[English] 日本語
Yorodumi
- PDB-7zmm: Crystal structure of human RECQL5 helicase APO form in complex wi... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 7zmm
TitleCrystal structure of human RECQL5 helicase APO form in complex with engineered nanobody (Gluebody) G2-001
Components
  • ATP-dependent DNA helicase Q5
  • Gluebody G2-001
KeywordsHYDROLASE / Helicase / Apo form / Nanobody complex
Function / homology
Function and homology information


mitotic DNA-templated DNA replication / chromosome separation / cellular response to camptothecin / four-way junction helicase activity / replication-born double-strand break repair via sister chromatid exchange / DNA 3'-5' helicase / transcription preinitiation complex / DNA metabolic process / negative regulation of transcription elongation by RNA polymerase II / DNA unwinding involved in DNA replication ...mitotic DNA-templated DNA replication / chromosome separation / cellular response to camptothecin / four-way junction helicase activity / replication-born double-strand break repair via sister chromatid exchange / DNA 3'-5' helicase / transcription preinitiation complex / DNA metabolic process / negative regulation of transcription elongation by RNA polymerase II / DNA unwinding involved in DNA replication / RNA polymerase II complex binding / 3'-5' DNA helicase activity / negative regulation of double-strand break repair via homologous recombination / DNA helicase activity / isomerase activity / helicase activity / replication fork / double-strand break repair via homologous recombination / cellular response to xenobiotic stimulus / chromosome / mitotic cell cycle / DNA replication / cell division / DNA repair / ATP hydrolysis activity / DNA binding / nucleoplasm / ATP binding / identical protein binding / nucleus / metal ion binding / cytoplasm / cytosol
Similarity search - Function
RecQ helicase-like 5 / RecQ helicase protein-like 5 (RecQ5) / ATP-dependent DNA helicase RecQ, zinc-binding domain / RecQ zinc-binding / DNA helicase, ATP-dependent, RecQ type / DNA/RNA helicase, ATP-dependent, DEAH-box type, conserved site / DEAH-box subfamily ATP-dependent helicases signature. / DEAD/DEAH box helicase / DEAD/DEAH box helicase domain / Helicase conserved C-terminal domain ...RecQ helicase-like 5 / RecQ helicase protein-like 5 (RecQ5) / ATP-dependent DNA helicase RecQ, zinc-binding domain / RecQ zinc-binding / DNA helicase, ATP-dependent, RecQ type / DNA/RNA helicase, ATP-dependent, DEAH-box type, conserved site / DEAH-box subfamily ATP-dependent helicases signature. / 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 / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
ATP-dependent DNA helicase Q5
Similarity search - Component
Biological speciesHomo sapiens (human)
Lama glama (llama)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å
AuthorsYe, M. / Makola, M. / Newman, J.A. / Fairhead, M. / MacLean, E. / Krojer, T. / Aitkenhead, H. / Bountra, C. / Gileadi, O. / von Delft, F.
Funding support China, 1items
OrganizationGrant numberCountry
Chinese Scholarship Council China
CitationJournal: To Be Published
Title: Gluebodies improve crystal reliability and diversity through transferable nanobody mutations that introduce constitutive crystal contacts
Authors: Ye, M. / Makola, M. / Newman, J.A. / Fairhead, M. / MacLean, E. / Krojer, T. / Wright, N.D. / Koekemoer, L. / Thompson, A. / Bezerra, G.A. / Yi, G. / Li, H. / Rangel, V.L. / Mamalis, D. / ...Authors: Ye, M. / Makola, M. / Newman, J.A. / Fairhead, M. / MacLean, E. / Krojer, T. / Wright, N.D. / Koekemoer, L. / Thompson, A. / Bezerra, G.A. / Yi, G. / Li, H. / Rangel, V.L. / Mamalis, D. / Aitkenhead, H. / Gilbert, R.J.C. / Duerr, K. / Davis, B.G. / Bountra, C. / Gileadi, O. / von Delft, F.
History
DepositionApr 19, 2022Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jun 22, 2022Provider: repository / Type: Initial release
Revision 2.0Oct 5, 2022Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Refinement description / Structure summary
Category: atom_site / entity ...atom_site / entity / pdbx_contact_author / pdbx_nonpoly_scheme / pdbx_struct_assembly_prop / pdbx_struct_conn_angle / pdbx_struct_sheet_hbond / pdbx_validate_torsion / refine / refine_ls_restr / refine_ls_restr_ncs / refine_ls_shell / struct_conn / struct_mon_prot_cis / struct_ncs_dom_lim
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 / _entity.pdbx_description / _pdbx_nonpoly_scheme.auth_seq_num / _pdbx_struct_assembly_prop.value / _pdbx_struct_conn_angle.value / _pdbx_struct_sheet_hbond.range_1_auth_seq_id / _pdbx_struct_sheet_hbond.range_1_label_seq_id / _pdbx_struct_sheet_hbond.range_2_auth_comp_id / _pdbx_struct_sheet_hbond.range_2_auth_seq_id / _pdbx_struct_sheet_hbond.range_2_label_comp_id / _pdbx_struct_sheet_hbond.range_2_label_seq_id / _pdbx_validate_torsion.phi / _pdbx_validate_torsion.psi / _refine.B_iso_mean / _refine.aniso_B[1][1] / _refine.aniso_B[1][3] / _refine.aniso_B[2][2] / _refine.aniso_B[3][3] / _refine.correlation_coeff_Fo_to_Fc / _refine.correlation_coeff_Fo_to_Fc_free / _refine.ls_R_factor_R_free / _refine.ls_R_factor_R_work / _refine.ls_R_factor_all / _refine.ls_wR_factor_R_free / _refine.ls_wR_factor_R_work / _refine.overall_SU_B / _refine.overall_SU_ML / _refine.pdbx_average_fsc_free / _refine.pdbx_average_fsc_work / _refine.pdbx_overall_ESU_R / _refine_ls_restr_ncs.rms_dev_position / _refine_ls_restr_ncs.weight_position / _refine_ls_shell.R_factor_R_free / _refine_ls_shell.R_factor_R_work / _refine_ls_shell.R_factor_all / _refine_ls_shell.pdbx_fsc_free / _refine_ls_shell.pdbx_fsc_work / _refine_ls_shell.wR_factor_R_work / _struct_mon_prot_cis.pdbx_omega_angle / _struct_ncs_dom_lim.pdbx_component_id
Description: Atoms with unrealistic or zero occupancies / Provider: author / Type: Coordinate replacement
Revision 2.1Jan 31, 2024Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id ..._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

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
B: ATP-dependent DNA helicase Q5
A: ATP-dependent DNA helicase Q5
C: ATP-dependent DNA helicase Q5
D: ATP-dependent DNA helicase Q5
K: Gluebody G2-001
E: Gluebody G2-001
F: Gluebody G2-001
G: Gluebody G2-001
hetero molecules


Theoretical massNumber of molelcules
Total (without water)255,86912
Polymers255,6088
Non-polymers2624
Water1,71195
1
B: ATP-dependent DNA helicase Q5
F: Gluebody G2-001
hetero molecules


Theoretical massNumber of molelcules
Total (without water)63,9673
Polymers63,9022
Non-polymers651
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1440 Å2
ΔGint-8 kcal/mol
Surface area26430 Å2
MethodPISA
2
A: ATP-dependent DNA helicase Q5
K: Gluebody G2-001
hetero molecules


Theoretical massNumber of molelcules
Total (without water)63,9673
Polymers63,9022
Non-polymers651
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1470 Å2
ΔGint-7 kcal/mol
Surface area26900 Å2
MethodPISA
3
C: ATP-dependent DNA helicase Q5
E: Gluebody G2-001
hetero molecules


Theoretical massNumber of molelcules
Total (without water)63,9673
Polymers63,9022
Non-polymers651
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1440 Å2
ΔGint-8 kcal/mol
Surface area26410 Å2
MethodPISA
4
D: ATP-dependent DNA helicase Q5
G: Gluebody G2-001
hetero molecules


Theoretical massNumber of molelcules
Total (without water)63,9673
Polymers63,9022
Non-polymers651
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1450 Å2
ΔGint-9 kcal/mol
Surface area26440 Å2
MethodPISA
Unit cell
Length a, b, c (Å)76.612, 183.969, 100.947
Angle α, β, γ (deg.)90.000, 108.124, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11B
21A
32B
42C
53B
63D
74A
84C
95A
105D
116C
126D
137K
147E
158K
168F
179K
189G
1910E
2010F
2111E
2211G
2312F
2412G

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111PROPROSERSERBA12 - 4504 - 442
211PROPROSERSERAB12 - 4504 - 442
322PROPROSERSERBA12 - 4524 - 444
422PROPROSERSERCC12 - 4524 - 444
533PROPROSERSERBA12 - 4524 - 444
633PROPROSERSERDD12 - 4524 - 444
744PROPROSERSERAB12 - 4504 - 442
844PROPROSERSERCC12 - 4504 - 442
955PROPROSERSERAB12 - 4504 - 442
1055PROPROSERSERDD12 - 4504 - 442
1166PROPROSERSERCC12 - 4524 - 444
1266PROPROSERSERDD12 - 4524 - 444
1377GLNGLNLEULEUKE1 - 1291 - 129
1477GLNGLNLEULEUEF1 - 1291 - 129
1588GLNGLNALAALAKE1 - 1251 - 125
1688GLNGLNALAALAFG1 - 1251 - 125
1799GLNGLNALAALAKE1 - 1261 - 126
1899GLNGLNALAALAGH1 - 1261 - 126
191010GLNGLNALAALAEF1 - 1251 - 125
201010GLNGLNALAALAFG1 - 1251 - 125
211111GLNGLNALAALAEF1 - 1261 - 126
221111GLNGLNALAALAGH1 - 1261 - 126
231212GLNGLNALAALAFG1 - 1251 - 125
241212GLNGLNALAALAGH1 - 1251 - 125

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

-
Components

#1: Protein
ATP-dependent DNA helicase Q5 / DNA helicase / RecQ-like type 5 / RecQ5 / RecQ protein-like 5


Mass: 49537.180 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RECQL5, RECQ5 / Production host: Escherichia coli (E. coli) / References: UniProt: O94762, DNA helicase
#2: Antibody
Gluebody G2-001


Mass: 14364.772 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Lama glama (llama) / Production host: Escherichia coli (E. coli)
#3: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Zn
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 95 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.68 Å3/Da / Density % sol: 54.13 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: 0.2M sodium chloride -- 25% PEG3350 -- 0.1M bis-tris pH 6.5

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.9762 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Oct 21, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9762 Å / Relative weight: 1
ReflectionResolution: 2.5→183.84 Å / Num. obs: 95510 / % possible obs: 99.2 % / Redundancy: 2.7 % / CC1/2: 1 / Net I/σ(I): 8.6
Reflection shellResolution: 2.5→2.55 Å / Num. unique obs: 4769 / CC1/2: 0.61

-
Processing

Software
NameVersionClassification
REFMAC5.8.0267refinement
xia2data reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5LB5
Resolution: 2.5→95.938 Å / Cor.coef. Fo:Fc: 0.941 / Cor.coef. Fo:Fc free: 0.927 / WRfactor Rfree: 0.287 / WRfactor Rwork: 0.24 / SU B: 15.088 / SU ML: 0.317 / Average fsc free: 0.8144 / Average fsc work: 0.8387 / Cross valid method: FREE R-VALUE / ESU R: 0.641 / ESU R Free: 0.324
Details: Hydrogens have been added in their riding positions
RfactorNum. reflection% reflection
Rfree0.2806 4407 4.844 %
Rwork0.2356 86568 -
all0.238 --
obs-90975 99.371 %
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: 79.866 Å2
Baniso -1Baniso -2Baniso -3
1-0.817 Å2-0 Å2-2.886 Å2
2--1.73 Å2-0 Å2
3----0.541 Å2
Refinement stepCycle: LAST / Resolution: 2.5→95.938 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17546 0 0 95 17641
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0060.01318018
X-RAY DIFFRACTIONr_bond_other_d0.0010.01717075
X-RAY DIFFRACTIONr_angle_refined_deg1.4111.64324406
X-RAY DIFFRACTIONr_angle_other_deg1.2481.57939251
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.46452306
X-RAY DIFFRACTIONr_dihedral_angle_2_deg29.55321.246939
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.321153063
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.14315145
X-RAY DIFFRACTIONr_chiral_restr0.060.22332
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.0220675
X-RAY DIFFRACTIONr_gen_planes_other0.0010.024311
X-RAY DIFFRACTIONr_nbd_refined0.2020.23305
X-RAY DIFFRACTIONr_symmetry_nbd_other0.1780.214645
X-RAY DIFFRACTIONr_nbtor_refined0.1580.28662
X-RAY DIFFRACTIONr_symmetry_nbtor_other0.0760.29357
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1660.2333
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_other0.1430.22
X-RAY DIFFRACTIONr_symmetry_nbd_refined0.4010.247
X-RAY DIFFRACTIONr_nbd_other0.3270.297
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_refined0.3040.27
X-RAY DIFFRACTIONr_xyhbond_nbd_other0.1240.21
X-RAY DIFFRACTIONr_mcbond_it8.0538.2759159
X-RAY DIFFRACTIONr_mcbond_other8.0478.2759158
X-RAY DIFFRACTIONr_mcangle_it11.83812.40111449
X-RAY DIFFRACTIONr_mcangle_other11.83712.40211450
X-RAY DIFFRACTIONr_scbond_it7.7638.7818859
X-RAY DIFFRACTIONr_scbond_other7.7638.788857
X-RAY DIFFRACTIONr_scangle_it11.79112.92112931
X-RAY DIFFRACTIONr_scangle_other11.79112.92112931
X-RAY DIFFRACTIONr_lrange_it18.154156.62872296
X-RAY DIFFRACTIONr_lrange_other18.155156.62972291
X-RAY DIFFRACTIONr_ncsr_local_group_10.0810.0513622
X-RAY DIFFRACTIONr_ncsr_local_group_20.0850.0513691
X-RAY DIFFRACTIONr_ncsr_local_group_30.0870.0513665
X-RAY DIFFRACTIONr_ncsr_local_group_40.0880.0513613
X-RAY DIFFRACTIONr_ncsr_local_group_50.0810.0513617
X-RAY DIFFRACTIONr_ncsr_local_group_60.090.0513661
X-RAY DIFFRACTIONr_ncsr_local_group_70.0980.053709
X-RAY DIFFRACTIONr_ncsr_local_group_80.0940.053629
X-RAY DIFFRACTIONr_ncsr_local_group_90.0850.053654
X-RAY DIFFRACTIONr_ncsr_local_group_100.0830.053667
X-RAY DIFFRACTIONr_ncsr_local_group_110.0970.053645
X-RAY DIFFRACTIONr_ncsr_local_group_120.0940.053637
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDRefine-IDTypeRms dev position (Å)Weight position
11BX-RAY DIFFRACTIONLocal ncs0.080620.05009
12AX-RAY DIFFRACTIONLocal ncs0.080620.05009
23BX-RAY DIFFRACTIONLocal ncs0.085070.05009
24CX-RAY DIFFRACTIONLocal ncs0.085070.05009
35BX-RAY DIFFRACTIONLocal ncs0.086590.05009
36DX-RAY DIFFRACTIONLocal ncs0.086590.05009
47AX-RAY DIFFRACTIONLocal ncs0.087880.05009
48CX-RAY DIFFRACTIONLocal ncs0.087880.05009
59AX-RAY DIFFRACTIONLocal ncs0.081220.05009
510DX-RAY DIFFRACTIONLocal ncs0.081220.05009
611CX-RAY DIFFRACTIONLocal ncs0.089710.05008
612DX-RAY DIFFRACTIONLocal ncs0.089710.05008
713KX-RAY DIFFRACTIONLocal ncs0.097960.05009
714EX-RAY DIFFRACTIONLocal ncs0.097960.05009
815KX-RAY DIFFRACTIONLocal ncs0.093750.0501
816FX-RAY DIFFRACTIONLocal ncs0.093750.0501
917KX-RAY DIFFRACTIONLocal ncs0.085160.05009
918GX-RAY DIFFRACTIONLocal ncs0.085160.05009
1019EX-RAY DIFFRACTIONLocal ncs0.083110.0501
1020FX-RAY DIFFRACTIONLocal ncs0.083110.0501
1121EX-RAY DIFFRACTIONLocal ncs0.096520.0501
1122GX-RAY DIFFRACTIONLocal ncs0.096520.0501
1223FX-RAY DIFFRACTIONLocal ncs0.094140.0501
1224GX-RAY DIFFRACTIONLocal ncs0.094140.0501
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
2.5-2.5650.3773310.36163580.36267370.6060.60699.28750.358
2.565-2.6350.3833440.34562040.34766030.6650.69899.1670.339
2.635-2.7110.382990.33360380.33563840.6850.71699.26380.324
2.711-2.7950.3862690.30959380.31262360.7630.79799.5350.295
2.795-2.8860.3633130.30456720.30760220.7880.81499.38560.285
2.886-2.9880.3722820.29454900.29858000.780.8299.51720.276
2.988-3.10.3262720.26953330.27256380.8390.87199.41470.252
3.1-3.2270.3162570.25651420.25954320.8580.88399.39250.244
3.227-3.370.3322510.2749320.27352130.8390.87299.42450.261
3.37-3.5340.322440.2646940.26349610.8720.90199.53640.256
3.534-3.7250.2852380.2544380.25247030.8880.91299.42590.247
3.725-3.9510.3131830.24442490.24744760.870.999.0170.245
3.951-4.2230.2551950.21740300.21942390.9150.92499.66970.222
4.223-4.5610.2341940.18937040.19139090.9290.9499.71860.2
4.561-4.9950.251700.18334160.18736050.9350.94999.4730.197
4.995-5.5830.2671550.21230990.21432750.9110.93199.35880.225
5.583-6.4430.2771490.22527220.22828850.9150.92699.51470.24
6.443-7.8820.2481300.20122840.20324370.9230.93499.05620.218
7.882-11.1090.198860.17618220.17719260.9550.95599.06540.198
11.109-95.9380.207450.25710030.25510700.9490.92897.94390.325

+
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://pdbjlvh1.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