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- PDB-8qyz: Crystal structure of hiNES2 in complex with Xpo1 and RanGTP -

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Basic information

Entry
Database: PDB / ID: 8qyz
TitleCrystal structure of hiNES2 in complex with Xpo1 and RanGTP
Components
  • Exportin-1
  • GTP-binding nuclear protein GSP1/CNR1
  • hiNES2
KeywordsTRANSPORT PROTEIN / NES / Exportin / RanGTP
Function / homology
Function and homology information


regulation of cell cycle phase transition / exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / regulation of nucleocytoplasmic transport / Postmitotic nuclear pore complex (NPC) reformation / tRNA re-export from nucleus / Transcriptional and post-translational regulation of MITF-M expression and activity / nuclear export signal receptor activity / tRNA export from nucleus / protein localization to kinetochore / U4 snRNA binding ...regulation of cell cycle phase transition / exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / regulation of nucleocytoplasmic transport / Postmitotic nuclear pore complex (NPC) reformation / tRNA re-export from nucleus / Transcriptional and post-translational regulation of MITF-M expression and activity / nuclear export signal receptor activity / tRNA export from nucleus / protein localization to kinetochore / U4 snRNA binding / spindle pole body / nuclear export / nuclear import signal receptor activity / poly(A)+ mRNA export from nucleus / nucleus organization / MAPK6/MAPK4 signaling / ribosomal large subunit export from nucleus / U5 snRNA binding / U2 snRNA binding / U6 snRNA binding / ribosomal subunit export from nucleus / mRNA export from nucleus / U1 snRNA binding / ribosomal small subunit export from nucleus / protein export from nucleus / small GTPase binding / kinetochore / protein import into nucleus / GTPase activity / GTP binding / perinuclear region of cytoplasm / nucleus / cytosol / cytoplasm
Similarity search - Function
Exportin-1, repeat 3 / Chromosome region maintenance repeat / Exportin-1, repeat 2 / Chromosome region maintenance or exportin repeat / CRM1 / Exportin repeat 2 / CRM1 / Exportin repeat 3 / CRM1 C terminal / Exportin-1, C-terminal / CRM1 C terminal / Exportin-1/5 ...Exportin-1, repeat 3 / Chromosome region maintenance repeat / Exportin-1, repeat 2 / Chromosome region maintenance or exportin repeat / CRM1 / Exportin repeat 2 / CRM1 / Exportin repeat 3 / CRM1 C terminal / Exportin-1, C-terminal / CRM1 C terminal / Exportin-1/5 / Exportin-1/Importin-beta-like / Exportin 1-like protein / small GTPase Ran family profile. / Ran GTPase / Importin-beta N-terminal domain / Importin-beta N-terminal domain / Importin-beta N-terminal domain profile. / Importin-beta, N-terminal domain / 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 nucleoside triphosphate hydrolase
Similarity search - Domain/homology
ACETATE ION / GUANOSINE-5'-TRIPHOSPHATE / Exportin-1 / GTP-binding nuclear protein GSP1/CNR1
Similarity search - Component
Biological speciesSaccharomyces cerevisiae S288C (yeast)
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3 Å
AuthorsRymarenko, O. / Huyton, T. / Gorlich, D.
Funding support Germany, 1items
OrganizationGrant numberCountry
Max Planck Society Germany
CitationJournal: To Be Published
Title: Exploring sequence space and engineering of Xpo1-dependent NESes
Authors: Rymarenko, O. / Huyton, T. / Gorlich, D.
History
DepositionOct 26, 2023Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 6, 2024Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: GTP-binding nuclear protein GSP1/CNR1
C: Exportin-1
B: GTP-binding nuclear protein GSP1/CNR1
D: Exportin-1
E: GTP-binding nuclear protein GSP1/CNR1
F: Exportin-1
G: GTP-binding nuclear protein GSP1/CNR1
H: Exportin-1
I: hiNES2
J: hiNES2
K: hiNES2
L: hiNES2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)573,42624
Polymers571,00012
Non-polymers2,42612
Water3,765209
1
A: GTP-binding nuclear protein GSP1/CNR1
C: Exportin-1
I: hiNES2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)143,3566
Polymers142,7503
Non-polymers6073
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7530 Å2
ΔGint-35 kcal/mol
Surface area48520 Å2
2
B: GTP-binding nuclear protein GSP1/CNR1
D: Exportin-1
J: hiNES2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)143,3566
Polymers142,7503
Non-polymers6073
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7710 Å2
ΔGint-34 kcal/mol
Surface area48400 Å2
3
E: GTP-binding nuclear protein GSP1/CNR1
F: Exportin-1
K: hiNES2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)143,3566
Polymers142,7503
Non-polymers6073
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7210 Å2
ΔGint-35 kcal/mol
Surface area49250 Å2
4
G: GTP-binding nuclear protein GSP1/CNR1
H: Exportin-1
L: hiNES2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)143,3566
Polymers142,7503
Non-polymers6073
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7200 Å2
ΔGint-33 kcal/mol
Surface area49560 Å2
Unit cell
Length a, b, c (Å)97.355, 105.572, 170.400
Angle α, β, γ (deg.)82.080, 86.668, 76.668
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21A
32A
42A
53A
63A
74A
84A
95A
105A
116A
126A
137A
147A
158A
168A
179A
189A
1910A
2010A
2111A
2211A
2312A
2412A
2513A
2613A
2714A
2814A
2915A
3015A
3116A
3216A
3317A
3417A
3518A
3618A

NCS domain segments:
Dom-IDComponent-IDEns-IDAuth asym-IDAuth seq-ID
111A10 - 181
211A10 - 181
322A10 - 178
422A10 - 178
533A10 - 178
633A10 - 178
744A5 - 1055
844A5 - 1055
955A5 - 1054
1055A5 - 1054
1166A5 - 1054
1266A5 - 1054
1377A10 - 178
1477A10 - 178
1588A10 - 178
1688A10 - 178
1799A5 - 1054
1899A5 - 1054
191010A5 - 1054
201010A5 - 1054
211111A10 - 179
221111A10 - 179
231212A5 - 1056
241212A5 - 1056
251313A0 - 15
261313A0 - 15
271414A0 - 15
281414A0 - 15
291515A0 - 15
301515A0 - 15
311616A0 - 15
321616A0 - 15
331717A0 - 15
341717A0 - 15
351818A0 - 15
361818A0 - 15

NCS ensembles :
IDDetails
1Local NCS retraints between domains: 1 2
2Local NCS retraints between domains: 3 4
3Local NCS retraints between domains: 5 6
4Local NCS retraints between domains: 7 8
5Local NCS retraints between domains: 9 10
6Local NCS retraints between domains: 11 12
7Local NCS retraints between domains: 13 14
8Local NCS retraints between domains: 15 16
9Local NCS retraints between domains: 17 18
10Local NCS retraints between domains: 19 20
11Local NCS retraints between domains: 21 22
12Local NCS retraints between domains: 23 24
13Local NCS retraints between domains: 25 26
14Local NCS retraints between domains: 27 28
15Local NCS retraints between domains: 29 30
16Local NCS retraints between domains: 31 32
17Local NCS retraints between domains: 33 34
18Local NCS retraints between domains: 35 36

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Components

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Protein , 2 types, 8 molecules ABEGCDFH

#1: Protein
GTP-binding nuclear protein GSP1/CNR1


Mass: 20672.861 Da / Num. of mol.: 4 / Mutation: 1-182, Q71L
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae S288C (yeast) / Gene: GSP1 / Production host: Escherichia coli (E. coli) / References: UniProt: P32835
#2: Protein
Exportin-1


Mass: 120327.117 Da / Num. of mol.: 4 / Mutation: del(377-413)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae S288C (yeast) / Gene: CRM1 / Production host: Escherichia coli (E. coli) / References: UniProt: P30822

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Protein/peptide , 1 types, 4 molecules IJKL

#3: Protein/peptide
hiNES2


Mass: 1749.958 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) synthetic construct (others) / Production host: Escherichia coli (E. coli)

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Non-polymers , 4 types, 221 molecules

#4: Chemical
ChemComp-GTP / GUANOSINE-5'-TRIPHOSPHATE


Mass: 523.180 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C10H16N5O14P3 / Comment: GTP, energy-carrying molecule*YM
#5: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg
#6: Chemical
ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C2H3O2
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 209 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestN
Has protein modificationN

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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: 2.95 Å3/Da / Density % sol: 58.38 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.4 / Details: Tris, PEG 20K, magnesium acetate

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1 Å
DetectorType: PSI PILATUS 6M / Detector: PIXEL / Date: May 20, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3→84.36 Å / Num. obs: 126263 / % possible obs: 96.47 % / Redundancy: 3.41 % / CC1/2: 0.8256 / Rmerge(I) obs: 0.1386 / Net I/σ(I): 8.05
Reflection shellResolution: 3→3.05 Å / Redundancy: 3.2 % / Rmerge(I) obs: 0.995 / Mean I/σ(I) obs: 0.8 / Num. unique obs: 6193 / CC1/2: 0.606 / % possible all: 94.69

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Processing

Software
NameVersionClassification
REFMAC5.8.0350refinement
Cootmodel building
DIALSdata reduction
DIALSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 3→82.792 Å / Cor.coef. Fo:Fc: 0.921 / Cor.coef. Fo:Fc free: 0.899 / SU B: 52.02 / SU ML: 0.402 / Cross valid method: FREE R-VALUE / ESU R Free: 0.436 / Details: Hydrogens have not been used
RfactorNum. reflection% reflection
Rfree0.2469 6264 4.962 %
Rwork0.2177 119969 -
all0.219 --
obs-126233 96.405 %
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK BULK SOLVENT
Displacement parametersBiso mean: 79.868 Å2
Baniso -1Baniso -2Baniso -3
1--0.12 Å2-1.416 Å22.28 Å2
2---0.602 Å2-0.887 Å2
3---0.015 Å2
Refinement stepCycle: LAST / Resolution: 3→82.792 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms38872 0 148 209 39229
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0040.01239847
X-RAY DIFFRACTIONr_angle_refined_deg1.1481.63253983
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.36654806
X-RAY DIFFRACTIONr_dihedral_angle_2_deg2.74710169
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.143107306
X-RAY DIFFRACTIONr_dihedral_angle_6_deg17.232101854
X-RAY DIFFRACTIONr_chiral_restr0.0870.26238
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.0229272
X-RAY DIFFRACTIONr_nbd_refined0.2220.221629
X-RAY DIFFRACTIONr_nbtor_refined0.3140.228044
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.160.21122
X-RAY DIFFRACTIONr_symmetry_nbd_refined0.3560.2146
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_refined0.2030.27
X-RAY DIFFRACTIONr_mcbond_it1.8664.55619252
X-RAY DIFFRACTIONr_mcangle_it3.1456.8324046
X-RAY DIFFRACTIONr_scbond_it2.1224.68920595
X-RAY DIFFRACTIONr_scangle_it3.5276.98229937
X-RAY DIFFRACTIONr_lrange_it9.011156.5791534427
X-RAY DIFFRACTIONr_ncsr_local_group_10.0730.055836
X-RAY DIFFRACTIONr_ncsr_local_group_20.1030.055575
X-RAY DIFFRACTIONr_ncsr_local_group_30.0940.055607
X-RAY DIFFRACTIONr_ncsr_local_group_40.0840.0536140
X-RAY DIFFRACTIONr_ncsr_local_group_50.1120.0535058
X-RAY DIFFRACTIONr_ncsr_local_group_60.1090.0535151
X-RAY DIFFRACTIONr_ncsr_local_group_70.0970.055575
X-RAY DIFFRACTIONr_ncsr_local_group_80.0910.055593
X-RAY DIFFRACTIONr_ncsr_local_group_90.110.0535005
X-RAY DIFFRACTIONr_ncsr_local_group_100.1060.0535045
X-RAY DIFFRACTIONr_ncsr_local_group_110.0960.055616
X-RAY DIFFRACTIONr_ncsr_local_group_120.1080.0535212
X-RAY DIFFRACTIONr_ncsr_local_group_130.1310.05413
X-RAY DIFFRACTIONr_ncsr_local_group_140.180.05418
X-RAY DIFFRACTIONr_ncsr_local_group_150.1610.05412
X-RAY DIFFRACTIONr_ncsr_local_group_160.1780.05405
X-RAY DIFFRACTIONr_ncsr_local_group_170.140.05410
X-RAY DIFFRACTIONr_ncsr_local_group_180.1680.05416
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDRefine-IDTypeRms dev position (Å)Weight position
11AX-RAY DIFFRACTIONLocal ncs0.072650.05011
12AX-RAY DIFFRACTIONLocal ncs0.072650.05011
23AX-RAY DIFFRACTIONLocal ncs0.103290.0501
24AX-RAY DIFFRACTIONLocal ncs0.103290.0501
35AX-RAY DIFFRACTIONLocal ncs0.094250.0501
36AX-RAY DIFFRACTIONLocal ncs0.094250.0501
47AX-RAY DIFFRACTIONLocal ncs0.084350.05011
48AX-RAY DIFFRACTIONLocal ncs0.084350.05011
59AX-RAY DIFFRACTIONLocal ncs0.111540.0501
510AX-RAY DIFFRACTIONLocal ncs0.111540.0501
611AX-RAY DIFFRACTIONLocal ncs0.108560.0501
612AX-RAY DIFFRACTIONLocal ncs0.108560.0501
713AX-RAY DIFFRACTIONLocal ncs0.096980.0501
714AX-RAY DIFFRACTIONLocal ncs0.096980.0501
815AX-RAY DIFFRACTIONLocal ncs0.090650.0501
816AX-RAY DIFFRACTIONLocal ncs0.090650.0501
917AX-RAY DIFFRACTIONLocal ncs0.109730.0501
918AX-RAY DIFFRACTIONLocal ncs0.109730.0501
1019AX-RAY DIFFRACTIONLocal ncs0.106240.0501
1020AX-RAY DIFFRACTIONLocal ncs0.106240.0501
1121AX-RAY DIFFRACTIONLocal ncs0.095870.0501
1122AX-RAY DIFFRACTIONLocal ncs0.095870.0501
1223AX-RAY DIFFRACTIONLocal ncs0.108220.0501
1224AX-RAY DIFFRACTIONLocal ncs0.108220.0501
1325AX-RAY DIFFRACTIONLocal ncs0.13130.05006
1326AX-RAY DIFFRACTIONLocal ncs0.13130.05006
1427AX-RAY DIFFRACTIONLocal ncs0.179580.05007
1428AX-RAY DIFFRACTIONLocal ncs0.179580.05007
1529AX-RAY DIFFRACTIONLocal ncs0.161460.05006
1530AX-RAY DIFFRACTIONLocal ncs0.161460.05006
1631AX-RAY DIFFRACTIONLocal ncs0.178290.05006
1632AX-RAY DIFFRACTIONLocal ncs0.178290.05006
1733AX-RAY DIFFRACTIONLocal ncs0.140480.05006
1734AX-RAY DIFFRACTIONLocal ncs0.140480.05006
1835AX-RAY DIFFRACTIONLocal ncs0.16830.05006
1836AX-RAY DIFFRACTIONLocal ncs0.16830.05006
LS refinement shell

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

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRfactor allNum. reflection allFsc freeFsc work% reflection obs (%)WRfactor Rwork
3-3.0780.3554680.33487400.33596680.9160.92495.2420.335
3.078-3.1620.3284500.30886720.30994240.9270.93696.79540.306
3.162-3.2530.3024590.28884280.28992040.9410.94696.55580.283
3.253-3.3530.2933930.26381900.26489010.9410.95496.42740.253
3.353-3.4630.2874030.28579170.28686350.9480.92596.35210.276
3.463-3.5840.2724080.2575660.25183380.9490.9695.63440.233
3.584-3.720.2953690.27771130.27780780.8460.90192.62190.26
3.72-3.8710.313550.25371920.25677330.9170.95397.59470.234
3.871-4.0430.243600.2169100.21174500.9620.97397.58390.187
4.043-4.240.233730.18865340.1971070.9670.97997.18590.164
4.24-4.4680.2073190.1862240.18167550.9740.9896.86160.159
4.468-4.7380.2023100.17558430.17763970.9740.98196.18570.155
4.738-5.0640.2222830.17754400.17960290.970.98194.92450.153
5.064-5.4690.2362790.18451960.18755750.9680.97998.20630.157
5.469-5.9880.2492150.19948180.20151450.9630.97797.82310.169
5.988-6.690.2472310.19842860.20146480.9710.97797.18160.17
6.69-7.7170.2381890.19337500.19541070.9660.9895.90940.171
7.717-9.4310.181620.13732810.13934900.9780.98998.65330.134
9.431-13.2510.1331650.13324730.13327090.9890.98997.37910.142
13.251-82.7920.305730.26313950.26515030.9350.94697.67130.285
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)
12.85540.27750.42422.47990.15343.22080.0550.2152-0.225-0.1239-0.0161-0.10680.34930.1872-0.03890.09130.04680.04140.0629-0.00270.061221.1946-3.125915.9318
20.6112-0.0421-0.39130.3697-0.21230.51740.00320.01160.02780.02040.03730.07060.0123-0.0421-0.04060.09780.01990.04670.0983-0.03850.066828.53359.891216.4761
32.6689-0.54560.63032.201-0.59433.0508-0.0094-0.3537-0.22010.25840.0950.12530.3509-0.3529-0.08560.20810.00510.10230.17130.05520.097843.340745.726129.2236
40.47690.0243-0.16980.35150.41920.5862-0.0183-0.0221-0.10280.03970.0479-0.05060.04680.0487-0.02960.18920.08250.10620.10970.07440.104742.500560.815628.6087
53.9931-0.93070.75762.24410.33363.6464-0.7002-0.38120.63760.48840.2784-0.5949-0.98810.0820.42180.9509-0.0676-0.03390.37940.03780.519-2.130442.7499-47.7433
60.76160.0619-0.06070.8135-0.2071.0601-0.14890.34720.142-0.48570.0942-0.1907-0.13010.20550.05470.4796-0.10480.16550.35120.00460.2489-12.467730.9523-49.6617
73.57210.87870.47791.47471.01282.482-0.640.84291.0028-0.37440.18180.3837-0.9520.41920.45821.1557-0.2507-0.01020.63480.07280.5575-12.001899.2674-75.9316
80.62860.06520.00680.97770.29771.04660.0523-0.28250.23840.4967-0.09140.057-0.266-0.14580.03910.6240.03160.16310.3488-0.00030.2333-7.965683.796-74.0001
97.61770.9081-1.21260.7071-1.49533.29320.1167-0.1459-0.40420.0662-0.0458-0.0401-0.12530.0902-0.07090.06010.0241-0.00320.1006-0.00460.268670.804-6.919922.9736
107.95120.6501-2.43797.9877-1.21254.0584-0.19810.1810.14470.14630.36790.619-0.2814-0.4664-0.16980.14310.05040.0190.2743-0.10270.1417-2.903564.663622.3391
110.68972.89690.791313.12842.40255.99320.01290.0079-0.11450.14580.326-0.31410.48590.1878-0.33880.08110.0935-0.00580.21720.0230.35595.78912.0479-19.1141
125.02463.0318-3.41364.77982.02098.07540.0996-0.3315-0.01330.3223-0.40790.28650.41840.06930.30830.16910.1135-0.07280.48030.10640.4116-37.431764.9969-103.78
Refinement TLS groupSelection: ALL

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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

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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

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