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Database: PDB
Entry: 1T6G
LinkDB: 1T6G
Original site: 1T6G 
HEADER    HYDROLASE INHIBITOR                     06-MAY-04   1T6G              
TITLE     CRYSTAL STRUCTURE OF THE TRITICUM AESTIVUM XYLANASE INHIBITOR-I IN    
TITLE    2 COMPLEX WITH ASPERGILLUS NIGER XYLANASE-I                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: XYLANASE INHIBITOR;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.2.1.8;                                                         
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: ENDO-1,4-BETA-XYLANASE I;                                  
COMPND   7 CHAIN: C, D;                                                         
COMPND   8 SYNONYM: XYLANASE I, 1,4-BETA-D-XYLAN XYLANOHYDROLASE I;             
COMPND   9 EC: 3.2.1.8                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: TRITICUM AESTIVUM;                              
SOURCE   3 ORGANISM_COMMON: BREAD WHEAT;                                        
SOURCE   4 ORGANISM_TAXID: 4565;                                                
SOURCE   5 OTHER_DETAILS: PURIFIED FROM WHEAT FLOUR;                            
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: ASPERGILLUS NIGER;                              
SOURCE   8 ORGANISM_TAXID: 5061                                                 
KEYWDS    PROTEIN-PROTEIN COMPLEX, TWO BETA-BARREL DOMAIN STRUCTURE, BETA-JELLY 
KEYWDS   2 ROLL STRUCTURE, HYDROLASE INHIBITOR                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.SANSEN,C.J.DE RANTER,K.GEBRUERS,K.BRIJS,C.M.COURTIN,J.A.DELCOUR,    
AUTHOR   2 A.RABIJNS                                                            
REVDAT   4   13-JUL-11 1T6G    1       VERSN                                    
REVDAT   3   24-FEB-09 1T6G    1       VERSN                                    
REVDAT   2   24-MAY-05 1T6G    3       REMARK ATOM                              
REVDAT   1   28-SEP-04 1T6G    0                                                
JRNL        AUTH   S.SANSEN,C.J.DE RANTER,K.GEBRUERS,K.BRIJS,C.M.COURTIN,       
JRNL        AUTH 2 J.A.DELCOUR,A.RABIJNS                                        
JRNL        TITL   STRUCTURAL BASIS FOR INHIBITION OF ASPERGILLUS NIGER         
JRNL        TITL 2 XYLANASE BY TRITICUM AESTIVUM XYLANASE INHIBITOR-I           
JRNL        REF    J.BIOL.CHEM.                  V. 279 36022 2004              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   15166216                                                     
JRNL        DOI    10.1074/JBC.M404212200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.74                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 94039                          
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) : 0.162                           
REMARK   3   R VALUE            (WORKING SET) : 0.158                           
REMARK   3   FREE R VALUE                     : 0.192                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 10511                           
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6936                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1560                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 772                          
REMARK   3   BIN FREE R VALUE                    : 0.2120                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8044                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 24                                      
REMARK   3   SOLVENT ATOMS            : 1074                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.58                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.11000                                              
REMARK   3    B22 (A**2) : 0.11000                                              
REMARK   3    B33 (A**2) : -0.16000                                             
REMARK   3    B12 (A**2) : 0.05000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.118         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.111         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.065         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.020         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.941                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8286 ; 0.010 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  7254 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11340 ; 1.364 ; 1.954       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 16888 ; 0.780 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1092 ; 6.890 ; 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):  1270 ; 0.082 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9446 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1664 ; 0.004 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1450 ; 0.199 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  8385 ; 0.253 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  4786 ; 0.083 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   811 ; 0.140 ; 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):    31 ; 0.346 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    92 ; 0.227 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    57 ; 0.339 ; 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):  5450 ; 0.639 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8734 ; 1.177 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2836 ; 1.827 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2606 ; 2.891 ; 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 : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   381                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.1056  11.3897   0.3859              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0156 T22:   0.0032                                     
REMARK   3      T33:   0.0106 T12:   0.0045                                     
REMARK   3      T13:  -0.0048 T23:   0.0007                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0930 L22:   0.2352                                     
REMARK   3      L33:   0.1253 L12:  -0.0331                                     
REMARK   3      L13:   0.0062 L23:  -0.0244                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0092 S12:   0.0029 S13:   0.0179                       
REMARK   3      S21:   0.0146 S22:   0.0089 S23:   0.0111                       
REMARK   3      S31:  -0.0264 S32:   0.0026 S33:   0.0003                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   381                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.1062 -62.4465  15.6373              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0146 T22:   0.0038                                     
REMARK   3      T33:   0.0104 T12:  -0.0042                                     
REMARK   3      T13:   0.0041 T23:   0.0005                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0932 L22:   0.2368                                     
REMARK   3      L33:   0.1303 L12:   0.0333                                     
REMARK   3      L13:  -0.0015 L23:  -0.0239                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0076 S12:  -0.0044 S13:  -0.0174                       
REMARK   3      S21:  -0.0151 S22:   0.0093 S23:   0.0118                       
REMARK   3      S31:   0.0266 S32:   0.0016 S33:  -0.0017                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     2        C   183                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.6998 -15.6066 -14.0369              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0061 T22:   0.0167                                     
REMARK   3      T33:   0.0084 T12:  -0.0018                                     
REMARK   3      T13:  -0.0058 T23:  -0.0029                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2051 L22:   0.1401                                     
REMARK   3      L33:   0.1573 L12:   0.0464                                     
REMARK   3      L13:   0.0680 L23:   0.0686                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0117 S12:  -0.0119 S13:   0.0095                       
REMARK   3      S21:  -0.0020 S22:  -0.0132 S23:   0.0189                       
REMARK   3      S31:   0.0014 S32:  -0.0197 S33:   0.0249                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     2        D   183                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.7025 -35.4395  30.0560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0060 T22:   0.0175                                     
REMARK   3      T33:   0.0086 T12:   0.0012                                     
REMARK   3      T13:   0.0067 T23:  -0.0028                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2026 L22:   0.1370                                     
REMARK   3      L33:   0.1473 L12:  -0.0522                                     
REMARK   3      L13:  -0.0562 L23:   0.0753                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0091 S12:   0.0123 S13:  -0.0104                       
REMARK   3      S21:   0.0008 S22:  -0.0141 S23:   0.0174                       
REMARK   3      S31:  -0.0028 S32:  -0.0185 S33:   0.0232                       
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 1T6G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUN-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB022371.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-NOV-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934                              
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSING GE(220)         
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 93187                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.740                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.1                               
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) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
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: AMORE                                                 
REMARK 200 STARTING MODEL: 1T6E, 1UKR                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.93                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.25 M MAGNESIUM ACETATE  0.1 M SODIUM   
REMARK 280  CACODYLATE BUFFER, 17% PEG8000, PH 6.5, VAPOR DIFFUSION, HANGING    
REMARK 280  DROP, TEMPERATURE 277K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       85.99667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       42.99833            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2370 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21260 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2320 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21330 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6750 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 40530 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000       44.21700            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000      -76.58609            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000      -42.99833            
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     PRO A    69                                                      
REMARK 465     SER A    70                                                      
REMARK 465     CYS A    71                                                      
REMARK 465     GLY A    72                                                      
REMARK 465     SER A    73                                                      
REMARK 465     ASP A    74                                                      
REMARK 465     LYS A    75                                                      
REMARK 465     HIS A    76                                                      
REMARK 465     ASP A    77                                                      
REMARK 465     LYS A    78                                                      
REMARK 465     HIS A   263                                                      
REMARK 465     ALA A   264                                                      
REMARK 465     ASN A   265                                                      
REMARK 465     PRO B    69                                                      
REMARK 465     SER B    70                                                      
REMARK 465     CYS B    71                                                      
REMARK 465     GLY B    72                                                      
REMARK 465     SER B    73                                                      
REMARK 465     ASP B    74                                                      
REMARK 465     LYS B    75                                                      
REMARK 465     HIS B    76                                                      
REMARK 465     ASP B    77                                                      
REMARK 465     LYS B    78                                                      
REMARK 465     HIS B   263                                                      
REMARK 465     ALA B   264                                                      
REMARK 465     ASN B   265                                                      
REMARK 465     SER C     1                                                      
REMARK 465     SER C   184                                                      
REMARK 465     SER D     1                                                      
REMARK 465     SER D   184                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O1   GOL C  2158     O    HOH A  1090     2544     1.01            
REMARK 500   O    HOH B  1161     O1   GOL D  2159     2544     1.04            
REMARK 500   O    HOH B  1161     C1   GOL D  2159     2544     2.11            
REMARK 500   C1   GOL C  2158     O    HOH A  1090     2544     2.13            
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  22   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP A  40   CB  -  CG  -  OD2 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    ARG A 163   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ARG A 163   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG A 211   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ASP B  22   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP C 113   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 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  40     -156.94   -132.74                                   
REMARK 500    PRO A  67      -79.67    -80.38                                   
REMARK 500    ALA A 104     -154.48   -151.83                                   
REMARK 500    SER A 132       -3.24     79.29                                   
REMARK 500    ALA A 329       32.34    -87.14                                   
REMARK 500    ASP B  40     -154.70   -133.80                                   
REMARK 500    GLU B  47       71.31    -65.20                                   
REMARK 500    ALA B 104     -152.89   -153.51                                   
REMARK 500    VAL B 113      -70.88   -116.10                                   
REMARK 500    SER B 132       -4.28     82.82                                   
REMARK 500    ALA B 329       31.03    -84.95                                   
REMARK 500    ALA C  60       21.59   -140.92                                   
REMARK 500    ASN C 163     -145.30    -98.02                                   
REMARK 500    ASN D 163     -145.61    -98.57                                   
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 GLY A   42     GLN A   43                  149.34                    
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 A1554        DISTANCE =  5.37 ANGSTROMS                       
REMARK 525    HOH A1659        DISTANCE =  7.11 ANGSTROMS                       
REMARK 525    HOH A1703        DISTANCE =  5.77 ANGSTROMS                       
REMARK 525    HOH A1916        DISTANCE =  5.99 ANGSTROMS                       
REMARK 525    HOH A2022        DISTANCE =  6.39 ANGSTROMS                       
REMARK 525    HOH A2028        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH B1555        DISTANCE =  5.28 ANGSTROMS                       
REMARK 525    HOH B1657        DISTANCE =  6.38 ANGSTROMS                       
REMARK 525    HOH B1671        DISTANCE =  7.49 ANGSTROMS                       
REMARK 525    HOH B1955        DISTANCE =  6.04 ANGSTROMS                       
REMARK 525    HOH B1980        DISTANCE =  6.34 ANGSTROMS                       
REMARK 525    HOH C1971        DISTANCE =  5.17 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 2158                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 2159                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 2160                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 2161                
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                                                          
DBREF  1T6G A    1   381  UNP    Q8H0K8   Q8H0K8_WHEAT    22    402             
DBREF  1T6G B    1   381  UNP    Q8H0K8   Q8H0K8_WHEAT    22    402             
DBREF  1T6G C    1   184  UNP    P55329   XYN1_ASPNG      28    211             
DBREF  1T6G D    1   184  UNP    P55329   XYN1_ASPNG      28    211             
SEQADV 1T6G ASN C   50  UNP  P55329    LYS    77 ENGINEERED                     
SEQADV 1T6G ASN D   50  UNP  P55329    LYS    77 ENGINEERED                     
SEQRES   1 A  381  LEU PRO VAL LEU ALA PRO VAL THR LYS ASP PRO ALA THR          
SEQRES   2 A  381  SER LEU TYR THR ILE PRO PHE HIS ASP GLY ALA SER LEU          
SEQRES   3 A  381  VAL LEU ASP VAL ALA GLY PRO LEU VAL TRP SER THR CYS          
SEQRES   4 A  381  ASP GLY GLY GLN PRO PRO ALA GLU ILE PRO CYS SER SER          
SEQRES   5 A  381  PRO THR CYS LEU LEU ALA ASN ALA TYR PRO ALA PRO GLY          
SEQRES   6 A  381  CYS PRO ALA PRO SER CYS GLY SER ASP LYS HIS ASP LYS          
SEQRES   7 A  381  PRO CYS THR ALA TYR PRO TYR ASN PRO VAL SER GLY ALA          
SEQRES   8 A  381  CYS ALA ALA GLY SER LEU SER HIS THR ARG PHE VAL ALA          
SEQRES   9 A  381  ASN THR THR ASP GLY SER LYS PRO VAL SER LYS VAL ASN          
SEQRES  10 A  381  VAL GLY VAL LEU ALA ALA CYS ALA PRO SER LYS LEU LEU          
SEQRES  11 A  381  ALA SER LEU PRO ARG GLY SER THR GLY VAL ALA GLY LEU          
SEQRES  12 A  381  ALA ASN SER GLY LEU ALA LEU PRO ALA GLN VAL ALA SER          
SEQRES  13 A  381  ALA GLN LYS VAL ALA ASN ARG PHE LEU LEU CYS LEU PRO          
SEQRES  14 A  381  THR GLY GLY PRO GLY VAL ALA ILE PHE GLY GLY GLY PRO          
SEQRES  15 A  381  VAL PRO TRP PRO GLN PHE THR GLN SER MET PRO TYR THR          
SEQRES  16 A  381  PRO LEU VAL THR LYS GLY GLY SER PRO ALA HIS TYR ILE          
SEQRES  17 A  381  SER ALA ARG SER ILE VAL VAL GLY ASP THR ARG VAL PRO          
SEQRES  18 A  381  VAL PRO GLU GLY ALA LEU ALA THR GLY GLY VAL MET LEU          
SEQRES  19 A  381  SER THR ARG LEU PRO TYR VAL LEU LEU ARG PRO ASP VAL          
SEQRES  20 A  381  TYR ARG PRO LEU MET ASP ALA PHE THR LYS ALA LEU ALA          
SEQRES  21 A  381  ALA GLN HIS ALA ASN GLY ALA PRO VAL ALA ARG ALA VAL          
SEQRES  22 A  381  GLU ALA VAL ALA PRO PHE GLY VAL CYS TYR ASP THR LYS          
SEQRES  23 A  381  THR LEU GLY ASN ASN LEU GLY GLY TYR ALA VAL PRO ASN          
SEQRES  24 A  381  VAL GLN LEU GLY LEU ASP GLY GLY SER ASP TRP THR MET          
SEQRES  25 A  381  THR GLY LYS ASN SER MET VAL ASP VAL LYS GLN GLY THR          
SEQRES  26 A  381  ALA CYS VAL ALA PHE VAL GLU MET LYS GLY VAL ALA ALA          
SEQRES  27 A  381  GLY ASP GLY ARG ALA PRO ALA VAL ILE LEU GLY GLY ALA          
SEQRES  28 A  381  GLN MET GLU ASP PHE VAL LEU ASP PHE ASP MET GLU LYS          
SEQRES  29 A  381  LYS ARG LEU GLY PHE SER ARG LEU PRO HIS PHE THR GLY          
SEQRES  30 A  381  CYS GLY GLY LEU                                              
SEQRES   1 B  381  LEU PRO VAL LEU ALA PRO VAL THR LYS ASP PRO ALA THR          
SEQRES   2 B  381  SER LEU TYR THR ILE PRO PHE HIS ASP GLY ALA SER LEU          
SEQRES   3 B  381  VAL LEU ASP VAL ALA GLY PRO LEU VAL TRP SER THR CYS          
SEQRES   4 B  381  ASP GLY GLY GLN PRO PRO ALA GLU ILE PRO CYS SER SER          
SEQRES   5 B  381  PRO THR CYS LEU LEU ALA ASN ALA TYR PRO ALA PRO GLY          
SEQRES   6 B  381  CYS PRO ALA PRO SER CYS GLY SER ASP LYS HIS ASP LYS          
SEQRES   7 B  381  PRO CYS THR ALA TYR PRO TYR ASN PRO VAL SER GLY ALA          
SEQRES   8 B  381  CYS ALA ALA GLY SER LEU SER HIS THR ARG PHE VAL ALA          
SEQRES   9 B  381  ASN THR THR ASP GLY SER LYS PRO VAL SER LYS VAL ASN          
SEQRES  10 B  381  VAL GLY VAL LEU ALA ALA CYS ALA PRO SER LYS LEU LEU          
SEQRES  11 B  381  ALA SER LEU PRO ARG GLY SER THR GLY VAL ALA GLY LEU          
SEQRES  12 B  381  ALA ASN SER GLY LEU ALA LEU PRO ALA GLN VAL ALA SER          
SEQRES  13 B  381  ALA GLN LYS VAL ALA ASN ARG PHE LEU LEU CYS LEU PRO          
SEQRES  14 B  381  THR GLY GLY PRO GLY VAL ALA ILE PHE GLY GLY GLY PRO          
SEQRES  15 B  381  VAL PRO TRP PRO GLN PHE THR GLN SER MET PRO TYR THR          
SEQRES  16 B  381  PRO LEU VAL THR LYS GLY GLY SER PRO ALA HIS TYR ILE          
SEQRES  17 B  381  SER ALA ARG SER ILE VAL VAL GLY ASP THR ARG VAL PRO          
SEQRES  18 B  381  VAL PRO GLU GLY ALA LEU ALA THR GLY GLY VAL MET LEU          
SEQRES  19 B  381  SER THR ARG LEU PRO TYR VAL LEU LEU ARG PRO ASP VAL          
SEQRES  20 B  381  TYR ARG PRO LEU MET ASP ALA PHE THR LYS ALA LEU ALA          
SEQRES  21 B  381  ALA GLN HIS ALA ASN GLY ALA PRO VAL ALA ARG ALA VAL          
SEQRES  22 B  381  GLU ALA VAL ALA PRO PHE GLY VAL CYS TYR ASP THR LYS          
SEQRES  23 B  381  THR LEU GLY ASN ASN LEU GLY GLY TYR ALA VAL PRO ASN          
SEQRES  24 B  381  VAL GLN LEU GLY LEU ASP GLY GLY SER ASP TRP THR MET          
SEQRES  25 B  381  THR GLY LYS ASN SER MET VAL ASP VAL LYS GLN GLY THR          
SEQRES  26 B  381  ALA CYS VAL ALA PHE VAL GLU MET LYS GLY VAL ALA ALA          
SEQRES  27 B  381  GLY ASP GLY ARG ALA PRO ALA VAL ILE LEU GLY GLY ALA          
SEQRES  28 B  381  GLN MET GLU ASP PHE VAL LEU ASP PHE ASP MET GLU LYS          
SEQRES  29 B  381  LYS ARG LEU GLY PHE SER ARG LEU PRO HIS PHE THR GLY          
SEQRES  30 B  381  CYS GLY GLY LEU                                              
SEQRES   1 C  184  SER ALA GLY ILE ASN TYR VAL GLN ASN TYR ASN GLY ASN          
SEQRES   2 C  184  LEU GLY ASP PHE THR TYR ASP GLU SER ALA GLY THR PHE          
SEQRES   3 C  184  SER MET TYR TRP GLU ASP GLY VAL SER SER ASP PHE VAL          
SEQRES   4 C  184  VAL GLY LEU GLY TRP THR THR GLY SER SER ASN ALA ILE          
SEQRES   5 C  184  THR TYR SER ALA GLU TYR SER ALA SER GLY SER SER SER          
SEQRES   6 C  184  TYR LEU ALA VAL TYR GLY TRP VAL ASN TYR PRO GLN ALA          
SEQRES   7 C  184  GLU TYR TYR ILE VAL GLU ASP TYR GLY ASP TYR ASN PRO          
SEQRES   8 C  184  CYS SER SER ALA THR SER LEU GLY THR VAL TYR SER ASP          
SEQRES   9 C  184  GLY SER THR TYR GLN VAL CYS THR ASP THR ARG THR ASN          
SEQRES  10 C  184  GLU PRO SER ILE THR GLY THR SER THR PHE THR GLN TYR          
SEQRES  11 C  184  PHE SER VAL ARG GLU SER THR ARG THR SER GLY THR VAL          
SEQRES  12 C  184  THR VAL ALA ASN HIS PHE ASN PHE TRP ALA GLN HIS GLY          
SEQRES  13 C  184  PHE GLY ASN SER ASP PHE ASN TYR GLN VAL MET ALA VAL          
SEQRES  14 C  184  GLU ALA TRP SER GLY ALA GLY SER ALA SER VAL THR ILE          
SEQRES  15 C  184  SER SER                                                      
SEQRES   1 D  184  SER ALA GLY ILE ASN TYR VAL GLN ASN TYR ASN GLY ASN          
SEQRES   2 D  184  LEU GLY ASP PHE THR TYR ASP GLU SER ALA GLY THR PHE          
SEQRES   3 D  184  SER MET TYR TRP GLU ASP GLY VAL SER SER ASP PHE VAL          
SEQRES   4 D  184  VAL GLY LEU GLY TRP THR THR GLY SER SER ASN ALA ILE          
SEQRES   5 D  184  THR TYR SER ALA GLU TYR SER ALA SER GLY SER SER SER          
SEQRES   6 D  184  TYR LEU ALA VAL TYR GLY TRP VAL ASN TYR PRO GLN ALA          
SEQRES   7 D  184  GLU TYR TYR ILE VAL GLU ASP TYR GLY ASP TYR ASN PRO          
SEQRES   8 D  184  CYS SER SER ALA THR SER LEU GLY THR VAL TYR SER ASP          
SEQRES   9 D  184  GLY SER THR TYR GLN VAL CYS THR ASP THR ARG THR ASN          
SEQRES  10 D  184  GLU PRO SER ILE THR GLY THR SER THR PHE THR GLN TYR          
SEQRES  11 D  184  PHE SER VAL ARG GLU SER THR ARG THR SER GLY THR VAL          
SEQRES  12 D  184  THR VAL ALA ASN HIS PHE ASN PHE TRP ALA GLN HIS GLY          
SEQRES  13 D  184  PHE GLY ASN SER ASP PHE ASN TYR GLN VAL MET ALA VAL          
SEQRES  14 D  184  GLU ALA TRP SER GLY ALA GLY SER ALA SER VAL THR ILE          
SEQRES  15 D  184  SER SER                                                      
HET    GOL  C2158       6                                                       
HET    GOL  D2159       6                                                       
HET    GOL  C2160       6                                                       
HET    GOL  D2161       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  GOL    4(C3 H8 O3)                                                  
FORMUL   9  HOH   *1074(H2 O)                                                   
HELIX    1   1 SER A   52  ASN A   59  1                                   8    
HELIX    2   2 PRO A  126  ALA A  131  5                                   6    
HELIX    3   3 ALA A  149  LYS A  159  1                                  11    
HELIX    4   4 TRP A  185  GLN A  190  1                                   6    
HELIX    5   5 ARG A  244  ALA A  261  1                                  18    
HELIX    6   6 LYS A  286  LEU A  288  5                                   3    
HELIX    7   7 THR A  313  SER A  317  1                                   5    
HELIX    8   8 GLY A  349  GLU A  354  1                                   6    
HELIX    9   9 SER B   52  ASN B   59  1                                   8    
HELIX   10  10 PRO B  126  ALA B  131  5                                   6    
HELIX   11  11 ALA B  149  LYS B  159  1                                  11    
HELIX   12  12 TRP B  185  GLN B  190  1                                   6    
HELIX   13  13 ARG B  244  ALA B  261  1                                  18    
HELIX   14  14 LYS B  286  LEU B  288  5                                   3    
HELIX   15  15 THR B  313  SER B  317  1                                   5    
HELIX   16  16 GLY B  349  GLU B  354  1                                   6    
HELIX   17  17 ASN C   11  GLY C   15  5                                   5    
HELIX   18  18 THR C  144  ALA C  153  1                                  10    
HELIX   19  19 GLN C  154  GLY C  156  5                                   3    
HELIX   20  20 ASN D   11  GLY D   15  5                                   5    
HELIX   21  21 THR D  144  ALA D  153  1                                  10    
HELIX   22  22 GLN D  154  GLY D  156  5                                   3    
SHEET    1   A13 TYR A 194  PRO A 196  0                                        
SHEET    2   A13 ARG A 366  ARG A 371 -1  O  LEU A 367   N  THR A 195           
SHEET    3   A13 PHE A 356  ASP A 361 -1  N  VAL A 357   O  SER A 370           
SHEET    4   A13 ARG A 163  CYS A 167 -1  N  PHE A 164   O  PHE A 360           
SHEET    5   A13 GLY A 174  PHE A 178 -1  O  VAL A 175   N  CYS A 167           
SHEET    6   A13 VAL A   3  LYS A   9 -1  N  VAL A   7   O  GLY A 174           
SHEET    7   A13 SER A  96  THR A 107 -1  O  ASN A 105   N  LEU A   4           
SHEET    8   A13 PRO A 112  CYS A 124 -1  O  VAL A 118   N  PHE A 102           
SHEET    9   A13 VAL A  35  SER A  37  1  N  VAL A  35   O  ALA A 123           
SHEET   10   A13 SER A 137  GLY A 142 -1  O  VAL A 140   N  TRP A  36           
SHEET   11   A13 ALA A  24  ASP A  29  1  N  VAL A  27   O  ALA A 141           
SHEET   12   A13 TYR A  16  HIS A  21 -1  N  PHE A  20   O  ALA A  24           
SHEET   13   A13 VAL A   3  LYS A   9 -1  N  THR A   8   O  THR A  17           
SHEET    1   B 5 TYR A 207  ILE A 208  0                                        
SHEET    2   B 5 VAL A 232  LEU A 234 -1  O  VAL A 232   N  ILE A 208           
SHEET    3   B 5 VAL A 346  LEU A 348  1  O  VAL A 346   N  MET A 233           
SHEET    4   B 5 VAL A 241  LEU A 243 -1  N  LEU A 242   O  ILE A 347           
SHEET    5   B 5 PHE A 330  GLU A 332  1  O  VAL A 331   N  VAL A 241           
SHEET    1   C 4 THR A 218  ARG A 219  0                                        
SHEET    2   C 4 ALA A 210  VAL A 215 -1  N  VAL A 215   O  THR A 218           
SHEET    3   C 4 VAL A 300  LEU A 304 -1  O  GLY A 303   N  ARG A 211           
SHEET    4   C 4 ASP A 309  MET A 312 -1  O  MET A 312   N  VAL A 300           
SHEET    1   D 4 ALA A 272  VAL A 273  0                                        
SHEET    2   D 4 CYS A 282  ASP A 284 -1  O  CYS A 282   N  VAL A 273           
SHEET    3   D 4 THR A 325  VAL A 328 -1  O  ALA A 326   N  TYR A 283           
SHEET    4   D 4 MET A 318  LYS A 322 -1  N  VAL A 319   O  CYS A 327           
SHEET    1   E 2 ASN A 290  ASN A 291  0                                        
SHEET    2   E 2 GLY A 294  TYR A 295 -1  O  GLY A 294   N  ASN A 291           
SHEET    1   F 8 THR B  81  ALA B  82  0                                        
SHEET    2   F 8 GLY B  95  THR B 107 -1  O  GLY B  95   N  ALA B  82           
SHEET    3   F 8 VAL B   3  LYS B   9 -1  N  LEU B   4   O  ASN B 105           
SHEET    4   F 8 GLY B 174  PHE B 178 -1  O  GLY B 174   N  VAL B   7           
SHEET    5   F 8 ARG B 163  CYS B 167 -1  N  CYS B 167   O  VAL B 175           
SHEET    6   F 8 PHE B 356  ASP B 361 -1  O  LEU B 358   N  LEU B 166           
SHEET    7   F 8 ARG B 366  ARG B 371 -1  O  SER B 370   N  VAL B 357           
SHEET    8   F 8 TYR B 194  PRO B 196 -1  N  THR B 195   O  LEU B 367           
SHEET    1   G13 THR B  81  ALA B  82  0                                        
SHEET    2   G13 GLY B  95  THR B 107 -1  O  GLY B  95   N  ALA B  82           
SHEET    3   G13 PRO B 112  CYS B 124 -1  O  VAL B 118   N  PHE B 102           
SHEET    4   G13 VAL B  35  SER B  37  1  N  VAL B  35   O  ALA B 123           
SHEET    5   G13 SER B 137  GLY B 142 -1  O  VAL B 140   N  TRP B  36           
SHEET    6   G13 ALA B  24  ASP B  29  1  N  VAL B  27   O  ALA B 141           
SHEET    7   G13 TYR B  16  HIS B  21 -1  N  PHE B  20   O  ALA B  24           
SHEET    8   G13 VAL B   3  LYS B   9 -1  N  THR B   8   O  THR B  17           
SHEET    9   G13 GLY B 174  PHE B 178 -1  O  GLY B 174   N  VAL B   7           
SHEET   10   G13 ARG B 163  CYS B 167 -1  N  CYS B 167   O  VAL B 175           
SHEET   11   G13 PHE B 356  ASP B 361 -1  O  LEU B 358   N  LEU B 166           
SHEET   12   G13 ARG B 366  ARG B 371 -1  O  SER B 370   N  VAL B 357           
SHEET   13   G13 TYR B 194  PRO B 196 -1  N  THR B 195   O  LEU B 367           
SHEET    1   H 5 TYR B 207  ILE B 208  0                                        
SHEET    2   H 5 VAL B 232  LEU B 234 -1  O  VAL B 232   N  ILE B 208           
SHEET    3   H 5 VAL B 346  LEU B 348  1  O  VAL B 346   N  MET B 233           
SHEET    4   H 5 VAL B 241  LEU B 243 -1  N  LEU B 242   O  ILE B 347           
SHEET    5   H 5 PHE B 330  GLU B 332  1  O  VAL B 331   N  VAL B 241           
SHEET    1   I 4 THR B 218  ARG B 219  0                                        
SHEET    2   I 4 ALA B 210  VAL B 215 -1  N  VAL B 215   O  THR B 218           
SHEET    3   I 4 VAL B 300  LEU B 304 -1  O  GLY B 303   N  ARG B 211           
SHEET    4   I 4 ASP B 309  MET B 312 -1  O  MET B 312   N  VAL B 300           
SHEET    1   J 4 ALA B 272  VAL B 273  0                                        
SHEET    2   J 4 CYS B 282  ASP B 284 -1  O  CYS B 282   N  VAL B 273           
SHEET    3   J 4 THR B 325  VAL B 328 -1  O  ALA B 326   N  TYR B 283           
SHEET    4   J 4 MET B 318  LYS B 322 -1  N  VAL B 319   O  CYS B 327           
SHEET    1   K 2 ASN B 290  ASN B 291  0                                        
SHEET    2   K 2 GLY B 294  TYR B 295 -1  O  GLY B 294   N  ASN B 291           
SHEET    1   L 8 TYR C   6  TYR C  10  0                                        
SHEET    2   L 8 PHE C  38  TRP C  44 -1  O  VAL C  39   N  TYR C  10           
SHEET    3   L 8 PHE C 162  ILE C 182 -1  O  GLN C 165   N  TRP C  44           
SHEET    4   L 8 SER C  63  VAL C  73 -1  N  TYR C  70   O  VAL C 166           
SHEET    5   L 8 ALA C  78  TYR C  86 -1  O  TYR C  80   N  GLY C  71           
SHEET    6   L 8 SER C 125  ARG C 134  1  O  SER C 132   N  VAL C  83           
SHEET    7   L 8 SER C 106  GLU C 118 -1  N  ARG C 115   O  PHE C 127           
SHEET    8   L 8 THR C  96  SER C 103 -1  N  LEU C  98   O  VAL C 110           
SHEET    1   M 5 ASP C  16  ASP C  20  0                                        
SHEET    2   M 5 THR C  25  VAL C  34 -1  O  THR C  25   N  ASP C  20           
SHEET    3   M 5 PHE C 162  ILE C 182 -1  O  VAL C 180   N  PHE C  26           
SHEET    4   M 5 ILE C  52  SER C  59 -1  N  SER C  55   O  THR C 181           
SHEET    5   M 5 SER C 140  VAL C 143 -1  O  VAL C 143   N  ILE C  52           
SHEET    1   N 8 TYR D   6  TYR D  10  0                                        
SHEET    2   N 8 PHE D  38  TRP D  44 -1  O  VAL D  39   N  TYR D  10           
SHEET    3   N 8 PHE D 162  GLY D 174 -1  O  GLN D 165   N  TRP D  44           
SHEET    4   N 8 SER D  63  VAL D  73 -1  N  ALA D  68   O  ALA D 168           
SHEET    5   N 8 ALA D  78  TYR D  86 -1  O  TYR D  80   N  GLY D  71           
SHEET    6   N 8 SER D 125  ARG D 134  1  O  SER D 132   N  VAL D  83           
SHEET    7   N 8 SER D 106  GLU D 118 -1  N  ARG D 115   O  PHE D 127           
SHEET    8   N 8 THR D  96  SER D 103 -1  N  LEU D  98   O  VAL D 110           
SHEET    1   O 5 ASP D  16  ASP D  20  0                                        
SHEET    2   O 5 THR D  25  TYR D  29 -1  O  THR D  25   N  ASP D  20           
SHEET    3   O 5 SER D 177  ILE D 182 -1  O  VAL D 180   N  PHE D  26           
SHEET    4   O 5 ILE D  52  SER D  59 -1  N  SER D  55   O  THR D 181           
SHEET    5   O 5 SER D 140  VAL D 143 -1  O  VAL D 143   N  ILE D  52           
SSBOND   1 CYS A   39    CYS A  124                          1555   1555  2.02  
SSBOND   2 CYS A   55    CYS A   80                          1555   1555  2.05  
SSBOND   3 CYS A   66    CYS A   92                          1555   1555  2.04  
SSBOND   4 CYS A  167    CYS A  378                          1555   1555  2.04  
SSBOND   5 CYS A  282    CYS A  327                          1555   1555  2.10  
SSBOND   6 CYS B   39    CYS B  124                          1555   1555  2.02  
SSBOND   7 CYS B   55    CYS B   80                          1555   1555  2.04  
SSBOND   8 CYS B   66    CYS B   92                          1555   1555  2.04  
SSBOND   9 CYS B  167    CYS B  378                          1555   1555  2.03  
SSBOND  10 CYS B  282    CYS B  327                          1555   1555  2.09  
SSBOND  11 CYS C   92    CYS C  111                          1555   1555  2.11  
SSBOND  12 CYS D   92    CYS D  111                          1555   1555  2.10  
CISPEP   1 ALA A  277    PRO A  278          0         6.83                     
CISPEP   2 ALA B  277    PRO B  278          0         6.03                     
CISPEP   3 TYR C   75    PRO C   76          0       -14.65                     
CISPEP   4 TYR D   75    PRO D   76          0       -15.12                     
SITE     1 AC1 11 VAL A 273  GLY A 280  VAL A 281  CYS A 282                    
SITE     2 AC1 11 HOH A1090  HOH A1620  TYR C 102  SER C 103                    
SITE     3 AC1 11 ASP C 104  GLY C 105  HOH C1323                               
SITE     1 AC2 11 VAL B 273  GLY B 280  VAL B 281  CYS B 282                    
SITE     2 AC2 11 HOH B1161  HOH B1756  TYR D 102  SER D 103                    
SITE     3 AC2 11 ASP D 104  GLY D 105  HOH D1386                               
SITE     1 AC3  9 GLY C  15  ASP C  16  TYR C  29  TRP C  30                    
SITE     2 AC3  9 GLU C  31  ASP C  32  HOH C1290  HOH C1646                    
SITE     3 AC3  9 HOH C1883                                                     
SITE     1 AC4  9 GLY D  15  ASP D  16  TYR D  29  TRP D  30                    
SITE     2 AC4  9 GLU D  31  ASP D  32  HOH D1281  HOH D1687                    
SITE     3 AC4  9 HOH D1726                                                     
CRYST1   88.434   88.434  128.995  90.00  90.00 120.00 P 32          6          
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      0.011308  0.006529  0.000000        0.00000                         
SCALE2      0.000000  0.013057  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007752        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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