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Database: PDB
Entry: 3RPN
LinkDB: 3RPN
Original site: 3RPN 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       27-APR-11   3RPN              
TITLE     CRYSTAL STRUCTURE OF HUMAN KAPPA CLASS GLUTATHIONE TRANSFERASE IN     
TITLE    2 COMPLEX WITH S-HEXYLGLUTATHIONE                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTATHIONE S-TRANSFERASE KAPPA 1;                         
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 SYNONYM: GST 13-13, GST CLASS-KAPPA, GSTK1-1, HGSTK1, GLUTATHIONE S- 
COMPND   5 TRANSFERASE SUBUNIT 13;                                              
COMPND   6 EC: 2.5.1.18;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GSTK1, HDCMD47P;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET22B                                    
KEYWDS    KAPPA GST, TRX DOMAIN, GSH BINDING, DETOXIFICATION, GTX, GLUTATHIONE  
KEYWDS   2 TRANSFERASE INHIBITOR COMPLEX, TRANSFERASE-TRANSFERASE INHIBITOR     
KEYWDS   3 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.WANG,Y.PENG,T.ZHANG,J.DING                                          
REVDAT   4   08-NOV-17 3RPN    1       REMARK                                   
REVDAT   3   03-JUL-13 3RPN    1       JRNL                                     
REVDAT   2   10-AUG-11 3RPN    1       KEYWDS                                   
REVDAT   1   13-JUL-11 3RPN    0                                                
JRNL        AUTH   B.WANG,Y.PENG,T.ZHANG,J.DING                                 
JRNL        TITL   CRYSTAL STRUCTURES AND KINETIC STUDIES OF HUMAN KAPPA CLASS  
JRNL        TITL 2 GLUTATHIONE TRANSFERASE PROVIDE INSIGHTS INTO THE CATALYTIC  
JRNL        TITL 3 MECHANISM.                                                   
JRNL        REF    BIOCHEM.J.                    V. 439   215 2011              
JRNL        REFN                   ISSN 0264-6021                               
JRNL        PMID   21728995                                                     
JRNL        DOI    10.1042/BJ20110753                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.6.4_486                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.95                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.550                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 116630                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.185                           
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5841                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 29.9546 -  4.0904    0.81     9390   536  0.1906 0.2060        
REMARK   3     2  4.0904 -  3.2479    0.85     9928   515  0.1728 0.2108        
REMARK   3     3  3.2479 -  2.8377    0.96    11182   575  0.1828 0.2082        
REMARK   3     4  2.8377 -  2.5784    0.99    11445   619  0.1852 0.2240        
REMARK   3     5  2.5784 -  2.3937    0.99    11501   613  0.1687 0.2218        
REMARK   3     6  2.3937 -  2.2526    0.99    11553   588  0.1684 0.2105        
REMARK   3     7  2.2526 -  2.1398    1.00    11474   607  0.1806 0.2310        
REMARK   3     8  2.1398 -  2.0467    0.99    11587   616  0.1939 0.2425        
REMARK   3     9  2.0467 -  1.9679    1.00    11512   590  0.1949 0.2455        
REMARK   3    10  1.9679 -  1.9000    0.97    11217   582  0.2186 0.2655        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.40                                          
REMARK   3   SHRINKAGE RADIUS   : 1.17                                          
REMARK   3   K_SOL              : 0.36                                          
REMARK   3   B_SOL              : 60.76                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.200            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.570           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.84390                                             
REMARK   3    B22 (A**2) : 1.00660                                              
REMARK   3    B33 (A**2) : 0.83740                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.43850                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007          10872                                  
REMARK   3   ANGLE     :  0.989          14706                                  
REMARK   3   CHIRALITY :  0.067           1596                                  
REMARK   3   PLANARITY :  0.004           1878                                  
REMARK   3   DIHEDRAL  : 13.720           4158                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):   5.9704 -33.6106  24.7373              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1199 T22:   0.0998                                     
REMARK   3      T33:   0.1025 T12:   0.0229                                     
REMARK   3      T13:  -0.0242 T23:  -0.0075                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0475 L22:   1.0038                                     
REMARK   3      L33:   0.2013 L12:   0.0053                                     
REMARK   3      L13:  -0.0303 L23:  -0.3327                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0019 S12:   0.0005 S13:  -0.0026                       
REMARK   3      S21:  -0.1607 S22:   0.0214 S23:   0.1411                       
REMARK   3      S31:   0.0741 S32:   0.0078 S33:  -0.0227                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3RPN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-MAY-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000065222.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-JUL-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 122112                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 73.3                               
REMARK 200  DATA REDUNDANCY                : 2.700                              
REMARK 200  R MERGE                    (I) : 0.04600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.6000                            
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) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 67.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.27900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.27900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1YZX                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% POLYETHYLENE GLYCOL 3350, 0.2M       
REMARK 280  NASCN, PH 7.0, HANGING DROP, TEMPERATURE 293K                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       99.91050            
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, 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: 4810 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 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: 4840 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18820 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E                                  
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4750 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F                                  
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     MET A     1                                                      
REMARK 465     VAL A   222                                                      
REMARK 465     ASN A   223                                                      
REMARK 465     ALA A   224                                                      
REMARK 465     ARG A   225                                                      
REMARK 465     LEU A   226                                                      
REMARK 465     LEU A   227                                                      
REMARK 465     GLU A   228                                                      
REMARK 465     HIS A   229                                                      
REMARK 465     HIS A   230                                                      
REMARK 465     HIS A   231                                                      
REMARK 465     HIS A   232                                                      
REMARK 465     HIS A   233                                                      
REMARK 465     HIS A   234                                                      
REMARK 465     MET B     1                                                      
REMARK 465     VAL B   222                                                      
REMARK 465     ASN B   223                                                      
REMARK 465     ALA B   224                                                      
REMARK 465     ARG B   225                                                      
REMARK 465     LEU B   226                                                      
REMARK 465     LEU B   227                                                      
REMARK 465     GLU B   228                                                      
REMARK 465     HIS B   229                                                      
REMARK 465     HIS B   230                                                      
REMARK 465     HIS B   231                                                      
REMARK 465     HIS B   232                                                      
REMARK 465     HIS B   233                                                      
REMARK 465     HIS B   234                                                      
REMARK 465     MET C     1                                                      
REMARK 465     VAL C   222                                                      
REMARK 465     ASN C   223                                                      
REMARK 465     ALA C   224                                                      
REMARK 465     ARG C   225                                                      
REMARK 465     LEU C   226                                                      
REMARK 465     LEU C   227                                                      
REMARK 465     GLU C   228                                                      
REMARK 465     HIS C   229                                                      
REMARK 465     HIS C   230                                                      
REMARK 465     HIS C   231                                                      
REMARK 465     HIS C   232                                                      
REMARK 465     HIS C   233                                                      
REMARK 465     HIS C   234                                                      
REMARK 465     MET D     1                                                      
REMARK 465     VAL D   222                                                      
REMARK 465     ASN D   223                                                      
REMARK 465     ALA D   224                                                      
REMARK 465     ARG D   225                                                      
REMARK 465     LEU D   226                                                      
REMARK 465     LEU D   227                                                      
REMARK 465     GLU D   228                                                      
REMARK 465     HIS D   229                                                      
REMARK 465     HIS D   230                                                      
REMARK 465     HIS D   231                                                      
REMARK 465     HIS D   232                                                      
REMARK 465     HIS D   233                                                      
REMARK 465     HIS D   234                                                      
REMARK 465     MET E     1                                                      
REMARK 465     VAL E   222                                                      
REMARK 465     ASN E   223                                                      
REMARK 465     ALA E   224                                                      
REMARK 465     ARG E   225                                                      
REMARK 465     LEU E   226                                                      
REMARK 465     LEU E   227                                                      
REMARK 465     GLU E   228                                                      
REMARK 465     HIS E   229                                                      
REMARK 465     HIS E   230                                                      
REMARK 465     HIS E   231                                                      
REMARK 465     HIS E   232                                                      
REMARK 465     HIS E   233                                                      
REMARK 465     HIS E   234                                                      
REMARK 465     MET F     1                                                      
REMARK 465     VAL F   222                                                      
REMARK 465     ASN F   223                                                      
REMARK 465     ALA F   224                                                      
REMARK 465     ARG F   225                                                      
REMARK 465     LEU F   226                                                      
REMARK 465     LEU F   227                                                      
REMARK 465     GLU F   228                                                      
REMARK 465     HIS F   229                                                      
REMARK 465     HIS F   230                                                      
REMARK 465     HIS F   231                                                      
REMARK 465     HIS F   232                                                      
REMARK 465     HIS F   233                                                      
REMARK 465     HIS F   234                                                      
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    SER A  96       20.30   -143.33                                   
REMARK 500    PRO C  55      109.99    -54.62                                   
REMARK 500    SER C  96       19.14   -141.81                                   
REMARK 500    SER C 127      -54.08   -128.75                                   
REMARK 500    SER D 127      -53.26   -123.86                                   
REMARK 500    SER E  96       17.39   -142.17                                   
REMARK 500    SER E 127      -59.01   -122.14                                   
REMARK 500    SER F  96       24.54   -140.61                                   
REMARK 500    SER F 127      -53.13   -130.34                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTX A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTX B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTX C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTX D 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTX E 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTX F 302                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3RPP   RELATED DB: PDB                                   
DBREF  3RPN A    1   226  UNP    Q9Y2Q3   GSTK1_HUMAN      1    226             
DBREF  3RPN B    1   226  UNP    Q9Y2Q3   GSTK1_HUMAN      1    226             
DBREF  3RPN C    1   226  UNP    Q9Y2Q3   GSTK1_HUMAN      1    226             
DBREF  3RPN D    1   226  UNP    Q9Y2Q3   GSTK1_HUMAN      1    226             
DBREF  3RPN E    1   226  UNP    Q9Y2Q3   GSTK1_HUMAN      1    226             
DBREF  3RPN F    1   226  UNP    Q9Y2Q3   GSTK1_HUMAN      1    226             
SEQADV 3RPN LEU A  227  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN GLU A  228  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS A  229  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS A  230  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS A  231  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS A  232  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS A  233  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS A  234  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN LEU B  227  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN GLU B  228  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS B  229  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS B  230  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS B  231  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS B  232  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS B  233  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS B  234  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN LEU C  227  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN GLU C  228  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS C  229  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS C  230  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS C  231  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS C  232  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS C  233  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS C  234  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN LEU D  227  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN GLU D  228  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS D  229  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS D  230  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS D  231  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS D  232  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS D  233  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS D  234  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN LEU E  227  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN GLU E  228  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS E  229  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS E  230  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS E  231  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS E  232  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS E  233  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS E  234  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN LEU F  227  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN GLU F  228  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS F  229  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS F  230  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS F  231  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS F  232  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS F  233  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQADV 3RPN HIS F  234  UNP  Q9Y2Q3              EXPRESSION TAG                 
SEQRES   1 A  234  MET GLY PRO LEU PRO ARG THR VAL GLU LEU PHE TYR ASP          
SEQRES   2 A  234  VAL LEU SER PRO TYR SER TRP LEU GLY PHE GLU ILE LEU          
SEQRES   3 A  234  CYS ARG TYR GLN ASN ILE TRP ASN ILE ASN LEU GLN LEU          
SEQRES   4 A  234  ARG PRO SER LEU ILE THR GLY ILE MET LYS ASP SER GLY          
SEQRES   5 A  234  ASN LYS PRO PRO GLY LEU LEU PRO ARG LYS GLY LEU TYR          
SEQRES   6 A  234  MET ALA ASN ASP LEU LYS LEU LEU ARG HIS HIS LEU GLN          
SEQRES   7 A  234  ILE PRO ILE HIS PHE PRO LYS ASP PHE LEU SER VAL MET          
SEQRES   8 A  234  LEU GLU LYS GLY SER LEU SER ALA MET ARG PHE LEU THR          
SEQRES   9 A  234  ALA VAL ASN LEU GLU HIS PRO GLU MET LEU GLU LYS ALA          
SEQRES  10 A  234  SER ARG GLU LEU TRP MET ARG VAL TRP SER ARG ASN GLU          
SEQRES  11 A  234  ASP ILE THR GLU PRO GLN SER ILE LEU ALA ALA ALA GLU          
SEQRES  12 A  234  LYS ALA GLY MET SER ALA GLU GLN ALA GLN GLY LEU LEU          
SEQRES  13 A  234  GLU LYS ILE ALA THR PRO LYS VAL LYS ASN GLN LEU LYS          
SEQRES  14 A  234  GLU THR THR GLU ALA ALA CYS ARG TYR GLY ALA PHE GLY          
SEQRES  15 A  234  LEU PRO ILE THR VAL ALA HIS VAL ASP GLY GLN THR HIS          
SEQRES  16 A  234  MET LEU PHE GLY SER ASP ARG MET GLU LEU LEU ALA HIS          
SEQRES  17 A  234  LEU LEU GLY GLU LYS TRP MET GLY PRO ILE PRO PRO ALA          
SEQRES  18 A  234  VAL ASN ALA ARG LEU LEU GLU HIS HIS HIS HIS HIS HIS          
SEQRES   1 B  234  MET GLY PRO LEU PRO ARG THR VAL GLU LEU PHE TYR ASP          
SEQRES   2 B  234  VAL LEU SER PRO TYR SER TRP LEU GLY PHE GLU ILE LEU          
SEQRES   3 B  234  CYS ARG TYR GLN ASN ILE TRP ASN ILE ASN LEU GLN LEU          
SEQRES   4 B  234  ARG PRO SER LEU ILE THR GLY ILE MET LYS ASP SER GLY          
SEQRES   5 B  234  ASN LYS PRO PRO GLY LEU LEU PRO ARG LYS GLY LEU TYR          
SEQRES   6 B  234  MET ALA ASN ASP LEU LYS LEU LEU ARG HIS HIS LEU GLN          
SEQRES   7 B  234  ILE PRO ILE HIS PHE PRO LYS ASP PHE LEU SER VAL MET          
SEQRES   8 B  234  LEU GLU LYS GLY SER LEU SER ALA MET ARG PHE LEU THR          
SEQRES   9 B  234  ALA VAL ASN LEU GLU HIS PRO GLU MET LEU GLU LYS ALA          
SEQRES  10 B  234  SER ARG GLU LEU TRP MET ARG VAL TRP SER ARG ASN GLU          
SEQRES  11 B  234  ASP ILE THR GLU PRO GLN SER ILE LEU ALA ALA ALA GLU          
SEQRES  12 B  234  LYS ALA GLY MET SER ALA GLU GLN ALA GLN GLY LEU LEU          
SEQRES  13 B  234  GLU LYS ILE ALA THR PRO LYS VAL LYS ASN GLN LEU LYS          
SEQRES  14 B  234  GLU THR THR GLU ALA ALA CYS ARG TYR GLY ALA PHE GLY          
SEQRES  15 B  234  LEU PRO ILE THR VAL ALA HIS VAL ASP GLY GLN THR HIS          
SEQRES  16 B  234  MET LEU PHE GLY SER ASP ARG MET GLU LEU LEU ALA HIS          
SEQRES  17 B  234  LEU LEU GLY GLU LYS TRP MET GLY PRO ILE PRO PRO ALA          
SEQRES  18 B  234  VAL ASN ALA ARG LEU LEU GLU HIS HIS HIS HIS HIS HIS          
SEQRES   1 C  234  MET GLY PRO LEU PRO ARG THR VAL GLU LEU PHE TYR ASP          
SEQRES   2 C  234  VAL LEU SER PRO TYR SER TRP LEU GLY PHE GLU ILE LEU          
SEQRES   3 C  234  CYS ARG TYR GLN ASN ILE TRP ASN ILE ASN LEU GLN LEU          
SEQRES   4 C  234  ARG PRO SER LEU ILE THR GLY ILE MET LYS ASP SER GLY          
SEQRES   5 C  234  ASN LYS PRO PRO GLY LEU LEU PRO ARG LYS GLY LEU TYR          
SEQRES   6 C  234  MET ALA ASN ASP LEU LYS LEU LEU ARG HIS HIS LEU GLN          
SEQRES   7 C  234  ILE PRO ILE HIS PHE PRO LYS ASP PHE LEU SER VAL MET          
SEQRES   8 C  234  LEU GLU LYS GLY SER LEU SER ALA MET ARG PHE LEU THR          
SEQRES   9 C  234  ALA VAL ASN LEU GLU HIS PRO GLU MET LEU GLU LYS ALA          
SEQRES  10 C  234  SER ARG GLU LEU TRP MET ARG VAL TRP SER ARG ASN GLU          
SEQRES  11 C  234  ASP ILE THR GLU PRO GLN SER ILE LEU ALA ALA ALA GLU          
SEQRES  12 C  234  LYS ALA GLY MET SER ALA GLU GLN ALA GLN GLY LEU LEU          
SEQRES  13 C  234  GLU LYS ILE ALA THR PRO LYS VAL LYS ASN GLN LEU LYS          
SEQRES  14 C  234  GLU THR THR GLU ALA ALA CYS ARG TYR GLY ALA PHE GLY          
SEQRES  15 C  234  LEU PRO ILE THR VAL ALA HIS VAL ASP GLY GLN THR HIS          
SEQRES  16 C  234  MET LEU PHE GLY SER ASP ARG MET GLU LEU LEU ALA HIS          
SEQRES  17 C  234  LEU LEU GLY GLU LYS TRP MET GLY PRO ILE PRO PRO ALA          
SEQRES  18 C  234  VAL ASN ALA ARG LEU LEU GLU HIS HIS HIS HIS HIS HIS          
SEQRES   1 D  234  MET GLY PRO LEU PRO ARG THR VAL GLU LEU PHE TYR ASP          
SEQRES   2 D  234  VAL LEU SER PRO TYR SER TRP LEU GLY PHE GLU ILE LEU          
SEQRES   3 D  234  CYS ARG TYR GLN ASN ILE TRP ASN ILE ASN LEU GLN LEU          
SEQRES   4 D  234  ARG PRO SER LEU ILE THR GLY ILE MET LYS ASP SER GLY          
SEQRES   5 D  234  ASN LYS PRO PRO GLY LEU LEU PRO ARG LYS GLY LEU TYR          
SEQRES   6 D  234  MET ALA ASN ASP LEU LYS LEU LEU ARG HIS HIS LEU GLN          
SEQRES   7 D  234  ILE PRO ILE HIS PHE PRO LYS ASP PHE LEU SER VAL MET          
SEQRES   8 D  234  LEU GLU LYS GLY SER LEU SER ALA MET ARG PHE LEU THR          
SEQRES   9 D  234  ALA VAL ASN LEU GLU HIS PRO GLU MET LEU GLU LYS ALA          
SEQRES  10 D  234  SER ARG GLU LEU TRP MET ARG VAL TRP SER ARG ASN GLU          
SEQRES  11 D  234  ASP ILE THR GLU PRO GLN SER ILE LEU ALA ALA ALA GLU          
SEQRES  12 D  234  LYS ALA GLY MET SER ALA GLU GLN ALA GLN GLY LEU LEU          
SEQRES  13 D  234  GLU LYS ILE ALA THR PRO LYS VAL LYS ASN GLN LEU LYS          
SEQRES  14 D  234  GLU THR THR GLU ALA ALA CYS ARG TYR GLY ALA PHE GLY          
SEQRES  15 D  234  LEU PRO ILE THR VAL ALA HIS VAL ASP GLY GLN THR HIS          
SEQRES  16 D  234  MET LEU PHE GLY SER ASP ARG MET GLU LEU LEU ALA HIS          
SEQRES  17 D  234  LEU LEU GLY GLU LYS TRP MET GLY PRO ILE PRO PRO ALA          
SEQRES  18 D  234  VAL ASN ALA ARG LEU LEU GLU HIS HIS HIS HIS HIS HIS          
SEQRES   1 E  234  MET GLY PRO LEU PRO ARG THR VAL GLU LEU PHE TYR ASP          
SEQRES   2 E  234  VAL LEU SER PRO TYR SER TRP LEU GLY PHE GLU ILE LEU          
SEQRES   3 E  234  CYS ARG TYR GLN ASN ILE TRP ASN ILE ASN LEU GLN LEU          
SEQRES   4 E  234  ARG PRO SER LEU ILE THR GLY ILE MET LYS ASP SER GLY          
SEQRES   5 E  234  ASN LYS PRO PRO GLY LEU LEU PRO ARG LYS GLY LEU TYR          
SEQRES   6 E  234  MET ALA ASN ASP LEU LYS LEU LEU ARG HIS HIS LEU GLN          
SEQRES   7 E  234  ILE PRO ILE HIS PHE PRO LYS ASP PHE LEU SER VAL MET          
SEQRES   8 E  234  LEU GLU LYS GLY SER LEU SER ALA MET ARG PHE LEU THR          
SEQRES   9 E  234  ALA VAL ASN LEU GLU HIS PRO GLU MET LEU GLU LYS ALA          
SEQRES  10 E  234  SER ARG GLU LEU TRP MET ARG VAL TRP SER ARG ASN GLU          
SEQRES  11 E  234  ASP ILE THR GLU PRO GLN SER ILE LEU ALA ALA ALA GLU          
SEQRES  12 E  234  LYS ALA GLY MET SER ALA GLU GLN ALA GLN GLY LEU LEU          
SEQRES  13 E  234  GLU LYS ILE ALA THR PRO LYS VAL LYS ASN GLN LEU LYS          
SEQRES  14 E  234  GLU THR THR GLU ALA ALA CYS ARG TYR GLY ALA PHE GLY          
SEQRES  15 E  234  LEU PRO ILE THR VAL ALA HIS VAL ASP GLY GLN THR HIS          
SEQRES  16 E  234  MET LEU PHE GLY SER ASP ARG MET GLU LEU LEU ALA HIS          
SEQRES  17 E  234  LEU LEU GLY GLU LYS TRP MET GLY PRO ILE PRO PRO ALA          
SEQRES  18 E  234  VAL ASN ALA ARG LEU LEU GLU HIS HIS HIS HIS HIS HIS          
SEQRES   1 F  234  MET GLY PRO LEU PRO ARG THR VAL GLU LEU PHE TYR ASP          
SEQRES   2 F  234  VAL LEU SER PRO TYR SER TRP LEU GLY PHE GLU ILE LEU          
SEQRES   3 F  234  CYS ARG TYR GLN ASN ILE TRP ASN ILE ASN LEU GLN LEU          
SEQRES   4 F  234  ARG PRO SER LEU ILE THR GLY ILE MET LYS ASP SER GLY          
SEQRES   5 F  234  ASN LYS PRO PRO GLY LEU LEU PRO ARG LYS GLY LEU TYR          
SEQRES   6 F  234  MET ALA ASN ASP LEU LYS LEU LEU ARG HIS HIS LEU GLN          
SEQRES   7 F  234  ILE PRO ILE HIS PHE PRO LYS ASP PHE LEU SER VAL MET          
SEQRES   8 F  234  LEU GLU LYS GLY SER LEU SER ALA MET ARG PHE LEU THR          
SEQRES   9 F  234  ALA VAL ASN LEU GLU HIS PRO GLU MET LEU GLU LYS ALA          
SEQRES  10 F  234  SER ARG GLU LEU TRP MET ARG VAL TRP SER ARG ASN GLU          
SEQRES  11 F  234  ASP ILE THR GLU PRO GLN SER ILE LEU ALA ALA ALA GLU          
SEQRES  12 F  234  LYS ALA GLY MET SER ALA GLU GLN ALA GLN GLY LEU LEU          
SEQRES  13 F  234  GLU LYS ILE ALA THR PRO LYS VAL LYS ASN GLN LEU LYS          
SEQRES  14 F  234  GLU THR THR GLU ALA ALA CYS ARG TYR GLY ALA PHE GLY          
SEQRES  15 F  234  LEU PRO ILE THR VAL ALA HIS VAL ASP GLY GLN THR HIS          
SEQRES  16 F  234  MET LEU PHE GLY SER ASP ARG MET GLU LEU LEU ALA HIS          
SEQRES  17 F  234  LEU LEU GLY GLU LYS TRP MET GLY PRO ILE PRO PRO ALA          
SEQRES  18 F  234  VAL ASN ALA ARG LEU LEU GLU HIS HIS HIS HIS HIS HIS          
HET    GTX  A 302      26                                                       
HET    GTX  B 301      26                                                       
HET    GTX  C 301      26                                                       
HET    GTX  D 302      26                                                       
HET    GTX  E 302      26                                                       
HET    GTX  F 302      26                                                       
HETNAM     GTX S-HEXYLGLUTATHIONE                                               
FORMUL   7  GTX    6(C16 H30 N3 O6 S 1+)                                        
FORMUL  13  HOH   *804(H2 O)                                                    
HELIX    1   1 SER A   16  GLN A   30  1                                  15    
HELIX    2   2 LEU A   43  GLY A   52  1                                  10    
HELIX    3   3 PRO A   55  LEU A   58  5                                   4    
HELIX    4   4 LEU A   59  GLN A   78  1                                  20    
HELIX    5   5 PHE A   87  GLY A   95  1                                   9    
HELIX    6   6 SER A   96  HIS A  110  1                                  15    
HELIX    7   7 MET A  113  SER A  127  1                                  15    
HELIX    8   8 GLU A  134  ALA A  145  1                                  12    
HELIX    9   9 SER A  148  GLU A  157  1                                  10    
HELIX   10  10 THR A  161  TYR A  178  1                                  18    
HELIX   11  11 ARG A  202  GLY A  211  1                                  10    
HELIX   12  12 SER B   16  GLN B   30  1                                  15    
HELIX   13  13 LEU B   43  GLY B   52  1                                  10    
HELIX   14  14 PRO B   55  LEU B   58  5                                   4    
HELIX   15  15 LEU B   59  GLN B   78  1                                  20    
HELIX   16  16 PHE B   87  GLY B   95  1                                   9    
HELIX   17  17 SER B   96  HIS B  110  1                                  15    
HELIX   18  18 MET B  113  SER B  127  1                                  15    
HELIX   19  19 GLU B  134  ALA B  145  1                                  12    
HELIX   20  20 SER B  148  GLU B  157  1                                  10    
HELIX   21  21 THR B  161  TYR B  178  1                                  18    
HELIX   22  22 ARG B  202  GLY B  211  1                                  10    
HELIX   23  23 SER C   16  GLN C   30  1                                  15    
HELIX   24  24 LEU C   43  GLY C   52  1                                  10    
HELIX   25  25 PRO C   55  LEU C   58  5                                   4    
HELIX   26  26 LEU C   59  GLN C   78  1                                  20    
HELIX   27  27 PHE C   87  GLY C   95  1                                   9    
HELIX   28  28 SER C   96  HIS C  110  1                                  15    
HELIX   29  29 MET C  113  TRP C  126  1                                  14    
HELIX   30  30 GLU C  134  ALA C  145  1                                  12    
HELIX   31  31 SER C  148  GLU C  157  1                                  10    
HELIX   32  32 THR C  161  TYR C  178  1                                  18    
HELIX   33  33 ARG C  202  GLY C  211  1                                  10    
HELIX   34  34 SER D   16  GLN D   30  1                                  15    
HELIX   35  35 LEU D   43  GLY D   52  1                                  10    
HELIX   36  36 PRO D   55  LEU D   58  5                                   4    
HELIX   37  37 LEU D   59  GLN D   78  1                                  20    
HELIX   38  38 ASP D   86  GLY D   95  1                                  10    
HELIX   39  39 SER D   96  HIS D  110  1                                  15    
HELIX   40  40 MET D  113  SER D  127  1                                  15    
HELIX   41  41 GLU D  134  ALA D  145  1                                  12    
HELIX   42  42 SER D  148  LYS D  158  1                                  11    
HELIX   43  43 THR D  161  TYR D  178  1                                  18    
HELIX   44  44 ARG D  202  GLY D  211  1                                  10    
HELIX   45  45 SER E   16  GLN E   30  1                                  15    
HELIX   46  46 LEU E   43  GLY E   52  1                                  10    
HELIX   47  47 PRO E   55  LEU E   58  5                                   4    
HELIX   48  48 LEU E   59  GLN E   78  1                                  20    
HELIX   49  49 PHE E   87  GLY E   95  1                                   9    
HELIX   50  50 SER E   96  HIS E  110  1                                  15    
HELIX   51  51 MET E  113  SER E  127  1                                  15    
HELIX   52  52 GLU E  134  ALA E  145  1                                  12    
HELIX   53  53 SER E  148  ILE E  159  1                                  12    
HELIX   54  54 THR E  161  TYR E  178  1                                  18    
HELIX   55  55 ARG E  202  GLY E  211  1                                  10    
HELIX   56  56 SER F   16  GLN F   30  1                                  15    
HELIX   57  57 LEU F   43  GLY F   52  1                                  10    
HELIX   58  58 PRO F   55  LEU F   58  5                                   4    
HELIX   59  59 LEU F   59  GLN F   78  1                                  20    
HELIX   60  60 PHE F   87  GLY F   95  1                                   9    
HELIX   61  61 SER F   96  HIS F  110  1                                  15    
HELIX   62  62 MET F  113  SER F  127  1                                  15    
HELIX   63  63 GLU F  134  ALA F  145  1                                  12    
HELIX   64  64 SER F  148  LYS F  158  1                                  11    
HELIX   65  65 THR F  161  TYR F  178  1                                  18    
HELIX   66  66 ARG F  202  GLY F  211  1                                  10    
SHEET    1   A 4 ILE A  35  PRO A  41  0                                        
SHEET    2   A 4 ARG A   6  TYR A  12  1  N  LEU A  10   O  ARG A  40           
SHEET    3   A 4 ILE A 185  VAL A 190 -1  O  VAL A 187   N  GLU A   9           
SHEET    4   A 4 GLN A 193  PHE A 198 -1  O  LEU A 197   N  THR A 186           
SHEET    1   B 4 ILE B  35  PRO B  41  0                                        
SHEET    2   B 4 ARG B   6  TYR B  12  1  N  LEU B  10   O  ARG B  40           
SHEET    3   B 4 ILE B 185  VAL B 190 -1  O  ILE B 185   N  PHE B  11           
SHEET    4   B 4 GLN B 193  PHE B 198 -1  O  LEU B 197   N  THR B 186           
SHEET    1   C 4 ILE C  35  PRO C  41  0                                        
SHEET    2   C 4 ARG C   6  TYR C  12  1  N  LEU C  10   O  ARG C  40           
SHEET    3   C 4 ILE C 185  VAL C 190 -1  O  ILE C 185   N  PHE C  11           
SHEET    4   C 4 GLN C 193  PHE C 198 -1  O  LEU C 197   N  THR C 186           
SHEET    1   D 4 ILE D  35  PRO D  41  0                                        
SHEET    2   D 4 ARG D   6  TYR D  12  1  N  VAL D   8   O  GLN D  38           
SHEET    3   D 4 ILE D 185  VAL D 190 -1  O  VAL D 187   N  GLU D   9           
SHEET    4   D 4 GLN D 193  PHE D 198 -1  O  LEU D 197   N  THR D 186           
SHEET    1   E 4 ILE E  35  PRO E  41  0                                        
SHEET    2   E 4 ARG E   6  TYR E  12  1  N  LEU E  10   O  ARG E  40           
SHEET    3   E 4 ILE E 185  VAL E 190 -1  O  VAL E 187   N  GLU E   9           
SHEET    4   E 4 GLN E 193  PHE E 198 -1  O  LEU E 197   N  THR E 186           
SHEET    1   F 4 ILE F  35  PRO F  41  0                                        
SHEET    2   F 4 ARG F   6  TYR F  12  1  N  VAL F   8   O  GLN F  38           
SHEET    3   F 4 ILE F 185  VAL F 190 -1  O  ILE F 185   N  PHE F  11           
SHEET    4   F 4 GLN F 193  PHE F 198 -1  O  LEU F 197   N  THR F 186           
CISPEP   1 LEU A  183    PRO A  184          0        -3.28                     
CISPEP   2 LEU B  183    PRO B  184          0         0.14                     
CISPEP   3 LEU C  183    PRO C  184          0         1.40                     
CISPEP   4 LEU D  183    PRO D  184          0        -2.12                     
CISPEP   5 LEU E  183    PRO E  184          0         1.37                     
CISPEP   6 LEU F  183    PRO F  184          0        -0.04                     
SITE     1 AC1 21 LEU A  15  SER A  16  PRO A  17  TYR A  18                    
SITE     2 AC1 21 ILE A  44  ASN A  53  PRO A  56  MET A  66                    
SITE     3 AC1 21 LEU A  88  MET A  91  PHE A 181  GLY A 182                    
SITE     4 AC1 21 LEU A 183  PHE A 198  GLY A 199  SER A 200                    
SITE     5 AC1 21 ASP A 201  HOH A 269  HOH A 670  LYS D  62                    
SITE     6 AC1 21 ARG D 202                                                     
SITE     1 AC2 18 LEU B  15  SER B  16  PRO B  17  TYR B  18                    
SITE     2 AC2 18 ASN B  53  PRO B  56  LEU B  88  MET B  91                    
SITE     3 AC2 18 LEU B  92  PHE B 181  GLY B 182  LEU B 183                    
SITE     4 AC2 18 PHE B 198  GLY B 199  SER B 200  ASP B 201                    
SITE     5 AC2 18 LYS E  62  ARG E 202                                          
SITE     1 AC3 20 LEU C  15  SER C  16  PRO C  17  TYR C  18                    
SITE     2 AC3 20 ILE C  44  ASN C  53  PRO C  56  MET C  91                    
SITE     3 AC3 20 LEU C  92  PHE C 181  GLY C 182  LEU C 183                    
SITE     4 AC3 20 PHE C 198  GLY C 199  SER C 200  ASP C 201                    
SITE     5 AC3 20 HOH C 365  HOH C 426  LYS F  62  ARG F 202                    
SITE     1 AC4 19 LYS A  62  ARG A 202  SER D  16  PRO D  17                    
SITE     2 AC4 19 TYR D  18  ILE D  44  ASN D  53  PRO D  56                    
SITE     3 AC4 19 MET D  66  LEU D  88  GLY D 182  LEU D 183                    
SITE     4 AC4 19 PHE D 198  GLY D 199  SER D 200  ASP D 201                    
SITE     5 AC4 19 HOH D 523  HOH D 530  HOH D 593                               
SITE     1 AC5 15 LYS B  62  ARG B 202  SER E  16  TYR E  18                    
SITE     2 AC5 15 ASN E  53  MET E  66  LEU E  88  GLY E 182                    
SITE     3 AC5 15 LEU E 183  PHE E 198  GLY E 199  SER E 200                    
SITE     4 AC5 15 ASP E 201  HOH E 337  HOH E 695                               
SITE     1 AC6 17 LYS C  62  ARG C 202  SER F  16  PRO F  17                    
SITE     2 AC6 17 TYR F  18  ASN F  53  PRO F  56  MET F  66                    
SITE     3 AC6 17 LEU F  88  TRP F 126  GLY F 182  LEU F 183                    
SITE     4 AC6 17 PHE F 198  GLY F 199  SER F 200  ASP F 201                    
SITE     5 AC6 17 HOH F 241                                                     
CRYST1   66.364  199.821   66.714  90.00 116.12  90.00 P 1 21 1     12          
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      0.015068  0.000000  0.007388        0.00000                         
SCALE2      0.000000  0.005004  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016694        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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