Header list of 1rf8.pdb file
Complete list - r 25 2 Bytes
HEADER BIOSYNTHETIC PROTEIN, TRANSLATION 07-NOV-03 1RF8
TITLE SOLUTION STRUCTURE OF THE YEAST TRANSLATION INITIATION FACTOR EIF4E IN
TITLE 2 COMPLEX WITH M7GDP AND EIF4GI RESIDUES 393 TO 490
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 4E;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: EIF4E, EIF-4E, MRNA CAP-BINDING PROTEIN, EIF-4F 25 KDA
COMPND 5 SUBUNIT;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: EUKARYOTIC INITIATION FACTOR 4F SUBUNIT P150;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: RESIDUES 391-488 (SWS:P39935);
COMPND 11 SYNONYM: EIF4F P150, EIF-4F P150, MRNA CAP-BINDING PROTEIN COMPLEX
COMPND 12 SUBUNIT P150;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: TIF45, CDC33, YOL139C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET30A;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 12 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 13 ORGANISM_TAXID: 4932;
SOURCE 14 GENE: TIF4631, YGR162W;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 17 EXPRESSION_SYSTEM_CELL_LINE: BL21;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS INITIATION FACTOR, PROTEIN BIOSYNTHESIS, TRANSLATION REGULATION,
KEYWDS 2 BIOSYNTHETIC PROTEIN, TRANSLATION
EXPDTA SOLUTION NMR
NUMMDL 11
AUTHOR J.D.GROSS,N.J.MOERKE,T.VON DER HAAR,A.A.LUGOVSKOY,A.B.SACHS,
AUTHOR 2 J.E.G.MCCARTHY,G.WAGNER
REVDAT 3 13-JUL-11 1RF8 1 VERSN
REVDAT 2 24-FEB-09 1RF8 1 VERSN
REVDAT 1 23-DEC-03 1RF8 0
JRNL AUTH J.D.GROSS,N.J.MOERKE,T.VON DER HAAR,A.A.LUGOVSKOY,A.B.SACHS,
JRNL AUTH 2 J.E.MCCARTHY,G.WAGNER
JRNL TITL RIBOSOME LOADING ONTO THE MRNA CAP IS DRIVEN BY
JRNL TITL 2 CONFORMATIONAL COUPLING BETWEEN EIF4G AND EIF4E.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 115 739 2003
JRNL REFN ISSN 0092-8674
JRNL PMID 14675538
JRNL DOI 10.1016/S0092-8674(03)00975-9
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1RF8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-DEC-03.
REMARK 100 THE RCSB ID CODE IS RCSB020694.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.6 MM 1:1:1 M7GDP/EIF4E/
REMARK 210 EIF4G(393-490) COMPLEX
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.851
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 11
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 SER B 301 H SER B 304 1.51
REMARK 500 O ILE A 78 H ILE A 81 1.51
REMARK 500 O GLN A 184 H LYS A 187 1.52
REMARK 500 O SER A 57 H ASP A 60 1.53
REMARK 500 O GLU A 103 H GLU A 107 1.57
REMARK 500 O ASP A 34 H THR B 248 1.58
REMARK 500 O TRP B 298 HG1 THR B 302 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 1 GLU A 4 96.58 -44.55
REMARK 500 1 GLU A 5 -63.56 -144.70
REMARK 500 1 VAL A 14 92.29 -65.93
REMARK 500 1 SER A 15 127.90 178.97
REMARK 500 1 ASP A 17 125.40 171.72
REMARK 500 1 ASP A 18 29.79 46.81
REMARK 500 1 THR A 19 96.98 -41.77
REMARK 500 1 THR A 20 173.08 -51.14
REMARK 500 1 ALA A 21 173.21 66.45
REMARK 500 1 THR A 22 84.63 171.60
REMARK 500 1 ASP A 29 -76.93 -79.29
REMARK 500 1 SER A 30 0.84 84.91
REMARK 500 1 ALA A 31 35.89 171.42
REMARK 500 1 HIS A 32 75.17 175.15
REMARK 500 1 ALA A 51 -43.30 -164.24
REMARK 500 1 SER A 55 4.89 -150.48
REMARK 500 1 GLU A 56 -98.52 -74.44
REMARK 500 1 SER A 57 131.91 171.62
REMARK 500 1 LEU A 62 125.99 -34.24
REMARK 500 1 VAL A 65 -138.76 -143.08
REMARK 500 1 THR A 66 109.20 -13.98
REMARK 500 1 THR A 70 -152.29 -124.55
REMARK 500 1 VAL A 71 -32.98 -141.06
REMARK 500 1 GLU A 73 -76.45 -74.57
REMARK 500 1 GLU A 83 -173.47 51.39
REMARK 500 1 HIS A 85 30.42 -167.31
REMARK 500 1 LEU A 89 -169.34 -50.52
REMARK 500 1 PHE A 96 -171.88 177.44
REMARK 500 1 ARG A 97 -25.86 146.63
REMARK 500 1 ASN A 98 -31.45 -33.22
REMARK 500 1 VAL A 100 -128.43 -128.42
REMARK 500 1 ARG A 101 -53.47 164.31
REMARK 500 1 PRO A 102 -71.97 -22.01
REMARK 500 1 GLU A 103 -166.95 156.61
REMARK 500 1 ASP A 106 -42.96 -153.19
REMARK 500 1 ALA A 110 -77.09 -81.78
REMARK 500 1 LYS A 122 -76.99 -125.06
REMARK 500 1 ALA A 124 -74.56 -144.50
REMARK 500 1 ASP A 125 33.86 -157.01
REMARK 500 1 CYS A 132 -32.58 -36.85
REMARK 500 1 ASP A 143 175.04 178.54
REMARK 500 1 GLU A 144 -64.29 75.75
REMARK 500 1 ASP A 145 -82.82 -84.29
REMARK 500 1 ASP A 146 44.68 -88.91
REMARK 500 1 ILE A 149 171.66 -42.26
REMARK 500 1 SER A 155 107.73 -161.01
REMARK 500 1 LYS A 168 -33.26 -35.28
REMARK 500 1 CYS A 169 -73.00 134.83
REMARK 500 1 GLU A 170 33.20 32.14
REMARK 500 1 ASP A 171 135.91 82.15
REMARK 500
REMARK 500 THIS ENTRY HAS 918 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTN A 320
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTN A 321
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTN A 322
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTN A 323
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE M7G A 325
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AP8 RELATED DB: PDB
REMARK 900 YEAST TRANSLATION INITATION FACTOR EIF4E IN COMPLEX WITH
REMARK 900 M7GDP
DBREF 1RF8 A 1 213 UNP P07260 IF4E_YEAST 1 213
DBREF 1RF8 B 215 314 UNP P39935 IF4F1_YEAST 391 488
SEQADV 1RF8 CYS A 120 UNP P07260 ARG 120 CONFLICT
SEQADV 1RF8 CYS A 132 UNP P07260 ARG 132 CONFLICT
SEQADV 1RF8 CYS A 169 UNP P07260 SER 169 CONFLICT
SEQADV 1RF8 CYS A 200 UNP P07260 SER 200 CONFLICT
SEQADV 1RF8 GLY B 215 UNP P39935 CLONING ARTIFACT
SEQADV 1RF8 SER B 216 UNP P39935 CLONING ARTIFACT
SEQRES 1 A 213 MET SER VAL GLU GLU VAL SER LYS LYS PHE GLU GLU ASN
SEQRES 2 A 213 VAL SER VAL ASP ASP THR THR ALA THR PRO LYS THR VAL
SEQRES 3 A 213 LEU SER ASP SER ALA HIS PHE ASP VAL LYS HIS PRO LEU
SEQRES 4 A 213 ASN THR LYS TRP THR LEU TRP TYR THR LYS PRO ALA VAL
SEQRES 5 A 213 ASP LYS SER GLU SER TRP SER ASP LEU LEU ARG PRO VAL
SEQRES 6 A 213 THR SER PHE GLN THR VAL GLU GLU PHE TRP ALA ILE ILE
SEQRES 7 A 213 GLN ASN ILE PRO GLU PRO HIS GLU LEU PRO LEU LYS SER
SEQRES 8 A 213 ASP TYR HIS VAL PHE ARG ASN ASP VAL ARG PRO GLU TRP
SEQRES 9 A 213 GLU ASP GLU ALA ASN ALA LYS GLY GLY LYS TRP SER PHE
SEQRES 10 A 213 GLN LEU CYS GLY LYS GLY ALA ASP ILE ASP GLU LEU TRP
SEQRES 11 A 213 LEU CYS THR LEU LEU ALA VAL ILE GLY GLU THR ILE ASP
SEQRES 12 A 213 GLU ASP ASP SER GLN ILE ASN GLY VAL VAL LEU SER ILE
SEQRES 13 A 213 ARG LYS GLY GLY ASN LYS PHE ALA LEU TRP THR LYS CYS
SEQRES 14 A 213 GLU ASP LYS GLU PRO LEU LEU ARG ILE GLY GLY LYS PHE
SEQRES 15 A 213 LYS GLN VAL LEU LYS LEU THR ASP ASP GLY HIS LEU GLU
SEQRES 16 A 213 PHE PHE PRO HIS CYS SER ALA ASN GLY ARG HIS PRO GLN
SEQRES 17 A 213 PRO SER ILE THR LEU
SEQRES 1 B 100 GLY SER ILE GLY LEU GLU ALA GLU ILE GLU THR THR THR
SEQRES 2 B 100 ASP GLU THR ASP ASP GLY THR ASN THR VAL SER HIS ILE
SEQRES 3 B 100 LEU ASN VAL LEU LYS ASP ALA THR PRO ILE GLU ASP VAL
SEQRES 4 B 100 PHE SER PHE ASN TYR PRO GLU GLY ILE GLU GLY PRO ASP
SEQRES 5 B 100 ILE LYS TYR LYS LYS GLU HIS VAL LYS TYR THR TYR GLY
SEQRES 6 B 100 PRO THR PHE LEU LEU GLN PHE LYS ASP LYS LEU ASN VAL
SEQRES 7 B 100 LYS ALA ASP ALA GLU TRP VAL GLN SER THR ALA SER LYS
SEQRES 8 B 100 ILE VAL ILE PRO PRO GLY MET GLY ARG
HET MTN A 320 27
HET MTN A 321 27
HET MTN A 322 27
HET MTN A 323 27
HET M7G A 325 44
HETNAM MTN S-[(1-OXYL-2,2,5,5-TETRAMETHYL-2,5-DIHYDRO-1H-PYRROL-3-
HETNAM 2 MTN YL)METHYL] METHANESULFONOTHIOATE
HETNAM M7G 7N-METHYL-8-HYDROGUANOSINE-5'-DIPHOSPHATE
HETSYN MTN MTSL
FORMUL 3 MTN 4(C10 H18 N O3 S2)
FORMUL 7 M7G C11 H19 N5 O11 P2
HELIX 1 1 THR A 25 SER A 30 1 6
HELIX 2 2 SER A 57 LEU A 62 1 6
HELIX 3 3 VAL A 71 ASN A 80 1 10
HELIX 4 4 ILE A 81 ILE A 81 5 1
HELIX 5 5 PRO A 82 GLU A 86 5 5
HELIX 6 6 ASP A 106 GLY A 112 1 7
HELIX 7 7 ASP A 125 GLU A 140 1 16
HELIX 8 8 ASP A 171 LEU A 186 1 16
HELIX 9 9 HIS A 199 ASN A 203 1 5
HELIX 10 10 THR B 236 ASP B 246 1 11
HELIX 11 11 ASP B 252 PHE B 256 5 5
HELIX 12 12 LYS B 268 GLU B 272 5 5
HELIX 13 13 GLY B 279 ASN B 291 1 13
HELIX 14 14 ALA B 296 ALA B 303 1 8
SHEET 1 A 8 ARG A 63 VAL A 65 0
SHEET 2 A 8 TRP A 43 THR A 48 -1 N LEU A 45 O VAL A 65
SHEET 3 A 8 ASP A 92 ARG A 97 -1 O PHE A 96 N THR A 44
SHEET 4 A 8 GLY A 151 SER A 155 -1 O VAL A 152 N VAL A 95
SHEET 5 A 8 ASN A 161 THR A 167 -1 O ALA A 164 N VAL A 153
SHEET 6 A 8 GLY A 113 LEU A 119 -1 N TRP A 115 O LEU A 165
SHEET 7 A 8 GLU A 195 PRO A 198 -1 O PHE A 197 N LYS A 114
SHEET 8 A 8 ILE A 211 THR A 212 -1 O ILE A 211 N PHE A 196
LINK S1 MTN A 320 SG CYS A 120 1555 1555 2.03
LINK S1 MTN A 321 SG CYS A 132 1555 1555 2.03
LINK S1 MTN A 322 SG CYS A 169 1555 1555 2.03
LINK S1 MTN A 323 SG CYS A 200 1555 1555 2.03
SITE 1 AC1 1 CYS A 120
SITE 1 AC2 3 GLU A 128 CYS A 132 LEU B 284
SITE 1 AC3 1 CYS A 169
SITE 1 AC4 2 CYS A 200 ASN A 203
SITE 1 AC5 6 TRP A 58 ASP A 92 GLU A 103 TRP A 104
SITE 2 AC5 6 GLU A 105 ARG A 157
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