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Database: PDB
Entry: 2H0I
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Original site: 2H0I 
HEADER    ISOMERASE                               15-MAY-06   2H0I              
TITLE     CRYSTAL STRUCTURE OF DSBG V216M MUTANT                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THIOL:DISULFIDE INTERCHANGE PROTEIN DSBG;                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 18-248;                                           
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: DSBG;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PBAD33                                    
KEYWDS    THIOREDOXIN FOLD, PERIPLASMIC DISULFIDE ISOMERASE, CHAPERONE, REDOX-  
KEYWDS   2 ACTIVE CENTER, ISOMERASE                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.HINIKER,B.HERAS,J.L.MARTIN,J.STUCKEY,J.C.A.BARDWELL                 
REVDAT   3   13-JUL-11 2H0I    1       VERSN                                    
REVDAT   2   24-FEB-09 2H0I    1       VERSN                                    
REVDAT   1   24-APR-07 2H0I    0                                                
JRNL        AUTH   A.HINIKER,B.HERAS,R.W.JOBSON,S.LAURINEC,J.L.MARTIN,          
JRNL        AUTH 2 J.STUCKEY,J.C.A.BARDWELL                                     
JRNL        TITL   SHORT-CIRCUITING DIVERGENT EVOLUTION: LABORATORY EVOLUTION   
JRNL        TITL 2 OF ONE DISULFIDE ISOMERASE TO RESEMBLE ANOTHER               
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   B.HERAS,M.A.EDELING,H.J.SCHIRRA,S.RAINA,J.L.MARTIN           
REMARK   1  TITL   CRYSTAL STRUCTURES OF THE DSBG DISULFIDE ISOMERASE REVEAL AN 
REMARK   1  TITL 2 UNSTABLE DISULFIDE.                                          
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V. 101  8876 2004              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1  PMID   15184683                                                     
REMARK   1  DOI    10.1073/PNAS.0402769101                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 20097                          
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 SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.258                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1984                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.55                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 74.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2930                       
REMARK   3   BIN FREE R VALUE                    : 0.3250                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 248                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.021                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3572                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 15                                      
REMARK   3   SOLVENT ATOMS            : 155                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.77000                                              
REMARK   3    B22 (A**2) : 3.01000                                              
REMARK   3    B33 (A**2) : -5.78000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 3.30000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.28                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.32                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.36                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.38                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.00                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.97                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 65.33                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  3  : SO4.PAR                                        
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2H0I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAY-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB037776.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-DEC-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 3.75                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9724                             
REMARK 200  MONOCHROMATOR                  : SI 220                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MX SYSTEM                          
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21710                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 76.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1V57                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG 4000, 0.1M SODIUM CITRATE,       
REMARK 280  0.2M AMMONIUM SULFATE, PH 3.75, VAPOR DIFFUSION, SITTING DROP,      
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       58.06050            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       28.60050            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       58.06050            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       28.60050            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2670 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 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      106.21483            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       83.69680            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2310 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23820 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350   BIOMT1   2 -1.000000  0.000000  0.000000      106.21483            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       83.69680            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 11700 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 40560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -102.0 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 350   BIOMT1   2 -1.000000  0.000000  0.000000      106.21483            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       83.69680            
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 292  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     GLU A     1                                                      
REMARK 465     LYS A   231                                                      
REMARK 465     HIS A   232                                                      
REMARK 465     HIS A   233                                                      
REMARK 465     HIS A   234                                                      
REMARK 465     HIS A   235                                                      
REMARK 465     HIS A   236                                                      
REMARK 465     HIS A   237                                                      
REMARK 465     GLU B     1                                                      
REMARK 465     LYS B   231                                                      
REMARK 465     HIS B   232                                                      
REMARK 465     HIS B   233                                                      
REMARK 465     HIS B   234                                                      
REMARK 465     HIS B   235                                                      
REMARK 465     HIS B   236                                                      
REMARK 465     HIS B   237                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A  139   CE   NZ                                             
REMARK 480     GLU A  141   CD   OE1  OE2                                       
REMARK 480     LYS A  153   CE   NZ                                             
REMARK 480     LYS A  208   CE   NZ                                             
REMARK 480     LYS B   95   CE                                                  
REMARK 480     LYS B  153   CD   CE   NZ                                        
REMARK 480     LYS B  208   CD   CE   NZ                                        
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    CYS B 109   CA  -  CB  -  SG  ANGL. DEV. =   7.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A  35     -122.16     66.42                                   
REMARK 500    LYS A 168        2.40    -62.40                                   
REMARK 500    PRO B   4      150.40    -48.37                                   
REMARK 500    ASP B  36       -2.50     68.54                                   
REMARK 500    LEU B 171       12.96    -67.84                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 301        DISTANCE =  5.30 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 238                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 238                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 239                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1V58   RELATED DB: PDB                                   
REMARK 900 DSBG REDUCED FORM                                                    
REMARK 900 RELATED ID: 1V57   RELATED DB: PDB                                   
REMARK 900 DSBG MIXREDOX FORM                                                   
REMARK 900 RELATED ID: 2H0G   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2H0H   RELATED DB: PDB                                   
DBREF  2H0I A    1   231  UNP    P77202   DSBG_ECOLI      18    248             
DBREF  2H0I B    1   231  UNP    P77202   DSBG_ECOLI      18    248             
SEQADV 2H0I MET A  216  UNP  P77202    VAL   233 ENGINEERED                     
SEQADV 2H0I HIS A  232  UNP  P77202              EXPRESSION TAG                 
SEQADV 2H0I HIS A  233  UNP  P77202              EXPRESSION TAG                 
SEQADV 2H0I HIS A  234  UNP  P77202              EXPRESSION TAG                 
SEQADV 2H0I HIS A  235  UNP  P77202              EXPRESSION TAG                 
SEQADV 2H0I HIS A  236  UNP  P77202              EXPRESSION TAG                 
SEQADV 2H0I HIS A  237  UNP  P77202              EXPRESSION TAG                 
SEQADV 2H0I MET B  216  UNP  P77202    VAL   233 ENGINEERED                     
SEQADV 2H0I HIS B  232  UNP  P77202              EXPRESSION TAG                 
SEQADV 2H0I HIS B  233  UNP  P77202              EXPRESSION TAG                 
SEQADV 2H0I HIS B  234  UNP  P77202              EXPRESSION TAG                 
SEQADV 2H0I HIS B  235  UNP  P77202              EXPRESSION TAG                 
SEQADV 2H0I HIS B  236  UNP  P77202              EXPRESSION TAG                 
SEQADV 2H0I HIS B  237  UNP  P77202              EXPRESSION TAG                 
SEQRES   1 A  237  GLU GLU LEU PRO ALA PRO VAL LYS ALA ILE GLU LYS GLN          
SEQRES   2 A  237  GLY ILE THR ILE ILE LYS THR PHE ASP ALA PRO GLY GLY          
SEQRES   3 A  237  MET LYS GLY TYR LEU GLY LYS TYR GLN ASP MET GLY VAL          
SEQRES   4 A  237  THR ILE TYR LEU THR PRO ASP GLY LYS HIS ALA ILE SER          
SEQRES   5 A  237  GLY TYR MET TYR ASN GLU LYS GLY GLU ASN LEU SER ASN          
SEQRES   6 A  237  THR LEU ILE GLU LYS GLU ILE TYR ALA PRO ALA GLY ARG          
SEQRES   7 A  237  GLU MET TRP GLN ARG MET GLU GLN SER HIS TRP LEU LEU          
SEQRES   8 A  237  ASP GLY LYS LYS ASP ALA PRO VAL ILE VAL TYR VAL PHE          
SEQRES   9 A  237  ALA ASP PRO PHE CYS PRO TYR CYS LYS GLN PHE TRP GLN          
SEQRES  10 A  237  GLN ALA ARG PRO TRP VAL ASP SER GLY LYS VAL GLN LEU          
SEQRES  11 A  237  ARG THR LEU LEU VAL GLY VAL ILE LYS PRO GLU SER PRO          
SEQRES  12 A  237  ALA THR ALA ALA ALA ILE LEU ALA SER LYS ASP PRO ALA          
SEQRES  13 A  237  LYS THR TRP GLN GLN TYR GLU ALA SER GLY GLY LYS LEU          
SEQRES  14 A  237  LYS LEU ASN VAL PRO ALA ASN VAL SER THR GLU GLN MET          
SEQRES  15 A  237  LYS VAL LEU SER ASP ASN GLU LYS LEU MET ASP ASP LEU          
SEQRES  16 A  237  GLY ALA ASN VAL THR PRO ALA ILE TYR TYR MET SER LYS          
SEQRES  17 A  237  GLU ASN THR LEU GLN GLN ALA MET GLY LEU PRO ASP GLN          
SEQRES  18 A  237  LYS THR LEU ASN ILE ILE MET GLY ASN LYS HIS HIS HIS          
SEQRES  19 A  237  HIS HIS HIS                                                  
SEQRES   1 B  237  GLU GLU LEU PRO ALA PRO VAL LYS ALA ILE GLU LYS GLN          
SEQRES   2 B  237  GLY ILE THR ILE ILE LYS THR PHE ASP ALA PRO GLY GLY          
SEQRES   3 B  237  MET LYS GLY TYR LEU GLY LYS TYR GLN ASP MET GLY VAL          
SEQRES   4 B  237  THR ILE TYR LEU THR PRO ASP GLY LYS HIS ALA ILE SER          
SEQRES   5 B  237  GLY TYR MET TYR ASN GLU LYS GLY GLU ASN LEU SER ASN          
SEQRES   6 B  237  THR LEU ILE GLU LYS GLU ILE TYR ALA PRO ALA GLY ARG          
SEQRES   7 B  237  GLU MET TRP GLN ARG MET GLU GLN SER HIS TRP LEU LEU          
SEQRES   8 B  237  ASP GLY LYS LYS ASP ALA PRO VAL ILE VAL TYR VAL PHE          
SEQRES   9 B  237  ALA ASP PRO PHE CYS PRO TYR CYS LYS GLN PHE TRP GLN          
SEQRES  10 B  237  GLN ALA ARG PRO TRP VAL ASP SER GLY LYS VAL GLN LEU          
SEQRES  11 B  237  ARG THR LEU LEU VAL GLY VAL ILE LYS PRO GLU SER PRO          
SEQRES  12 B  237  ALA THR ALA ALA ALA ILE LEU ALA SER LYS ASP PRO ALA          
SEQRES  13 B  237  LYS THR TRP GLN GLN TYR GLU ALA SER GLY GLY LYS LEU          
SEQRES  14 B  237  LYS LEU ASN VAL PRO ALA ASN VAL SER THR GLU GLN MET          
SEQRES  15 B  237  LYS VAL LEU SER ASP ASN GLU LYS LEU MET ASP ASP LEU          
SEQRES  16 B  237  GLY ALA ASN VAL THR PRO ALA ILE TYR TYR MET SER LYS          
SEQRES  17 B  237  GLU ASN THR LEU GLN GLN ALA MET GLY LEU PRO ASP GLN          
SEQRES  18 B  237  LYS THR LEU ASN ILE ILE MET GLY ASN LYS HIS HIS HIS          
SEQRES  19 B  237  HIS HIS HIS                                                  
HET    SO4  B 238       5                                                       
HET    SO4  A 238       5                                                       
HET    SO4  A 239       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  SO4    3(O4 S 2-)                                                   
FORMUL   6  HOH   *155(H2 O)                                                    
HELIX    1   1 PRO A    4  LYS A   12  1                                   9    
HELIX    2   2 ASN A   62  ILE A   72  1                                  11    
HELIX    3   3 TYR A   73  GLN A   86  1                                  14    
HELIX    4   4 CYS A  109  SER A  125  1                                  17    
HELIX    5   5 GLU A  141  ALA A  151  1                                  11    
HELIX    6   6 ASP A  154  SER A  165  1                                  12    
HELIX    7   7 SER A  178  ASP A  194  1                                  17    
HELIX    8   8 ASP A  220  MET A  228  1                                   9    
HELIX    9   9 PRO B    4  GLN B   13  1                                  10    
HELIX   10  10 PRO B   24  GLY B   26  5                                   3    
HELIX   11  11 ASN B   62  ILE B   72  1                                  11    
HELIX   12  12 TYR B   73  GLN B   86  1                                  14    
HELIX   13  13 CYS B  109  SER B  125  1                                  17    
HELIX   14  14 GLU B  141  ALA B  151  1                                  11    
HELIX   15  15 ASP B  154  SER B  165  1                                  12    
HELIX   16  16 SER B  178  GLY B  196  1                                  19    
HELIX   17  17 ASP B  220  MET B  228  1                                   9    
SHEET    1   A 4 THR A  16  ASP A  22  0                                        
SHEET    2   A 4 LYS A  28  TYR A  34 -1  O  LEU A  31   N  ILE A  18           
SHEET    3   A 4 MET A  37  LEU A  43 -1  O  VAL A  39   N  GLY A  32           
SHEET    4   A 4 ALA A  50  SER A  52 -1  O  ILE A  51   N  TYR A  42           
SHEET    1   B 5 LEU A  90  ASP A  92  0                                        
SHEET    2   B 5 VAL A 128  LEU A 134 -1  O  THR A 132   N  LEU A  90           
SHEET    3   B 5 VAL A  99  ALA A 105  1  N  VAL A 101   O  ARG A 131           
SHEET    4   B 5 ALA A 202  MET A 206 -1  O  TYR A 204   N  TYR A 102           
SHEET    5   B 5 LEU A 212  MET A 216 -1  O  GLN A 213   N  TYR A 205           
SHEET    1   C 4 THR B  16  ASP B  22  0                                        
SHEET    2   C 4 LYS B  28  TYR B  34 -1  O  LEU B  31   N  ILE B  18           
SHEET    3   C 4 MET B  37  LEU B  43 -1  O  ILE B  41   N  TYR B  30           
SHEET    4   C 4 ALA B  50  SER B  52 -1  O  ILE B  51   N  TYR B  42           
SHEET    1   D 5 LEU B  90  ASP B  92  0                                        
SHEET    2   D 5 VAL B 128  LEU B 134 -1  O  LEU B 130   N  ASP B  92           
SHEET    3   D 5 VAL B  99  ALA B 105  1  N  VAL B 101   O  ARG B 131           
SHEET    4   D 5 ALA B 202  MET B 206 -1  O  TYR B 204   N  TYR B 102           
SHEET    5   D 5 LEU B 212  MET B 216 -1  O  GLN B 213   N  TYR B 205           
SSBOND   1 CYS B  109    CYS B  112                          1555   1555  2.12  
CISPEP   1 THR A  200    PRO A  201          0         0.41                     
CISPEP   2 THR B  200    PRO B  201          0         1.13                     
SITE     1 AC1  2 GLU B  85  ARG B 131                                          
SITE     1 AC2  2 GLU A  85  ARG A 131                                          
SITE     1 AC3  3 HIS A  49  ASN A  57  LEU A  63                               
CRYST1  116.121   57.201   84.281  90.00  96.75  90.00 C 1 2 1       8          
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      0.008612  0.000000  0.001019        0.00000                         
SCALE2      0.000000  0.017482  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011948        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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