Header list of 1e5u.pdb file
Complete list - 25 20 Bytes
HEADER INTIMIN 02-AUG-00 1E5U TITLE NMR REPRESENTATIVE STRUCTURE OF INTIMIN-190 (INT190) FROM TITLE 2 ENTEROPATHOGENIC E. COLI COMPND MOL_ID: 1; COMPND 2 MOLECULE: INTIMIN; COMPND 3 CHAIN: I; COMPND 4 FRAGMENT: C-TERMINAL 190 RESIDUE-FRAGMENT; COMPND 5 SYNONYM: INT190; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562; SOURCE 4 STRAIN: ENTEROPATHOGENIC SEROTYPE O127\:H6; SOURCE 5 VARIANT: STRAIN E2348/69; SOURCE 6 CELL: BACTERIAL; SOURCE 7 CELLULAR_LOCATION: OUTER MEMBRANE/SURFACE; SOURCE 8 GENE: EAE; SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 11 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PET3A/PLYSS; SOURCE 13 EXPRESSION_SYSTEM_GENE: EAE [TRUNCATION]; SOURCE 14 OTHER_DETAILS: RECOMBINANT KEYWDS INTIMIN, ESCHERICHIA COLI, CELL ADHESION, OUTER MEMBRANE KEYWDS 2 PROTEIN, NMR SPECTROSCOPY EXPDTA SOLUTION NMR MDLTYP MINIMIZED AVERAGE AUTHOR S.PRASANNAN,S.J.MATTHEWS,M.BATCHELOR,S.DANIELL,S.REECE, AUTHOR 2 G.FRANKEL,G.DOUGAN,I.CONNERTON,G.BLOOMBERG REVDAT 3 24-FEB-09 1E5U 1 VERSN REVDAT 2 03-OCT-00 1E5U 1 SPRSDE ATOM REVDAT 1 16-AUG-00 1E5U 0 SPRSDE 03-OCT-00 1E5U 1E1B JRNL AUTH M.BATCHELOR,S.PRASANNAN,S.DANIELL,S.REECE, JRNL AUTH 2 I.CONNERTON,G.BLOOMBERG,G.DOUGAN,G.FRANKEL, JRNL AUTH 3 S.J.MATTHEWS JRNL TITL STRUCTURAL BASIS FOR RECOGNITION OF THE JRNL TITL 2 TRANSLOCATED INTIMIN RECEPTOR (TIR) BY INTIMIN JRNL TITL 3 FROM ENTEROPATHOGENIC E. COLI JRNL REF EMBO J. V. 19 2452 2000 JRNL REFN ISSN 0261-4189 JRNL PMID 10835344 JRNL DOI 10.1093/EMBOJ/19.11.2452 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: INT190 IS A TRUNCATION OF INT280 REMARK 3 (30KDA) WHOSE GLOBAL FOLD WAS PUBLISHED IN NATURE STRUCTURAL REMARK 3 BIOLOGY (1999) VOL.6, PP. 313-318. REMARK 4 REMARK 4 1E5U COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-AUG-00. REMARK 100 THE PDBE ID CODE IS EBI-5224. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 310 REMARK 210 PH : 5.2 REMARK 210 IONIC STRENGTH : 20 MM ACETATE REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : HSQC, TRIPLE RESONANCE, REMARK 210 15N-NOESY, 13C-NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 REMARK 210 SPECTROMETER MODEL : DRX500 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWIN-NMR, AURELIA, X-PLOR REMARK 210 METHOD USED : HYBRID TORSION ANGLE/ REMARK 210 CARTESIAN CO-ORDINATE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 15 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: REPRESENTATIVE STRUCTURE, LEAST ENERGY. RESONANCE REMARK 210 ASSIGNMENTS MADE USING TRIPLE RESONANCE EXPERIMENTS WERE REMARK 210 FOLLOWED BY COLLATION OF DISTANCE RESTRAINTS USING NOESY REMARK 210 EXPERIMENTS ON 15N,13C-LABELLED INT190 REMARK 210 EXPERIMENTS ON 15N, 13C-LABELLED INT190. ONE BOND DIPOLAR REMARK 210 COUPLINGS WERE MEASURED USING COUPLED HSQC AND TRIPLE RESONANCE REMARK 210 EXPERIMENTS. 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 400 REMARK 400 COMPOUND REMARK 400 FUNCTION: MEDIATES ADHERENCE REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT 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 ILE I 9 - HA LYS I 17 1.57 REMARK 500 O ILE I 11 - N GLY I 13 2.08 REMARK 500 CA VAL I 12 - O GLN I 29 2.19 REMARK 500 HA VAL I 12 - O GLN I 29 1.41 REMARK 500 H GLY I 37 - OG SER I 75 1.46 REMARK 500 HA SER I 45 - HG12 ILE I 70 1.45 REMARK 500 N ALA I 46 - O THR I 69 2.15 REMARK 500 HB3 MET I 95 - HB2 TYR I 182 1.48 REMARK 500 O LEU I 122 - H PHE I 126 1.58 REMARK 500 O TYR I 138 - H SER I 141 1.51 REMARK 500 H SER I 146 - O TYR I 163 1.60 REMARK 500 HD1 TRP I 147 - H TYR I 182 1.49 REMARK 500 HE1 TRP I 147 - H ASN I 180 1.58 REMARK 500 HE1 TRP I 147 - H ALA I 181 1.58 REMARK 500 H THR I 162 - O LEU I 171 1.59 REMARK 500 HA TYR I 163 - HA PRO I 170 1.56 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 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 PRO I 21 -116.47 -87.99 REMARK 500 GLN I 26 -156.70 123.04 REMARK 500 ALA I 46 -8.06 57.41 REMARK 500 ASN I 47 138.18 80.56 REMARK 500 LYS I 63 4.65 -155.87 REMARK 500 GLU I 64 109.56 167.08 REMARK 500 ASN I 77 31.28 91.09 REMARK 500 ALA I 85 -59.76 -138.03 REMARK 500 PRO I 87 -157.12 -67.95 REMARK 500 ASN I 88 70.17 74.52 REMARK 500 MET I 95 74.19 174.84 REMARK 500 ASN I 133 59.36 -150.05 REMARK 500 TYR I 135 -84.21 65.90 REMARK 500 SER I 141 74.15 -175.43 REMARK 500 GLN I 142 -42.96 -26.62 REMARK 500 GLN I 168 4.75 169.13 REMARK 500 ASN I 169 -166.83 96.54 REMARK 500 ASN I 173 85.83 88.51 REMARK 500 LYS I 175 -30.43 169.57 REMARK 500 GLU I 178 36.02 106.24 REMARK 500 SER I 179 62.67 150.27 REMARK 500 ALA I 181 -86.55 -152.63 REMARK 500 TYR I 182 176.91 160.04 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 I 44 0.31 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED. REMARK 700 REMARK 700 SHEET REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED. DBREF 1E5U I 1 187 UNP P19809 EAE1_ECOLI 753 939 SEQRES 1 I 187 THR LEU THR ILE ASP ASP GLY ASN ILE GLU ILE VAL GLY SEQRES 2 I 187 THR GLY VAL LYS GLY LYS LEU PRO THR VAL TRP LEU GLN SEQRES 3 I 187 TYR GLY GLN VAL ASN LEU LYS ALA SER GLY GLY ASN GLY SEQRES 4 I 187 LYS TYR THR TRP ARG SER ALA ASN PRO ALA ILE ALA SER SEQRES 5 I 187 VAL ASP ALA SER SER GLY GLN VAL THR LEU LYS GLU LYS SEQRES 6 I 187 GLY THR THR THR ILE SER VAL ILE SER SER ASP ASN GLN SEQRES 7 I 187 THR ALA THR TYR THR ILE ALA THR PRO ASN SER LEU ILE SEQRES 8 I 187 VAL PRO ASN MET SER LYS ARG VAL THR TYR ASN ASP ALA SEQRES 9 I 187 VAL ASN THR CYS LYS ASN PHE GLY GLY LYS LEU PRO SER SEQRES 10 I 187 SER GLN ASN GLU LEU GLU ASN VAL PHE LYS ALA TRP GLY SEQRES 11 I 187 ALA ALA ASN LYS TYR GLU TYR TYR LYS SER SER GLN THR SEQRES 12 I 187 ILE ILE SER TRP VAL GLN GLN THR ALA GLN ASP ALA LYS SEQRES 13 I 187 SER GLY VAL ALA SER THR TYR ASP LEU VAL LYS GLN ASN SEQRES 14 I 187 PRO LEU ASN ASN ILE LYS ALA SER GLU SER ASN ALA TYR SEQRES 15 I 187 ALA THR CYS VAL LYS HELIX 1 1 THR I 100 PHE I 111 1 12 HELIX 2 2 SER I 118 GLY I 130 1 13 HELIX 3 3 LYS I 134 SER I 141 5 8 HELIX 4 4 THR I 151 SER I 157 1 7 SHEET 1 A 5 VAL I 16 GLY I 18 0 SHEET 2 A 5 THR I 3 ILE I 11 -1 O ILE I 9 N GLY I 18 SHEET 3 A 5 GLN I 29 SER I 35 -1 O ASN I 31 N GLU I 10 SHEET 4 A 5 GLY I 58 THR I 61 -1 O GLY I 58 N LEU I 32 SHEET 5 A 5 SER I 52 ASP I 54 -1 O SER I 52 N THR I 61 SHEET 1 B 3 TRP I 43 ARG I 44 0 SHEET 2 B 3 THR I 68 VAL I 72 -1 O SER I 71 N ARG I 44 SHEET 3 B 3 ALA I 80 ILE I 84 -1 O ALA I 80 N VAL I 72 SHEET 1 C 2 ILE I 91 ASN I 94 0 SHEET 2 C 2 ALA I 183 VAL I 186 -1 O ALA I 183 N ASN I 94 SHEET 1 D 3 ILE I 145 VAL I 148 0 SHEET 2 D 3 ALA I 160 ASP I 164 -1 O SER I 161 N VAL I 148 SHEET 3 D 3 ASN I 169 ILE I 174 -1 O ASN I 169 N ASP I 164 SSBOND 1 CYS I 108 CYS I 185 1555 1555 2.02 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 - 25 20 Bytes