[English] 日本語
Yorodumi
- PDB-4ygo: Dodecameric structure of spermidine N-acetyltransferase from Vibr... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 4ygo
TitleDodecameric structure of spermidine N-acetyltransferase from Vibrio cholerae in intermediate state
ComponentsSpermidine n1-acetyltransferase
KeywordsTRANSFERASE / SpeG / Structural Genomics / CSGID / Center for Structural Genomics of Infectious Diseases
Function / homology
Function and homology information


spermidine catabolic process / polyamine catabolic process / spermine catabolic process / diamine N-acetyltransferase / diamine N-acetyltransferase activity / magnesium ion binding / cytoplasm
Similarity search - Function
Acetyltransferase (GNAT) domain / Gcn5-related N-acetyltransferase (GNAT) / Gcn5-related N-acetyltransferase (GNAT) domain profile. / GNAT domain / Acyl-CoA N-acyltransferase / Aminopeptidase / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
METHANOL / Spermidine N(1)-acetyltransferase
Similarity search - Component
Biological speciesVibrio cholerae serotype O1 (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å
AuthorsFilippova, E.V. / Minasov, G. / Kiryukhina, O. / Anderson, W.F. / Center for Structural Genomics of Infectious Diseases (CSGID)
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID) United States
CitationJournal: J.Mol.Biol. / Year: 2015
Title: Substrate-Induced Allosteric Change in the Quaternary Structure of the Spermidine N-Acetyltransferase SpeG.
Authors: Filippova, E.V. / Weigand, S. / Osipiuk, J. / Kiryukhina, O. / Joachimiak, A. / Anderson, W.F.
History
DepositionFeb 26, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 7, 2015Provider: repository / Type: Initial release
Revision 1.1Nov 11, 2015Group: Database references
Revision 1.2Sep 20, 2017Group: Author supporting evidence / Database references ...Author supporting evidence / Database references / Derived calculations / Refinement description
Category: citation / pdbx_audit_support ...citation / pdbx_audit_support / pdbx_struct_oper_list / software
Item: _citation.journal_id_CSD / _pdbx_audit_support.funding_organization ..._citation.journal_id_CSD / _pdbx_audit_support.funding_organization / _pdbx_struct_oper_list.symmetry_operation / _software.classification
Revision 1.3Dec 11, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.4Sep 27, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn
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.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.ptnr1_symmetry / _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
Revision 1.5Nov 29, 2023Group: Database references / Category: pdbx_database_related / Item: _pdbx_database_related.db_name

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Spermidine n1-acetyltransferase
B: Spermidine n1-acetyltransferase
D: Spermidine n1-acetyltransferase
C: Spermidine n1-acetyltransferase
E: Spermidine n1-acetyltransferase
F: Spermidine n1-acetyltransferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)124,49313
Polymers124,2206
Non-polymers2737
Water2,594144
1
A: Spermidine n1-acetyltransferase
B: Spermidine n1-acetyltransferase
D: Spermidine n1-acetyltransferase
C: Spermidine n1-acetyltransferase
E: Spermidine n1-acetyltransferase
F: Spermidine n1-acetyltransferase
hetero molecules

A: Spermidine n1-acetyltransferase
B: Spermidine n1-acetyltransferase
D: Spermidine n1-acetyltransferase
C: Spermidine n1-acetyltransferase
E: Spermidine n1-acetyltransferase
F: Spermidine n1-acetyltransferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)248,98626
Polymers248,44112
Non-polymers54514
Water21612
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_556-x,y,-z+11
Buried area32660 Å2
ΔGint-202.7 kcal/mol
Surface area84450 Å2
MethodPISA
Unit cell
Length a, b, c (Å)155.118, 135.793, 72.848
Angle α, β, γ (deg.)90.00, 117.13, 90.00
Int Tables number5
Space group name H-MC121
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.572187, -0.040617, -0.819116), (0.048787, -0.99869, 0.015441), (-0.81867, -0.031127, 0.573419)4.72499, 178.90036, 2.0502
3given(-0.158355, -0.781637, -0.603298), (0.77485, -0.477083, 0.414727), (-0.611989, -0.401791, 0.6812)70.63577, 131.01723, 35.26604
4given(0.62751, -0.758127, -0.177412), (0.747195, 0.522282, 0.411001), (-0.218931, -0.390469, 0.894205)67.11399, 40.35147, 33.76793
5given(0.63343, 0.743532, -0.214305), (-0.759131, 0.543445, -0.358311), (-0.149952, 0.389651, 0.908673)-64.79691, 39.72213, -32.54556
6given(-0.234689, 0.709998, -0.663946), (-0.707463, -0.593172, -0.384244), (-0.666646, 0.379539, 0.641508)-60.5214, 141.73587, -32.84689

-
Components

#1: Protein
Spermidine n1-acetyltransferase


Mass: 20703.385 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Vibrio cholerae serotype O1 (ATCC 39315 / El Tor Inaba N16961) (bacteria)
Strain: ATCC 39315 / El Tor Inaba N16961 / Gene: VC_A0947 / Plasmid: pMCSG7 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) magic / References: UniProt: Q9KL03
#2: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Ca
#3: Chemical ChemComp-MOH / METHANOL / Methanol


Mass: 32.042 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Formula: CH4O
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 144 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION

-
Sample preparation

CrystalDensity Matthews: 2.85 Å3/Da / Density % sol: 56.77 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 8.5
Details: 0.01 M CaCl2, 0.1 M Tris HCl, 20% Methanol, 25 % MPD

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.97872 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Dec 9, 2011
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97872 Å / Relative weight: 1
ReflectionResolution: 2.5→30 Å / Num. obs: 46610 / % possible obs: 100 % / Redundancy: 3.8 % / Biso Wilson estimate: 54.8 Å2 / Rmerge(I) obs: 0.065 / Net I/σ(I): 25.4
Reflection shellResolution: 2.5→2.54 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.59 / Mean I/σ(I) obs: 2 / % possible all: 100

-
Processing

Software
NameVersionClassification
REFMAC5.8.0103refinement
BLU-MAXdata collection
HKL-3000data scaling
PHASERphasing
Cootmodel building
HKL-3000phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3EG7

3eg7
PDB Unreleased entry


Resolution: 2.5→30 Å / Cor.coef. Fo:Fc: 0.962 / Cor.coef. Fo:Fc free: 0.93 / SU B: 20.949 / SU ML: 0.216 / Cross valid method: THROUGHOUT / ESU R: 0.448 / ESU R Free: 0.286 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.25274 2408 5.2 %RANDOM
Rwork0.18011 ---
obs0.18368 44197 99.35 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 61.62 Å2
Baniso -1Baniso -2Baniso -3
1--3.99 Å2-0 Å2-1.54 Å2
2--0.6 Å2-0 Å2
3---3.26 Å2
Refinement stepCycle: LAST / Resolution: 2.5→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8611 0 8 144 8763
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0150.0198821
X-RAY DIFFRACTIONr_bond_other_d0.0020.028303
X-RAY DIFFRACTIONr_angle_refined_deg1.7621.93511891
X-RAY DIFFRACTIONr_angle_other_deg1.052318956
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.20251011
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.80524.011531
X-RAY DIFFRACTIONr_dihedral_angle_3_deg18.511151554
X-RAY DIFFRACTIONr_dihedral_angle_4_deg18.1581569
X-RAY DIFFRACTIONr_chiral_restr0.1040.21252
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.0210108
X-RAY DIFFRACTIONr_gen_planes_other0.0020.022309
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it1.9793.9344069
X-RAY DIFFRACTIONr_mcbond_other1.9783.9344067
X-RAY DIFFRACTIONr_mcangle_it3.0695.8895069
X-RAY DIFFRACTIONr_mcangle_other3.0695.8895070
X-RAY DIFFRACTIONr_scbond_it2.5324.2034752
X-RAY DIFFRACTIONr_scbond_other2.5324.2044753
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other3.8466.2116823
X-RAY DIFFRACTIONr_long_range_B_refined5.58730.9969704
X-RAY DIFFRACTIONr_long_range_B_other5.5830.9619691
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.5→2.556 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.35 183 -
Rwork0.279 3013 -
obs--92.72 %
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)
14.6781-1.72281.50145.84171.84885.80730.23970.4346-0.1009-0.5687-0.12-0.20760.0478-0.5253-0.11960.2143-0.04820.08330.1998-0.01430.0488-29.276-21.93570.3547
24.64870.52440.42134.58680.34160.4713-0.3906-0.32270.2960.19210.1999-0.0602-0.1078-0.11340.19070.2134-0.00180.01790.1031-0.07510.1721-30.8919-13.660311.396
34.6208-0.0537-0.98482.4528-1.87837.630.03850.3263-0.4523-0.36480.00240.06510.5751-0.0293-0.04090.1455-0.02350.03150.0739-0.01880.1031-32.0261-25.67133.9822
47.81111.9539-2.71025.0099-1.78934.49430.16170.0295-0.07680.1582-0.52210.05110.20480.16050.36030.0807-0.05630.00310.1421-0.01890.1053-44.5451-27.981514.556
55.22073.22160.24265.299-1.69464.8893-0.24090.82180.0255-0.75260.29090.35890.2746-0.065-0.05010.2932-0.00640.0260.3143-0.01430.0918-40.2016-25.0044-4.0128
61.3326-0.2007-0.04723.7303-0.26632.55710.01180.3069-0.0118-0.555-0.10750.40710.1108-0.32670.09570.1108-0.0599-0.05370.2639-0.03390.0512-51.121-21.08194.043
73.15070.43331.77797.4468-1.63882.4170.0436-0.1088-0.3544-0.7465-0.0208-0.38280.13110.543-0.02280.2488-0.01330.1210.42170.06840.162916.1105-15.929224.8781
82.0143-1.79312.7725.5911-0.43524.86520.2223-0.0106-0.1761-0.2418-0.13280.35970.2953-0.0441-0.08960.15190.03060.08730.15080.09310.1657.9567-23.287732.8345
90.59420.7998-0.15392.22321.4946.26840.02580.11570.0922-0.1244-0.0345-0.175-0.27160.45930.00880.08470.03570.03260.31180.09380.208615.9087-11.379634.5745
106.27470.0391-2.56558.41875.16127.0394-0.17210.1636-0.2125-0.13270.1852-0.6183-0.26880.6531-0.01310.08190.02740.04160.37390.09260.154127.0873-13.717330.3925
111.133-0.624-0.05623.5553-0.37871.5596-0.14080.02690.0647-0.03020.0637-0.5745-0.01210.46660.07710.03030.00520.03520.29650.02870.17925.6544-15.443844.7311
126.73672.67670.73792.7749-0.40171.99040.05240.5002-0.0098-0.1452-0.108-0.1794-0.00790.31370.05560.1542-0.0470.04550.14480.02420.172.73624.595417.5654
136.4756-0.44560.69121.24791.123.19290.1004-0.0665-0.16970.2864-0.07060.1160.24830.228-0.02980.1663-0.0249-0.03090.0567-0.00220.14980.8716-1.8629.2734
143.8166-1.67-3.60162.07482.07526.9754-0.00070.18170.257-0.09840.202-0.0403-0.44530.1746-0.20130.1352-0.0969-0.02410.11590.01890.1535-2.014610.877424.3561
151.16091.3571-0.47044.084-4.52388.785-0.02040.0840.0815-0.5387-0.1814-0.21070.03750.30910.20180.4821-0.06420.10860.30330.03320.34319.860715.852517.752
166.2601-0.43441.43530.5806-0.98412.8762-0.09680.25190.3929-0.0462-0.0834-0.0605-0.42010.21040.18020.287-0.0809-0.01310.07360.0240.21531.749820.631928.4894
172.1561-2.65671.94383.855-2.20982.602-0.14490.11820.4161-0.007-0.1627-0.2659-0.4060.34080.30760.2938-0.1097-0.04250.11010.00460.27265.092819.411636.1475
182.31111.2069-0.26841.23510.94235.7719-0.25440.4773-0.1339-0.36540.2059-0.2927-0.3227-0.24580.04850.2926-0.0260.07080.17980.04520.2344-20.06171.1295.11
192.8368-0.23780.37935.31954.63044.16030.08750.25240.3768-0.12070.146-0.3818-0.13390.1567-0.23360.25830.0837-0.05160.1022-0.02020.2427-17.98888.52817.5675
208.03393.2213-1.04273.14650.93831.2154-0.1772-0.1764-0.37580.10210.1626-0.34230.06710.17370.01460.18340.0099-0.05770.0888-0.0240.2073-17.1853-2.382619.2423
213.9895-2.2079-0.55792.78141.75911.42990.26260.27640.1645-0.5738-0.154-0.1668-0.4376-0.0504-0.10860.27830.02310.02820.06950.0670.0825-28.85543.286110.3254
222.30370.57840.41420.9585-0.56181.411-0.1340.17920.1063-0.3184-0.07240.0176-0.2080.13750.20640.36940.0493-0.01940.11790.07160.19-30.829110.84976.6021
233.01961.0462.97110.78091.43534.5252-0.29570.34270.2424-0.20510.0561-0.0137-0.4330.15760.23960.3010.0573-0.05610.09980.06580.1838-33.872418.767712.8965
244.59371.4913-0.40886.92860.87592.00450.08680.4689-0.05350.0577-0.3744-0.70440.12030.170.28760.1501-0.03660.05960.18410.08340.1793-15.5718-43.04948.3224
254.79190.68522.05085.8298-1.0231.5301-0.0688-0.17980.05740.2011-0.08480.11270.1344-0.18340.15370.156-0.09540.06840.10550.00210.1286-24.6318-37.116314.9753
262.64441.1828-3.70263.7792-2.15216.9256-0.1479-0.0304-0.21740.1302-0.0155-0.51810.35710.12340.16340.0856-0.0427-0.02630.10020.01470.1293-19.0894-50.490914.9495
272.6992-0.6425-0.20572.5464-0.11134.15480.23680.1192-0.31940.0695-0.2697-0.27260.35030.36780.03290.2409-0.0166-0.00020.07360.00720.1012-23.0353-56.903910.0333
284.3318-1.3127-0.010.43520.50368.8805-0.17640.33350.01550.1019-0.08990.00110.2655-0.24260.26630.19750.0034-0.00320.1587-0.02810.1765-30.0018-63.14626.8979
296.0921-2.57331.19523.60410.1441.60050.4093-0.2175-0.7469-0.1583-0.10580.45020.3513-0.0452-0.30350.3645-0.11430.02870.068-0.0390.1815-34.4258-57.605514.7736
305.85140.53421.48914.8811-1.11524.75590.02030.7036-0.7427-0.37850.20160.23460.6067-0.0937-0.22190.2130.05190.0350.1691-0.04190.13951.4047-42.271422.9531
313.7303-1.4268-3.1172.528-0.38476.2309-0.13110.5167-0.1362-0.15860.00030.16060.27010.09740.13090.2290.02930.05470.32250.01610.1184.9667-37.696325.5576
322.59441.28411.13410.95471.71368.40970.0674-0.0169-0.0368-0.1835-0.0916-0.1633-0.1068-0.30410.02420.32840.12630.13440.117-0.00040.20126.7772-42.66440.8044
331.99770.11281.04251.9145-0.05312.6311-0.01070.4382-0.2574-0.2577-0.1797-0.26910.50540.50550.19030.39310.24480.1780.3326-0.01160.188713.5653-48.036530.7446
348.79524.4296-0.25343.63670.5572.86560.20620.5744-0.6755-0.24230.1142-0.58170.540.3047-0.32040.40110.18080.09830.1254-0.03980.239810.2977-60.239935.1435
355.57783.4068-0.25492.6505-0.06711.16640.01480.3882-0.7988-0.37430.0377-0.63180.31990.1703-0.05250.40870.21290.11530.1687-0.05690.305511.252-55.396237.9744
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A2 - 24
2X-RAY DIFFRACTION2A25 - 48
3X-RAY DIFFRACTION3A49 - 73
4X-RAY DIFFRACTION4A74 - 85
5X-RAY DIFFRACTION5A86 - 111
6X-RAY DIFFRACTION6A112 - 170
7X-RAY DIFFRACTION7B2 - 23
8X-RAY DIFFRACTION8B24 - 52
9X-RAY DIFFRACTION9B53 - 85
10X-RAY DIFFRACTION10B86 - 108
11X-RAY DIFFRACTION11B109 - 170
12X-RAY DIFFRACTION12C2 - 23
13X-RAY DIFFRACTION13C24 - 53
14X-RAY DIFFRACTION14C54 - 88
15X-RAY DIFFRACTION15C89 - 103
16X-RAY DIFFRACTION16C104 - 139
17X-RAY DIFFRACTION17C140 - 171
18X-RAY DIFFRACTION18D2 - 22
19X-RAY DIFFRACTION19D23 - 34
20X-RAY DIFFRACTION20D35 - 52
21X-RAY DIFFRACTION21D53 - 87
22X-RAY DIFFRACTION22D88 - 128
23X-RAY DIFFRACTION23D129 - 173
24X-RAY DIFFRACTION24E4 - 22
25X-RAY DIFFRACTION25E23 - 53
26X-RAY DIFFRACTION26E54 - 87
27X-RAY DIFFRACTION27E88 - 129
28X-RAY DIFFRACTION28E130 - 138
29X-RAY DIFFRACTION29E139 - 170
30X-RAY DIFFRACTION30F2 - 42
31X-RAY DIFFRACTION31F43 - 71
32X-RAY DIFFRACTION32F72 - 85
33X-RAY DIFFRACTION33F86 - 125
34X-RAY DIFFRACTION34F126 - 149
35X-RAY DIFFRACTION35F150 - 173

+
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