HEADER TRANSLATION, RIBOSOME 22-AUG-02 1MI6
TITLE DOCKING OF THE MODIFIED RF2 X-RAY STRUCTURE INTO THE LOW RESOLUTION
TITLE 2 CRYO-EM MAP OF RF2 E.COLI 70S RIBOSOME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEPTIDE CHAIN RELEASE FACTOR RF-2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RELEASE FACTOR 2; RF2
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12
KEYWDS RF2, RELEASE COMPLEX, CONFORMATIONAL CHANGES, TRANSLATION, RIBOSOME
EXPDTA ELECTRON MICROSCOPY
MDLTYP CA ATOMS ONLY, CHAIN A
AUTHOR U.B.S.RAWAT,A.V.ZAVIALOV,J.SENGUPTA,M.VALLE,R.A.GRASSUCCI,J.LINDE,
AUTHOR 2 B.VESTERGAARD,M.EHRENBERG,J.FRANK
REVDAT 6 14-FEB-24 1MI6 1 REMARK SEQADV
REVDAT 5 18-JUL-18 1MI6 1 REMARK
REVDAT 4 01-FEB-17 1MI6 1 AUTHOR
REVDAT 3 13-JUL-11 1MI6 1 VERSN
REVDAT 2 24-FEB-09 1MI6 1 VERSN
REVDAT 1 14-JAN-03 1MI6 0
JRNL AUTH U.B.S.RAWAT,A.V.ZAVIALOV,J.SENGUPTA,M.VALLE,R.A.GRASSUCCI,
JRNL AUTH 2 J.LINDE,B.VESTERGAARD,M.EHRENBERG,J.FRANK
JRNL TITL A CRYO-ELECTRON MICROSCOPIC STUDY OF RIBOSOME-BOUND
JRNL TITL 2 TERMINATION FACTOR RF2
JRNL REF NATURE V. 421 87 2003
JRNL REFN ISSN 0028-0836
JRNL PMID 12511960
JRNL DOI 10.1038/NATURE01224
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 TITL THE CRYSTAL STRUCTURE OF HUMAN EUKARYOTIC RELEASE FACTOR
REMARK 1 TITL 2 ERF1-MECHANISM OF STOP CODON RECOGNITION AND PEPTIDYL-TRNA
REMARK 1 TITL 3 HYDROLYSIS
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 100 311 2000
REMARK 1 REFN ISSN 0092-8674
REMARK 1 REFERENCE 2
REMARK 1 TITL BACTERIAL POLYPEPTIDE RELEASE FACTOR RF2 IS STRUCTURALLY
REMARK 1 TITL 2 DISTINCT FROM EUKARYOTIC ERF1
REMARK 1 REF MOL.CELL V. 8 1375 2001
REMARK 1 REFN ISSN 1097-2765
REMARK 2
REMARK 2 RESOLUTION. 12.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : O, SPIDER
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : 1GQE
REMARK 3 REFINEMENT SPACE : REAL
REMARK 3 REFINEMENT PROTOCOL : OTHER
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : METHOD--MANUAL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 12.80
REMARK 3 NUMBER OF PARTICLES : 18199
REMARK 3 CTF CORRECTION METHOD : NULL
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: TMV
REMARK 3
REMARK 3 OTHER DETAILS: SPIDER PACKAGE
REMARK 4
REMARK 4 1MI6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-AUG-02.
REMARK 100 THE DEPOSITION ID IS D_1000016929.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : VITREOUS ICE (CRYO EM)
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : E.COLI 70S RIBOSOME - RF2(WT)
REMARK 245 COMPLEX
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 32.00
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : RAPID-FREEZING IN LIQUID ETHANE
REMARK 245 SAMPLE BUFFER : POLYMIX BUFFER
REMARK 245 PH : 7.50
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : 08-NOV-01
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : 93.00
REMARK 245 MICROSCOPE MODEL : FEI TECNAI F20
REMARK 245 DETECTOR TYPE : KODAK SO-163 FILM
REMARK 245 MINIMUM DEFOCUS (NM) : 2500.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 4000.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : 0.00
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : 0.00
REMARK 245 NOMINAL CS : 2.00
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 2000.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 50000
REMARK 245 CALIBRATED MAGNIFICATION : 49696
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 200
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
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. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 PHE A 2
REMARK 465 GLU A 3
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GQE RELATED DB: PDB
REMARK 900 POLYPEPTIDE CHAIN RELEASE FACTOR 2 (RF2) FROM E. COLI
REMARK 900 RELATED ID: 1DT9 RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF HUMAN EUKARYOTIC RELEASE FACTOR ERF1
REMARK 900 RELATED ID: EMD-1006 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-1007 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-1008 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-1009 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-1010 RELATED DB: EMDB
DBREF 1MI6 A 1 365 UNP P07012 RF2_ECOLI 1 365
SEQADV 1MI6 ALA A 246 UNP P07012 THR 246 CONFLICT
SEQADV 1MI6 VAL A 298 UNP P07012 LEU 298 CONFLICT
SEQRES 1 A 365 MET PHE GLU ILE ASN PRO VAL ASN ASN ARG ILE GLN ASP
SEQRES 2 A 365 LEU THR GLU ARG SER ASP VAL LEU ARG GLY TYR LEU ASP
SEQRES 3 A 365 TYR ASP ALA LYS LYS GLU ARG LEU GLU GLU VAL ASN ALA
SEQRES 4 A 365 GLU LEU GLU GLN PRO ASP VAL TRP ASN GLU PRO GLU ARG
SEQRES 5 A 365 ALA GLN ALA LEU GLY LYS GLU ARG SER SER LEU GLU ALA
SEQRES 6 A 365 VAL VAL ASP THR LEU ASP GLN MET LYS GLN GLY LEU GLU
SEQRES 7 A 365 ASP VAL SER GLY LEU LEU GLU LEU ALA VAL GLU ALA ASP
SEQRES 8 A 365 ASP GLU GLU THR PHE ASN GLU ALA VAL ALA GLU LEU ASP
SEQRES 9 A 365 ALA LEU GLU GLU LYS LEU ALA GLN LEU GLU PHE ARG ARG
SEQRES 10 A 365 MET PHE SER GLY GLU TYR ASP SER ALA ASP CYS TYR LEU
SEQRES 11 A 365 ASP ILE GLN ALA GLY SER GLY GLY THR GLU ALA GLN ASP
SEQRES 12 A 365 TRP ALA SER MET LEU GLU ARG MET TYR LEU ARG TRP ALA
SEQRES 13 A 365 GLU SER ARG GLY PHE LYS THR GLU ILE ILE GLU GLU SER
SEQRES 14 A 365 GLU GLY GLU VAL ALA GLY ILE LYS SER VAL THR ILE LYS
SEQRES 15 A 365 ILE SER GLY ASP TYR ALA TYR GLY TRP LEU ARG THR GLU
SEQRES 16 A 365 THR GLY VAL HIS ARG LEU VAL ARG LYS SER PRO PHE ASP
SEQRES 17 A 365 SER GLY GLY ARG ARG HIS THR SER PHE SER SER ALA PHE
SEQRES 18 A 365 VAL TYR PRO GLU VAL ASP ASP ASP ILE ASP ILE GLU ILE
SEQRES 19 A 365 ASN PRO ALA ASP LEU ARG ILE ASP VAL TYR ARG ALA SER
SEQRES 20 A 365 GLY ALA GLY GLY GLN HIS VAL ASN ARG THR GLU SER ALA
SEQRES 21 A 365 VAL ARG ILE THR HIS ILE PRO THR GLY ILE VAL THR GLN
SEQRES 22 A 365 CYS GLN ASN ASP ARG SER GLN HIS LYS ASN LYS ASP GLN
SEQRES 23 A 365 ALA MET LYS GLN MET LYS ALA LYS LEU TYR GLU VAL GLU
SEQRES 24 A 365 MET GLN LYS LYS ASN ALA GLU LYS GLN ALA MET GLU ASP
SEQRES 25 A 365 ASN LYS SER ASP ILE GLY TRP GLY SER GLN ILE ARG SER
SEQRES 26 A 365 TYR VAL LEU ASP ASP SER ARG ILE LYS ASP LEU ARG THR
SEQRES 27 A 365 GLY VAL GLU THR ARG ASN THR GLN ALA VAL LEU ASP GLY
SEQRES 28 A 365 SER LEU ASP GLN PHE ILE GLU ALA SER LEU LYS ALA GLY
SEQRES 29 A 365 LEU
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
(ATOM LINES ARE NOT SHOWN.)
END
