Header list of 1r9k.pdb file
Complete list - 24 20 Bytes
HEADER CELL INVASION 30-OCT-03 1R9K
TITLE REPRESENTATIVE SOLUTION STRUCTURE OF THE CATALYTIC DOMAIN OF SOPE2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYPEIII-SECRETED PROTEIN EFFECTOR: INVASION-ASSOCIATED
COMPND 3 PROTEIN;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: SOPE2 GEF DOMAIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;
SOURCE 3 ORGANISM_TAXID: 99287;
SOURCE 4 STRAIN: LT2;
SOURCE 5 GENE: SOPE2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
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: PGEX-2T
KEYWDS SALMONELLA, INVASION, TYPE III, GEF, SOPE, CELL INVASION
EXPDTA SOLUTION NMR
AUTHOR C.WILLIAMS,E.E.GALYOV,S.BAGBY
REVDAT 5 24-JAN-18 1R9K 1 JRNL
REVDAT 4 21-MAR-12 1R9K 1 SCALE1 SCALE2 SCALE3
REVDAT 3 13-JUL-11 1R9K 1 VERSN
REVDAT 2 24-FEB-09 1R9K 1 VERSN
REVDAT 1 28-SEP-04 1R9K 0
JRNL AUTH C.WILLIAMS,E.E.GALYOV,S.BAGBY
JRNL TITL SOLUTION STRUCTURE, BACKBONE DYNAMICS, AND INTERACTION WITH
JRNL TITL 2 CDC42 OF SALMONELLA GUANINE NUCLEOTIDE EXCHANGE FACTOR
JRNL TITL 3 SOPE2(,).
JRNL REF BIOCHEMISTRY V. 43 11998 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15379540
JRNL DOI 10.1021/BI0490744
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.WILLIAMS
REMARK 1 TITL BIOCHEMICAL AND STRUCTURAL ANALYSIS OF SALMONELLA AND
REMARK 1 TITL 2 BURKHOLDERIA VIRULENCE PROTEINS
REMARK 1 REF TO BE PUBLISHED 2003
REMARK 1 REFN
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.WILLIAMS,E.E.GALYOV,S.BAGBY
REMARK 1 TITL ASSIGNMENT OF THE 1H,13C AND 15N RESONANCES OF THE CATALYTIC
REMARK 1 TITL 2 DOMAIN OF GUANINE NUCELOTIDE EXCHANGE FACTOR SOPE2 FROM
REMARK 1 TITL 3 SALMONELLA DUBLIN
REMARK 1 REF J.BIOMOL.NMR V. 26 379 2003
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1024057108445
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.1, XPLOR-NIH 2.06
REMARK 3 AUTHORS : DELAGLIO ET AL (NMRPIPE), SCHWIETERS ET AL (XPLOR
REMARK 3 -NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 HE STRUCTURES ARE BASED ON A TOTAL OF 3065 RESTRAINTS, 2682 ARE
REMARK 3 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 249 DIHEDRAL ANGLE RESTRAINTS,134 DISTANCE
REMARK 3 RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1R9K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000020606.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298; 298
REMARK 210 PH : 7; 7; 7
REMARK 210 IONIC STRENGTH : 0; 0; 0
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM SOPE2 U-15N,13C; 20MM HEPES
REMARK 210 BUFFER; 90% H2O, 10% D2O; 1MM
REMARK 210 SOPE2 UNLABELLED; 20MM TRIS
REMARK 210 BUFFER; 99.6% D2O; 1MM SOPE2 U-
REMARK 210 15N; 20MM HEPES BUFFER; 90% H2O,
REMARK 210 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY; HNHA
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 : SPARKY 3.1, XPLOR-NIH 2.06
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS,STRUCTURES WITH THE
REMARK 210 LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 69
REMARK 465 ASN A 70
REMARK 465 ALA A 71
REMARK 465 SER A 72
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 HZ2 LYS A 90 OG SER A 93 1.29
REMARK 500 O VAL A 83 H MET A 87 1.30
REMARK 500 HZ2 LYS A 203 OE1 GLN A 225 1.31
REMARK 500 HZ3 LYS A 133 OG SER A 240 1.31
REMARK 500 HZ3 LYS A 158 OG1 THR A 163 1.33
REMARK 500 O LEU A 212 HZ3 LYS A 215 1.35
REMARK 500 O ASN A 121 H GLN A 125 1.36
REMARK 500 HZ2 LYS A 133 O LEU A 236 1.36
REMARK 500 OG SER A 120 HZ2 LYS A 123 1.36
REMARK 500 O VAL A 205 H VAL A 209 1.38
REMARK 500 O ILE A 137 H LEU A 141 1.38
REMARK 500 HZ1 LYS A 102 OD1 ASP A 103 1.39
REMARK 500 O MET A 206 HG1 THR A 210 1.39
REMARK 500 HZ3 LYS A 97 OE2 GLU A 208 1.39
REMARK 500 O TYR A 106 HG1 THR A 110 1.40
REMARK 500 OD1 ASP A 95 HZ2 LYS A 97 1.41
REMARK 500 O VAL A 195 HZ2 LYS A 198 1.41
REMARK 500 HZ1 LYS A 207 OE1 GLU A 208 1.41
REMARK 500 O GLU A 229 H ASN A 233 1.42
REMARK 500 HZ1 LYS A 81 OD1 ASP A 85 1.42
REMARK 500 O GLN A 225 H GLU A 229 1.43
REMARK 500 OE2 GLU A 202 HZ3 LYS A 203 1.44
REMARK 500 O LEU A 129 HG SER A 132 1.45
REMARK 500 HZ3 LYS A 234 OD1 ASN A 238 1.46
REMARK 500 O ALA A 117 H ASN A 121 1.46
REMARK 500 O ILE A 177 HG SER A 181 1.47
REMARK 500 HZ2 LYS A 142 OE1 GLU A 146 1.47
REMARK 500 OE1 GLU A 156 HZ1 LYS A 158 1.47
REMARK 500 HZ1 LYS A 142 OE2 GLU A 143 1.49
REMARK 500 O VAL A 173 H ILE A 177 1.49
REMARK 500 O GLY A 74 HE ARG A 75 1.50
REMARK 500 O ASN A 99 H ASP A 103 1.53
REMARK 500 O ALA A 105 H GLN A 109 1.54
REMARK 500 O GLN A 223 HG1 THR A 227 1.55
REMARK 500 OD1 ASN A 92 HZ3 LYS A 207 1.55
REMARK 500 HD21 ASN A 190 OE1 GLN A 193 1.55
REMARK 500 O SER A 179 H LYS A 183 1.55
REMARK 500 O GLU A 146 H ASN A 150 1.56
REMARK 500 OE2 GLU A 73 HZ2 LYS A 81 1.56
REMARK 500 H LYS A 158 O VAL A 161 1.57
REMARK 500 O ILE A 228 H ILE A 231 1.58
REMARK 500 O GLU A 156 H THR A 163 1.59
REMARK 500 O PRO A 221 H GLN A 225 1.60
REMARK 500 O ASN A 238 H SER A 240 1.60
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 VAL A 77 -40.69 -134.64
REMARK 500 LEU A 78 28.82 36.79
REMARK 500 THR A 79 -176.61 -69.58
REMARK 500 SER A 80 75.57 46.41
REMARK 500 LYS A 81 91.22 79.04
REMARK 500 THR A 82 -60.01 -101.11
REMARK 500 VAL A 135 -150.03 -82.82
REMARK 500 LYS A 158 -132.50 -139.42
REMARK 500 ASN A 159 76.87 -63.30
REMARK 500 ASN A 170 102.49 71.32
REMARK 500 THR A 217 35.15 -148.80
REMARK 500 GLN A 237 -90.39 -68.57
REMARK 500 ALA A 239 -51.67 69.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 75 0.31 SIDE CHAIN
REMARK 500 ARG A 108 0.31 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5701 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFTS
DBREF 1R9K A 69 240 UNP Q9KIZ2 Q9KIZ2_SALTY 69 240
SEQRES 1 A 172 GLY ASN ALA SER GLU GLY ARG ALA VAL LEU THR SER LYS
SEQRES 2 A 172 THR VAL LYS ASP PHE MET LEU GLN LYS LEU ASN SER LEU
SEQRES 3 A 172 ASP ILE LYS GLY ASN ALA SER LYS ASP PRO ALA TYR ALA
SEQRES 4 A 172 ARG GLN THR CYS GLU ALA ILE LEU SER ALA VAL TYR SER
SEQRES 5 A 172 ASN ASN LYS ASP GLN CYS CYS LYS LEU LEU ILE SER LYS
SEQRES 6 A 172 GLY VAL SER ILE THR PRO PHE LEU LYS GLU ILE GLY GLU
SEQRES 7 A 172 ALA ALA GLN ASN ALA GLY LEU PRO GLY GLU ILE LYS ASN
SEQRES 8 A 172 GLY VAL PHE THR PRO GLY GLY ALA GLY ALA ASN PRO PHE
SEQRES 9 A 172 VAL VAL PRO LEU ILE ALA SER ALA SER ILE LYS TYR PRO
SEQRES 10 A 172 HIS MET PHE ILE ASN HIS ASN GLN GLN VAL SER PHE LYS
SEQRES 11 A 172 ALA TYR ALA GLU LYS ILE VAL MET LYS GLU VAL THR PRO
SEQRES 12 A 172 LEU PHE ASN LYS GLY THR MET PRO THR PRO GLN GLN PHE
SEQRES 13 A 172 GLN LEU THR ILE GLU ASN ILE ALA ASN LYS TYR LEU GLN
SEQRES 14 A 172 ASN ALA SER
HELIX 1 1 THR A 82 ASP A 95 1 14
HELIX 2 2 ASP A 95 ASP A 103 1 9
HELIX 3 3 ASP A 103 GLY A 134 1 32
HELIX 4 4 SER A 136 ALA A 151 1 16
HELIX 5 5 PHE A 172 TYR A 184 1 13
HELIX 6 6 TYR A 184 ILE A 189 1 6
HELIX 7 7 ASN A 192 THR A 210 1 19
HELIX 8 8 PRO A 211 ASN A 214 5 4
HELIX 9 9 THR A 220 GLN A 237 1 18
SHEET 1 A 2 GLU A 156 ILE A 157 0
SHEET 2 A 2 PHE A 162 THR A 163 -1 O THR A 163 N GLU A 156
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
Complete list - 24 20 Bytes