Header list of 1r6e.pdb file
Complete list - r 25 2 Bytes
HEADER CELL INVASION 15-OCT-03 1R6E
TITLE 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 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, GUANINE NUCLEOTIDE EXCHANGE FACTOR,TYPE III
KEYWDS 2 SECRETION, CELL INVASION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.WILLIAMS,E.E.GALYOV,S.BAGBY
REVDAT 3 13-JUL-11 1R6E 1 VERSN
REVDAT 2 24-FEB-09 1R6E 1 VERSN
REVDAT 1 24-SEP-04 1R6E 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 SOPE2
JRNL REF BIOCHEMISTRY V. 43 11998 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15379540
JRNL DOI 10.1021/BI0490744
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XPLOR-NIH 2.06
REMARK 3 AUTHORS : SCHWIETERS ET AL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 2931 RESTRAINTS, 2548 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 1R6E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-NOV-03.
REMARK 100 THE RCSB ID CODE IS RCSB020492.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : ~1MM U-15N,13C; 20MM HEPES
REMARK 210 BUFFER, PH 7.0, 90% H2O, 10%D2O;
REMARK 210 1MM UNLABELLED, 20MM TRIS-D11,
REMARK 210 1MM DTT-D10
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 2D
REMARK 210 NOESY; 3D_15N-SEPARATED_NOESY;
REMARK 210 HNHA; 2D TOCSY
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 3.106, XPLOR-NIH 2.02,
REMARK 210 NMRPIPE 2.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES WITH
REMARK 210 FAVORABLE NON-BOND ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE 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 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 OG SER A 120 HZ2 LYS A 123 1.28
REMARK 500 O VAL A 83 H MET A 87 1.30
REMARK 500 HZ3 LYS A 90 OG SER A 179 1.34
REMARK 500 O LEU A 212 HZ3 LYS A 215 1.34
REMARK 500 O SER A 80 HZ2 LYS A 84 1.36
REMARK 500 OE1 GLN A 125 HZ3 LYS A 128 1.36
REMARK 500 O ASN A 121 H GLN A 125 1.36
REMARK 500 HZ1 LYS A 133 O LEU A 236 1.36
REMARK 500 O ILE A 137 H LEU A 141 1.37
REMARK 500 OE1 GLU A 143 HZ1 LYS A 234 1.37
REMARK 500 HG SER A 120 O GLY A 168 1.37
REMARK 500 HZ2 LYS A 203 OE1 GLN A 225 1.38
REMARK 500 O MET A 206 HG1 THR A 210 1.38
REMARK 500 HZ3 LYS A 81 OD2 ASP A 85 1.39
REMARK 500 HZ1 LYS A 102 OD2 ASP A 103 1.39
REMARK 500 O ILE A 157 HZ1 LYS A 158 1.40
REMARK 500 O GLN A 225 H GLU A 229 1.40
REMARK 500 OD1 ASN A 92 HZ3 LYS A 207 1.41
REMARK 500 OE1 GLU A 156 HZ3 LYS A 158 1.41
REMARK 500 HZ2 LYS A 97 OE2 GLU A 208 1.41
REMARK 500 O GLN A 125 HZ2 LYS A 128 1.41
REMARK 500 HZ3 LYS A 142 OE1 GLU A 146 1.42
REMARK 500 OD1 ASN A 99 HZ2 LYS A 102 1.42
REMARK 500 HH TYR A 119 OG1 THR A 163 1.43
REMARK 500 O GLU A 229 H ASN A 233 1.43
REMARK 500 HZ2 LYS A 133 OXT SER A 240 1.43
REMARK 500 O VAL A 205 H VAL A 209 1.44
REMARK 500 O ALA A 117 H ASN A 121 1.44
REMARK 500 OD2 ASP A 124 HZ2 LYS A 198 1.45
REMARK 500 O PRO A 175 HG SER A 179 1.45
REMARK 500 OD1 ASP A 95 HZ1 LYS A 97 1.46
REMARK 500 O LEU A 129 HG SER A 132 1.46
REMARK 500 HZ2 LYS A 207 OE1 GLU A 208 1.46
REMARK 500 H2 GLU A 73 OD1 ASP A 85 1.47
REMARK 500 O LEU A 78 HG1 THR A 79 1.49
REMARK 500 HH12 ARG A 108 OE2 GLU A 112 1.51
REMARK 500 HA2 GLY A 145 HB3 ALA A 148 1.53
REMARK 500 H1 GLU A 73 OE1 GLN A 89 1.53
REMARK 500 O TYR A 106 HG1 THR A 110 1.54
REMARK 500 O ILE A 177 HG SER A 181 1.54
REMARK 500 O PRO A 221 H GLN A 225 1.54
REMARK 500 O SER A 179 H LYS A 183 1.54
REMARK 500 HB3 LEU A 130 HG12 VAL A 135 1.54
REMARK 500 O VAL A 173 H ILE A 177 1.55
REMARK 500 O GLN A 223 HG1 THR A 227 1.56
REMARK 500 O ALA A 239 HG SER A 240 1.57
REMARK 500 O GLU A 146 H ASN A 150 1.57
REMARK 500 O ILE A 228 H ILE A 231 1.58
REMARK 500 OE2 GLU A 143 HH TYR A 235 1.58
REMARK 500 HH22 ARG A 108 OE1 GLU A 112 1.58
REMARK 500
REMARK 500 THIS ENTRY HAS 942 CLOSE CONTACTS
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 1 VAL A 77 -54.54 -144.37
REMARK 500 1 LEU A 78 -76.39 62.80
REMARK 500 1 THR A 79 159.99 59.32
REMARK 500 1 SER A 80 -59.53 61.92
REMARK 500 1 THR A 82 -65.25 -102.00
REMARK 500 1 ASP A 95 62.68 35.54
REMARK 500 1 VAL A 135 -149.00 -76.71
REMARK 500 1 LYS A 158 -136.91 -149.94
REMARK 500 1 ASN A 159 75.75 -62.25
REMARK 500 1 ALA A 167 44.83 -83.64
REMARK 500 1 ALA A 169 40.11 -107.20
REMARK 500 1 ASN A 170 116.15 74.78
REMARK 500 1 LYS A 215 28.13 -75.05
REMARK 500 1 GLN A 237 -84.43 -60.20
REMARK 500 1 ALA A 239 -54.96 67.43
REMARK 500 2 ARG A 75 -69.17 -120.05
REMARK 500 2 VAL A 77 -51.47 -141.03
REMARK 500 2 THR A 79 -41.26 178.07
REMARK 500 2 THR A 82 -60.56 -103.38
REMARK 500 2 LYS A 158 -130.64 -147.27
REMARK 500 2 ASN A 159 75.19 -65.66
REMARK 500 2 ALA A 169 -79.07 -84.52
REMARK 500 2 ASN A 170 119.92 178.28
REMARK 500 2 GLN A 237 -89.29 -63.23
REMARK 500 2 ALA A 239 -58.09 69.77
REMARK 500 3 VAL A 77 -63.94 -150.14
REMARK 500 3 LEU A 78 -155.51 -162.06
REMARK 500 3 THR A 79 -35.59 168.28
REMARK 500 3 SER A 80 73.16 -62.04
REMARK 500 3 LYS A 81 76.60 57.18
REMARK 500 3 THR A 82 -61.90 -103.73
REMARK 500 3 VAL A 135 -148.27 -77.13
REMARK 500 3 LYS A 158 -139.58 -145.43
REMARK 500 3 ASN A 159 76.29 -60.84
REMARK 500 3 ALA A 169 -78.23 -99.30
REMARK 500 3 ASN A 170 116.62 -176.27
REMARK 500 3 GLN A 237 -90.78 -70.80
REMARK 500 3 ALA A 239 -53.24 69.09
REMARK 500 4 ARG A 75 -148.93 -128.11
REMARK 500 4 VAL A 77 -61.21 -142.90
REMARK 500 4 LEU A 78 -131.07 -140.48
REMARK 500 4 THR A 79 -175.15 92.10
REMARK 500 4 SER A 80 -66.31 65.84
REMARK 500 4 LYS A 81 68.14 -167.68
REMARK 500 4 ASP A 95 71.15 42.15
REMARK 500 4 VAL A 135 -147.33 -80.23
REMARK 500 4 LEU A 153 74.76 -116.30
REMARK 500 4 LYS A 158 -134.68 -138.84
REMARK 500 4 ASN A 159 76.62 -62.83
REMARK 500 4 ALA A 169 -68.04 -107.22
REMARK 500
REMARK 500 THIS ENTRY HAS 255 RAMACHANDRAN OUTLIERS.
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 1 ARG A 75 0.23 SIDE CHAIN
REMARK 500 1 ARG A 108 0.29 SIDE CHAIN
REMARK 500 2 ARG A 75 0.31 SIDE CHAIN
REMARK 500 2 ARG A 108 0.21 SIDE CHAIN
REMARK 500 3 ARG A 75 0.22 SIDE CHAIN
REMARK 500 3 ARG A 108 0.17 SIDE CHAIN
REMARK 500 4 ARG A 75 0.26 SIDE CHAIN
REMARK 500 4 ARG A 108 0.22 SIDE CHAIN
REMARK 500 5 ARG A 75 0.31 SIDE CHAIN
REMARK 500 5 ARG A 108 0.21 SIDE CHAIN
REMARK 500 6 ARG A 75 0.20 SIDE CHAIN
REMARK 500 6 ARG A 108 0.24 SIDE CHAIN
REMARK 500 7 ARG A 75 0.22 SIDE CHAIN
REMARK 500 7 ARG A 108 0.29 SIDE CHAIN
REMARK 500 8 ARG A 75 0.29 SIDE CHAIN
REMARK 500 8 ARG A 108 0.28 SIDE CHAIN
REMARK 500 9 ARG A 75 0.20 SIDE CHAIN
REMARK 500 9 ARG A 108 0.27 SIDE CHAIN
REMARK 500 10 ARG A 75 0.31 SIDE CHAIN
REMARK 500 10 ARG A 108 0.20 SIDE CHAIN
REMARK 500 11 ARG A 75 0.30 SIDE CHAIN
REMARK 500 11 ARG A 108 0.17 SIDE CHAIN
REMARK 500 12 ARG A 75 0.31 SIDE CHAIN
REMARK 500 12 ARG A 108 0.25 SIDE CHAIN
REMARK 500 13 ARG A 75 0.32 SIDE CHAIN
REMARK 500 13 ARG A 108 0.23 SIDE CHAIN
REMARK 500 14 ARG A 75 0.28 SIDE CHAIN
REMARK 500 14 ARG A 108 0.24 SIDE CHAIN
REMARK 500 15 ARG A 75 0.29 SIDE CHAIN
REMARK 500 15 ARG A 108 0.30 SIDE CHAIN
REMARK 500 16 ARG A 75 0.26 SIDE CHAIN
REMARK 500 16 ARG A 108 0.21 SIDE CHAIN
REMARK 500 17 ARG A 75 0.24 SIDE CHAIN
REMARK 500 17 ARG A 108 0.23 SIDE CHAIN
REMARK 500 18 ARG A 75 0.31 SIDE CHAIN
REMARK 500 18 ARG A 108 0.23 SIDE CHAIN
REMARK 500 19 ARG A 75 0.30 SIDE CHAIN
REMARK 500 19 ARG A 108 0.31 SIDE CHAIN
REMARK 500 20 ARG A 75 0.31 SIDE CHAIN
REMARK 500 20 ARG A 108 0.17 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5701 RELATED DB: BMRB
DBREF 1R6E A 73 240 UNP Q9KIZ2 Q9KIZ2_SALTY 73 240
SEQRES 1 A 168 GLU GLY ARG ALA VAL LEU THR SER LYS THR VAL LYS ASP
SEQRES 2 A 168 PHE MET LEU GLN LYS LEU ASN SER LEU ASP ILE LYS GLY
SEQRES 3 A 168 ASN ALA SER LYS ASP PRO ALA TYR ALA ARG GLN THR CYS
SEQRES 4 A 168 GLU ALA ILE LEU SER ALA VAL TYR SER ASN ASN LYS ASP
SEQRES 5 A 168 GLN CYS CYS LYS LEU LEU ILE SER LYS GLY VAL SER ILE
SEQRES 6 A 168 THR PRO PHE LEU LYS GLU ILE GLY GLU ALA ALA GLN ASN
SEQRES 7 A 168 ALA GLY LEU PRO GLY GLU ILE LYS ASN GLY VAL PHE THR
SEQRES 8 A 168 PRO GLY GLY ALA GLY ALA ASN PRO PHE VAL VAL PRO LEU
SEQRES 9 A 168 ILE ALA SER ALA SER ILE LYS TYR PRO HIS MET PHE ILE
SEQRES 10 A 168 ASN HIS ASN GLN GLN VAL SER PHE LYS ALA TYR ALA GLU
SEQRES 11 A 168 LYS ILE VAL MET LYS GLU VAL THR PRO LEU PHE ASN LYS
SEQRES 12 A 168 GLY THR MET PRO THR PRO GLN GLN PHE GLN LEU THR ILE
SEQRES 13 A 168 GLU ASN ILE ALA ASN LYS TYR LEU GLN 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 190 THR A 210 1 21
HELIX 8 8 PRO A 211 ASN A 214 5 4
HELIX 9 9 THR A 220 ASN A 238 1 19
SHEET 1 A 2 GLY A 155 ILE A 157 0
SHEET 2 A 2 PHE A 162 PRO A 164 -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
MODEL 1
Complete list - r 25 2 Bytes