[English] 日本語
Yorodumi
- PDB-3nc0: Crystal structure of the HIV-1 Rev NES-CRM1-RanGTP nuclear export... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 3nc0
TitleCrystal structure of the HIV-1 Rev NES-CRM1-RanGTP nuclear export complex (crystal II)
Components
  • Exportin-1Karyopherin
  • GTP-binding nuclear protein Ran
  • Snurportin-1SPN1
KeywordsGTP-binding protein/transport protein / protein transport / GTP-binding protein-transport protein complex
Function / homology
Function and homology information


Estrogen-dependent nuclear events downstream of ESR-membrane signaling / Heme signaling / Cyclin A/B1/B2 associated events during G2/M transition / HuR (ELAVL1) binds and stabilizes mRNA / RNA import into nucleus / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / Deactivation of the beta-catenin transactivating complex / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Resolution of Sister Chromatid Cohesion ...Estrogen-dependent nuclear events downstream of ESR-membrane signaling / Heme signaling / Cyclin A/B1/B2 associated events during G2/M transition / HuR (ELAVL1) binds and stabilizes mRNA / RNA import into nucleus / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / Deactivation of the beta-catenin transactivating complex / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Resolution of Sister Chromatid Cohesion / annulate lamellae / regulation of proteasomal ubiquitin-dependent protein catabolic process / RHO GTPases Activate Formins / Separation of Sister Chromatids / RNA cap binding / regulation of centrosome duplication / MAPK6/MAPK4 signaling / RNA nuclear export complex / nuclear export signal receptor activity / pre-miRNA export from nucleus / snRNA import into nucleus / cellular response to mineralocorticoid stimulus / manchette / Regulation of cholesterol biosynthesis by SREBP (SREBF) / importin-alpha family protein binding / NLS-dependent protein nuclear import complex / regulation of protein export from nucleus / protein localization to nucleolus / Rev-mediated nuclear export of HIV RNA / Nuclear import of Rev protein / NEP/NS2 Interacts with the Cellular Export Machinery / tRNA processing in the nucleus / GTP metabolic process / Postmitotic nuclear pore complex (NPC) reformation / nucleocytoplasmic transport / MicroRNA (miRNA) biogenesis / nuclear import signal receptor activity / DNA metabolic process / dynein intermediate chain binding / ribosomal subunit export from nucleus / regulation of protein catabolic process / spermatid development / mitotic sister chromatid segregation / ribosomal small subunit export from nucleus / protein localization to nucleus / ribosomal large subunit export from nucleus / sperm flagellum / Cajal body / mRNA export from nucleus / nuclear pore / protein export from nucleus / centriole / viral process / mitotic spindle organization / G protein activity / male germ cell nucleus / hippocampus development / Transcriptional regulation by small RNAs / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / kinetochore / recycling endosome / small GTPase binding / positive regulation of protein import into nucleus / protein import into nucleus / GDP binding / melanosome / ribosome biogenesis / mitotic cell cycle / nuclear envelope / snRNP Assembly / positive regulation of protein binding / midbody / actin cytoskeleton organization / nuclear membrane / DNA-binding transcription factor binding / cadherin binding / ribonucleoprotein complex / protein heterodimerization activity / cell division / protein domain specific binding / intracellular membrane-bounded organelle / GTPase activity / chromatin binding / chromatin / GTP binding / nucleolus / negative regulation of transcription by RNA polymerase II / magnesium ion binding / protein-containing complex / RNA binding / extracellular exosome / nucleoplasm / membrane / nucleus / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Snurportin-1 / Snurportin-1, N-terminal / : / Snurportin1 / Exportin-1, C-terminal / Exportin-1, repeat 3 / Chromosome region maintenance repeat / Exportin-1, repeat 2 / CRM1 C terminal / Chromosome region maintenance or exportin repeat ...Snurportin-1 / Snurportin-1, N-terminal / : / Snurportin1 / Exportin-1, C-terminal / Exportin-1, repeat 3 / Chromosome region maintenance repeat / Exportin-1, repeat 2 / CRM1 C terminal / Chromosome region maintenance or exportin repeat / CRM1 / Exportin repeat 2 / CRM1 / Exportin repeat 3 / CRM1 C terminal / DNA ligase/mRNA capping enzyme / Exportin-1/5 / Exportin-1/Importin-beta-like / Exportin 1-like protein / small GTPase Ran family profile. / Ran GTPase / Importin-beta N-terminal domain profile. / Importin-beta N-terminal domain / Importin-beta N-terminal domain / Importin-beta, N-terminal domain / Importin-alpha, importin-beta-binding domain / IBB domain profile. / D-amino Acid Aminotransferase; Chain A, domain 1 / Ran (Ras-related nuclear proteins) /TC4 subfamily of small GTPases / Rho (Ras homology) subfamily of Ras-like small GTPases / Ras subfamily of RAS small GTPases / Small GTPase / Ras family / Rab subfamily of small GTPases / Armadillo-like helical / Small GTP-binding protein domain / Armadillo-type fold / P-loop containing nucleotide triphosphate hydrolases / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
GUANOSINE-5'-TRIPHOSPHATE / PHENOL / DI(HYDROXYETHYL)ETHER / Snurportin-1 / GTP-binding nuclear protein Ran / Exportin-1
Similarity search - Component
Biological speciesMus musculus (house mouse)
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 2.9 Å
AuthorsGuttler, T. / Madl, T. / Neumann, P. / Deichsel, D. / Corsini, L. / Monecke, T. / Ficner, R. / Sattler, M. / Gorlich, D.
CitationJournal: Nat.Struct.Mol.Biol. / Year: 2010
Title: NES consensus redefined by structures of PKI-type and Rev-type nuclear export signals bound to CRM1.
Authors: Guttler, T. / Madl, T. / Neumann, P. / Deichsel, D. / Corsini, L. / Monecke, T. / Ficner, R. / Sattler, M. / Gorlich, D.
History
DepositionJun 4, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 27, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Oct 6, 2021Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_conn_angle ...database_2 / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._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.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _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.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_label_asym_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.3Sep 6, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Exportin-1
B: Snurportin-1
C: GTP-binding nuclear protein Ran
D: Exportin-1
E: Snurportin-1
F: GTP-binding nuclear protein Ran
hetero molecules


Theoretical massNumber of molelcules
Total (without water)373,36733
Polymers369,9836
Non-polymers3,38327
Water11,331629
1
A: Exportin-1
B: Snurportin-1
C: GTP-binding nuclear protein Ran
D: Exportin-1
F: GTP-binding nuclear protein Ran
hetero molecules


Theoretical massNumber of molelcules
Total (without water)331,64429
Polymers328,5515
Non-polymers3,09324
Water905
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area14470 Å2
ΔGint-23 kcal/mol
Surface area67850 Å2
MethodPISA
2
A: Exportin-1
B: Snurportin-1
C: GTP-binding nuclear protein Ran
D: Exportin-1
E: Snurportin-1
F: GTP-binding nuclear protein Ran
hetero molecules


Theoretical massNumber of molelcules
Total (without water)373,26132
Polymers369,9836
Non-polymers3,27726
Water1086
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area14600 Å2
ΔGint-21 kcal/mol
Surface area68120 Å2
MethodPISA
Unit cell
Length a, b, c (Å)73.262, 225.895, 163.984
Angle α, β, γ (deg.)90.00, 100.75, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(0.999998, -0.00154, -0.001355), (-0.001541, -0.999999, -0.000523), (-0.001354, 0.000525, -0.999999)36.447399, -214.190002, -5.11945
2given(0.999997, 0.001843, 0.001709), (0.001838, -0.999994, 0.002936), (0.001714, -0.002932, -0.999994)36.899799, -214.149002, -5.64844
3given(0.999996, -0.002075, -0.002152), (-0.002076, -0.999998, -0.000646), (-0.002151, 0.00065, -0.999997)36.401901, -214.162994, -5.09039

-
Components

-
Protein , 3 types, 6 molecules ADBECF

#1: Protein Exportin-1 / Karyopherin / Exp1 / Chromosome region maintenance 1 protein homolog


Mass: 123367.234 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Crm1, Xpo1, Xpo1 (GeneID: 103573) / Production host: Escherichia coli (E. coli) / Strain (production host): BLR / References: UniProt: Q6P5F9
#2: Protein Snurportin-1 / SPN1 / RNA U transporter 1


Mass: 41431.902 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Strain: rev isolate D.ZA.85.R286 / Gene: SNUPN (GeneID: 10073), RNUT1, SNUPN, SPN1 / Production host: Escherichia coli (E. coli) / Strain (production host): BLR / References: UniProt: O95149
#3: Protein GTP-binding nuclear protein Ran / GTPase Ran / Ras-related nuclear protein / Ras-like protein TC4 / Androgen receptor-associated protein 24


Mass: 20192.484 Da / Num. of mol.: 2 / Mutation: Q69L
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ARA24, OK/SW-cl.81, RAN, RAN (GeneID: 5901) / Production host: Escherichia coli (E. coli) / Strain (production host): BLR / References: UniProt: P62826

-
Non-polymers , 6 types, 656 molecules

#4: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C3H8O3
#5: Chemical
ChemComp-PEG / DI(HYDROXYETHYL)ETHER / Diethylene glycol


Mass: 106.120 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: C4H10O3
#6: Chemical ChemComp-IPH / PHENOL / Phenol


Mass: 94.111 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H6O
#7: Chemical ChemComp-GTP / GUANOSINE-5'-TRIPHOSPHATE / Guanosine triphosphate


Mass: 523.180 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H16N5O14P3 / Comment: GTP, energy-carrying molecule*YM
#8: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#9: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 629 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 3.6 Å3/Da / Density % sol: 65.86 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.8
Details: 0.1 M Tris/HCl, 16% (w/v) PEG 1000, 2 mM phenol, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-2 / Wavelength: 0.8726 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Oct 10, 2009 / Details: mirrors
RadiationMonochromator: YALE MIRRORS / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.8726 Å / Relative weight: 1
ReflectionHighest resolution: 2.9 Å / Num. obs: 110353 / % possible obs: 95.4 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 37.846 Å2 / Rmerge F obs: 0.171 / Rmerge(I) obs: 0.143 / Rrim(I) all: 0.162 / Net I/σ(I): 8.97 / Num. measured all: 465206

-
Processing

Software
NameVersionClassificationNB
XSCALEdata processing
PHENIX1.6.1_357refinement
PDB_EXTRACT3.1data extraction
MAR345dtbdata collection
XDSdata reduction
XSCALEdata scaling
CNSphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: 3GJX
Resolution: 2.9→39.046 Å / Occupancy max: 1 / Occupancy min: 0.5 / SU ML: 0.43 / Isotropic thermal model: Isotropic / σ(F): 1.36 / Phase error: 30.09 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2947 5516 5 %
Rwork0.2421 --
obs0.2448 110315 95.46 %
all-115337 -
Solvent computationShrinkage radii: 0.8 Å / VDW probe radii: 1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 42.078 Å2 / ksol: 0.307 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1--7.9178 Å20 Å20.7153 Å2
2--0.7669 Å2-0 Å2
3----0.1102 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.43 Å0.39 Å
Luzzati d res low-8 Å
Luzzati sigma a0.43 Å0.4 Å
Refinement stepCycle: LAST / Resolution: 2.9→39.046 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms24325 0 217 629 25171
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00325108
X-RAY DIFFRACTIONf_angle_d0.74733958
X-RAY DIFFRACTIONf_dihedral_angle_d16.1039373
X-RAY DIFFRACTIONf_chiral_restr0.0553805
X-RAY DIFFRACTIONf_plane_restr0.0034297
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.9-2.93290.37781580.31122999X-RAY DIFFRACTION81
2.9329-2.96740.30851540.29942927X-RAY DIFFRACTION81
2.9674-3.00360.38431530.29132913X-RAY DIFFRACTION81
3.0036-3.04160.36771580.28683005X-RAY DIFFRACTION81
3.0416-3.08160.34911540.28122919X-RAY DIFFRACTION81
3.0816-3.12380.32341540.27092935X-RAY DIFFRACTION81
3.1238-3.16840.33231700.25383223X-RAY DIFFRACTION87
3.1684-3.21570.3151900.26193631X-RAY DIFFRACTION100
3.2157-3.26590.32831910.26823632X-RAY DIFFRACTION100
3.2659-3.31950.29811950.25693687X-RAY DIFFRACTION100
3.3195-3.37670.32331880.26543590X-RAY DIFFRACTION100
3.3767-3.4380.33481920.24363645X-RAY DIFFRACTION100
3.438-3.50410.30711960.23823712X-RAY DIFFRACTION100
3.5041-3.57560.28751890.22953595X-RAY DIFFRACTION100
3.5756-3.65330.30771940.23153687X-RAY DIFFRACTION100
3.6533-3.73820.29561900.22863599X-RAY DIFFRACTION100
3.7382-3.83160.30051930.23423679X-RAY DIFFRACTION100
3.8316-3.93510.28721910.22413622X-RAY DIFFRACTION100
3.9351-4.05080.2641940.21573681X-RAY DIFFRACTION100
4.0508-4.18140.25271890.21133608X-RAY DIFFRACTION100
4.1814-4.33070.22821940.21743698X-RAY DIFFRACTION100
4.3307-4.50380.28771910.2133613X-RAY DIFFRACTION100
4.5038-4.70850.2531910.20593634X-RAY DIFFRACTION100
4.7085-4.95620.30891920.21223660X-RAY DIFFRACTION100
4.9562-5.26610.27611930.22293656X-RAY DIFFRACTION99
5.2661-5.67150.28771930.24273658X-RAY DIFFRACTION99
5.6715-6.24020.32221910.25083627X-RAY DIFFRACTION99
6.2402-7.13840.28121920.24733647X-RAY DIFFRACTION99
7.1384-8.97560.24971920.22383654X-RAY DIFFRACTION99
8.9756-39.04990.23851940.23753663X-RAY DIFFRACTION98
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)
10.16650.0206-0.20950.3709-0.11250.2807-0.0588-0.09990.1056-0.0696-0.0679-0.02710.0128-0.05290.10970.02830.02030.01780.115-0.18370.324555.9182-62.6206-2.0221
20.12650.01160.01840.16530.04960.07150.01790.0540.244-0.0409-0.0308-0.05160.09370.04260.01420.0735-0.01380.0182-0.0283-0.03430.213628.3207-61.8094-4.907
30.00250.00350.00230.21410.14350.09670.04760.0115-0.00640.13570.0297-0.06280.0797-0.0609-0.06140.2767-0.010.12520.03270.070.263730.0275-107.29736.3774
40.0353-0.03980.01220.065-0.04880.0744-0.05630.00180.0580.1163-0.0539-0.075-0.0204-0.05630.09730.0892-0.0048-0.01610.0301-0.12820.272119.3422-151.7475-3.0815
50.20160.13190.02430.1610.04550.2250.0363-0.0165-0.28450.00640.0562-0.0717-0.01210.1067-0.04080.04910.00590.0096-0.0581-0.01290.208-8.2034-152.3845-0.2858
60.1078-0.0022-0.10150.09690.02650.1031-0.03340.01690.0279-0.02620.0226-0.0065-0.0564-0.05580.01250.4593-0.0734-0.07950.42480.07060.2619-6.2078-107.3603-11.264
70.2877-0.0105-0.1870.1225-0.01350.1181-0.010.2977-0.0112-0.1664-0.069-0.03480.11-0.14180.03390.13390.0337-0.03910.1677-0.0426-0.038142.5779-93.5153-46.0132
80.1072-0.00040.11950.06170.11640.28610.0944-0.18830.00260.0841-0.00840.01340.0916-0.1825-0.00240.04260.01630.1490.147-0.0014-0.19076.0033-120.698140.8344
90.0787-0.0079-0.03820.00340.00350.0185-0.0664-0.0664-0.03490.0220.01610.03450.0311-0.01530.04740.3195-0.01860.15250.3997-0.1390.435261.2542-132.7241-50.1627
100.1952-0.0264-0.04020.2548-0.02640.1313-0.10060.1089-0.0763-0.03920.00120.0030.1355-0.03970.07020.2442-0.02080.07230.3105-0.24890.24148.9261-131.0136-46.8894
110.00370.00830.00260.05970.02150.009-0.00940.0518-0.07210.1188-0.05880.07960.0433-0.01470.06240.18520.07760.08640.08-0.12390.221545.5787-131.0122-33.4139
120.1047-0.09280.04420.32950.17510.1539-0.03170.0911-0.14230.05110.2220.03630.06090.01-0.1028-0.030.17990.0938-0.2942-0.23210.003335.9774-116.4428-18.9085
130.07930.05750.0390.0280.0430.05480.025-0.0095-0.06690.08550.0845-0.02690.0035-0.0806-0.04790.086-0.0368-0.0157-0.1102-0.09580.089433.8887-94.2648-5.8282
140.2362-0.18360.12590.29870.11660.4684-0.1491-0.00970.16570.1969-0.0807-0.0120.0379-0.00320.19420.0748-0.0171-0.00360.0027-0.00760.127254.8133-77.4148-6.9545
150.16730.16490.06640.17490.03560.05970.02020.03850.0142-0.04540.05790.0152-0.0670.0052-0.0422-0.0467-0.1149-0.0357-0.0163-0.01520.111568.3872-71.604-21.3352
160.0026-0.002-0.00470.00130.00180.0068-0.0063-0.02260.00650.0507-0.0254-0.00960.0792-0.04590.02920.073-0.0719-0.0150.0743-0.0812-0.013667.1849-87.7623-28.9662
170.009-0.02570.03170.0889-0.08680.11620.0376-0.0395-0.0180.00360.0298-0.02120.0692-0.0724-0.06850.0826-0.11750.02170.2095-0.13110.252144.4581-87.3172-24.8263
180.15120.00090.03840.01490.0020.0773-0.01290.0423-0.0527-0.00580.0502-0.0445-0.03090.0689-0.04460.05120.01670.01680.2079-0.10630.136678.3881-82.4698-34.3069
190.1281-0.0161-0.04520.27780.16030.28890.00330.18580.0105-0.08340.1715-0.0944-0.02420.1317-0.1187-0.0061-0.076-0.04370.326-0.0617-0.032576.7837-86.8217-41.4991
200.38050.08550.1160.02620.07510.33660.07550.1587-0.017-0.01910.1541-0.0162-0.04770.2469-0.14310.1095-0.1257-0.00250.5095-0.01930.039974.2879-90.0443-58.1974
210.09040.06090.01960.336-0.10530.0609-0.00390.23-0.04850.06420.031-0.0305-0.04220.1397-0.02820.0805-0.0290.02550.787-0.21720.113763.1688-107.1689-68.1658
220.03550.00520.01720.12310.03660.01990.01410.0217-0.0081-0.01990.0792-0.062-0.01540.0561-0.0450.0648-0.16920.11080.4872-0.23690.080849.8607-108.0613-69.5662
230.0006-0.0028-0.00020.0039-0.00190.00730.07220.0310.04920.03-0.0015-0.02680.0430.0532-0.05350.4083-0.03770.06870.8259-0.41250.140143.4102-111.3248-72.5297
240.0830.01480.06260.10790.09560.1113-0.01880.053-0.0347-0.17510.07240.0567-0.1560.075-0.06310.19330.0815-0.03460.7655-0.11250.096127.1474-106.6947-67.6229
250.0060.0026-0.01070.0004-0.00310.03130.0216-0.05240.0010.0214-0.0217-0.00060.0159-0.02180.00010.2991-0.0162-0.17850.3758-0.17150.267624.6868-81.077944.965
260.13970.00980.02350.29330.13650.0624-0.0899-0.0660.0437-0.1731-0.03410.0851-0.1261-0.03580.09790.1132-0.0213-0.12870.0144-0.3110.172812.3921-83.222741.7231
270.00710.02530.01560.04270.03050.0334-0.03010.03680.0188-0.14670.00090.1364-0.08750.04740.03730.2712-0.1125-0.12660.0155-0.25990.18199.0457-83.196428.2339
280.0075-0.0316-0.0490.13890.12280.10070.0582-0.08190.0645-0.05470.0767-0.05880.0158-0.052-0.05350.03920.0229-0.0181-0.3104-0.2863-0.0912-0.6047-97.788913.7339
290.0699-0.0493-0.02920.0628-0.02470.0547-0.01170.0080.09070.13770.0863-0.1204-0.09160.025-0.0530.1308-0.01270.0147-0.0707-0.06210.1447-2.7491-119.9060.6258
300.1208-0.059-0.04550.27230.03950.21180.0037-0.0312-0.0497-0.1726-0.1060.0117-0.01640.03260.08490.08650.03070.0091-0.001-0.00960.111918.161-136.74381.724
310.078-0.0856-0.05370.14260.03530.06260.0260.04370.0148-0.0780.033-0.01010.07610.0969-0.0226-0.04440.14180.02290.0763-0.00340.064631.7463-142.619416.0938
320.20080.0066-0.07640.04730.06110.11710.0577-0.01270.0159-0.01050.054-0.0778-0.0323-0.0141-0.06980.1071-0.04180.00090.03290.010.082830.5783-126.489823.7431
330.00730.0136-0.00390.0295-0.01450.09530.02280.0358-0.0014-0.04420.0116-0.0195-0.0672-0.0885-0.03120.05780.07760.09380.1817-0.0460.10547.6948-127.078219.5913
340.05750.0155-0.02080.0815-0.00310.0995-0.008-0.04-0.002-0.012-0.04080.02190.04750.11830.01850.07390.1045-0.04250.2413-0.05570.066941.7816-131.80729.0648
350.1866-0.0093-0.02160.08770.10050.34490.0583-0.0591-0.04360.00710.00760.01110.0250.109-0.0504-0.00730.0440.010.1897-0.06020.030140.1828-127.4736.2835
360.3296-0.1855-0.00580.14670.11390.37190.0439-0.1845-0.0117-0.07490.21910.0340.10440.1322-0.17520.10660.0642-0.00650.51610.06420.047437.7148-124.217952.9738
370.0129-0.02040.01170.0091-0.0103-0.00060.0015-0.11760.02420.0601-0.06640.0299-0.060.01660.0470.10760.014-0.0220.7413-0.18130.064626.6383-107.063562.9413
380.0352-0.0244-0.04350.11230.01670.05780.029-0.0445-0.0138-0.02590.0621-0.0197-0.00370.0657-0.0630.1690.1628-0.11180.7809-0.26720.118913.3504-106.249564.4361
390.00450.0030.00650.0024-0.00360.1199-0.0017-0.0070.0101-0.01640.0327-0.01640.0307-0.08860.0050.15380.0880.02760.6732-0.31180.06866.8901-102.907767.7023
400.19880.28140.10410.4310.08490.2847-0.00170.00120.05970.022-0.06410.09820.1001-0.07930.06310.0456-0.01640.08020.68350.03940.0384-9.8989-107.932562.3534
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain B and resid 1:39
2X-RAY DIFFRACTION2chain B and resid 40:290
3X-RAY DIFFRACTION3chain B and resid 330:365
4X-RAY DIFFRACTION4chain E and resid 1:39
5X-RAY DIFFRACTION5chain E and resid 40:290
6X-RAY DIFFRACTION6chain E and resid 330:365
7X-RAY DIFFRACTION7chain C
8X-RAY DIFFRACTION8chain F
9X-RAY DIFFRACTION9chain A and resid 1028:1059
10X-RAY DIFFRACTION10chain A and resid 969:1027
11X-RAY DIFFRACTION11chain A and resid 908:963
12X-RAY DIFFRACTION12chain A and resid 767:907
13X-RAY DIFFRACTION13chain A and resid 627:766
14X-RAY DIFFRACTION14chain A and resid 533:626
15X-RAY DIFFRACTION15chain A and resid 468:532
16X-RAY DIFFRACTION16chain A and resid 449:467
17X-RAY DIFFRACTION17chain A and resid 425:448
18X-RAY DIFFRACTION18chain A and resid 402:424
19X-RAY DIFFRACTION19chain A and resid 311:401
20X-RAY DIFFRACTION20chain A and resid 240:310
21X-RAY DIFFRACTION21chain A and resid 145:239
22X-RAY DIFFRACTION22chain A and resid 120:144
23X-RAY DIFFRACTION23chain A and resid 67:119
24X-RAY DIFFRACTION24chain A and resid 4:66
25X-RAY DIFFRACTION25chain D and resid 1028:1059
26X-RAY DIFFRACTION26chain D and resid 969:1027
27X-RAY DIFFRACTION27chain D and resid 908:963
28X-RAY DIFFRACTION28chain D and resid 767:907
29X-RAY DIFFRACTION29chain D and resid 627:766
30X-RAY DIFFRACTION30chain D and resid 533:626
31X-RAY DIFFRACTION31chain D and resid 468:532
32X-RAY DIFFRACTION32chain D and resid 449:467
33X-RAY DIFFRACTION33chain D and resid 425:448
34X-RAY DIFFRACTION34chain D and resid 402:424
35X-RAY DIFFRACTION35chain D and resid 311:401
36X-RAY DIFFRACTION36chain D and resid 240:310
37X-RAY DIFFRACTION37chain D and resid 145:239
38X-RAY DIFFRACTION38chain D and resid 120:144
39X-RAY DIFFRACTION39chain D and resid 67:119
40X-RAY DIFFRACTION40chain D and resid 4:66

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more