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- PDB-1eg0: FITTING OF COMPONENTS WITH KNOWN STRUCTURE INTO AN 11.5 A CRYO-EM... -

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Entry
Database: PDB / ID: 1eg0
TitleFITTING OF COMPONENTS WITH KNOWN STRUCTURE INTO AN 11.5 A CRYO-EM MAP OF THE E.COLI 70S RIBOSOME
Components
  • (PROTEIN (RIBOSOMAL PROTEIN ...) x 3
  • FORMYL-METHIONYL-TRNA
  • FRAGMENT OF 16S RRNA HELIX 23
  • FRAGMENT OF 23S RRNA
  • HELIX 95 OF 23S RRNA
  • PROTEIN (S15 RIBOSOMAL PROTEIN)
  • PROTEIN (S17 RIBOSOMAL PROTEIN)
  • PROTEIN (S20 RIBOSOMAL PROTEIN)
  • PROTEIN (S4 RIBOSOMAL PROTEIN)
  • PROTEIN (S5 RIBOSOMAL PROTEIN)
  • PROTEIN (S6 RIBOSOMAL PROTEIN)
  • PROTEIN (S7 RIBOSOMAL PROTEIN)
  • PROTEIN (S8 RIBOSOMAL PROTEIN)
KeywordsRIBOSOME / 70S RIBOSOME / LOW RESOLUTION MODEL
Function / homology
Function and homology information


ribosomal small subunit biogenesis / large ribosomal subunit / regulation of translation / small ribosomal subunit / large ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / cytoplasmic translation / cytosolic large ribosomal subunit / tRNA binding / rRNA binding ...ribosomal small subunit biogenesis / large ribosomal subunit / regulation of translation / small ribosomal subunit / large ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / cytoplasmic translation / cytosolic large ribosomal subunit / tRNA binding / rRNA binding / ribosome / structural constituent of ribosome / ribonucleoprotein complex / translation / response to antibiotic / cytoplasm
Similarity search - Function
Ribosomal protein L1, bacterial-type / Ribosomal protein L1, conserved site / Ribosomal protein L1 signature. / Ribosomal protein L1 / Ribosomal protein L1, 3-layer alpha/beta-sandwich / Ribosomal protein L1-like / Ribosomal protein L1/ribosomal biogenesis protein / Ribosomal protein L1p/L10e family / Ribosomal protein L11, bacterial-type / Ribosomal protein L11, conserved site ...Ribosomal protein L1, bacterial-type / Ribosomal protein L1, conserved site / Ribosomal protein L1 signature. / Ribosomal protein L1 / Ribosomal protein L1, 3-layer alpha/beta-sandwich / Ribosomal protein L1-like / Ribosomal protein L1/ribosomal biogenesis protein / Ribosomal protein L1p/L10e family / Ribosomal protein L11, bacterial-type / Ribosomal protein L11, conserved site / Ribosomal protein L11 signature. / Ribosomal protein L6, conserved site / Ribosomal protein L6 signature 1. / Ribosomal protein L11, N-terminal / Ribosomal protein L11, N-terminal domain / Ribosomal protein L11/L12 / Ribosomal protein L11, C-terminal / Ribosomal protein L11, C-terminal domain superfamily / Ribosomal protein L11/L12, N-terminal domain superfamily / Ribosomal protein L11, RNA binding domain / Ribosomal protein L11/L12 / Ribosomal protein L6, bacterial-type / Ribosomal protein S6, conserved site / Ribosomal protein S6 signature. / Ribosomal protein S7, bacterial/organellar-type / Ribosomal protein S4, bacterial-type / 30S ribosomal protein S17 / Ribosomal protein S5, bacterial-type / Ribosomal protein S6, plastid/chloroplast / Ribosomal protein S15, bacterial-type / Ribosomal protein S6 / Ribosomal protein S6 / Ribosomal protein S6 superfamily / Translation elongation factor EF1B/ribosomal protein S6 / : / Ribosomal protein S5, N-terminal, conserved site / Ribosomal protein S5 signature. / Ribosomal protein S7, conserved site / Ribosomal protein S7 signature. / Ribosomal protein S5 / Ribosomal protein S17, conserved site / Ribosomal protein S17 signature. / S5 double stranded RNA-binding domain profile. / Ribosomal protein S5, N-terminal / Ribosomal protein S5, N-terminal domain / Ribosomal protein S5, C-terminal / Ribosomal protein S5, C-terminal domain / Ribosomal protein S8 signature. / Ribosomal protein L6, alpha-beta domain / Ribosomal protein L6 / Ribosomal protein L6 / Ribosomal protein S4/S9 N-terminal domain / Ribosomal protein L6, alpha-beta domain superfamily / Ribosomal protein S4, conserved site / Ribosomal protein S4 signature. / Ribosomal protein S4/S9 N-terminal domain / Ribosomal protein S4/S9, N-terminal / Ribosomal protein S15 signature. / Ribosomal protein S4/S9 / Ribosomal protein S8 / Ribosomal protein S8 superfamily / Ribosomal protein S8 / S4 RNA-binding domain profile. / S4 RNA-binding domain / S4 domain / RNA-binding S4 domain / RNA-binding S4 domain superfamily / Ribosomal protein S5/S7 / Ribosomal protein S7 domain / Ribosomal protein S7 domain superfamily / Ribosomal protein S7p/S5e / Ribosomal protein S17/S11 / Ribosomal protein S17 / Ribosomal protein S15 / Ribosomal_S15 / Ribosomal protein S15 / S15/NS1, RNA-binding / Ribosomal protein S5 domain 2-type fold, subgroup / Ribosomal protein S5 domain 2-type fold / Nucleic acid-binding, OB-fold
Similarity search - Domain/homology
: / RNA / RNA (> 10) / Small ribosomal subunit protein uS5 / Large ribosomal subunit protein uL6 / Small ribosomal subunit protein uS8 / Small ribosomal subunit protein uS7 / Small ribosomal subunit protein uS4 / Small ribosomal subunit protein uS5 / Small ribosomal subunit protein bS6 ...: / RNA / RNA (> 10) / Small ribosomal subunit protein uS5 / Large ribosomal subunit protein uL6 / Small ribosomal subunit protein uS8 / Small ribosomal subunit protein uS7 / Small ribosomal subunit protein uS4 / Small ribosomal subunit protein uS5 / Small ribosomal subunit protein bS6 / Small ribosomal subunit protein uS17 / Large ribosomal subunit protein uL1 / Large ribosomal subunit protein uL11 / Small ribosomal subunit protein uS15 / Small ribosomal subunit protein uS4 / Large ribosomal subunit protein uL6 / Small ribosomal subunit protein uS15 / Large ribosomal subunit protein uL1 / Small ribosomal subunit protein bS6
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 11.5 Å
Model detailsREFINEMENT DONE BY PROGRAMS O AND SPIDER. ALL COMPONENTS WERE FIT INTO MAP AS RIGID BODIES USING ...REFINEMENT DONE BY PROGRAMS O AND SPIDER. ALL COMPONENTS WERE FIT INTO MAP AS RIGID BODIES USING COORDINATES FROM THE REFERRED SOURCES EXCEPT FOR L1, FOR WHICH ABOUT 15-DEGREE ROTATION WAS INTRODUCED BETWEEN THE TWO DOMAINS; FITTING OF PROTEIN S17 IS RELATIVELY UNCERTAIN; CONFORMATIONAL CHANGES OF ANTICODON AND ACCEPTOR REGIONS OF TRNAFMET UPON BINDING TO THE RIBOSOME WERE NOT MODELED.
AuthorsGabashvili, I.S. / Agrawal, R.K. / Spahn, C.M.T. / Grassucci, R.A. / Svergun, D.I. / Frank, J. / Penczek, P.
Citation
Journal: Cell / Year: 2000
Title: Solution structure of the E. coli 70S ribosome at 11.5 A resolution.
Authors: I S Gabashvili / R K Agrawal / C M Spahn / R A Grassucci / D I Svergun / J Frank / P Penczek /
Abstract: Over 73,000 projections of the E. coli ribosome bound with formyl-methionyl initiator tRNAf(Met) were used to obtain an 11.5 A cryo-electron microscopy map of the complex. This map allows ...Over 73,000 projections of the E. coli ribosome bound with formyl-methionyl initiator tRNAf(Met) were used to obtain an 11.5 A cryo-electron microscopy map of the complex. This map allows identification of RNA helices, peripheral proteins, and intersubunit bridges. Comparison of double-stranded RNA regions and positions of proteins identified in both cryo-EM and X-ray maps indicates good overall agreement but points to rearrangements of ribosomal components required for the subunit association. Fitting of known components of the 50S stalk base region into the map defines the architecture of the GTPase-associated center and reveals a major change in the orientation of the alpha-sarcin-ricin loop. Analysis of the bridging connections between the subunits provides insight into the dynamic signaling mechanism between the ribosomal subunits.
#1: Journal: Embo J. / Year: 1998
Title: The Crystal Structure of Ribosomal Protein S4 Reveals a Two-Domain Molecule with an Extensive RNA-Binding Surface: One Domain Shows Structural Homology to the Ets DNA-Binding Motif
Authors: Davies, C. / Gerstner, R.B. / Draper, D.E. / Ramakrishnan, V. / White, S.W.
#2: Journal: Nature / Year: 1992
Title: The Structure of Ribosomal Protein S5 Reveals Sites of Interaction with 16S Rrna
Authors: Ramakrishnan, V. / White, S.W.
#3: Journal: Embo J. / Year: 1994
Title: Crystal Structure of the Ribosomal Protein S6 from Thermus Thermophilus
Authors: Lindahl, M. / Svensson, L.A. / Liljas, A. / Sedelnikova, I.A. / Eliseikina, I.A. / Fomenkova, N.P. / Nevskaya, N. / Nikonov, S.V. / Garber, M.B. / Muranova, T.A. / Rykonova, A.I. / Amons, R.
#4: Journal: Structure / Year: 1997
Title: The Structure of Ribosomal Protein S7 at 1.9 A Resolution Reveals a Beta- Hairpin Motif that Binds Double-Stranded Nucleic Acids
Authors: Wimberly, B.T. / White, S.W. / Ramakrishnan, V.
#5: Journal: J.Mol.Biol. / Year: 1998
Title: Crystal Structure of Ribosomal Protein S8 from Thermus Thermophilus Reveals a High Degree of Structural Conservation of a Specific RNA Binding Site
Authors: Nevskaya, N. / Tischenko, S. / Nikulin, A. / Al-Karadaghi, S. / Liljas, A. / Ehresmann, B. / Ehresmann, C. / Garber, M. / Nikonov, S.
#6: Journal: Structure / Year: 1998
Title: Conformational Variability of the N-Terminal Helix in the Structure of Ribosomal Protein S15
Authors: Clemons Jr., W.M. / Davies, C.R. / White, S.W. / Ramakrishnan, V.
#7: Journal: Biochemistry / Year: 1996
Title: Solution Structure of Prokaryotic Ribosomal Protein S17 by High-Resolution NMR Spectroscopy
Authors: Jaishree, T. / Ramakrishnan, V. / White, S.W.
#8: Journal: Nature / Year: 1999
Title: Structure of a bacterial 30S ribosomal subunit at 5.5 A resolution
Authors: Clemons Jr., W.M. / May, J.L.C. / Wimberly, B.T. / Mccutcheon, J.P. / Capel, M.S. / Ramakrishnan, V.
#9: Journal: Embo J. / Year: 1993
Title: Ribosomal Protein L6: Structural Evidence of Gene Duplication from a Primitive RNA-Binding Protein
Authors: Golden, B.L. / Davies, C. / Ramakrishnan, V. / White, S.W.
#10: Journal: Cell(Cambridge,Mass.) / Year: 1999
Title: A Detailed View of a Ribosomal Active Site: The Structure of the L11-RNA Complex
Authors: Wimberly, B.T. / Guymon, R. / Mccutcheon, J.P. / Ramakrishnan, S.W. / White, V.
#11: Journal: J.Mol.Biol. / Year: 1999
Title: The Two Faces of the Escherichia Coli 23 S Rrna Sarcin/Ricin Domain: The Structure at 1.11 A Resolution
Authors: Correll, C.C. / Wool, I.G. / Munishkin, A.
#12: Journal: Embo J. / Year: 1996
Title: Crystal Structure of the RNA Binding Ribosomal Prot L1 from Thermus Thermophilus
Authors: Nikonov, S. / Nevskaya, N. / Eliseikina, I. / Briand, C. / Al-Karadaghi, S. / Svensson, A. / Liljas, A. / Aebarson, A.
#13: Journal: Embo J. / Year: 1998
Title: Crystal Structure of Methionyl-Trnafmet Transformylase Complexed with the Initiator Formyl-Methionyl-Trnafmet
Authors: Schmitt, E. / Panvert, M. / Blanquet, S. / Mechulam, Y.
History
DepositionFeb 11, 2000Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 6, 2000Provider: repository / Type: Initial release
Revision 1.1Oct 16, 2007Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 2.0Feb 7, 2024Group: Data collection / Database references / Polymer sequence
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / em_image_scans / entity_poly / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _entity_poly.pdbx_seq_one_letter_code / _struct_ref_seq_dif.details

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Assembly

Deposited unit
I: FRAGMENT OF 16S RRNA HELIX 23
L: FRAGMENT OF 23S RRNA
M: HELIX 95 OF 23S RRNA
O: FORMYL-METHIONYL-TRNA
A: PROTEIN (S4 RIBOSOMAL PROTEIN)
B: PROTEIN (S5 RIBOSOMAL PROTEIN)
C: PROTEIN (S6 RIBOSOMAL PROTEIN)
D: PROTEIN (S7 RIBOSOMAL PROTEIN)
E: PROTEIN (S8 RIBOSOMAL PROTEIN)
F: PROTEIN (S15 RIBOSOMAL PROTEIN)
G: PROTEIN (S17 RIBOSOMAL PROTEIN)
H: PROTEIN (S20 RIBOSOMAL PROTEIN)
N: PROTEIN (RIBOSOMAL PROTEIN L1)
J: PROTEIN (RIBOSOMAL PROTEIN L6)
K: PROTEIN (RIBOSOMAL PROTEIN L11)


Theoretical massNumber of molelcules
Total (without water)224,43815
Polymers224,43815
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

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RNA chain , 4 types, 4 molecules ILMO

#1: RNA chain FRAGMENT OF 16S RRNA HELIX 23 / Coordinate model: P atoms only


Mass: 6426.170 Da / Num. of mol.: 1 / Fragment: RESIDUES 673-713 / Source method: isolated from a natural source
Details: MODELED AS ANALOGOUS FRAGMENT OF T. THERMOPHILUS TAKEN FROM PDB ENTRY 1QD7
Source: (natural) Escherichia coli (E. coli)
#2: RNA chain FRAGMENT OF 23S RRNA / Coordinate model: P atoms only


Mass: 18347.938 Da / Num. of mol.: 1 / Fragment: RESIDUES 1051-1108 / Source method: isolated from a natural source
Details: T. MARITIMA RNA SEQUENCE AND MODEL TAKEN FROM PDB ENTRY 1MMS
Source: (natural) Escherichia coli (E. coli)
#3: RNA chain HELIX 95 OF 23S RRNA / Coordinate model: P atoms only


Mass: 8438.090 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Details: E.COLI RNA SEQUENCE AND MODEL TAKEN FROM PDB ENTRY 480D
Source: (natural) Escherichia coli (E. coli)
#4: RNA chain FORMYL-METHIONYL-TRNA / FMET-TRNA / Coordinate model: P atoms only


Mass: 24526.750 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Details: E.COLI FMET-TRNA SEQUENCE AND MODEL TAKEN FROM PDB ENTRY 2FMT
Source: (natural) Escherichia coli (E. coli)

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Protein , 8 types, 8 molecules ABCDEFGH

#5: Protein PROTEIN (S4 RIBOSOMAL PROTEIN) / Coordinate model: Cα atoms only


Mass: 18624.359 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Details: MODELED BY ANALOGOUS PROTEIN OF B. STEAROTHERMOPHILUS TAKEN FROM PDB ENTRY 1C06
Source: (natural) Escherichia coli (E. coli) / References: UniProt: P81288, UniProt: P21466*PLUS
#6: Protein PROTEIN (S5 RIBOSOMAL PROTEIN) / Coordinate model: Cα atoms only


Mass: 15686.305 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Details: MODELED BY ANALOGOUS PROTEIN OF B. STEAROTHERMOPHILUS TAKEN FROM PDB ENTRY 1PKP
Source: (natural) Escherichia coli (E. coli) / References: UniProt: P02357, UniProt: P21467*PLUS
#7: Protein PROTEIN (S6 RIBOSOMAL PROTEIN) / Coordinate model: Cα atoms only


Mass: 11619.337 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Details: MODELED BY ANALOGOUS PROTEIN OF T.THERMOPHILUS TAKEN FROM PDB ENTRY 1RIS
Source: (natural) Escherichia coli (E. coli) / References: UniProt: P23370, UniProt: Q5SLP8*PLUS
#8: Protein PROTEIN (S7 RIBOSOMAL PROTEIN) / Coordinate model: Cα atoms only


Mass: 16758.543 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Details: MODELED BY ANALOGOUS PROTEIN OF T. THERMOPHILUS TAKEN FROM PDB ENTRY 1RSS
Source: (natural) Escherichia coli (E. coli) / References: UniProt: P17291
#9: Protein PROTEIN (S8 RIBOSOMAL PROTEIN) / Coordinate model: Cα atoms only


Mass: 15868.570 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Details: MODELED BY ANALOGOUS PROTEIN OF T. THERMOPHILUS TAKEN FROM PDB ENTRY 1AN7
Source: (natural) Escherichia coli (E. coli) / References: PIR: A53870, UniProt: P0DOY9*PLUS
#10: Protein PROTEIN (S15 RIBOSOMAL PROTEIN) / Coordinate model: Cα atoms only


Mass: 10578.407 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Details: MODELED BY ANALOGOUS PROTEIN OF B. STEAROTHERMOPHILUS TAKEN FROM PDB ENTRY 1A32
Source: (natural) Escherichia coli (E. coli) / References: UniProt: P80378, UniProt: Q5SJ76*PLUS
#11: Protein PROTEIN (S17 RIBOSOMAL PROTEIN) / Coordinate model: Cα atoms only


Mass: 10569.341 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Details: MODELED BY ANALOGOUS PROTEIN OF B. STEAROTHERMOPHILUS TAKEN FROM PDB ENTRIES 1RIP AND 1QD7
Source: (natural) Escherichia coli (E. coli) / References: UniProt: P23828
#12: Protein PROTEIN (S20 RIBOSOMAL PROTEIN) / Coordinate model: Cα atoms only


Mass: 8528.504 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Details: MODELED BY ANALOGOUS PROTEIN OF T. THERMOPHILUS TAKEN FROM PDB ENTRY 1QD7
Source: (natural) Escherichia coli (E. coli)

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PROTEIN (RIBOSOMAL PROTEIN ... , 3 types, 3 molecules NJK

#13: Protein PROTEIN (RIBOSOMAL PROTEIN L1) / Coordinate model: Cα atoms only


Mass: 24867.699 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Details: MODELED BY ANALOGOUS PROTEIN OF T. THERMOPHILUS TAKEN FROM PDB ENTRY 1AD2
Source: (natural) Escherichia coli (E. coli) / References: UniProt: P27150, UniProt: Q5SLP7*PLUS
#14: Protein PROTEIN (RIBOSOMAL PROTEIN L6) / Coordinate model: Cα atoms only


Mass: 18601.459 Da / Num. of mol.: 1 / Mutation: B. STEAROTHERMOPHILUS SEQUENCE AND MODEL / Source method: isolated from a natural source
Details: MODELED BY ANALOGOUS PROTEIN OF T. STEAROTHERMOPHILUS TAKEN FROM PDB ENTRY 1RL6
Source: (natural) Escherichia coli (E. coli) / References: UniProt: P02391, UniProt: Q5L408*PLUS
#15: Protein PROTEIN (RIBOSOMAL PROTEIN L11) / Coordinate model: Cα atoms only


Mass: 14996.835 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Details: MODELED BY ANALOGOUS PROTEIN OF T. MARITIMA TAKEN FROM PDB ENTRY 1MMS
Source: (natural) Escherichia coli (E. coli) / References: UniProt: P29395

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Details

Sequence detailsONLY COORDINATES OF PHOSPHATE AND CA-ATOMS ARE DEPOSITED

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: E.COLI 70S RIBOSOME / Type: RIBOSOME
Buffer solutionpH: 7.6 / Details: 20 mM Hepes, 6 mM Mg(CH3COO)2 150 mM NH4Cl, 4 mM
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationInstrument: HOMEMADE PLUNGER / Cryogen name: ETHANE
Crystal grow
*PLUS
Method: other / Details: Electron Microscopy

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Electron microscopy imaging

MicroscopyModel: FEI/PHILIPS CM200FEG/ST / Date: Jan 1, 1997
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal magnification: 50000 X / Nominal defocus max: 4340 nm / Nominal defocus min: 730 nm
Image recordingElectron dose: 10 e/Å2 / Film or detector model: KODAK SO-163 FILM
ReflectionHighest resolution: 11.5 Å

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Processing

Software
NameClassification
Omodel building
SPIDERmodel building
SPIDERphasing
SymmetryPoint symmetry: C1 (asymmetric)
3D reconstructionResolution: 11.5 Å / Num. of particles: 73523 / Symmetry type: POINT
Atomic model buildingProtocol: RIGID BODY FIT / Space: RECIPROCAL / Target criteria: VECTOR R-FACTOR
Details: REFINEMENT PROTOCOL--RIGID BODY REFINEMENT DETAILS--ALL COMPONENTS WERE FIT INTO MAP AS RIGID BODIES USING COORDINATES FROM THE REFERRED SOURCES EXCEPT FOR L1, FOR WHICH ABOUT 15-DEGREE ...Details: REFINEMENT PROTOCOL--RIGID BODY REFINEMENT DETAILS--ALL COMPONENTS WERE FIT INTO MAP AS RIGID BODIES USING COORDINATES FROM THE REFERRED SOURCES EXCEPT FOR L1, FOR WHICH ABOUT 15-DEGREE ROTATION WAS INTRODUCED BETWEEN THE TWO DOMAINS; FITTING OF PROTEIN S17 IS RELATIVELY UNCERTAIN; CONFORMATIONAL CHANGES OF ANTICODON AND ACCEPTOR REGIONS OF TRNAFMET UPON BINDING TO THE RIBOSOME WERE NOT MODELED.
RefinementHighest resolution: 11.5 Å
Details: ALL COMPONENTS WERE FIT INTO MAP AS RIGID BODIES USING COORDINATES FROM THE REFERRED SOURCES EXCEPT FOR L1, FOR WHICH ABOUT 15-DEGREE ROTATION WAS INTRODUCED BETWEEN THE TWO DOMAINS; FITTING ...Details: ALL COMPONENTS WERE FIT INTO MAP AS RIGID BODIES USING COORDINATES FROM THE REFERRED SOURCES EXCEPT FOR L1, FOR WHICH ABOUT 15-DEGREE ROTATION WAS INTRODUCED BETWEEN THE TWO DOMAINS; FITTING OF PROTEIN S17 IS RELATIVELY UNCERTAIN; CONFORMATIONAL CHANGES OF ANTICODON AND ACCEPTOR REGIONS OF TRNAFMET UPON BINDING TO THE RIBOSOME WERE NOT MODELED.
Refinement stepCycle: LAST / Highest resolution: 11.5 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1466 192 0 0 1658

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