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- PDB-4wfd: Structure of the Rrp6-Rrp47-Mtr4 interaction -

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Basic information

Entry
Database: PDB / ID: 4wfd
TitleStructure of the Rrp6-Rrp47-Mtr4 interaction
Components
  • ATP-dependent RNA helicase DOB1
  • Exosome complex exonuclease RRP6
  • Exosome complex protein LRP1
KeywordsHYDROLASE / Rrp6-Rrp47 complex / nuclear exosome / RNA degradation / RNA processing
Function / homology
Function and homology information


nuclear mRNA surveillance of mRNA 3'-end processing / nuclear polyadenylation-dependent antisense transcript catabolic process / nuclear polyadenylation-dependent snoRNA catabolic process / nuclear polyadenylation-dependent snRNA catabolic process / TRAMP complex / U1 snRNA 3'-end processing / nuclear polyadenylation-dependent CUT catabolic process / nuclear polyadenylation-dependent mRNA catabolic process / U5 snRNA 3'-end processing / TRAMP-dependent tRNA surveillance pathway ...nuclear mRNA surveillance of mRNA 3'-end processing / nuclear polyadenylation-dependent antisense transcript catabolic process / nuclear polyadenylation-dependent snoRNA catabolic process / nuclear polyadenylation-dependent snRNA catabolic process / TRAMP complex / U1 snRNA 3'-end processing / nuclear polyadenylation-dependent CUT catabolic process / nuclear polyadenylation-dependent mRNA catabolic process / U5 snRNA 3'-end processing / TRAMP-dependent tRNA surveillance pathway / RNA fragment catabolic process / U4 snRNA 3'-end processing / nuclear polyadenylation-dependent rRNA catabolic process / poly(A)-dependent snoRNA 3'-end processing / exosome (RNase complex) / nuclear exosome (RNase complex) / exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / 3'-5' RNA helicase activity / rRNA catabolic process / post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery / histone mRNA catabolic process / nuclear mRNA surveillance / rRNA primary transcript binding / poly(A) binding / RNA catabolic process / maturation of 5.8S rRNA / Major pathway of rRNA processing in the nucleolus and cytosol / RNA processing / enzyme regulator activity / mRNA processing / double-stranded RNA binding / Hydrolases; Acting on ester bonds; Exoribonucleases producing 5'-phosphomonoesters / 3'-5'-RNA exonuclease activity / double-stranded DNA binding / regulation of gene expression / RNA helicase activity / single-stranded RNA binding / oxidoreductase activity / RNA helicase / nucleotide binding / mRNA binding / protein-containing complex binding / nucleolus / ATP hydrolysis activity / DNA binding / RNA binding / ATP binding / nucleus
Similarity search - Function
Exosome-associated factor Rrp47/DNA strand repair C1D / : / Exosome-associated factor Rrp6, N-terminal / Exosome complex exonuclease Rrp6-like / PMC2NT (NUC016) domain / rRNA-processing arch domain / Mtr4-like, beta-barrel domain / : / Exosome RNA helicase MTR4-like, stalk / ATP-dependent RNA helicase Ski2, C-terminal ...Exosome-associated factor Rrp47/DNA strand repair C1D / : / Exosome-associated factor Rrp6, N-terminal / Exosome complex exonuclease Rrp6-like / PMC2NT (NUC016) domain / rRNA-processing arch domain / Mtr4-like, beta-barrel domain / : / Exosome RNA helicase MTR4-like, stalk / ATP-dependent RNA helicase Ski2, C-terminal / ATP-dependent RNA helicase Ski2-like / DSHCT (NUC185) domain / DSHCT / Sas10/Utp3/C1D / Sas10/Utp3/C1D family / Helicase and RNase D C-terminal / HRDC domain / HRDC domain / HRDC domain profile. / HRDC domain superfamily / Prismane-like superfamily / 3'-5' exonuclease / 3'-5' exonuclease / 3'-5' exonuclease domain / HRDC-like superfamily / DEAD/DEAH box helicase / DEAD/DEAH box helicase domain / Helicase conserved C-terminal domain / helicase superfamily c-terminal domain / Superfamilies 1 and 2 helicase C-terminal domain profile. / Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. / DEAD-like helicases superfamily / Helicase, C-terminal / Helicase superfamily 1/2, ATP-binding domain / Ribonuclease H superfamily / Ribonuclease H-like superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
YTTRIUM (III) ION / Exosome complex protein LRP1 / ATP-dependent RNA helicase DOB1 / Exosome complex exonuclease RRP6
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.4 Å
AuthorsSchuch, B. / Conti, E.
Funding support Germany, 3items
OrganizationGrant numberCountry
European Research CouncilAdvanced Investigator Grant 294371
Marie CurieITN RNPnet
German Research FoundationDFG SFB646, SFB1035, GRK1721, FOR1680, CIPSM Germany
CitationJournal: Embo J. / Year: 2014
Title: The exosome-binding factors Rrp6 and Rrp47 form a composite surface for recruiting the Mtr4 helicase.
Authors: Schuch, B. / Feigenbutz, M. / Makino, D.L. / Falk, S. / Basquin, C. / Mitchell, P. / Conti, E.
History
DepositionSep 14, 2014Deposition site: RCSB / Processing site: PDBE
Revision 1.0Oct 29, 2014Provider: repository / Type: Initial release
Revision 1.1Dec 10, 2014Group: Database references
Revision 2.0Sep 6, 2017Group: Advisory / Atomic model ...Advisory / Atomic model / Author supporting evidence / Derived calculations / Refinement description
Category: atom_site / pdbx_audit_support ...atom_site / pdbx_audit_support / pdbx_struct_conn_angle / pdbx_validate_close_contact / software / struct_conn / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_seq_id / _pdbx_audit_support.funding_organization / _struct_site.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_seq_id / _struct_site_gen.auth_seq_id
Revision 3.0Jan 10, 2024Group: Atomic model / Data collection ...Atomic model / Data collection / Database references / Derived calculations / Refinement description
Category: atom_site / chem_comp_atom ...atom_site / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim
Item: _atom_site.occupancy / _database_2.pdbx_DOI ..._atom_site.occupancy / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr1_symmetry / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_symmetry / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.ptnr3_symmetry / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_conn.ptnr2_symmetry / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Exosome complex exonuclease RRP6
B: Exosome complex protein LRP1
C: ATP-dependent RNA helicase DOB1
D: Exosome complex exonuclease RRP6
E: Exosome complex protein LRP1
F: ATP-dependent RNA helicase DOB1
G: Exosome complex exonuclease RRP6
H: Exosome complex protein LRP1
I: ATP-dependent RNA helicase DOB1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)83,55531
Polymers81,5999
Non-polymers1,95622
Water2,324129
1
A: Exosome complex exonuclease RRP6
B: Exosome complex protein LRP1
C: ATP-dependent RNA helicase DOB1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)27,91111
Polymers27,2003
Non-polymers7118
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7300 Å2
ΔGint-73 kcal/mol
Surface area11110 Å2
MethodPISA
2
D: Exosome complex exonuclease RRP6
E: Exosome complex protein LRP1
F: ATP-dependent RNA helicase DOB1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)27,82210
Polymers27,2003
Non-polymers6227
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6650 Å2
ΔGint-71 kcal/mol
Surface area10470 Å2
MethodPISA
3
G: Exosome complex exonuclease RRP6
H: Exosome complex protein LRP1
I: ATP-dependent RNA helicase DOB1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)27,82210
Polymers27,2003
Non-polymers6227
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6450 Å2
ΔGint-76 kcal/mol
Surface area10220 Å2
MethodPISA
Unit cell
Length a, b, c (Å)142.745, 142.745, 63.450
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number149
Space group name H-MP312
Components on special symmetry positions
IDModelComponents
11A-204-

YT3

21A-205-

YT3

31A-206-

YT3

41B-201-

YT3

51C-101-

YT3

61D-203-

YT3

71D-204-

YT3

81E-201-

YT3

91F-101-

YT3

101H-205-

HOH

Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11chain A
21chain D
31chain G
12chain B
22chain E
32chain H
13chain F
23chain I

NCS domain segments:

Component-ID: 1

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11GLUGLUASNASNchain AAA4 - 1048 - 108
21ASPASPASNASNchain DDD7 - 10411 - 108
31PROPROASNASNchain GGG6 - 10410 - 108
12METMETSERSERchain BBB1 - 1001 - 100
22METMETASNASNchain EEE1 - 1011 - 101
32GLUGLUASPASPchain HHH2 - 942 - 94
13ASPASPGLUGLUchain FFF5 - 125 - 12
23ASPASPGLUGLUchain III5 - 125 - 12

NCS ensembles :
ID
1
2
3

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Components

#1: Protein Exosome complex exonuclease RRP6 / Ribosomal RNA-processing protein 6


Mass: 12862.192 Da / Num. of mol.: 3 / Fragment: UNP residues 1-111
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Strain: ATCC 204508 / S288c / Gene: RRP6, UNC733, YOR001W / Production host: Escherichia coli (E. coli)
References: UniProt: Q12149, Hydrolases; Acting on ester bonds; Exoribonucleases producing 5'-phosphomonoesters
#2: Protein Exosome complex protein LRP1 / / Like an rRNA processing protein 1 / Yeast C1D domain-containing protein / rRNA processing protein 47


Mass: 12023.088 Da / Num. of mol.: 3 / Fragment: UNP residues 1-103
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Strain: ATCC 204508 / S288c / Gene: LRP1, RRP47, YC1D, YHR081W / Production host: Escherichia coli (E. coli) / References: UniProt: P38801
#3: Protein/peptide ATP-dependent RNA helicase DOB1 / mRNA transport regulator MTR4


Mass: 2314.539 Da / Num. of mol.: 3 / Fragment: UNP residues 1-19 / Source method: obtained synthetically / Source: (synth.) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P47047, RNA helicase
#4: Chemical...
ChemComp-YT3 / YTTRIUM (III) ION / Yttrium


Mass: 88.906 Da / Num. of mol.: 22 / Source method: obtained synthetically / Formula: Y
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 129 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.29 Å3/Da / Density % sol: 46.22 %
Crystal growTemperature: 293.15 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: 12% PEG 1000, 0.1M imidazole pH 7.5, 0.125 M calcium acetate, 5mM yttrium chloride

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 2M-F / Detector: PIXEL / Date: Dec 22, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
Reflection twinOperator: -h,-k,l / Fraction: 0.5
ReflectionResolution: 2.4→47.42 Å / Num. obs: 56538 / % possible obs: 99.5 % / Redundancy: 17.3 % / Rmerge F obs: 1 / Rmerge(I) obs: 0.094 / Rrim(I) all: 0.095 / Χ2: 1.076 / Net I/σ(I): 25.7 / Num. measured all: 500154
Reflection shell

Diffraction-ID: 1 / Rejects: 0

Resolution (Å)Highest resolution (Å)Redundancy (%)Rmerge F obsMean I/σ(I) obsNum. measured obsNum. possibleNum. unique obsRrim(I) all% possible allRmerge(I) obs
2.4-2.4917.20.6021.779421918589391.78496.5
2.54-2.720.7952.5276761860986021.03999.90.98
2.72-2.930.8983.8469274801480070.65599.90.616
2.93-3.210.9757.9264218737473720.3141000.296
3.21-3.590.99716.8261267667766770.1431000.135
3.59-4.140.99930.8552845590859080.0721000.068
4.14-5.060.99949.5942896497849780.041000.038
5.06-7.12149.4934711389438940.0431000.04
7.12199.6618760217021600.01899.50.017

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Processing

Software
NameVersionClassification
XDSdata reduction
PHENIX(phenix.refine: 1.9_1692)refinement
Cootmodel building
XSCALEdata scaling
PHENIXphasing
RefinementMethod to determine structure: SAD
Starting model: 4wfc
Resolution: 2.4→47.42 Å / Cross valid method: FREE R-VALUE / σ(F): 1.91 / Phase error: 26.28 / Stereochemistry target values: TWIN_LSQ_F
RfactorNum. reflection% reflection
Rfree0.2426 2872 5.08 %
Rwork0.2007 53613 -
obs0.2028 56538 99.53 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 241.35 Å2 / Biso mean: 69.501 Å2 / Biso min: 35 Å2
Refinement stepCycle: final / Resolution: 2.4→47.42 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4560 0 22 129 4711
Biso mean--107.66 58.51 -
Num. residues----582
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0094604
X-RAY DIFFRACTIONf_angle_d1.296182
X-RAY DIFFRACTIONf_chiral_restr0.057723
X-RAY DIFFRACTIONf_plane_restr0.006792
X-RAY DIFFRACTIONf_dihedral_angle_d14.6071752
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A1097X-RAY DIFFRACTION9.183TORSIONAL
12D1097X-RAY DIFFRACTION9.183TORSIONAL
13G1097X-RAY DIFFRACTION9.183TORSIONAL
21B1401X-RAY DIFFRACTION9.183TORSIONAL
22E1401X-RAY DIFFRACTION9.183TORSIONAL
23H1401X-RAY DIFFRACTION9.183TORSIONAL
31F68X-RAY DIFFRACTION9.183TORSIONAL
32I68X-RAY DIFFRACTION9.183TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 20

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.3983-2.43970.29471420.3012555269789
2.4397-2.4840.32871230.29992686280996
2.484-2.53170.30491850.28932659284493
2.5317-2.58330.30141390.27892680281995
2.5833-2.63940.27351190.27742726284596
2.6394-2.70070.27891670.26692620278794
2.7007-2.76820.30741460.26772691283795
2.7682-2.84290.23941340.27322714284895
2.8429-2.92640.28711330.25192663279695
2.9264-3.02060.31611590.23742700285994
3.0206-3.12840.26591370.22192694283195
3.1284-3.25330.22481440.21912699284395
3.2533-3.40090.24221640.20652664282894
3.4009-3.57960.27961340.19312678281295
3.5796-3.8030.2481400.19042704284495
3.803-4.09520.17091440.16862684282895
4.0952-4.50470.25131540.15882677283195
4.5047-5.15040.18271350.15992685282095
5.1504-6.46610.23131450.18462714285995
6.4661-23.36320.25321240.17292720284496
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
11.4232-1.4768-0.71631.45710.78491.25250.5123-0.5445-0.45810.7981-0.4464-0.03720.34940.1101-0.00180.6106-0.0286-0.06460.54750.01150.50455.13351.304581.8423
20.07160.0961-0.00060.14310.00440.0791-0.2702-0.0783-0.0390.2718-0.373-0.7231-0.82850.03910.00090.65130.0572-0.02660.76410.02310.784224.416866.246778.7286
31.5613-1.0661-0.13711.5824-0.31992.29160.20650.03240.49130.1084-0.07420.1091-0.27190.13130.00150.5987-0.0199-0.0010.6015-0.01110.5934-4.196264.041974.3851
41.4495-0.5392-0.64191.8864-0.57472.35550.0120.1404-0.19170.1950.0894-0.07090.36380.0487-0.00030.62720.03440.00090.48910.00910.55651.283454.992475.6485
51.4467-1.19850.68431.25330.11311.8491-0.0611-0.65070.27790.51230.33190.2238-0.0248-0.1406-0.00070.9540.05630.01760.7503-0.06440.6213-8.726160.630688.1081
60.1164-0.11490.06280.1101-0.07760.04730.5399-1.7096-0.98332.2-0.155-0.03820.63530.16820.01441.0173-0.06480.01520.83070.14620.64341.144156.534590.0614
70.003-0.01550.01150.1088-0.0830.0381-0.0374-0.0131-0.0186-0.79960.41130.4854-0.2730.3817-0.00021.020.10090.08831.27410.04230.86116.35957.196390.3541
81.2188-0.8380.42471.9133-0.28441.69330.175-0.0710.07810.40140.00020.3776-0.1706-0.51470.00070.59090.01320.05970.58760.01130.5745-11.485223.005475.4623
90.1624-0.1337-0.13760.10120.07030.1698-0.66630.2441-0.5108-0.37730.02860.29890.14210.5498-0.00481.1562-0.19940.14671.0501-0.04180.699210.512216.455166.1572
101.5306-1.1812-0.61551.4003-0.29321.41050.4671-0.0315-1.02850.8513-0.2867-0.45560.55610.91940.00620.7047-0.0325-0.11210.6999-0.05840.799716.112718.756279.8357
110.4787-0.18420.53491.22641.0722.12970.13910.12740.9958-0.01450.08160.5464-0.5266-0.7561-0.00120.57710.10570.0130.62770.06810.6215-13.320329.20474.7604
120.15420.0403-0.12370.0212-0.05840.1272-0.1279-0.05520.7593-0.311-0.0998-0.9372-0.17021.0468-0.00060.589-0.03250.03510.8212-0.04160.73816.330829.593369.4102
131.3654-1.4034-0.30351.37640.46522.70690.1796-0.0735-0.26880.467-0.0592-0.14990.0921-0.24330.00050.6464-0.0299-0.02620.4758-0.01270.53952.311521.677579.7167
140.9404-0.91450.05450.9152-0.38481.45730.5404-0.6472-0.08291.1772-0.2478-0.340.07630.46910.00110.814-0.0196-0.06440.8303-0.0890.633712.386724.552588.7697
150.0606-0.0412-0.03730.0620.05230.02820.1188-1.63530.41661.95240.55260.3818-0.5903-0.16970.00930.83680.1372-0.0640.5757-0.03850.7378-1.880925.252490.1422
160.2567-0.2682-0.0740.34240.26650.3734-0.29590.71830.6151-0.57330.38660.49240.38280.1149-0.00110.83860.0654-0.12640.98740.18940.805942.110448.138676.9634
170.15160.04460.1010.3062-0.18850.05250.0668-0.0380.02170.0837-0.02520.4315-0.2262-0.02590.00010.7733-0.003-0.05760.75890.00040.814751.841356.148486.4083
181.2117-0.8967-0.31070.8607-0.24180.78350.1507-0.1825-0.2319-0.53220.274-0.691-0.2657-0.21580.00390.8028-0.0650.00910.6917-0.03150.935852.379124.865878.5668
190.1056-0.2328-0.28830.28060.29140.21690.027-0.02190.19220.26910.0228-0.1474-0.5534-0.49140.00010.73760.0717-0.01740.88040.10850.882642.252255.150783.7759
200.2018-0.0221-0.13990.12190.0460.09560.14420.3619-0.2460.305-0.10470.66411.0332-0.37870.00210.887-0.1321-0.21370.8690.17970.95741.856926.392789.2232
210.5685-0.43650.06630.3416-0.04630.8585-0.04160.18080.00410.102-0.16730.14950.08790.015-0.00010.6538-0.1008-0.04450.850.13180.79947.82837.328279.1849
220.2919-0.28120.13120.2942-0.02210.7807-0.27570.97940.0273-0.4860.7407-0.0898-0.2380.4001-0.00160.9231-0.00880.02431.01520.0830.792652.01435.493371.4144
230.1096-0.04860.05180.0192-0.00950.1051-0.75640.46310.0671-0.52360.24930.005-0.83580.3914-0.00390.97190.23030.08141.27010.19850.721146.370942.786168.5564
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 4 through 25 )A0
2X-RAY DIFFRACTION2chain 'A' and (resid 26 through 35 )A0
3X-RAY DIFFRACTION3chain 'A' and (resid 36 through 104 )A0
4X-RAY DIFFRACTION4chain 'B' and (resid 1 through 67 )B0
5X-RAY DIFFRACTION5chain 'B' and (resid 68 through 100 )B0
6X-RAY DIFFRACTION6chain 'C' and (resid 4 through 11 )C0
7X-RAY DIFFRACTION7chain 'C' and (resid 12 through 17 )C0
8X-RAY DIFFRACTION8chain 'D' and (resid 7 through 60 )D0
9X-RAY DIFFRACTION9chain 'D' and (resid 61 through 78 )D0
10X-RAY DIFFRACTION10chain 'D' and (resid 79 through 104 )D0
11X-RAY DIFFRACTION11chain 'E' and (resid 1 through 30 )E0
12X-RAY DIFFRACTION12chain 'E' and (resid 31 through 42 )E0
13X-RAY DIFFRACTION13chain 'E' and (resid 43 through 73 )E0
14X-RAY DIFFRACTION14chain 'E' and (resid 74 through 101 )E0
15X-RAY DIFFRACTION15chain 'F' and (resid 5 through 12 )F0
16X-RAY DIFFRACTION16chain 'G' and (resid 6 through 25 )G0
17X-RAY DIFFRACTION17chain 'G' and (resid 26 through 60 )G0
18X-RAY DIFFRACTION18chain 'G' and (resid 61 through 104 )G0
19X-RAY DIFFRACTION19chain 'H' and (resid 2 through 28 )H0
20X-RAY DIFFRACTION20chain 'H' and (resid 29 through 42 )H0
21X-RAY DIFFRACTION21chain 'H' and (resid 43 through 68 )H0
22X-RAY DIFFRACTION22chain 'H' and (resid 69 through 94 )H0
23X-RAY DIFFRACTION23chain 'I' and (resid 5 through 12 )I0

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