GenomeNet

Database: PDB
Entry: 3UBL
LinkDB: 3UBL
Original site: 3UBL 
HEADER    TRANSFERASE                             24-OCT-11   3UBL              
TITLE     CRYSTAL STRUCTURE OF GLUTATHIONE TRANSFERASE (TARGET EFI-501770) FROM 
TITLE    2 LEPTOSPIRA INTERROGANS WITH GSH BOUND                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTATHIONE TRANSFERASE;                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: LEPTOSPIRA INTERROGANS SEROVAR LAI;             
SOURCE   3 ORGANISM_TAXID: 189518;                                              
SOURCE   4 STRAIN: 56601;                                                       
SOURCE   5 GENE: GST, LA_2623;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET                                       
KEYWDS    TRANSFERASE, GSH BINDING SITE                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.PATSKOVSKY,R.TORO,R.BHOSLE,W.D.ZENCHECK,B.HILLERICH,R.D.SEIDEL,     
AUTHOR   2 E.WASHINGTON,A.SCOTT GLENN,S.CHOWDHURY,B.EVANS,J.HAMMONDS,H.J.IMKER, 
AUTHOR   3 R.N.ARMSTRONG,J.A.GERLT,S.C.ALMO,ENZYME FUNCTION INITIATIVE (EFI)    
REVDAT   3   29-FEB-12 3UBL    1       AUTHOR JRNL                              
REVDAT   2   21-DEC-11 3UBL    1       HETATM HETNAM                            
REVDAT   1   09-NOV-11 3UBL    0                                                
JRNL        AUTH   Y.PATSKOVSKY,R.TORO,R.BHOSLE,W.D.ZENCHECK,B.HILLERICH,       
JRNL        AUTH 2 R.D.SEIDEL,E.WASHINGTON,A.SCOTT GLENN,S.CHOWDHURY,B.EVANS,   
JRNL        AUTH 3 J.HAMMONDS,H.J.IMKER,R.N.ARMSTRONG,J.A.GERLT,S.C.ALMO        
JRNL        TITL   CRYSTAL STRUCTURE OF GLUTATHIONE S-TRANSFERASE FROM          
JRNL        TITL 2 LEPTOSPIRA INTERROGANS                                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 39582                          
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) : 0.201                           
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.235                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1272                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2384                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 80.80                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2870                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 69                           
REMARK   3   BIN FREE R VALUE                    : 0.3010                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3349                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 88                                      
REMARK   3   SOLVENT ATOMS            : 142                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 39.32                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.86                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.87000                                              
REMARK   3    B22 (A**2) : 1.87000                                              
REMARK   3    B33 (A**2) : -3.74000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.145         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.113         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.067         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3555 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4803 ; 1.017 ; 2.017       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   421 ; 4.544 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   144 ;31.334 ;24.167       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   631 ;14.310 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;14.943 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   538 ; 0.068 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2600 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  2106 ; 3.250 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3429 ; 4.647 ; 3.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1449 ; 6.598 ; 4.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1371 ; 9.525 ; 6.000       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3UBL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-OCT-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB068549.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-OCT-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.075                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45757                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.940                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -5.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.5                               
REMARK 200  DATA REDUNDANCY                : 15.200                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.94                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 60.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.60                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.92000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MR                           
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3UBK                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.79                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS, PH 5.5, 2M AMMONIUM       
REMARK 280  SULFATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+3/4                                              
REMARK 290       4555   Y,-X,Z+1/4                                              
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z+1/2                                             
REMARK 290       7555   Y,X,-Z+1/4                                              
REMARK 290       8555   -Y,-X,-Z+3/4                                            
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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       87.85050            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      131.77575            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       43.92525            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       87.85050            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       43.92525            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      131.77575            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6010 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -105.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 320  LIES ON A SPECIAL POSITION.                          
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     PRO A   111                                                      
REMARK 465     ALA A   112                                                      
REMARK 465     LYS A   214                                                      
REMARK 465     THR A   215                                                      
REMARK 465     LYS A   216                                                      
REMARK 465     ILE A   217                                                      
REMARK 465     GLY A   218                                                      
REMARK 465     ALA A   219                                                      
REMARK 465     GLU A   220                                                      
REMARK 465     ASN A   221                                                      
REMARK 465     LEU A   222                                                      
REMARK 465     TYR A   223                                                      
REMARK 465     PHE A   224                                                      
REMARK 465     GLN A   225                                                      
REMARK 465     SER A   226                                                      
REMARK 465     HIS A   227                                                      
REMARK 465     HIS A   228                                                      
REMARK 465     HIS A   229                                                      
REMARK 465     HIS A   230                                                      
REMARK 465     HIS A   231                                                      
REMARK 465     HIS A   232                                                      
REMARK 465     TRP A   233                                                      
REMARK 465     SER A   234                                                      
REMARK 465     HIS A   235                                                      
REMARK 465     PRO A   236                                                      
REMARK 465     GLN A   237                                                      
REMARK 465     PHE A   238                                                      
REMARK 465     GLU A   239                                                      
REMARK 465     LYS A   240                                                      
REMARK 465     MET B    -1                                                      
REMARK 465     LEU B   110                                                      
REMARK 465     PRO B   111                                                      
REMARK 465     ALA B   112                                                      
REMARK 465     ALA B   113                                                      
REMARK 465     LYS B   114                                                      
REMARK 465     VAL B   115                                                      
REMARK 465     SER B   116                                                      
REMARK 465     LYS B   214                                                      
REMARK 465     THR B   215                                                      
REMARK 465     LYS B   216                                                      
REMARK 465     ILE B   217                                                      
REMARK 465     GLY B   218                                                      
REMARK 465     ALA B   219                                                      
REMARK 465     GLU B   220                                                      
REMARK 465     ASN B   221                                                      
REMARK 465     LEU B   222                                                      
REMARK 465     TYR B   223                                                      
REMARK 465     PHE B   224                                                      
REMARK 465     GLN B   225                                                      
REMARK 465     SER B   226                                                      
REMARK 465     HIS B   227                                                      
REMARK 465     HIS B   228                                                      
REMARK 465     HIS B   229                                                      
REMARK 465     HIS B   230                                                      
REMARK 465     HIS B   231                                                      
REMARK 465     HIS B   232                                                      
REMARK 465     TRP B   233                                                      
REMARK 465     SER B   234                                                      
REMARK 465     HIS B   235                                                      
REMARK 465     PRO B   236                                                      
REMARK 465     GLN B   237                                                      
REMARK 465     PHE B   238                                                      
REMARK 465     GLU B   239                                                      
REMARK 465     LYS B   240                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASP A  55    CG   OD1  OD2                                       
REMARK 470     LYS A 114    CG   CD   CE   NZ                                   
REMARK 470     LEU B 210    CG   CD1  CD2                                       
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  35      143.03   -179.10                                   
REMARK 500    GLU A  61      121.11     97.32                                   
REMARK 500    ILE A 108      -72.07    -96.01                                   
REMARK 500    ASN A 173      -10.03     77.48                                   
REMARK 500    GLU B  61      113.16     72.49                                   
REMARK 500    PHE B  73       73.49   -119.20                                   
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 GSH A 241                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 242                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 243                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 244                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 245                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 246                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 247                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 248                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH B 241                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 242                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 243                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 244                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3UBK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: EFI-501770   RELATED DB: TARGETTRACK                     
DBREF  3UBL A    1   218  UNP    Q8F2Y8   Q8F2Y8_LEPIN     1    218             
DBREF  3UBL B    1   218  UNP    Q8F2Y8   Q8F2Y8_LEPIN     1    218             
SEQADV 3UBL MET A   -1  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL VAL A    0  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL ALA A  219  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL GLU A  220  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL ASN A  221  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL LEU A  222  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL TYR A  223  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL PHE A  224  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL GLN A  225  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL SER A  226  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL HIS A  227  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL HIS A  228  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL HIS A  229  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL HIS A  230  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL HIS A  231  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL HIS A  232  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL TRP A  233  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL SER A  234  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL HIS A  235  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL PRO A  236  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL GLN A  237  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL PHE A  238  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL GLU A  239  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL LYS A  240  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL MET B   -1  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL VAL B    0  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL ALA B  219  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL GLU B  220  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL ASN B  221  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL LEU B  222  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL TYR B  223  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL PHE B  224  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL GLN B  225  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL SER B  226  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL HIS B  227  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL HIS B  228  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL HIS B  229  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL HIS B  230  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL HIS B  231  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL HIS B  232  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL TRP B  233  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL SER B  234  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL HIS B  235  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL PRO B  236  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL GLN B  237  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL PHE B  238  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL GLU B  239  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQADV 3UBL LYS B  240  UNP  Q8F2Y8              EXPRESSION TAG                 
SEQRES   1 A  242  MET VAL MET ILE LYS LEU HIS GLY ALA SER ILE SER ASN          
SEQRES   2 A  242  TYR VAL ASN LYS VAL LYS LEU GLY ILE LEU GLU LYS GLY          
SEQRES   3 A  242  LEU GLU TYR GLU GLN ILE ARG ILE ALA PRO SER GLN GLU          
SEQRES   4 A  242  GLU ASP PHE LEU LYS ILE SER PRO MET GLY LYS ILE PRO          
SEQRES   5 A  242  VAL LEU GLU MET ASP GLY LYS PHE ILE PHE GLU SER GLY          
SEQRES   6 A  242  ALA ILE LEU GLU PHE LEU ASP THR ILE PHE PRO GLN THR          
SEQRES   7 A  242  PRO LYS LEU ILE PRO GLU ASP PRO TRP GLU ALA ALA ARG          
SEQRES   8 A  242  VAL ARG GLU ILE SER THR ILE ILE GLU THR TYR LEU ASP          
SEQRES   9 A  242  ILE PRO ALA ARG ARG ILE TYR LEU PRO ALA ALA LYS VAL          
SEQRES  10 A  242  SER PRO GLU ILE VAL GLU GLU VAL HIS SER THR LEU VAL          
SEQRES  11 A  242  LYS GLY ILE LYS ALA LEU GLN ARG VAL VAL ARG PHE SER          
SEQRES  12 A  242  PRO TYR ILE ALA GLY ASN VAL PHE THR LEU ALA ASP CYS          
SEQRES  13 A  242  SER GLY PHE ALA HIS LEU SER VAL LEU ASP GLU GLU LEU          
SEQRES  14 A  242  ARG PRO PHE TYR PRO ASN ASN HIS PRO LEU ASP LEU LEU          
SEQRES  15 A  242  ASN GLY TRP LYS GLU TYR PHE VAL PHE MET LYS THR LYS          
SEQRES  16 A  242  ALA GLY PRO ALA LEU VAL GLU LYS ASP LYS GLN ILE LEU          
SEQRES  17 A  242  LYS LYS ILE LEU ALA ARG ALA LYS THR LYS ILE GLY ALA          
SEQRES  18 A  242  GLU ASN LEU TYR PHE GLN SER HIS HIS HIS HIS HIS HIS          
SEQRES  19 A  242  TRP SER HIS PRO GLN PHE GLU LYS                              
SEQRES   1 B  242  MET VAL MET ILE LYS LEU HIS GLY ALA SER ILE SER ASN          
SEQRES   2 B  242  TYR VAL ASN LYS VAL LYS LEU GLY ILE LEU GLU LYS GLY          
SEQRES   3 B  242  LEU GLU TYR GLU GLN ILE ARG ILE ALA PRO SER GLN GLU          
SEQRES   4 B  242  GLU ASP PHE LEU LYS ILE SER PRO MET GLY LYS ILE PRO          
SEQRES   5 B  242  VAL LEU GLU MET ASP GLY LYS PHE ILE PHE GLU SER GLY          
SEQRES   6 B  242  ALA ILE LEU GLU PHE LEU ASP THR ILE PHE PRO GLN THR          
SEQRES   7 B  242  PRO LYS LEU ILE PRO GLU ASP PRO TRP GLU ALA ALA ARG          
SEQRES   8 B  242  VAL ARG GLU ILE SER THR ILE ILE GLU THR TYR LEU ASP          
SEQRES   9 B  242  ILE PRO ALA ARG ARG ILE TYR LEU PRO ALA ALA LYS VAL          
SEQRES  10 B  242  SER PRO GLU ILE VAL GLU GLU VAL HIS SER THR LEU VAL          
SEQRES  11 B  242  LYS GLY ILE LYS ALA LEU GLN ARG VAL VAL ARG PHE SER          
SEQRES  12 B  242  PRO TYR ILE ALA GLY ASN VAL PHE THR LEU ALA ASP CYS          
SEQRES  13 B  242  SER GLY PHE ALA HIS LEU SER VAL LEU ASP GLU GLU LEU          
SEQRES  14 B  242  ARG PRO PHE TYR PRO ASN ASN HIS PRO LEU ASP LEU LEU          
SEQRES  15 B  242  ASN GLY TRP LYS GLU TYR PHE VAL PHE MET LYS THR LYS          
SEQRES  16 B  242  ALA GLY PRO ALA LEU VAL GLU LYS ASP LYS GLN ILE LEU          
SEQRES  17 B  242  LYS LYS ILE LEU ALA ARG ALA LYS THR LYS ILE GLY ALA          
SEQRES  18 B  242  GLU ASN LEU TYR PHE GLN SER HIS HIS HIS HIS HIS HIS          
SEQRES  19 B  242  TRP SER HIS PRO GLN PHE GLU LYS                              
HET    GSH  A 241      40                                                       
HET    SO4  A 242       5                                                       
HET    SO4  A 243       5                                                       
HET    SO4  A 244       5                                                       
HET    GOL  A 245       6                                                       
HET     CL  A 246       1                                                       
HET    GOL  A 247       6                                                       
HET    GOL  A 248       6                                                       
HET    UNX  A 249       1                                                       
HET    GSH  B 241      40                                                       
HET    SO4  B 242       5                                                       
HET    GOL  B 243       6                                                       
HET     CL  B 244       1                                                       
HET    UNX  B 245       1                                                       
HETNAM     GSH GLUTATHIONE                                                      
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM      CL CHLORIDE ION                                                     
HETNAM     UNX UNKNOWN ATOM OR ION                                              
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  GSH    2(C10 H17 N3 O6 S)                                           
FORMUL   4  SO4    4(O4 S 2-)                                                   
FORMUL   7  GOL    4(C3 H8 O3)                                                  
FORMUL   8   CL    2(CL 1-)                                                     
FORMUL  11  UNX    2(X)                                                         
FORMUL  17  HOH   *142(H2 O)                                                    
HELIX    1   1 SER A   10  GLY A   24  1                                  15    
HELIX    2   2 GLU A   37  LYS A   42  1                                   6    
HELIX    3   3 GLU A   61  PHE A   73  1                                  13    
HELIX    4   4 ASP A   83  LEU A  101  1                                  19    
HELIX    5   5 LEU A  101  LEU A  110  1                                  10    
HELIX    6   6 SER A  116  ARG A  136  1                                  21    
HELIX    7   7 THR A  150  TYR A  171  1                                  22    
HELIX    8   8 HIS A  175  LEU A  180  5                                   6    
HELIX    9   9 GLY A  182  THR A  192  1                                  11    
HELIX   10  10 LYS A  193  ALA A  211  1                                  19    
HELIX   11  11 SER B   10  LYS B   23  1                                  14    
HELIX   12  12 GLU B   37  LYS B   42  1                                   6    
HELIX   13  13 GLU B   61  PHE B   73  1                                  13    
HELIX   14  14 ASP B   83  TYR B  100  1                                  18    
HELIX   15  15 LEU B  101  ARG B  106  1                                   6    
HELIX   16  16 ARG B  107  TYR B  109  5                                   3    
HELIX   17  17 ILE B  119  GLN B  135  1                                  17    
HELIX   18  18 THR B  150  ARG B  168  1                                  19    
HELIX   19  19 HIS B  175  LEU B  180  5                                   6    
HELIX   20  20 GLY B  182  THR B  192  1                                  11    
HELIX   21  21 LYS B  193  LEU B  210  1                                  18    
SHEET    1   A 4 TYR A  27  ILE A  30  0                                        
SHEET    2   A 4 ILE A   2  HIS A   5  1  N  LEU A   4   O  ILE A  30           
SHEET    3   A 4 VAL A  51  MET A  54 -1  O  VAL A  51   N  HIS A   5           
SHEET    4   A 4 LYS A  57  PHE A  60 -1  O  ILE A  59   N  LEU A  52           
SHEET    1   B 4 TYR B  27  ILE B  30  0                                        
SHEET    2   B 4 ILE B   2  HIS B   5  1  N  LEU B   4   O  GLU B  28           
SHEET    3   B 4 VAL B  51  MET B  54 -1  O  VAL B  51   N  HIS B   5           
SHEET    4   B 4 LYS B  57  PHE B  60 -1  O  ILE B  59   N  LEU B  52           
CISPEP   1 ILE A   49    PRO A   50          0         6.07                     
CISPEP   2 THR A   76    PRO A   77          0        -1.65                     
CISPEP   3 SER A  141    PRO A  142          0         0.48                     
CISPEP   4 ILE B   49    PRO B   50          0         5.34                     
CISPEP   5 THR B   76    PRO B   77          0         2.10                     
CISPEP   6 SER B  141    PRO B  142          0         1.33                     
SITE     1 AC1 15 SER A  10  ASN A  11  TYR A  12  PRO A  34                    
SITE     2 AC1 15 LYS A  48  ILE A  49  PRO A  50  GLU A  61                    
SITE     3 AC1 15 SER A  62  ARG A 106  HOH A 270  HOH A 312                    
SITE     4 AC1 15 HOH A 314  HOH A 315  TYR B 100                               
SITE     1 AC2  4 LYS A 193  ALA A 194  HOH A 250  HOH A 321                    
SITE     1 AC3  6 GLN A  75  THR A  76  HOH A 263  LYS B  78                    
SITE     2 AC3  6 GLU B  82  HOH B 257                                          
SITE     1 AC4  5 LEU A 180  GLY A 182  TRP A 183  LYS A 184                    
SITE     2 AC4  5 GLU A 185                                                     
SITE     1 AC5  3 MET A   1  GLU A  26  ASP B  83                               
SITE     1 AC6  2 SER A   8  ARG A  31                                          
SITE     1 AC7  6 GLN A  29  ASP A 202  HOH A 279  LYS B 193                    
SITE     2 AC7  6 GOL B 243  HOH B 295                                          
SITE     1 AC8  6 PHE A 140  SER A 141  PRO A 142  TYR A 186                    
SITE     2 AC8  6 HOH A 297  HOH A 318                                          
SITE     1 AC9 15 TYR A 100  SER B  10  ASN B  11  TYR B  12                    
SITE     2 AC9 15 PRO B  34  LYS B  48  ILE B  49  PRO B  50                    
SITE     3 AC9 15 GLU B  61  SER B  62  ARG B 106  HOH B 262                    
SITE     4 AC9 15 HOH B 272  HOH B 300  HOH B 301                               
SITE     1 BC1  6 LEU B 180  ASN B 181  GLY B 182  TRP B 183                    
SITE     2 BC1  6 LYS B 184  GLU B 185                                          
SITE     1 BC2  8 LEU A 198  LYS A 201  ASP A 202  GOL A 247                    
SITE     2 BC2  8 GLU B  22  TYR B 143  LYS B 193  HOH B 261                    
SITE     1 BC3  4 ALA B   7  SER B   8  ARG B  31  HOH B 312                    
CRYST1   82.591   82.591  175.701  90.00  90.00  90.00 P 43 2 2     16          
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      0.012108  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012108  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005691        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system