GenomeNet

Database: PDB
Entry: 3BP3
LinkDB: 3BP3
Original site: 3BP3 
HEADER    TRANSFERASE                             18-DEC-07   3BP3              
TITLE     CRYSTAL STRUCTURE OF EIIB                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUCOSE-SPECIFIC PHOSPHOTRANSFERASE ENZYME IIB             
COMPND   3 COMPONENT;                                                           
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 SYNONYM: EIIB, PTS SYSTEM GLUCOSE-SPECIFIC EIIB COMPONENT;           
COMPND   6 EC: 2.7.1.69;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: PTSG, GLCA, UMG;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: B834(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PJHK                                      
KEYWDS    TRANSCRIPTION REGULATION, INNER MEMBRANE, KINASE, MEMBRANE,           
KEYWDS   2 PHOSPHOPROTEIN, PHOSPHOTRANSFERASE SYSTEM, SUGAR TRANSPORT,          
KEYWDS   3 TRANSFERASE, TRANSMEMBRANE, TRANSPORT                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.S.CHA,H.I.JUNG,Y.J.AN                                               
REVDAT   2   24-FEB-09 3BP3    1       VERSN                                    
REVDAT   1   04-NOV-08 3BP3    0                                                
JRNL        AUTH   T.W.NAM,H.I.JUNG,Y.J.AN,Y.H.PARK,S.H.LEE,Y.J.SEOK,           
JRNL        AUTH 2 S.S.CHA                                                      
JRNL        TITL   ANALYSES OF MLC-IIBGLC INTERACTION AND A PLAUSIBLE           
JRNL        TITL 2 MOLECULAR MECHANISM OF MLC INACTIVATION BY                   
JRNL        TITL 3 MEMBRANE SEQUESTRATION.                                      
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 105  3751 2008              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   18319344                                                     
JRNL        DOI    10.1073/PNAS.0709295105                                      
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 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) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.76                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 662511.410                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 19901                          
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) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.241                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1951                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
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) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1134                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 153                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.77000                                              
REMARK   3    B22 (A**2) : -2.14000                                             
REMARK   3    B33 (A**2) : 1.37000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.23                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.35                            
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) : 0.26                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.40                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.84                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
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 : FLAT MODEL                                           
REMARK   3   KSOL        : 0.36                                                 
REMARK   3   BSOL        : 51.25                                                
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3BP3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-DEC-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB045790.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-APR-06                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-5A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97884, 0.97901, 0.97121          
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19901                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.760                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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       14.47350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       14.47350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       54.09650            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       54.07450            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       54.09650            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       54.07450            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       14.47350            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       54.09650            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       54.07450            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       14.47350            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       54.09650            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       54.07450            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: MONOMERIC                         
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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 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 B 150  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     HIS A    89                                                      
REMARK 465     HIS B    89                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     THR A   8    OG1  CG2                                            
REMARK 470     ARG A  38    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  84    CG   CD   OE1  OE2                                  
REMARK 470     ASN A  88    CG   OD1  ND2                                       
REMARK 470     THR B   8    OG1  CG2                                            
REMARK 470     ARG B  38    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  84    CG   CD   OE1  OE2                                  
REMARK 470     ASN B  88    CG   OD1  ND2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B   136     O    HOH B   136     4566     2.03            
REMARK 500   O    HOH A   146     O    HOH A   146     3656     2.16            
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    CYS A  33     -131.98   -109.97                                   
REMARK 500    SER A  65       31.19    -82.76                                   
REMARK 500    CYS B  33     -131.89   -109.61                                   
REMARK 500    SER B  65       31.18    -82.79                                   
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 133        DISTANCE =  5.22 ANGSTROMS                       
REMARK 525    HOH B 150        DISTANCE =  8.24 ANGSTROMS                       
REMARK 525    HOH B 151        DISTANCE =  9.55 ANGSTROMS                       
REMARK 525    HOH B 152        DISTANCE = 13.62 ANGSTROMS                       
REMARK 525    HOH B 169        DISTANCE = 13.97 ANGSTROMS                       
REMARK 525    HOH A 163        DISTANCE =  9.94 ANGSTROMS                       
REMARK 525    HOH A 165        DISTANCE =  6.22 ANGSTROMS                       
REMARK 525    HOH A 169        DISTANCE =  6.59 ANGSTROMS                       
REMARK 525    HOH A 170        DISTANCE =  8.45 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 A 1                   
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2                   
DBREF  3BP3 A    8    89  UNP    P69786   PTGCB_ECOLI    396    477             
DBREF  3BP3 B    8    89  UNP    P69786   PTGCB_ECOLI    396    477             
SEQRES   1 A   82  THR GLY THR SER GLU MSE ALA PRO ALA LEU VAL ALA ALA          
SEQRES   2 A   82  PHE GLY GLY LYS GLU ASN ILE THR ASN LEU ASP ALA CYS          
SEQRES   3 A   82  ILE THR ARG LEU ARG VAL SER VAL ALA ASP VAL SER LYS          
SEQRES   4 A   82  VAL ASP GLN ALA GLY LEU LYS LYS LEU GLY ALA ALA GLY          
SEQRES   5 A   82  VAL VAL VAL ALA GLY SER GLY VAL GLN ALA ILE PHE GLY          
SEQRES   6 A   82  THR LYS SER ASP ASN LEU LYS THR GLU MSE ASP GLU TYR          
SEQRES   7 A   82  ILE ARG ASN HIS                                              
SEQRES   1 B   82  THR GLY THR SER GLU MSE ALA PRO ALA LEU VAL ALA ALA          
SEQRES   2 B   82  PHE GLY GLY LYS GLU ASN ILE THR ASN LEU ASP ALA CYS          
SEQRES   3 B   82  ILE THR ARG LEU ARG VAL SER VAL ALA ASP VAL SER LYS          
SEQRES   4 B   82  VAL ASP GLN ALA GLY LEU LYS LYS LEU GLY ALA ALA GLY          
SEQRES   5 B   82  VAL VAL VAL ALA GLY SER GLY VAL GLN ALA ILE PHE GLY          
SEQRES   6 B   82  THR LYS SER ASP ASN LEU LYS THR GLU MSE ASP GLU TYR          
SEQRES   7 B   82  ILE ARG ASN HIS                                              
MODRES 3BP3 MSE A   13  MET  SELENOMETHIONINE                                   
MODRES 3BP3 MSE A   82  MET  SELENOMETHIONINE                                   
MODRES 3BP3 MSE B   13  MET  SELENOMETHIONINE                                   
MODRES 3BP3 MSE B   82  MET  SELENOMETHIONINE                                   
HET    MSE  A  13       8                                                       
HET    MSE  A  82       8                                                       
HET    MSE  B  13       8                                                       
HET    MSE  B  82       8                                                       
HET    SO4  A   1       5                                                       
HET    SO4  B   2       5                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  MSE    4(C5 H11 N O2 SE)                                            
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   5  HOH   *153(H2 O)                                                    
HELIX    1   1 GLU A   12  PHE A   21  1                                  10    
HELIX    2   2 GLY A   23  GLU A   25  5                                   3    
HELIX    3   3 ASP A   43  VAL A   47  5                                   5    
HELIX    4   4 ASP A   48  LEU A   55  1                                   8    
HELIX    5   5 LYS A   74  ASN A   88  1                                  15    
HELIX    6   6 GLU B   12  PHE B   21  1                                  10    
HELIX    7   7 GLY B   23  GLU B   25  5                                   3    
HELIX    8   8 ASP B   43  VAL B   47  5                                   5    
HELIX    9   9 ASP B   48  LEU B   55  1                                   8    
HELIX   10  10 LYS B   74  ASN B   88  1                                  15    
SHEET    1   A 5 GLY A  59  ALA A  63  0                                        
SHEET    2   A 5 GLY A  66  ILE A  70 -1  O  GLN A  68   N  VAL A  61           
SHEET    3   A 5 ARG A  36  VAL A  41 -1  N  LEU A  37   O  ALA A  69           
SHEET    4   A 5 ILE A  27  ALA A  32 -1  N  ASP A  31   O  ARG A  38           
SHEET    5   A 5 THR B  10  SER B  11 -1  O  THR B  10   N  LEU A  30           
SHEET    1   B 4 ILE B  27  ALA B  32  0                                        
SHEET    2   B 4 ARG B  36  VAL B  41 -1  O  ARG B  38   N  ASP B  31           
SHEET    3   B 4 GLY B  66  ILE B  70 -1  O  ALA B  69   N  LEU B  37           
SHEET    4   B 4 GLY B  59  ALA B  63 -1  N  VAL B  61   O  GLN B  68           
LINK         C   GLU A  12                 N   MSE A  13     1555   1555  1.33  
LINK         C   MSE A  13                 N   ALA A  14     1555   1555  1.33  
LINK         C   GLU A  81                 N   MSE A  82     1555   1555  1.33  
LINK         C   MSE A  82                 N   ASP A  83     1555   1555  1.33  
LINK         C   GLU B  12                 N   MSE B  13     1555   1555  1.33  
LINK         C   MSE B  13                 N   ALA B  14     1555   1555  1.33  
LINK         C   GLU B  81                 N   MSE B  82     1555   1555  1.33  
LINK         C   MSE B  82                 N   ASP B  83     1555   1555  1.33  
SITE     1 AC1  7 CYS A  33  ILE A  34  THR A  35  ARG A  36                    
SITE     2 AC1  7 LYS A  53  HOH A  94  HOH A 140                               
SITE     1 AC2  7 CYS B  33  ILE B  34  THR B  35  ARG B  36                    
SITE     2 AC2  7 LYS B  53  HOH B 128  HOH B 129                               
CRYST1  108.193  108.149   28.947  90.00  90.00  90.00 C 2 2 21     16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009243  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009247  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.034546        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system