HEADER CELL INVASION, SIGNALING PROTEIN 14-MAR-07 2JOL
TITLE AVERAGE NMR STRUCTURE OF THE CATALYTIC DOMAIN OF GUANINE NUCLEOTIDE
TITLE 2 EXCHANGE FACTOR BOPE FROM BURKHOLDERIA PSEUDOMALLEI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE G-NUCLEOTIDE EXCHANGE FACTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 78-261;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA PSEUDOMALLEI;
SOURCE 3 ORGANISM_TAXID: 28450;
SOURCE 4 GENE: BOPE;
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: VECTOR;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PGEX
KEYWDS GUANINE NUCLEOTIDE EXCHANGE FACTOR, BURKHOLDERIA PSEUDOMALLEI, TYPE
KEYWDS 2 III SECRETION, SOPE, SOPE2, CELL INVASION, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR H.WU,A.UPADHYAY,C.WILLIAMS,E.E.GALYOV,J.M.H.VAN DEN ELSEN,S.BAGBY
REVDAT 5 20-DEC-23 2JOL 1 REMARK
REVDAT 4 09-MAR-22 2JOL 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2JOL 1 VERSN
REVDAT 2 29-APR-08 2JOL 1 JRNL
REVDAT 1 27-MAR-07 2JOL 0
SPRSDE 27-MAR-07 2JOL 2AIC
JRNL AUTH A.UPADHYAY,H.L.WU,C.WILLIAMS,T.FIELD,E.E.GALYOV,
JRNL AUTH 2 J.M.VAN DEN ELSEN,S.BAGBY
JRNL TITL THE GUANINE-NUCLEOTIDE-EXCHANGE FACTOR BOPE FROM
JRNL TITL 2 BURKHOLDERIA PSEUDOMALLEI ADOPTS A COMPACT VERSION OF THE
JRNL TITL 3 SALMONELLA SOPE/SOPE2 FOLD AND UNDERGOES A CLOSED-TO-OPEN
JRNL TITL 4 CONFORMATIONAL CHANGE UPON INTERACTION WITH CDC42
JRNL REF BIOCHEM.J. V. 411 485 2008
JRNL REFN ISSN 0264-6021
JRNL PMID 18052936
JRNL DOI 10.1042/BJ20071546
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SPARKY, X-PLOR NIH
REMARK 3 AUTHORS : GODDARD (SPARKY), SCHWIETERS, KUSZEWSKI, TJANDRA
REMARK 3 AND CLORE (X-PLOR NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2JOL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAR-07.
REMARK 100 THE DEPOSITION ID IS D_1000100093.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : 100
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.8 MM PROTEIN, 20 MM POTASSIUM
REMARK 210 PHOSPHATE, 50 MM SODIUM CHLORIDE,
REMARK 210 10 MM DTT, 1 MM BENZAMIDINE, 90%
REMARK 210 H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HSQC;
REMARK 210 2D 1H-1H TOCSY; 2D 1H-1H NOESY;
REMARK 210 3D CBCA(CO)NH; 3D C(CO)NH; 3D
REMARK 210 HNCO; 3D HNCA; 3D HNCACB; 3D
REMARK 210 HBHA(CO)NH; 3D HN(CO)CA; 3D
REMARK 210 H(CCO)NH; 3D HCCH-TOCSY; 3D HNHA;
REMARK 210 3D 1H-15N NOESY; 3D 1H-15N
REMARK 210 TOCSY; 3D 1H-13C NOESY; IPAP-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, X-PLOR NIH, TALOS
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 RES C SSSEQI
REMARK 465 GLY A 76
REMARK 465 SER A 77
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O THR A 235 HG1 THR A 239 1.48
REMARK 500 O GLU A 201 H GLN A 203 1.49
REMARK 500 O GLU A 103 H ASP A 107 1.55
REMARK 500 O ASP A 107 H GLU A 109 1.58
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 ASP A 80 84.19 -174.29
REMARK 500 ALA A 81 -16.58 -48.46
REMARK 500 ALA A 84 -78.46 -61.87
REMARK 500 ALA A 108 64.26 -64.71
REMARK 500 GLU A 109 -36.35 -145.98
REMARK 500 VAL A 141 14.67 -170.21
REMARK 500 ALA A 172 67.92 36.26
REMARK 500 ASN A 175 -41.81 143.41
REMARK 500 LEU A 202 37.61 -61.31
REMARK 500 PRO A 219 -166.62 -66.19
REMARK 500 GLU A 221 -81.13 -64.56
REMARK 500 LYS A 252 176.28 -27.55
REMARK 500 ALA A 254 -85.28 -71.77
REMARK 500 THR A 255 -61.05 -27.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5974 RELATED DB: BMRB
REMARK 900 BOPE RESONANCE ASSIGNMENTS
REMARK 900 RELATED ID: 1R6E RELATED DB: PDB
REMARK 900 NMR SOLUTION STRUCTURE OF THE CATALYTIC DOMAIN OF SOPE2
REMARK 900 RELATED ID: 1R9K RELATED DB: PDB
REMARK 900 NMR SOLUTION STRUCTURE OF THE CATALYTIC DOMAIN OF SOPE2
REMARK 900 RELATED ID: 1GZS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SOPE-CDC42 COMPLEX
REMARK 900 RELATED ID: 2JOK RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF BOPE
DBREF 2JOL A 78 261 UNP Q63K41 Q63K41_BURPS 78 261
SEQADV 2JOL GLY A 76 UNP Q63K41 CLONING ARTIFACT
SEQADV 2JOL SER A 77 UNP Q63K41 CLONING ARTIFACT
SEQRES 1 A 186 GLY SER THR GLY ASP ALA LYS GLN ALA ILE ARG HIS PHE
SEQRES 2 A 186 VAL ASP GLU ALA VAL LYS GLN VAL ALA HIS ALA ARG THR
SEQRES 3 A 186 PRO GLU ILE ARG GLN ASP ALA GLU PHE GLY ARG GLN VAL
SEQRES 4 A 186 TYR GLU ALA THR LEU CYS ALA ILE PHE SER GLU ALA LYS
SEQRES 5 A 186 ASP ARG PHE CYS MET ASP PRO ALA THR ARG ALA GLY ASN
SEQRES 6 A 186 VAL ARG PRO ALA PHE ILE GLU ALA LEU GLY ASP ALA ALA
SEQRES 7 A 186 ARG ALA THR GLY LEU PRO GLY ALA ASP LYS GLN GLY VAL
SEQRES 8 A 186 PHE THR PRO SER GLY ALA GLY THR ASN PRO LEU TYR THR
SEQRES 9 A 186 GLU ILE ARG LEU ARG ALA ASP THR LEU MET GLY ALA GLU
SEQRES 10 A 186 LEU ALA ALA ARG PRO GLU TYR ARG GLU LEU GLN PRO TYR
SEQRES 11 A 186 ALA ARG GLN GLN ALA ILE ASP LEU VAL ALA ASN ALA LEU
SEQRES 12 A 186 PRO ALA GLU ARG SER ASN THR LEU VAL GLU PHE ARG GLN
SEQRES 13 A 186 THR VAL GLN THR LEU GLU ALA THR TYR ARG ARG ALA ALA
SEQRES 14 A 186 GLN ASP ALA SER ARG ASP GLU LYS GLY ALA THR ASN ALA
SEQRES 15 A 186 ALA ASP GLY ALA
HELIX 1 1 GLN A 83 ASP A 107 1 25
HELIX 2 2 GLU A 109 ASP A 133 1 25
HELIX 3 3 PRO A 134 ARG A 137 5 4
HELIX 4 4 VAL A 141 THR A 156 1 16
HELIX 5 5 PRO A 176 GLY A 190 1 15
HELIX 6 6 ALA A 191 ARG A 196 1 6
HELIX 7 7 PRO A 197 LEU A 202 1 6
HELIX 8 8 GLN A 203 ALA A 217 1 15
HELIX 9 9 PRO A 219 LYS A 252 1 34
HELIX 10 10 LYS A 252 ALA A 258 1 7
SHEET 1 A 2 ALA A 161 LYS A 163 0
SHEET 2 A 2 VAL A 166 THR A 168 -1 O VAL A 166 N LYS A 163
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
