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- PDB-6ojm: Crystal structure of 1,4-dihydroxy-2-naphthoyl-CoA synthase Eliza... -

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Basic information

Entry
Database: PDB / ID: 6ojm
TitleCrystal structure of 1,4-dihydroxy-2-naphthoyl-CoA synthase Elizabethkingia anophelis NUHP1
Components1,4-dihydroxy-2-naphthoyl-CoA synthase
KeywordsLYASE / SSGCID / Structural Genomics / DHNA-CoA synthase / Seattle Structural Genomics Center for Infectious Disease
Function / homology
Function and homology information


1,4-dihydroxy-2-naphthoyl-CoA synthase / 1,4-dihydroxy-2-naphthoyl-CoA synthase activity / menaquinone biosynthetic process
Similarity search - Function
1,4-Dihydroxy-2-naphthoyl-CoA synthase, MenB / Lyase 2-enoyl-coa Hydratase, Chain A, domain 2 / Lyase 2-enoyl-coa Hydratase; Chain A, domain 2 / Enoyl-CoA hydratase, C-terminal / Enoyl-CoA hydratase/isomerase / Enoyl-CoA hydratase/isomerase / 2-enoyl-CoA Hydratase; Chain A, domain 1 / 2-enoyl-CoA Hydratase; Chain A, domain 1 / ClpP/crotonase-like domain superfamily / Alpha-Beta Complex ...1,4-Dihydroxy-2-naphthoyl-CoA synthase, MenB / Lyase 2-enoyl-coa Hydratase, Chain A, domain 2 / Lyase 2-enoyl-coa Hydratase; Chain A, domain 2 / Enoyl-CoA hydratase, C-terminal / Enoyl-CoA hydratase/isomerase / Enoyl-CoA hydratase/isomerase / 2-enoyl-CoA Hydratase; Chain A, domain 1 / 2-enoyl-CoA Hydratase; Chain A, domain 1 / ClpP/crotonase-like domain superfamily / Alpha-Beta Complex / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
1,4-dihydroxy-2-naphthoyl-CoA synthase
Similarity search - Component
Biological speciesElizabethkingia anophelis NUHP1 (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.6 Å
AuthorsSeattle Structural Genomics Center for Infectious Disease (SSGCID)
CitationJournal: TO BE PUBLISHED
Title: Crystal structure of 1,4-dihydroxy-2-naphthoyl-CoA synthase Elizabethkingia anophelis NUHP1
Authors: Abendroth, J. / Dranow, D.M. / Lorimer, D.D. / Horanyi, P.S. / Edwards, T.E.
History
DepositionApr 11, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 8, 2019Provider: repository / Type: Initial release
Revision 1.1Oct 11, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: 1,4-dihydroxy-2-naphthoyl-CoA synthase
B: 1,4-dihydroxy-2-naphthoyl-CoA synthase
C: 1,4-dihydroxy-2-naphthoyl-CoA synthase
D: 1,4-dihydroxy-2-naphthoyl-CoA synthase
E: 1,4-dihydroxy-2-naphthoyl-CoA synthase
F: 1,4-dihydroxy-2-naphthoyl-CoA synthase


Theoretical massNumber of molelcules
Total (without water)192,5006
Polymers192,5006
Non-polymers00
Water26,1041449
1
A: 1,4-dihydroxy-2-naphthoyl-CoA synthase
B: 1,4-dihydroxy-2-naphthoyl-CoA synthase

A: 1,4-dihydroxy-2-naphthoyl-CoA synthase
B: 1,4-dihydroxy-2-naphthoyl-CoA synthase

A: 1,4-dihydroxy-2-naphthoyl-CoA synthase
B: 1,4-dihydroxy-2-naphthoyl-CoA synthase


Theoretical massNumber of molelcules
Total (without water)192,5006
Polymers192,5006
Non-polymers00
Water1086
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_565-y,x-y+1,z1
crystal symmetry operation3_455-x+y-1,-x,z1
Buried area38020 Å2
ΔGint-205 kcal/mol
Surface area48000 Å2
MethodPISA
2
C: 1,4-dihydroxy-2-naphthoyl-CoA synthase
D: 1,4-dihydroxy-2-naphthoyl-CoA synthase

C: 1,4-dihydroxy-2-naphthoyl-CoA synthase
D: 1,4-dihydroxy-2-naphthoyl-CoA synthase

C: 1,4-dihydroxy-2-naphthoyl-CoA synthase
D: 1,4-dihydroxy-2-naphthoyl-CoA synthase


Theoretical massNumber of molelcules
Total (without water)192,5006
Polymers192,5006
Non-polymers00
Water1086
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_565-y,x-y+1,z1
crystal symmetry operation3_455-x+y-1,-x,z1
Buried area35350 Å2
ΔGint-196 kcal/mol
Surface area47620 Å2
MethodPISA
3
E: 1,4-dihydroxy-2-naphthoyl-CoA synthase
F: 1,4-dihydroxy-2-naphthoyl-CoA synthase

E: 1,4-dihydroxy-2-naphthoyl-CoA synthase
F: 1,4-dihydroxy-2-naphthoyl-CoA synthase

E: 1,4-dihydroxy-2-naphthoyl-CoA synthase
F: 1,4-dihydroxy-2-naphthoyl-CoA synthase


Theoretical massNumber of molelcules
Total (without water)192,5006
Polymers192,5006
Non-polymers00
Water1086
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_555-y,x-y,z1
crystal symmetry operation3_555-x+y,-x,z1
Buried area38070 Å2
ΔGint-201 kcal/mol
Surface area48050 Å2
MethodPISA
Unit cell
Length a, b, c (Å)138.490, 138.490, 141.430
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number150
Space group name H-MP321
Components on special symmetry positions
IDModelComponents
11F-70-

ASP

21A-493-

HOH

31A-516-

HOH

41A-542-

HOH

51A-555-

HOH

61A-557-

HOH

71B-493-

HOH

81B-526-

HOH

91B-535-

HOH

101B-536-

HOH

111C-473-

HOH

121C-508-

HOH

131C-509-

HOH

141C-518-

HOH

151C-519-

HOH

161D-474-

HOH

171D-507-

HOH

181D-515-

HOH

191D-516-

HOH

201E-483-

HOH

211E-506-

HOH

221E-535-

HOH

231E-549-

HOH

241E-550-

HOH

251E-551-

HOH

261F-467-

HOH

271F-487-

HOH

281F-493-

HOH

291F-508-

HOH

301F-543-

HOH

311F-556-

HOH

321F-557-

HOH

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Components

#1: Protein
1,4-dihydroxy-2-naphthoyl-CoA synthase / DHNA-CoA synthase


Mass: 32083.297 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Elizabethkingia anophelis NUHP1 (bacteria)
Gene: menB, BD94_2634 / Plasmid: ElanA.01530.a.B1
Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
Strain (production host): BL21(DE3)
References: UniProt: A0A077EJG6, 1,4-dihydroxy-2-naphthoyl-CoA synthase
#2: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 1449 / 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: 2.04 Å3/Da / Density % sol: 39.65 %
Crystal growTemperature: 290 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: Molecular Dimensions Morpheus screen, C7: 10% (w/v) PEG 4000, 20% (v/v) glycerol, 30mM of each sodium nitrate, disodium hydrogen phosphate, ammonium sulfate: 100mM MOPS/HEPES-Na pH 7.5: ...Details: Molecular Dimensions Morpheus screen, C7: 10% (w/v) PEG 4000, 20% (v/v) glycerol, 30mM of each sodium nitrate, disodium hydrogen phosphate, ammonium sulfate: 100mM MOPS/HEPES-Na pH 7.5: ElanA.01530.a.B1.PW38414 at 20.1 mg/ml: cryo: direct: tray 298241c7: puck uya9-1

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.97872 Å
DetectorType: RAYONIX MX-300 / Detector: CCD / Date: Apr 12, 2018
RadiationMonochromator: C(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97872 Å / Relative weight: 1
ReflectionResolution: 1.6→43.876 Å / Num. obs: 204876 / % possible obs: 99.7 % / Redundancy: 6.191 % / Biso Wilson estimate: 23.947 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.053 / Rrim(I) all: 0.057 / Χ2: 1.029 / Net I/σ(I): 21.94
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. unique obsCC1/2Rrim(I) all% possible all
1.6-1.646.250.53.46149870.8870.54599.4
1.64-1.696.2550.4144.2146310.9140.45199.5
1.69-1.746.2540.3455.01142830.9410.37699.7
1.74-1.796.2580.2766.36137960.9610.30199.6
1.79-1.856.2630.2247.96134720.9720.24499.7
1.85-1.916.2370.17310.26129840.9850.18899.8
1.91-1.986.2090.13712.95126150.9910.1599.9
1.98-2.076.2080.10916.01121290.9940.11999.9
2.07-2.166.1830.08719.9116620.9960.09599.9
2.16-2.266.160.07223.41111010.9990.07999.9
2.26-2.396.1920.06127.28106220.9980.066100
2.39-2.536.2150.05429.99100420.9980.05999.9
2.53-2.76.1920.04833.794540.9980.05299.9
2.7-2.926.1940.03939.5587750.9990.04399.9
2.92-3.26.1490.03245.4681560.9990.03599.9
3.2-3.586.0750.02752.4173420.9990.0399.8
3.58-4.136.0160.02458.2365300.9990.02699.6
4.13-5.065.9920.02261.91551310.02499.4
5.06-7.165.9810.02357.5543390.9990.02699.4
7.16-43.8765.6910.02160.9324430.9990.02497.4

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Processing

Software
NameVersionClassification
PHENIXrefinement
XDSdata reduction
XSCALEdata scaling
PDB_EXTRACT3.25data extraction
MoRDaphasing
PHASERphasing
ARP/wARPmodel building
Cootmodel building
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 3t8a, chain A
Resolution: 1.6→43.876 Å / SU ML: 0.15 / Cross valid method: THROUGHOUT / σ(F): 1.36 / Phase error: 15
RfactorNum. reflection% reflectionSelection details
Rfree0.1753 1983 0.97 %0
Rwork0.145 ---
obs0.1453 204839 99.71 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 73.18 Å2 / Biso mean: 21.7539 Å2 / Biso min: 3.72 Å2
Refinement stepCycle: final / Resolution: 1.6→43.876 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12518 0 0 1470 13988
Biso mean---32.73 -
Num. residues----1616
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00713146
X-RAY DIFFRACTIONf_angle_d0.9117833
X-RAY DIFFRACTIONf_dihedral_angle_d13.5517873
X-RAY DIFFRACTIONf_chiral_restr0.0591884
X-RAY DIFFRACTIONf_plane_restr0.0062348
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 14

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
1.6-1.640.23011510.1916143001445199
1.64-1.68440.21781550.1721143441449999
1.6844-1.73390.17051470.16031437814525100
1.7339-1.78990.21761620.15361432914491100
1.7899-1.85390.18231260.1521440914535100
1.8539-1.92810.19131570.15291442314580100
1.9281-2.01590.20731150.14431448014595100
2.0159-2.12210.16561510.14281444514596100
2.1221-2.25510.18891380.14151446514603100
2.2551-2.42920.17891580.14251452414682100
2.4292-2.67360.16131370.14631457614713100
2.6736-3.06040.17971100.14451460014710100
3.0604-3.85550.15571310.13381467014801100
3.8555-43.8920.15871450.1412149131505899
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)
12.07750.1128-0.20852.95310.5321.6240.0141-0.02940.15570.10970.0213-0.2879-0.0550.1987-0.03470.08060.0084-0.03240.1732-0.0220.1934-38.623540.680116.3831
20.9264-0.4958-0.86582.59111.26033.49220.15750.62330.4198-0.5470.205-0.4183-0.75140.4412-0.30770.295-0.09630.07180.3910.05570.3092-43.893152.645811.7193
30.5698-0.14580.06240.6173-0.07310.56450.0002-0.02590.010.03940.0205-0.05450.01270.078-0.02070.07030.0023-0.00310.0941-0.00630.1055-55.154239.504914.6638
44.19250.8216-2.25043.5696-0.97234.6991-0.23310.2522-0.5758-0.19890.1804-0.30070.43740.27370.12130.33150.0777-0.02990.1828-0.07210.3062-55.831510.1761-14.3324
52.4706-0.36360.05894.45370.39231.12130.0350.13340.1174-0.2205-0.0633-0.5096-0.04870.39070.00780.129-0.01340.05220.3023-0.04620.2281-34.204742.554-19.6042
62.1473-0.4929-0.11534.5966-0.39192.07120.01160.1317-0.1959-0.30610.0488-0.17190.22080.2678-0.03910.11890.02220.00920.2435-0.04610.1831-39.985433.5662-21.0987
71.4984-0.13210.04732.9856-0.13581.64460.0147-0.09960.07740.17670.0266-0.1817-0.04530.2519-0.05390.1058-0.00220.01910.2428-0.0290.1762-40.650841.6998-12.1476
81.512-0.1163-0.23461.8437-0.03392.1348-0.0266-0.0579-0.34160.06830.0133-0.08860.43130.379-0.00550.14180.0598-0.00940.2077-0.00130.2289-44.202528.5091-12.9977
91.06550.4338-0.18670.95080.11970.7865-0.01790.1344-0.0633-0.12130.0455-0.06180.03810.0614-0.02640.11160.01050.00490.1294-0.01610.1025-57.191133.4333-21.5118
101.4699-1.9155-1.88246.35775.7815.52040.08130.11110.0688-0.42790.0975-0.2838-0.32840.2273-0.19620.1693-0.02820.04640.18520.01680.1496-47.805350.2481-26.7384
110.7728-1.153-0.53672.09970.01552.53050.0305-0.06510.11790.07550.0181-0.1441-0.24250.1824-0.05490.093-0.01730.00070.1137-0.01040.1098-56.219251.7868-3.8228
126.7596-1.87523.38753.8444-0.66347.4532-0.19880.190.3393-0.03950.1701-0.5628-0.340.8330.10370.2297-0.08520.03610.2669-0.04780.3187-50.009667.591110.8812
136.2358-3.45554.02782.031-2.56453.6969-0.4122-0.09350.58170.2720.1998-0.2334-0.56510.09020.21790.2807-0.04370.01660.1574-0.04670.2364-59.115770.935112.9369
143.0652-0.6182-0.64212.84490.99362.09040.12710.0130.171-0.00290.0139-0.4072-0.24320.2557-0.09810.2288-0.07830.03250.14450.01740.2163-52.925265.027853.6787
150.691-0.1309-0.01410.8541-0.14450.91550.0268-0.00160.07720.01520.02230.031-0.1705-0.021-0.0570.1325-0.00660.01090.0948-0.00010.1073-66.777754.418958.8371
163.8283-1.18070.50022.8818-0.37511.3533-0.0608-0.12760.3575-0.02410.0473-0.1306-0.31170.10090.01430.2713-0.08970.02210.1601-0.0430.1873-54.900167.006586.349
174.03720.1035-0.39793.26041.45226.24380.0409-0.16270.3695-0.06290.06330.3506-0.7007-0.3046-0.08450.36180.01690.04320.1776-0.01890.2525-67.436769.077692.5094
181.09240.1593-0.05410.254-0.03710.6840.0318-0.12870.06520.06270.0034-0.0206-0.12450.0241-0.03320.1865-0.01060.0050.1384-0.02080.116-65.145754.204990.3429
190.5463-0.92740.19731.89150.54682.636-0.04570.01380.0541-0.04880.0783-0.1579-0.05820.3628-0.03160.1196-0.02160.00540.1612-0.01140.1131-52.416745.795573.3339
201.92130.565-0.21316.671-2.36363.52480.156-0.15890.1131-0.2296-0.2115-0.4211-0.12390.51670.07310.164-0.00220.03320.4065-0.05780.2682-36.486938.31757.795
213.18140.54860.18833.3021-0.21581.03770.0829-0.2380.06860.23550.00680.3836-0.1026-0.1922-0.05670.15530.05630.09060.2185-0.0020.1716-27.880315.679954.2371
221.96870.4760.01991.6759-0.21230.92970.0044-0.09010.04090.07970.05430.2909-0.0776-0.1435-0.08120.12920.05890.06430.1870.00720.1904-25.313913.731350.3397
232.3079-0.11270.20522.144-1.88696.48830.38730.4627-0.2735-0.35290.15950.53250.2791-0.701-0.51840.2060.0415-0.04110.37450.02490.295-27.94432.215148.0069
240.4867-0.1997-0.15121.0165-0.00950.69710.0022-0.1346-0.00760.15240.03340.0707-0.0102-0.0991-0.0350.1140.00850.02460.14840.01460.0913-14.10411.690253.4109
251.89981.1688-1.58941.6524-1.15671.77990.121-0.26020.17760.3474-0.0530.1672-0.2543-0.0242-0.08610.22760.03780.05290.2027-0.04920.1439-12.747819.884760.07
261.0670.4704-0.22070.32950.28541.67270.0398-0.00870.1911-0.03770.0144-0.0146-0.2874-0.0428-0.06010.12930.0160.02270.0898-0.00060.1117-4.901917.414237.1449
277.6904-2.85842.60634.6574-0.98574.2926-0.04220.37840.6192-0.00080.027-0.0784-0.3695-0.05190.01550.2723-0.01720.05250.11150.03360.2413.638932.450721.585
284.0119-0.2211-1.16641.9865-1.59761.7438-0.00070.03370.1975-0.1465-0.11540.6218-0.0263-0.33120.09770.09270.0644-0.02050.18060.03310.2137-32.506716.073315.5524
291.81070.5828-0.04223.35740.2341.4313-0.0238-0.04810.1369-0.04190.04630.1288-0.0879-0.1155-0.02780.06960.04980.00230.12940.0210.1362-24.771515.623719.7477
301.1317-0.0004-0.00221.24780.11091.23790.0155-0.09160.32720.14010.0711-0.0545-0.5157-0.0539-0.07890.21860.04050.03050.1278-0.01540.2279-15.748822.70523.3382
310.96980.18670.07260.4304-0.01920.47150.01420.09340.0372-0.04210.00980.0254-0.0531-0.0374-0.0180.09960.01450.00450.10120.0110.1015-10.06179.955713.5789
320.0846-0.22720.32572.05560.00061.79810.0238-0.0948-0.07090.0631-0.01340.16530.1208-0.2518-0.0280.0763-0.00480.00810.11860.01490.0979-17.2001-3.580832.2154
335.55560.0373-1.68932.7728-0.19473.2494-0.0584-0.0767-0.29310.48480.330.7030.0021-0.7238-0.19530.2597-0.03390.04790.44980.18040.35-26.9816-18.563947.8322
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 73 )A1 - 73
2X-RAY DIFFRACTION2chain 'A' and (resid 74 through 99 )A74 - 99
3X-RAY DIFFRACTION3chain 'A' and (resid 100 through 252 )A100 - 252
4X-RAY DIFFRACTION4chain 'A' and (resid 253 through 278 )A253 - 278
5X-RAY DIFFRACTION5chain 'B' and (resid 1 through 18 )B1 - 18
6X-RAY DIFFRACTION6chain 'B' and (resid 19 through 36 )B19 - 36
7X-RAY DIFFRACTION7chain 'B' and (resid 37 through 63 )B37 - 63
8X-RAY DIFFRACTION8chain 'B' and (resid 64 through 109 )B64 - 109
9X-RAY DIFFRACTION9chain 'B' and (resid 110 through 199 )B110 - 199
10X-RAY DIFFRACTION10chain 'B' and (resid 200 through 218 )B200 - 218
11X-RAY DIFFRACTION11chain 'B' and (resid 219 through 252 )B219 - 252
12X-RAY DIFFRACTION12chain 'B' and (resid 253 through 264 )B253 - 264
13X-RAY DIFFRACTION13chain 'B' and (resid 265 through 278 )B265 - 278
14X-RAY DIFFRACTION14chain 'C' and (resid 1 through 99 )C1 - 99
15X-RAY DIFFRACTION15chain 'C' and (resid 100 through 278 )C100 - 278
16X-RAY DIFFRACTION16chain 'D' and (resid 1 through 63 )D1 - 63
17X-RAY DIFFRACTION17chain 'D' and (resid 64 through 99 )D64 - 99
18X-RAY DIFFRACTION18chain 'D' and (resid 100 through 218 )D100 - 218
19X-RAY DIFFRACTION19chain 'D' and (resid 219 through 252 )D219 - 252
20X-RAY DIFFRACTION20chain 'D' and (resid 253 through 278 )D253 - 278
21X-RAY DIFFRACTION21chain 'E' and (resid 1 through 36 )E1 - 36
22X-RAY DIFFRACTION22chain 'E' and (resid 37 through 73 )E37 - 73
23X-RAY DIFFRACTION23chain 'E' and (resid 74 through 99 )E74 - 99
24X-RAY DIFFRACTION24chain 'E' and (resid 100 through 199 )E100 - 199
25X-RAY DIFFRACTION25chain 'E' and (resid 200 through 218 )E200 - 218
26X-RAY DIFFRACTION26chain 'E' and (resid 219 through 252 )E219 - 252
27X-RAY DIFFRACTION27chain 'E' and (resid 253 through 278 )E253 - 278
28X-RAY DIFFRACTION28chain 'F' and (resid 1 through 12 )F1 - 12
29X-RAY DIFFRACTION29chain 'F' and (resid 13 through 63 )F13 - 63
30X-RAY DIFFRACTION30chain 'F' and (resid 64 through 109 )F64 - 109
31X-RAY DIFFRACTION31chain 'F' and (resid 110 through 218 )F110 - 218
32X-RAY DIFFRACTION32chain 'F' and (resid 219 through 252 )F219 - 252
33X-RAY DIFFRACTION33chain 'F' and (resid 253 through 278 )F253 - 278

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