HEADER TRANSLATION INITIATION FACTOR 04-AUG-98 2IF1
TITLE HUMAN TRANSLATION INITIATION FACTOR EIF1, NMR, 29 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EIF1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SUI1;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: N-TERMINAL POLY-HISTIDINE TAG
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL_LINE: BL21;
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_PLASMID: PQE31(HIS6-EIF1)
KEYWDS TRANSLATION INITIATION FACTOR
EXPDTA SOLUTION NMR
NUMMDL 29
AUTHOR C.M.FLETCHER,C.U.T.HELLEN,T.V.PESTOVA,G.WAGNER
REVDAT 3 09-MAR-22 2IF1 1 REMARK
REVDAT 2 24-FEB-09 2IF1 1 VERSN
REVDAT 1 18-MAY-99 2IF1 0
JRNL AUTH C.M.FLETCHER,T.V.PESTOVA,C.U.HELLEN,G.WAGNER
JRNL TITL STRUCTURE AND INTERACTIONS OF THE TRANSLATION INITIATION
JRNL TITL 2 FACTOR EIF1.
JRNL REF EMBO J. V. 18 2631 1999
JRNL REFN ISSN 0261-4189
JRNL PMID 10228174
JRNL DOI 10.1093/EMBOJ/18.9.2631
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 2IF1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178240.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 400 MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 400 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.851
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 29
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOW 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: 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
DBREF 2IF1 A 14 126 UNP P41567 EIF1_HUMAN 1 113
SEQRES 1 A 126 MET ARG GLY SER HIS HIS HIS HIS HIS HIS THR ASP PRO
SEQRES 2 A 126 MET SER ALA ILE GLN ASN LEU HIS SER PHE ASP PRO PHE
SEQRES 3 A 126 ALA ASP ALA SER LYS GLY ASP ASP LEU LEU PRO ALA GLY
SEQRES 4 A 126 THR GLU ASP TYR ILE HIS ILE ARG ILE GLN GLN ARG ASN
SEQRES 5 A 126 GLY ARG LYS THR LEU THR THR VAL GLN GLY ILE ALA ASP
SEQRES 6 A 126 ASP TYR ASP LYS LYS LYS LEU VAL LYS ALA PHE LYS LYS
SEQRES 7 A 126 LYS PHE ALA CYS ASN GLY THR VAL ILE GLU HIS PRO GLU
SEQRES 8 A 126 TYR GLY GLU VAL ILE GLN LEU GLN GLY ASP GLN ARG LYS
SEQRES 9 A 126 ASN ILE CYS GLN PHE LEU VAL GLU ILE GLY LEU ALA LYS
SEQRES 10 A 126 ASP ASP GLN LEU LYS VAL HIS GLY PHE
HELIX 1 A1 LYS A 69 PHE A 80 1 12
HELIX 2 A2 ILE A 106 ILE A 113 1 8
SHEET 1 B1 5 GLN A 120 PHE A 126 0
SHEET 2 B1 5 ILE A 44 GLN A 50 1
SHEET 3 B1 5 THR A 56 GLN A 61 -1
SHEET 4 B1 5 GLU A 94 GLN A 99 -1
SHEET 5 B1 5 ASN A 83 GLU A 88 -1
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
(ATOM LINES ARE NOT SHOWN.)
END
