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Database: PDB
Entry: 3R2Q
LinkDB: 3R2Q
Original site: 3R2Q 
HEADER    TRANSFERASE                             14-MAR-11   3R2Q              
TITLE     CRYSTAL STRUCTURE ANALYSIS OF YIBF FROM E. COLI                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UNCHARACTERIZED GST-LIKE PROTEIN YIBF;                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12;                                                         
SOURCE   5 GENE: B3592, JW3565, YIBF;                                           
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: PET20B(+)                                 
KEYWDS    TRANSFERASE, GLUTATHIONE, GST                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.E.LADNER,J.HARP,M.SCHAAB,N.V.STOURNAN,R.N.ARMSTRONG                 
REVDAT   1   14-MAR-12 3R2Q    0                                                
JRNL        AUTH   J.E.LADNER,N.V.STOURNAN,M.C.BRANCH,J.HARP,M.SCHAAB,          
JRNL        AUTH 2 D.W.BROWN,R.N.ARMSTRONG                                      
JRNL        TITL   STRUCTURAL AND FUNCTIONAL GENOMICS OF YIBF, A GLUTATHIONE    
JRNL        TITL 2 TRANSFERASE HOMOLOGUE FROM ESCHERICHIA COLI                  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.3                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R                         
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.132                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.153                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 5366                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.121                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.142                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 4654                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 92438                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 1587                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 33                                            
REMARK   3   SOLVENT ATOMS      : 281                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 1876.55                 
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 1584.00                 
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 24                      
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 18731                   
REMARK   3   NUMBER OF RESTRAINTS                     : 25172                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.016                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.033                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.027                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.080                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.099                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.213                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.006                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.053                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.099                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-228        
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: ANISOTROPIC REFINEMENT, FINAL             
REMARK   3  REFINEMENT WITH RIDING HYDROGENS                                    
REMARK   4                                                                      
REMARK   4 3R2Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAR-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB064414.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-JUL-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 107437                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.050                              
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     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 7.800                              
REMARK 200  R MERGE                    (I) : 0.06900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.09                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: ARP/WARP                                              
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.82                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 5 MICROL PROTEIN IN 50 MM HEPES PH       
REMARK 280  7.5, 1 MM DTT, 4 MICROL RESERVOIR (0.1M NA ACETATE PH 4.6,1M        
REMARK 280  AMMONIUM PHOSPHATE MONOBASIC), 1 MICROL 100MM GLUTATHIONE PH 7.0,   
REMARK 280  VAPOR DIFFUSION, TEMPERATURE 298K                                   
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       55.67000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.67000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.67000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       55.67000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       55.67000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.67000            
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       55.67000            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000       55.67000            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000       55.67000            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000       55.67000            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000       55.67000            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000       55.67000            
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       55.67000            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000       55.67000            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000       55.67000            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000       55.67000            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000       55.67000            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000       55.67000            
REMARK 290   SMTRY1  13  0.000000  1.000000  0.000000       27.83500            
REMARK 290   SMTRY2  13  1.000000  0.000000  0.000000       83.50500            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       83.50500            
REMARK 290   SMTRY1  14  0.000000 -1.000000  0.000000       27.83500            
REMARK 290   SMTRY2  14 -1.000000  0.000000  0.000000       27.83500            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       27.83500            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       83.50500            
REMARK 290   SMTRY2  15 -1.000000  0.000000  0.000000       83.50500            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000       27.83500            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       83.50500            
REMARK 290   SMTRY2  16  1.000000  0.000000  0.000000       27.83500            
REMARK 290   SMTRY3  16  0.000000  0.000000  1.000000       83.50500            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000       27.83500            
REMARK 290   SMTRY2  17  0.000000  0.000000  1.000000       83.50500            
REMARK 290   SMTRY3  17  0.000000 -1.000000  0.000000       83.50500            
REMARK 290   SMTRY1  18 -1.000000  0.000000  0.000000       83.50500            
REMARK 290   SMTRY2  18  0.000000  0.000000  1.000000       27.83500            
REMARK 290   SMTRY3  18  0.000000  1.000000  0.000000       83.50500            
REMARK 290   SMTRY1  19 -1.000000  0.000000  0.000000       27.83500            
REMARK 290   SMTRY2  19  0.000000  0.000000 -1.000000       27.83500            
REMARK 290   SMTRY3  19  0.000000 -1.000000  0.000000       27.83500            
REMARK 290   SMTRY1  20  1.000000  0.000000  0.000000       83.50500            
REMARK 290   SMTRY2  20  0.000000  0.000000 -1.000000       83.50500            
REMARK 290   SMTRY3  20  0.000000  1.000000  0.000000       27.83500            
REMARK 290   SMTRY1  21  0.000000  0.000000  1.000000       27.83500            
REMARK 290   SMTRY2  21  0.000000  1.000000  0.000000       83.50500            
REMARK 290   SMTRY3  21 -1.000000  0.000000  0.000000       83.50500            
REMARK 290   SMTRY1  22  0.000000  0.000000  1.000000       83.50500            
REMARK 290   SMTRY2  22  0.000000 -1.000000  0.000000       83.50500            
REMARK 290   SMTRY3  22  1.000000  0.000000  0.000000       27.83500            
REMARK 290   SMTRY1  23  0.000000  0.000000 -1.000000       83.50500            
REMARK 290   SMTRY2  23  0.000000  1.000000  0.000000       27.83500            
REMARK 290   SMTRY3  23  1.000000  0.000000  0.000000       83.50500            
REMARK 290   SMTRY1  24  0.000000  0.000000 -1.000000       27.83500            
REMARK 290   SMTRY2  24  0.000000 -1.000000  0.000000       27.83500            
REMARK 290   SMTRY3  24 -1.000000  0.000000  0.000000       27.83500            
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: 6110 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17680 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 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      -83.50500            
REMARK 350   BIOMT2   2  0.000000  0.000000 -1.000000       27.83500            
REMARK 350   BIOMT3   2  0.000000 -1.000000  0.000000       27.83500            
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 A1251  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1089  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1186  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1243  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1248  LIES ON A SPECIAL POSITION.                          
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    MET A  73   CA  -  C   -  O   ANGL. DEV. = -13.8 DEGREES          
REMARK 500    MET A  73   CA  -  C   -  N   ANGL. DEV. =  17.9 DEGREES          
REMARK 500    ARG A  89   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG A  91   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG A 109   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.3 DEGREES          
REMARK 500    ARG A 113   NE  -  CZ  -  NH1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG A 113   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ARG A 125   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A 132   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ARG A 132   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    LYS A 201   CB  -  CA  -  C   ANGL. DEV. = -12.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    CSX A 175        -11.21                                           
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 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 309                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 310                 
DBREF  3R2Q A    1   202  UNP    P0ACA1   YIBF_ECOLI       1    202             
SEQRES   1 A  202  MET LYS LEU VAL GLY SER TYR THR SER PRO PHE VAL ARG          
SEQRES   2 A  202  LYS LEU SER ILE LEU LEU LEU GLU LYS GLY ILE THR PHE          
SEQRES   3 A  202  GLU PHE ILE ASN GLU LEU PRO TYR ASN ALA ASP ASN GLY          
SEQRES   4 A  202  VAL ALA GLN PHE ASN PRO LEU GLY LYS VAL PRO VAL LEU          
SEQRES   5 A  202  VAL THR GLU GLU GLY GLU CYS TRP PHE ASP SER PRO ILE          
SEQRES   6 A  202  ILE ALA GLU TYR ILE GLU LEU MET ASN VAL ALA PRO ALA          
SEQRES   7 A  202  MET LEU PRO ARG ASP PRO LEU GLU SER LEU ARG VAL ARG          
SEQRES   8 A  202  LYS ILE GLU ALA LEU ALA ASP GLY ILE MET ASP ALA GLY          
SEQRES   9 A  202  LEU VAL SER VAL ARG GLU GLN ALA ARG PRO ALA ALA GLN          
SEQRES  10 A  202  GLN SER GLU ASP GLU LEU LEU ARG GLN ARG GLU LYS ILE          
SEQRES  11 A  202  ASN ARG SER LEU ASP VAL LEU GLU GLY TYR LEU VAL ASP          
SEQRES  12 A  202  GLY THR LEU LYS THR ASP THR VAL ASN LEU ALA THR ILE          
SEQRES  13 A  202  ALA ILE ALA CYS ALA VAL GLY TYR LEU ASN PHE ARG ARG          
SEQRES  14 A  202  VAL ALA PRO GLY TRP CSX VAL ASP ARG PRO HIS LEU VAL          
SEQRES  15 A  202  LYS LEU VAL GLU ASN LEU PHE SER ARG GLU SER PHE ALA          
SEQRES  16 A  202  ARG THR GLU PRO PRO LYS ALA                                  
MODRES 3R2Q CSX A  175  CYS  S-OXY CYSTEINE                                     
HET    CSX  A 175       7                                                       
HET    GSH  A 301      23                                                       
HET    PO4  A 305       5                                                       
HET    EDO  A 309       4                                                       
HET    EDO  A 310       4                                                       
HETNAM     CSX S-OXY CYSTEINE                                                   
HETNAM     GSH GLUTATHIONE                                                      
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  CSX    C3 H7 N O3 S                                                 
FORMUL   2  GSH    C10 H17 N3 O6 S                                              
FORMUL   3  PO4    O4 P 3-                                                      
FORMUL   4  EDO    2(C2 H6 O2)                                                  
FORMUL   6  HOH   *281(H2 O)                                                    
HELIX    1   1 SER A    9  LYS A   22  1                                  14    
HELIX    2   2 ASP A   62  MET A   73  1                                  12    
HELIX    3   3 ASP A   83  ARG A  113  1                                  31    
HELIX    4   4 PRO A  114  GLN A  118  5                                   5    
HELIX    5   5 SER A  119  ASP A  143  1                                  25    
HELIX    6   6 ASN A  152  ARG A  169  1                                  18    
HELIX    7   7 ARG A  178  SER A  190  1                                  13    
HELIX    8   8 ARG A  191  ARG A  196  1                                   6    
SHEET    1   A 4 GLU A  27  ASN A  30  0                                        
SHEET    2   A 4 LYS A   2  GLY A   5  1  N  LEU A   3   O  ILE A  29           
SHEET    3   A 4 VAL A  51  VAL A  53 -1  O  VAL A  51   N  VAL A   4           
SHEET    4   A 4 CYS A  59  TRP A  60 -1  O  TRP A  60   N  LEU A  52           
LINK         C   TRP A 174                 N   CSX A 175     1555   1555  1.35  
LINK         C   CSX A 175                 N   VAL A 176     1555   1555  1.28  
CISPEP   1 VAL A   49    PRO A   50          0         6.88                     
CISPEP   2 PHE A   61    ASP A   62          0       -14.49                     
CISPEP   3 ALA A   76    PRO A   77          0        -3.14                     
SITE     1 AC1 22 SER A   9  PHE A  11  PRO A  33  TYR A  34                    
SITE     2 AC1 22 LYS A  48  VAL A  49  PRO A  50  ASP A  62                    
SITE     3 AC1 22 SER A  63  PRO A  64  LEU A 105  ARG A 125                    
SITE     4 AC1 22 LYS A 129  HOH A1009  HOH A1010  HOH A1028                    
SITE     5 AC1 22 HOH A1030  HOH A1051  HOH A1096  HOH A1099                    
SITE     6 AC1 22 HOH A1116  HOH A1234                                          
SITE     1 AC2  8 ARG A 127  ASN A 131  ALA A 171  PRO A 172                    
SITE     2 AC2  8 GLY A 173  HOH A1136  HOH A1147  HOH A1253                    
SITE     1 AC3  6 ARG A  13  PHE A 189  GLU A 198  HOH A1069                    
SITE     2 AC3  6 HOH A1077  HOH A1130                                          
SITE     1 AC4  5 PHE A 167  ARG A 168  ARG A 169  HOH A1057                    
SITE     2 AC4  5 HOH A1082                                                     
CRYST1  111.340  111.340  111.340  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      0.008981  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008981  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008981        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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