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Database: PDB
Entry: 3UAP
LinkDB: 3UAP
Original site: 3UAP 
HEADER    TRANSFERASE                             21-OCT-11   3UAP              
TITLE     CRYSTAL STRUCTURE OF GLUTATHIONE TRANSFERASE (TARGET EFI-501774) FROM 
TITLE    2 METHYLOCOCCUS CAPSULATUS STR. BATH                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTATHIONE S-TRANSFERASE;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 2.5.1.18;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: METHYLOCOCCUS CAPSULATUS;                       
SOURCE   3 ORGANISM_TAXID: 243233;                                              
SOURCE   4 STRAIN: NCIMB 11132 / BATH;                                          
SOURCE   5 ATCC: 33009;                                                         
SOURCE   6 GENE: GST, MCA0074;                                                  
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET                                       
KEYWDS    TRANSFERASE, GSH BINDING SITE, STRUCTURAL GENOMICS                    
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   4   13-SEP-23 3UAP    1       REMARK SEQADV                            
REVDAT   3   24-JAN-18 3UAP    1       AUTHOR                                   
REVDAT   2   29-FEB-12 3UAP    1       AUTHOR JRNL                              
REVDAT   1   02-NOV-11 3UAP    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 METHYLOCOCCUS CAPSULATUS                                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.08                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 9260                           
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) : 0.195                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 281                             
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) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 670                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3540                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 19                           
REMARK   3   BIN FREE R VALUE                    : 0.4250                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1607                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 6                                       
REMARK   3   SOLVENT ATOMS            : 3                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 114.9                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 102.5                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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): 0.308         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.225         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.375        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.936                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1662 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2258 ; 1.050 ; 1.987       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   204 ; 4.789 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    74 ;36.623 ;23.784       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   278 ;17.629 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    11 ;16.097 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   244 ; 0.058 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1266 ; 0.004 ; 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):  1014 ; 2.856 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1626 ; 5.401 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   648 ; 7.555 ; 4.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   631 ;11.787 ; 6.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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   : 1.00                                          
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 3UAP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-OCT-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000068517.                                   
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                             : 7.0                                
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   : 10645                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
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     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 11.90                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.75                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.90                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.800                              
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 2DSA                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM CHLORIDE, 0.1M TRIS-HCL,     
REMARK 280  30% PEG3000, PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE     
REMARK 280  294K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 3 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z+1/2,-X+1/2,-Y                                         
REMARK 290       7555   -Z+1/2,-X,Y+1/2                                         
REMARK 290       8555   -Z,X+1/2,-Y+1/2                                         
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z+1/2,-X+1/2                                         
REMARK 290      11555   Y+1/2,-Z+1/2,-X                                         
REMARK 290      12555   -Y+1/2,-Z,X+1/2                                         
REMARK 290      13555   Y+1/4,X+3/4,-Z+3/4                                      
REMARK 290      14555   -Y+1/4,-X+1/4,-Z+1/4                                    
REMARK 290      15555   Y+3/4,-X+3/4,Z+1/4                                      
REMARK 290      16555   -Y+3/4,X+1/4,Z+3/4                                      
REMARK 290      17555   X+1/4,Z+3/4,-Y+3/4                                      
REMARK 290      18555   -X+3/4,Z+1/4,Y+3/4                                      
REMARK 290      19555   -X+1/4,-Z+1/4,-Y+1/4                                    
REMARK 290      20555   X+3/4,-Z+3/4,Y+1/4                                      
REMARK 290      21555   Z+1/4,Y+3/4,-X+3/4                                      
REMARK 290      22555   Z+3/4,-Y+3/4,X+1/4                                      
REMARK 290      23555   -Z+3/4,Y+1/4,X+3/4                                      
REMARK 290      24555   -Z+1/4,-Y+1/4,-X+1/4                                    
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       64.62300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       64.62300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       64.62300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       64.62300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       64.62300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       64.62300            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000       64.62300            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000       64.62300            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000       64.62300            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000       64.62300            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000       64.62300            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000       64.62300            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000       64.62300            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000       64.62300            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000       64.62300            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000       64.62300            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000       64.62300            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000       64.62300            
REMARK 290   SMTRY1  13  0.000000  1.000000  0.000000       32.31150            
REMARK 290   SMTRY2  13  1.000000  0.000000  0.000000       96.93450            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       96.93450            
REMARK 290   SMTRY1  14  0.000000 -1.000000  0.000000       32.31150            
REMARK 290   SMTRY2  14 -1.000000  0.000000  0.000000       32.31150            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       32.31150            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       96.93450            
REMARK 290   SMTRY2  15 -1.000000  0.000000  0.000000       96.93450            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000       32.31150            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       96.93450            
REMARK 290   SMTRY2  16  1.000000  0.000000  0.000000       32.31150            
REMARK 290   SMTRY3  16  0.000000  0.000000  1.000000       96.93450            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000       32.31150            
REMARK 290   SMTRY2  17  0.000000  0.000000  1.000000       96.93450            
REMARK 290   SMTRY3  17  0.000000 -1.000000  0.000000       96.93450            
REMARK 290   SMTRY1  18 -1.000000  0.000000  0.000000       96.93450            
REMARK 290   SMTRY2  18  0.000000  0.000000  1.000000       32.31150            
REMARK 290   SMTRY3  18  0.000000  1.000000  0.000000       96.93450            
REMARK 290   SMTRY1  19 -1.000000  0.000000  0.000000       32.31150            
REMARK 290   SMTRY2  19  0.000000  0.000000 -1.000000       32.31150            
REMARK 290   SMTRY3  19  0.000000 -1.000000  0.000000       32.31150            
REMARK 290   SMTRY1  20  1.000000  0.000000  0.000000       96.93450            
REMARK 290   SMTRY2  20  0.000000  0.000000 -1.000000       96.93450            
REMARK 290   SMTRY3  20  0.000000  1.000000  0.000000       32.31150            
REMARK 290   SMTRY1  21  0.000000  0.000000  1.000000       32.31150            
REMARK 290   SMTRY2  21  0.000000  1.000000  0.000000       96.93450            
REMARK 290   SMTRY3  21 -1.000000  0.000000  0.000000       96.93450            
REMARK 290   SMTRY1  22  0.000000  0.000000  1.000000       96.93450            
REMARK 290   SMTRY2  22  0.000000 -1.000000  0.000000       96.93450            
REMARK 290   SMTRY3  22  1.000000  0.000000  0.000000       32.31150            
REMARK 290   SMTRY1  23  0.000000  0.000000 -1.000000       96.93450            
REMARK 290   SMTRY2  23  0.000000  1.000000  0.000000       32.31150            
REMARK 290   SMTRY3  23  1.000000  0.000000  0.000000       96.93450            
REMARK 290   SMTRY1  24  0.000000  0.000000 -1.000000       32.31150            
REMARK 290   SMTRY2  24  0.000000 -1.000000  0.000000       32.31150            
REMARK 290   SMTRY3  24 -1.000000  0.000000  0.000000       32.31150            
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: 3610 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16840 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      -32.31150            
REMARK 350   BIOMT2   2  0.000000  0.000000  1.000000       32.31150            
REMARK 350   BIOMT3   2  0.000000  1.000000  0.000000      -32.31150            
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     GLN A   203                                                      
REMARK 465     ALA A   204                                                      
REMARK 465     GLU A   205                                                      
REMARK 465     ASN A   206                                                      
REMARK 465     LEU A   207                                                      
REMARK 465     TYR A   208                                                      
REMARK 465     PHE A   209                                                      
REMARK 465     GLN A   210                                                      
REMARK 465     SER A   211                                                      
REMARK 465     HIS A   212                                                      
REMARK 465     HIS A   213                                                      
REMARK 465     HIS A   214                                                      
REMARK 465     HIS A   215                                                      
REMARK 465     HIS A   216                                                      
REMARK 465     HIS A   217                                                      
REMARK 465     TRP A   218                                                      
REMARK 465     SER A   219                                                      
REMARK 465     HIS A   220                                                      
REMARK 465     PRO A   221                                                      
REMARK 465     GLN A   222                                                      
REMARK 465     PHE A   223                                                      
REMARK 465     GLU A   224                                                      
REMARK 465     LYS A   225                                                      
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    VAL A  46      -72.34    -65.07                                   
REMARK 500    ASP A  59        4.53    -59.60                                   
REMARK 500    GLU A  65      103.10     84.21                                   
REMARK 500    MET A  83      135.54   -170.15                                   
REMARK 500    PRO A 118      177.61    -44.83                                   
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 GOL A 226                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3UAR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: EFI-501774   RELATED DB: TARGETTRACK                     
DBREF  3UAP A    1   203  UNP    Q60CN1   Q60CN1_METCA     1    203             
SEQADV 3UAP MET A   -1  UNP  Q60CN1              EXPRESSION TAG                 
SEQADV 3UAP VAL A    0  UNP  Q60CN1              EXPRESSION TAG                 
SEQADV 3UAP ALA A  204  UNP  Q60CN1              EXPRESSION TAG                 
SEQADV 3UAP GLU A  205  UNP  Q60CN1              EXPRESSION TAG                 
SEQADV 3UAP ASN A  206  UNP  Q60CN1              EXPRESSION TAG                 
SEQADV 3UAP LEU A  207  UNP  Q60CN1              EXPRESSION TAG                 
SEQADV 3UAP TYR A  208  UNP  Q60CN1              EXPRESSION TAG                 
SEQADV 3UAP PHE A  209  UNP  Q60CN1              EXPRESSION TAG                 
SEQADV 3UAP GLN A  210  UNP  Q60CN1              EXPRESSION TAG                 
SEQADV 3UAP SER A  211  UNP  Q60CN1              EXPRESSION TAG                 
SEQADV 3UAP HIS A  212  UNP  Q60CN1              EXPRESSION TAG                 
SEQADV 3UAP HIS A  213  UNP  Q60CN1              EXPRESSION TAG                 
SEQADV 3UAP HIS A  214  UNP  Q60CN1              EXPRESSION TAG                 
SEQADV 3UAP HIS A  215  UNP  Q60CN1              EXPRESSION TAG                 
SEQADV 3UAP HIS A  216  UNP  Q60CN1              EXPRESSION TAG                 
SEQADV 3UAP HIS A  217  UNP  Q60CN1              EXPRESSION TAG                 
SEQADV 3UAP TRP A  218  UNP  Q60CN1              EXPRESSION TAG                 
SEQADV 3UAP SER A  219  UNP  Q60CN1              EXPRESSION TAG                 
SEQADV 3UAP HIS A  220  UNP  Q60CN1              EXPRESSION TAG                 
SEQADV 3UAP PRO A  221  UNP  Q60CN1              EXPRESSION TAG                 
SEQADV 3UAP GLN A  222  UNP  Q60CN1              EXPRESSION TAG                 
SEQADV 3UAP PHE A  223  UNP  Q60CN1              EXPRESSION TAG                 
SEQADV 3UAP GLU A  224  UNP  Q60CN1              EXPRESSION TAG                 
SEQADV 3UAP LYS A  225  UNP  Q60CN1              EXPRESSION TAG                 
SEQRES   1 A  227  MET VAL MET LYS LEU TYR TYR PHE PRO GLY ALA CYS SER          
SEQRES   2 A  227  LEU ALA PRO HIS ILE VAL LEU ARG GLU ALA GLY LEU ASP          
SEQRES   3 A  227  PHE GLU LEU GLU ASN VAL ASP LEU GLY THR LYS LYS THR          
SEQRES   4 A  227  GLY SER GLY ALA ASP PHE LEU GLN VAL ASN PRO LYS GLY          
SEQRES   5 A  227  TYR VAL PRO ALA LEU GLN LEU ASP ASP GLY GLN VAL LEU          
SEQRES   6 A  227  THR GLU ASP GLN VAL ILE LEU GLN TYR LEU ALA ASP LEU          
SEQRES   7 A  227  LYS PRO GLU SER GLY LEU MET PRO PRO SER GLY THR PHE          
SEQRES   8 A  227  GLU ARG TYR ARG LEU LEU GLU TRP LEU ALA PHE ILE SER          
SEQRES   9 A  227  THR GLU ILE HIS LYS THR PHE GLY PRO PHE TRP ASN PRO          
SEQRES  10 A  227  GLU SER PRO GLU ALA SER LYS GLN ILE ALA LEU GLY LEU          
SEQRES  11 A  227  LEU SER ARG ARG LEU ASP TYR VAL GLU ASP ARG LEU GLU          
SEQRES  12 A  227  ALA GLY GLY PRO TRP LEU MET GLY ASP ARG TYR SER VAL          
SEQRES  13 A  227  ALA ASP ALA TYR LEU SER THR VAL LEU GLY TRP CYS GLU          
SEQRES  14 A  227  TYR LEU LYS ILE ASP LEU SER LYS TRP PRO ARG ILE LEU          
SEQRES  15 A  227  ALA TYR LEU GLU ARG ASN GLN ALA ARG PRO ALA VAL GLN          
SEQRES  16 A  227  ALA ALA MET LYS ALA GLU GLY LEU ILE GLN ALA GLU ASN          
SEQRES  17 A  227  LEU TYR PHE GLN SER HIS HIS HIS HIS HIS HIS TRP SER          
SEQRES  18 A  227  HIS PRO GLN PHE GLU LYS                                      
HET    GOL  A 226       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  GOL    C3 H8 O3                                                     
FORMUL   3  HOH   *3(H2 O)                                                      
HELIX    1   1 SER A   11  ALA A   21  1                                  11    
HELIX    2   2 ASP A   42  ASN A   47  1                                   6    
HELIX    3   3 GLU A   65  LYS A   77  1                                  13    
HELIX    4   4 PRO A   78  GLY A   81  5                                   4    
HELIX    5   5 PHE A   89  ILE A  105  1                                  17    
HELIX    6   6 HIS A  106  ASN A  114  5                                   9    
HELIX    7   7 PRO A  118  GLY A  143  1                                  26    
HELIX    8   8 SER A  153  GLY A  164  1                                  12    
HELIX    9   9 GLY A  164  LEU A  169  1                                   6    
HELIX   10  10 TRP A  176  ALA A  188  1                                  13    
HELIX   11  11 ARG A  189  GLU A  199  1                                  11    
SHEET    1   A 5 LYS A  36  THR A  37  0                                        
SHEET    2   A 5 PHE A  25  ASP A  31 -1  N  ASP A  31   O  LYS A  36           
SHEET    3   A 5 MET A   1  TYR A   5  1  N  LEU A   3   O  GLU A  28           
SHEET    4   A 5 ALA A  54  GLN A  56 -1  O  GLN A  56   N  LYS A   2           
SHEET    5   A 5 VAL A  62  THR A  64 -1  O  LEU A  63   N  LEU A  55           
CISPEP   1 VAL A   52    PRO A   53          0        11.34                     
SITE     1 AC1  4 LYS A  49  GLU A  96  TRP A  97  TYR A 135                    
CRYST1  129.246  129.246  129.246  90.00  90.00  90.00 P 43 3 2     24          
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      0.007737  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007737  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007737        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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