA VAL LYS PRO VAL ALA PRO PHE GLU LEU CYS TYR ASP          
SEQRES  23 C  389  THR LYS THR LEU GLY ASN ASN PRO GLY GLY TYR TRP VAL          
SEQRES  24 C  389  PRO ASN VAL LEU LEU GLU LEU ASP GLY GLY SER ASP TRP          
SEQRES  25 C  389  ALA MET THR GLY LYS ASN SER MET VAL ASP VAL LYS PRO          
SEQRES  26 C  389  GLY THR ALA CYS VAL ALA PHE VAL GLU MET LYS GLY VAL          
SEQRES  27 C  389  ASP ALA GLY ASP GLY SER ALA PRO ALA VAL ILE LEU GLY          
SEQRES  28 C  389  GLY ALA GLN MET GLU ASP PHE VAL LEU ASP PHE ASP MET          
SEQRES  29 C  389  GLU LYS LYS ARG LEU GLY PHE LEU ARG LEU PRO HIS PHE          
SEQRES  30 C  389  THR GLY CYS SER SER PHE ASN PHE ALA ARG SER THR              
SEQRES   1 D  185  ALA SER THR ASP TYR TRP GLN ASN TRP THR ASP GLY GLY          
SEQRES   2 D  185  GLY ILE VAL ASN ALA VAL ASN GLY SER GLY GLY ASN TYR          
SEQRES   3 D  185  SER VAL ASN TRP SER ASN THR GLY ASN PHE VAL VAL GLY          
SEQRES   4 D  185  LYS GLY TRP THR THR GLY SER PRO PHE ARG THR ILE ASN          
SEQRES   5 D  185  TYR ASN ALA GLY VAL TRP ALA PRO ASN GLY ASN GLY TYR          
SEQRES   6 D  185  LEU THR LEU TYR GLY TRP THR ARG SER PRO LEU ILE GLU          
SEQRES   7 D  185  TYR TYR VAL VAL ASP SER TRP GLY THR TYR ARG PRO THR          
SEQRES   8 D  185  GLY THR TYR LYS GLY THR VAL LYS SER ASP GLY GLY THR          
SEQRES   9 D  185  TYR ASP ILE TYR THR THR THR ARG TYR ASN ALA PRO SER          
SEQRES  10 D  185  ILE ASP GLY ASP ARG THR THR PHE THR GLN TYR TRP SER          
SEQRES  11 D  185  VAL ARG GLN SER LYS ARG PRO THR GLY SER ASN ALA THR          
SEQRES  12 D  185  ILE THR PHE THR ASN HIS VAL ASN ALA TRP LYS SER HIS          
SEQRES  13 D  185  GLY MET ASN LEU GLY SER ASN TRP ALA TYR GLN VAL MET          
SEQRES  14 D  185  ALA THR GLU GLY TYR GLN SER SER GLY SER SER ASN VAL          
SEQRES  15 D  185  THR VAL TRP                                                  
FORMUL   5  HOH   *42(H2 O)                                                     
HELIX    1   1 SER A   54  ASN A   61  1                                   8    
HELIX    2   2 PRO A  128  ALA A  133  5                                   6    
HELIX    3   3 ALA A  151  LYS A  161  1                                  11    
HELIX    4   4 TRP A  187  GLN A  192  1                                   6    
HELIX    5   5 ARG A  246  ALA A  263  1                                  18    
HELIX    6   6 LYS A  288  LEU A  290  5                                   3    
HELIX    7   7 THR A  315  SER A  319  1                                   5    
HELIX    8   8 GLY A  351  MET A  355  5                                   5    
HELIX    9   9 GLY A  379  PHE A  383  5                                   5    
HELIX   10  10 PHE B  146  SER B  155  1                                  10    
HELIX   11  11 SER C   54  ASN C   61  1                                   8    
HELIX   12  12 PRO C  128  ALA C  133  5                                   6    
HELIX   13  13 ALA C  151  LYS C  161  1                                  11    
HELIX   14  14 TRP C  187  GLN C  192  1                                   6    
HELIX   15  15 ARG C  246  ALA C  263  1                                  18    
HELIX   16  16 LYS C  288  LEU C  290  5                                   3    
HELIX   17  17 THR C  315  SER C  319  1                                   5    
HELIX   18  18 GLY C  351  GLU C  356  1                                   6    
HELIX   19  19 GLY C  379  PHE C  383  5                                   5    
HELIX   20  20 PHE D  146  SER D  155  1                                  10    
SHEET    1   A 8 THR A  83  ALA A  84  0                                        
SHEET    2   A 8 GLY A  97  THR A 109 -1  O  GLY A  97   N  ALA A  84           
SHEET    3   A 8 VAL A   5  LYS A  11 -1  N  LEU A   6   O  ASN A 107           
SHEET    4   A 8 GLY A 176  PHE A 180 -1  O  PHE A 180   N  VAL A   5           
SHEET    5   A 8 LYS A 165  CYS A 169 -1  N  LEU A 167   O  ILE A 179           
SHEET    6   A 8 PHE A 358  ASP A 363 -1  O  LEU A 360   N  LEU A 168           
SHEET    7   A 8 ARG A 368  ARG A 373 -1  O  ARG A 368   N  ASP A 363           
SHEET    8   A 8 ASP A 195  PRO A 198 -1  N  THR A 197   O  LEU A 369           
SHEET    1   B13 THR A  83  ALA A  84  0                                        
SHEET    2   B13 GLY A  97  THR A 109 -1  O  GLY A  97   N  ALA A  84           
SHEET    3   B13 PRO A 114  CYS A 126 -1  O  VAL A 122   N  THR A 102           
SHEET    4   B13 VAL A  37  SER A  39  1  N  SER A  39   O  ALA A 125           
SHEET    5   B13 SER A 139  GLY A 144 -1  O  VAL A 142   N  TRP A  38           
SHEET    6   B13 ALA A  26  ASP A  31  1  N  VAL A  29   O  ALA A 143           
SHEET    7   B13 TYR A  18  HIS A  23 -1  N  TYR A  18   O  LEU A  30           
SHEET    8   B13 VAL A   5  LYS A  11 -1  N  THR A  10   O  THR A  19           
SHEET    9   B13 GLY A 176  PHE A 180 -1  O  PHE A 180   N  VAL A   5           
SHEET   10   B13 LYS A 165  CYS A 169 -1  N  LEU A 167   O  ILE A 179           
SHEET   11   B13 PHE A 358  ASP A 363 -1  O  LEU A 360   N  LEU A 168           
SHEET   12   B13 ARG A 368  ARG A 373 -1  O  ARG A 368   N  ASP A 363           
SHEET   13   B13 ASP A 195  PRO A 198 -1  N  THR A 197   O  LEU A 369           
SHEET    1   C 5 TYR A 209  ILE A 210  0                                        
SHEET    2   C 5 VAL A 234  LEU A 236 -1  O  VAL A 234   N  ILE A 210           
SHEET    3   C 5 VAL A 348  LEU A 350  1  O  VAL A 348   N  MET A 235           
SHEET    4   C 5 VAL A 243  LEU A 245 -1  N  LEU A 244   O  ILE A 349           
SHEET    5   C 5 PHE A 332  GLU A 334  1  O  VAL A 333   N  LEU A 245           
SHEET    1   D 4 THR A 220  ARG A 221  0                                        
SHEET    2   D 4 ALA A 212  VAL A 217 -1  N  VAL A 217   O  THR A 220           
SHEET    3   D 4 VAL A 302  LEU A 306 -1  O  LEU A 303   N  LYS A 216           
SHEET    4   D 4 ASP A 311  MET A 314 -1  O  TRP A 312   N  LEU A 304           
SHEET    1   E 4 ALA A 274  VAL A 275  0                                        
SHEET    2   E 4 CYS A 284  ASP A 286 -1  O  CYS A 284   N  VAL A 275           
SHEET    3   E 4 THR A 327  VAL A 330 -1  O  ALA A 328   N  TYR A 285           
SHEET    4   E 4 MET A 320  LYS A 324 -1  N  VAL A 321   O  CYS A 329           
SHEET    1   F 2 ASN A 292  ASN A 293  0                                        
SHEET    2   F 2 GLY A 296  TYR A 297 -1  O  GLY A 296   N  ASN A 293           
SHEET    1   G 8 TYR B   5  THR B  10  0                                        
SHEET    2   G 8 ASN B  35  TRP B  42 -1  O  VAL B  37   N  TRP B   9           
SHEET    3   G 8 ASN B 163  TRP B 185 -1  O  THR B 171   N  VAL B  38           
SHEET    4   G 8 THR B  50  ARG B  73 -1  N  THR B  67   O  ALA B 170           
SHEET    5   G 8 ILE B  77  TRP B  85 -1  O  VAL B  81   N  LEU B  68           
SHEET    6   G 8 GLY B 120  ARG B 132  1  O  SER B 130   N  TYR B  80           
SHEET    7   G 8 GLY B 103  SER B 117 -1  N  ARG B 112   O  PHE B 125           
SHEET    8   G 8 THR B  93  SER B 100 -1  N  GLY B  96   O  ILE B 107           
SHEET    1   H 5 ILE B  15  ASN B  20  0                                        
SHEET    2   H 5 ASN B  25  SER B  31 -1  O  ASN B  29   N  ASN B  17           
SHEET    3   H 5 ASN B 163  TRP B 185 -1  O  GLY B 178   N  TRP B  30           
SHEET    4   H 5 THR B  50  ARG B  73 -1  N  THR B  67   O  ALA B 170           
SHEET    5   H 5 ALA B 142  THR B 145 -1  O  ALA B 142   N  TYR B  53           
SHEET    1   I 8 THR C  83  ALA C  84  0                                        
SHEET    2   I 8 GLY C  97  THR C 109 -1  O  GLY C  97   N  ALA C  84           
SHEET    3   I 8 VAL C   5  LYS C  11 -1  N  LEU C   6   O  ASN C 107           
SHEET    4   I 8 PRO C 175  PHE C 180 -1  O  PHE C 180   N  VAL C   5           
SHEET    5   I 8 LYS C 165  CYS C 169 -1  N  CYS C 169   O  VAL C 177           
SHEET    6   I 8 PHE C 358  ASP C 363 -1  O  LEU C 360   N  LEU C 168           
SHEET    7   I 8 ARG C 368  ARG C 373 -1  O  GLY C 370   N  ASP C 361           
SHEET    8   I 8 ASP C 195  PRO C 198 -1  N  THR C 197   O  LEU C 369           
SHEET    1   J13 THR C  83  ALA C  84  0                                        
SHEET    2   J13 GLY C  97  THR C 109 -1  O  GLY C  97   N  ALA C  84           
SHEET    3   J13 PRO C 114  CYS C 126 -1  O  VAL C 120   N  PHE C 104           
SHEET    4   J13 VAL C  37  SER C  39  1  N  SER C  39   O  ALA C 125           
SHEET    5   J13 SER C 139  GLY C 144 -1  O  VAL C 142   N  TRP C  38           
SHEET    6   J13 ALA C  26  ASP C  31  1  N  VAL C  29   O  ALA C 143           
SHEET    7   J13 TYR C  18  HIS C  23 -1  N  TYR C  18   O  LEU C  30           
SHEET    8   J13 VAL C   5  LYS C  11 -1  N  THR C  10   O  THR C  19           
SHEET    9   J13 PRO C 175  PHE C 180 -1  O  PHE C 180   N  VAL C   5           
SHEET   10   J13 LYS C 165  CYS C 169 -1  N  CYS C 169   O  VAL C 177           
SHEET   11   J13 PHE C 358  ASP C 363 -1  O  LEU C 360   N  LEU C 168           
SHEET   12   J13 ARG C 368  ARG C 373 -1  O  GLY C 370   N  ASP C 361           
SHEET   13   J13 ASP C 195  PRO C 198 -1  N  THR C 197   O  LEU C 369           
SHEET    1   K 5 TYR C 209  ILE C 210  0                                        
SHEET    2   K 5 VAL C 234  LEU C 236 -1  O  VAL C 234   N  ILE C 210           
SHEET    3   K 5 VAL C 348  LEU C 350  1  O  VAL C 348   N  MET C 235           
SHEET    4   K 5 VAL C 243  LEU C 245 -1  N  LEU C 244   O  ILE C 349           
SHEET    5   K 5 PHE C 332  GLU C 334  1  O  VAL C 333   N  VAL C 243           
SHEET    1   L 4 THR C 220  ARG C 221  0                                        
SHEET    2   L 4 ALA C 212  VAL C 217 -1  N  VAL C 217   O  THR C 220           
SHEET    3   L 4 VAL C 302  LEU C 306 -1  O  LEU C 303   N  LYS C 216           
SHEET    4   L 4 SER C 310  MET C 314 -1  O  TRP C 312   N  LEU C 304           
SHEET    1   M 4 ALA C 274  VAL C 275  0                                        
SHEET    2   M 4 CYS C 284  ASP C 286 -1  O  CYS C 284   N  VAL C 275           
SHEET    3   M 4 THR C 327  VAL C 330 -1  O  ALA C 328   N  TYR C 285           
SHEET    4   M 4 MET C 320  LYS C 324 -1  N  LYS C 324   O  THR C 327           
SHEET    1   N 2 ASN C 292  ASN C 293  0                                        
SHEET    2   N 2 GLY C 296  TYR C 297 -1  O  GLY C 296   N  ASN C 293           
SHEET    1   O 8 TYR D   5  THR D  10  0                                        
SHEET    2   O 8 ASN D  35  TRP D  42 -1  O  VAL D  37   N  TRP D   9           
SHEET    3   O 8 ASN D 163  TRP D 185 -1  O  GLN D 167   N  TRP D  42           
SHEET    4   O 8 THR D  50  ARG D  73 -1  N  THR D  67   O  ALA D 170           
SHEET    5   O 8 ILE D  77  TRP D  85 -1  O  VAL D  81   N  LEU D  68           
SHEET    6   O 8 GLY D 120  ARG D 132  1  O  SER D 130   N  VAL D  82           
SHEET    7   O 8 GLY D 103  SER D 117 -1  N  ASP D 106   O  VAL D 131           
SHEET    8   O 8 THR D  93  SER D 100 -1  N  GLY D  96   O  ILE D 107           
SHEET    1   P 5 ILE D  15  ASN D  20  0                                        
SHEET    2   P 5 ASN D  25  SER D  31 -1  O  ASN D  29   N  ASN D  17           
SHEET    3   P 5 ASN D 163  TRP D 185 -1  O  GLY D 178   N  TRP D  30           
SHEET    4   P 5 THR D  50  ARG D  73 -1  N  THR D  67   O  ALA D 170           
SHEET    5   P 5 ASN D 141  THR D 145 -1  O  ALA D 142   N  TYR D  53           
SSBOND   1 CYS A   41    CYS A  126                          1555   1555  2.10  
SSBOND   2 CYS A   57    CYS A   82                          1555   1555  2.08  
SSBOND   3 CYS A   68    CYS A   94                          1555   1555  2.06  
SSBOND   4 CYS A  169    CYS A  380                          1555   1555  2.02  
SSBOND   5 CYS A  284    CYS A  329                          1555   1555  2.07  
SSBOND   6 CYS C   41    CYS C  126                          1555   1555  2.03  
SSBOND   7 CYS C   57    CYS C   82                          1555   1555  2.08  
SSBOND   8 CYS C   68    CYS C   94                          1555   1555  2.04  
SSBOND   9 CYS C  169    CYS C  380                          1555   1555  1.99  
SSBOND  10 CYS C  284    CYS C  329                          1555   1555  2.06  
CISPEP   1 ALA A  279    PRO A  280          0         7.47                     
CISPEP   2 SER B   74    PRO B   75          0        -0.32                     
CISPEP   3 ALA C  279    PRO C  280          0         3.54                     
CISPEP   4 SER D   74    PRO D   75          0        -8.09                     
CRYST1   77.351   60.300  134.187  90.00 101.49  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      0.012928  0.000000  0.002628        0.00000                         
SCALE2      0.000000  0.016584  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007605        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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